data_4BC0
# 
_entry.id   4BC0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4BC0         
PDBE  EBI-54256    
WWPDB D_1290054256 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 1C2B unspecified 'ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE' 
PDB 1C2O unspecified 'ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE' 
PDB 1J06 unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN THE APOFORM' 
PDB 1J07 unspecified 'CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE- DECIDIUM COMPLEX' 
PDB 1KU6 unspecified 'FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX' 
PDB 1MAA unspecified 'MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN, GLYCOSYLATEDPROTEIN' 
PDB 1MAH unspecified 'FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX' 
PDB 1N5M unspecified 'CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE- GALLAMINE COMPLEX' 
PDB 1N5R unspecified 'CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE- PROPIDIUM COMPLEX' 
PDB 1Q83 unspecified 'CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE- TZ2PA6SYN COMPLEX' 
PDB 1Q84 unspecified 'CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE- TZ2PA6ANTI COMPLEX' 
PDB 2C0P unspecified 'AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY TABUN' 
PDB 2C0Q unspecified 'NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY TABUN' 
PDB 2H9Y unspecified 
'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEXEDWITH M-(N,N,N-TRIMETHYLAMMONIO) TRIFLUOROACETOPHENONE'     
PDB 2HA0 unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEXEDWITH 4-KETOAMYLTRIMETHYLAMMONIUM' 
PDB 2HA2 unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEXEDWITH SUCCINYLCHOLINE' 
PDB 2HA3 unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEXEDWITH CHOLINE' 
PDB 2HA4 unspecified 'CRYSTAL STRUCTURE OF MUTANT S203A OF MOUSEACETYLCHOLINESTERASE COMPLEXED WITH ACETYLCHOLINE' 
PDB 2HA5 unspecified 'CRYSTAL STRUCTURE OF MUTANT S203A OF ACETYLCHOLINESTERASECOMPLEXED WITH ACETYLTHIOCHOLINE' 
PDB 2HA6 unspecified 'CRYSTAL STRUCTURE OF MUTANT S203A OF MOUSEACETYLCHOLINESTERASE COMPLEXED WITH SUCCINYLCHOLINE' 
PDB 2HA7 unspecified 'CRYSTAL STRUCTURE OF MUTANT S203A OF MOUSEACETYLCHOLINESTERASE COMPLEXED WITH BUTYRYLTHIOCHOLINE' 
PDB 2JEY unspecified 'MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH HLO-7' 
PDB 2JEZ unspecified 'MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN AND HLO-7' 
PDB 2JF0 unspecified 'MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN AND ORTHO-7' 
PDB 2JGE unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-AGED METHAMIDOPHOS' 
PDB 2JGF unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-AGED FENAMIPHOS' 
PDB 2JGG unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-AGED SARIN' 
PDB 2JGH unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-AGED VX' 
PDB 2JGI unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)' 
PDB 2JGJ unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY AGED METHAMIDOPHOS' 
PDB 2JGK unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY AGED FENAMIPHOS' 
PDB 2JGL unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY AGED VX AND SARIN' 
PDB 2JGM unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)' 
PDB 2WHP unspecified 'CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY SARIN AND IN COMPLEX WITH HI-6' 
PDB 2WHQ unspecified 'CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY SARIN (AGED) IN COMPLEX WITH HI-6' 
PDB 2WHR unspecified 'CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN COMPLEX WITH K027' 
PDB 2WLS unspecified 'CRYSTAL STRUCTURE OF MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH AMTS13' 
PDB 2WU3 unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX WITH FENAMIPHOS AND HI-6' 
PDB 2WU4 unspecified 'CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX WITH FENAMIPHOS AND ORTHO-7' 
PDB 2XUD unspecified 'CRYSTAL STRUCTURE OF THE Y337A MUTANT OF MOUSE ACETYLCHOLINESTERASE' 
PDB 2XUF unspecified 'CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX ( 1 MTH)' 
PDB 2XUG unspecified 'CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX ( 1 WK)' 
PDB 2XUH unspecified 'CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX ( 10 MTH)' 
PDB 2XUI unspecified 'CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1 WK)' 
PDB 2XUJ unspecified 'CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1 MTH)' 
PDB 2XUK unspecified 'CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX ( 10 MTH)' 
PDB 2XUO unspecified 'CRYSTAL STRUCTURE OF MACHE-Y337A MUTANT IN COMPLEX WITH SOAKED TZ2PA6 ANTI INHIBITOR' 
PDB 2XUP unspecified 'CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX WITH SOAKED TZ2PA6 SYN INHIBITOR' 
PDB 2XUQ unspecified 'CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX WITH SOAKED TZ2PA6 ANTI-SYN INHIBITORS' 
PDB 4A16 unspecified 'STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEX WITH HUPRINE DERIVATIVE' 
PDB 4A23 unspecified 'MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH RACEMIC C5685' 
PDB 4ARA unspecified 'MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (R)- C5685 AT 2.5 A RESOLUTION.' 
PDB 4ARB unspecified 'MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (S)- C5685 AT 2.25 A RESOLUTION.' 
PDB 4B7Z unspecified 
'MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2- DIETHYLAMINO-ETHYL)-1-(4-METHYLPHENYL)-METHANESULFONAMIDE'  
PDB 4B80 unspecified 
'MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2- DIETHYLAMINO-ETHYL)-1-(4-FLUORO-PHENYL)-METHANESULFONAMIDE' 
PDB 4B81 unspecified 
'MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 1-(4- CHLORO-PHENYL)-N-(2-DIETHYLAMINO-ETHYL)-METHANESULFONAMIDE' 
PDB 4B82 unspecified 'MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2- DIETHYLAMINO-ETHYL)-2-FLUORANYL-BENZENESULFONAMIDE' 
PDB 4B83 unspecified 'MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2- DIETHYLAMINO-ETHYL)-3-METHOXY-BENZENESULFONAMIDE' 
PDB 4B84 unspecified 
'MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2- DIETHYLAMINO-ETHYL)-3-TRIFLUOROMETHYL-BENZENESULFONAMIDE'   
PDB 4B85 unspecified 'MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 4- CHLORANYL-N-(2-DIETHYLAMINO-ETHYL)-BENZENESULFONAMIDE' 
PDB 4BBZ unspecified 'STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP (2-MIN SOAK): CRESYL-PHOSPHOSERINE ADDUCT' 
PDB 4BC1 unspecified 
'STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY CBDP (30-MIN SOAK): CRESYL-SALIGENIN-PHOSPHOSERINE ADDUCT'     
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4BC0 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2012-09-30 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Carletti, E.'     1 
'Colletier, J.-P.' 2 
'Schopfer, L.M.'   3 
'Santoni, G.'      4 
'Masson, P.'       5 
'Lockridge, O.'    6 
'Nachon, F.'       7 
'Weik, M.'         8 
# 
_citation.id                        primary 
_citation.title                     
;Inhibition Pathways of the Potent Organophosphate Cbdp with Cholinesterases Revealed by X-Ray Crystallographic Snapshots and Mass Spectrometry
;
_citation.journal_abbrev            Chem.Res.Toxicol. 
_citation.journal_volume            26 
_citation.page_first                280 
_citation.page_last                 ? 
_citation.year                      2013 
_citation.journal_id_ASTM           CRTOEC 
_citation.country                   US 
_citation.journal_id_ISSN           0893-228X 
_citation.journal_id_CSD            2140 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   23339663 
_citation.pdbx_database_id_DOI      10.1021/TX3004505 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Carletti, E.'     1 
primary 'Colletier, J.-P.' 2 
primary 'Schopfer, L.M.'   3 
primary 'Santoni, G.'      4 
primary 'Masson, P.'       5 
primary 'Lockridge, O.'    6 
primary 'Nachon, F.'       7 
primary 'Weik, M.'         8 
# 
_cell.entry_id           4BC0 
_cell.length_a           136.940 
_cell.length_b           174.040 
_cell.length_c           225.620 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              16 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         4BC0 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
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 ACETYLCHOLINESTERASE                    59764.488 4   3.1.1.7 ? ? 'CRESYL-PHOSPHATE ADDUCT ON S203' 
2 non-polymer syn '(2-methylphenyl) dihydrogen phosphate' 188.118   4   ?       ? ? ?                                 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE                  221.208   7   ?       ? ? ?                                 
4 non-polymer syn 'SULFATE ION'                           96.063    13  ?       ? ? ?                                 
5 non-polymer syn 'CHLORIDE ION'                          35.453    8   ?       ? ? ?                                 
6 water       nat water                                   18.015    411 ?       ? ? ?                                 
# 
_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       
;EGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGF
EGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLA
LPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVS
AGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGD
FQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSA
VVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYW
TNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSAT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;EGREDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGF
EGTEMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLA
LPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVS
AGEARRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGD
FQDLQVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSA
VVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYW
TNFARTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSAT
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLU n 
1 2   GLY n 
1 3   ARG n 
1 4   GLU n 
1 5   ASP n 
1 6   PRO n 
1 7   GLN n 
1 8   LEU n 
1 9   LEU n 
1 10  VAL n 
1 11  ARG n 
1 12  VAL n 
1 13  ARG n 
1 14  GLY n 
1 15  GLY n 
1 16  GLN n 
1 17  LEU n 
1 18  ARG n 
1 19  GLY n 
1 20  ILE n 
1 21  ARG n 
1 22  LEU n 
1 23  LYS n 
1 24  ALA n 
1 25  PRO n 
1 26  GLY n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  SER n 
1 31  ALA n 
1 32  PHE n 
1 33  LEU n 
1 34  GLY n 
1 35  ILE n 
1 36  PRO n 
1 37  PHE n 
1 38  ALA n 
1 39  GLU n 
1 40  PRO n 
1 41  PRO n 
1 42  VAL n 
1 43  GLY n 
1 44  SER n 
1 45  ARG n 
1 46  ARG n 
1 47  PHE n 
1 48  MET n 
1 49  PRO n 
1 50  PRO n 
1 51  GLU n 
1 52  PRO n 
1 53  LYS n 
1 54  ARG n 
1 55  PRO n 
1 56  TRP n 
1 57  SER n 
1 58  GLY n 
1 59  VAL n 
1 60  LEU n 
1 61  ASP n 
1 62  ALA n 
1 63  THR n 
1 64  THR n 
1 65  PHE n 
1 66  GLN n 
1 67  ASN n 
1 68  VAL n 
1 69  CYS n 
1 70  TYR n 
1 71  GLN n 
1 72  TYR n 
1 73  VAL n 
1 74  ASP n 
1 75  THR n 
1 76  LEU n 
1 77  TYR n 
1 78  PRO n 
1 79  GLY n 
1 80  PHE n 
1 81  GLU n 
1 82  GLY n 
1 83  THR n 
1 84  GLU n 
1 85  MET n 
1 86  TRP n 
1 87  ASN n 
1 88  PRO n 
1 89  ASN n 
1 90  ARG n 
1 91  GLU n 
1 92  LEU n 
1 93  SER n 
1 94  GLU n 
1 95  ASP n 
1 96  CYS n 
1 97  LEU n 
1 98  TYR n 
1 99  LEU n 
1 100 ASN n 
1 101 VAL n 
1 102 TRP n 
1 103 THR n 
1 104 PRO n 
1 105 TYR n 
1 106 PRO n 
1 107 ARG n 
1 108 PRO n 
1 109 ALA n 
1 110 SER n 
1 111 PRO n 
1 112 THR n 
1 113 PRO n 
1 114 VAL n 
1 115 LEU n 
1 116 ILE n 
1 117 TRP n 
1 118 ILE n 
1 119 TYR n 
1 120 GLY n 
1 121 GLY n 
1 122 GLY n 
1 123 PHE n 
1 124 TYR n 
1 125 SER n 
1 126 GLY n 
1 127 ALA n 
1 128 ALA n 
1 129 SER n 
1 130 LEU n 
1 131 ASP n 
1 132 VAL n 
1 133 TYR n 
1 134 ASP n 
1 135 GLY n 
1 136 ARG n 
1 137 PHE n 
1 138 LEU n 
1 139 ALA n 
1 140 GLN n 
1 141 VAL n 
1 142 GLU n 
1 143 GLY n 
1 144 ALA n 
1 145 VAL n 
1 146 LEU n 
1 147 VAL n 
1 148 SER n 
1 149 MET n 
1 150 ASN n 
1 151 TYR n 
1 152 ARG n 
1 153 VAL n 
1 154 GLY n 
1 155 THR n 
1 156 PHE n 
1 157 GLY n 
1 158 PHE n 
1 159 LEU n 
1 160 ALA n 
1 161 LEU n 
1 162 PRO n 
1 163 GLY n 
1 164 SER n 
1 165 ARG n 
1 166 GLU n 
1 167 ALA n 
1 168 PRO n 
1 169 GLY n 
1 170 ASN n 
1 171 VAL n 
1 172 GLY n 
1 173 LEU n 
1 174 LEU n 
1 175 ASP n 
1 176 GLN n 
1 177 ARG n 
1 178 LEU n 
1 179 ALA n 
1 180 LEU n 
1 181 GLN n 
1 182 TRP n 
1 183 VAL n 
1 184 GLN n 
1 185 GLU n 
1 186 ASN n 
1 187 ILE n 
1 188 ALA n 
1 189 ALA n 
1 190 PHE n 
1 191 GLY n 
1 192 GLY n 
1 193 ASP n 
1 194 PRO n 
1 195 MET n 
1 196 SER n 
1 197 VAL n 
1 198 THR n 
1 199 LEU n 
1 200 PHE n 
1 201 GLY n 
1 202 GLU n 
1 203 SER n 
1 204 ALA n 
1 205 GLY n 
1 206 ALA n 
1 207 ALA n 
1 208 SER n 
1 209 VAL n 
1 210 GLY n 
1 211 MET n 
1 212 HIS n 
1 213 ILE n 
1 214 LEU n 
1 215 SER n 
1 216 LEU n 
1 217 PRO n 
1 218 SER n 
1 219 ARG n 
1 220 SER n 
1 221 LEU n 
1 222 PHE n 
1 223 HIS n 
1 224 ARG n 
1 225 ALA n 
1 226 VAL n 
1 227 LEU n 
1 228 GLN n 
1 229 SER n 
1 230 GLY n 
1 231 THR n 
1 232 PRO n 
1 233 ASN n 
1 234 GLY n 
1 235 PRO n 
1 236 TRP n 
1 237 ALA n 
1 238 THR n 
1 239 VAL n 
1 240 SER n 
1 241 ALA n 
1 242 GLY n 
1 243 GLU n 
1 244 ALA n 
1 245 ARG n 
1 246 ARG n 
1 247 ARG n 
1 248 ALA n 
1 249 THR n 
1 250 LEU n 
1 251 LEU n 
1 252 ALA n 
1 253 ARG n 
1 254 LEU n 
1 255 VAL n 
1 256 GLY n 
1 257 CYS n 
1 258 PRO n 
1 259 PRO n 
1 260 GLY n 
1 261 GLY n 
1 262 ALA n 
1 263 GLY n 
1 264 GLY n 
1 265 ASN n 
1 266 ASP n 
1 267 THR n 
1 268 GLU n 
1 269 LEU n 
1 270 ILE n 
1 271 ALA n 
1 272 CYS n 
1 273 LEU n 
1 274 ARG n 
1 275 THR n 
1 276 ARG n 
1 277 PRO n 
1 278 ALA n 
1 279 GLN n 
1 280 ASP n 
1 281 LEU n 
1 282 VAL n 
1 283 ASP n 
1 284 HIS n 
1 285 GLU n 
1 286 TRP n 
1 287 HIS n 
1 288 VAL n 
1 289 LEU n 
1 290 PRO n 
1 291 GLN n 
1 292 GLU n 
1 293 SER n 
1 294 ILE n 
1 295 PHE n 
1 296 ARG n 
1 297 PHE n 
1 298 SER n 
1 299 PHE n 
1 300 VAL n 
1 301 PRO n 
1 302 VAL n 
1 303 VAL n 
1 304 ASP n 
1 305 GLY n 
1 306 ASP n 
1 307 PHE n 
1 308 LEU n 
1 309 SER n 
1 310 ASP n 
1 311 THR n 
1 312 PRO n 
1 313 GLU n 
1 314 ALA n 
1 315 LEU n 
1 316 ILE n 
1 317 ASN n 
1 318 THR n 
1 319 GLY n 
1 320 ASP n 
1 321 PHE n 
1 322 GLN n 
1 323 ASP n 
1 324 LEU n 
1 325 GLN n 
1 326 VAL n 
1 327 LEU n 
1 328 VAL n 
1 329 GLY n 
1 330 VAL n 
1 331 VAL n 
1 332 LYS n 
1 333 ASP n 
1 334 GLU n 
1 335 GLY n 
1 336 SER n 
1 337 TYR n 
1 338 PHE n 
1 339 LEU n 
1 340 VAL n 
1 341 TYR n 
1 342 GLY n 
1 343 VAL n 
1 344 PRO n 
1 345 GLY n 
1 346 PHE n 
1 347 SER n 
1 348 LYS n 
1 349 ASP n 
1 350 ASN n 
1 351 GLU n 
1 352 SER n 
1 353 LEU n 
1 354 ILE n 
1 355 SER n 
1 356 ARG n 
1 357 ALA n 
1 358 GLN n 
1 359 PHE n 
1 360 LEU n 
1 361 ALA n 
1 362 GLY n 
1 363 VAL n 
1 364 ARG n 
1 365 ILE n 
1 366 GLY n 
1 367 VAL n 
1 368 PRO n 
1 369 GLN n 
1 370 ALA n 
1 371 SER n 
1 372 ASP n 
1 373 LEU n 
1 374 ALA n 
1 375 ALA n 
1 376 GLU n 
1 377 ALA n 
1 378 VAL n 
1 379 VAL n 
1 380 LEU n 
1 381 HIS n 
1 382 TYR n 
1 383 THR n 
1 384 ASP n 
1 385 TRP n 
1 386 LEU n 
1 387 HIS n 
1 388 PRO n 
1 389 GLU n 
1 390 ASP n 
1 391 PRO n 
1 392 THR n 
1 393 HIS n 
1 394 LEU n 
1 395 ARG n 
1 396 ASP n 
1 397 ALA n 
1 398 MET n 
1 399 SER n 
1 400 ALA n 
1 401 VAL n 
1 402 VAL n 
1 403 GLY n 
1 404 ASP n 
1 405 HIS n 
1 406 ASN n 
1 407 VAL n 
1 408 VAL n 
1 409 CYS n 
1 410 PRO n 
1 411 VAL n 
1 412 ALA n 
1 413 GLN n 
1 414 LEU n 
1 415 ALA n 
1 416 GLY n 
1 417 ARG n 
1 418 LEU n 
1 419 ALA n 
1 420 ALA n 
1 421 GLN n 
1 422 GLY n 
1 423 ALA n 
1 424 ARG n 
1 425 VAL n 
1 426 TYR n 
1 427 ALA n 
1 428 TYR n 
1 429 ILE n 
1 430 PHE n 
1 431 GLU n 
1 432 HIS n 
1 433 ARG n 
1 434 ALA n 
1 435 SER n 
1 436 THR n 
1 437 LEU n 
1 438 THR n 
1 439 TRP n 
1 440 PRO n 
1 441 LEU n 
1 442 TRP n 
1 443 MET n 
1 444 GLY n 
1 445 VAL n 
1 446 PRO n 
1 447 HIS n 
1 448 GLY n 
1 449 TYR n 
1 450 GLU n 
1 451 ILE n 
1 452 GLU n 
1 453 PHE n 
1 454 ILE n 
1 455 PHE n 
1 456 GLY n 
1 457 LEU n 
1 458 PRO n 
1 459 LEU n 
1 460 ASP n 
1 461 PRO n 
1 462 SER n 
1 463 LEU n 
1 464 ASN n 
1 465 TYR n 
1 466 THR n 
1 467 THR n 
1 468 GLU n 
1 469 GLU n 
1 470 ARG n 
1 471 ILE n 
1 472 PHE n 
1 473 ALA n 
1 474 GLN n 
1 475 ARG n 
1 476 LEU n 
1 477 MET n 
1 478 LYS n 
1 479 TYR n 
1 480 TRP n 
1 481 THR n 
1 482 ASN n 
1 483 PHE n 
1 484 ALA n 
1 485 ARG n 
1 486 THR n 
1 487 GLY n 
1 488 ASP n 
1 489 PRO n 
1 490 ASN n 
1 491 ASP n 
1 492 PRO n 
1 493 ARG n 
1 494 ASP n 
1 495 SER n 
1 496 LYS n 
1 497 SER n 
1 498 PRO n 
1 499 GLN n 
1 500 TRP n 
1 501 PRO n 
1 502 PRO n 
1 503 TYR n 
1 504 THR n 
1 505 THR n 
1 506 ALA n 
1 507 ALA n 
1 508 GLN n 
1 509 GLN n 
1 510 TYR n 
1 511 VAL n 
1 512 SER n 
1 513 LEU n 
1 514 ASN n 
1 515 LEU n 
1 516 LYS n 
1 517 PRO n 
1 518 LEU n 
1 519 GLU n 
1 520 VAL n 
1 521 ARG n 
1 522 ARG n 
1 523 GLY n 
1 524 LEU n 
1 525 ARG n 
1 526 ALA n 
1 527 GLN n 
1 528 THR n 
1 529 CYS n 
1 530 ALA n 
1 531 PHE n 
1 532 TRP n 
1 533 ASN n 
1 534 ARG n 
1 535 PHE n 
1 536 LEU n 
1 537 PRO n 
1 538 LYS n 
1 539 LEU n 
1 540 LEU n 
1 541 SER n 
1 542 ALA n 
1 543 THR 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               'HOUSE MOUSE' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'MUS MUSCULUS' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10090 
_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               'CHINESE HAMSTER' 
_entity_src_gen.pdbx_host_org_scientific_name      'CRICETULUS GRISEUS' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     10029 
_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            CHO-K1 
_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          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       PGS 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ACES_MOUSE 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          P21836 
_struct_ref.pdbx_db_isoform            ? 
# 
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 4BC0 A 1 ? 543 ? P21836 32 ? 574 ? 1 543 
2 1 4BC0 B 1 ? 543 ? P21836 32 ? 574 ? 1 543 
3 1 4BC0 C 1 ? 543 ? P21836 32 ? 574 ? 1 543 
4 1 4BC0 D 1 ? 543 ? P21836 32 ? 574 ? 1 543 
# 
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 
4OJ non-polymer         . '(2-methylphenyl) dihydrogen phosphate' o-cresyl-phosphate 'C7 H9 O4 P'     188.118 
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 
CL  non-polymer         . 'CHLORIDE ION'                          ?                  'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE                                ?                  'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                               ?                  'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                         ?                  'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                 ?                  'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                               ?                  'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                   ?                  'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                              ?                  'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                 ?                  'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                  ?                  'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                              ?                  'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE                  ?                  'C8 H15 N O6'    221.208 
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 
SO4 non-polymer         . 'SULFATE ION'                           ?                  'O4 S -2'        96.063  
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 
# 
_exptl.entry_id          4BC0 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      5.63 
_exptl_crystal.density_percent_sol   78 
_exptl_crystal.description           NONE 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.4 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '0.1 M TRIS HCL BUFFER PH 7.4, 1.6 M AMMONIUM SULFATE' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315r' 
_diffrn_detector.pdbx_collection_date   2010-04-15 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9765 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE ID14-4' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   ID14-4 
_diffrn_source.pdbx_wavelength             0.9765 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4BC0 
_reflns.observed_criterion_sigma_I   -3.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             48.60 
_reflns.d_resolution_high            3.35 
_reflns.number_obs                   75488 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         96.6 
_reflns.pdbx_Rmerge_I_obs            0.08 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.20 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              3.5 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             3.35 
_reflns_shell.d_res_low              3.40 
_reflns_shell.percent_possible_all   98.6 
_reflns_shell.Rmerge_I_obs           0.58 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.80 
_reflns_shell.pdbx_redundancy        3.4 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4BC0 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     75467 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             48.615 
_refine.ls_d_res_high                            3.35 
_refine.ls_percent_reflns_obs                    96.66 
_refine.ls_R_factor_obs                          0.1631 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1618 
_refine.ls_R_factor_R_free                       0.2076 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 3.0 
_refine.ls_number_reflns_R_free                  2265 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 4A16' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.37 
_refine.pdbx_overall_phase_error                 21.06 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        16806 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         215 
_refine_hist.number_atoms_solvent             411 
_refine_hist.number_atoms_total               17432 
_refine_hist.d_res_high                       3.35 
_refine_hist.d_res_low                        48.615 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.009  ? ? 17527 'X-RAY DIFFRACTION' ? 
f_angle_d          1.482  ? ? 23960 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 17.136 ? ? 6287  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.108  ? ? 2568  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.008  ? ? 3140  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
1 A 17 ?     ? POSITIONAL 1 1 'X-RAY DIFFRACTION' ? ? ? 
2 B 17 0.033 ? POSITIONAL 1 2 'X-RAY DIFFRACTION' ? ? ? 
3 C 17 0.042 ? POSITIONAL 1 3 'X-RAY DIFFRACTION' ? ? ? 
4 D 17 0.036 ? POSITIONAL 1 4 'X-RAY DIFFRACTION' ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' . 3.3500 3.4228  4577 0.3099 98.00 0.3324 . . 141 . . 
'X-RAY DIFFRACTION' . 3.4228 3.5024  4587 0.2724 98.00 0.3306 . . 142 . . 
'X-RAY DIFFRACTION' . 3.5024 3.5900  4602 0.2434 98.00 0.3231 . . 143 . . 
'X-RAY DIFFRACTION' . 3.5900 3.6870  4591 0.2201 98.00 0.2878 . . 142 . . 
'X-RAY DIFFRACTION' . 3.6870 3.7955  4575 0.1967 98.00 0.2294 . . 141 . . 
'X-RAY DIFFRACTION' . 3.7955 3.9179  4575 0.1796 98.00 0.2341 . . 142 . . 
'X-RAY DIFFRACTION' . 3.9179 4.0579  4611 0.1588 98.00 0.2154 . . 142 . . 
'X-RAY DIFFRACTION' . 4.0579 4.2203  4556 0.1478 98.00 0.1801 . . 141 . . 
'X-RAY DIFFRACTION' . 4.2203 4.4122  4605 0.1311 97.00 0.1661 . . 143 . . 
'X-RAY DIFFRACTION' . 4.4122 4.6447  4553 0.1188 97.00 0.1639 . . 140 . . 
'X-RAY DIFFRACTION' . 4.6447 4.9354  4565 0.1146 96.00 0.1708 . . 142 . . 
'X-RAY DIFFRACTION' . 4.9354 5.3161  4555 0.1199 96.00 0.1512 . . 141 . . 
'X-RAY DIFFRACTION' . 5.3161 5.8502  4574 0.1284 96.00 0.1845 . . 141 . . 
'X-RAY DIFFRACTION' . 5.8502 6.6949  4547 0.1481 95.00 0.2121 . . 141 . . 
'X-RAY DIFFRACTION' . 6.6949 8.4277  4523 0.1525 94.00 0.2013 . . 140 . . 
'X-RAY DIFFRACTION' . 8.4277 48.6198 4606 0.1725 92.00 0.1997 . . 143 . . 
# 
loop_
_struct_ncs_dom.id 
_struct_ncs_dom.details 
_struct_ncs_dom.pdbx_ens_id 
1 ? 1 
2 ? 1 
3 ? 1 
4 ? 1 
# 
loop_
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.selection_details 
1 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 1 'CHAIN A AND (RESSEQ 203 OR RESSEQ 600)' 
2 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 1 'CHAIN B AND (RESSEQ 203 OR RESSEQ 600)' 
3 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 1 'CHAIN C AND (RESSEQ 203 OR RESSEQ 600)' 
4 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 1 'CHAIN D AND (RESSEQ 203 OR RESSEQ 600)' 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                  4BC0 
_struct.title                     
'Structure of mouse acetylcholinesterase inhibited by CBDP (12-h soak) : Cresyl-phosphoserine adduct' 
_struct.pdbx_descriptor           'ACETYLCHOLINESTERASE (E.C.3.1.1.7)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4BC0 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
'HYDROLASE, ACETYLCHOLINESTERASE, BUTYRYLCHOLINESTERASE, NERVE TRANSMISSION, INHIBITION, ALPHA-BETA HYDROLASE' 
# 
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 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 4 ? 
H  N N 4 ? 
I  N N 4 ? 
J  N N 4 ? 
K  N N 4 ? 
L  N N 2 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 4 ? 
P  N N 4 ? 
Q  N N 4 ? 
R  N N 2 ? 
S  N N 3 ? 
T  N N 5 ? 
U  N N 5 ? 
V  N N 4 ? 
W  N N 4 ? 
X  N N 5 ? 
Y  N N 5 ? 
Z  N N 5 ? 
AA N N 2 ? 
BA N N 3 ? 
CA N N 3 ? 
DA N N 3 ? 
EA N N 4 ? 
FA N N 4 ? 
GA N N 4 ? 
HA N N 5 ? 
IA N N 5 ? 
JA N N 5 ? 
KA N N 6 ? 
LA N N 6 ? 
MA N N 6 ? 
NA N N 6 ? 
# 
_struct_biol.id   1 
# 
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   1   VAL A 42  ? ARG A 46  ? VAL A 42  ARG A 46  5 ? 5  
HELX_P HELX_P2   2   PHE A 80  ? MET A 85  ? PHE A 80  MET A 85  1 ? 6  
HELX_P HELX_P3   3   LEU A 130 ? ASP A 134 ? LEU A 130 ASP A 134 5 ? 5  
HELX_P HELX_P4   4   GLY A 135 ? GLY A 143 ? GLY A 135 GLY A 143 1 ? 9  
HELX_P HELX_P5   5   VAL A 153 ? LEU A 159 ? VAL A 153 LEU A 159 1 ? 7  
HELX_P HELX_P6   6   ASN A 170 ? ILE A 187 ? ASN A 170 ILE A 187 1 ? 18 
HELX_P HELX_P7   7   ALA A 188 ? GLY A 191 ? ALA A 188 GLY A 191 5 ? 4  
HELX_P HELX_P8   8   SER A 203 ? SER A 215 ? SER A 203 SER A 215 1 ? 13 
HELX_P HELX_P9   9   SER A 215 ? SER A 220 ? SER A 215 SER A 220 1 ? 6  
HELX_P HELX_P10  10  SER A 240 ? VAL A 255 ? SER A 240 VAL A 255 1 ? 16 
HELX_P HELX_P11  11  ASN A 265 ? ARG A 274 ? ASN A 265 ARG A 274 1 ? 10 
HELX_P HELX_P12  12  PRO A 277 ? GLU A 285 ? PRO A 277 GLU A 285 1 ? 9  
HELX_P HELX_P13  13  THR A 311 ? GLY A 319 ? THR A 311 GLY A 319 1 ? 9  
HELX_P HELX_P14  14  GLY A 335 ? VAL A 340 ? GLY A 335 VAL A 340 1 ? 6  
HELX_P HELX_P15  15  SER A 355 ? VAL A 367 ? SER A 355 VAL A 367 1 ? 13 
HELX_P HELX_P16  16  ALA A 374 ? THR A 383 ? ALA A 374 THR A 383 1 ? 10 
HELX_P HELX_P17  17  ASP A 390 ? VAL A 407 ? ASP A 390 VAL A 407 1 ? 18 
HELX_P HELX_P18  18  VAL A 407 ? GLN A 421 ? VAL A 407 GLN A 421 1 ? 15 
HELX_P HELX_P19  19  PRO A 440 ? GLY A 444 ? PRO A 440 GLY A 444 5 ? 5  
HELX_P HELX_P20  20  GLU A 450 ? PHE A 455 ? GLU A 450 PHE A 455 1 ? 6  
HELX_P HELX_P21  21  GLY A 456 ? ASP A 460 ? GLY A 456 ASP A 460 5 ? 5  
HELX_P HELX_P22  22  ASP A 460 ? ASN A 464 ? ASP A 460 ASN A 464 5 ? 5  
HELX_P HELX_P23  23  THR A 466 ? GLY A 487 ? THR A 466 GLY A 487 1 ? 22 
HELX_P HELX_P24  24  ARG A 525 ? ARG A 534 ? ARG A 525 ARG A 534 1 ? 10 
HELX_P HELX_P25  25  ARG A 534 ? SER A 541 ? ARG A 534 SER A 541 1 ? 8  
HELX_P HELX_P26  26  VAL B 42  ? ARG B 46  ? VAL B 42  ARG B 46  5 ? 5  
HELX_P HELX_P27  27  PHE B 80  ? MET B 85  ? PHE B 80  MET B 85  1 ? 6  
HELX_P HELX_P28  28  GLY B 135 ? GLY B 143 ? GLY B 135 GLY B 143 1 ? 9  
HELX_P HELX_P29  29  VAL B 153 ? LEU B 159 ? VAL B 153 LEU B 159 1 ? 7  
HELX_P HELX_P30  30  ASN B 170 ? ILE B 187 ? ASN B 170 ILE B 187 1 ? 18 
HELX_P HELX_P31  31  ALA B 188 ? PHE B 190 ? ALA B 188 PHE B 190 5 ? 3  
HELX_P HELX_P32  32  SER B 203 ? SER B 215 ? SER B 203 SER B 215 1 ? 13 
HELX_P HELX_P33  33  LEU B 216 ? PHE B 222 ? LEU B 216 PHE B 222 5 ? 7  
HELX_P HELX_P34  34  ALA B 241 ? VAL B 255 ? ALA B 241 VAL B 255 1 ? 15 
HELX_P HELX_P35  35  PRO B 258 ? ALA B 262 ? PRO B 258 ALA B 262 5 ? 5  
HELX_P HELX_P36  36  ASN B 265 ? ARG B 274 ? ASN B 265 ARG B 274 1 ? 10 
HELX_P HELX_P37  37  PRO B 277 ? GLU B 285 ? PRO B 277 GLU B 285 1 ? 9  
HELX_P HELX_P38  38  TRP B 286 ? VAL B 288 ? TRP B 286 VAL B 288 5 ? 3  
HELX_P HELX_P39  39  THR B 311 ? GLY B 319 ? THR B 311 GLY B 319 1 ? 9  
HELX_P HELX_P40  40  GLY B 335 ? VAL B 340 ? GLY B 335 VAL B 340 1 ? 6  
HELX_P HELX_P41  41  SER B 355 ? VAL B 367 ? SER B 355 VAL B 367 1 ? 13 
HELX_P HELX_P42  42  SER B 371 ? THR B 383 ? SER B 371 THR B 383 1 ? 13 
HELX_P HELX_P43  43  ASP B 390 ? VAL B 407 ? ASP B 390 VAL B 407 1 ? 18 
HELX_P HELX_P44  44  VAL B 407 ? GLN B 421 ? VAL B 407 GLN B 421 1 ? 15 
HELX_P HELX_P45  45  PRO B 440 ? GLY B 444 ? PRO B 440 GLY B 444 5 ? 5  
HELX_P HELX_P46  46  GLU B 450 ? PHE B 455 ? GLU B 450 PHE B 455 1 ? 6  
HELX_P HELX_P47  47  GLY B 456 ? ASP B 460 ? GLY B 456 ASP B 460 5 ? 5  
HELX_P HELX_P48  48  ASP B 460 ? ASN B 464 ? ASP B 460 ASN B 464 5 ? 5  
HELX_P HELX_P49  49  THR B 466 ? GLY B 487 ? THR B 466 GLY B 487 1 ? 22 
HELX_P HELX_P50  50  THR B 528 ? ARG B 534 ? THR B 528 ARG B 534 1 ? 7  
HELX_P HELX_P51  51  ARG B 534 ? SER B 541 ? ARG B 534 SER B 541 1 ? 8  
HELX_P HELX_P52  52  VAL C 42  ? ARG C 46  ? VAL C 42  ARG C 46  5 ? 5  
HELX_P HELX_P53  53  PHE C 80  ? MET C 85  ? PHE C 80  MET C 85  1 ? 6  
HELX_P HELX_P54  54  LEU C 130 ? ASP C 134 ? LEU C 130 ASP C 134 5 ? 5  
HELX_P HELX_P55  55  GLY C 135 ? GLU C 142 ? GLY C 135 GLU C 142 1 ? 8  
HELX_P HELX_P56  56  GLY C 154 ? LEU C 159 ? GLY C 154 LEU C 159 1 ? 6  
HELX_P HELX_P57  57  ASN C 170 ? ILE C 187 ? ASN C 170 ILE C 187 1 ? 18 
HELX_P HELX_P58  58  ALA C 188 ? PHE C 190 ? ALA C 188 PHE C 190 5 ? 3  
HELX_P HELX_P59  59  SER C 203 ? SER C 215 ? SER C 203 SER C 215 1 ? 13 
HELX_P HELX_P60  60  SER C 215 ? SER C 220 ? SER C 215 SER C 220 1 ? 6  
HELX_P HELX_P61  61  ALA C 241 ? VAL C 255 ? ALA C 241 VAL C 255 1 ? 15 
HELX_P HELX_P62  62  ASN C 265 ? ARG C 274 ? ASN C 265 ARG C 274 1 ? 10 
HELX_P HELX_P63  63  PRO C 277 ? TRP C 286 ? PRO C 277 TRP C 286 1 ? 10 
HELX_P HELX_P64  64  HIS C 287 ? LEU C 289 ? HIS C 287 LEU C 289 5 ? 3  
HELX_P HELX_P65  65  THR C 311 ? GLY C 319 ? THR C 311 GLY C 319 1 ? 9  
HELX_P HELX_P66  66  GLY C 335 ? VAL C 340 ? GLY C 335 VAL C 340 1 ? 6  
HELX_P HELX_P67  67  SER C 355 ? VAL C 367 ? SER C 355 VAL C 367 1 ? 13 
HELX_P HELX_P68  68  SER C 371 ? THR C 383 ? SER C 371 THR C 383 1 ? 13 
HELX_P HELX_P69  69  ASP C 390 ? VAL C 407 ? ASP C 390 VAL C 407 1 ? 18 
HELX_P HELX_P70  70  VAL C 407 ? GLN C 421 ? VAL C 407 GLN C 421 1 ? 15 
HELX_P HELX_P71  71  PRO C 440 ? GLY C 444 ? PRO C 440 GLY C 444 5 ? 5  
HELX_P HELX_P72  72  GLU C 450 ? PHE C 455 ? GLU C 450 PHE C 455 1 ? 6  
HELX_P HELX_P73  73  GLY C 456 ? ASP C 460 ? GLY C 456 ASP C 460 5 ? 5  
HELX_P HELX_P74  74  ASP C 460 ? ASN C 464 ? ASP C 460 ASN C 464 5 ? 5  
HELX_P HELX_P75  75  THR C 466 ? GLY C 487 ? THR C 466 GLY C 487 1 ? 22 
HELX_P HELX_P76  76  ARG C 525 ? ARG C 534 ? ARG C 525 ARG C 534 1 ? 10 
HELX_P HELX_P77  77  ARG C 534 ? SER C 541 ? ARG C 534 SER C 541 1 ? 8  
HELX_P HELX_P78  78  VAL D 42  ? ARG D 46  ? VAL D 42  ARG D 46  5 ? 5  
HELX_P HELX_P79  79  PHE D 80  ? MET D 85  ? PHE D 80  MET D 85  1 ? 6  
HELX_P HELX_P80  80  LEU D 130 ? ASP D 134 ? LEU D 130 ASP D 134 5 ? 5  
HELX_P HELX_P81  81  GLY D 135 ? GLY D 143 ? GLY D 135 GLY D 143 1 ? 9  
HELX_P HELX_P82  82  VAL D 153 ? LEU D 159 ? VAL D 153 LEU D 159 1 ? 7  
HELX_P HELX_P83  83  ASN D 170 ? ILE D 187 ? ASN D 170 ILE D 187 1 ? 18 
HELX_P HELX_P84  84  ALA D 188 ? PHE D 190 ? ALA D 188 PHE D 190 5 ? 3  
HELX_P HELX_P85  85  SER D 203 ? LEU D 214 ? SER D 203 LEU D 214 1 ? 12 
HELX_P HELX_P86  86  SER D 215 ? PHE D 222 ? SER D 215 PHE D 222 5 ? 8  
HELX_P HELX_P87  87  SER D 240 ? VAL D 255 ? SER D 240 VAL D 255 1 ? 16 
HELX_P HELX_P88  88  ASN D 265 ? ARG D 274 ? ASN D 265 ARG D 274 1 ? 10 
HELX_P HELX_P89  89  PRO D 277 ? TRP D 286 ? PRO D 277 TRP D 286 1 ? 10 
HELX_P HELX_P90  90  THR D 311 ? THR D 318 ? THR D 311 THR D 318 1 ? 8  
HELX_P HELX_P91  91  GLY D 335 ? VAL D 340 ? GLY D 335 VAL D 340 1 ? 6  
HELX_P HELX_P92  92  SER D 355 ? VAL D 367 ? SER D 355 VAL D 367 1 ? 13 
HELX_P HELX_P93  93  SER D 371 ? THR D 383 ? SER D 371 THR D 383 1 ? 13 
HELX_P HELX_P94  94  ASP D 390 ? VAL D 407 ? ASP D 390 VAL D 407 1 ? 18 
HELX_P HELX_P95  95  VAL D 407 ? GLN D 421 ? VAL D 407 GLN D 421 1 ? 15 
HELX_P HELX_P96  96  PRO D 440 ? GLY D 444 ? PRO D 440 GLY D 444 5 ? 5  
HELX_P HELX_P97  97  GLU D 450 ? GLY D 456 ? GLU D 450 GLY D 456 1 ? 7  
HELX_P HELX_P98  98  LEU D 457 ? ASN D 464 ? LEU D 457 ASN D 464 5 ? 8  
HELX_P HELX_P99  99  THR D 466 ? GLY D 487 ? THR D 466 GLY D 487 1 ? 22 
HELX_P HELX_P100 100 ARG D 525 ? ARG D 534 ? ARG D 525 ARG D 534 1 ? 10 
HELX_P HELX_P101 101 ARG D 534 ? THR D 543 ? ARG D 534 THR D 543 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A  CYS 69  SG  ? ? ? 1_555 A  CYS 96  SG ? ? A CYS 69  A CYS 96  1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf2  disulf ? ? A  CYS 257 SG  ? ? ? 1_555 A  CYS 272 SG ? ? A CYS 257 A CYS 272 1_555 ? ? ? ? ? ? ? 2.054 ? 
disulf3  disulf ? ? A  CYS 409 SG  ? ? ? 1_555 A  CYS 529 SG ? ? A CYS 409 A CYS 529 1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf4  disulf ? ? B  CYS 69  SG  ? ? ? 1_555 B  CYS 96  SG ? ? B CYS 69  B CYS 96  1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf5  disulf ? ? B  CYS 257 SG  ? ? ? 1_555 B  CYS 272 SG ? ? B CYS 257 B CYS 272 1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf6  disulf ? ? B  CYS 409 SG  ? ? ? 1_555 B  CYS 529 SG ? ? B CYS 409 B CYS 529 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf7  disulf ? ? C  CYS 69  SG  ? ? ? 1_555 C  CYS 96  SG ? ? C CYS 69  C CYS 96  1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf8  disulf ? ? C  CYS 257 SG  ? ? ? 1_555 C  CYS 272 SG ? ? C CYS 257 C CYS 272 1_555 ? ? ? ? ? ? ? 2.061 ? 
disulf9  disulf ? ? C  CYS 409 SG  ? ? ? 1_555 C  CYS 529 SG ? ? C CYS 409 C CYS 529 1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf10 disulf ? ? D  CYS 69  SG  ? ? ? 1_555 D  CYS 96  SG ? ? D CYS 69  D CYS 96  1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf11 disulf ? ? D  CYS 257 SG  ? ? ? 1_555 D  CYS 272 SG ? ? D CYS 257 D CYS 272 1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf12 disulf ? ? D  CYS 409 SG  ? ? ? 1_555 D  CYS 529 SG ? ? D CYS 409 D CYS 529 1_555 ? ? ? ? ? ? ? 2.048 ? 
covale1  covale ? ? A  ASN 265 ND2 ? ? ? 1_555 F  NAG .   C1 ? ? A ASN 265 A NAG 701 1_555 ? ? ? ? ? ? ? 1.456 ? 
covale2  covale ? ? E  4OJ .   P13 ? ? ? 1_555 A  SER 203 OG ? ? A 4OJ 600 A SER 203 1_555 ? ? ? ? ? ? ? 1.576 ? 
covale3  covale ? ? B  ASN 265 ND2 ? ? ? 1_555 M  NAG .   C1 ? ? B ASN 265 B NAG 701 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale4  covale ? ? B  ASN 350 ND2 ? ? ? 1_555 N  NAG .   C1 ? ? B ASN 350 B NAG 702 1_555 ? ? ? ? ? ? ? 1.457 ? 
covale5  covale ? ? L  4OJ .   P13 ? ? ? 1_555 B  SER 203 OG ? ? B 4OJ 600 B SER 203 1_555 ? ? ? ? ? ? ? 1.558 ? 
covale6  covale ? ? R  4OJ .   P13 ? ? ? 1_555 C  SER 203 OG ? ? C 4OJ 600 C SER 203 1_555 ? ? ? ? ? ? ? 1.592 ? 
covale7  covale ? ? D  ASN 265 ND2 ? ? ? 1_555 BA NAG .   C1 ? ? D ASN 265 D NAG 701 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale8  covale ? ? D  ASN 350 ND2 ? ? ? 1_555 CA NAG .   C1 ? ? D ASN 350 D NAG 702 1_555 ? ? ? ? ? ? ? 1.472 ? 
covale9  covale ? ? D  ASN 464 ND2 ? ? ? 1_555 DA NAG .   C1 ? ? D ASN 464 D NAG 703 1_555 ? ? ? ? ? ? ? 1.453 ? 
covale10 covale ? ? AA 4OJ .   P13 ? ? ? 1_555 D  SER 203 OG ? ? D 4OJ 600 D SER 203 1_555 ? ? ? ? ? ? ? 1.584 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 105 A . ? TYR 105 A PRO 106 A ? PRO 106 A 1 0.86   
2 PRO 258 A . ? PRO 258 A PRO 259 A ? PRO 259 A 1 -13.89 
3 TYR 105 B . ? TYR 105 B PRO 106 B ? PRO 106 B 1 12.49  
4 CYS 257 B . ? CYS 257 B PRO 258 B ? PRO 258 B 1 -6.88  
5 SER 495 B . ? SER 495 B LYS 496 B ? LYS 496 B 1 -8.68  
6 SER 497 B . ? SER 497 B PRO 498 B ? PRO 498 B 1 -0.35  
7 TYR 105 C . ? TYR 105 C PRO 106 C ? PRO 106 C 1 -1.65  
8 TYR 105 D . ? TYR 105 D PRO 106 D ? PRO 106 D 1 6.20   
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 3  ? 
AB ? 11 ? 
AC ? 2  ? 
BA ? 3  ? 
BB ? 11 ? 
BC ? 2  ? 
BD ? 2  ? 
CA ? 3  ? 
CB ? 11 ? 
CC ? 2  ? 
CD ? 2  ? 
DA ? 3  ? 
DB ? 11 ? 
DC ? 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 
AA 1  2  ? anti-parallel 
AA 2  3  ? parallel      
AB 1  2  ? anti-parallel 
AB 2  3  ? anti-parallel 
AB 3  4  ? anti-parallel 
AB 4  5  ? parallel      
AB 5  6  ? parallel      
AB 6  7  ? parallel      
AB 7  8  ? parallel      
AB 8  9  ? parallel      
AB 9  10 ? parallel      
AB 10 11 ? anti-parallel 
AC 1  2  ? parallel      
BA 1  2  ? anti-parallel 
BA 2  3  ? parallel      
BB 1  2  ? anti-parallel 
BB 2  3  ? anti-parallel 
BB 3  4  ? anti-parallel 
BB 4  5  ? parallel      
BB 5  6  ? parallel      
BB 6  7  ? parallel      
BB 7  8  ? parallel      
BB 8  9  ? parallel      
BB 9  10 ? parallel      
BB 10 11 ? anti-parallel 
BC 1  2  ? parallel      
BD 1  2  ? parallel      
CA 1  2  ? anti-parallel 
CA 2  3  ? parallel      
CB 1  2  ? anti-parallel 
CB 2  3  ? anti-parallel 
CB 3  4  ? anti-parallel 
CB 4  5  ? parallel      
CB 5  6  ? parallel      
CB 6  7  ? parallel      
CB 7  8  ? parallel      
CB 8  9  ? parallel      
CB 9  10 ? parallel      
CB 10 11 ? anti-parallel 
CC 1  2  ? parallel      
CD 1  2  ? parallel      
DA 1  2  ? anti-parallel 
DA 2  3  ? parallel      
DB 1  2  ? anti-parallel 
DB 2  3  ? anti-parallel 
DB 3  4  ? anti-parallel 
DB 4  5  ? parallel      
DB 5  6  ? parallel      
DB 6  7  ? parallel      
DB 7  8  ? parallel      
DB 8  9  ? parallel      
DB 9  10 ? parallel      
DB 10 11 ? anti-parallel 
DC 1  2  ? 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 
AA 1  LEU A 9   ? VAL A 12  ? LEU A 9   VAL A 12  
AA 2  GLY A 15  ? ARG A 18  ? GLY A 15  ARG A 18  
AA 3  VAL A 59  ? ASP A 61  ? VAL A 59  ASP A 61  
AB 1  ILE A 20  ? LYS A 23  ? ILE A 20  LYS A 23  
AB 2  PRO A 28  ? PRO A 36  ? PRO A 28  PRO A 36  
AB 3  TYR A 98  ? PRO A 104 ? TYR A 98  PRO A 104 
AB 4  VAL A 145 ? MET A 149 ? VAL A 145 MET A 149 
AB 5  VAL A 114 ? ILE A 118 ? VAL A 114 ILE A 118 
AB 6  VAL A 197 ? GLU A 202 ? VAL A 197 GLU A 202 
AB 7  ARG A 224 ? GLN A 228 ? ARG A 224 GLN A 228 
AB 8  GLN A 325 ? VAL A 331 ? GLN A 325 VAL A 331 
AB 9  ARG A 424 ? PHE A 430 ? ARG A 424 PHE A 430 
AB 10 GLN A 509 ? LEU A 513 ? GLN A 509 LEU A 513 
AB 11 VAL A 520 ? ARG A 522 ? VAL A 520 ARG A 522 
AC 1  VAL A 68  ? CYS A 69  ? VAL A 68  CYS A 69  
AC 2  LEU A 92  ? SER A 93  ? LEU A 92  SER A 93  
BA 1  LEU B 9   ? VAL B 10  ? LEU B 9   VAL B 10  
BA 2  LEU B 17  ? ARG B 18  ? LEU B 17  ARG B 18  
BA 3  LEU B 60  ? ASP B 61  ? LEU B 60  ASP B 61  
BB 1  ILE B 20  ? ALA B 24  ? ILE B 20  ALA B 24  
BB 2  GLY B 27  ? PRO B 36  ? GLY B 27  PRO B 36  
BB 3  TYR B 98  ? PRO B 104 ? TYR B 98  PRO B 104 
BB 4  VAL B 145 ? MET B 149 ? VAL B 145 MET B 149 
BB 5  THR B 112 ? ILE B 118 ? THR B 112 ILE B 118 
BB 6  GLY B 192 ? GLU B 202 ? GLY B 192 GLU B 202 
BB 7  ARG B 224 ? GLN B 228 ? ARG B 224 GLN B 228 
BB 8  GLN B 325 ? VAL B 331 ? GLN B 325 VAL B 331 
BB 9  ARG B 424 ? PHE B 430 ? ARG B 424 PHE B 430 
BB 10 GLN B 509 ? LEU B 513 ? GLN B 509 LEU B 513 
BB 11 GLU B 519 ? ARG B 522 ? GLU B 519 ARG B 522 
BC 1  VAL B 68  ? CYS B 69  ? VAL B 68  CYS B 69  
BC 2  LEU B 92  ? SER B 93  ? LEU B 92  SER B 93  
BD 1  VAL B 239 ? SER B 240 ? VAL B 239 SER B 240 
BD 2  VAL B 302 ? VAL B 303 ? VAL B 302 VAL B 303 
CA 1  LEU C 9   ? VAL C 12  ? LEU C 9   VAL C 12  
CA 2  GLY C 15  ? ARG C 18  ? GLY C 15  ARG C 18  
CA 3  VAL C 59  ? ASP C 61  ? VAL C 59  ASP C 61  
CB 1  ILE C 20  ? ALA C 24  ? ILE C 20  ALA C 24  
CB 2  GLY C 27  ? PRO C 36  ? GLY C 27  PRO C 36  
CB 3  TYR C 98  ? PRO C 104 ? TYR C 98  PRO C 104 
CB 4  VAL C 145 ? MET C 149 ? VAL C 145 MET C 149 
CB 5  THR C 112 ? ILE C 118 ? THR C 112 ILE C 118 
CB 6  GLY C 192 ? GLU C 202 ? GLY C 192 GLU C 202 
CB 7  ARG C 224 ? GLN C 228 ? ARG C 224 GLN C 228 
CB 8  GLN C 325 ? VAL C 331 ? GLN C 325 VAL C 331 
CB 9  ARG C 424 ? PHE C 430 ? ARG C 424 PHE C 430 
CB 10 GLN C 509 ? LEU C 513 ? GLN C 509 LEU C 513 
CB 11 VAL C 520 ? ARG C 522 ? VAL C 520 ARG C 522 
CC 1  VAL C 68  ? CYS C 69  ? VAL C 68  CYS C 69  
CC 2  LEU C 92  ? SER C 93  ? LEU C 92  SER C 93  
CD 1  VAL C 239 ? SER C 240 ? VAL C 239 SER C 240 
CD 2  VAL C 302 ? VAL C 303 ? VAL C 302 VAL C 303 
DA 1  LEU D 9   ? VAL D 12  ? LEU D 9   VAL D 12  
DA 2  GLY D 15  ? ARG D 18  ? GLY D 15  ARG D 18  
DA 3  VAL D 59  ? ASP D 61  ? VAL D 59  ASP D 61  
DB 1  ILE D 20  ? ALA D 24  ? ILE D 20  ALA D 24  
DB 2  GLY D 27  ? PRO D 36  ? GLY D 27  PRO D 36  
DB 3  TYR D 98  ? PRO D 104 ? TYR D 98  PRO D 104 
DB 4  VAL D 145 ? MET D 149 ? VAL D 145 MET D 149 
DB 5  THR D 112 ? ILE D 118 ? THR D 112 ILE D 118 
DB 6  GLY D 192 ? GLU D 202 ? GLY D 192 GLU D 202 
DB 7  ARG D 224 ? GLN D 228 ? ARG D 224 GLN D 228 
DB 8  GLN D 325 ? VAL D 331 ? GLN D 325 VAL D 331 
DB 9  ARG D 424 ? PHE D 430 ? ARG D 424 PHE D 430 
DB 10 GLN D 509 ? LEU D 513 ? GLN D 509 LEU D 513 
DB 11 GLU D 519 ? ARG D 522 ? GLU D 519 ARG D 522 
DC 1  VAL D 68  ? CYS D 69  ? VAL D 68  CYS D 69  
DC 2  LEU D 92  ? SER D 93  ? LEU D 92  SER D 93  
# 
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 
AA 1  2  N VAL A 12  ? N VAL A 12  O GLY A 15  ? O GLY A 15  
AA 2  3  N ARG A 18  ? N ARG A 18  O LEU A 60  ? O LEU A 60  
AB 1  2  N LEU A 22  ? N LEU A 22  O VAL A 29  ? O VAL A 29  
AB 2  3  N ILE A 35  ? N ILE A 35  O LEU A 99  ? O LEU A 99  
AB 3  4  N TRP A 102 ? N TRP A 102 O LEU A 146 ? O LEU A 146 
AB 4  5  N VAL A 147 ? N VAL A 147 O LEU A 115 ? O LEU A 115 
AB 5  6  N ILE A 116 ? N ILE A 116 O THR A 198 ? O THR A 198 
AB 6  7  N LEU A 199 ? N LEU A 199 O ARG A 224 ? O ARG A 224 
AB 7  8  N ALA A 225 ? N ALA A 225 O GLN A 325 ? O GLN A 325 
AB 8  9  N VAL A 326 ? N VAL A 326 O ARG A 424 ? O ARG A 424 
AB 9  10 N ILE A 429 ? N ILE A 429 O VAL A 511 ? O VAL A 511 
AB 10 11 N TYR A 510 ? N TYR A 510 O ARG A 521 ? O ARG A 521 
AC 1  2  O VAL A 68  ? O VAL A 68  N SER A 93  ? N SER A 93  
BA 1  2  N VAL B 10  ? N VAL B 10  O LEU B 17  ? O LEU B 17  
BA 2  3  N ARG B 18  ? N ARG B 18  O LEU B 60  ? O LEU B 60  
BB 1  2  N ALA B 24  ? N ALA B 24  O GLY B 27  ? O GLY B 27  
BB 2  3  N GLY B 34  ? N GLY B 34  O LEU B 99  ? O LEU B 99  
BB 3  4  N TRP B 102 ? N TRP B 102 O LEU B 146 ? O LEU B 146 
BB 4  5  N VAL B 145 ? N VAL B 145 O PRO B 113 ? O PRO B 113 
BB 5  6  O THR B 112 ? O THR B 112 N ASP B 193 ? N ASP B 193 
BB 6  7  N LEU B 199 ? N LEU B 199 O ARG B 224 ? O ARG B 224 
BB 7  8  N ALA B 225 ? N ALA B 225 O GLN B 325 ? O GLN B 325 
BB 8  9  N VAL B 326 ? N VAL B 326 O ARG B 424 ? O ARG B 424 
BB 9  10 N ILE B 429 ? N ILE B 429 O VAL B 511 ? O VAL B 511 
BB 10 11 N SER B 512 ? N SER B 512 O GLU B 519 ? O GLU B 519 
BC 1  2  O VAL B 68  ? O VAL B 68  N SER B 93  ? N SER B 93  
BD 1  2  O VAL B 239 ? O VAL B 239 N VAL B 303 ? N VAL B 303 
CA 1  2  N VAL C 12  ? N VAL C 12  O GLY C 15  ? O GLY C 15  
CA 2  3  N ARG C 18  ? N ARG C 18  O LEU C 60  ? O LEU C 60  
CB 1  2  N ALA C 24  ? N ALA C 24  O GLY C 27  ? O GLY C 27  
CB 2  3  N ILE C 35  ? N ILE C 35  O LEU C 99  ? O LEU C 99  
CB 3  4  N TRP C 102 ? N TRP C 102 O LEU C 146 ? O LEU C 146 
CB 4  5  N VAL C 145 ? N VAL C 145 O PRO C 113 ? O PRO C 113 
CB 5  6  O THR C 112 ? O THR C 112 N ASP C 193 ? N ASP C 193 
CB 6  7  N LEU C 199 ? N LEU C 199 O ARG C 224 ? O ARG C 224 
CB 7  8  N ALA C 225 ? N ALA C 225 O GLN C 325 ? O GLN C 325 
CB 8  9  N VAL C 326 ? N VAL C 326 O ARG C 424 ? O ARG C 424 
CB 9  10 N ILE C 429 ? N ILE C 429 O VAL C 511 ? O VAL C 511 
CB 10 11 N TYR C 510 ? N TYR C 510 O ARG C 521 ? O ARG C 521 
CC 1  2  O VAL C 68  ? O VAL C 68  N SER C 93  ? N SER C 93  
CD 1  2  O VAL C 239 ? O VAL C 239 N VAL C 303 ? N VAL C 303 
DA 1  2  N VAL D 12  ? N VAL D 12  O GLY D 15  ? O GLY D 15  
DA 2  3  N ARG D 18  ? N ARG D 18  O LEU D 60  ? O LEU D 60  
DB 1  2  N ALA D 24  ? N ALA D 24  O GLY D 27  ? O GLY D 27  
DB 2  3  N ILE D 35  ? N ILE D 35  O LEU D 99  ? O LEU D 99  
DB 3  4  N TRP D 102 ? N TRP D 102 O LEU D 146 ? O LEU D 146 
DB 4  5  N VAL D 145 ? N VAL D 145 O PRO D 113 ? O PRO D 113 
DB 5  6  O THR D 112 ? O THR D 112 N ASP D 193 ? N ASP D 193 
DB 6  7  N LEU D 199 ? N LEU D 199 O ARG D 224 ? O ARG D 224 
DB 7  8  N ALA D 225 ? N ALA D 225 O GLN D 325 ? O GLN D 325 
DB 8  9  N VAL D 326 ? N VAL D 326 O ARG D 424 ? O ARG D 424 
DB 9  10 N ILE D 429 ? N ILE D 429 O VAL D 511 ? O VAL D 511 
DB 10 11 N SER D 512 ? N SER D 512 O GLU D 519 ? O GLU D 519 
DC 1  2  O VAL D 68  ? O VAL D 68  N SER D 93  ? N SER D 93  
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE 4OJ A 600'                            
AC2 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE 4OJ B 600'                            
AC3 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE 4OJ C 600'                            
AC4 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG C 701'                            
AC5 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE 4OJ D 600'                            
AC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CL C 3000'                            
AC7 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE CL C 3001'                            
AC8 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE CL C 1544'                            
AC9 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE CL D 3001'                            
BC1 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE CL D 3002'                            
BC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE CL C 1545'                            
BC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 B 1544'                           
BC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 1544'                           
BC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 1545'                           
BC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 D 1544'                           
BC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 C 1546'                           
BC8 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE SO4 A 1546'                           
BC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 B 1545'                           
CC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 C 1547'                           
CC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 1547'                           
CC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 D 1545'                           
CC4 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE SO4 B 1546'                           
CC5 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE SO4 A 1548'                           
CC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE SO4 D 1546'                           
CC7 Software ? ? ? ? 1 'BINDING SITE FOR MONO-SACCHARIDE NAG A 701 BOUND TO ASN A 265' 
CC8 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG B 701 BOUND TO ASN B 265' 
CC9 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG B 702 BOUND TO ASN B 350' 
DC1 Software ? ? ? ? 1 'BINDING SITE FOR MONO-SACCHARIDE NAG D 701 BOUND TO ASN D 265' 
DC2 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG D 702 BOUND TO ASN D 350' 
DC3 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG D 703 BOUND TO ASN D 464' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 8 TRP A  86  ? TRP A 86   . ? 1_555 ? 
2  AC1 8 GLY A  121 ? GLY A 121  . ? 1_555 ? 
3  AC1 8 GLY A  122 ? GLY A 122  . ? 1_555 ? 
4  AC1 8 GLU A  202 ? GLU A 202  . ? 1_555 ? 
5  AC1 8 SER A  203 ? SER A 203  . ? 1_555 ? 
6  AC1 8 ALA A  204 ? ALA A 204  . ? 1_555 ? 
7  AC1 8 HOH KA .   ? HOH A 2042 . ? 1_555 ? 
8  AC1 8 HOH KA .   ? HOH A 2101 . ? 1_555 ? 
9  AC2 8 TRP B  86  ? TRP B 86   . ? 1_555 ? 
10 AC2 8 GLY B  121 ? GLY B 121  . ? 1_555 ? 
11 AC2 8 GLY B  122 ? GLY B 122  . ? 1_555 ? 
12 AC2 8 TYR B  124 ? TYR B 124  . ? 1_555 ? 
13 AC2 8 GLU B  202 ? GLU B 202  . ? 1_555 ? 
14 AC2 8 SER B  203 ? SER B 203  . ? 1_555 ? 
15 AC2 8 ALA B  204 ? ALA B 204  . ? 1_555 ? 
16 AC2 8 HIS B  447 ? HIS B 447  . ? 1_555 ? 
17 AC3 8 GLY C  121 ? GLY C 121  . ? 1_555 ? 
18 AC3 8 GLY C  122 ? GLY C 122  . ? 1_555 ? 
19 AC3 8 GLU C  202 ? GLU C 202  . ? 1_555 ? 
20 AC3 8 SER C  203 ? SER C 203  . ? 1_555 ? 
21 AC3 8 ALA C  204 ? ALA C 204  . ? 1_555 ? 
22 AC3 8 HIS C  447 ? HIS C 447  . ? 1_555 ? 
23 AC3 8 HOH MA .   ? HOH C 2048 . ? 1_555 ? 
24 AC3 8 HOH MA .   ? HOH C 2100 . ? 1_555 ? 
25 AC4 1 ASN C  265 ? ASN C 265  . ? 1_555 ? 
26 AC5 9 GLY D  121 ? GLY D 121  . ? 1_555 ? 
27 AC5 9 GLY D  122 ? GLY D 122  . ? 1_555 ? 
28 AC5 9 GLU D  202 ? GLU D 202  . ? 1_555 ? 
29 AC5 9 SER D  203 ? SER D 203  . ? 1_555 ? 
30 AC5 9 ALA D  204 ? ALA D 204  . ? 1_555 ? 
31 AC5 9 PHE D  295 ? PHE D 295  . ? 1_555 ? 
32 AC5 9 PHE D  297 ? PHE D 297  . ? 1_555 ? 
33 AC5 9 HIS D  447 ? HIS D 447  . ? 1_555 ? 
34 AC5 9 HOH NA .   ? HOH D 2088 . ? 1_555 ? 
35 AC6 2 ARG C  11  ? ARG C 11   . ? 1_555 ? 
36 AC6 2 HOH MA .   ? HOH C 2005 . ? 1_555 ? 
37 AC7 1 ARG C  136 ? ARG C 136  . ? 1_555 ? 
38 AC8 1 ARG C  356 ? ARG C 356  . ? 1_555 ? 
39 AC9 1 ARG D  136 ? ARG D 136  . ? 1_555 ? 
40 BC1 1 ARG D  90  ? ARG D 90   . ? 1_555 ? 
41 BC2 2 GLN C  413 ? GLN C 413  . ? 1_555 ? 
42 BC2 2 ARG C  417 ? ARG C 417  . ? 1_555 ? 
43 BC3 3 ARG B  525 ? ARG B 525  . ? 1_555 ? 
44 BC3 3 GLN B  527 ? GLN B 527  . ? 1_555 ? 
45 BC3 3 THR B  528 ? THR B 528  . ? 1_555 ? 
46 BC4 4 ARG A  525 ? ARG A 525  . ? 1_555 ? 
47 BC4 4 ALA A  526 ? ALA A 526  . ? 1_555 ? 
48 BC4 4 GLN A  527 ? GLN A 527  . ? 1_555 ? 
49 BC4 4 THR A  528 ? THR A 528  . ? 1_555 ? 
50 BC5 4 GLN A  413 ? GLN A 413  . ? 1_555 ? 
51 BC5 4 ARG A  417 ? ARG A 417  . ? 1_555 ? 
52 BC5 4 HOH KA .   ? HOH A 2113 . ? 1_555 ? 
53 BC5 4 HOH KA .   ? HOH A 2115 . ? 1_555 ? 
54 BC6 4 ARG D  525 ? ARG D 525  . ? 1_555 ? 
55 BC6 4 ALA D  526 ? ALA D 526  . ? 1_555 ? 
56 BC6 4 GLN D  527 ? GLN D 527  . ? 1_555 ? 
57 BC6 4 THR D  528 ? THR D 528  . ? 1_555 ? 
58 BC7 4 ARG C  525 ? ARG C 525  . ? 1_555 ? 
59 BC7 4 ALA C  526 ? ALA C 526  . ? 1_555 ? 
60 BC7 4 GLN C  527 ? GLN C 527  . ? 1_555 ? 
61 BC7 4 THR C  528 ? THR C 528  . ? 1_555 ? 
62 BC8 1 ARG A  356 ? ARG A 356  . ? 1_555 ? 
63 BC9 3 GLN B  413 ? GLN B 413  . ? 1_555 ? 
64 BC9 3 ARG B  417 ? ARG B 417  . ? 1_555 ? 
65 BC9 3 HOH LA .   ? HOH B 2082 . ? 1_555 ? 
66 CC1 5 LEU C  380 ? LEU C 380  . ? 1_555 ? 
67 CC1 5 HIS C  381 ? HIS C 381  . ? 1_555 ? 
68 CC1 5 PHE C  531 ? PHE C 531  . ? 1_555 ? 
69 CC1 5 LEU D  380 ? LEU D 380  . ? 1_555 ? 
70 CC1 5 HIS D  381 ? HIS D 381  . ? 1_555 ? 
71 CC2 4 LEU A  380 ? LEU A 380  . ? 1_555 ? 
72 CC2 4 HIS A  381 ? HIS A 381  . ? 1_555 ? 
73 CC2 4 LEU B  380 ? LEU B 380  . ? 1_555 ? 
74 CC2 4 HIS B  381 ? HIS B 381  . ? 1_555 ? 
75 CC3 3 HOH MA .   ? HOH C 2115 . ? 1_555 ? 
76 CC3 3 ARG D  356 ? ARG D 356  . ? 1_555 ? 
77 CC3 3 LEU D  360 ? LEU D 360  . ? 1_555 ? 
78 CC4 2 ARG B  356 ? ARG B 356  . ? 1_555 ? 
79 CC4 2 LEU B  360 ? LEU B 360  . ? 1_555 ? 
80 CC5 1 ARG A  136 ? ARG A 136  . ? 1_555 ? 
81 CC6 2 GLN D  413 ? GLN D 413  . ? 1_555 ? 
82 CC6 2 ARG D  417 ? ARG D 417  . ? 1_555 ? 
83 CC7 1 ASN A  265 ? ASN A 265  . ? 1_555 ? 
84 CC8 3 ASN B  265 ? ASN B 265  . ? 1_555 ? 
85 CC8 3 THR B  267 ? THR B 267  . ? 1_555 ? 
86 CC8 3 GLU B  268 ? GLU B 268  . ? 1_555 ? 
87 CC9 2 SER B  347 ? SER B 347  . ? 1_555 ? 
88 CC9 2 ASN B  350 ? ASN B 350  . ? 1_555 ? 
89 DC1 1 ASN D  265 ? ASN D 265  . ? 1_555 ? 
90 DC2 3 SER D  347 ? SER D 347  . ? 1_555 ? 
91 DC2 3 ASN D  350 ? ASN D 350  . ? 1_555 ? 
92 DC2 3 GLN D  358 ? GLN D 358  . ? 1_555 ? 
93 DC3 2 SER D  462 ? SER D 462  . ? 1_555 ? 
94 DC3 2 ASN D  464 ? ASN D 464  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4BC0 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    4BC0 
_atom_sites.fract_transf_matrix[1][1]   0.007302 
_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]   0.005746 
_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]   0.004432 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
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   . GLY A  1 2   ? 0.151   -69.524 11.288  1.00 67.84  ? 2    GLY A N   1 
ATOM   2     C  CA  . GLY A  1 2   ? 0.947   -68.329 11.064  1.00 72.06  ? 2    GLY A CA  1 
ATOM   3     C  C   . GLY A  1 2   ? 0.128   -67.092 10.717  1.00 78.11  ? 2    GLY A C   1 
ATOM   4     O  O   . GLY A  1 2   ? -0.956  -66.879 11.270  1.00 80.04  ? 2    GLY A O   1 
ATOM   5     N  N   . ARG A  1 3   ? 0.681   -66.252 9.840   1.00 105.69 ? 3    ARG A N   1 
ATOM   6     C  CA  . ARG A  1 3   ? 0.017   -65.054 9.291   1.00 107.33 ? 3    ARG A CA  1 
ATOM   7     C  C   . ARG A  1 3   ? -0.119  -63.892 10.296  1.00 100.02 ? 3    ARG A C   1 
ATOM   8     O  O   . ARG A  1 3   ? -0.281  -62.739 9.895   1.00 102.46 ? 3    ARG A O   1 
ATOM   9     C  CB  . ARG A  1 3   ? -1.348  -65.404 8.655   1.00 103.59 ? 3    ARG A CB  1 
ATOM   10    C  CG  . ARG A  1 3   ? -2.004  -64.301 7.800   1.00 105.81 ? 3    ARG A CG  1 
ATOM   11    C  CD  . ARG A  1 3   ? -1.278  -64.068 6.459   1.00 108.77 ? 3    ARG A CD  1 
ATOM   12    N  NE  . ARG A  1 3   ? -1.283  -65.248 5.586   1.00 111.19 ? 3    ARG A NE  1 
ATOM   13    C  CZ  . ARG A  1 3   ? -0.887  -65.250 4.312   1.00 110.42 ? 3    ARG A CZ  1 
ATOM   14    N  NH1 . ARG A  1 3   ? -0.453  -64.132 3.743   1.00 110.78 ? 3    ARG A NH1 1 
ATOM   15    N  NH2 . ARG A  1 3   ? -0.928  -66.371 3.600   1.00 108.83 ? 3    ARG A NH2 1 
ATOM   16    N  N   . GLU A  1 4   ? 0.010   -64.182 11.588  1.00 59.76  ? 4    GLU A N   1 
ATOM   17    C  CA  . GLU A  1 4   ? -0.161  -63.155 12.609  1.00 51.24  ? 4    GLU A CA  1 
ATOM   18    C  C   . GLU A  1 4   ? 1.174   -62.593 13.045  1.00 43.76  ? 4    GLU A C   1 
ATOM   19    O  O   . GLU A  1 4   ? 1.947   -63.288 13.684  1.00 45.34  ? 4    GLU A O   1 
ATOM   20    C  CB  . GLU A  1 4   ? -0.884  -63.716 13.842  1.00 71.74  ? 4    GLU A CB  1 
ATOM   21    C  CG  . GLU A  1 4   ? -2.389  -63.447 13.907  1.00 75.85  ? 4    GLU A CG  1 
ATOM   22    C  CD  . GLU A  1 4   ? -2.749  -61.988 14.211  1.00 77.53  ? 4    GLU A CD  1 
ATOM   23    O  OE1 . GLU A  1 4   ? -1.838  -61.120 14.225  1.00 78.63  ? 4    GLU A OE1 1 
ATOM   24    O  OE2 . GLU A  1 4   ? -3.959  -61.714 14.430  1.00 75.92  ? 4    GLU A OE2 1 
ATOM   25    N  N   . ASP A  1 5   ? 1.441   -61.333 12.724  1.00 42.20  ? 5    ASP A N   1 
ATOM   26    C  CA  . ASP A  1 5   ? 2.643   -60.666 13.213  1.00 37.39  ? 5    ASP A CA  1 
ATOM   27    C  C   . ASP A  1 5   ? 2.541   -60.559 14.736  1.00 33.77  ? 5    ASP A C   1 
ATOM   28    O  O   . ASP A  1 5   ? 1.635   -59.876 15.239  1.00 31.07  ? 5    ASP A O   1 
ATOM   29    C  CB  . ASP A  1 5   ? 2.725   -59.270 12.589  1.00 43.76  ? 5    ASP A CB  1 
ATOM   30    C  CG  . ASP A  1 5   ? 4.053   -58.571 12.843  1.00 42.56  ? 5    ASP A CG  1 
ATOM   31    O  OD1 . ASP A  1 5   ? 4.902   -59.108 13.592  1.00 40.73  ? 5    ASP A OD1 1 
ATOM   32    O  OD2 . ASP A  1 5   ? 4.232   -57.459 12.290  1.00 42.29  ? 5    ASP A OD2 1 
ATOM   33    N  N   . PRO A  1 6   ? 3.465   -61.231 15.473  1.00 38.44  ? 6    PRO A N   1 
ATOM   34    C  CA  . PRO A  1 6   ? 3.458   -61.258 16.945  1.00 37.20  ? 6    PRO A CA  1 
ATOM   35    C  C   . PRO A  1 6   ? 3.743   -59.876 17.518  1.00 34.31  ? 6    PRO A C   1 
ATOM   36    O  O   . PRO A  1 6   ? 3.552   -59.630 18.708  1.00 31.43  ? 6    PRO A O   1 
ATOM   37    C  CB  . PRO A  1 6   ? 4.594   -62.230 17.294  1.00 31.40  ? 6    PRO A CB  1 
ATOM   38    C  CG  . PRO A  1 6   ? 5.516   -62.157 16.150  1.00 33.50  ? 6    PRO A CG  1 
ATOM   39    C  CD  . PRO A  1 6   ? 4.627   -61.962 14.933  1.00 34.40  ? 6    PRO A CD  1 
ATOM   40    N  N   . GLN A  1 7   ? 4.221   -58.978 16.671  1.00 29.07  ? 7    GLN A N   1 
ATOM   41    C  CA  . GLN A  1 7   ? 4.453   -57.623 17.105  1.00 35.38  ? 7    GLN A CA  1 
ATOM   42    C  C   . GLN A  1 7   ? 3.142   -56.834 17.185  1.00 34.84  ? 7    GLN A C   1 
ATOM   43    O  O   . GLN A  1 7   ? 2.995   -55.930 18.010  1.00 36.43  ? 7    GLN A O   1 
ATOM   44    C  CB  . GLN A  1 7   ? 5.477   -56.941 16.197  1.00 28.18  ? 7    GLN A CB  1 
ATOM   45    C  CG  . GLN A  1 7   ? 6.689   -56.479 16.953  1.00 29.85  ? 7    GLN A CG  1 
ATOM   46    C  CD  . GLN A  1 7   ? 7.184   -57.548 17.904  1.00 33.62  ? 7    GLN A CD  1 
ATOM   47    O  OE1 . GLN A  1 7   ? 7.205   -57.371 19.132  1.00 34.42  ? 7    GLN A OE1 1 
ATOM   48    N  NE2 . GLN A  1 7   ? 7.570   -58.682 17.340  1.00 36.31  ? 7    GLN A NE2 1 
ATOM   49    N  N   . LEU A  1 8   ? 2.184   -57.164 16.330  1.00 29.79  ? 8    LEU A N   1 
ATOM   50    C  CA  . LEU A  1 8   ? 0.926   -56.425 16.343  1.00 29.74  ? 8    LEU A CA  1 
ATOM   51    C  C   . LEU A  1 8   ? -0.197  -57.056 17.192  1.00 27.90  ? 8    LEU A C   1 
ATOM   52    O  O   . LEU A  1 8   ? -1.221  -56.421 17.441  1.00 26.98  ? 8    LEU A O   1 
ATOM   53    C  CB  . LEU A  1 8   ? 0.461   -56.159 14.911  1.00 35.47  ? 8    LEU A CB  1 
ATOM   54    C  CG  . LEU A  1 8   ? 1.492   -55.501 13.992  1.00 27.95  ? 8    LEU A CG  1 
ATOM   55    C  CD1 . LEU A  1 8   ? 0.811   -55.031 12.712  1.00 28.51  ? 8    LEU A CD1 1 
ATOM   56    C  CD2 . LEU A  1 8   ? 2.204   -54.363 14.702  1.00 26.85  ? 8    LEU A CD2 1 
ATOM   57    N  N   . LEU A  1 9   ? 0.009   -58.294 17.635  1.00 28.43  ? 9    LEU A N   1 
ATOM   58    C  CA  . LEU A  1 9   ? -0.914  -58.982 18.529  1.00 27.62  ? 9    LEU A CA  1 
ATOM   59    C  C   . LEU A  1 9   ? -0.576  -58.624 19.969  1.00 26.67  ? 9    LEU A C   1 
ATOM   60    O  O   . LEU A  1 9   ? 0.575   -58.746 20.388  1.00 26.62  ? 9    LEU A O   1 
ATOM   61    C  CB  . LEU A  1 9   ? -0.770  -60.491 18.360  1.00 28.89  ? 9    LEU A CB  1 
ATOM   62    C  CG  . LEU A  1 9   ? -2.035  -61.314 18.125  1.00 35.67  ? 9    LEU A CG  1 
ATOM   63    C  CD1 . LEU A  1 9   ? -1.896  -62.755 18.640  1.00 35.25  ? 9    LEU A CD1 1 
ATOM   64    C  CD2 . LEU A  1 9   ? -3.232  -60.618 18.740  1.00 35.60  ? 9    LEU A CD2 1 
ATOM   65    N  N   . VAL A  1 10  ? -1.566  -58.173 20.733  1.00 26.03  ? 10   VAL A N   1 
ATOM   66    C  CA  . VAL A  1 10  ? -1.345  -57.884 22.147  1.00 25.26  ? 10   VAL A CA  1 
ATOM   67    C  C   . VAL A  1 10  ? -2.533  -58.375 22.937  1.00 26.70  ? 10   VAL A C   1 
ATOM   68    O  O   . VAL A  1 10  ? -3.671  -58.194 22.498  1.00 25.54  ? 10   VAL A O   1 
ATOM   69    C  CB  . VAL A  1 10  ? -1.181  -56.376 22.393  1.00 24.10  ? 10   VAL A CB  1 
ATOM   70    C  CG1 . VAL A  1 10  ? -1.088  -56.066 23.880  1.00 23.41  ? 10   VAL A CG1 1 
ATOM   71    C  CG2 . VAL A  1 10  ? 0.049   -55.867 21.685  1.00 40.36  ? 10   VAL A CG2 1 
ATOM   72    N  N   . ARG A  1 11  ? -2.283  -59.021 24.078  1.00 28.66  ? 11   ARG A N   1 
ATOM   73    C  CA  . ARG A  1 11  ? -3.373  -59.333 25.013  1.00 29.03  ? 11   ARG A CA  1 
ATOM   74    C  C   . ARG A  1 11  ? -3.336  -58.394 26.208  1.00 30.85  ? 11   ARG A C   1 
ATOM   75    O  O   . ARG A  1 11  ? -2.404  -58.435 27.022  1.00 32.38  ? 11   ARG A O   1 
ATOM   76    C  CB  . ARG A  1 11  ? -3.349  -60.790 25.502  1.00 26.74  ? 11   ARG A CB  1 
ATOM   77    C  CG  . ARG A  1 11  ? -4.446  -61.100 26.529  1.00 26.95  ? 11   ARG A CG  1 
ATOM   78    C  CD  . ARG A  1 11  ? -4.362  -62.501 27.125  1.00 28.08  ? 11   ARG A CD  1 
ATOM   79    N  NE  . ARG A  1 11  ? -3.209  -62.686 28.001  1.00 27.99  ? 11   ARG A NE  1 
ATOM   80    C  CZ  . ARG A  1 11  ? -3.146  -62.245 29.254  1.00 27.47  ? 11   ARG A CZ  1 
ATOM   81    N  NH1 . ARG A  1 11  ? -4.173  -61.589 29.772  1.00 26.97  ? 11   ARG A NH1 1 
ATOM   82    N  NH2 . ARG A  1 11  ? -2.059  -62.454 29.991  1.00 27.55  ? 11   ARG A NH2 1 
ATOM   83    N  N   . VAL A  1 12  ? -4.343  -57.536 26.308  1.00 24.10  ? 12   VAL A N   1 
ATOM   84    C  CA  . VAL A  1 12  ? -4.446  -56.683 27.473  1.00 23.29  ? 12   VAL A CA  1 
ATOM   85    C  C   . VAL A  1 12  ? -5.448  -57.312 28.425  1.00 23.79  ? 12   VAL A C   1 
ATOM   86    O  O   . VAL A  1 12  ? -6.098  -58.305 28.088  1.00 24.71  ? 12   VAL A O   1 
ATOM   87    C  CB  . VAL A  1 12  ? -4.904  -55.259 27.112  1.00 22.67  ? 12   VAL A CB  1 
ATOM   88    C  CG1 . VAL A  1 12  ? -3.945  -54.619 26.100  1.00 22.05  ? 12   VAL A CG1 1 
ATOM   89    C  CG2 . VAL A  1 12  ? -6.349  -55.278 26.607  1.00 22.79  ? 12   VAL A CG2 1 
ATOM   90    N  N   . ARG A  1 13  ? -5.588  -56.703 29.598  1.00 26.60  ? 13   ARG A N   1 
ATOM   91    C  CA  . ARG A  1 13  ? -6.398  -57.248 30.678  1.00 30.98  ? 13   ARG A CA  1 
ATOM   92    C  C   . ARG A  1 13  ? -7.780  -57.630 30.172  1.00 25.83  ? 13   ARG A C   1 
ATOM   93    O  O   . ARG A  1 13  ? -8.294  -58.684 30.513  1.00 25.39  ? 13   ARG A O   1 
ATOM   94    C  CB  . ARG A  1 13  ? -6.503  -56.233 31.824  1.00 56.18  ? 13   ARG A CB  1 
ATOM   95    C  CG  . ARG A  1 13  ? -6.842  -56.815 33.187  1.00 65.87  ? 13   ARG A CG  1 
ATOM   96    C  CD  . ARG A  1 13  ? -5.678  -57.590 33.781  1.00 72.97  ? 13   ARG A CD  1 
ATOM   97    N  NE  . ARG A  1 13  ? -4.507  -56.750 34.032  1.00 75.53  ? 13   ARG A NE  1 
ATOM   98    C  CZ  . ARG A  1 13  ? -4.325  -56.034 35.137  1.00 74.62  ? 13   ARG A CZ  1 
ATOM   99    N  NH1 . ARG A  1 13  ? -5.245  -56.039 36.094  1.00 73.60  ? 13   ARG A NH1 1 
ATOM   100   N  NH2 . ARG A  1 13  ? -3.224  -55.310 35.279  1.00 73.15  ? 13   ARG A NH2 1 
ATOM   101   N  N   . GLY A  1 14  ? -8.356  -56.798 29.319  1.00 24.02  ? 14   GLY A N   1 
ATOM   102   C  CA  . GLY A  1 14  ? -9.718  -57.020 28.884  1.00 24.67  ? 14   GLY A CA  1 
ATOM   103   C  C   . GLY A  1 14  ? -9.916  -57.925 27.680  1.00 25.59  ? 14   GLY A C   1 
ATOM   104   O  O   . GLY A  1 14  ? -11.054 -58.252 27.337  1.00 26.35  ? 14   GLY A O   1 
ATOM   105   N  N   . GLY A  1 15  ? -8.826  -58.328 27.030  1.00 33.70  ? 15   GLY A N   1 
ATOM   106   C  CA  . GLY A  1 15  ? -8.927  -59.129 25.815  1.00 34.78  ? 15   GLY A CA  1 
ATOM   107   C  C   . GLY A  1 15  ? -7.777  -58.951 24.825  1.00 34.33  ? 15   GLY A C   1 
ATOM   108   O  O   . GLY A  1 15  ? -6.761  -58.304 25.122  1.00 32.82  ? 15   GLY A O   1 
ATOM   109   N  N   . GLN A  1 16  ? -7.929  -59.534 23.639  1.00 28.12  ? 16   GLN A N   1 
ATOM   110   C  CA  . GLN A  1 16  ? -6.876  -59.452 22.638  1.00 27.08  ? 16   GLN A CA  1 
ATOM   111   C  C   . GLN A  1 16  ? -7.197  -58.463 21.542  1.00 28.11  ? 16   GLN A C   1 
ATOM   112   O  O   . GLN A  1 16  ? -8.313  -58.405 21.047  1.00 30.11  ? 16   GLN A O   1 
ATOM   113   C  CB  . GLN A  1 16  ? -6.614  -60.812 22.031  1.00 28.35  ? 16   GLN A CB  1 
ATOM   114   C  CG  . GLN A  1 16  ? -5.458  -61.503 22.664  1.00 28.46  ? 16   GLN A CG  1 
ATOM   115   C  CD  . GLN A  1 16  ? -5.324  -62.914 22.189  1.00 29.84  ? 16   GLN A CD  1 
ATOM   116   O  OE1 . GLN A  1 16  ? -5.642  -63.839 22.923  1.00 30.52  ? 16   GLN A OE1 1 
ATOM   117   N  NE2 . GLN A  1 16  ? -4.858  -63.101 20.949  1.00 30.38  ? 16   GLN A NE2 1 
ATOM   118   N  N   . LEU A  1 17  ? -6.208  -57.677 21.161  1.00 26.10  ? 17   LEU A N   1 
ATOM   119   C  CA  . LEU A  1 17  ? -6.390  -56.751 20.062  1.00 25.94  ? 17   LEU A CA  1 
ATOM   120   C  C   . LEU A  1 17  ? -5.213  -56.881 19.112  1.00 28.79  ? 17   LEU A C   1 
ATOM   121   O  O   . LEU A  1 17  ? -4.113  -57.284 19.515  1.00 28.39  ? 17   LEU A O   1 
ATOM   122   C  CB  . LEU A  1 17  ? -6.524  -55.321 20.582  1.00 24.76  ? 17   LEU A CB  1 
ATOM   123   C  CG  . LEU A  1 17  ? -5.456  -54.867 21.579  1.00 23.82  ? 17   LEU A CG  1 
ATOM   124   C  CD1 . LEU A  1 17  ? -4.269  -54.218 20.879  1.00 23.49  ? 17   LEU A CD1 1 
ATOM   125   C  CD2 . LEU A  1 17  ? -6.058  -53.943 22.603  1.00 22.96  ? 17   LEU A CD2 1 
ATOM   126   N  N   . ARG A  1 18  ? -5.453  -56.564 17.848  1.00 28.28  ? 18   ARG A N   1 
ATOM   127   C  CA  . ARG A  1 18  ? -4.389  -56.548 16.865  1.00 31.25  ? 18   ARG A CA  1 
ATOM   128   C  C   . ARG A  1 18  ? -4.274  -55.137 16.340  1.00 29.05  ? 18   ARG A C   1 
ATOM   129   O  O   . ARG A  1 18  ? -5.288  -54.531 15.976  1.00 28.68  ? 18   ARG A O   1 
ATOM   130   C  CB  . ARG A  1 18  ? -4.700  -57.505 15.724  1.00 50.46  ? 18   ARG A CB  1 
ATOM   131   C  CG  . ARG A  1 18  ? -4.204  -57.042 14.368  1.00 56.49  ? 18   ARG A CG  1 
ATOM   132   C  CD  . ARG A  1 18  ? -4.907  -57.781 13.237  1.00 62.74  ? 18   ARG A CD  1 
ATOM   133   N  NE  . ARG A  1 18  ? -6.356  -57.875 13.436  1.00 66.53  ? 18   ARG A NE  1 
ATOM   134   C  CZ  . ARG A  1 18  ? -6.992  -58.987 13.810  1.00 68.48  ? 18   ARG A CZ  1 
ATOM   135   N  NH1 . ARG A  1 18  ? -6.304  -60.112 14.024  1.00 65.76  ? 18   ARG A NH1 1 
ATOM   136   N  NH2 . ARG A  1 18  ? -8.316  -58.977 13.967  1.00 69.42  ? 18   ARG A NH2 1 
ATOM   137   N  N   . GLY A  1 19  ? -3.048  -54.612 16.328  1.00 31.20  ? 19   GLY A N   1 
ATOM   138   C  CA  . GLY A  1 19  ? -2.774  -53.287 15.799  1.00 25.43  ? 19   GLY A CA  1 
ATOM   139   C  C   . GLY A  1 19  ? -2.281  -53.293 14.364  1.00 27.12  ? 19   GLY A C   1 
ATOM   140   O  O   . GLY A  1 19  ? -2.487  -54.242 13.607  1.00 27.43  ? 19   GLY A O   1 
ATOM   141   N  N   . ILE A  1 20  ? -1.607  -52.220 13.984  1.00 33.22  ? 20   ILE A N   1 
ATOM   142   C  CA  . ILE A  1 20  ? -1.231  -52.025 12.593  1.00 35.69  ? 20   ILE A CA  1 
ATOM   143   C  C   . ILE A  1 20  ? 0.187   -51.456 12.484  1.00 34.46  ? 20   ILE A C   1 
ATOM   144   O  O   . ILE A  1 20  ? 0.619   -50.696 13.353  1.00 31.89  ? 20   ILE A O   1 
ATOM   145   C  CB  . ILE A  1 20  ? -2.255  -51.109 11.871  1.00 26.99  ? 20   ILE A CB  1 
ATOM   146   C  CG1 . ILE A  1 20  ? -2.014  -51.138 10.379  1.00 29.12  ? 20   ILE A CG1 1 
ATOM   147   C  CG2 . ILE A  1 20  ? -2.199  -49.676 12.385  1.00 25.91  ? 20   ILE A CG2 1 
ATOM   148   C  CD1 . ILE A  1 20  ? -2.480  -49.904 9.701   1.00 31.57  ? 20   ILE A CD1 1 
ATOM   149   N  N   . ARG A  1 21  ? 0.916   -51.837 11.434  1.00 35.07  ? 21   ARG A N   1 
ATOM   150   C  CA  . ARG A  1 21  ? 2.255   -51.294 11.214  1.00 37.89  ? 21   ARG A CA  1 
ATOM   151   C  C   . ARG A  1 21  ? 2.185   -50.054 10.340  1.00 39.96  ? 21   ARG A C   1 
ATOM   152   O  O   . ARG A  1 21  ? 1.697   -50.111 9.215   1.00 44.34  ? 21   ARG A O   1 
ATOM   153   C  CB  . ARG A  1 21  ? 3.173   -52.326 10.562  1.00 42.55  ? 21   ARG A CB  1 
ATOM   154   C  CG  . ARG A  1 21  ? 4.654   -52.096 10.831  1.00 42.52  ? 21   ARG A CG  1 
ATOM   155   C  CD  . ARG A  1 21  ? 5.514   -53.122 10.117  1.00 45.90  ? 21   ARG A CD  1 
ATOM   156   N  NE  . ARG A  1 21  ? 5.988   -52.630 8.829   1.00 53.39  ? 21   ARG A NE  1 
ATOM   157   C  CZ  . ARG A  1 21  ? 7.181   -52.917 8.313   1.00 62.30  ? 21   ARG A CZ  1 
ATOM   158   N  NH1 . ARG A  1 21  ? 8.023   -53.707 8.974   1.00 64.84  ? 21   ARG A NH1 1 
ATOM   159   N  NH2 . ARG A  1 21  ? 7.540   -52.420 7.133   1.00 66.06  ? 21   ARG A NH2 1 
ATOM   160   N  N   . LEU A  1 22  ? 2.671   -48.936 10.869  1.00 36.87  ? 22   LEU A N   1 
ATOM   161   C  CA  . LEU A  1 22  ? 2.665   -47.665 10.162  1.00 35.39  ? 22   LEU A CA  1 
ATOM   162   C  C   . LEU A  1 22  ? 4.072   -47.339 9.722   1.00 41.58  ? 22   LEU A C   1 
ATOM   163   O  O   . LEU A  1 22  ? 5.032   -47.748 10.381  1.00 39.49  ? 22   LEU A O   1 
ATOM   164   C  CB  . LEU A  1 22  ? 2.162   -46.548 11.066  1.00 25.88  ? 22   LEU A CB  1 
ATOM   165   C  CG  . LEU A  1 22  ? 0.726   -46.691 11.557  1.00 25.98  ? 22   LEU A CG  1 
ATOM   166   C  CD1 . LEU A  1 22  ? 0.202   -45.348 12.087  1.00 26.83  ? 22   LEU A CD1 1 
ATOM   167   C  CD2 . LEU A  1 22  ? -0.167  -47.253 10.456  1.00 26.46  ? 22   LEU A CD2 1 
ATOM   168   N  N   . LYS A  1 23  ? 4.198   -46.631 8.599   1.00 52.26  ? 23   LYS A N   1 
ATOM   169   C  CA  . LYS A  1 23  ? 5.501   -46.120 8.191   1.00 56.26  ? 23   LYS A CA  1 
ATOM   170   C  C   . LYS A  1 23  ? 5.669   -44.688 8.684   1.00 54.06  ? 23   LYS A C   1 
ATOM   171   O  O   . LYS A  1 23  ? 4.955   -43.778 8.269   1.00 54.62  ? 23   LYS A O   1 
ATOM   172   C  CB  . LYS A  1 23  ? 5.721   -46.219 6.671   1.00 66.66  ? 23   LYS A CB  1 
ATOM   173   C  CG  . LYS A  1 23  ? 6.198   -47.596 6.169   1.00 72.61  ? 23   LYS A CG  1 
ATOM   174   C  CD  . LYS A  1 23  ? 7.689   -47.870 6.465   1.00 74.93  ? 23   LYS A CD  1 
ATOM   175   C  CE  . LYS A  1 23  ? 8.072   -49.380 6.347   1.00 82.07  ? 23   LYS A CE  1 
ATOM   176   N  NZ  . LYS A  1 23  ? 8.079   -50.028 4.976   1.00 80.55  ? 23   LYS A NZ  1 
ATOM   177   N  N   . ALA A  1 24  ? 6.583   -44.523 9.630   1.00 52.06  ? 24   ALA A N   1 
ATOM   178   C  CA  . ALA A  1 24  ? 7.105   -43.226 10.013  1.00 48.82  ? 24   ALA A CA  1 
ATOM   179   C  C   . ALA A  1 24  ? 8.261   -42.959 9.064   1.00 48.78  ? 24   ALA A C   1 
ATOM   180   O  O   . ALA A  1 24  ? 8.737   -43.883 8.396   1.00 52.72  ? 24   ALA A O   1 
ATOM   181   C  CB  . ALA A  1 24  ? 7.587   -43.268 11.438  1.00 42.25  ? 24   ALA A CB  1 
ATOM   182   N  N   . PRO A  1 25  ? 8.708   -41.703 8.973   1.00 38.91  ? 25   PRO A N   1 
ATOM   183   C  CA  . PRO A  1 25  ? 9.773   -41.433 8.010   1.00 41.32  ? 25   PRO A CA  1 
ATOM   184   C  C   . PRO A  1 25  ? 11.023  -42.263 8.272   1.00 42.03  ? 25   PRO A C   1 
ATOM   185   O  O   . PRO A  1 25  ? 11.537  -42.908 7.355   1.00 41.34  ? 25   PRO A O   1 
ATOM   186   C  CB  . PRO A  1 25  ? 10.061  -39.949 8.240   1.00 40.45  ? 25   PRO A CB  1 
ATOM   187   C  CG  . PRO A  1 25  ? 8.740   -39.404 8.649   1.00 38.30  ? 25   PRO A CG  1 
ATOM   188   C  CD  . PRO A  1 25  ? 8.139   -40.463 9.520   1.00 36.36  ? 25   PRO A CD  1 
ATOM   189   N  N   . GLY A  1 26  ? 11.470  -42.290 9.522   1.00 44.68  ? 26   GLY A N   1 
ATOM   190   C  CA  . GLY A  1 26  ? 12.709  -42.969 9.855   1.00 45.01  ? 26   GLY A CA  1 
ATOM   191   C  C   . GLY A  1 26  ? 12.674  -44.482 9.733   1.00 44.47  ? 26   GLY A C   1 
ATOM   192   O  O   . GLY A  1 26  ? 13.620  -45.080 9.235   1.00 43.84  ? 26   GLY A O   1 
ATOM   193   N  N   . GLY A  1 27  ? 11.575  -45.091 10.172  1.00 53.65  ? 27   GLY A N   1 
ATOM   194   C  CA  . GLY A  1 27  ? 11.465  -46.536 10.303  1.00 56.18  ? 27   GLY A CA  1 
ATOM   195   C  C   . GLY A  1 27  ? 10.005  -46.939 10.357  1.00 56.63  ? 27   GLY A C   1 
ATOM   196   O  O   . GLY A  1 27  ? 9.144   -46.153 9.979   1.00 59.60  ? 27   GLY A O   1 
ATOM   197   N  N   . PRO A  1 28  ? 9.706   -48.192 10.729  1.00 46.03  ? 28   PRO A N   1 
ATOM   198   C  CA  . PRO A  1 28  ? 8.276   -48.405 10.922  1.00 41.40  ? 28   PRO A CA  1 
ATOM   199   C  C   . PRO A  1 28  ? 7.928   -48.236 12.397  1.00 38.08  ? 28   PRO A C   1 
ATOM   200   O  O   . PRO A  1 28  ? 8.853   -48.172 13.222  1.00 35.75  ? 28   PRO A O   1 
ATOM   201   C  CB  . PRO A  1 28  ? 8.094   -49.854 10.476  1.00 29.80  ? 28   PRO A CB  1 
ATOM   202   C  CG  . PRO A  1 28  ? 9.475   -50.504 10.669  1.00 30.42  ? 28   PRO A CG  1 
ATOM   203   C  CD  . PRO A  1 28  ? 10.476  -49.418 10.992  1.00 32.81  ? 28   PRO A CD  1 
ATOM   204   N  N   . VAL A  1 29  ? 6.630   -48.237 12.718  1.00 26.20  ? 29   VAL A N   1 
ATOM   205   C  CA  . VAL A  1 29  ? 6.134   -48.139 14.096  1.00 25.02  ? 29   VAL A CA  1 
ATOM   206   C  C   . VAL A  1 29  ? 4.887   -48.981 14.213  1.00 24.94  ? 29   VAL A C   1 
ATOM   207   O  O   . VAL A  1 29  ? 4.270   -49.338 13.210  1.00 25.65  ? 29   VAL A O   1 
ATOM   208   C  CB  . VAL A  1 29  ? 5.726   -46.707 14.539  1.00 24.07  ? 29   VAL A CB  1 
ATOM   209   C  CG1 . VAL A  1 29  ? 6.918   -45.778 14.666  1.00 24.06  ? 29   VAL A CG1 1 
ATOM   210   C  CG2 . VAL A  1 29  ? 4.690   -46.145 13.591  1.00 24.27  ? 29   VAL A CG2 1 
ATOM   211   N  N   . SER A  1 30  ? 4.530   -49.284 15.456  1.00 35.55  ? 30   SER A N   1 
ATOM   212   C  CA  . SER A  1 30  ? 3.359   -50.077 15.774  1.00 34.60  ? 30   SER A CA  1 
ATOM   213   C  C   . SER A  1 30  ? 2.312   -49.134 16.329  1.00 32.64  ? 30   SER A C   1 
ATOM   214   O  O   . SER A  1 30  ? 2.586   -48.383 17.266  1.00 34.73  ? 30   SER A O   1 
ATOM   215   C  CB  . SER A  1 30  ? 3.706   -51.131 16.830  1.00 39.52  ? 30   SER A CB  1 
ATOM   216   O  OG  . SER A  1 30  ? 4.902   -51.832 16.511  1.00 43.68  ? 30   SER A OG  1 
ATOM   217   N  N   . ALA A  1 31  ? 1.121   -49.158 15.742  1.00 23.38  ? 31   ALA A N   1 
ATOM   218   C  CA  . ALA A  1 31  ? 0.036   -48.309 16.202  1.00 22.65  ? 31   ALA A CA  1 
ATOM   219   C  C   . ALA A  1 31  ? -1.146  -49.167 16.612  1.00 22.77  ? 31   ALA A C   1 
ATOM   220   O  O   . ALA A  1 31  ? -1.587  -50.021 15.853  1.00 23.79  ? 31   ALA A O   1 
ATOM   221   C  CB  . ALA A  1 31  ? -0.372  -47.353 15.112  1.00 22.96  ? 31   ALA A CB  1 
ATOM   222   N  N   . PHE A  1 32  ? -1.661  -48.951 17.814  1.00 24.36  ? 32   PHE A N   1 
ATOM   223   C  CA  . PHE A  1 32  ? -2.840  -49.667 18.271  1.00 26.50  ? 32   PHE A CA  1 
ATOM   224   C  C   . PHE A  1 32  ? -3.903  -48.631 18.542  1.00 27.64  ? 32   PHE A C   1 
ATOM   225   O  O   . PHE A  1 32  ? -3.779  -47.879 19.489  1.00 29.02  ? 32   PHE A O   1 
ATOM   226   C  CB  . PHE A  1 32  ? -2.505  -50.457 19.537  1.00 21.81  ? 32   PHE A CB  1 
ATOM   227   C  CG  . PHE A  1 32  ? -1.371  -51.438 19.349  1.00 23.54  ? 32   PHE A CG  1 
ATOM   228   C  CD1 . PHE A  1 32  ? -0.051  -51.046 19.548  1.00 22.08  ? 32   PHE A CD1 1 
ATOM   229   C  CD2 . PHE A  1 32  ? -1.624  -52.741 18.947  1.00 23.28  ? 32   PHE A CD2 1 
ATOM   230   C  CE1 . PHE A  1 32  ? 0.992   -51.930 19.369  1.00 22.70  ? 32   PHE A CE1 1 
ATOM   231   C  CE2 . PHE A  1 32  ? -0.586  -53.626 18.757  1.00 23.88  ? 32   PHE A CE2 1 
ATOM   232   C  CZ  . PHE A  1 32  ? 0.729   -53.218 18.974  1.00 23.59  ? 32   PHE A CZ  1 
ATOM   233   N  N   . LEU A  1 33  ? -4.947  -48.588 17.720  1.00 22.16  ? 33   LEU A N   1 
ATOM   234   C  CA  . LEU A  1 33  ? -5.879  -47.461 17.742  1.00 21.84  ? 33   LEU A CA  1 
ATOM   235   C  C   . LEU A  1 33  ? -7.319  -47.839 18.040  1.00 22.15  ? 33   LEU A C   1 
ATOM   236   O  O   . LEU A  1 33  ? -7.876  -48.744 17.413  1.00 23.06  ? 33   LEU A O   1 
ATOM   237   C  CB  . LEU A  1 33  ? -5.867  -46.775 16.392  1.00 22.37  ? 33   LEU A CB  1 
ATOM   238   C  CG  . LEU A  1 33  ? -4.505  -46.475 15.791  1.00 26.26  ? 33   LEU A CG  1 
ATOM   239   C  CD1 . LEU A  1 33  ? -4.707  -45.915 14.403  1.00 29.38  ? 33   LEU A CD1 1 
ATOM   240   C  CD2 . LEU A  1 33  ? -3.746  -45.482 16.646  1.00 23.82  ? 33   LEU A CD2 1 
ATOM   241   N  N   . GLY A  1 34  ? -7.950  -47.123 18.964  1.00 23.36  ? 34   GLY A N   1 
ATOM   242   C  CA  . GLY A  1 34  ? -9.375  -47.329 19.180  1.00 26.04  ? 34   GLY A CA  1 
ATOM   243   C  C   . GLY A  1 34  ? -9.651  -48.461 20.142  1.00 26.44  ? 34   GLY A C   1 
ATOM   244   O  O   . GLY A  1 34  ? -10.673 -49.148 20.061  1.00 25.76  ? 34   GLY A O   1 
ATOM   245   N  N   . ILE A  1 35  ? -8.701  -48.650 21.049  1.00 21.40  ? 35   ILE A N   1 
ATOM   246   C  CA  . ILE A  1 35  ? -8.816  -49.603 22.129  1.00 21.44  ? 35   ILE A CA  1 
ATOM   247   C  C   . ILE A  1 35  ? -9.801  -49.019 23.109  1.00 26.71  ? 35   ILE A C   1 
ATOM   248   O  O   . ILE A  1 35  ? -9.553  -47.961 23.674  1.00 20.34  ? 35   ILE A O   1 
ATOM   249   C  CB  . ILE A  1 35  ? -7.457  -49.757 22.800  1.00 20.87  ? 35   ILE A CB  1 
ATOM   250   C  CG1 . ILE A  1 35  ? -6.400  -49.884 21.707  1.00 21.10  ? 35   ILE A CG1 1 
ATOM   251   C  CG2 . ILE A  1 35  ? -7.460  -50.913 23.788  1.00 21.13  ? 35   ILE A CG2 1 
ATOM   252   C  CD1 . ILE A  1 35  ? -5.063  -50.310 22.181  1.00 20.87  ? 35   ILE A CD1 1 
ATOM   253   N  N   . PRO A  1 36  ? -10.950 -49.674 23.282  1.00 21.81  ? 36   PRO A N   1 
ATOM   254   C  CA  . PRO A  1 36  ? -11.924 -49.118 24.228  1.00 29.60  ? 36   PRO A CA  1 
ATOM   255   C  C   . PRO A  1 36  ? -11.432 -49.218 25.671  1.00 28.40  ? 36   PRO A C   1 
ATOM   256   O  O   . PRO A  1 36  ? -11.086 -50.311 26.128  1.00 28.75  ? 36   PRO A O   1 
ATOM   257   C  CB  . PRO A  1 36  ? -13.133 -50.019 24.031  1.00 28.31  ? 36   PRO A CB  1 
ATOM   258   C  CG  . PRO A  1 36  ? -12.533 -51.336 23.584  1.00 31.55  ? 36   PRO A CG  1 
ATOM   259   C  CD  . PRO A  1 36  ? -11.351 -50.981 22.744  1.00 22.86  ? 36   PRO A CD  1 
ATOM   260   N  N   . PHE A  1 37  ? -11.409 -48.102 26.390  1.00 31.16  ? 37   PHE A N   1 
ATOM   261   C  CA  . PHE A  1 37  ? -11.030 -48.156 27.791  1.00 28.90  ? 37   PHE A CA  1 
ATOM   262   C  C   . PHE A  1 37  ? -12.246 -48.099 28.692  1.00 28.31  ? 37   PHE A C   1 
ATOM   263   O  O   . PHE A  1 37  ? -12.132 -48.216 29.914  1.00 29.05  ? 37   PHE A O   1 
ATOM   264   C  CB  . PHE A  1 37  ? -10.016 -47.067 28.152  1.00 24.34  ? 37   PHE A CB  1 
ATOM   265   C  CG  . PHE A  1 37  ? -10.563 -45.672 28.075  1.00 23.34  ? 37   PHE A CG  1 
ATOM   266   C  CD1 . PHE A  1 37  ? -10.536 -44.967 26.881  1.00 21.84  ? 37   PHE A CD1 1 
ATOM   267   C  CD2 . PHE A  1 37  ? -11.083 -45.054 29.202  1.00 23.43  ? 37   PHE A CD2 1 
ATOM   268   C  CE1 . PHE A  1 37  ? -11.032 -43.686 26.806  1.00 21.05  ? 37   PHE A CE1 1 
ATOM   269   C  CE2 . PHE A  1 37  ? -11.583 -43.770 29.134  1.00 22.54  ? 37   PHE A CE2 1 
ATOM   270   C  CZ  . PHE A  1 37  ? -11.561 -43.088 27.935  1.00 21.30  ? 37   PHE A CZ  1 
ATOM   271   N  N   . ALA A  1 38  ? -13.415 -47.924 28.092  1.00 23.25  ? 38   ALA A N   1 
ATOM   272   C  CA  . ALA A  1 38  ? -14.625 -47.793 28.892  1.00 25.07  ? 38   ALA A CA  1 
ATOM   273   C  C   . ALA A  1 38  ? -15.868 -48.244 28.155  1.00 30.27  ? 38   ALA A C   1 
ATOM   274   O  O   . ALA A  1 38  ? -15.953 -48.142 26.930  1.00 35.54  ? 38   ALA A O   1 
ATOM   275   C  CB  . ALA A  1 38  ? -14.793 -46.367 29.372  1.00 22.09  ? 38   ALA A CB  1 
ATOM   276   N  N   . GLU A  1 39  ? -16.835 -48.749 28.907  1.00 26.72  ? 39   GLU A N   1 
ATOM   277   C  CA  . GLU A  1 39  ? -18.120 -49.055 28.328  1.00 28.44  ? 39   GLU A CA  1 
ATOM   278   C  C   . GLU A  1 39  ? -18.707 -47.719 27.889  1.00 27.21  ? 39   GLU A C   1 
ATOM   279   O  O   . GLU A  1 39  ? -18.623 -46.746 28.646  1.00 26.54  ? 39   GLU A O   1 
ATOM   280   C  CB  . GLU A  1 39  ? -18.993 -49.769 29.355  1.00 39.71  ? 39   GLU A CB  1 
ATOM   281   C  CG  . GLU A  1 39  ? -18.708 -51.264 29.449  1.00 46.76  ? 39   GLU A CG  1 
ATOM   282   C  CD  . GLU A  1 39  ? -19.436 -52.069 28.366  1.00 55.35  ? 39   GLU A CD  1 
ATOM   283   O  OE1 . GLU A  1 39  ? -20.645 -51.798 28.139  1.00 59.88  ? 39   GLU A OE1 1 
ATOM   284   O  OE2 . GLU A  1 39  ? -18.808 -52.962 27.739  1.00 55.35  ? 39   GLU A OE2 1 
ATOM   285   N  N   . PRO A  1 40  ? -19.261 -47.657 26.654  1.00 27.38  ? 40   PRO A N   1 
ATOM   286   C  CA  . PRO A  1 40  ? -19.817 -46.438 26.042  1.00 28.09  ? 40   PRO A CA  1 
ATOM   287   C  C   . PRO A  1 40  ? -20.870 -45.747 26.892  1.00 28.37  ? 40   PRO A C   1 
ATOM   288   O  O   . PRO A  1 40  ? -21.875 -46.356 27.272  1.00 25.95  ? 40   PRO A O   1 
ATOM   289   C  CB  . PRO A  1 40  ? -20.483 -46.953 24.759  1.00 25.76  ? 40   PRO A CB  1 
ATOM   290   C  CG  . PRO A  1 40  ? -20.630 -48.409 24.958  1.00 27.27  ? 40   PRO A CG  1 
ATOM   291   C  CD  . PRO A  1 40  ? -19.410 -48.802 25.750  1.00 25.51  ? 40   PRO A CD  1 
ATOM   292   N  N   . PRO A  1 41  ? -20.655 -44.449 27.145  1.00 33.87  ? 41   PRO A N   1 
ATOM   293   C  CA  . PRO A  1 41  ? -21.493 -43.669 28.050  1.00 33.45  ? 41   PRO A CA  1 
ATOM   294   C  C   . PRO A  1 41  ? -22.721 -43.177 27.330  1.00 33.69  ? 41   PRO A C   1 
ATOM   295   O  O   . PRO A  1 41  ? -22.909 -41.968 27.240  1.00 36.90  ? 41   PRO A O   1 
ATOM   296   C  CB  . PRO A  1 41  ? -20.594 -42.483 28.407  1.00 27.75  ? 41   PRO A CB  1 
ATOM   297   C  CG  . PRO A  1 41  ? -19.710 -42.308 27.221  1.00 26.17  ? 41   PRO A CG  1 
ATOM   298   C  CD  . PRO A  1 41  ? -19.498 -43.678 26.645  1.00 27.04  ? 41   PRO A CD  1 
ATOM   299   N  N   . VAL A  1 42  ? -23.547 -44.085 26.825  1.00 26.62  ? 42   VAL A N   1 
ATOM   300   C  CA  . VAL A  1 42  ? -24.703 -43.656 26.045  1.00 29.73  ? 42   VAL A CA  1 
ATOM   301   C  C   . VAL A  1 42  ? -26.038 -44.043 26.671  1.00 34.00  ? 42   VAL A C   1 
ATOM   302   O  O   . VAL A  1 42  ? -26.111 -44.933 27.524  1.00 33.45  ? 42   VAL A O   1 
ATOM   303   C  CB  . VAL A  1 42  ? -24.655 -44.180 24.623  1.00 28.36  ? 42   VAL A CB  1 
ATOM   304   C  CG1 . VAL A  1 42  ? -23.236 -44.202 24.152  1.00 27.20  ? 42   VAL A CG1 1 
ATOM   305   C  CG2 . VAL A  1 42  ? -25.265 -45.556 24.555  1.00 29.52  ? 42   VAL A CG2 1 
ATOM   306   N  N   . GLY A  1 43  ? -27.091 -43.344 26.256  1.00 44.91  ? 43   GLY A N   1 
ATOM   307   C  CA  . GLY A  1 43  ? -28.400 -43.564 26.830  1.00 49.74  ? 43   GLY A CA  1 
ATOM   308   C  C   . GLY A  1 43  ? -28.401 -43.157 28.286  1.00 51.05  ? 43   GLY A C   1 
ATOM   309   O  O   . GLY A  1 43  ? -28.061 -42.023 28.615  1.00 53.01  ? 43   GLY A O   1 
ATOM   310   N  N   . SER A  1 44  ? -28.771 -44.091 29.154  1.00 46.83  ? 44   SER A N   1 
ATOM   311   C  CA  . SER A  1 44  ? -28.822 -43.842 30.591  1.00 45.99  ? 44   SER A CA  1 
ATOM   312   C  C   . SER A  1 44  ? -27.447 -43.596 31.222  1.00 42.64  ? 44   SER A C   1 
ATOM   313   O  O   . SER A  1 44  ? -27.352 -43.235 32.395  1.00 42.66  ? 44   SER A O   1 
ATOM   314   C  CB  . SER A  1 44  ? -29.544 -44.987 31.301  1.00 51.62  ? 44   SER A CB  1 
ATOM   315   O  OG  . SER A  1 44  ? -29.251 -46.231 30.683  1.00 54.53  ? 44   SER A OG  1 
ATOM   316   N  N   . ARG A  1 45  ? -26.383 -43.791 30.455  1.00 42.57  ? 45   ARG A N   1 
ATOM   317   C  CA  . ARG A  1 45  ? -25.057 -43.521 30.985  1.00 45.41  ? 45   ARG A CA  1 
ATOM   318   C  C   . ARG A  1 45  ? -24.558 -42.109 30.683  1.00 43.18  ? 45   ARG A C   1 
ATOM   319   O  O   . ARG A  1 45  ? -23.423 -41.771 31.027  1.00 44.86  ? 45   ARG A O   1 
ATOM   320   C  CB  . ARG A  1 45  ? -24.036 -44.564 30.517  1.00 53.44  ? 45   ARG A CB  1 
ATOM   321   C  CG  . ARG A  1 45  ? -24.159 -45.916 31.216  1.00 59.61  ? 45   ARG A CG  1 
ATOM   322   C  CD  . ARG A  1 45  ? -24.485 -45.768 32.707  1.00 64.18  ? 45   ARG A CD  1 
ATOM   323   N  NE  . ARG A  1 45  ? -23.313 -45.496 33.544  1.00 66.05  ? 45   ARG A NE  1 
ATOM   324   C  CZ  . ARG A  1 45  ? -23.356 -45.380 34.872  1.00 66.48  ? 45   ARG A CZ  1 
ATOM   325   N  NH1 . ARG A  1 45  ? -24.517 -45.509 35.506  1.00 70.98  ? 45   ARG A NH1 1 
ATOM   326   N  NH2 . ARG A  1 45  ? -22.248 -45.137 35.566  1.00 60.97  ? 45   ARG A NH2 1 
ATOM   327   N  N   . ARG A  1 46  ? -25.398 -41.291 30.047  1.00 31.17  ? 46   ARG A N   1 
ATOM   328   C  CA  . ARG A  1 46  ? -25.007 -39.926 29.670  1.00 26.13  ? 46   ARG A CA  1 
ATOM   329   C  C   . ARG A  1 46  ? -24.985 -39.035 30.905  1.00 25.74  ? 46   ARG A C   1 
ATOM   330   O  O   . ARG A  1 46  ? -25.889 -39.116 31.745  1.00 26.56  ? 46   ARG A O   1 
ATOM   331   C  CB  . ARG A  1 46  ? -25.947 -39.347 28.605  1.00 27.11  ? 46   ARG A CB  1 
ATOM   332   C  CG  . ARG A  1 46  ? -25.574 -37.959 28.103  1.00 26.56  ? 46   ARG A CG  1 
ATOM   333   C  CD  . ARG A  1 46  ? -26.767 -37.259 27.453  1.00 34.69  ? 46   ARG A CD  1 
ATOM   334   N  NE  . ARG A  1 46  ? -26.876 -37.483 26.009  1.00 35.20  ? 46   ARG A NE  1 
ATOM   335   C  CZ  . ARG A  1 46  ? -27.955 -37.197 25.272  1.00 35.02  ? 46   ARG A CZ  1 
ATOM   336   N  NH1 . ARG A  1 46  ? -29.048 -36.678 25.833  1.00 34.03  ? 46   ARG A NH1 1 
ATOM   337   N  NH2 . ARG A  1 46  ? -27.941 -37.433 23.962  1.00 34.35  ? 46   ARG A NH2 1 
ATOM   338   N  N   . PHE A  1 47  ? -23.935 -38.211 30.995  1.00 32.13  ? 47   PHE A N   1 
ATOM   339   C  CA  . PHE A  1 47  ? -23.629 -37.355 32.151  1.00 30.30  ? 47   PHE A CA  1 
ATOM   340   C  C   . PHE A  1 47  ? -22.982 -38.100 33.326  1.00 27.95  ? 47   PHE A C   1 
ATOM   341   O  O   . PHE A  1 47  ? -22.728 -37.502 34.365  1.00 26.50  ? 47   PHE A O   1 
ATOM   342   C  CB  . PHE A  1 47  ? -24.836 -36.548 32.639  1.00 28.78  ? 47   PHE A CB  1 
ATOM   343   C  CG  . PHE A  1 47  ? -25.552 -35.797 31.555  1.00 29.53  ? 47   PHE A CG  1 
ATOM   344   C  CD1 . PHE A  1 47  ? -24.955 -34.725 30.922  1.00 30.50  ? 47   PHE A CD1 1 
ATOM   345   C  CD2 . PHE A  1 47  ? -26.839 -36.143 31.196  1.00 29.55  ? 47   PHE A CD2 1 
ATOM   346   C  CE1 . PHE A  1 47  ? -25.633 -34.027 29.938  1.00 31.74  ? 47   PHE A CE1 1 
ATOM   347   C  CE2 . PHE A  1 47  ? -27.512 -35.444 30.216  1.00 27.77  ? 47   PHE A CE2 1 
ATOM   348   C  CZ  . PHE A  1 47  ? -26.911 -34.393 29.586  1.00 31.63  ? 47   PHE A CZ  1 
ATOM   349   N  N   . MET A  1 48  ? -22.748 -39.402 33.182  1.00 29.50  ? 48   MET A N   1 
ATOM   350   C  CA  . MET A  1 48  ? -22.339 -40.221 34.319  1.00 31.08  ? 48   MET A CA  1 
ATOM   351   C  C   . MET A  1 48  ? -20.894 -40.674 34.192  1.00 36.65  ? 48   MET A C   1 
ATOM   352   O  O   . MET A  1 48  ? -20.394 -40.839 33.078  1.00 40.40  ? 48   MET A O   1 
ATOM   353   C  CB  . MET A  1 48  ? -23.227 -41.464 34.411  1.00 24.65  ? 48   MET A CB  1 
ATOM   354   C  CG  . MET A  1 48  ? -24.716 -41.170 34.429  1.00 25.92  ? 48   MET A CG  1 
ATOM   355   S  SD  . MET A  1 48  ? -25.527 -41.679 35.958  1.00 65.54  ? 48   MET A SD  1 
ATOM   356   C  CE  . MET A  1 48  ? -24.193 -41.459 37.133  1.00 25.78  ? 48   MET A CE  1 
ATOM   357   N  N   . PRO A  1 49  ? -20.221 -40.887 35.340  1.00 34.11  ? 49   PRO A N   1 
ATOM   358   C  CA  . PRO A  1 49  ? -18.836 -41.370 35.375  1.00 30.43  ? 49   PRO A CA  1 
ATOM   359   C  C   . PRO A  1 49  ? -18.656 -42.648 34.575  1.00 29.66  ? 49   PRO A C   1 
ATOM   360   O  O   . PRO A  1 49  ? -19.560 -43.473 34.509  1.00 30.27  ? 49   PRO A O   1 
ATOM   361   C  CB  . PRO A  1 49  ? -18.580 -41.615 36.869  1.00 21.31  ? 49   PRO A CB  1 
ATOM   362   C  CG  . PRO A  1 49  ? -19.922 -41.591 37.511  1.00 22.36  ? 49   PRO A CG  1 
ATOM   363   C  CD  . PRO A  1 49  ? -20.729 -40.641 36.697  1.00 24.18  ? 49   PRO A CD  1 
ATOM   364   N  N   . PRO A  1 50  ? -17.496 -42.796 33.942  1.00 31.24  ? 50   PRO A N   1 
ATOM   365   C  CA  . PRO A  1 50  ? -17.321 -43.932 33.049  1.00 36.46  ? 50   PRO A CA  1 
ATOM   366   C  C   . PRO A  1 50  ? -17.280 -45.246 33.810  1.00 42.70  ? 50   PRO A C   1 
ATOM   367   O  O   . PRO A  1 50  ? -16.539 -45.352 34.786  1.00 44.30  ? 50   PRO A O   1 
ATOM   368   C  CB  . PRO A  1 50  ? -15.965 -43.648 32.404  1.00 31.00  ? 50   PRO A CB  1 
ATOM   369   C  CG  . PRO A  1 50  ? -15.257 -42.828 33.384  1.00 19.35  ? 50   PRO A CG  1 
ATOM   370   C  CD  . PRO A  1 50  ? -16.267 -42.005 34.084  1.00 19.69  ? 50   PRO A CD  1 
ATOM   371   N  N   . GLU A  1 51  ? -18.065 -46.225 33.368  1.00 39.00  ? 51   GLU A N   1 
ATOM   372   C  CA  . GLU A  1 51  ? -17.860 -47.600 33.791  1.00 41.75  ? 51   GLU A CA  1 
ATOM   373   C  C   . GLU A  1 51  ? -16.723 -48.163 32.933  1.00 40.18  ? 51   GLU A C   1 
ATOM   374   O  O   . GLU A  1 51  ? -16.652 -47.880 31.736  1.00 41.53  ? 51   GLU A O   1 
ATOM   375   C  CB  . GLU A  1 51  ? -19.129 -48.425 33.597  1.00 62.07  ? 51   GLU A CB  1 
ATOM   376   C  CG  . GLU A  1 51  ? -20.311 -47.986 34.451  1.00 71.58  ? 51   GLU A CG  1 
ATOM   377   C  CD  . GLU A  1 51  ? -21.589 -48.781 34.152  1.00 80.23  ? 51   GLU A CD  1 
ATOM   378   O  OE1 . GLU A  1 51  ? -22.190 -48.579 33.067  1.00 82.32  ? 51   GLU A OE1 1 
ATOM   379   O  OE2 . GLU A  1 51  ? -21.994 -49.607 35.005  1.00 82.57  ? 51   GLU A OE2 1 
ATOM   380   N  N   . PRO A  1 52  ? -15.830 -48.965 33.535  1.00 44.97  ? 52   PRO A N   1 
ATOM   381   C  CA  . PRO A  1 52  ? -14.681 -49.509 32.809  1.00 42.97  ? 52   PRO A CA  1 
ATOM   382   C  C   . PRO A  1 52  ? -15.112 -50.583 31.810  1.00 48.49  ? 52   PRO A C   1 
ATOM   383   O  O   . PRO A  1 52  ? -16.146 -51.230 32.005  1.00 52.35  ? 52   PRO A O   1 
ATOM   384   C  CB  . PRO A  1 52  ? -13.855 -50.128 33.922  1.00 21.86  ? 52   PRO A CB  1 
ATOM   385   C  CG  . PRO A  1 52  ? -14.873 -50.583 34.895  1.00 22.74  ? 52   PRO A CG  1 
ATOM   386   C  CD  . PRO A  1 52  ? -15.939 -49.543 34.885  1.00 22.76  ? 52   PRO A CD  1 
ATOM   387   N  N   . LYS A  1 53  ? -14.318 -50.766 30.756  1.00 45.66  ? 53   LYS A N   1 
ATOM   388   C  CA  . LYS A  1 53  ? -14.715 -51.592 29.613  1.00 40.15  ? 53   LYS A CA  1 
ATOM   389   C  C   . LYS A  1 53  ? -14.961 -53.027 30.006  1.00 36.04  ? 53   LYS A C   1 
ATOM   390   O  O   . LYS A  1 53  ? -14.108 -53.673 30.604  1.00 35.26  ? 53   LYS A O   1 
ATOM   391   C  CB  . LYS A  1 53  ? -13.663 -51.531 28.501  1.00 30.64  ? 53   LYS A CB  1 
ATOM   392   C  CG  . LYS A  1 53  ? -13.967 -52.424 27.310  1.00 30.42  ? 53   LYS A CG  1 
ATOM   393   C  CD  . LYS A  1 53  ? -15.333 -52.159 26.704  1.00 29.47  ? 53   LYS A CD  1 
ATOM   394   C  CE  . LYS A  1 53  ? -15.467 -52.854 25.352  1.00 30.39  ? 53   LYS A CE  1 
ATOM   395   N  NZ  . LYS A  1 53  ? -16.796 -53.507 25.184  1.00 32.31  ? 53   LYS A NZ  1 
ATOM   396   N  N   . ARG A  1 54  ? -16.140 -53.521 29.673  1.00 28.35  ? 54   ARG A N   1 
ATOM   397   C  CA  . ARG A  1 54  ? -16.437 -54.916 29.924  1.00 34.77  ? 54   ARG A CA  1 
ATOM   398   C  C   . ARG A  1 54  ? -15.648 -55.735 28.907  1.00 32.97  ? 54   ARG A C   1 
ATOM   399   O  O   . ARG A  1 54  ? -15.577 -55.367 27.723  1.00 33.05  ? 54   ARG A O   1 
ATOM   400   C  CB  . ARG A  1 54  ? -17.940 -55.180 29.814  1.00 57.07  ? 54   ARG A CB  1 
ATOM   401   C  CG  . ARG A  1 54  ? -18.653 -55.409 31.144  1.00 64.56  ? 54   ARG A CG  1 
ATOM   402   C  CD  . ARG A  1 54  ? -20.132 -55.069 31.016  1.00 73.23  ? 54   ARG A CD  1 
ATOM   403   N  NE  . ARG A  1 54  ? -20.665 -55.491 29.721  1.00 82.00  ? 54   ARG A NE  1 
ATOM   404   C  CZ  . ARG A  1 54  ? -21.680 -54.901 29.095  1.00 87.25  ? 54   ARG A CZ  1 
ATOM   405   N  NH1 . ARG A  1 54  ? -22.289 -53.850 29.646  1.00 86.96  ? 54   ARG A NH1 1 
ATOM   406   N  NH2 . ARG A  1 54  ? -22.083 -55.362 27.913  1.00 88.71  ? 54   ARG A NH2 1 
ATOM   407   N  N   . PRO A  1 55  ? -15.045 -56.848 29.365  1.00 27.83  ? 55   PRO A N   1 
ATOM   408   C  CA  . PRO A  1 55  ? -14.092 -57.637 28.580  1.00 27.72  ? 55   PRO A CA  1 
ATOM   409   C  C   . PRO A  1 55  ? -14.759 -58.323 27.401  1.00 29.73  ? 55   PRO A C   1 
ATOM   410   O  O   . PRO A  1 55  ? -15.951 -58.611 27.445  1.00 29.20  ? 55   PRO A O   1 
ATOM   411   C  CB  . PRO A  1 55  ? -13.594 -58.665 29.588  1.00 27.61  ? 55   PRO A CB  1 
ATOM   412   C  CG  . PRO A  1 55  ? -14.759 -58.863 30.469  1.00 28.36  ? 55   PRO A CG  1 
ATOM   413   C  CD  . PRO A  1 55  ? -15.336 -57.493 30.654  1.00 27.58  ? 55   PRO A CD  1 
ATOM   414   N  N   . TRP A  1 56  ? -13.966 -58.579 26.366  1.00 41.77  ? 56   TRP A N   1 
ATOM   415   C  CA  . TRP A  1 56  ? -14.459 -59.072 25.091  1.00 45.90  ? 56   TRP A CA  1 
ATOM   416   C  C   . TRP A  1 56  ? -13.707 -60.316 24.637  1.00 52.77  ? 56   TRP A C   1 
ATOM   417   O  O   . TRP A  1 56  ? -12.499 -60.452 24.873  1.00 56.23  ? 56   TRP A O   1 
ATOM   418   C  CB  . TRP A  1 56  ? -14.280 -57.994 24.031  1.00 32.33  ? 56   TRP A CB  1 
ATOM   419   C  CG  . TRP A  1 56  ? -12.827 -57.644 23.792  1.00 29.55  ? 56   TRP A CG  1 
ATOM   420   C  CD1 . TRP A  1 56  ? -11.977 -58.228 22.897  1.00 30.36  ? 56   TRP A CD1 1 
ATOM   421   C  CD2 . TRP A  1 56  ? -12.066 -56.639 24.467  1.00 26.23  ? 56   TRP A CD2 1 
ATOM   422   N  NE1 . TRP A  1 56  ? -10.743 -57.643 22.969  1.00 26.86  ? 56   TRP A NE1 1 
ATOM   423   C  CE2 . TRP A  1 56  ? -10.771 -56.666 23.924  1.00 25.84  ? 56   TRP A CE2 1 
ATOM   424   C  CE3 . TRP A  1 56  ? -12.357 -55.718 25.472  1.00 25.43  ? 56   TRP A CE3 1 
ATOM   425   C  CZ2 . TRP A  1 56  ? -9.766  -55.808 24.360  1.00 52.72  ? 56   TRP A CZ2 1 
ATOM   426   C  CZ3 . TRP A  1 56  ? -11.357 -54.862 25.898  1.00 24.28  ? 56   TRP A CZ3 1 
ATOM   427   C  CH2 . TRP A  1 56  ? -10.077 -54.917 25.347  1.00 23.94  ? 56   TRP A CH2 1 
ATOM   428   N  N   . SER A  1 57  ? -14.424 -61.216 23.968  1.00 51.65  ? 57   SER A N   1 
ATOM   429   C  CA  . SER A  1 57  ? -13.805 -62.394 23.378  1.00 50.78  ? 57   SER A CA  1 
ATOM   430   C  C   . SER A  1 57  ? -13.511 -62.089 21.929  1.00 44.75  ? 57   SER A C   1 
ATOM   431   O  O   . SER A  1 57  ? -13.947 -61.069 21.403  1.00 43.75  ? 57   SER A O   1 
ATOM   432   C  CB  . SER A  1 57  ? -14.768 -63.561 23.441  1.00 66.49  ? 57   SER A CB  1 
ATOM   433   O  OG  . SER A  1 57  ? -15.972 -63.198 22.784  1.00 72.27  ? 57   SER A OG  1 
ATOM   434   N  N   . GLY A  1 58  ? -12.829 -63.005 21.260  1.00 39.37  ? 58   GLY A N   1 
ATOM   435   C  CA  . GLY A  1 58  ? -12.290 -62.710 19.944  1.00 39.00  ? 58   GLY A CA  1 
ATOM   436   C  C   . GLY A  1 58  ? -11.149 -61.698 19.997  1.00 36.51  ? 58   GLY A C   1 
ATOM   437   O  O   . GLY A  1 58  ? -10.765 -61.211 21.084  1.00 32.33  ? 58   GLY A O   1 
ATOM   438   N  N   . VAL A  1 59  ? -10.599 -61.386 18.822  1.00 39.35  ? 59   VAL A N   1 
ATOM   439   C  CA  . VAL A  1 59  ? -9.572  -60.353 18.713  1.00 40.77  ? 59   VAL A CA  1 
ATOM   440   C  C   . VAL A  1 59  ? -10.108 -59.018 18.195  1.00 42.62  ? 59   VAL A C   1 
ATOM   441   O  O   . VAL A  1 59  ? -10.529 -58.906 17.047  1.00 42.04  ? 59   VAL A O   1 
ATOM   442   C  CB  . VAL A  1 59  ? -8.426  -60.796 17.835  1.00 30.75  ? 59   VAL A CB  1 
ATOM   443   C  CG1 . VAL A  1 59  ? -7.579  -59.614 17.455  1.00 31.90  ? 59   VAL A CG1 1 
ATOM   444   C  CG2 . VAL A  1 59  ? -7.604  -61.783 18.577  1.00 30.94  ? 59   VAL A CG2 1 
ATOM   445   N  N   . LEU A  1 60  ? -10.072 -58.009 19.060  1.00 55.21  ? 60   LEU A N   1 
ATOM   446   C  CA  . LEU A  1 60  ? -10.587 -56.681 18.766  1.00 56.06  ? 60   LEU A CA  1 
ATOM   447   C  C   . LEU A  1 60  ? -9.703  -55.973 17.753  1.00 61.16  ? 60   LEU A C   1 
ATOM   448   O  O   . LEU A  1 60  ? -8.483  -56.133 17.772  1.00 65.71  ? 60   LEU A O   1 
ATOM   449   C  CB  . LEU A  1 60  ? -10.631 -55.885 20.060  1.00 39.24  ? 60   LEU A CB  1 
ATOM   450   C  CG  . LEU A  1 60  ? -11.193 -54.476 20.012  1.00 36.32  ? 60   LEU A CG  1 
ATOM   451   C  CD1 . LEU A  1 60  ? -12.250 -54.313 21.105  1.00 35.88  ? 60   LEU A CD1 1 
ATOM   452   C  CD2 . LEU A  1 60  ? -10.056 -53.483 20.186  1.00 35.49  ? 60   LEU A CD2 1 
ATOM   453   N  N   . ASP A  1 61  ? -10.300 -55.185 16.866  1.00 51.40  ? 61   ASP A N   1 
ATOM   454   C  CA  . ASP A  1 61  ? -9.504  -54.585 15.805  1.00 49.83  ? 61   ASP A CA  1 
ATOM   455   C  C   . ASP A  1 61  ? -9.026  -53.188 16.160  1.00 46.23  ? 61   ASP A C   1 
ATOM   456   O  O   . ASP A  1 61  ? -9.787  -52.224 16.136  1.00 50.04  ? 61   ASP A O   1 
ATOM   457   C  CB  . ASP A  1 61  ? -10.298 -54.536 14.508  1.00 56.58  ? 61   ASP A CB  1 
ATOM   458   C  CG  . ASP A  1 61  ? -9.482  -54.008 13.357  1.00 60.06  ? 61   ASP A CG  1 
ATOM   459   O  OD1 . ASP A  1 61  ? -9.420  -52.772 13.204  1.00 59.81  ? 61   ASP A OD1 1 
ATOM   460   O  OD2 . ASP A  1 61  ? -8.894  -54.827 12.614  1.00 63.62  ? 61   ASP A OD2 1 
ATOM   461   N  N   . ALA A  1 62  ? -7.738  -53.085 16.446  1.00 29.85  ? 62   ALA A N   1 
ATOM   462   C  CA  . ALA A  1 62  ? -7.132  -51.831 16.856  1.00 25.69  ? 62   ALA A CA  1 
ATOM   463   C  C   . ALA A  1 62  ? -6.452  -51.078 15.724  1.00 30.03  ? 62   ALA A C   1 
ATOM   464   O  O   . ALA A  1 62  ? -5.655  -50.175 15.981  1.00 32.30  ? 62   ALA A O   1 
ATOM   465   C  CB  . ALA A  1 62  ? -6.196  -52.040 17.990  1.00 29.46  ? 62   ALA A CB  1 
ATOM   466   N  N   . THR A  1 63  ? -6.678  -51.511 14.486  1.00 36.17  ? 63   THR A N   1 
ATOM   467   C  CA  . THR A  1 63  ? -6.008  -50.922 13.320  1.00 38.33  ? 63   THR A CA  1 
ATOM   468   C  C   . THR A  1 63  ? -6.438  -49.514 12.932  1.00 40.02  ? 63   THR A C   1 
ATOM   469   O  O   . THR A  1 63  ? -5.857  -48.929 12.024  1.00 38.78  ? 63   THR A O   1 
ATOM   470   C  CB  . THR A  1 63  ? -6.209  -51.765 12.064  1.00 51.27  ? 63   THR A CB  1 
ATOM   471   O  OG1 . THR A  1 63  ? -7.609  -51.979 11.859  1.00 51.45  ? 63   THR A OG1 1 
ATOM   472   C  CG2 . THR A  1 63  ? -5.501  -53.096 12.195  1.00 56.08  ? 63   THR A CG2 1 
ATOM   473   N  N   . THR A  1 64  ? -7.456  -48.961 13.574  1.00 59.58  ? 64   THR A N   1 
ATOM   474   C  CA  . THR A  1 64  ? -7.917  -47.668 13.109  1.00 59.58  ? 64   THR A CA  1 
ATOM   475   C  C   . THR A  1 64  ? -8.584  -46.793 14.160  1.00 58.05  ? 64   THR A C   1 
ATOM   476   O  O   . THR A  1 64  ? -9.144  -47.311 15.128  1.00 59.42  ? 64   THR A O   1 
ATOM   477   C  CB  . THR A  1 64  ? -8.875  -47.846 11.948  1.00 55.47  ? 64   THR A CB  1 
ATOM   478   O  OG1 . THR A  1 64  ? -9.224  -46.553 11.446  1.00 61.07  ? 64   THR A OG1 1 
ATOM   479   C  CG2 . THR A  1 64  ? -10.130 -48.611 12.403  1.00 50.21  ? 64   THR A CG2 1 
ATOM   480   N  N   . PHE A  1 65  ? -8.538  -45.472 13.934  1.00 47.01  ? 65   PHE A N   1 
ATOM   481   C  CA  . PHE A  1 65  ? -9.082  -44.465 14.861  1.00 41.49  ? 65   PHE A CA  1 
ATOM   482   C  C   . PHE A  1 65  ? -10.567 -44.645 15.069  1.00 42.44  ? 65   PHE A C   1 
ATOM   483   O  O   . PHE A  1 65  ? -11.279 -45.104 14.177  1.00 46.20  ? 65   PHE A O   1 
ATOM   484   C  CB  . PHE A  1 65  ? -8.825  -43.025 14.382  1.00 30.35  ? 65   PHE A CB  1 
ATOM   485   C  CG  . PHE A  1 65  ? -7.448  -42.502 14.710  1.00 29.59  ? 65   PHE A CG  1 
ATOM   486   C  CD1 . PHE A  1 65  ? -7.114  -42.153 16.002  1.00 28.05  ? 65   PHE A CD1 1 
ATOM   487   C  CD2 . PHE A  1 65  ? -6.481  -42.362 13.717  1.00 32.18  ? 65   PHE A CD2 1 
ATOM   488   C  CE1 . PHE A  1 65  ? -5.839  -41.683 16.300  1.00 28.88  ? 65   PHE A CE1 1 
ATOM   489   C  CE2 . PHE A  1 65  ? -5.203  -41.889 14.009  1.00 31.26  ? 65   PHE A CE2 1 
ATOM   490   C  CZ  . PHE A  1 65  ? -4.886  -41.546 15.299  1.00 29.94  ? 65   PHE A CZ  1 
ATOM   491   N  N   . GLN A  1 66  ? -11.028 -44.271 16.257  1.00 35.86  ? 66   GLN A N   1 
ATOM   492   C  CA  . GLN A  1 66  ? -12.432 -44.398 16.608  1.00 32.57  ? 66   GLN A CA  1 
ATOM   493   C  C   . GLN A  1 66  ? -13.177 -43.070 16.559  1.00 35.25  ? 66   GLN A C   1 
ATOM   494   O  O   . GLN A  1 66  ? -12.611 -42.032 16.205  1.00 39.26  ? 66   GLN A O   1 
ATOM   495   C  CB  . GLN A  1 66  ? -12.571 -45.028 17.982  1.00 23.03  ? 66   GLN A CB  1 
ATOM   496   C  CG  . GLN A  1 66  ? -12.680 -46.522 17.930  1.00 25.18  ? 66   GLN A CG  1 
ATOM   497   C  CD  . GLN A  1 66  ? -14.087 -46.994 17.594  1.00 30.04  ? 66   GLN A CD  1 
ATOM   498   O  OE1 . GLN A  1 66  ? -14.934 -46.221 17.132  1.00 29.91  ? 66   GLN A OE1 1 
ATOM   499   N  NE2 . GLN A  1 66  ? -14.350 -48.270 17.851  1.00 33.15  ? 66   GLN A NE2 1 
ATOM   500   N  N   . ASN A  1 67  ? -14.455 -43.112 16.912  1.00 26.83  ? 67   ASN A N   1 
ATOM   501   C  CA  . ASN A  1 67  ? -15.289 -41.929 16.848  1.00 26.47  ? 67   ASN A CA  1 
ATOM   502   C  C   . ASN A  1 67  ? -14.817 -40.833 17.769  1.00 25.51  ? 67   ASN A C   1 
ATOM   503   O  O   . ASN A  1 67  ? -14.251 -41.091 18.839  1.00 22.26  ? 67   ASN A O   1 
ATOM   504   C  CB  . ASN A  1 67  ? -16.715 -42.277 17.213  1.00 38.07  ? 67   ASN A CB  1 
ATOM   505   C  CG  . ASN A  1 67  ? -17.216 -43.421 16.429  1.00 47.01  ? 67   ASN A CG  1 
ATOM   506   O  OD1 . ASN A  1 67  ? -16.964 -43.505 15.234  1.00 51.78  ? 67   ASN A OD1 1 
ATOM   507   N  ND2 . ASN A  1 67  ? -17.902 -44.343 17.090  1.00 50.46  ? 67   ASN A ND2 1 
ATOM   508   N  N   . VAL A  1 68  ? -15.080 -39.605 17.334  1.00 28.19  ? 68   VAL A N   1 
ATOM   509   C  CA  . VAL A  1 68  ? -14.796 -38.414 18.101  1.00 26.92  ? 68   VAL A CA  1 
ATOM   510   C  C   . VAL A  1 68  ? -15.987 -38.087 18.994  1.00 27.05  ? 68   VAL A C   1 
ATOM   511   O  O   . VAL A  1 68  ? -17.132 -38.231 18.577  1.00 31.09  ? 68   VAL A O   1 
ATOM   512   C  CB  . VAL A  1 68  ? -14.524 -37.260 17.155  1.00 37.95  ? 68   VAL A CB  1 
ATOM   513   C  CG1 . VAL A  1 68  ? -14.417 -35.975 17.921  1.00 39.88  ? 68   VAL A CG1 1 
ATOM   514   C  CG2 . VAL A  1 68  ? -13.246 -37.525 16.374  1.00 38.29  ? 68   VAL A CG2 1 
ATOM   515   N  N   . CYS A  1 69  ? -15.716 -37.673 20.228  1.00 28.13  ? 69   CYS A N   1 
ATOM   516   C  CA  . CYS A  1 69  ? -16.772 -37.324 21.167  1.00 27.81  ? 69   CYS A CA  1 
ATOM   517   C  C   . CYS A  1 69  ? -17.597 -36.191 20.619  1.00 29.62  ? 69   CYS A C   1 
ATOM   518   O  O   . CYS A  1 69  ? -17.073 -35.297 19.955  1.00 33.82  ? 69   CYS A O   1 
ATOM   519   C  CB  . CYS A  1 69  ? -16.184 -36.950 22.518  1.00 20.83  ? 69   CYS A CB  1 
ATOM   520   S  SG  . CYS A  1 69  ? -15.402 -38.357 23.336  1.00 57.68  ? 69   CYS A SG  1 
ATOM   521   N  N   . TYR A  1 70  ? -18.893 -36.242 20.890  1.00 23.75  ? 70   TYR A N   1 
ATOM   522   C  CA  . TYR A  1 70  ? -19.838 -35.310 20.298  1.00 24.22  ? 70   TYR A CA  1 
ATOM   523   C  C   . TYR A  1 70  ? -19.512 -33.866 20.621  1.00 23.76  ? 70   TYR A C   1 
ATOM   524   O  O   . TYR A  1 70  ? -19.368 -33.505 21.787  1.00 32.94  ? 70   TYR A O   1 
ATOM   525   C  CB  . TYR A  1 70  ? -21.232 -35.638 20.784  1.00 27.87  ? 70   TYR A CB  1 
ATOM   526   C  CG  . TYR A  1 70  ? -22.156 -35.788 19.644  1.00 26.47  ? 70   TYR A CG  1 
ATOM   527   C  CD1 . TYR A  1 70  ? -22.771 -34.684 19.095  1.00 34.56  ? 70   TYR A CD1 1 
ATOM   528   C  CD2 . TYR A  1 70  ? -22.377 -37.028 19.079  1.00 35.70  ? 70   TYR A CD2 1 
ATOM   529   C  CE1 . TYR A  1 70  ? -23.603 -34.807 18.032  1.00 40.24  ? 70   TYR A CE1 1 
ATOM   530   C  CE2 . TYR A  1 70  ? -23.209 -37.177 18.014  1.00 39.70  ? 70   TYR A CE2 1 
ATOM   531   C  CZ  . TYR A  1 70  ? -23.828 -36.060 17.484  1.00 45.70  ? 70   TYR A CZ  1 
ATOM   532   O  OH  . TYR A  1 70  ? -24.684 -36.193 16.403  1.00 53.47  ? 70   TYR A OH  1 
ATOM   533   N  N   . GLN A  1 71  ? -19.398 -33.028 19.599  1.00 24.23  ? 71   GLN A N   1 
ATOM   534   C  CA  . GLN A  1 71  ? -18.956 -31.656 19.844  1.00 27.99  ? 71   GLN A CA  1 
ATOM   535   C  C   . GLN A  1 71  ? -19.388 -30.607 18.827  1.00 30.96  ? 71   GLN A C   1 
ATOM   536   O  O   . GLN A  1 71  ? -19.834 -30.918 17.720  1.00 33.98  ? 71   GLN A O   1 
ATOM   537   C  CB  . GLN A  1 71  ? -17.428 -31.592 20.029  1.00 28.02  ? 71   GLN A CB  1 
ATOM   538   C  CG  . GLN A  1 71  ? -16.609 -31.680 18.750  1.00 25.59  ? 71   GLN A CG  1 
ATOM   539   C  CD  . GLN A  1 71  ? -15.324 -32.433 18.968  1.00 24.17  ? 71   GLN A CD  1 
ATOM   540   O  OE1 . GLN A  1 71  ? -14.246 -31.978 18.594  1.00 25.61  ? 71   GLN A OE1 1 
ATOM   541   N  NE2 . GLN A  1 71  ? -15.429 -33.591 19.593  1.00 21.66  ? 71   GLN A NE2 1 
ATOM   542   N  N   . TYR A  1 72  ? -19.258 -29.350 19.228  1.00 35.41  ? 72   TYR A N   1 
ATOM   543   C  CA  . TYR A  1 72  ? -19.464 -28.250 18.315  1.00 41.21  ? 72   TYR A CA  1 
ATOM   544   C  C   . TYR A  1 72  ? -18.361 -28.292 17.260  1.00 41.11  ? 72   TYR A C   1 
ATOM   545   O  O   . TYR A  1 72  ? -17.179 -28.445 17.594  1.00 38.73  ? 72   TYR A O   1 
ATOM   546   C  CB  . TYR A  1 72  ? -19.465 -26.931 19.088  1.00 58.38  ? 72   TYR A CB  1 
ATOM   547   C  CG  . TYR A  1 72  ? -19.518 -25.699 18.222  1.00 65.08  ? 72   TYR A CG  1 
ATOM   548   C  CD1 . TYR A  1 72  ? -20.705 -25.291 17.622  1.00 68.09  ? 72   TYR A CD1 1 
ATOM   549   C  CD2 . TYR A  1 72  ? -18.376 -24.933 18.013  1.00 67.36  ? 72   TYR A CD2 1 
ATOM   550   C  CE1 . TYR A  1 72  ? -20.747 -24.157 16.827  1.00 70.57  ? 72   TYR A CE1 1 
ATOM   551   C  CE2 . TYR A  1 72  ? -18.408 -23.801 17.226  1.00 69.14  ? 72   TYR A CE2 1 
ATOM   552   C  CZ  . TYR A  1 72  ? -19.590 -23.415 16.634  1.00 70.57  ? 72   TYR A CZ  1 
ATOM   553   O  OH  . TYR A  1 72  ? -19.599 -22.284 15.849  1.00 71.11  ? 72   TYR A OH  1 
ATOM   554   N  N   . VAL A  1 73  ? -18.758 -28.210 15.989  1.00 46.83  ? 73   VAL A N   1 
ATOM   555   C  CA  . VAL A  1 73  ? -17.798 -28.118 14.888  1.00 46.19  ? 73   VAL A CA  1 
ATOM   556   C  C   . VAL A  1 73  ? -17.679 -26.668 14.436  1.00 48.94  ? 73   VAL A C   1 
ATOM   557   O  O   . VAL A  1 73  ? -18.656 -26.073 13.973  1.00 48.53  ? 73   VAL A O   1 
ATOM   558   C  CB  . VAL A  1 73  ? -18.209 -28.975 13.682  1.00 38.73  ? 73   VAL A CB  1 
ATOM   559   C  CG1 . VAL A  1 73  ? -17.206 -28.808 12.547  1.00 35.78  ? 73   VAL A CG1 1 
ATOM   560   C  CG2 . VAL A  1 73  ? -18.336 -30.430 14.080  1.00 38.53  ? 73   VAL A CG2 1 
ATOM   561   N  N   . ASP A  1 74  ? -16.477 -26.111 14.560  1.00 48.55  ? 74   ASP A N   1 
ATOM   562   C  CA  . ASP A  1 74  ? -16.286 -24.676 14.415  1.00 53.33  ? 74   ASP A CA  1 
ATOM   563   C  C   . ASP A  1 74  ? -16.478 -24.167 12.986  1.00 57.75  ? 74   ASP A C   1 
ATOM   564   O  O   . ASP A  1 74  ? -15.818 -24.612 12.042  1.00 57.47  ? 74   ASP A O   1 
ATOM   565   C  CB  . ASP A  1 74  ? -14.925 -24.251 14.962  1.00 61.12  ? 74   ASP A CB  1 
ATOM   566   C  CG  . ASP A  1 74  ? -14.621 -22.797 14.671  1.00 66.41  ? 74   ASP A CG  1 
ATOM   567   O  OD1 . ASP A  1 74  ? -15.272 -21.916 15.273  1.00 66.33  ? 74   ASP A OD1 1 
ATOM   568   O  OD2 . ASP A  1 74  ? -13.736 -22.535 13.830  1.00 70.12  ? 74   ASP A OD2 1 
ATOM   569   N  N   . THR A  1 75  ? -17.418 -23.236 12.853  1.00 77.59  ? 75   THR A N   1 
ATOM   570   C  CA  . THR A  1 75  ? -17.796 -22.661 11.567  1.00 80.62  ? 75   THR A CA  1 
ATOM   571   C  C   . THR A  1 75  ? -17.215 -21.281 11.238  1.00 79.80  ? 75   THR A C   1 
ATOM   572   O  O   . THR A  1 75  ? -17.623 -20.681 10.244  1.00 84.06  ? 75   THR A O   1 
ATOM   573   C  CB  . THR A  1 75  ? -19.330 -22.653 11.371  1.00 78.45  ? 75   THR A CB  1 
ATOM   574   O  OG1 . THR A  1 75  ? -19.972 -23.303 12.480  1.00 77.32  ? 75   THR A OG1 1 
ATOM   575   C  CG2 . THR A  1 75  ? -19.688 -23.381 10.084  1.00 80.46  ? 75   THR A CG2 1 
ATOM   576   N  N   . LEU A  1 76  ? -16.322 -20.757 12.079  1.00 68.75  ? 76   LEU A N   1 
ATOM   577   C  CA  . LEU A  1 76  ? -15.818 -19.388 11.887  1.00 66.90  ? 76   LEU A CA  1 
ATOM   578   C  C   . LEU A  1 76  ? -15.261 -19.096 10.497  1.00 71.22  ? 76   LEU A C   1 
ATOM   579   O  O   . LEU A  1 76  ? -15.820 -18.287 9.755   1.00 76.38  ? 76   LEU A O   1 
ATOM   580   C  CB  . LEU A  1 76  ? -14.773 -18.992 12.934  1.00 44.82  ? 76   LEU A CB  1 
ATOM   581   C  CG  . LEU A  1 76  ? -14.121 -17.623 12.630  1.00 38.84  ? 76   LEU A CG  1 
ATOM   582   C  CD1 . LEU A  1 76  ? -15.151 -16.478 12.510  1.00 37.55  ? 76   LEU A CD1 1 
ATOM   583   C  CD2 . LEU A  1 76  ? -13.028 -17.257 13.625  1.00 33.85  ? 76   LEU A CD2 1 
ATOM   584   N  N   . TYR A  1 77  ? -14.151 -19.729 10.152  1.00 61.77  ? 77   TYR A N   1 
ATOM   585   C  CA  . TYR A  1 77  ? -13.563 -19.504 8.844   1.00 65.22  ? 77   TYR A CA  1 
ATOM   586   C  C   . TYR A  1 77  ? -13.548 -20.827 8.092   1.00 65.65  ? 77   TYR A C   1 
ATOM   587   O  O   . TYR A  1 77  ? -12.566 -21.560 8.169   1.00 68.87  ? 77   TYR A O   1 
ATOM   588   C  CB  . TYR A  1 77  ? -12.118 -19.016 8.966   1.00 72.97  ? 77   TYR A CB  1 
ATOM   589   C  CG  . TYR A  1 77  ? -11.887 -17.623 9.520   1.00 73.91  ? 77   TYR A CG  1 
ATOM   590   C  CD1 . TYR A  1 77  ? -12.373 -16.496 8.872   1.00 75.34  ? 77   TYR A CD1 1 
ATOM   591   C  CD2 . TYR A  1 77  ? -11.111 -17.438 10.659  1.00 74.23  ? 77   TYR A CD2 1 
ATOM   592   C  CE1 . TYR A  1 77  ? -12.124 -15.222 9.373   1.00 77.46  ? 77   TYR A CE1 1 
ATOM   593   C  CE2 . TYR A  1 77  ? -10.857 -16.175 11.167  1.00 75.15  ? 77   TYR A CE2 1 
ATOM   594   C  CZ  . TYR A  1 77  ? -11.362 -15.067 10.526  1.00 76.17  ? 77   TYR A CZ  1 
ATOM   595   O  OH  . TYR A  1 77  ? -11.097 -13.812 11.046  1.00 74.59  ? 77   TYR A OH  1 
ATOM   596   N  N   . PRO A  1 78  ? -14.632 -21.149 7.365   1.00 64.81  ? 78   PRO A N   1 
ATOM   597   C  CA  . PRO A  1 78  ? -14.708 -22.466 6.719   1.00 63.34  ? 78   PRO A CA  1 
ATOM   598   C  C   . PRO A  1 78  ? -13.609 -22.687 5.672   1.00 63.25  ? 78   PRO A C   1 
ATOM   599   O  O   . PRO A  1 78  ? -13.166 -21.737 5.022   1.00 63.57  ? 78   PRO A O   1 
ATOM   600   C  CB  . PRO A  1 78  ? -16.093 -22.453 6.060   1.00 55.17  ? 78   PRO A CB  1 
ATOM   601   C  CG  . PRO A  1 78  ? -16.860 -21.405 6.786   1.00 54.57  ? 78   PRO A CG  1 
ATOM   602   C  CD  . PRO A  1 78  ? -15.849 -20.356 7.129   1.00 55.51  ? 78   PRO A CD  1 
ATOM   603   N  N   . GLY A  1 79  ? -13.172 -23.937 5.534   1.00 59.92  ? 79   GLY A N   1 
ATOM   604   C  CA  . GLY A  1 79  ? -12.148 -24.312 4.572   1.00 60.23  ? 79   GLY A CA  1 
ATOM   605   C  C   . GLY A  1 79  ? -10.827 -23.607 4.792   1.00 59.79  ? 79   GLY A C   1 
ATOM   606   O  O   . GLY A  1 79  ? -10.129 -23.274 3.840   1.00 62.65  ? 79   GLY A O   1 
ATOM   607   N  N   . PHE A  1 80  ? -10.490 -23.381 6.054   1.00 63.79  ? 80   PHE A N   1 
ATOM   608   C  CA  . PHE A  1 80  ? -9.294  -22.637 6.423   1.00 62.84  ? 80   PHE A CA  1 
ATOM   609   C  C   . PHE A  1 80  ? -8.452  -23.467 7.388   1.00 67.85  ? 80   PHE A C   1 
ATOM   610   O  O   . PHE A  1 80  ? -8.908  -23.781 8.491   1.00 71.73  ? 80   PHE A O   1 
ATOM   611   C  CB  . PHE A  1 80  ? -9.702  -21.302 7.052   1.00 44.89  ? 80   PHE A CB  1 
ATOM   612   C  CG  . PHE A  1 80  ? -8.590  -20.589 7.751   1.00 43.50  ? 80   PHE A CG  1 
ATOM   613   C  CD1 . PHE A  1 80  ? -7.418  -20.275 7.083   1.00 45.77  ? 80   PHE A CD1 1 
ATOM   614   C  CD2 . PHE A  1 80  ? -8.719  -20.212 9.070   1.00 44.97  ? 80   PHE A CD2 1 
ATOM   615   C  CE1 . PHE A  1 80  ? -6.377  -19.612 7.728   1.00 46.60  ? 80   PHE A CE1 1 
ATOM   616   C  CE2 . PHE A  1 80  ? -7.686  -19.549 9.722   1.00 47.55  ? 80   PHE A CE2 1 
ATOM   617   C  CZ  . PHE A  1 80  ? -6.509  -19.252 9.048   1.00 47.19  ? 80   PHE A CZ  1 
ATOM   618   N  N   . GLU A  1 81  ? -7.233  -23.819 6.971   1.00 59.78  ? 81   GLU A N   1 
ATOM   619   C  CA  . GLU A  1 81  ? -6.375  -24.739 7.731   1.00 59.32  ? 81   GLU A CA  1 
ATOM   620   C  C   . GLU A  1 81  ? -6.274  -24.396 9.229   1.00 58.38  ? 81   GLU A C   1 
ATOM   621   O  O   . GLU A  1 81  ? -6.356  -25.282 10.086  1.00 56.34  ? 81   GLU A O   1 
ATOM   622   C  CB  . GLU A  1 81  ? -4.965  -24.825 7.108   1.00 61.95  ? 81   GLU A CB  1 
ATOM   623   C  CG  . GLU A  1 81  ? -4.000  -25.805 7.828   1.00 113.33 ? 81   GLU A CG  1 
ATOM   624   C  CD  . GLU A  1 81  ? -2.566  -25.267 7.999   1.00 112.46 ? 81   GLU A CD  1 
ATOM   625   O  OE1 . GLU A  1 81  ? -2.289  -24.580 9.011   1.00 110.69 ? 81   GLU A OE1 1 
ATOM   626   O  OE2 . GLU A  1 81  ? -1.708  -25.549 7.133   1.00 112.64 ? 81   GLU A OE2 1 
ATOM   627   N  N   . GLY A  1 82  ? -6.118  -23.110 9.534   1.00 65.23  ? 82   GLY A N   1 
ATOM   628   C  CA  . GLY A  1 82  ? -5.951  -22.657 10.904  1.00 63.38  ? 82   GLY A CA  1 
ATOM   629   C  C   . GLY A  1 82  ? -7.047  -23.099 11.859  1.00 60.81  ? 82   GLY A C   1 
ATOM   630   O  O   . GLY A  1 82  ? -6.768  -23.546 12.974  1.00 61.59  ? 82   GLY A O   1 
ATOM   631   N  N   . THR A  1 83  ? -8.298  -22.943 11.438  1.00 46.31  ? 83   THR A N   1 
ATOM   632   C  CA  . THR A  1 83  ? -9.427  -23.363 12.254  1.00 45.71  ? 83   THR A CA  1 
ATOM   633   C  C   . THR A  1 83  ? -9.733  -24.839 12.122  1.00 46.06  ? 83   THR A C   1 
ATOM   634   O  O   . THR A  1 83  ? -10.154 -25.471 13.095  1.00 48.14  ? 83   THR A O   1 
ATOM   635   C  CB  . THR A  1 83  ? -10.703 -22.596 11.908  1.00 60.06  ? 83   THR A CB  1 
ATOM   636   O  OG1 . THR A  1 83  ? -10.659 -22.208 10.532  1.00 63.38  ? 83   THR A OG1 1 
ATOM   637   C  CG2 . THR A  1 83  ? -10.835 -21.363 12.782  1.00 61.95  ? 83   THR A CG2 1 
ATOM   638   N  N   . GLU A  1 84  ? -9.539  -25.387 10.923  1.00 42.38  ? 84   GLU A N   1 
ATOM   639   C  CA  . GLU A  1 84  ? -10.061 -26.721 10.621  1.00 46.27  ? 84   GLU A CA  1 
ATOM   640   C  C   . GLU A  1 84  ? -9.109  -27.891 10.914  1.00 45.21  ? 84   GLU A C   1 
ATOM   641   O  O   . GLU A  1 84  ? -9.503  -29.067 10.856  1.00 42.41  ? 84   GLU A O   1 
ATOM   642   C  CB  . GLU A  1 84  ? -10.621 -26.766 9.199   1.00 71.61  ? 84   GLU A CB  1 
ATOM   643   C  CG  . GLU A  1 84  ? -11.713 -25.731 8.996   1.00 79.28  ? 84   GLU A CG  1 
ATOM   644   C  CD  . GLU A  1 84  ? -12.483 -25.914 7.706   1.00 87.54  ? 84   GLU A CD  1 
ATOM   645   O  OE1 . GLU A  1 84  ? -11.976 -26.604 6.792   1.00 90.72  ? 84   GLU A OE1 1 
ATOM   646   O  OE2 . GLU A  1 84  ? -13.603 -25.359 7.609   1.00 89.65  ? 84   GLU A OE2 1 
ATOM   647   N  N   . MET A  1 85  ? -7.866  -27.571 11.259  1.00 63.18  ? 85   MET A N   1 
ATOM   648   C  CA  . MET A  1 85  ? -6.950  -28.597 11.729  1.00 62.62  ? 85   MET A CA  1 
ATOM   649   C  C   . MET A  1 85  ? -7.525  -29.168 13.015  1.00 62.66  ? 85   MET A C   1 
ATOM   650   O  O   . MET A  1 85  ? -7.377  -30.352 13.303  1.00 65.01  ? 85   MET A O   1 
ATOM   651   C  CB  . MET A  1 85  ? -5.537  -28.031 11.945  1.00 51.39  ? 85   MET A CB  1 
ATOM   652   C  CG  . MET A  1 85  ? -5.372  -27.065 13.115  1.00 48.09  ? 85   MET A CG  1 
ATOM   653   S  SD  . MET A  1 85  ? -3.860  -26.067 13.035  1.00 66.60  ? 85   MET A SD  1 
ATOM   654   C  CE  . MET A  1 85  ? -2.613  -27.309 12.686  1.00 49.19  ? 85   MET A CE  1 
ATOM   655   N  N   . TRP A  1 86  ? -8.225  -28.312 13.754  1.00 49.98  ? 86   TRP A N   1 
ATOM   656   C  CA  . TRP A  1 86  ? -8.725  -28.628 15.081  1.00 45.63  ? 86   TRP A CA  1 
ATOM   657   C  C   . TRP A  1 86  ? -10.024 -29.423 15.032  1.00 44.47  ? 86   TRP A C   1 
ATOM   658   O  O   . TRP A  1 86  ? -10.376 -30.098 16.001  1.00 46.08  ? 86   TRP A O   1 
ATOM   659   C  CB  . TRP A  1 86  ? -8.901  -27.337 15.899  1.00 47.57  ? 86   TRP A CB  1 
ATOM   660   C  CG  . TRP A  1 86  ? -7.651  -26.472 15.934  1.00 51.22  ? 86   TRP A CG  1 
ATOM   661   C  CD1 . TRP A  1 86  ? -7.477  -25.251 15.337  1.00 54.00  ? 86   TRP A CD1 1 
ATOM   662   C  CD2 . TRP A  1 86  ? -6.405  -26.775 16.576  1.00 50.85  ? 86   TRP A CD2 1 
ATOM   663   N  NE1 . TRP A  1 86  ? -6.208  -24.776 15.574  1.00 52.19  ? 86   TRP A NE1 1 
ATOM   664   C  CE2 . TRP A  1 86  ? -5.531  -25.692 16.333  1.00 51.66  ? 86   TRP A CE2 1 
ATOM   665   C  CE3 . TRP A  1 86  ? -5.947  -27.850 17.337  1.00 51.99  ? 86   TRP A CE3 1 
ATOM   666   C  CZ2 . TRP A  1 86  ? -4.232  -25.658 16.822  1.00 53.80  ? 86   TRP A CZ2 1 
ATOM   667   C  CZ3 . TRP A  1 86  ? -4.654  -27.814 17.822  1.00 53.71  ? 86   TRP A CZ3 1 
ATOM   668   C  CH2 . TRP A  1 86  ? -3.811  -26.726 17.561  1.00 54.28  ? 86   TRP A CH2 1 
ATOM   669   N  N   . ASN A  1 87  ? -10.722 -29.364 13.900  1.00 41.27  ? 87   ASN A N   1 
ATOM   670   C  CA  . ASN A  1 87  ? -12.067 -29.946 13.794  1.00 42.36  ? 87   ASN A CA  1 
ATOM   671   C  C   . ASN A  1 87  ? -12.052 -31.470 13.665  1.00 38.81  ? 87   ASN A C   1 
ATOM   672   O  O   . ASN A  1 87  ? -11.105 -32.026 13.107  1.00 38.07  ? 87   ASN A O   1 
ATOM   673   C  CB  . ASN A  1 87  ? -12.848 -29.312 12.629  1.00 53.50  ? 87   ASN A CB  1 
ATOM   674   C  CG  . ASN A  1 87  ? -13.408 -27.930 12.965  1.00 56.23  ? 87   ASN A CG  1 
ATOM   675   O  OD1 . ASN A  1 87  ? -13.593 -27.574 14.137  1.00 57.96  ? 87   ASN A OD1 1 
ATOM   676   N  ND2 . ASN A  1 87  ? -13.694 -27.149 11.928  1.00 55.87  ? 87   ASN A ND2 1 
ATOM   677   N  N   . PRO A  1 88  ? -13.116 -32.145 14.157  1.00 43.57  ? 88   PRO A N   1 
ATOM   678   C  CA  . PRO A  1 88  ? -13.198 -33.615 14.216  1.00 41.29  ? 88   PRO A CA  1 
ATOM   679   C  C   . PRO A  1 88  ? -12.908 -34.286 12.881  1.00 42.47  ? 88   PRO A C   1 
ATOM   680   O  O   . PRO A  1 88  ? -13.534 -33.952 11.889  1.00 48.04  ? 88   PRO A O   1 
ATOM   681   C  CB  . PRO A  1 88  ? -14.672 -33.859 14.546  1.00 33.84  ? 88   PRO A CB  1 
ATOM   682   C  CG  . PRO A  1 88  ? -15.094 -32.663 15.293  1.00 34.85  ? 88   PRO A CG  1 
ATOM   683   C  CD  . PRO A  1 88  ? -14.298 -31.504 14.765  1.00 36.08  ? 88   PRO A CD  1 
ATOM   684   N  N   . ASN A  1 89  ? -11.969 -35.219 12.855  1.00 33.61  ? 89   ASN A N   1 
ATOM   685   C  CA  . ASN A  1 89  ? -11.660 -35.940 11.624  1.00 38.36  ? 89   ASN A CA  1 
ATOM   686   C  C   . ASN A  1 89  ? -12.229 -37.360 11.487  1.00 40.80  ? 89   ASN A C   1 
ATOM   687   O  O   . ASN A  1 89  ? -11.918 -38.069 10.531  1.00 44.55  ? 89   ASN A O   1 
ATOM   688   C  CB  . ASN A  1 89  ? -10.161 -35.934 11.349  1.00 49.68  ? 89   ASN A CB  1 
ATOM   689   C  CG  . ASN A  1 89  ? -9.382  -36.644 12.409  1.00 49.35  ? 89   ASN A CG  1 
ATOM   690   O  OD1 . ASN A  1 89  ? -9.960  -37.260 13.301  1.00 44.92  ? 89   ASN A OD1 1 
ATOM   691   N  ND2 . ASN A  1 89  ? -8.058  -36.566 12.324  1.00 52.57  ? 89   ASN A ND2 1 
ATOM   692   N  N   . ARG A  1 90  ? -13.001 -37.800 12.470  1.00 40.68  ? 90   ARG A N   1 
ATOM   693   C  CA  . ARG A  1 90  ? -13.745 -39.047 12.342  1.00 37.99  ? 90   ARG A CA  1 
ATOM   694   C  C   . ARG A  1 90  ? -15.178 -38.709 12.697  1.00 41.21  ? 90   ARG A C   1 
ATOM   695   O  O   . ARG A  1 90  ? -15.473 -37.564 13.035  1.00 41.02  ? 90   ARG A O   1 
ATOM   696   C  CB  . ARG A  1 90  ? -13.197 -40.127 13.273  1.00 31.34  ? 90   ARG A CB  1 
ATOM   697   C  CG  . ARG A  1 90  ? -11.826 -40.633 12.899  1.00 30.31  ? 90   ARG A CG  1 
ATOM   698   C  CD  . ARG A  1 90  ? -11.853 -41.325 11.561  1.00 35.55  ? 90   ARG A CD  1 
ATOM   699   N  NE  . ARG A  1 90  ? -10.594 -42.003 11.252  1.00 41.96  ? 90   ARG A NE  1 
ATOM   700   C  CZ  . ARG A  1 90  ? -9.525  -41.400 10.727  1.00 47.40  ? 90   ARG A CZ  1 
ATOM   701   N  NH1 . ARG A  1 90  ? -9.557  -40.091 10.467  1.00 47.29  ? 90   ARG A NH1 1 
ATOM   702   N  NH2 . ARG A  1 90  ? -8.418  -42.101 10.465  1.00 48.90  ? 90   ARG A NH2 1 
ATOM   703   N  N   . GLU A  1 91  ? -16.070 -39.690 12.631  1.00 46.33  ? 91   GLU A N   1 
ATOM   704   C  CA  . GLU A  1 91  ? -17.487 -39.410 12.828  1.00 50.11  ? 91   GLU A CA  1 
ATOM   705   C  C   . GLU A  1 91  ? -17.847 -39.162 14.290  1.00 42.74  ? 91   GLU A C   1 
ATOM   706   O  O   . GLU A  1 91  ? -17.313 -39.796 15.197  1.00 41.94  ? 91   GLU A O   1 
ATOM   707   C  CB  . GLU A  1 91  ? -18.349 -40.518 12.232  1.00 76.51  ? 91   GLU A CB  1 
ATOM   708   C  CG  . GLU A  1 91  ? -19.464 -40.000 11.348  1.00 88.85  ? 91   GLU A CG  1 
ATOM   709   C  CD  . GLU A  1 91  ? -20.340 -41.115 10.821  1.00 100.06 ? 91   GLU A CD  1 
ATOM   710   O  OE1 . GLU A  1 91  ? -19.849 -42.266 10.744  1.00 102.53 ? 91   GLU A OE1 1 
ATOM   711   O  OE2 . GLU A  1 91  ? -21.516 -40.841 10.488  1.00 104.42 ? 91   GLU A OE2 1 
ATOM   712   N  N   . LEU A  1 92  ? -18.755 -38.220 14.501  1.00 34.88  ? 92   LEU A N   1 
ATOM   713   C  CA  . LEU A  1 92  ? -19.211 -37.856 15.831  1.00 32.68  ? 92   LEU A CA  1 
ATOM   714   C  C   . LEU A  1 92  ? -20.068 -38.950 16.453  1.00 35.01  ? 92   LEU A C   1 
ATOM   715   O  O   . LEU A  1 92  ? -21.049 -39.386 15.849  1.00 39.30  ? 92   LEU A O   1 
ATOM   716   C  CB  . LEU A  1 92  ? -20.056 -36.586 15.745  1.00 27.32  ? 92   LEU A CB  1 
ATOM   717   C  CG  . LEU A  1 92  ? -19.396 -35.212 15.789  1.00 26.70  ? 92   LEU A CG  1 
ATOM   718   C  CD1 . LEU A  1 92  ? -20.163 -34.381 16.778  1.00 41.17  ? 92   LEU A CD1 1 
ATOM   719   C  CD2 . LEU A  1 92  ? -17.923 -35.258 16.171  1.00 25.38  ? 92   LEU A CD2 1 
ATOM   720   N  N   . SER A  1 93  ? -19.725 -39.384 17.662  1.00 32.79  ? 93   SER A N   1 
ATOM   721   C  CA  . SER A  1 93  ? -20.605 -40.295 18.395  1.00 35.05  ? 93   SER A CA  1 
ATOM   722   C  C   . SER A  1 93  ? -20.619 -40.071 19.893  1.00 33.87  ? 93   SER A C   1 
ATOM   723   O  O   . SER A  1 93  ? -19.686 -39.496 20.460  1.00 31.93  ? 93   SER A O   1 
ATOM   724   C  CB  . SER A  1 93  ? -20.228 -41.746 18.153  1.00 47.51  ? 93   SER A CB  1 
ATOM   725   O  OG  . SER A  1 93  ? -20.925 -42.559 19.077  1.00 50.07  ? 93   SER A OG  1 
ATOM   726   N  N   . GLU A  1 94  ? -21.674 -40.560 20.537  1.00 39.71  ? 94   GLU A N   1 
ATOM   727   C  CA  . GLU A  1 94  ? -21.752 -40.483 21.986  1.00 37.95  ? 94   GLU A CA  1 
ATOM   728   C  C   . GLU A  1 94  ? -20.909 -41.604 22.570  1.00 34.07  ? 94   GLU A C   1 
ATOM   729   O  O   . GLU A  1 94  ? -20.536 -41.570 23.742  1.00 33.17  ? 94   GLU A O   1 
ATOM   730   C  CB  . GLU A  1 94  ? -23.200 -40.558 22.475  1.00 38.07  ? 94   GLU A CB  1 
ATOM   731   C  CG  . GLU A  1 94  ? -23.478 -39.650 23.668  1.00 38.25  ? 94   GLU A CG  1 
ATOM   732   C  CD  . GLU A  1 94  ? -24.954 -39.324 23.853  1.00 41.94  ? 94   GLU A CD  1 
ATOM   733   O  OE1 . GLU A  1 94  ? -25.776 -39.613 22.950  1.00 44.84  ? 94   GLU A OE1 1 
ATOM   734   O  OE2 . GLU A  1 94  ? -25.291 -38.761 24.912  1.00 42.39  ? 94   GLU A OE2 1 
ATOM   735   N  N   . ASP A  1 95  ? -20.580 -42.577 21.725  1.00 31.07  ? 95   ASP A N   1 
ATOM   736   C  CA  . ASP A  1 95  ? -19.731 -43.680 22.132  1.00 28.38  ? 95   ASP A CA  1 
ATOM   737   C  C   . ASP A  1 95  ? -18.362 -43.307 21.580  1.00 27.68  ? 95   ASP A C   1 
ATOM   738   O  O   . ASP A  1 95  ? -17.986 -43.687 20.467  1.00 25.57  ? 95   ASP A O   1 
ATOM   739   C  CB  . ASP A  1 95  ? -20.305 -44.891 21.392  1.00 34.49  ? 95   ASP A CB  1 
ATOM   740   C  CG  . ASP A  1 95  ? -19.437 -46.116 21.437  1.00 38.25  ? 95   ASP A CG  1 
ATOM   741   O  OD1 . ASP A  1 95  ? -18.245 -46.035 21.797  1.00 41.93  ? 95   ASP A OD1 1 
ATOM   742   O  OD2 . ASP A  1 95  ? -19.975 -47.187 21.073  1.00 38.79  ? 95   ASP A OD2 1 
ATOM   743   N  N   . CYS A  1 96  ? -17.612 -42.565 22.388  1.00 25.05  ? 96   CYS A N   1 
ATOM   744   C  CA  . CYS A  1 96  ? -16.270 -42.149 22.025  1.00 22.09  ? 96   CYS A CA  1 
ATOM   745   C  C   . CYS A  1 96  ? -15.082 -42.629 22.855  1.00 21.18  ? 96   CYS A C   1 
ATOM   746   O  O   . CYS A  1 96  ? -13.942 -42.308 22.515  1.00 20.61  ? 96   CYS A O   1 
ATOM   747   C  CB  . CYS A  1 96  ? -16.221 -40.647 21.827  1.00 34.16  ? 96   CYS A CB  1 
ATOM   748   S  SG  . CYS A  1 96  ? -16.925 -39.718 23.177  1.00 45.08  ? 96   CYS A SG  1 
ATOM   749   N  N   . LEU A  1 97  ? -15.302 -43.368 23.940  1.00 21.12  ? 97   LEU A N   1 
ATOM   750   C  CA  . LEU A  1 97  ? -14.184 -43.533 24.864  1.00 20.25  ? 97   LEU A CA  1 
ATOM   751   C  C   . LEU A  1 97  ? -13.380 -44.727 24.421  1.00 21.13  ? 97   LEU A C   1 
ATOM   752   O  O   . LEU A  1 97  ? -13.738 -45.885 24.677  1.00 20.92  ? 97   LEU A O   1 
ATOM   753   C  CB  . LEU A  1 97  ? -14.659 -43.715 26.306  1.00 20.15  ? 97   LEU A CB  1 
ATOM   754   C  CG  . LEU A  1 97  ? -15.590 -42.645 26.875  1.00 20.19  ? 97   LEU A CG  1 
ATOM   755   C  CD1 . LEU A  1 97  ? -15.964 -42.970 28.289  1.00 20.21  ? 97   LEU A CD1 1 
ATOM   756   C  CD2 . LEU A  1 97  ? -14.939 -41.306 26.834  1.00 19.46  ? 97   LEU A CD2 1 
ATOM   757   N  N   . TYR A  1 98  ? -12.243 -44.376 23.810  1.00 27.93  ? 98   TYR A N   1 
ATOM   758   C  CA  . TYR A  1 98  ? -11.292 -45.270 23.152  1.00 25.86  ? 98   TYR A CA  1 
ATOM   759   C  C   . TYR A  1 98  ? -9.974  -44.565 23.280  1.00 22.07  ? 98   TYR A C   1 
ATOM   760   O  O   . TYR A  1 98  ? -9.948  -43.342 23.420  1.00 20.79  ? 98   TYR A O   1 
ATOM   761   C  CB  . TYR A  1 98  ? -11.609 -45.435 21.666  1.00 20.88  ? 98   TYR A CB  1 
ATOM   762   C  CG  . TYR A  1 98  ? -12.947 -46.071 21.428  1.00 23.58  ? 98   TYR A CG  1 
ATOM   763   C  CD1 . TYR A  1 98  ? -13.095 -47.444 21.461  1.00 24.26  ? 98   TYR A CD1 1 
ATOM   764   C  CD2 . TYR A  1 98  ? -14.079 -45.299 21.205  1.00 24.85  ? 98   TYR A CD2 1 
ATOM   765   C  CE1 . TYR A  1 98  ? -14.337 -48.040 21.263  1.00 27.41  ? 98   TYR A CE1 1 
ATOM   766   C  CE2 . TYR A  1 98  ? -15.333 -45.885 21.003  1.00 26.86  ? 98   TYR A CE2 1 
ATOM   767   C  CZ  . TYR A  1 98  ? -15.455 -47.258 21.032  1.00 28.17  ? 98   TYR A CZ  1 
ATOM   768   O  OH  . TYR A  1 98  ? -16.685 -47.858 20.829  1.00 29.90  ? 98   TYR A OH  1 
ATOM   769   N  N   . LEU A  1 99  ? -8.884  -45.325 23.243  1.00 19.21  ? 99   LEU A N   1 
ATOM   770   C  CA  . LEU A  1 99  ? -7.548  -44.740 23.293  1.00 18.61  ? 99   LEU A CA  1 
ATOM   771   C  C   . LEU A  1 99  ? -6.593  -45.312 22.254  1.00 18.98  ? 99   LEU A C   1 
ATOM   772   O  O   . LEU A  1 99  ? -6.837  -46.365 21.644  1.00 19.68  ? 99   LEU A O   1 
ATOM   773   C  CB  . LEU A  1 99  ? -6.959  -44.834 24.701  1.00 18.04  ? 99   LEU A CB  1 
ATOM   774   C  CG  . LEU A  1 99  ? -7.103  -46.137 25.471  1.00 18.33  ? 99   LEU A CG  1 
ATOM   775   C  CD1 . LEU A  1 99  ? -6.087  -47.074 24.988  1.00 18.63  ? 99   LEU A CD1 1 
ATOM   776   C  CD2 . LEU A  1 99  ? -6.912  -45.924 26.933  1.00 17.86  ? 99   LEU A CD2 1 
ATOM   777   N  N   . ASN A  1 100 ? -5.502  -44.585 22.059  1.00 22.89  ? 100  ASN A N   1 
ATOM   778   C  CA  . ASN A  1 100 ? -4.473  -44.923 21.081  1.00 24.14  ? 100  ASN A CA  1 
ATOM   779   C  C   . ASN A  1 100 ? -3.088  -45.104 21.716  1.00 25.27  ? 100  ASN A C   1 
ATOM   780   O  O   . ASN A  1 100 ? -2.695  -44.354 22.616  1.00 18.02  ? 100  ASN A O   1 
ATOM   781   C  CB  . ASN A  1 100 ? -4.417  -43.835 20.009  1.00 25.69  ? 100  ASN A CB  1 
ATOM   782   C  CG  . ASN A  1 100 ? -5.799  -43.406 19.548  1.00 26.08  ? 100  ASN A CG  1 
ATOM   783   O  OD1 . ASN A  1 100 ? -6.580  -44.215 19.038  1.00 27.86  ? 100  ASN A OD1 1 
ATOM   784   N  ND2 . ASN A  1 100 ? -6.116  -42.131 19.745  1.00 24.33  ? 100  ASN A ND2 1 
ATOM   785   N  N   . VAL A  1 101 ? -2.364  -46.111 21.248  1.00 19.15  ? 101  VAL A N   1 
ATOM   786   C  CA  . VAL A  1 101 ? -1.025  -46.389 21.726  1.00 19.04  ? 101  VAL A CA  1 
ATOM   787   C  C   . VAL A  1 101 ? -0.062  -46.516 20.555  1.00 19.62  ? 101  VAL A C   1 
ATOM   788   O  O   . VAL A  1 101 ? -0.259  -47.371 19.694  1.00 20.34  ? 101  VAL A O   1 
ATOM   789   C  CB  . VAL A  1 101 ? -0.977  -47.721 22.459  1.00 19.28  ? 101  VAL A CB  1 
ATOM   790   C  CG1 . VAL A  1 101 ? 0.386   -47.892 23.115  1.00 19.18  ? 101  VAL A CG1 1 
ATOM   791   C  CG2 . VAL A  1 101 ? -2.100  -47.817 23.470  1.00 18.97  ? 101  VAL A CG2 1 
ATOM   792   N  N   . TRP A  1 102 ? 0.974   -45.679 20.512  1.00 19.43  ? 102  TRP A N   1 
ATOM   793   C  CA  . TRP A  1 102 ? 2.037   -45.849 19.521  1.00 20.08  ? 102  TRP A CA  1 
ATOM   794   C  C   . TRP A  1 102 ? 3.279   -46.360 20.223  1.00 20.84  ? 102  TRP A C   1 
ATOM   795   O  O   . TRP A  1 102 ? 3.652   -45.838 21.271  1.00 19.58  ? 102  TRP A O   1 
ATOM   796   C  CB  . TRP A  1 102 ? 2.404   -44.527 18.852  1.00 26.69  ? 102  TRP A CB  1 
ATOM   797   C  CG  . TRP A  1 102 ? 1.431   -43.988 17.873  1.00 26.67  ? 102  TRP A CG  1 
ATOM   798   C  CD1 . TRP A  1 102 ? 1.449   -44.156 16.521  1.00 27.94  ? 102  TRP A CD1 1 
ATOM   799   C  CD2 . TRP A  1 102 ? 0.325   -43.139 18.160  1.00 27.38  ? 102  TRP A CD2 1 
ATOM   800   N  NE1 . TRP A  1 102 ? 0.401   -43.481 15.950  1.00 28.98  ? 102  TRP A NE1 1 
ATOM   801   C  CE2 . TRP A  1 102 ? -0.306  -42.851 16.942  1.00 29.33  ? 102  TRP A CE2 1 
ATOM   802   C  CE3 . TRP A  1 102 ? -0.204  -42.606 19.333  1.00 29.86  ? 102  TRP A CE3 1 
ATOM   803   C  CZ2 . TRP A  1 102 ? -1.446  -42.054 16.866  1.00 33.21  ? 102  TRP A CZ2 1 
ATOM   804   C  CZ3 . TRP A  1 102 ? -1.337  -41.813 19.255  1.00 31.83  ? 102  TRP A CZ3 1 
ATOM   805   C  CH2 . TRP A  1 102 ? -1.944  -41.545 18.033  1.00 33.02  ? 102  TRP A CH2 1 
ATOM   806   N  N   . THR A  1 103 ? 3.916   -47.376 19.648  1.00 32.85  ? 103  THR A N   1 
ATOM   807   C  CA  . THR A  1 103 ? 5.191   -47.877 20.160  1.00 35.45  ? 103  THR A CA  1 
ATOM   808   C  C   . THR A  1 103 ? 6.115   -48.129 18.988  1.00 38.48  ? 103  THR A C   1 
ATOM   809   O  O   . THR A  1 103 ? 5.669   -48.135 17.840  1.00 42.75  ? 103  THR A O   1 
ATOM   810   C  CB  . THR A  1 103 ? 5.057   -49.195 20.956  1.00 23.63  ? 103  THR A CB  1 
ATOM   811   O  OG1 . THR A  1 103 ? 4.811   -50.278 20.054  1.00 22.19  ? 103  THR A OG1 1 
ATOM   812   C  CG2 . THR A  1 103 ? 3.946   -49.105 21.982  1.00 24.80  ? 103  THR A CG2 1 
ATOM   813   N  N   . PRO A  1 104 ? 7.414   -48.301 19.267  1.00 22.48  ? 104  PRO A N   1 
ATOM   814   C  CA  . PRO A  1 104 ? 8.358   -48.662 18.208  1.00 23.52  ? 104  PRO A CA  1 
ATOM   815   C  C   . PRO A  1 104 ? 8.066   -50.019 17.581  1.00 24.32  ? 104  PRO A C   1 
ATOM   816   O  O   . PRO A  1 104 ? 7.339   -50.814 18.155  1.00 24.12  ? 104  PRO A O   1 
ATOM   817   C  CB  . PRO A  1 104 ? 9.691   -48.693 18.945  1.00 33.88  ? 104  PRO A CB  1 
ATOM   818   C  CG  . PRO A  1 104 ? 9.517   -47.678 20.029  1.00 33.79  ? 104  PRO A CG  1 
ATOM   819   C  CD  . PRO A  1 104 ? 8.106   -47.850 20.487  1.00 30.81  ? 104  PRO A CD  1 
ATOM   820   N  N   . TYR A  1 105 ? 8.590   -50.249 16.384  1.00 39.11  ? 105  TYR A N   1 
ATOM   821   C  CA  . TYR A  1 105 ? 8.541   -51.563 15.749  1.00 41.73  ? 105  TYR A CA  1 
ATOM   822   C  C   . TYR A  1 105 ? 9.951   -52.135 15.543  1.00 45.31  ? 105  TYR A C   1 
ATOM   823   O  O   . TYR A  1 105 ? 10.788  -51.510 14.903  1.00 49.38  ? 105  TYR A O   1 
ATOM   824   C  CB  . TYR A  1 105 ? 7.792   -51.483 14.430  1.00 26.81  ? 105  TYR A CB  1 
ATOM   825   C  CG  . TYR A  1 105 ? 7.438   -52.817 13.818  1.00 27.78  ? 105  TYR A CG  1 
ATOM   826   C  CD1 . TYR A  1 105 ? 8.363   -53.525 13.065  1.00 29.02  ? 105  TYR A CD1 1 
ATOM   827   C  CD2 . TYR A  1 105 ? 6.162   -53.349 13.961  1.00 30.41  ? 105  TYR A CD2 1 
ATOM   828   C  CE1 . TYR A  1 105 ? 8.034   -54.737 12.490  1.00 30.01  ? 105  TYR A CE1 1 
ATOM   829   C  CE2 . TYR A  1 105 ? 5.823   -54.555 13.386  1.00 28.56  ? 105  TYR A CE2 1 
ATOM   830   C  CZ  . TYR A  1 105 ? 6.764   -55.244 12.656  1.00 29.76  ? 105  TYR A CZ  1 
ATOM   831   O  OH  . TYR A  1 105 ? 6.440   -56.450 12.091  1.00 30.84  ? 105  TYR A OH  1 
ATOM   832   N  N   . PRO A  1 106 ? 10.228  -53.317 16.096  1.00 35.97  ? 106  PRO A N   1 
ATOM   833   C  CA  . PRO A  1 106 ? 9.325   -54.160 16.878  1.00 38.79  ? 106  PRO A CA  1 
ATOM   834   C  C   . PRO A  1 106 ? 9.165   -53.596 18.261  1.00 43.62  ? 106  PRO A C   1 
ATOM   835   O  O   . PRO A  1 106 ? 10.011  -52.797 18.684  1.00 45.79  ? 106  PRO A O   1 
ATOM   836   C  CB  . PRO A  1 106 ? 10.083  -55.476 16.979  1.00 32.46  ? 106  PRO A CB  1 
ATOM   837   C  CG  . PRO A  1 106 ? 11.481  -55.069 16.962  1.00 33.10  ? 106  PRO A CG  1 
ATOM   838   C  CD  . PRO A  1 106 ? 11.567  -53.907 16.008  1.00 32.22  ? 106  PRO A CD  1 
ATOM   839   N  N   . ARG A  1 107 ? 8.119   -54.053 18.947  1.00 38.78  ? 107  ARG A N   1 
ATOM   840   C  CA  . ARG A  1 107 ? 7.753   -53.594 20.272  1.00 36.57  ? 107  ARG A CA  1 
ATOM   841   C  C   . ARG A  1 107 ? 9.019   -53.609 21.123  1.00 35.36  ? 107  ARG A C   1 
ATOM   842   O  O   . ARG A  1 107 ? 9.826   -54.526 20.988  1.00 39.87  ? 107  ARG A O   1 
ATOM   843   C  CB  . ARG A  1 107 ? 6.714   -54.568 20.832  1.00 46.63  ? 107  ARG A CB  1 
ATOM   844   C  CG  . ARG A  1 107 ? 5.559   -53.916 21.566  1.00 50.90  ? 107  ARG A CG  1 
ATOM   845   C  CD  . ARG A  1 107 ? 4.187   -54.165 20.923  1.00 51.31  ? 107  ARG A CD  1 
ATOM   846   N  NE  . ARG A  1 107 ? 3.879   -55.580 20.701  1.00 51.91  ? 107  ARG A NE  1 
ATOM   847   C  CZ  . ARG A  1 107 ? 3.710   -56.490 21.657  1.00 49.68  ? 107  ARG A CZ  1 
ATOM   848   N  NH1 . ARG A  1 107 ? 3.833   -56.160 22.933  1.00 48.21  ? 107  ARG A NH1 1 
ATOM   849   N  NH2 . ARG A  1 107 ? 3.425   -57.742 21.331  1.00 49.69  ? 107  ARG A NH2 1 
ATOM   850   N  N   . PRO A  1 108 ? 9.229   -52.570 21.958  1.00 33.25  ? 108  PRO A N   1 
ATOM   851   C  CA  . PRO A  1 108 ? 10.487  -52.370 22.700  1.00 33.07  ? 108  PRO A CA  1 
ATOM   852   C  C   . PRO A  1 108 ? 10.970  -53.546 23.586  1.00 35.49  ? 108  PRO A C   1 
ATOM   853   O  O   . PRO A  1 108 ? 10.168  -54.218 24.256  1.00 32.53  ? 108  PRO A O   1 
ATOM   854   C  CB  . PRO A  1 108 ? 10.195  -51.122 23.548  1.00 31.45  ? 108  PRO A CB  1 
ATOM   855   C  CG  . PRO A  1 108 ? 8.726   -50.972 23.530  1.00 22.54  ? 108  PRO A CG  1 
ATOM   856   C  CD  . PRO A  1 108 ? 8.290   -51.465 22.203  1.00 31.93  ? 108  PRO A CD  1 
ATOM   857   N  N   . ALA A  1 109 ? 12.284  -53.791 23.576  1.00 45.46  ? 109  ALA A N   1 
ATOM   858   C  CA  . ALA A  1 109 ? 12.881  -54.841 24.412  1.00 48.24  ? 109  ALA A CA  1 
ATOM   859   C  C   . ALA A  1 109 ? 12.778  -54.508 25.899  1.00 51.93  ? 109  ALA A C   1 
ATOM   860   O  O   . ALA A  1 109 ? 12.181  -55.259 26.672  1.00 50.24  ? 109  ALA A O   1 
ATOM   861   C  CB  . ALA A  1 109 ? 14.340  -55.069 24.029  1.00 34.50  ? 109  ALA A CB  1 
ATOM   862   N  N   . SER A  1 110 ? 13.350  -53.365 26.280  1.00 59.09  ? 110  SER A N   1 
ATOM   863   C  CA  . SER A  1 110 ? 13.293  -52.860 27.654  1.00 57.43  ? 110  SER A CA  1 
ATOM   864   C  C   . SER A  1 110 ? 12.084  -51.964 27.879  1.00 50.67  ? 110  SER A C   1 
ATOM   865   O  O   . SER A  1 110 ? 11.578  -51.346 26.954  1.00 51.96  ? 110  SER A O   1 
ATOM   866   C  CB  . SER A  1 110 ? 14.586  -52.118 28.021  1.00 56.22  ? 110  SER A CB  1 
ATOM   867   O  OG  . SER A  1 110 ? 15.103  -51.405 26.911  1.00 58.26  ? 110  SER A OG  1 
ATOM   868   N  N   . PRO A  1 111 ? 11.631  -51.869 29.124  1.00 33.30  ? 111  PRO A N   1 
ATOM   869   C  CA  . PRO A  1 111 ? 10.403  -51.129 29.402  1.00 30.85  ? 111  PRO A CA  1 
ATOM   870   C  C   . PRO A  1 111 ? 10.574  -49.621 29.251  1.00 29.33  ? 111  PRO A C   1 
ATOM   871   O  O   . PRO A  1 111 ? 10.904  -48.938 30.219  1.00 29.34  ? 111  PRO A O   1 
ATOM   872   C  CB  . PRO A  1 111 ? 10.104  -51.491 30.859  1.00 37.83  ? 111  PRO A CB  1 
ATOM   873   C  CG  . PRO A  1 111 ? 10.755  -52.798 31.054  1.00 40.26  ? 111  PRO A CG  1 
ATOM   874   C  CD  . PRO A  1 111 ? 12.018  -52.716 30.260  1.00 41.28  ? 111  PRO A CD  1 
ATOM   875   N  N   . THR A  1 112 ? 10.406  -49.123 28.030  1.00 33.89  ? 112  THR A N   1 
ATOM   876   C  CA  . THR A  1 112 ? 10.456  -47.685 27.760  1.00 37.55  ? 112  THR A CA  1 
ATOM   877   C  C   . THR A  1 112 ? 9.398   -46.867 28.533  1.00 30.81  ? 112  THR A C   1 
ATOM   878   O  O   . THR A  1 112 ? 8.265   -47.330 28.713  1.00 27.70  ? 112  THR A O   1 
ATOM   879   C  CB  . THR A  1 112 ? 10.257  -47.425 26.267  1.00 52.82  ? 112  THR A CB  1 
ATOM   880   O  OG1 . THR A  1 112 ? 8.970   -47.917 25.887  1.00 54.20  ? 112  THR A OG1 1 
ATOM   881   C  CG2 . THR A  1 112 ? 11.343  -48.131 25.443  1.00 54.52  ? 112  THR A CG2 1 
ATOM   882   N  N   . PRO A  1 113 ? 9.773   -45.646 28.988  1.00 22.68  ? 113  PRO A N   1 
ATOM   883   C  CA  . PRO A  1 113 ? 8.844   -44.739 29.669  1.00 20.46  ? 113  PRO A CA  1 
ATOM   884   C  C   . PRO A  1 113 ? 7.739   -44.243 28.736  1.00 20.51  ? 113  PRO A C   1 
ATOM   885   O  O   . PRO A  1 113 ? 7.917   -44.194 27.516  1.00 18.59  ? 113  PRO A O   1 
ATOM   886   C  CB  . PRO A  1 113 ? 9.746   -43.582 30.123  1.00 18.97  ? 113  PRO A CB  1 
ATOM   887   C  CG  . PRO A  1 113 ? 10.876  -43.606 29.197  1.00 19.63  ? 113  PRO A CG  1 
ATOM   888   C  CD  . PRO A  1 113 ? 11.124  -45.063 28.919  1.00 20.22  ? 113  PRO A CD  1 
ATOM   889   N  N   . VAL A  1 114 ? 6.611   -43.870 29.331  1.00 17.76  ? 114  VAL A N   1 
ATOM   890   C  CA  . VAL A  1 114 ? 5.374   -43.650 28.601  1.00 27.68  ? 114  VAL A CA  1 
ATOM   891   C  C   . VAL A  1 114 ? 4.968   -42.182 28.647  1.00 27.36  ? 114  VAL A C   1 
ATOM   892   O  O   . VAL A  1 114 ? 5.172   -41.511 29.653  1.00 28.62  ? 114  VAL A O   1 
ATOM   893   C  CB  . VAL A  1 114 ? 4.241   -44.507 29.201  1.00 17.24  ? 114  VAL A CB  1 
ATOM   894   C  CG1 . VAL A  1 114 ? 3.092   -44.557 28.274  1.00 20.24  ? 114  VAL A CG1 1 
ATOM   895   C  CG2 . VAL A  1 114 ? 4.714   -45.915 29.441  1.00 23.33  ? 114  VAL A CG2 1 
ATOM   896   N  N   . LEU A  1 115 ? 4.406   -41.683 27.550  1.00 27.66  ? 115  LEU A N   1 
ATOM   897   C  CA  . LEU A  1 115 ? 3.921   -40.312 27.479  1.00 24.20  ? 115  LEU A CA  1 
ATOM   898   C  C   . LEU A  1 115 ? 2.447   -40.354 27.209  1.00 26.04  ? 115  LEU A C   1 
ATOM   899   O  O   . LEU A  1 115 ? 2.038   -40.812 26.139  1.00 30.24  ? 115  LEU A O   1 
ATOM   900   C  CB  . LEU A  1 115 ? 4.582   -39.575 26.319  1.00 19.43  ? 115  LEU A CB  1 
ATOM   901   C  CG  . LEU A  1 115 ? 6.009   -39.068 26.505  1.00 18.23  ? 115  LEU A CG  1 
ATOM   902   C  CD1 . LEU A  1 115 ? 6.520   -38.529 25.204  1.00 17.74  ? 115  LEU A CD1 1 
ATOM   903   C  CD2 . LEU A  1 115 ? 6.039   -37.988 27.550  1.00 16.63  ? 115  LEU A CD2 1 
ATOM   904   N  N   . ILE A  1 116 ? 1.639   -39.893 28.158  1.00 19.60  ? 116  ILE A N   1 
ATOM   905   C  CA  . ILE A  1 116 ? 0.198   -39.823 27.920  1.00 15.52  ? 116  ILE A CA  1 
ATOM   906   C  C   . ILE A  1 116 ? -0.189  -38.392 27.530  1.00 18.43  ? 116  ILE A C   1 
ATOM   907   O  O   . ILE A  1 116 ? 0.095   -37.429 28.263  1.00 16.02  ? 116  ILE A O   1 
ATOM   908   C  CB  . ILE A  1 116 ? -0.616  -40.281 29.132  1.00 15.36  ? 116  ILE A CB  1 
ATOM   909   C  CG1 . ILE A  1 116 ? -0.336  -41.736 29.455  1.00 15.66  ? 116  ILE A CG1 1 
ATOM   910   C  CG2 . ILE A  1 116 ? -2.072  -40.142 28.854  1.00 28.66  ? 116  ILE A CG2 1 
ATOM   911   C  CD1 . ILE A  1 116 ? -0.949  -42.155 30.743  1.00 15.62  ? 116  ILE A CD1 1 
ATOM   912   N  N   . TRP A  1 117 ? -0.817  -38.256 26.363  1.00 15.53  ? 117  TRP A N   1 
ATOM   913   C  CA  . TRP A  1 117 ? -1.205  -36.950 25.855  1.00 15.50  ? 117  TRP A CA  1 
ATOM   914   C  C   . TRP A  1 117 ? -2.699  -36.693 26.050  1.00 15.42  ? 117  TRP A C   1 
ATOM   915   O  O   . TRP A  1 117 ? -3.543  -37.453 25.588  1.00 15.64  ? 117  TRP A O   1 
ATOM   916   C  CB  . TRP A  1 117 ? -0.827  -36.811 24.378  1.00 15.95  ? 117  TRP A CB  1 
ATOM   917   C  CG  . TRP A  1 117 ? -1.471  -35.626 23.714  1.00 16.09  ? 117  TRP A CG  1 
ATOM   918   C  CD1 . TRP A  1 117 ? -2.668  -35.602 23.045  1.00 16.33  ? 117  TRP A CD1 1 
ATOM   919   C  CD2 . TRP A  1 117 ? -0.967  -34.291 23.670  1.00 17.21  ? 117  TRP A CD2 1 
ATOM   920   N  NE1 . TRP A  1 117 ? -2.935  -34.338 22.588  1.00 17.53  ? 117  TRP A NE1 1 
ATOM   921   C  CE2 . TRP A  1 117 ? -1.907  -33.508 22.959  1.00 19.13  ? 117  TRP A CE2 1 
ATOM   922   C  CE3 . TRP A  1 117 ? 0.187   -33.672 24.170  1.00 17.28  ? 117  TRP A CE3 1 
ATOM   923   C  CZ2 . TRP A  1 117 ? -1.732  -32.144 22.737  1.00 21.18  ? 117  TRP A CZ2 1 
ATOM   924   C  CZ3 . TRP A  1 117 ? 0.365   -32.319 23.945  1.00 18.58  ? 117  TRP A CZ3 1 
ATOM   925   C  CH2 . TRP A  1 117 ? -0.594  -31.569 23.235  1.00 21.24  ? 117  TRP A CH2 1 
ATOM   926   N  N   . ILE A  1 118 ? -3.028  -35.621 26.752  1.00 15.18  ? 118  ILE A N   1 
ATOM   927   C  CA  . ILE A  1 118 ? -4.411  -35.200 26.866  1.00 15.22  ? 118  ILE A CA  1 
ATOM   928   C  C   . ILE A  1 118 ? -4.590  -33.973 25.975  1.00 17.64  ? 118  ILE A C   1 
ATOM   929   O  O   . ILE A  1 118 ? -3.878  -32.982 26.148  1.00 17.39  ? 118  ILE A O   1 
ATOM   930   C  CB  . ILE A  1 118 ? -4.760  -34.836 28.317  1.00 14.93  ? 118  ILE A CB  1 
ATOM   931   C  CG1 . ILE A  1 118 ? -4.351  -35.953 29.261  1.00 14.80  ? 118  ILE A CG1 1 
ATOM   932   C  CG2 . ILE A  1 118 ? -6.240  -34.588 28.468  1.00 15.08  ? 118  ILE A CG2 1 
ATOM   933   C  CD1 . ILE A  1 118 ? -4.749  -35.676 30.678  1.00 14.65  ? 118  ILE A CD1 1 
ATOM   934   N  N   . TYR A  1 119 ? -5.522  -34.038 25.020  1.00 16.41  ? 119  TYR A N   1 
ATOM   935   C  CA  . TYR A  1 119 ? -5.768  -32.916 24.098  1.00 16.44  ? 119  TYR A CA  1 
ATOM   936   C  C   . TYR A  1 119 ? -6.480  -31.708 24.716  1.00 18.86  ? 119  TYR A C   1 
ATOM   937   O  O   . TYR A  1 119 ? -7.112  -31.811 25.770  1.00 15.94  ? 119  TYR A O   1 
ATOM   938   C  CB  . TYR A  1 119 ? -6.492  -33.363 22.810  1.00 16.80  ? 119  TYR A CB  1 
ATOM   939   C  CG  . TYR A  1 119 ? -7.875  -33.993 22.990  1.00 20.55  ? 119  TYR A CG  1 
ATOM   940   C  CD1 . TYR A  1 119 ? -9.018  -33.214 23.162  1.00 17.24  ? 119  TYR A CD1 1 
ATOM   941   C  CD2 . TYR A  1 119 ? -8.033  -35.375 22.939  1.00 22.44  ? 119  TYR A CD2 1 
ATOM   942   C  CE1 . TYR A  1 119 ? -10.265 -33.802 23.307  1.00 17.57  ? 119  TYR A CE1 1 
ATOM   943   C  CE2 . TYR A  1 119 ? -9.274  -35.964 23.087  1.00 21.99  ? 119  TYR A CE2 1 
ATOM   944   C  CZ  . TYR A  1 119 ? -10.383 -35.181 23.269  1.00 21.91  ? 119  TYR A CZ  1 
ATOM   945   O  OH  . TYR A  1 119 ? -11.596 -35.812 23.414  1.00 18.08  ? 119  TYR A OH  1 
ATOM   946   N  N   . GLY A  1 120 ? -6.345  -30.566 24.044  1.00 16.49  ? 120  GLY A N   1 
ATOM   947   C  CA  . GLY A  1 120 ? -7.080  -29.363 24.386  1.00 19.46  ? 120  GLY A CA  1 
ATOM   948   C  C   . GLY A  1 120 ? -8.328  -29.139 23.527  1.00 19.83  ? 120  GLY A C   1 
ATOM   949   O  O   . GLY A  1 120 ? -8.929  -30.093 23.001  1.00 17.52  ? 120  GLY A O   1 
ATOM   950   N  N   . GLY A  1 121 ? -8.700  -27.873 23.333  1.00 32.12  ? 121  GLY A N   1 
ATOM   951   C  CA  . GLY A  1 121 ? -9.987  -27.566 22.733  1.00 33.54  ? 121  GLY A CA  1 
ATOM   952   C  C   . GLY A  1 121 ? -11.083 -27.036 23.648  1.00 31.82  ? 121  GLY A C   1 
ATOM   953   O  O   . GLY A  1 121 ? -12.262 -27.129 23.315  1.00 32.58  ? 121  GLY A O   1 
ATOM   954   N  N   . GLY A  1 122 ? -10.702 -26.549 24.826  1.00 23.11  ? 122  GLY A N   1 
ATOM   955   C  CA  . GLY A  1 122 ? -11.593 -25.759 25.668  1.00 20.61  ? 122  GLY A CA  1 
ATOM   956   C  C   . GLY A  1 122 ? -12.686 -26.490 26.428  1.00 18.21  ? 122  GLY A C   1 
ATOM   957   O  O   . GLY A  1 122 ? -13.627 -25.879 26.916  1.00 18.61  ? 122  GLY A O   1 
ATOM   958   N  N   . PHE A  1 123 ? -12.536 -27.801 26.526  1.00 18.36  ? 123  PHE A N   1 
ATOM   959   C  CA  . PHE A  1 123 ? -13.525 -28.705 27.076  1.00 21.10  ? 123  PHE A CA  1 
ATOM   960   C  C   . PHE A  1 123 ? -14.839 -28.648 26.292  1.00 26.74  ? 123  PHE A C   1 
ATOM   961   O  O   . PHE A  1 123 ? -15.850 -29.191 26.737  1.00 28.19  ? 123  PHE A O   1 
ATOM   962   C  CB  . PHE A  1 123 ? -13.833 -28.339 28.537  1.00 17.83  ? 123  PHE A CB  1 
ATOM   963   C  CG  . PHE A  1 123 ? -12.632 -28.275 29.438  1.00 17.14  ? 123  PHE A CG  1 
ATOM   964   C  CD1 . PHE A  1 123 ? -11.937 -29.428 29.794  1.00 17.74  ? 123  PHE A CD1 1 
ATOM   965   C  CD2 . PHE A  1 123 ? -12.223 -27.072 29.989  1.00 17.74  ? 123  PHE A CD2 1 
ATOM   966   C  CE1 . PHE A  1 123 ? -10.809 -29.375 30.661  1.00 16.13  ? 123  PHE A CE1 1 
ATOM   967   C  CE2 . PHE A  1 123 ? -11.115 -27.012 30.851  1.00 17.68  ? 123  PHE A CE2 1 
ATOM   968   C  CZ  . PHE A  1 123 ? -10.408 -28.169 31.183  1.00 16.11  ? 123  PHE A CZ  1 
ATOM   969   N  N   . TYR A  1 124 ? -14.853 -28.018 25.123  1.00 38.70  ? 124  TYR A N   1 
ATOM   970   C  CA  . TYR A  1 124 ? -16.025 -28.133 24.250  1.00 42.54  ? 124  TYR A CA  1 
ATOM   971   C  C   . TYR A  1 124 ? -15.733 -29.002 23.034  1.00 39.49  ? 124  TYR A C   1 
ATOM   972   O  O   . TYR A  1 124 ? -16.625 -29.267 22.222  1.00 40.17  ? 124  TYR A O   1 
ATOM   973   C  CB  . TYR A  1 124 ? -16.635 -26.757 23.865  1.00 45.96  ? 124  TYR A CB  1 
ATOM   974   C  CG  . TYR A  1 124 ? -15.725 -25.889 23.036  1.00 41.66  ? 124  TYR A CG  1 
ATOM   975   C  CD1 . TYR A  1 124 ? -14.713 -25.167 23.638  1.00 40.67  ? 124  TYR A CD1 1 
ATOM   976   C  CD2 . TYR A  1 124 ? -15.866 -25.811 21.655  1.00 40.88  ? 124  TYR A CD2 1 
ATOM   977   C  CE1 . TYR A  1 124 ? -13.851 -24.396 22.899  1.00 45.11  ? 124  TYR A CE1 1 
ATOM   978   C  CE2 . TYR A  1 124 ? -15.012 -25.039 20.896  1.00 44.97  ? 124  TYR A CE2 1 
ATOM   979   C  CZ  . TYR A  1 124 ? -13.991 -24.326 21.525  1.00 48.41  ? 124  TYR A CZ  1 
ATOM   980   O  OH  . TYR A  1 124 ? -13.096 -23.532 20.806  1.00 50.94  ? 124  TYR A OH  1 
ATOM   981   N  N   . SER A  1 125 ? -14.484 -29.446 22.906  1.00 22.22  ? 125  SER A N   1 
ATOM   982   C  CA  . SER A  1 125 ? -14.052 -29.935 21.604  1.00 21.06  ? 125  SER A CA  1 
ATOM   983   C  C   . SER A  1 125 ? -12.792 -30.757 21.590  1.00 20.42  ? 125  SER A C   1 
ATOM   984   O  O   . SER A  1 125 ? -12.115 -30.900 22.601  1.00 21.16  ? 125  SER A O   1 
ATOM   985   C  CB  . SER A  1 125 ? -13.772 -28.744 20.701  1.00 24.24  ? 125  SER A CB  1 
ATOM   986   O  OG  . SER A  1 125 ? -12.440 -28.299 20.890  1.00 19.99  ? 125  SER A OG  1 
ATOM   987   N  N   . GLY A  1 126 ? -12.468 -31.250 20.399  1.00 19.87  ? 126  GLY A N   1 
ATOM   988   C  CA  . GLY A  1 126 ? -11.216 -31.931 20.154  1.00 25.24  ? 126  GLY A CA  1 
ATOM   989   C  C   . GLY A  1 126 ? -11.293 -33.441 20.192  1.00 22.56  ? 126  GLY A C   1 
ATOM   990   O  O   . GLY A  1 126 ? -12.347 -34.004 20.500  1.00 19.64  ? 126  GLY A O   1 
ATOM   991   N  N   . ALA A  1 127 ? -10.157 -34.086 19.909  1.00 19.11  ? 127  ALA A N   1 
ATOM   992   C  CA  . ALA A  1 127 ? -10.057 -35.544 19.838  1.00 19.14  ? 127  ALA A CA  1 
ATOM   993   C  C   . ALA A  1 127 ? -8.632  -36.004 19.579  1.00 18.86  ? 127  ALA A C   1 
ATOM   994   O  O   . ALA A  1 127 ? -7.831  -35.296 18.981  1.00 18.94  ? 127  ALA A O   1 
ATOM   995   C  CB  . ALA A  1 127 ? -10.964 -36.087 18.731  1.00 20.11  ? 127  ALA A CB  1 
ATOM   996   N  N   . ALA A  1 128 ? -8.354  -37.243 19.957  1.00 22.61  ? 128  ALA A N   1 
ATOM   997   C  CA  . ALA A  1 128 ? -7.021  -37.785 19.827  1.00 18.46  ? 128  ALA A CA  1 
ATOM   998   C  C   . ALA A  1 128 ? -6.731  -38.145 18.379  1.00 20.46  ? 128  ALA A C   1 
ATOM   999   O  O   . ALA A  1 128 ? -5.588  -38.412 18.025  1.00 22.92  ? 128  ALA A O   1 
ATOM   1000  C  CB  . ALA A  1 128 ? -6.869  -38.993 20.709  1.00 19.83  ? 128  ALA A CB  1 
ATOM   1001  N  N   . SER A  1 129 ? -7.762  -38.140 17.539  1.00 19.97  ? 129  SER A N   1 
ATOM   1002  C  CA  . SER A  1 129 ? -7.616  -38.529 16.136  1.00 20.87  ? 129  SER A CA  1 
ATOM   1003  C  C   . SER A  1 129 ? -6.884  -37.478 15.298  1.00 21.16  ? 129  SER A C   1 
ATOM   1004  O  O   . SER A  1 129 ? -6.275  -37.811 14.284  1.00 33.91  ? 129  SER A O   1 
ATOM   1005  C  CB  . SER A  1 129 ? -8.981  -38.816 15.505  1.00 47.48  ? 129  SER A CB  1 
ATOM   1006  O  OG  . SER A  1 129 ? -9.884  -39.433 16.401  1.00 53.21  ? 129  SER A OG  1 
ATOM   1007  N  N   . LEU A  1 130 ? -6.918  -36.221 15.742  1.00 25.87  ? 130  LEU A N   1 
ATOM   1008  C  CA  . LEU A  1 130 ? -6.358  -35.089 14.988  1.00 24.81  ? 130  LEU A CA  1 
ATOM   1009  C  C   . LEU A  1 130 ? -4.912  -35.287 14.526  1.00 27.33  ? 130  LEU A C   1 
ATOM   1010  O  O   . LEU A  1 130 ? -4.082  -35.871 15.232  1.00 26.67  ? 130  LEU A O   1 
ATOM   1011  C  CB  . LEU A  1 130 ? -6.440  -33.809 15.820  1.00 20.62  ? 130  LEU A CB  1 
ATOM   1012  C  CG  . LEU A  1 130 ? -7.854  -33.346 16.114  1.00 20.75  ? 130  LEU A CG  1 
ATOM   1013  C  CD1 . LEU A  1 130 ? -7.858  -32.117 17.009  1.00 20.23  ? 130  LEU A CD1 1 
ATOM   1014  C  CD2 . LEU A  1 130 ? -8.490  -33.054 14.788  1.00 34.12  ? 130  LEU A CD2 1 
ATOM   1015  N  N   . ASP A  1 131 ? -4.624  -34.783 13.332  1.00 39.29  ? 131  ASP A N   1 
ATOM   1016  C  CA  . ASP A  1 131 ? -3.340  -35.023 12.675  1.00 43.51  ? 131  ASP A CA  1 
ATOM   1017  C  C   . ASP A  1 131 ? -2.112  -34.514 13.458  1.00 38.57  ? 131  ASP A C   1 
ATOM   1018  O  O   . ASP A  1 131 ? -1.074  -35.159 13.480  1.00 36.54  ? 131  ASP A O   1 
ATOM   1019  C  CB  . ASP A  1 131 ? -3.367  -34.453 11.248  1.00 49.31  ? 131  ASP A CB  1 
ATOM   1020  C  CG  . ASP A  1 131 ? -4.519  -35.010 10.405  1.00 51.88  ? 131  ASP A CG  1 
ATOM   1021  O  OD1 . ASP A  1 131 ? -5.351  -35.792 10.920  1.00 54.30  ? 131  ASP A OD1 1 
ATOM   1022  O  OD2 . ASP A  1 131 ? -4.602  -34.639 9.220   1.00 51.31  ? 131  ASP A OD2 1 
ATOM   1023  N  N   . VAL A  1 132 ? -2.229  -33.370 14.112  1.00 41.10  ? 132  VAL A N   1 
ATOM   1024  C  CA  . VAL A  1 132 ? -1.100  -32.842 14.862  1.00 41.24  ? 132  VAL A CA  1 
ATOM   1025  C  C   . VAL A  1 132 ? -0.687  -33.708 16.061  1.00 43.18  ? 132  VAL A C   1 
ATOM   1026  O  O   . VAL A  1 132 ? 0.451   -33.623 16.507  1.00 46.33  ? 132  VAL A O   1 
ATOM   1027  C  CB  . VAL A  1 132 ? -1.366  -31.409 15.351  1.00 32.40  ? 132  VAL A CB  1 
ATOM   1028  C  CG1 . VAL A  1 132 ? -1.512  -30.482 14.178  1.00 33.42  ? 132  VAL A CG1 1 
ATOM   1029  C  CG2 . VAL A  1 132 ? -2.617  -31.374 16.189  1.00 31.38  ? 132  VAL A CG2 1 
ATOM   1030  N  N   . TYR A  1 133 ? -1.588  -34.535 16.589  1.00 30.62  ? 133  TYR A N   1 
ATOM   1031  C  CA  . TYR A  1 133 ? -1.245  -35.356 17.756  1.00 25.26  ? 133  TYR A CA  1 
ATOM   1032  C  C   . TYR A  1 133 ? -0.718  -36.750 17.383  1.00 22.62  ? 133  TYR A C   1 
ATOM   1033  O  O   . TYR A  1 133 ? -0.536  -37.601 18.252  1.00 21.23  ? 133  TYR A O   1 
ATOM   1034  C  CB  . TYR A  1 133 ? -2.424  -35.519 18.718  1.00 18.37  ? 133  TYR A CB  1 
ATOM   1035  C  CG  . TYR A  1 133 ? -3.178  -34.261 19.083  1.00 18.33  ? 133  TYR A CG  1 
ATOM   1036  C  CD1 . TYR A  1 133 ? -2.524  -33.057 19.304  1.00 18.09  ? 133  TYR A CD1 1 
ATOM   1037  C  CD2 . TYR A  1 133 ? -4.573  -34.290 19.222  1.00 20.64  ? 133  TYR A CD2 1 
ATOM   1038  C  CE1 . TYR A  1 133 ? -3.255  -31.903 19.643  1.00 28.31  ? 133  TYR A CE1 1 
ATOM   1039  C  CE2 . TYR A  1 133 ? -5.300  -33.156 19.558  1.00 18.16  ? 133  TYR A CE2 1 
ATOM   1040  C  CZ  . TYR A  1 133 ? -4.646  -31.970 19.764  1.00 29.54  ? 133  TYR A CZ  1 
ATOM   1041  O  OH  . TYR A  1 133 ? -5.383  -30.859 20.090  1.00 18.08  ? 133  TYR A OH  1 
ATOM   1042  N  N   . ASP A  1 134 ? -0.507  -36.998 16.095  1.00 20.05  ? 134  ASP A N   1 
ATOM   1043  C  CA  . ASP A  1 134 ? -0.059  -38.312 15.644  1.00 20.78  ? 134  ASP A CA  1 
ATOM   1044  C  C   . ASP A  1 134 ? 1.230   -38.714 16.349  1.00 20.17  ? 134  ASP A C   1 
ATOM   1045  O  O   . ASP A  1 134 ? 2.237   -38.029 16.242  1.00 20.32  ? 134  ASP A O   1 
ATOM   1046  C  CB  . ASP A  1 134 ? 0.153   -38.280 14.130  1.00 42.82  ? 134  ASP A CB  1 
ATOM   1047  C  CG  . ASP A  1 134 ? 0.525   -39.628 13.560  1.00 50.61  ? 134  ASP A CG  1 
ATOM   1048  O  OD1 . ASP A  1 134 ? -0.218  -40.610 13.767  1.00 52.36  ? 134  ASP A OD1 1 
ATOM   1049  O  OD2 . ASP A  1 134 ? 1.569   -39.703 12.891  1.00 54.85  ? 134  ASP A OD2 1 
ATOM   1050  N  N   . GLY A  1 135 ? 1.200   -39.849 17.042  1.00 23.86  ? 135  GLY A N   1 
ATOM   1051  C  CA  . GLY A  1 135 ? 2.301   -40.253 17.903  1.00 24.97  ? 135  GLY A CA  1 
ATOM   1052  C  C   . GLY A  1 135 ? 3.422   -40.960 17.166  1.00 25.01  ? 135  GLY A C   1 
ATOM   1053  O  O   . GLY A  1 135 ? 4.455   -41.300 17.746  1.00 22.32  ? 135  GLY A O   1 
ATOM   1054  N  N   . ARG A  1 136 ? 3.216   -41.163 15.870  1.00 24.83  ? 136  ARG A N   1 
ATOM   1055  C  CA  . ARG A  1 136 ? 4.116   -41.959 15.043  1.00 25.71  ? 136  ARG A CA  1 
ATOM   1056  C  C   . ARG A  1 136 ? 5.585   -41.543 15.114  1.00 26.16  ? 136  ARG A C   1 
ATOM   1057  O  O   . ARG A  1 136 ? 6.457   -42.399 15.197  1.00 22.67  ? 136  ARG A O   1 
ATOM   1058  C  CB  . ARG A  1 136 ? 3.608   -41.966 13.601  1.00 27.97  ? 136  ARG A CB  1 
ATOM   1059  C  CG  . ARG A  1 136 ? 4.621   -41.584 12.557  1.00 26.63  ? 136  ARG A CG  1 
ATOM   1060  C  CD  . ARG A  1 136 ? 3.926   -40.997 11.322  1.00 29.91  ? 136  ARG A CD  1 
ATOM   1061  N  NE  . ARG A  1 136 ? 3.262   -41.987 10.466  1.00 30.54  ? 136  ARG A NE  1 
ATOM   1062  C  CZ  . ARG A  1 136 ? 1.963   -42.281 10.506  1.00 29.56  ? 136  ARG A CZ  1 
ATOM   1063  N  NH1 . ARG A  1 136 ? 1.153   -41.680 11.367  1.00 28.92  ? 136  ARG A NH1 1 
ATOM   1064  N  NH2 . ARG A  1 136 ? 1.474   -43.192 9.683   1.00 30.50  ? 136  ARG A NH2 1 
ATOM   1065  N  N   . PHE A  1 137 ? 5.847   -40.238 15.125  1.00 34.11  ? 137  PHE A N   1 
ATOM   1066  C  CA  . PHE A  1 137 ? 7.220   -39.719 15.074  1.00 34.87  ? 137  PHE A CA  1 
ATOM   1067  C  C   . PHE A  1 137 ? 7.972   -39.810 16.385  1.00 31.81  ? 137  PHE A C   1 
ATOM   1068  O  O   . PHE A  1 137 ? 9.168   -40.072 16.383  1.00 30.68  ? 137  PHE A O   1 
ATOM   1069  C  CB  . PHE A  1 137 ? 7.254   -38.267 14.594  1.00 32.49  ? 137  PHE A CB  1 
ATOM   1070  C  CG  . PHE A  1 137 ? 6.458   -38.032 13.361  1.00 33.16  ? 137  PHE A CG  1 
ATOM   1071  C  CD1 . PHE A  1 137 ? 6.997   -38.291 12.117  1.00 32.63  ? 137  PHE A CD1 1 
ATOM   1072  C  CD2 . PHE A  1 137 ? 5.160   -37.565 13.449  1.00 34.63  ? 137  PHE A CD2 1 
ATOM   1073  C  CE1 . PHE A  1 137 ? 6.259   -38.084 10.983  1.00 35.95  ? 137  PHE A CE1 1 
ATOM   1074  C  CE2 . PHE A  1 137 ? 4.414   -37.350 12.321  1.00 36.40  ? 137  PHE A CE2 1 
ATOM   1075  C  CZ  . PHE A  1 137 ? 4.962   -37.613 11.081  1.00 38.11  ? 137  PHE A CZ  1 
ATOM   1076  N  N   . LEU A  1 138 ? 7.290   -39.552 17.498  1.00 27.94  ? 138  LEU A N   1 
ATOM   1077  C  CA  . LEU A  1 138 ? 7.922   -39.707 18.797  1.00 27.12  ? 138  LEU A CA  1 
ATOM   1078  C  C   . LEU A  1 138 ? 8.249   -41.179 18.994  1.00 26.51  ? 138  LEU A C   1 
ATOM   1079  O  O   . LEU A  1 138 ? 9.333   -41.543 19.463  1.00 29.91  ? 138  LEU A O   1 
ATOM   1080  C  CB  . LEU A  1 138 ? 7.025   -39.178 19.911  1.00 19.65  ? 138  LEU A CB  1 
ATOM   1081  C  CG  . LEU A  1 138 ? 7.047   -37.661 19.999  1.00 19.48  ? 138  LEU A CG  1 
ATOM   1082  C  CD1 . LEU A  1 138 ? 5.890   -37.199 20.807  1.00 18.66  ? 138  LEU A CD1 1 
ATOM   1083  C  CD2 . LEU A  1 138 ? 8.320   -37.182 20.634  1.00 19.67  ? 138  LEU A CD2 1 
ATOM   1084  N  N   . ALA A  1 139 ? 7.314   -42.024 18.588  1.00 20.88  ? 139  ALA A N   1 
ATOM   1085  C  CA  . ALA A  1 139 ? 7.515   -43.455 18.656  1.00 22.86  ? 139  ALA A CA  1 
ATOM   1086  C  C   . ALA A  1 139 ? 8.771   -43.826 17.885  1.00 25.14  ? 139  ALA A C   1 
ATOM   1087  O  O   . ALA A  1 139 ? 9.688   -44.409 18.442  1.00 26.38  ? 139  ALA A O   1 
ATOM   1088  C  CB  . ALA A  1 139 ? 6.307   -44.186 18.084  1.00 33.04  ? 139  ALA A CB  1 
ATOM   1089  N  N   . GLN A  1 140 ? 8.817   -43.473 16.605  1.00 30.70  ? 140  GLN A N   1 
ATOM   1090  C  CA  . GLN A  1 140 ? 9.910   -43.926 15.762  1.00 30.33  ? 140  GLN A CA  1 
ATOM   1091  C  C   . GLN A  1 140 ? 11.237  -43.316 16.190  1.00 30.98  ? 140  GLN A C   1 
ATOM   1092  O  O   . GLN A  1 140 ? 12.177  -44.046 16.480  1.00 34.14  ? 140  GLN A O   1 
ATOM   1093  C  CB  . GLN A  1 140 ? 9.622   -43.641 14.288  1.00 31.54  ? 140  GLN A CB  1 
ATOM   1094  C  CG  . GLN A  1 140 ? 10.420  -44.486 13.322  1.00 38.03  ? 140  GLN A CG  1 
ATOM   1095  C  CD  . GLN A  1 140 ? 11.878  -44.059 13.246  1.00 45.65  ? 140  GLN A CD  1 
ATOM   1096  O  OE1 . GLN A  1 140 ? 12.187  -42.862 13.189  1.00 47.71  ? 140  GLN A OE1 1 
ATOM   1097  N  NE2 . GLN A  1 140 ? 12.784  -45.035 13.264  1.00 46.65  ? 140  GLN A NE2 1 
ATOM   1098  N  N   . VAL A  1 141 ? 11.302  -41.988 16.247  1.00 25.36  ? 141  VAL A N   1 
ATOM   1099  C  CA  . VAL A  1 141 ? 12.560  -41.263 16.478  1.00 26.82  ? 141  VAL A CA  1 
ATOM   1100  C  C   . VAL A  1 141 ? 13.077  -41.358 17.904  1.00 25.73  ? 141  VAL A C   1 
ATOM   1101  O  O   . VAL A  1 141 ? 14.258  -41.626 18.130  1.00 24.66  ? 141  VAL A O   1 
ATOM   1102  C  CB  . VAL A  1 141 ? 12.407  -39.761 16.173  1.00 37.48  ? 141  VAL A CB  1 
ATOM   1103  C  CG1 . VAL A  1 141 ? 13.742  -39.037 16.325  1.00 37.10  ? 141  VAL A CG1 1 
ATOM   1104  C  CG2 . VAL A  1 141 ? 11.843  -39.564 14.797  1.00 40.64  ? 141  VAL A CG2 1 
ATOM   1105  N  N   . GLU A  1 142 ? 12.198  -41.089 18.863  1.00 22.90  ? 142  GLU A N   1 
ATOM   1106  C  CA  . GLU A  1 142 ? 12.602  -41.102 20.257  1.00 22.65  ? 142  GLU A CA  1 
ATOM   1107  C  C   . GLU A  1 142 ? 12.299  -42.421 20.929  1.00 22.25  ? 142  GLU A C   1 
ATOM   1108  O  O   . GLU A  1 142 ? 12.431  -42.546 22.146  1.00 22.33  ? 142  GLU A O   1 
ATOM   1109  C  CB  . GLU A  1 142 ? 11.993  -39.939 21.028  1.00 31.72  ? 142  GLU A CB  1 
ATOM   1110  C  CG  . GLU A  1 142 ? 12.716  -38.643 20.783  1.00 38.66  ? 142  GLU A CG  1 
ATOM   1111  C  CD  . GLU A  1 142 ? 14.209  -38.783 20.978  1.00 46.94  ? 142  GLU A CD  1 
ATOM   1112  O  OE1 . GLU A  1 142 ? 14.630  -39.521 21.908  1.00 51.70  ? 142  GLU A OE1 1 
ATOM   1113  O  OE2 . GLU A  1 142 ? 14.957  -38.157 20.193  1.00 47.62  ? 142  GLU A OE2 1 
ATOM   1114  N  N   . GLY A  1 143 ? 11.843  -43.384 20.132  1.00 31.74  ? 143  GLY A N   1 
ATOM   1115  C  CA  . GLY A  1 143 ? 11.624  -44.743 20.597  1.00 33.92  ? 143  GLY A CA  1 
ATOM   1116  C  C   . GLY A  1 143 ? 10.685  -44.815 21.774  1.00 34.47  ? 143  GLY A C   1 
ATOM   1117  O  O   . GLY A  1 143 ? 10.826  -45.690 22.627  1.00 35.31  ? 143  GLY A O   1 
ATOM   1118  N  N   . ALA A  1 144 ? 9.733   -43.889 21.830  1.00 30.57  ? 144  ALA A N   1 
ATOM   1119  C  CA  . ALA A  1 144 ? 8.909   -43.773 23.014  1.00 27.68  ? 144  ALA A CA  1 
ATOM   1120  C  C   . ALA A  1 144 ? 7.620   -44.540 22.836  1.00 26.44  ? 144  ALA A C   1 
ATOM   1121  O  O   . ALA A  1 144 ? 7.333   -45.031 21.743  1.00 27.43  ? 144  ALA A O   1 
ATOM   1122  C  CB  . ALA A  1 144 ? 8.616   -42.334 23.291  1.00 20.76  ? 144  ALA A CB  1 
ATOM   1123  N  N   . VAL A  1 145 ? 6.846   -44.613 23.917  1.00 21.34  ? 145  VAL A N   1 
ATOM   1124  C  CA  . VAL A  1 145 ? 5.527   -45.216 23.903  1.00 18.91  ? 145  VAL A CA  1 
ATOM   1125  C  C   . VAL A  1 145 ? 4.569   -44.133 24.265  1.00 18.19  ? 145  VAL A C   1 
ATOM   1126  O  O   . VAL A  1 145 ? 4.658   -43.557 25.341  1.00 35.28  ? 145  VAL A O   1 
ATOM   1127  C  CB  . VAL A  1 145 ? 5.394   -46.333 24.924  1.00 22.44  ? 145  VAL A CB  1 
ATOM   1128  C  CG1 . VAL A  1 145 ? 3.935   -46.611 25.232  1.00 18.60  ? 145  VAL A CG1 1 
ATOM   1129  C  CG2 . VAL A  1 145 ? 6.054   -47.580 24.400  1.00 23.98  ? 145  VAL A CG2 1 
ATOM   1130  N  N   . LEU A  1 146 ? 3.651   -43.851 23.355  1.00 26.35  ? 146  LEU A N   1 
ATOM   1131  C  CA  . LEU A  1 146 ? 2.791   -42.687 23.486  1.00 27.08  ? 146  LEU A CA  1 
ATOM   1132  C  C   . LEU A  1 146 ? 1.321   -43.070 23.544  1.00 28.29  ? 146  LEU A C   1 
ATOM   1133  O  O   . LEU A  1 146 ? 0.847   -43.824 22.689  1.00 29.20  ? 146  LEU A O   1 
ATOM   1134  C  CB  . LEU A  1 146 ? 3.023   -41.764 22.303  1.00 18.09  ? 146  LEU A CB  1 
ATOM   1135  C  CG  . LEU A  1 146 ? 2.464   -40.376 22.513  1.00 17.44  ? 146  LEU A CG  1 
ATOM   1136  C  CD1 . LEU A  1 146 ? 3.539   -39.399 22.156  1.00 17.65  ? 146  LEU A CD1 1 
ATOM   1137  C  CD2 . LEU A  1 146 ? 1.238   -40.198 21.644  1.00 29.70  ? 146  LEU A CD2 1 
ATOM   1138  N  N   . VAL A  1 147 ? 0.603   -42.558 24.545  1.00 20.22  ? 147  VAL A N   1 
ATOM   1139  C  CA  . VAL A  1 147 ? -0.821  -42.844 24.663  1.00 20.75  ? 147  VAL A CA  1 
ATOM   1140  C  C   . VAL A  1 147 ? -1.645  -41.582 24.540  1.00 22.08  ? 147  VAL A C   1 
ATOM   1141  O  O   . VAL A  1 147 ? -1.223  -40.523 25.011  1.00 23.10  ? 147  VAL A O   1 
ATOM   1142  C  CB  . VAL A  1 147 ? -1.177  -43.495 25.996  1.00 16.70  ? 147  VAL A CB  1 
ATOM   1143  C  CG1 . VAL A  1 147 ? -2.501  -44.258 25.855  1.00 16.97  ? 147  VAL A CG1 1 
ATOM   1144  C  CG2 . VAL A  1 147 ? -0.076  -44.417 26.439  1.00 16.93  ? 147  VAL A CG2 1 
ATOM   1145  N  N   . SER A  1 148 ? -2.810  -41.695 23.897  1.00 23.24  ? 148  SER A N   1 
ATOM   1146  C  CA  . SER A  1 148 ? -3.783  -40.596 23.866  1.00 21.93  ? 148  SER A CA  1 
ATOM   1147  C  C   . SER A  1 148 ? -5.223  -41.089 23.979  1.00 24.05  ? 148  SER A C   1 
ATOM   1148  O  O   . SER A  1 148 ? -5.656  -41.944 23.209  1.00 29.17  ? 148  SER A O   1 
ATOM   1149  C  CB  . SER A  1 148 ? -3.621  -39.742 22.605  1.00 16.97  ? 148  SER A CB  1 
ATOM   1150  O  OG  . SER A  1 148 ? -3.738  -40.520 21.429  1.00 17.61  ? 148  SER A OG  1 
ATOM   1151  N  N   . MET A  1 149 ? -5.981  -40.536 24.917  1.00 16.60  ? 149  MET A N   1 
ATOM   1152  C  CA  . MET A  1 149 ? -7.353  -40.992 25.109  1.00 16.91  ? 149  MET A CA  1 
ATOM   1153  C  C   . MET A  1 149 ? -8.334  -39.923 24.693  1.00 17.06  ? 149  MET A C   1 
ATOM   1154  O  O   . MET A  1 149 ? -7.999  -38.740 24.685  1.00 16.77  ? 149  MET A O   1 
ATOM   1155  C  CB  . MET A  1 149 ? -7.614  -41.415 26.561  1.00 16.68  ? 149  MET A CB  1 
ATOM   1156  C  CG  . MET A  1 149 ? -7.994  -40.289 27.513  1.00 16.31  ? 149  MET A CG  1 
ATOM   1157  S  SD  . MET A  1 149 ? -6.777  -38.978 27.537  1.00 15.79  ? 149  MET A SD  1 
ATOM   1158  C  CE  . MET A  1 149 ? -5.477  -39.735 28.527  1.00 15.52  ? 149  MET A CE  1 
ATOM   1159  N  N   . ASN A  1 150 ? -9.528  -40.359 24.302  1.00 17.63  ? 150  ASN A N   1 
ATOM   1160  C  CA  . ASN A  1 150 ? -10.663 -39.465 24.146  1.00 20.73  ? 150  ASN A CA  1 
ATOM   1161  C  C   . ASN A  1 150 ? -11.319 -39.214 25.487  1.00 17.67  ? 150  ASN A C   1 
ATOM   1162  O  O   . ASN A  1 150 ? -11.390 -40.103 26.317  1.00 17.64  ? 150  ASN A O   1 
ATOM   1163  C  CB  . ASN A  1 150 ? -11.671 -40.074 23.189  1.00 18.76  ? 150  ASN A CB  1 
ATOM   1164  C  CG  . ASN A  1 150 ? -11.321 -39.800 21.759  1.00 21.21  ? 150  ASN A CG  1 
ATOM   1165  O  OD1 . ASN A  1 150 ? -10.267 -39.231 21.473  1.00 21.21  ? 150  ASN A OD1 1 
ATOM   1166  N  ND2 . ASN A  1 150 ? -12.194 -40.196 20.844  1.00 21.17  ? 150  ASN A ND2 1 
ATOM   1167  N  N   . TYR A  1 151 ? -11.785 -38.003 25.726  1.00 17.59  ? 151  TYR A N   1 
ATOM   1168  C  CA  . TYR A  1 151 ? -12.609 -37.795 26.900  1.00 22.32  ? 151  TYR A CA  1 
ATOM   1169  C  C   . TYR A  1 151 ? -13.832 -37.014 26.478  1.00 21.25  ? 151  TYR A C   1 
ATOM   1170  O  O   . TYR A  1 151 ? -13.760 -36.209 25.555  1.00 18.51  ? 151  TYR A O   1 
ATOM   1171  C  CB  . TYR A  1 151 ? -11.846 -37.080 28.016  1.00 16.93  ? 151  TYR A CB  1 
ATOM   1172  C  CG  . TYR A  1 151 ? -11.254 -35.754 27.618  1.00 16.66  ? 151  TYR A CG  1 
ATOM   1173  C  CD1 . TYR A  1 151 ? -10.087 -35.702 26.882  1.00 16.42  ? 151  TYR A CD1 1 
ATOM   1174  C  CD2 . TYR A  1 151 ? -11.845 -34.560 27.994  1.00 16.74  ? 151  TYR A CD2 1 
ATOM   1175  C  CE1 . TYR A  1 151 ? -9.519  -34.508 26.515  1.00 16.27  ? 151  TYR A CE1 1 
ATOM   1176  C  CE2 . TYR A  1 151 ? -11.288 -33.350 27.635  1.00 17.69  ? 151  TYR A CE2 1 
ATOM   1177  C  CZ  . TYR A  1 151 ? -10.117 -33.334 26.888  1.00 17.80  ? 151  TYR A CZ  1 
ATOM   1178  O  OH  . TYR A  1 151 ? -9.518  -32.154 26.499  1.00 18.74  ? 151  TYR A OH  1 
ATOM   1179  N  N   . ARG A  1 152 ? -14.958 -37.269 27.132  1.00 18.61  ? 152  ARG A N   1 
ATOM   1180  C  CA  . ARG A  1 152 ? -16.157 -36.501 26.850  1.00 20.18  ? 152  ARG A CA  1 
ATOM   1181  C  C   . ARG A  1 152 ? -15.951 -34.988 27.041  1.00 18.97  ? 152  ARG A C   1 
ATOM   1182  O  O   . ARG A  1 152 ? -15.517 -34.514 28.092  1.00 18.45  ? 152  ARG A O   1 
ATOM   1183  C  CB  . ARG A  1 152 ? -17.331 -37.020 27.678  1.00 19.84  ? 152  ARG A CB  1 
ATOM   1184  C  CG  . ARG A  1 152 ? -17.925 -38.291 27.131  1.00 20.55  ? 152  ARG A CG  1 
ATOM   1185  C  CD  . ARG A  1 152 ? -18.829 -38.937 28.133  1.00 21.06  ? 152  ARG A CD  1 
ATOM   1186  N  NE  . ARG A  1 152 ? -18.116 -39.284 29.353  1.00 20.42  ? 152  ARG A NE  1 
ATOM   1187  C  CZ  . ARG A  1 152 ? -18.706 -39.756 30.442  1.00 27.45  ? 152  ARG A CZ  1 
ATOM   1188  N  NH1 . ARG A  1 152 ? -20.015 -39.931 30.459  1.00 28.35  ? 152  ARG A NH1 1 
ATOM   1189  N  NH2 . ARG A  1 152 ? -17.997 -40.049 31.518  1.00 20.27  ? 152  ARG A NH2 1 
ATOM   1190  N  N   . VAL A  1 153 ? -16.251 -34.238 25.994  1.00 22.55  ? 153  VAL A N   1 
ATOM   1191  C  CA  . VAL A  1 153 ? -16.201 -32.796 26.044  1.00 19.34  ? 153  VAL A CA  1 
ATOM   1192  C  C   . VAL A  1 153 ? -17.629 -32.276 26.075  1.00 21.19  ? 153  VAL A C   1 
ATOM   1193  O  O   . VAL A  1 153 ? -18.584 -33.061 25.985  1.00 20.86  ? 153  VAL A O   1 
ATOM   1194  C  CB  . VAL A  1 153 ? -15.525 -32.276 24.788  1.00 24.14  ? 153  VAL A CB  1 
ATOM   1195  C  CG1 . VAL A  1 153 ? -14.038 -32.545 24.855  1.00 23.57  ? 153  VAL A CG1 1 
ATOM   1196  C  CG2 . VAL A  1 153 ? -16.143 -32.943 23.549  1.00 23.17  ? 153  VAL A CG2 1 
ATOM   1197  N  N   . GLY A  1 154 ? -17.779 -30.957 26.177  1.00 23.92  ? 154  GLY A N   1 
ATOM   1198  C  CA  . GLY A  1 154 ? -19.087 -30.324 26.068  1.00 28.43  ? 154  GLY A CA  1 
ATOM   1199  C  C   . GLY A  1 154 ? -20.041 -30.636 27.210  1.00 29.88  ? 154  GLY A C   1 
ATOM   1200  O  O   . GLY A  1 154 ? -19.606 -30.803 28.345  1.00 21.01  ? 154  GLY A O   1 
ATOM   1201  N  N   . THR A  1 155 ? -21.341 -30.703 26.920  1.00 28.68  ? 155  THR A N   1 
ATOM   1202  C  CA  . THR A  1 155 ? -22.322 -30.996 27.963  1.00 28.32  ? 155  THR A CA  1 
ATOM   1203  C  C   . THR A  1 155 ? -22.158 -32.430 28.444  1.00 33.22  ? 155  THR A C   1 
ATOM   1204  O  O   . THR A  1 155 ? -22.286 -32.713 29.633  1.00 36.77  ? 155  THR A O   1 
ATOM   1205  C  CB  . THR A  1 155 ? -23.771 -30.767 27.499  1.00 24.56  ? 155  THR A CB  1 
ATOM   1206  O  OG1 . THR A  1 155 ? -23.904 -31.183 26.141  1.00 25.06  ? 155  THR A OG1 1 
ATOM   1207  C  CG2 . THR A  1 155 ? -24.145 -29.309 27.597  1.00 24.98  ? 155  THR A CG2 1 
ATOM   1208  N  N   . PHE A  1 156 ? -21.852 -33.327 27.512  1.00 38.42  ? 156  PHE A N   1 
ATOM   1209  C  CA  . PHE A  1 156 ? -21.721 -34.743 27.816  1.00 38.75  ? 156  PHE A CA  1 
ATOM   1210  C  C   . PHE A  1 156 ? -20.580 -34.971 28.765  1.00 39.40  ? 156  PHE A C   1 
ATOM   1211  O  O   . PHE A  1 156 ? -20.644 -35.844 29.623  1.00 44.52  ? 156  PHE A O   1 
ATOM   1212  C  CB  . PHE A  1 156 ? -21.449 -35.525 26.547  1.00 33.60  ? 156  PHE A CB  1 
ATOM   1213  C  CG  . PHE A  1 156 ? -22.293 -35.104 25.408  1.00 35.74  ? 156  PHE A CG  1 
ATOM   1214  C  CD1 . PHE A  1 156 ? -23.539 -35.661 25.221  1.00 38.64  ? 156  PHE A CD1 1 
ATOM   1215  C  CD2 . PHE A  1 156 ? -21.851 -34.133 24.531  1.00 36.76  ? 156  PHE A CD2 1 
ATOM   1216  C  CE1 . PHE A  1 156 ? -24.326 -35.265 24.177  1.00 41.86  ? 156  PHE A CE1 1 
ATOM   1217  C  CE2 . PHE A  1 156 ? -22.634 -33.730 23.484  1.00 38.88  ? 156  PHE A CE2 1 
ATOM   1218  C  CZ  . PHE A  1 156 ? -23.873 -34.296 23.302  1.00 41.74  ? 156  PHE A CZ  1 
ATOM   1219  N  N   . GLY A  1 157 ? -19.505 -34.226 28.572  1.00 31.34  ? 157  GLY A N   1 
ATOM   1220  C  CA  . GLY A  1 157 ? -18.395 -34.297 29.492  1.00 32.22  ? 157  GLY A CA  1 
ATOM   1221  C  C   . GLY A  1 157 ? -18.535 -33.513 30.779  1.00 31.72  ? 157  GLY A C   1 
ATOM   1222  O  O   . GLY A  1 157 ? -18.150 -33.975 31.855  1.00 33.54  ? 157  GLY A O   1 
ATOM   1223  N  N   . PHE A  1 158 ? -18.939 -32.261 30.644  1.00 25.43  ? 158  PHE A N   1 
ATOM   1224  C  CA  . PHE A  1 158 ? -18.979 -31.365 31.793  1.00 26.11  ? 158  PHE A CA  1 
ATOM   1225  C  C   . PHE A  1 158 ? -20.286 -30.828 32.385  1.00 25.57  ? 158  PHE A C   1 
ATOM   1226  O  O   . PHE A  1 158 ? -20.230 -30.037 33.327  1.00 25.41  ? 158  PHE A O   1 
ATOM   1227  C  CB  . PHE A  1 158 ? -17.881 -30.309 31.680  1.00 27.05  ? 158  PHE A CB  1 
ATOM   1228  C  CG  . PHE A  1 158 ? -16.526 -30.911 31.453  1.00 25.74  ? 158  PHE A CG  1 
ATOM   1229  C  CD1 . PHE A  1 158 ? -15.774 -31.363 32.515  1.00 23.54  ? 158  PHE A CD1 1 
ATOM   1230  C  CD2 . PHE A  1 158 ? -16.035 -31.087 30.167  1.00 24.82  ? 158  PHE A CD2 1 
ATOM   1231  C  CE1 . PHE A  1 158 ? -14.551 -31.923 32.304  1.00 22.76  ? 158  PHE A CE1 1 
ATOM   1232  C  CE2 . PHE A  1 158 ? -14.811 -31.657 29.954  1.00 22.02  ? 158  PHE A CE2 1 
ATOM   1233  C  CZ  . PHE A  1 158 ? -14.069 -32.069 31.023  1.00 22.89  ? 158  PHE A CZ  1 
ATOM   1234  N  N   . LEU A  1 159 ? -21.443 -31.193 31.835  1.00 27.41  ? 159  LEU A N   1 
ATOM   1235  C  CA  . LEU A  1 159 ? -22.685 -30.666 32.399  1.00 26.51  ? 159  LEU A CA  1 
ATOM   1236  C  C   . LEU A  1 159 ? -22.794 -31.226 33.803  1.00 27.73  ? 159  LEU A C   1 
ATOM   1237  O  O   . LEU A  1 159 ? -22.565 -32.413 34.012  1.00 28.72  ? 159  LEU A O   1 
ATOM   1238  C  CB  . LEU A  1 159 ? -23.916 -31.029 31.558  1.00 23.93  ? 159  LEU A CB  1 
ATOM   1239  C  CG  . LEU A  1 159 ? -25.251 -30.431 32.026  1.00 25.13  ? 159  LEU A CG  1 
ATOM   1240  C  CD1 . LEU A  1 159 ? -26.141 -30.105 30.840  1.00 26.14  ? 159  LEU A CD1 1 
ATOM   1241  C  CD2 . LEU A  1 159 ? -25.967 -31.356 33.010  1.00 25.72  ? 159  LEU A CD2 1 
ATOM   1242  N  N   . ALA A  1 160 ? -23.109 -30.377 34.771  1.00 23.13  ? 160  ALA A N   1 
ATOM   1243  C  CA  . ALA A  1 160 ? -23.076 -30.819 36.153  1.00 23.16  ? 160  ALA A CA  1 
ATOM   1244  C  C   . ALA A  1 160 ? -24.188 -30.189 36.940  1.00 26.30  ? 160  ALA A C   1 
ATOM   1245  O  O   . ALA A  1 160 ? -24.447 -28.994 36.813  1.00 24.51  ? 160  ALA A O   1 
ATOM   1246  C  CB  . ALA A  1 160 ? -21.745 -30.481 36.794  1.00 28.80  ? 160  ALA A CB  1 
ATOM   1247  N  N   . LEU A  1 161 ? -24.838 -31.014 37.755  1.00 41.13  ? 161  LEU A N   1 
ATOM   1248  C  CA  . LEU A  1 161 ? -25.795 -30.562 38.749  1.00 38.28  ? 161  LEU A CA  1 
ATOM   1249  C  C   . LEU A  1 161 ? -25.263 -31.054 40.065  1.00 35.19  ? 161  LEU A C   1 
ATOM   1250  O  O   . LEU A  1 161 ? -25.727 -32.064 40.573  1.00 34.76  ? 161  LEU A O   1 
ATOM   1251  C  CB  . LEU A  1 161 ? -27.164 -31.165 38.488  1.00 32.07  ? 161  LEU A CB  1 
ATOM   1252  C  CG  . LEU A  1 161 ? -27.832 -30.548 37.277  1.00 27.76  ? 161  LEU A CG  1 
ATOM   1253  C  CD1 . LEU A  1 161 ? -29.168 -31.161 37.094  1.00 29.17  ? 161  LEU A CD1 1 
ATOM   1254  C  CD2 . LEU A  1 161 ? -27.971 -29.076 37.515  1.00 28.00  ? 161  LEU A CD2 1 
ATOM   1255  N  N   . PRO A  1 162 ? -24.287 -30.322 40.622  1.00 33.67  ? 162  PRO A N   1 
ATOM   1256  C  CA  . PRO A  1 162 ? -23.376 -30.758 41.687  1.00 37.61  ? 162  PRO A CA  1 
ATOM   1257  C  C   . PRO A  1 162 ? -24.092 -31.299 42.914  1.00 42.23  ? 162  PRO A C   1 
ATOM   1258  O  O   . PRO A  1 162 ? -25.024 -30.680 43.440  1.00 40.94  ? 162  PRO A O   1 
ATOM   1259  C  CB  . PRO A  1 162 ? -22.618 -29.480 42.038  1.00 31.65  ? 162  PRO A CB  1 
ATOM   1260  C  CG  . PRO A  1 162 ? -22.744 -28.626 40.830  1.00 29.51  ? 162  PRO A CG  1 
ATOM   1261  C  CD  . PRO A  1 162 ? -24.104 -28.898 40.305  1.00 28.21  ? 162  PRO A CD  1 
ATOM   1262  N  N   . GLY A  1 163 ? -23.651 -32.466 43.361  1.00 49.26  ? 163  GLY A N   1 
ATOM   1263  C  CA  . GLY A  1 163 ? -24.298 -33.122 44.478  1.00 53.36  ? 163  GLY A CA  1 
ATOM   1264  C  C   . GLY A  1 163 ? -25.427 -34.055 44.087  1.00 51.04  ? 163  GLY A C   1 
ATOM   1265  O  O   . GLY A  1 163 ? -26.163 -34.532 44.944  1.00 52.16  ? 163  GLY A O   1 
ATOM   1266  N  N   . SER A  1 164 ? -25.565 -34.317 42.794  1.00 43.15  ? 164  SER A N   1 
ATOM   1267  C  CA  . SER A  1 164 ? -26.549 -35.278 42.315  1.00 42.02  ? 164  SER A CA  1 
ATOM   1268  C  C   . SER A  1 164 ? -25.846 -36.520 41.782  1.00 42.22  ? 164  SER A C   1 
ATOM   1269  O  O   . SER A  1 164 ? -24.743 -36.436 41.244  1.00 44.34  ? 164  SER A O   1 
ATOM   1270  C  CB  . SER A  1 164 ? -27.396 -34.677 41.201  1.00 34.98  ? 164  SER A CB  1 
ATOM   1271  O  OG  . SER A  1 164 ? -26.969 -35.204 39.958  1.00 33.86  ? 164  SER A OG  1 
ATOM   1272  N  N   . ARG A  1 165 ? -26.486 -37.674 41.935  1.00 34.02  ? 165  ARG A N   1 
ATOM   1273  C  CA  . ARG A  1 165 ? -25.907 -38.916 41.460  1.00 34.36  ? 165  ARG A CA  1 
ATOM   1274  C  C   . ARG A  1 165 ? -25.979 -38.937 39.940  1.00 30.49  ? 165  ARG A C   1 
ATOM   1275  O  O   . ARG A  1 165 ? -25.179 -39.597 39.287  1.00 28.69  ? 165  ARG A O   1 
ATOM   1276  C  CB  . ARG A  1 165 ? -26.606 -40.144 42.085  1.00 56.17  ? 165  ARG A CB  1 
ATOM   1277  C  CG  . ARG A  1 165 ? -27.488 -40.970 41.128  1.00 65.66  ? 165  ARG A CG  1 
ATOM   1278  C  CD  . ARG A  1 165 ? -27.035 -42.437 41.022  1.00 73.89  ? 165  ARG A CD  1 
ATOM   1279  N  NE  . ARG A  1 165 ? -27.726 -43.179 39.958  1.00 82.65  ? 165  ARG A NE  1 
ATOM   1280  C  CZ  . ARG A  1 165 ? -27.359 -44.381 39.500  1.00 89.27  ? 165  ARG A CZ  1 
ATOM   1281  N  NH1 . ARG A  1 165 ? -26.292 -45.000 40.005  1.00 89.68  ? 165  ARG A NH1 1 
ATOM   1282  N  NH2 . ARG A  1 165 ? -28.059 -44.970 38.529  1.00 91.57  ? 165  ARG A NH2 1 
ATOM   1283  N  N   . GLU A  1 166 ? -26.931 -38.199 39.382  1.00 39.02  ? 166  GLU A N   1 
ATOM   1284  C  CA  . GLU A  1 166 ? -27.248 -38.321 37.960  1.00 42.80  ? 166  GLU A CA  1 
ATOM   1285  C  C   . GLU A  1 166 ? -26.334 -37.540 37.003  1.00 33.55  ? 166  GLU A C   1 
ATOM   1286  O  O   . GLU A  1 166 ? -26.107 -37.967 35.869  1.00 29.96  ? 166  GLU A O   1 
ATOM   1287  C  CB  . GLU A  1 166 ? -28.720 -37.973 37.717  1.00 69.02  ? 166  GLU A CB  1 
ATOM   1288  C  CG  . GLU A  1 166 ? -29.482 -39.049 36.983  1.00 80.51  ? 166  GLU A CG  1 
ATOM   1289  C  CD  . GLU A  1 166 ? -29.356 -40.406 37.647  1.00 89.59  ? 166  GLU A CD  1 
ATOM   1290  O  OE1 . GLU A  1 166 ? -29.789 -40.536 38.813  1.00 93.68  ? 166  GLU A OE1 1 
ATOM   1291  O  OE2 . GLU A  1 166 ? -28.820 -41.340 37.005  1.00 91.20  ? 166  GLU A OE2 1 
ATOM   1292  N  N   . ALA A  1 167 ? -25.856 -36.382 37.448  1.00 26.19  ? 167  ALA A N   1 
ATOM   1293  C  CA  . ALA A  1 167 ? -24.981 -35.541 36.641  1.00 25.13  ? 167  ALA A CA  1 
ATOM   1294  C  C   . ALA A  1 167 ? -23.942 -34.899 37.563  1.00 24.92  ? 167  ALA A C   1 
ATOM   1295  O  O   . ALA A  1 167 ? -23.965 -33.697 37.853  1.00 24.19  ? 167  ALA A O   1 
ATOM   1296  C  CB  . ALA A  1 167 ? -25.786 -34.505 35.896  1.00 30.07  ? 167  ALA A CB  1 
ATOM   1297  N  N   . PRO A  1 168 ? -23.026 -35.725 38.043  1.00 23.61  ? 168  PRO A N   1 
ATOM   1298  C  CA  . PRO A  1 168 ? -22.153 -35.367 39.148  1.00 25.27  ? 168  PRO A CA  1 
ATOM   1299  C  C   . PRO A  1 168 ? -21.105 -34.335 38.756  1.00 28.12  ? 168  PRO A C   1 
ATOM   1300  O  O   . PRO A  1 168 ? -20.601 -33.623 39.635  1.00 30.95  ? 168  PRO A O   1 
ATOM   1301  C  CB  . PRO A  1 168 ? -21.479 -36.696 39.487  1.00 30.93  ? 168  PRO A CB  1 
ATOM   1302  C  CG  . PRO A  1 168 ? -22.221 -37.744 38.707  1.00 33.06  ? 168  PRO A CG  1 
ATOM   1303  C  CD  . PRO A  1 168 ? -22.706 -37.049 37.508  1.00 23.46  ? 168  PRO A CD  1 
ATOM   1304  N  N   . GLY A  1 169 ? -20.756 -34.274 37.471  1.00 38.42  ? 169  GLY A N   1 
ATOM   1305  C  CA  . GLY A  1 169 ? -19.718 -33.367 37.006  1.00 36.19  ? 169  GLY A CA  1 
ATOM   1306  C  C   . GLY A  1 169 ? -18.307 -33.932 36.989  1.00 34.11  ? 169  GLY A C   1 
ATOM   1307  O  O   . GLY A  1 169 ? -17.961 -34.823 37.771  1.00 36.72  ? 169  GLY A O   1 
ATOM   1308  N  N   . ASN A  1 170 ? -17.492 -33.372 36.098  1.00 28.68  ? 170  ASN A N   1 
ATOM   1309  C  CA  . ASN A  1 170 ? -16.135 -33.840 35.790  1.00 25.08  ? 170  ASN A CA  1 
ATOM   1310  C  C   . ASN A  1 170 ? -16.062 -35.267 35.253  1.00 24.25  ? 170  ASN A C   1 
ATOM   1311  O  O   . ASN A  1 170 ? -15.008 -35.911 35.308  1.00 20.47  ? 170  ASN A O   1 
ATOM   1312  C  CB  . ASN A  1 170 ? -15.201 -33.727 36.990  1.00 19.54  ? 170  ASN A CB  1 
ATOM   1313  C  CG  . ASN A  1 170 ? -15.297 -32.410 37.676  1.00 18.03  ? 170  ASN A CG  1 
ATOM   1314  O  OD1 . ASN A  1 170 ? -15.541 -31.377 37.052  1.00 18.08  ? 170  ASN A OD1 1 
ATOM   1315  N  ND2 . ASN A  1 170 ? -15.104 -32.429 38.987  1.00 18.59  ? 170  ASN A ND2 1 
ATOM   1316  N  N   . VAL A  1 171 ? -17.160 -35.761 34.706  1.00 30.58  ? 171  VAL A N   1 
ATOM   1317  C  CA  . VAL A  1 171 ? -17.127 -37.112 34.193  1.00 30.40  ? 171  VAL A CA  1 
ATOM   1318  C  C   . VAL A  1 171 ? -16.080 -37.204 33.069  1.00 28.82  ? 171  VAL A C   1 
ATOM   1319  O  O   . VAL A  1 171 ? -15.459 -38.246 32.896  1.00 31.89  ? 171  VAL A O   1 
ATOM   1320  C  CB  . VAL A  1 171 ? -18.547 -37.657 33.837  1.00 29.10  ? 171  VAL A CB  1 
ATOM   1321  C  CG1 . VAL A  1 171 ? -19.502 -37.386 34.981  1.00 20.75  ? 171  VAL A CG1 1 
ATOM   1322  C  CG2 . VAL A  1 171 ? -19.074 -37.048 32.571  1.00 20.36  ? 171  VAL A CG2 1 
ATOM   1323  N  N   . GLY A  1 172 ? -15.831 -36.101 32.361  1.00 23.57  ? 172  GLY A N   1 
ATOM   1324  C  CA  . GLY A  1 172 ? -14.775 -36.081 31.359  1.00 23.71  ? 172  GLY A CA  1 
ATOM   1325  C  C   . GLY A  1 172 ? -13.374 -36.302 31.939  1.00 24.17  ? 172  GLY A C   1 
ATOM   1326  O  O   . GLY A  1 172 ? -12.553 -37.076 31.403  1.00 24.50  ? 172  GLY A O   1 
ATOM   1327  N  N   . LEU A  1 173 ? -13.103 -35.610 33.045  1.00 16.89  ? 173  LEU A N   1 
ATOM   1328  C  CA  . LEU A  1 173 ? -11.848 -35.734 33.764  1.00 16.27  ? 173  LEU A CA  1 
ATOM   1329  C  C   . LEU A  1 173 ? -11.722 -37.164 34.296  1.00 16.69  ? 173  LEU A C   1 
ATOM   1330  O  O   . LEU A  1 173 ? -10.621 -37.724 34.420  1.00 16.10  ? 173  LEU A O   1 
ATOM   1331  C  CB  . LEU A  1 173 ? -11.803 -34.717 34.914  1.00 16.80  ? 173  LEU A CB  1 
ATOM   1332  C  CG  . LEU A  1 173 ? -11.480 -33.248 34.591  1.00 16.03  ? 173  LEU A CG  1 
ATOM   1333  C  CD1 . LEU A  1 173 ? -11.644 -32.381 35.816  1.00 16.18  ? 173  LEU A CD1 1 
ATOM   1334  C  CD2 . LEU A  1 173 ? -10.074 -33.078 34.042  1.00 15.53  ? 173  LEU A CD2 1 
ATOM   1335  N  N   . LEU A  1 174 ? -12.868 -37.758 34.599  1.00 19.11  ? 174  LEU A N   1 
ATOM   1336  C  CA  . LEU A  1 174 ? -12.896 -39.135 35.051  1.00 21.37  ? 174  LEU A CA  1 
ATOM   1337  C  C   . LEU A  1 174 ? -12.546 -40.086 33.913  1.00 21.77  ? 174  LEU A C   1 
ATOM   1338  O  O   . LEU A  1 174 ? -11.902 -41.108 34.142  1.00 22.56  ? 174  LEU A O   1 
ATOM   1339  C  CB  . LEU A  1 174 ? -14.264 -39.482 35.632  1.00 24.38  ? 174  LEU A CB  1 
ATOM   1340  C  CG  . LEU A  1 174 ? -14.587 -38.730 36.908  1.00 18.22  ? 174  LEU A CG  1 
ATOM   1341  C  CD1 . LEU A  1 174 ? -15.907 -39.205 37.450  1.00 19.11  ? 174  LEU A CD1 1 
ATOM   1342  C  CD2 . LEU A  1 174 ? -13.453 -38.932 37.909  1.00 17.89  ? 174  LEU A CD2 1 
ATOM   1343  N  N   . ASP A  1 175 ? -12.994 -39.756 32.699  1.00 19.55  ? 175  ASP A N   1 
ATOM   1344  C  CA  . ASP A  1 175 ? -12.675 -40.545 31.515  1.00 20.38  ? 175  ASP A CA  1 
ATOM   1345  C  C   . ASP A  1 175 ? -11.178 -40.597 31.405  1.00 21.88  ? 175  ASP A C   1 
ATOM   1346  O  O   . ASP A  1 175 ? -10.581 -41.677 31.273  1.00 21.49  ? 175  ASP A O   1 
ATOM   1347  C  CB  . ASP A  1 175 ? -13.220 -39.884 30.254  1.00 19.47  ? 175  ASP A CB  1 
ATOM   1348  C  CG  . ASP A  1 175 ? -14.723 -39.942 30.170  1.00 20.56  ? 175  ASP A CG  1 
ATOM   1349  O  OD1 . ASP A  1 175 ? -15.322 -40.760 30.907  1.00 18.86  ? 175  ASP A OD1 1 
ATOM   1350  O  OD2 . ASP A  1 175 ? -15.300 -39.181 29.355  1.00 19.72  ? 175  ASP A OD2 1 
ATOM   1351  N  N   . GLN A  1 176 ? -10.588 -39.404 31.471  1.00 28.98  ? 176  GLN A N   1 
ATOM   1352  C  CA  . GLN A  1 176 ? -9.142  -39.262 31.467  1.00 25.79  ? 176  GLN A CA  1 
ATOM   1353  C  C   . GLN A  1 176 ? -8.499  -40.157 32.512  1.00 28.34  ? 176  GLN A C   1 
ATOM   1354  O  O   . GLN A  1 176 ? -7.658  -40.986 32.172  1.00 32.47  ? 176  GLN A O   1 
ATOM   1355  C  CB  . GLN A  1 176 ? -8.758  -37.818 31.755  1.00 15.85  ? 176  GLN A CB  1 
ATOM   1356  C  CG  . GLN A  1 176 ? -9.011  -36.866 30.616  1.00 15.56  ? 176  GLN A CG  1 
ATOM   1357  C  CD  . GLN A  1 176 ? -8.750  -35.439 31.014  1.00 15.32  ? 176  GLN A CD  1 
ATOM   1358  O  OE1 . GLN A  1 176 ? -8.314  -35.163 32.136  1.00 15.13  ? 176  GLN A OE1 1 
ATOM   1359  N  NE2 . GLN A  1 176 ? -9.026  -34.515 30.103  1.00 15.44  ? 176  GLN A NE2 1 
ATOM   1360  N  N   . ARG A  1 177 ? -8.901  -40.010 33.775  1.00 17.36  ? 177  ARG A N   1 
ATOM   1361  C  CA  . ARG A  1 177 ? -8.306  -40.812 34.849  1.00 16.08  ? 177  ARG A CA  1 
ATOM   1362  C  C   . ARG A  1 177 ? -8.429  -42.299 34.579  1.00 16.49  ? 177  ARG A C   1 
ATOM   1363  O  O   . ARG A  1 177 ? -7.505  -43.059 34.843  1.00 16.53  ? 177  ARG A O   1 
ATOM   1364  C  CB  . ARG A  1 177 ? -8.929  -40.505 36.218  1.00 32.36  ? 177  ARG A CB  1 
ATOM   1365  C  CG  . ARG A  1 177 ? -8.472  -41.470 37.328  1.00 16.64  ? 177  ARG A CG  1 
ATOM   1366  C  CD  . ARG A  1 177 ? -9.142  -41.190 38.661  1.00 19.92  ? 177  ARG A CD  1 
ATOM   1367  N  NE  . ARG A  1 177 ? -8.779  -39.875 39.179  1.00 21.61  ? 177  ARG A NE  1 
ATOM   1368  C  CZ  . ARG A  1 177 ? -9.523  -39.165 40.027  1.00 23.36  ? 177  ARG A CZ  1 
ATOM   1369  N  NH1 . ARG A  1 177 ? -10.691 -39.647 40.467  1.00 23.08  ? 177  ARG A NH1 1 
ATOM   1370  N  NH2 . ARG A  1 177 ? -9.099  -37.965 40.431  1.00 22.49  ? 177  ARG A NH2 1 
ATOM   1371  N  N   . LEU A  1 178 ? -9.581  -42.707 34.057  1.00 27.15  ? 178  LEU A N   1 
ATOM   1372  C  CA  . LEU A  1 178 ? -9.838  -44.111 33.755  1.00 27.97  ? 178  LEU A CA  1 
ATOM   1373  C  C   . LEU A  1 178 ? -8.787  -44.609 32.786  1.00 17.27  ? 178  LEU A C   1 
ATOM   1374  O  O   . LEU A  1 178 ? -8.167  -45.633 33.019  1.00 17.49  ? 178  LEU A O   1 
ATOM   1375  C  CB  . LEU A  1 178 ? -11.240 -44.322 33.170  1.00 17.99  ? 178  LEU A CB  1 
ATOM   1376  C  CG  . LEU A  1 178 ? -11.621 -45.799 33.067  1.00 18.71  ? 178  LEU A CG  1 
ATOM   1377  C  CD1 . LEU A  1 178 ? -11.741 -46.390 34.443  1.00 26.80  ? 178  LEU A CD1 1 
ATOM   1378  C  CD2 . LEU A  1 178 ? -12.906 -45.978 32.326  1.00 27.42  ? 178  LEU A CD2 1 
ATOM   1379  N  N   . ALA A  1 179 ? -8.582  -43.858 31.712  1.00 16.95  ? 179  ALA A N   1 
ATOM   1380  C  CA  . ALA A  1 179 ? -7.550  -44.190 30.743  1.00 16.85  ? 179  ALA A CA  1 
ATOM   1381  C  C   . ALA A  1 179 ? -6.144  -44.191 31.371  1.00 16.53  ? 179  ALA A C   1 
ATOM   1382  O  O   . ALA A  1 179 ? -5.261  -44.939 30.946  1.00 16.67  ? 179  ALA A O   1 
ATOM   1383  C  CB  . ALA A  1 179 ? -7.623  -43.234 29.572  1.00 16.66  ? 179  ALA A CB  1 
ATOM   1384  N  N   . LEU A  1 180 ? -5.940  -43.356 32.384  1.00 17.64  ? 180  LEU A N   1 
ATOM   1385  C  CA  . LEU A  1 180 ? -4.687  -43.379 33.132  1.00 16.06  ? 180  LEU A CA  1 
ATOM   1386  C  C   . LEU A  1 180 ? -4.513  -44.703 33.843  1.00 18.37  ? 180  LEU A C   1 
ATOM   1387  O  O   . LEU A  1 180 ? -3.443  -45.312 33.766  1.00 20.19  ? 180  LEU A O   1 
ATOM   1388  C  CB  . LEU A  1 180 ? -4.614  -42.244 34.142  1.00 15.76  ? 180  LEU A CB  1 
ATOM   1389  C  CG  . LEU A  1 180 ? -3.934  -40.977 33.640  1.00 15.35  ? 180  LEU A CG  1 
ATOM   1390  C  CD1 . LEU A  1 180 ? -4.652  -40.413 32.430  1.00 15.24  ? 180  LEU A CD1 1 
ATOM   1391  C  CD2 . LEU A  1 180 ? -3.888  -39.971 34.742  1.00 15.19  ? 180  LEU A CD2 1 
ATOM   1392  N  N   . GLN A  1 181 ? -5.564  -45.149 34.532  1.00 17.63  ? 181  GLN A N   1 
ATOM   1393  C  CA  . GLN A  1 181 ? -5.574  -46.475 35.151  1.00 21.44  ? 181  GLN A CA  1 
ATOM   1394  C  C   . GLN A  1 181 ? -5.285  -47.516 34.090  1.00 19.89  ? 181  GLN A C   1 
ATOM   1395  O  O   . GLN A  1 181 ? -4.462  -48.397 34.300  1.00 20.23  ? 181  GLN A O   1 
ATOM   1396  C  CB  . GLN A  1 181 ? -6.914  -46.792 35.808  1.00 36.10  ? 181  GLN A CB  1 
ATOM   1397  C  CG  . GLN A  1 181 ? -7.276  -45.917 36.976  1.00 43.92  ? 181  GLN A CG  1 
ATOM   1398  C  CD  . GLN A  1 181 ? -8.723  -46.104 37.365  1.00 53.94  ? 181  GLN A CD  1 
ATOM   1399  O  OE1 . GLN A  1 181 ? -9.259  -47.209 37.254  1.00 60.91  ? 181  GLN A OE1 1 
ATOM   1400  N  NE2 . GLN A  1 181 ? -9.377  -45.026 37.797  1.00 53.52  ? 181  GLN A NE2 1 
ATOM   1401  N  N   . TRP A  1 182 ? -5.953  -47.395 32.949  1.00 17.76  ? 182  TRP A N   1 
ATOM   1402  C  CA  . TRP A  1 182 ? -5.787  -48.344 31.863  1.00 18.16  ? 182  TRP A CA  1 
ATOM   1403  C  C   . TRP A  1 182 ? -4.323  -48.473 31.476  1.00 18.02  ? 182  TRP A C   1 
ATOM   1404  O  O   . TRP A  1 182 ? -3.829  -49.578 31.274  1.00 18.52  ? 182  TRP A O   1 
ATOM   1405  C  CB  . TRP A  1 182 ? -6.615  -47.954 30.635  1.00 18.16  ? 182  TRP A CB  1 
ATOM   1406  C  CG  . TRP A  1 182 ? -6.614  -49.032 29.577  1.00 18.75  ? 182  TRP A CG  1 
ATOM   1407  C  CD1 . TRP A  1 182 ? -7.577  -49.975 29.380  1.00 19.47  ? 182  TRP A CD1 1 
ATOM   1408  C  CD2 . TRP A  1 182 ? -5.585  -49.302 28.602  1.00 18.80  ? 182  TRP A CD2 1 
ATOM   1409  N  NE1 . TRP A  1 182 ? -7.225  -50.804 28.336  1.00 19.96  ? 182  TRP A NE1 1 
ATOM   1410  C  CE2 . TRP A  1 182 ? -6.009  -50.410 27.845  1.00 19.56  ? 182  TRP A CE2 1 
ATOM   1411  C  CE3 . TRP A  1 182 ? -4.370  -48.703 28.286  1.00 18.39  ? 182  TRP A CE3 1 
ATOM   1412  C  CZ2 . TRP A  1 182 ? -5.260  -50.925 26.796  1.00 19.89  ? 182  TRP A CZ2 1 
ATOM   1413  C  CZ3 . TRP A  1 182 ? -3.636  -49.220 27.245  1.00 21.87  ? 182  TRP A CZ3 1 
ATOM   1414  C  CH2 . TRP A  1 182 ? -4.080  -50.317 26.515  1.00 19.46  ? 182  TRP A CH2 1 
ATOM   1415  N  N   . VAL A  1 183 ? -3.640  -47.341 31.360  1.00 17.45  ? 183  VAL A N   1 
ATOM   1416  C  CA  . VAL A  1 183 ? -2.211  -47.361 31.102  1.00 17.40  ? 183  VAL A CA  1 
ATOM   1417  C  C   . VAL A  1 183 ? -1.488  -48.099 32.215  1.00 18.07  ? 183  VAL A C   1 
ATOM   1418  O  O   . VAL A  1 183 ? -0.656  -48.954 31.930  1.00 20.21  ? 183  VAL A O   1 
ATOM   1419  C  CB  . VAL A  1 183 ? -1.634  -45.959 30.899  1.00 16.83  ? 183  VAL A CB  1 
ATOM   1420  C  CG1 . VAL A  1 183 ? -0.131  -46.002 30.910  1.00 16.91  ? 183  VAL A CG1 1 
ATOM   1421  C  CG2 . VAL A  1 183 ? -2.128  -45.406 29.590  1.00 16.71  ? 183  VAL A CG2 1 
ATOM   1422  N  N   . GLN A  1 184 ? -1.824  -47.812 33.473  1.00 17.64  ? 184  GLN A N   1 
ATOM   1423  C  CA  . GLN A  1 184 ? -1.199  -48.546 34.582  1.00 18.09  ? 184  GLN A CA  1 
ATOM   1424  C  C   . GLN A  1 184 ? -1.335  -50.066 34.424  1.00 21.57  ? 184  GLN A C   1 
ATOM   1425  O  O   . GLN A  1 184 ? -0.324  -50.776 34.421  1.00 22.57  ? 184  GLN A O   1 
ATOM   1426  C  CB  . GLN A  1 184 ? -1.733  -48.104 35.942  1.00 24.48  ? 184  GLN A CB  1 
ATOM   1427  C  CG  . GLN A  1 184 ? -0.997  -48.744 37.102  1.00 30.39  ? 184  GLN A CG  1 
ATOM   1428  C  CD  . GLN A  1 184 ? -1.401  -48.197 38.483  1.00 34.67  ? 184  GLN A CD  1 
ATOM   1429  O  OE1 . GLN A  1 184 ? -2.471  -48.538 39.029  1.00 34.22  ? 184  GLN A OE1 1 
ATOM   1430  N  NE2 . GLN A  1 184 ? -0.522  -47.367 39.066  1.00 35.25  ? 184  GLN A NE2 1 
ATOM   1431  N  N   . GLU A  1 185 ? -2.571  -50.548 34.258  1.00 26.26  ? 185  GLU A N   1 
ATOM   1432  C  CA  . GLU A  1 185 ? -2.859  -51.977 34.127  1.00 31.43  ? 185  GLU A CA  1 
ATOM   1433  C  C   . GLU A  1 185 ? -2.250  -52.660 32.905  1.00 31.10  ? 185  GLU A C   1 
ATOM   1434  O  O   . GLU A  1 185 ? -1.689  -53.744 33.012  1.00 37.14  ? 185  GLU A O   1 
ATOM   1435  C  CB  . GLU A  1 185 ? -4.360  -52.217 34.102  1.00 54.73  ? 185  GLU A CB  1 
ATOM   1436  C  CG  . GLU A  1 185 ? -5.060  -51.897 35.400  1.00 67.74  ? 185  GLU A CG  1 
ATOM   1437  C  CD  . GLU A  1 185 ? -6.521  -52.336 35.387  1.00 80.72  ? 185  GLU A CD  1 
ATOM   1438  O  OE1 . GLU A  1 185 ? -6.841  -53.322 34.676  1.00 83.60  ? 185  GLU A OE1 1 
ATOM   1439  O  OE2 . GLU A  1 185 ? -7.348  -51.691 36.078  1.00 85.51  ? 185  GLU A OE2 1 
ATOM   1440  N  N   . ASN A  1 186 ? -2.449  -52.085 31.731  1.00 24.36  ? 186  ASN A N   1 
ATOM   1441  C  CA  . ASN A  1 186 ? -1.983  -52.710 30.492  1.00 21.48  ? 186  ASN A CA  1 
ATOM   1442  C  C   . ASN A  1 186 ? -0.749  -52.205 29.737  1.00 21.69  ? 186  ASN A C   1 
ATOM   1443  O  O   . ASN A  1 186 ? -0.443  -52.765 28.696  1.00 23.53  ? 186  ASN A O   1 
ATOM   1444  C  CB  . ASN A  1 186 ? -3.134  -52.779 29.494  1.00 20.72  ? 186  ASN A CB  1 
ATOM   1445  C  CG  . ASN A  1 186 ? -4.430  -53.104 30.148  1.00 25.21  ? 186  ASN A CG  1 
ATOM   1446  O  OD1 . ASN A  1 186 ? -4.821  -54.256 30.189  1.00 31.44  ? 186  ASN A OD1 1 
ATOM   1447  N  ND2 . ASN A  1 186 ? -5.105  -52.094 30.684  1.00 20.07  ? 186  ASN A ND2 1 
ATOM   1448  N  N   . ILE A  1 187 ? -0.073  -51.140 30.151  1.00 19.33  ? 187  ILE A N   1 
ATOM   1449  C  CA  . ILE A  1 187 ? 0.875   -50.565 29.182  1.00 23.96  ? 187  ILE A CA  1 
ATOM   1450  C  C   . ILE A  1 187 ? 2.119   -51.431 28.988  1.00 25.50  ? 187  ILE A C   1 
ATOM   1451  O  O   . ILE A  1 187 ? 2.744   -51.401 27.929  1.00 25.62  ? 187  ILE A O   1 
ATOM   1452  C  CB  . ILE A  1 187 ? 1.285   -49.096 29.465  1.00 18.47  ? 187  ILE A CB  1 
ATOM   1453  C  CG1 . ILE A  1 187 ? 1.577   -48.361 28.154  1.00 18.31  ? 187  ILE A CG1 1 
ATOM   1454  C  CG2 . ILE A  1 187 ? 2.523   -49.036 30.342  1.00 18.57  ? 187  ILE A CG2 1 
ATOM   1455  C  CD1 . ILE A  1 187 ? 0.457   -48.405 27.151  1.00 18.36  ? 187  ILE A CD1 1 
ATOM   1456  N  N   . ALA A  1 188 ? 2.464   -52.223 29.996  1.00 24.77  ? 188  ALA A N   1 
ATOM   1457  C  CA  . ALA A  1 188 ? 3.657   -53.035 29.898  1.00 28.01  ? 188  ALA A CA  1 
ATOM   1458  C  C   . ALA A  1 188 ? 3.461   -54.084 28.824  1.00 29.45  ? 188  ALA A C   1 
ATOM   1459  O  O   . ALA A  1 188 ? 4.415   -54.519 28.193  1.00 31.55  ? 188  ALA A O   1 
ATOM   1460  C  CB  . ALA A  1 188 ? 3.985   -53.668 31.227  1.00 43.33  ? 188  ALA A CB  1 
ATOM   1461  N  N   . ALA A  1 189 ? 2.219   -54.479 28.600  1.00 21.67  ? 189  ALA A N   1 
ATOM   1462  C  CA  . ALA A  1 189 ? 1.927   -55.416 27.528  1.00 22.38  ? 189  ALA A CA  1 
ATOM   1463  C  C   . ALA A  1 189 ? 2.423   -54.884 26.197  1.00 22.32  ? 189  ALA A C   1 
ATOM   1464  O  O   . ALA A  1 189 ? 2.814   -55.662 25.336  1.00 23.45  ? 189  ALA A O   1 
ATOM   1465  C  CB  . ALA A  1 189 ? 0.440   -55.705 27.451  1.00 34.72  ? 189  ALA A CB  1 
ATOM   1466  N  N   . PHE A  1 190 ? 2.424   -53.562 26.036  1.00 26.11  ? 190  PHE A N   1 
ATOM   1467  C  CA  . PHE A  1 190 ? 2.884   -52.938 24.797  1.00 26.29  ? 190  PHE A CA  1 
ATOM   1468  C  C   . PHE A  1 190 ? 4.367   -52.563 24.822  1.00 26.97  ? 190  PHE A C   1 
ATOM   1469  O  O   . PHE A  1 190 ? 4.868   -52.003 23.856  1.00 26.22  ? 190  PHE A O   1 
ATOM   1470  C  CB  . PHE A  1 190 ? 2.074   -51.680 24.493  1.00 20.76  ? 190  PHE A CB  1 
ATOM   1471  C  CG  . PHE A  1 190 ? 0.610   -51.924 24.317  1.00 22.21  ? 190  PHE A CG  1 
ATOM   1472  C  CD1 . PHE A  1 190 ? -0.239  -51.945 25.407  1.00 20.46  ? 190  PHE A CD1 1 
ATOM   1473  C  CD2 . PHE A  1 190 ? 0.074   -52.122 23.055  1.00 25.15  ? 190  PHE A CD2 1 
ATOM   1474  C  CE1 . PHE A  1 190 ? -1.593  -52.177 25.239  1.00 20.61  ? 190  PHE A CE1 1 
ATOM   1475  C  CE2 . PHE A  1 190 ? -1.283  -52.347 22.880  1.00 21.40  ? 190  PHE A CE2 1 
ATOM   1476  C  CZ  . PHE A  1 190 ? -2.112  -52.377 23.970  1.00 21.65  ? 190  PHE A CZ  1 
ATOM   1477  N  N   . GLY A  1 191 ? 5.066   -52.848 25.918  1.00 21.69  ? 191  GLY A N   1 
ATOM   1478  C  CA  . GLY A  1 191 ? 6.461   -52.451 26.051  1.00 21.85  ? 191  GLY A CA  1 
ATOM   1479  C  C   . GLY A  1 191 ? 6.666   -51.187 26.875  1.00 21.08  ? 191  GLY A C   1 
ATOM   1480  O  O   . GLY A  1 191 ? 7.775   -50.651 26.967  1.00 21.20  ? 191  GLY A O   1 
ATOM   1481  N  N   . GLY A  1 192 ? 5.583   -50.709 27.477  1.00 33.04  ? 192  GLY A N   1 
ATOM   1482  C  CA  . GLY A  1 192 ? 5.622   -49.512 28.294  1.00 32.61  ? 192  GLY A CA  1 
ATOM   1483  C  C   . GLY A  1 192 ? 6.188   -49.799 29.667  1.00 30.10  ? 192  GLY A C   1 
ATOM   1484  O  O   . GLY A  1 192 ? 6.513   -50.944 29.974  1.00 30.07  ? 192  GLY A O   1 
ATOM   1485  N  N   . ASP A  1 193 ? 6.318   -48.755 30.481  1.00 19.42  ? 193  ASP A N   1 
ATOM   1486  C  CA  . ASP A  1 193 ? 6.850   -48.869 31.838  1.00 19.65  ? 193  ASP A CA  1 
ATOM   1487  C  C   . ASP A  1 193 ? 5.936   -48.179 32.841  1.00 19.06  ? 193  ASP A C   1 
ATOM   1488  O  O   . ASP A  1 193 ? 6.048   -46.977 33.028  1.00 18.60  ? 193  ASP A O   1 
ATOM   1489  C  CB  . ASP A  1 193 ? 8.254   -48.252 31.912  1.00 30.95  ? 193  ASP A CB  1 
ATOM   1490  C  CG  . ASP A  1 193 ? 8.901   -48.415 33.287  1.00 32.96  ? 193  ASP A CG  1 
ATOM   1491  O  OD1 . ASP A  1 193 ? 8.407   -49.252 34.078  1.00 37.07  ? 193  ASP A OD1 1 
ATOM   1492  O  OD2 . ASP A  1 193 ? 9.906   -47.719 33.571  1.00 29.23  ? 193  ASP A OD2 1 
ATOM   1493  N  N   . PRO A  1 194 ? 5.018   -48.918 33.480  1.00 21.68  ? 194  PRO A N   1 
ATOM   1494  C  CA  . PRO A  1 194 ? 4.107   -48.226 34.395  1.00 21.08  ? 194  PRO A CA  1 
ATOM   1495  C  C   . PRO A  1 194 ? 4.852   -47.436 35.460  1.00 25.05  ? 194  PRO A C   1 
ATOM   1496  O  O   . PRO A  1 194 ? 4.298   -46.479 35.995  1.00 27.03  ? 194  PRO A O   1 
ATOM   1497  C  CB  . PRO A  1 194 ? 3.303   -49.367 35.026  1.00 22.90  ? 194  PRO A CB  1 
ATOM   1498  C  CG  . PRO A  1 194 ? 3.319   -50.425 34.005  1.00 25.10  ? 194  PRO A CG  1 
ATOM   1499  C  CD  . PRO A  1 194 ? 4.700   -50.348 33.386  1.00 27.00  ? 194  PRO A CD  1 
ATOM   1500  N  N   . MET A  1 195 ? 6.095   -47.802 35.740  1.00 19.29  ? 195  MET A N   1 
ATOM   1501  C  CA  . MET A  1 195 ? 6.863   -47.070 36.722  1.00 19.44  ? 195  MET A CA  1 
ATOM   1502  C  C   . MET A  1 195 ? 7.259   -45.659 36.244  1.00 23.91  ? 195  MET A C   1 
ATOM   1503  O  O   . MET A  1 195 ? 7.655   -44.804 37.042  1.00 18.97  ? 195  MET A O   1 
ATOM   1504  C  CB  . MET A  1 195 ? 8.081   -47.881 37.147  1.00 21.19  ? 195  MET A CB  1 
ATOM   1505  C  CG  . MET A  1 195 ? 7.734   -49.159 37.898  1.00 22.40  ? 195  MET A CG  1 
ATOM   1506  S  SD  . MET A  1 195 ? 9.145   -50.259 38.183  1.00 55.12  ? 195  MET A SD  1 
ATOM   1507  C  CE  . MET A  1 195 ? 10.401  -49.099 38.743  1.00 22.49  ? 195  MET A CE  1 
ATOM   1508  N  N   . SER A  1 196 ? 7.176   -45.390 34.950  1.00 18.60  ? 196  SER A N   1 
ATOM   1509  C  CA  . SER A  1 196 ? 7.436   -44.023 34.508  1.00 18.19  ? 196  SER A CA  1 
ATOM   1510  C  C   . SER A  1 196 ? 6.356   -43.504 33.552  1.00 17.53  ? 196  SER A C   1 
ATOM   1511  O  O   . SER A  1 196 ? 6.255   -43.914 32.406  1.00 17.55  ? 196  SER A O   1 
ATOM   1512  C  CB  . SER A  1 196 ? 8.839   -43.926 33.898  1.00 18.71  ? 196  SER A CB  1 
ATOM   1513  O  OG  . SER A  1 196 ? 9.181   -42.601 33.547  1.00 18.46  ? 196  SER A OG  1 
ATOM   1514  N  N   . VAL A  1 197 ? 5.565   -42.560 34.023  1.00 20.06  ? 197  VAL A N   1 
ATOM   1515  C  CA  . VAL A  1 197 ? 4.472   -42.048 33.219  1.00 21.12  ? 197  VAL A CA  1 
ATOM   1516  C  C   . VAL A  1 197 ? 4.488   -40.534 33.274  1.00 21.59  ? 197  VAL A C   1 
ATOM   1517  O  O   . VAL A  1 197 ? 4.410   -39.943 34.345  1.00 19.90  ? 197  VAL A O   1 
ATOM   1518  C  CB  . VAL A  1 197 ? 3.086   -42.560 33.692  1.00 16.31  ? 197  VAL A CB  1 
ATOM   1519  C  CG1 . VAL A  1 197 ? 2.023   -41.983 32.834  1.00 15.90  ? 197  VAL A CG1 1 
ATOM   1520  C  CG2 . VAL A  1 197 ? 3.009   -44.058 33.617  1.00 16.73  ? 197  VAL A CG2 1 
ATOM   1521  N  N   . THR A  1 198 ? 4.609   -39.909 32.114  1.00 27.54  ? 198  THR A N   1 
ATOM   1522  C  CA  . THR A  1 198 ? 4.531   -38.475 32.032  1.00 31.41  ? 198  THR A CA  1 
ATOM   1523  C  C   . THR A  1 198 ? 3.231   -38.096 31.343  1.00 35.86  ? 198  THR A C   1 
ATOM   1524  O  O   . THR A  1 198 ? 2.986   -38.517 30.205  1.00 41.59  ? 198  THR A O   1 
ATOM   1525  C  CB  . THR A  1 198 ? 5.706   -37.933 31.261  1.00 16.11  ? 198  THR A CB  1 
ATOM   1526  O  OG1 . THR A  1 198 ? 6.892   -38.205 32.006  1.00 30.22  ? 198  THR A OG1 1 
ATOM   1527  C  CG2 . THR A  1 198 ? 5.566   -36.445 31.074  1.00 15.94  ? 198  THR A CG2 1 
ATOM   1528  N  N   . LEU A  1 199 ? 2.386   -37.334 32.046  1.00 21.38  ? 199  LEU A N   1 
ATOM   1529  C  CA  . LEU A  1 199 ? 1.197   -36.751 31.427  1.00 17.16  ? 199  LEU A CA  1 
ATOM   1530  C  C   . LEU A  1 199 ? 1.619   -35.465 30.713  1.00 19.08  ? 199  LEU A C   1 
ATOM   1531  O  O   . LEU A  1 199 ? 2.326   -34.646 31.296  1.00 21.84  ? 199  LEU A O   1 
ATOM   1532  C  CB  . LEU A  1 199 ? 0.142   -36.412 32.486  1.00 22.09  ? 199  LEU A CB  1 
ATOM   1533  C  CG  . LEU A  1 199 ? -0.585  -37.474 33.309  1.00 24.51  ? 199  LEU A CG  1 
ATOM   1534  C  CD1 . LEU A  1 199 ? -1.648  -36.821 34.158  1.00 14.63  ? 199  LEU A CD1 1 
ATOM   1535  C  CD2 . LEU A  1 199 ? -1.204  -38.537 32.428  1.00 14.81  ? 199  LEU A CD2 1 
ATOM   1536  N  N   . PHE A  1 200 ? 1.222   -35.276 29.457  1.00 18.11  ? 200  PHE A N   1 
ATOM   1537  C  CA  . PHE A  1 200 ? 1.447   -33.969 28.824  1.00 17.63  ? 200  PHE A CA  1 
ATOM   1538  C  C   . PHE A  1 200 ? 0.287   -33.514 27.969  1.00 19.47  ? 200  PHE A C   1 
ATOM   1539  O  O   . PHE A  1 200 ? -0.292  -34.309 27.225  1.00 15.12  ? 200  PHE A O   1 
ATOM   1540  C  CB  . PHE A  1 200 ? 2.788   -33.859 28.079  1.00 15.43  ? 200  PHE A CB  1 
ATOM   1541  C  CG  . PHE A  1 200 ? 2.840   -34.548 26.727  1.00 15.72  ? 200  PHE A CG  1 
ATOM   1542  C  CD1 . PHE A  1 200 ? 2.451   -35.871 26.569  1.00 15.70  ? 200  PHE A CD1 1 
ATOM   1543  C  CD2 . PHE A  1 200 ? 3.352   -33.875 25.622  1.00 16.13  ? 200  PHE A CD2 1 
ATOM   1544  C  CE1 . PHE A  1 200 ? 2.545   -36.500 25.324  1.00 16.07  ? 200  PHE A CE1 1 
ATOM   1545  C  CE2 . PHE A  1 200 ? 3.447   -34.496 24.383  1.00 16.51  ? 200  PHE A CE2 1 
ATOM   1546  C  CZ  . PHE A  1 200 ? 3.034   -35.810 24.232  1.00 16.48  ? 200  PHE A CZ  1 
ATOM   1547  N  N   . GLY A  1 201 ? -0.049  -32.229 28.107  1.00 29.64  ? 201  GLY A N   1 
ATOM   1548  C  CA  . GLY A  1 201 ? -1.248  -31.674 27.490  1.00 26.67  ? 201  GLY A CA  1 
ATOM   1549  C  C   . GLY A  1 201 ? -1.118  -30.208 27.130  1.00 28.19  ? 201  GLY A C   1 
ATOM   1550  O  O   . GLY A  1 201 ? -0.187  -29.519 27.565  1.00 32.37  ? 201  GLY A O   1 
ATOM   1551  N  N   . GLU A  1 202 ? -2.051  -29.718 26.327  1.00 25.18  ? 202  GLU A N   1 
ATOM   1552  C  CA  . GLU A  1 202 ? -1.989  -28.336 25.872  1.00 28.91  ? 202  GLU A CA  1 
ATOM   1553  C  C   . GLU A  1 202 ? -3.347  -27.637 25.987  1.00 30.48  ? 202  GLU A C   1 
ATOM   1554  O  O   . GLU A  1 202 ? -4.381  -28.238 25.702  1.00 33.61  ? 202  GLU A O   1 
ATOM   1555  C  CB  . GLU A  1 202 ? -1.477  -28.291 24.436  1.00 32.63  ? 202  GLU A CB  1 
ATOM   1556  C  CG  . GLU A  1 202 ? -1.028  -26.926 23.971  1.00 38.14  ? 202  GLU A CG  1 
ATOM   1557  C  CD  . GLU A  1 202 ? -2.146  -26.133 23.303  1.00 45.21  ? 202  GLU A CD  1 
ATOM   1558  O  OE1 . GLU A  1 202 ? -3.303  -26.613 23.242  1.00 46.26  ? 202  GLU A OE1 1 
ATOM   1559  O  OE2 . GLU A  1 202 ? -1.863  -25.016 22.830  1.00 48.26  ? 202  GLU A OE2 1 
ATOM   1560  N  N   . SER A  1 203 ? -3.335  -26.369 26.395  1.00 24.66  ? 203  SER A N   1 
ATOM   1561  C  CA  . SER A  1 203 ? -4.561  -25.589 26.612  1.00 25.72  ? 203  SER A CA  1 
ATOM   1562  C  C   . SER A  1 203 ? -5.484  -26.192 27.700  1.00 24.33  ? 203  SER A C   1 
ATOM   1563  O  O   . SER A  1 203 ? -5.083  -26.360 28.855  1.00 20.66  ? 203  SER A O   1 
ATOM   1564  C  CB  . SER A  1 203 ? -5.316  -25.365 25.284  1.00 29.28  ? 203  SER A CB  1 
ATOM   1565  O  OG  . SER A  1 203 ? -6.208  -24.260 25.354  1.00 30.82  ? 203  SER A OG  1 
ATOM   1566  N  N   . ALA A  1 204 ? -6.731  -26.474 27.330  1.00 35.51  ? 204  ALA A N   1 
ATOM   1567  C  CA  . ALA A  1 204 ? -7.655  -27.146 28.220  1.00 33.93  ? 204  ALA A CA  1 
ATOM   1568  C  C   . ALA A  1 204 ? -7.011  -28.449 28.667  1.00 31.37  ? 204  ALA A C   1 
ATOM   1569  O  O   . ALA A  1 204 ? -7.135  -28.848 29.821  1.00 30.22  ? 204  ALA A O   1 
ATOM   1570  C  CB  . ALA A  1 204 ? -8.950  -27.412 27.515  1.00 16.46  ? 204  ALA A CB  1 
ATOM   1571  N  N   . GLY A  1 205 ? -6.303  -29.096 27.747  1.00 22.15  ? 205  GLY A N   1 
ATOM   1572  C  CA  . GLY A  1 205 ? -5.617  -30.336 28.045  1.00 21.22  ? 205  GLY A CA  1 
ATOM   1573  C  C   . GLY A  1 205 ? -4.546  -30.180 29.107  1.00 23.53  ? 205  GLY A C   1 
ATOM   1574  O  O   . GLY A  1 205 ? -4.442  -31.003 30.020  1.00 27.08  ? 205  GLY A O   1 
ATOM   1575  N  N   . ALA A  1 206 ? -3.740  -29.131 28.989  1.00 22.04  ? 206  ALA A N   1 
ATOM   1576  C  CA  . ALA A  1 206 ? -2.748  -28.837 30.013  1.00 22.05  ? 206  ALA A CA  1 
ATOM   1577  C  C   . ALA A  1 206 ? -3.440  -28.598 31.356  1.00 22.31  ? 206  ALA A C   1 
ATOM   1578  O  O   . ALA A  1 206 ? -2.950  -29.035 32.409  1.00 20.23  ? 206  ALA A O   1 
ATOM   1579  C  CB  . ALA A  1 206 ? -1.904  -27.635 29.619  1.00 19.83  ? 206  ALA A CB  1 
ATOM   1580  N  N   . ALA A  1 207 ? -4.592  -27.925 31.309  1.00 22.93  ? 207  ALA A N   1 
ATOM   1581  C  CA  . ALA A  1 207 ? -5.376  -27.679 32.511  1.00 22.32  ? 207  ALA A CA  1 
ATOM   1582  C  C   . ALA A  1 207 ? -5.820  -29.005 33.105  1.00 22.39  ? 207  ALA A C   1 
ATOM   1583  O  O   . ALA A  1 207 ? -5.850  -29.176 34.331  1.00 16.67  ? 207  ALA A O   1 
ATOM   1584  C  CB  . ALA A  1 207 ? -6.556  -26.831 32.198  1.00 15.39  ? 207  ALA A CB  1 
ATOM   1585  N  N   . SER A  1 208 ? -6.141  -29.951 32.232  1.00 14.84  ? 208  SER A N   1 
ATOM   1586  C  CA  . SER A  1 208 ? -6.547  -31.264 32.680  1.00 31.23  ? 208  SER A CA  1 
ATOM   1587  C  C   . SER A  1 208 ? -5.403  -31.886 33.432  1.00 14.58  ? 208  SER A C   1 
ATOM   1588  O  O   . SER A  1 208 ? -5.585  -32.383 34.542  1.00 16.63  ? 208  SER A O   1 
ATOM   1589  C  CB  . SER A  1 208 ? -6.976  -32.131 31.509  1.00 14.85  ? 208  SER A CB  1 
ATOM   1590  O  OG  . SER A  1 208 ? -8.181  -31.625 30.955  1.00 15.16  ? 208  SER A OG  1 
ATOM   1591  N  N   . VAL A  1 209 ? -4.215  -31.816 32.838  1.00 14.48  ? 209  VAL A N   1 
ATOM   1592  C  CA  . VAL A  1 209 ? -3.013  -32.366 33.460  1.00 17.67  ? 209  VAL A CA  1 
ATOM   1593  C  C   . VAL A  1 209 ? -2.873  -31.809 34.861  1.00 14.51  ? 209  VAL A C   1 
ATOM   1594  O  O   . VAL A  1 209 ? -2.746  -32.553 35.839  1.00 14.58  ? 209  VAL A O   1 
ATOM   1595  C  CB  . VAL A  1 209 ? -1.757  -32.049 32.632  1.00 17.50  ? 209  VAL A CB  1 
ATOM   1596  C  CG1 . VAL A  1 209 ? -0.489  -32.390 33.404  1.00 14.54  ? 209  VAL A CG1 1 
ATOM   1597  C  CG2 . VAL A  1 209 ? -1.813  -32.796 31.310  1.00 17.54  ? 209  VAL A CG2 1 
ATOM   1598  N  N   . GLY A  1 210 ? -2.945  -30.491 34.960  1.00 17.50  ? 210  GLY A N   1 
ATOM   1599  C  CA  . GLY A  1 210 ? -2.842  -29.852 36.253  1.00 18.30  ? 210  GLY A CA  1 
ATOM   1600  C  C   . GLY A  1 210 ? -3.865  -30.388 37.232  1.00 17.38  ? 210  GLY A C   1 
ATOM   1601  O  O   . GLY A  1 210 ? -3.538  -30.701 38.383  1.00 16.93  ? 210  GLY A O   1 
ATOM   1602  N  N   . MET A  1 211 ? -5.106  -30.515 36.771  1.00 14.89  ? 211  MET A N   1 
ATOM   1603  C  CA  . MET A  1 211 ? -6.167  -31.051 37.612  1.00 15.10  ? 211  MET A CA  1 
ATOM   1604  C  C   . MET A  1 211 ? -5.861  -32.452 38.161  1.00 15.12  ? 211  MET A C   1 
ATOM   1605  O  O   . MET A  1 211 ? -6.167  -32.752 39.314  1.00 15.42  ? 211  MET A O   1 
ATOM   1606  C  CB  . MET A  1 211 ? -7.490  -31.018 36.869  1.00 15.20  ? 211  MET A CB  1 
ATOM   1607  C  CG  . MET A  1 211 ? -8.435  -30.033 37.481  1.00 15.76  ? 211  MET A CG  1 
ATOM   1608  S  SD  . MET A  1 211 ? -9.363  -29.174 36.234  1.00 23.46  ? 211  MET A SD  1 
ATOM   1609  C  CE  . MET A  1 211 ? -8.813  -27.497 36.493  1.00 15.82  ? 211  MET A CE  1 
ATOM   1610  N  N   . HIS A  1 212 ? -5.237  -33.298 37.343  1.00 17.99  ? 212  HIS A N   1 
ATOM   1611  C  CA  . HIS A  1 212 ? -4.774  -34.601 37.822  1.00 17.72  ? 212  HIS A CA  1 
ATOM   1612  C  C   . HIS A  1 212 ? -3.649  -34.481 38.827  1.00 15.14  ? 212  HIS A C   1 
ATOM   1613  O  O   . HIS A  1 212 ? -3.515  -35.331 39.691  1.00 19.60  ? 212  HIS A O   1 
ATOM   1614  C  CB  . HIS A  1 212 ? -4.296  -35.466 36.676  1.00 14.81  ? 212  HIS A CB  1 
ATOM   1615  C  CG  . HIS A  1 212 ? -5.395  -35.947 35.803  1.00 14.82  ? 212  HIS A CG  1 
ATOM   1616  N  ND1 . HIS A  1 212 ? -6.340  -36.851 36.234  1.00 15.10  ? 212  HIS A ND1 1 
ATOM   1617  C  CD2 . HIS A  1 212 ? -5.709  -35.654 34.519  1.00 14.72  ? 212  HIS A CD2 1 
ATOM   1618  C  CE1 . HIS A  1 212 ? -7.187  -37.097 35.252  1.00 17.32  ? 212  HIS A CE1 1 
ATOM   1619  N  NE2 . HIS A  1 212 ? -6.828  -36.382 34.199  1.00 15.41  ? 212  HIS A NE2 1 
ATOM   1620  N  N   . ILE A  1 213 ? -2.815  -33.454 38.692  1.00 16.37  ? 213  ILE A N   1 
ATOM   1621  C  CA  . ILE A  1 213 ? -1.794  -33.217 39.704  1.00 15.64  ? 213  ILE A CA  1 
ATOM   1622  C  C   . ILE A  1 213 ? -2.479  -32.926 41.023  1.00 15.72  ? 213  ILE A C   1 
ATOM   1623  O  O   . ILE A  1 213 ? -2.080  -33.430 42.068  1.00 16.16  ? 213  ILE A O   1 
ATOM   1624  C  CB  . ILE A  1 213 ? -0.879  -32.020 39.351  1.00 15.67  ? 213  ILE A CB  1 
ATOM   1625  C  CG1 . ILE A  1 213 ? 0.000   -32.347 38.140  1.00 15.15  ? 213  ILE A CG1 1 
ATOM   1626  C  CG2 . ILE A  1 213 ? -0.026  -31.603 40.563  1.00 15.81  ? 213  ILE A CG2 1 
ATOM   1627  C  CD1 . ILE A  1 213 ? 0.532   -31.125 37.450  1.00 15.15  ? 213  ILE A CD1 1 
ATOM   1628  N  N   . LEU A  1 214 ? -3.531  -32.121 40.965  1.00 20.11  ? 214  LEU A N   1 
ATOM   1629  C  CA  . LEU A  1 214 ? -4.186  -31.639 42.175  1.00 23.35  ? 214  LEU A CA  1 
ATOM   1630  C  C   . LEU A  1 214 ? -5.187  -32.604 42.817  1.00 29.15  ? 214  LEU A C   1 
ATOM   1631  O  O   . LEU A  1 214 ? -5.627  -32.358 43.940  1.00 33.57  ? 214  LEU A O   1 
ATOM   1632  C  CB  . LEU A  1 214 ? -4.868  -30.304 41.890  1.00 16.14  ? 214  LEU A CB  1 
ATOM   1633  C  CG  . LEU A  1 214 ? -3.856  -29.228 41.539  1.00 16.08  ? 214  LEU A CG  1 
ATOM   1634  C  CD1 . LEU A  1 214 ? -4.531  -27.947 41.086  1.00 16.13  ? 214  LEU A CD1 1 
ATOM   1635  C  CD2 . LEU A  1 214 ? -2.992  -29.007 42.757  1.00 16.54  ? 214  LEU A CD2 1 
ATOM   1636  N  N   . SER A  1 215 ? -5.553  -33.678 42.113  1.00 25.36  ? 215  SER A N   1 
ATOM   1637  C  CA  . SER A  1 215 ? -6.514  -34.666 42.629  1.00 25.88  ? 215  SER A CA  1 
ATOM   1638  C  C   . SER A  1 215 ? -5.815  -35.960 43.039  1.00 28.28  ? 215  SER A C   1 
ATOM   1639  O  O   . SER A  1 215 ? -5.206  -36.635 42.218  1.00 32.24  ? 215  SER A O   1 
ATOM   1640  C  CB  . SER A  1 215 ? -7.598  -34.971 41.587  1.00 24.44  ? 215  SER A CB  1 
ATOM   1641  O  OG  . SER A  1 215 ? -8.617  -35.813 42.102  1.00 24.37  ? 215  SER A OG  1 
ATOM   1642  N  N   . LEU A  1 216 ? -5.929  -36.305 44.312  1.00 17.59  ? 216  LEU A N   1 
ATOM   1643  C  CA  . LEU A  1 216 ? -5.195  -37.415 44.908  1.00 17.75  ? 216  LEU A CA  1 
ATOM   1644  C  C   . LEU A  1 216 ? -5.302  -38.789 44.204  1.00 17.99  ? 216  LEU A C   1 
ATOM   1645  O  O   . LEU A  1 216 ? -4.304  -39.510 44.098  1.00 17.71  ? 216  LEU A O   1 
ATOM   1646  C  CB  . LEU A  1 216 ? -5.593  -37.515 46.378  1.00 41.66  ? 216  LEU A CB  1 
ATOM   1647  C  CG  . LEU A  1 216 ? -4.606  -38.004 47.423  1.00 19.17  ? 216  LEU A CG  1 
ATOM   1648  C  CD1 . LEU A  1 216 ? -4.942  -39.432 47.735  1.00 19.68  ? 216  LEU A CD1 1 
ATOM   1649  C  CD2 . LEU A  1 216 ? -3.170  -37.851 46.953  1.00 18.82  ? 216  LEU A CD2 1 
ATOM   1650  N  N   . PRO A  1 217 ? -6.505  -39.170 43.732  1.00 26.31  ? 217  PRO A N   1 
ATOM   1651  C  CA  . PRO A  1 217 ? -6.593  -40.455 43.022  1.00 26.49  ? 217  PRO A CA  1 
ATOM   1652  C  C   . PRO A  1 217 ? -5.827  -40.488 41.713  1.00 30.63  ? 217  PRO A C   1 
ATOM   1653  O  O   . PRO A  1 217 ? -5.423  -41.557 41.267  1.00 34.60  ? 217  PRO A O   1 
ATOM   1654  C  CB  . PRO A  1 217 ? -8.086  -40.588 42.736  1.00 17.91  ? 217  PRO A CB  1 
ATOM   1655  C  CG  . PRO A  1 217 ? -8.728  -39.834 43.821  1.00 18.33  ? 217  PRO A CG  1 
ATOM   1656  C  CD  . PRO A  1 217 ? -7.845  -38.648 44.048  1.00 17.97  ? 217  PRO A CD  1 
ATOM   1657  N  N   . SER A  1 218 ? -5.645  -39.333 41.092  1.00 28.17  ? 218  SER A N   1 
ATOM   1658  C  CA  . SER A  1 218 ? -4.874  -39.265 39.863  1.00 26.95  ? 218  SER A CA  1 
ATOM   1659  C  C   . SER A  1 218 ? -3.355  -39.300 40.111  1.00 26.43  ? 218  SER A C   1 
ATOM   1660  O  O   . SER A  1 218 ? -2.604  -39.783 39.264  1.00 26.73  ? 218  SER A O   1 
ATOM   1661  C  CB  . SER A  1 218 ? -5.280  -38.035 39.046  1.00 21.40  ? 218  SER A CB  1 
ATOM   1662  O  OG  . SER A  1 218 ? -6.599  -38.175 38.549  1.00 15.77  ? 218  SER A OG  1 
ATOM   1663  N  N   . ARG A  1 219 ? -2.914  -38.808 41.269  1.00 23.48  ? 219  ARG A N   1 
ATOM   1664  C  CA  . ARG A  1 219 ? -1.486  -38.741 41.583  1.00 29.45  ? 219  ARG A CA  1 
ATOM   1665  C  C   . ARG A  1 219 ? -0.758  -40.097 41.573  1.00 37.03  ? 219  ARG A C   1 
ATOM   1666  O  O   . ARG A  1 219 ? 0.452   -40.153 41.304  1.00 38.10  ? 219  ARG A O   1 
ATOM   1667  C  CB  . ARG A  1 219 ? -1.247  -38.080 42.946  1.00 34.04  ? 219  ARG A CB  1 
ATOM   1668  C  CG  . ARG A  1 219 ? -1.164  -36.563 42.976  1.00 37.20  ? 219  ARG A CG  1 
ATOM   1669  C  CD  . ARG A  1 219 ? -0.221  -35.992 41.943  1.00 41.21  ? 219  ARG A CD  1 
ATOM   1670  N  NE  . ARG A  1 219 ? 0.951   -36.819 41.678  1.00 47.36  ? 219  ARG A NE  1 
ATOM   1671  C  CZ  . ARG A  1 219 ? 2.165   -36.583 42.168  1.00 54.64  ? 219  ARG A CZ  1 
ATOM   1672  N  NH1 . ARG A  1 219 ? 2.365   -35.546 42.976  1.00 56.06  ? 219  ARG A NH1 1 
ATOM   1673  N  NH2 . ARG A  1 219 ? 3.180   -37.388 41.847  1.00 57.06  ? 219  ARG A NH2 1 
ATOM   1674  N  N   . SER A  1 220 ? -1.484  -41.176 41.882  1.00 45.65  ? 220  SER A N   1 
ATOM   1675  C  CA  . SER A  1 220 ? -0.886  -42.512 41.981  1.00 41.43  ? 220  SER A CA  1 
ATOM   1676  C  C   . SER A  1 220 ? -0.627  -43.127 40.614  1.00 39.02  ? 220  SER A C   1 
ATOM   1677  O  O   . SER A  1 220 ? 0.022   -44.165 40.516  1.00 40.52  ? 220  SER A O   1 
ATOM   1678  C  CB  . SER A  1 220 ? -1.795  -43.451 42.781  1.00 29.63  ? 220  SER A CB  1 
ATOM   1679  O  OG  . SER A  1 220 ? -2.525  -42.733 43.761  1.00 29.79  ? 220  SER A OG  1 
ATOM   1680  N  N   . LEU A  1 221 ? -1.173  -42.507 39.569  1.00 29.90  ? 221  LEU A N   1 
ATOM   1681  C  CA  . LEU A  1 221 ? -1.066  -43.034 38.210  1.00 26.07  ? 221  LEU A CA  1 
ATOM   1682  C  C   . LEU A  1 221 ? 0.069   -42.508 37.313  1.00 28.01  ? 221  LEU A C   1 
ATOM   1683  O  O   . LEU A  1 221 ? 0.366   -43.102 36.278  1.00 30.71  ? 221  LEU A O   1 
ATOM   1684  C  CB  . LEU A  1 221 ? -2.393  -42.823 37.498  1.00 16.31  ? 221  LEU A CB  1 
ATOM   1685  C  CG  . LEU A  1 221 ? -3.514  -43.437 38.316  1.00 16.72  ? 221  LEU A CG  1 
ATOM   1686  C  CD1 . LEU A  1 221 ? -4.847  -43.366 37.587  1.00 19.45  ? 221  LEU A CD1 1 
ATOM   1687  C  CD2 . LEU A  1 221 ? -3.144  -44.860 38.598  1.00 17.28  ? 221  LEU A CD2 1 
ATOM   1688  N  N   . PHE A  1 222 ? 0.726   -41.426 37.702  1.00 16.17  ? 222  PHE A N   1 
ATOM   1689  C  CA  . PHE A  1 222 ? 1.744   -40.848 36.843  1.00 16.02  ? 222  PHE A CA  1 
ATOM   1690  C  C   . PHE A  1 222 ? 2.807   -40.187 37.691  1.00 23.35  ? 222  PHE A C   1 
ATOM   1691  O  O   . PHE A  1 222 ? 2.571   -39.817 38.850  1.00 25.16  ? 222  PHE A O   1 
ATOM   1692  C  CB  . PHE A  1 222 ? 1.140   -39.820 35.893  1.00 15.53  ? 222  PHE A CB  1 
ATOM   1693  C  CG  . PHE A  1 222 ? 0.653   -38.571 36.577  1.00 21.14  ? 222  PHE A CG  1 
ATOM   1694  C  CD1 . PHE A  1 222 ? -0.591  -38.537 37.184  1.00 21.15  ? 222  PHE A CD1 1 
ATOM   1695  C  CD2 . PHE A  1 222 ? 1.432   -37.428 36.604  1.00 15.31  ? 222  PHE A CD2 1 
ATOM   1696  C  CE1 . PHE A  1 222 ? -1.037  -37.391 37.812  1.00 15.23  ? 222  PHE A CE1 1 
ATOM   1697  C  CE2 . PHE A  1 222 ? 0.991   -36.283 37.232  1.00 15.23  ? 222  PHE A CE2 1 
ATOM   1698  C  CZ  . PHE A  1 222 ? -0.239  -36.264 37.835  1.00 20.82  ? 222  PHE A CZ  1 
ATOM   1699  N  N   . HIS A  1 223 ? 4.003   -40.086 37.137  1.00 16.42  ? 223  HIS A N   1 
ATOM   1700  C  CA  . HIS A  1 223 ? 5.096   -39.519 37.882  1.00 16.80  ? 223  HIS A CA  1 
ATOM   1701  C  C   . HIS A  1 223 ? 5.551   -38.102 37.519  1.00 22.76  ? 223  HIS A C   1 
ATOM   1702  O  O   . HIS A  1 223 ? 6.331   -37.511 38.246  1.00 23.95  ? 223  HIS A O   1 
ATOM   1703  C  CB  . HIS A  1 223 ? 6.227   -40.530 37.799  1.00 29.29  ? 223  HIS A CB  1 
ATOM   1704  C  CG  . HIS A  1 223 ? 5.742   -41.944 37.905  1.00 24.28  ? 223  HIS A CG  1 
ATOM   1705  N  ND1 . HIS A  1 223 ? 5.132   -42.599 36.860  1.00 20.95  ? 223  HIS A ND1 1 
ATOM   1706  C  CD2 . HIS A  1 223 ? 5.718   -42.802 38.952  1.00 23.31  ? 223  HIS A CD2 1 
ATOM   1707  C  CE1 . HIS A  1 223 ? 4.778   -43.811 37.247  1.00 20.32  ? 223  HIS A CE1 1 
ATOM   1708  N  NE2 . HIS A  1 223 ? 5.124   -43.961 38.513  1.00 21.43  ? 223  HIS A NE2 1 
ATOM   1709  N  N   . ARG A  1 224 ? 5.055   -37.541 36.427  1.00 16.20  ? 224  ARG A N   1 
ATOM   1710  C  CA  . ARG A  1 224 ? 5.639   -36.309 35.909  1.00 16.20  ? 224  ARG A CA  1 
ATOM   1711  C  C   . ARG A  1 224 ? 4.669   -35.544 35.052  1.00 16.16  ? 224  ARG A C   1 
ATOM   1712  O  O   . ARG A  1 224 ? 3.849   -36.152 34.355  1.00 15.45  ? 224  ARG A O   1 
ATOM   1713  C  CB  . ARG A  1 224 ? 6.818   -36.662 35.029  1.00 27.83  ? 224  ARG A CB  1 
ATOM   1714  C  CG  . ARG A  1 224 ? 8.091   -36.040 35.469  1.00 31.17  ? 224  ARG A CG  1 
ATOM   1715  C  CD  . ARG A  1 224 ? 9.225   -36.936 35.084  1.00 33.67  ? 224  ARG A CD  1 
ATOM   1716  N  NE  . ARG A  1 224 ? 8.920   -38.325 35.397  1.00 35.01  ? 224  ARG A NE  1 
ATOM   1717  C  CZ  . ARG A  1 224 ? 9.848   -39.249 35.592  1.00 40.92  ? 224  ARG A CZ  1 
ATOM   1718  N  NH1 . ARG A  1 224 ? 11.130  -38.911 35.516  1.00 42.73  ? 224  ARG A NH1 1 
ATOM   1719  N  NH2 . ARG A  1 224 ? 9.499   -40.502 35.872  1.00 44.45  ? 224  ARG A NH2 1 
ATOM   1720  N  N   . ALA A  1 225 ? 4.790   -34.225 35.000  1.00 15.71  ? 225  ALA A N   1 
ATOM   1721  C  CA  . ALA A  1 225 ? 3.778   -33.505 34.231  1.00 17.17  ? 225  ALA A CA  1 
ATOM   1722  C  C   . ALA A  1 225 ? 4.326   -32.459 33.269  1.00 18.42  ? 225  ALA A C   1 
ATOM   1723  O  O   . ALA A  1 225 ? 5.327   -31.826 33.563  1.00 18.22  ? 225  ALA A O   1 
ATOM   1724  C  CB  . ALA A  1 225 ? 2.748   -32.894 35.172  1.00 23.60  ? 225  ALA A CB  1 
ATOM   1725  N  N   . VAL A  1 226 ? 3.673   -32.291 32.116  1.00 29.39  ? 226  VAL A N   1 
ATOM   1726  C  CA  . VAL A  1 226 ? 3.963   -31.181 31.207  1.00 27.49  ? 226  VAL A CA  1 
ATOM   1727  C  C   . VAL A  1 226 ? 2.689   -30.428 30.873  1.00 25.98  ? 226  VAL A C   1 
ATOM   1728  O  O   . VAL A  1 226 ? 1.787   -30.962 30.199  1.00 27.27  ? 226  VAL A O   1 
ATOM   1729  C  CB  . VAL A  1 226 ? 4.591   -31.638 29.890  1.00 15.77  ? 226  VAL A CB  1 
ATOM   1730  C  CG1 . VAL A  1 226 ? 5.039   -30.456 29.085  1.00 16.14  ? 226  VAL A CG1 1 
ATOM   1731  C  CG2 . VAL A  1 226 ? 5.748   -32.532 30.154  1.00 22.87  ? 226  VAL A CG2 1 
ATOM   1732  N  N   . LEU A  1 227 ? 2.643   -29.182 31.343  1.00 15.82  ? 227  LEU A N   1 
ATOM   1733  C  CA  . LEU A  1 227 ? 1.566   -28.247 31.061  1.00 15.37  ? 227  LEU A CA  1 
ATOM   1734  C  C   . LEU A  1 227 ? 2.000   -27.211 29.998  1.00 22.12  ? 227  LEU A C   1 
ATOM   1735  O  O   . LEU A  1 227 ? 2.868   -26.328 30.237  1.00 25.15  ? 227  LEU A O   1 
ATOM   1736  C  CB  . LEU A  1 227 ? 1.129   -27.557 32.350  1.00 15.35  ? 227  LEU A CB  1 
ATOM   1737  C  CG  . LEU A  1 227 ? 0.622   -28.452 33.476  1.00 15.09  ? 227  LEU A CG  1 
ATOM   1738  C  CD1 . LEU A  1 227 ? 1.738   -28.850 34.364  1.00 22.84  ? 227  LEU A CD1 1 
ATOM   1739  C  CD2 . LEU A  1 227 ? -0.413  -27.725 34.283  1.00 37.43  ? 227  LEU A CD2 1 
ATOM   1740  N  N   . GLN A  1 228 ? 1.412   -27.337 28.810  1.00 19.27  ? 228  GLN A N   1 
ATOM   1741  C  CA  . GLN A  1 228 ? 1.755   -26.451 27.711  1.00 17.37  ? 228  GLN A CA  1 
ATOM   1742  C  C   . GLN A  1 228 ? 0.615   -25.482 27.485  1.00 16.64  ? 228  GLN A C   1 
ATOM   1743  O  O   . GLN A  1 228 ? -0.432  -25.865 26.971  1.00 16.88  ? 228  GLN A O   1 
ATOM   1744  C  CB  . GLN A  1 228 ? 1.975   -27.250 26.427  1.00 25.06  ? 228  GLN A CB  1 
ATOM   1745  C  CG  . GLN A  1 228 ? 2.910   -28.444 26.569  1.00 28.86  ? 228  GLN A CG  1 
ATOM   1746  C  CD  . GLN A  1 228 ? 3.157   -29.154 25.242  1.00 33.39  ? 228  GLN A CD  1 
ATOM   1747  O  OE1 . GLN A  1 228 ? 4.133   -29.890 25.080  1.00 34.07  ? 228  GLN A OE1 1 
ATOM   1748  N  NE2 . GLN A  1 228 ? 2.270   -28.929 24.286  1.00 36.04  ? 228  GLN A NE2 1 
ATOM   1749  N  N   . SER A  1 229 ? 0.837   -24.226 27.854  1.00 17.44  ? 229  SER A N   1 
ATOM   1750  C  CA  . SER A  1 229 ? -0.086  -23.123 27.559  1.00 19.73  ? 229  SER A CA  1 
ATOM   1751  C  C   . SER A  1 229 ? -1.471  -23.277 28.169  1.00 20.09  ? 229  SER A C   1 
ATOM   1752  O  O   . SER A  1 229 ? -2.468  -22.947 27.534  1.00 16.93  ? 229  SER A O   1 
ATOM   1753  C  CB  . SER A  1 229 ? -0.198  -22.869 26.050  1.00 25.89  ? 229  SER A CB  1 
ATOM   1754  O  OG  . SER A  1 229 ? 1.000   -22.331 25.510  1.00 27.86  ? 229  SER A OG  1 
ATOM   1755  N  N   . GLY A  1 230 ? -1.518  -23.772 29.401  1.00 16.32  ? 230  GLY A N   1 
ATOM   1756  C  CA  . GLY A  1 230 ? -2.759  -23.871 30.143  1.00 16.12  ? 230  GLY A CA  1 
ATOM   1757  C  C   . GLY A  1 230 ? -2.462  -24.323 31.558  1.00 16.67  ? 230  GLY A C   1 
ATOM   1758  O  O   . GLY A  1 230 ? -1.412  -24.901 31.804  1.00 17.21  ? 230  GLY A O   1 
ATOM   1759  N  N   . THR A  1 231 ? -3.380  -24.056 32.484  1.00 21.06  ? 231  THR A N   1 
ATOM   1760  C  CA  . THR A  1 231 ? -3.179  -24.319 33.909  1.00 23.43  ? 231  THR A CA  1 
ATOM   1761  C  C   . THR A  1 231 ? -4.527  -24.650 34.568  1.00 20.43  ? 231  THR A C   1 
ATOM   1762  O  O   . THR A  1 231 ? -5.564  -24.286 34.034  1.00 17.20  ? 231  THR A O   1 
ATOM   1763  C  CB  . THR A  1 231 ? -2.586  -23.071 34.562  1.00 39.56  ? 231  THR A CB  1 
ATOM   1764  O  OG1 . THR A  1 231 ? -3.194  -21.917 33.972  1.00 43.83  ? 231  THR A OG1 1 
ATOM   1765  C  CG2 . THR A  1 231 ? -1.088  -22.991 34.317  1.00 40.97  ? 231  THR A CG2 1 
ATOM   1766  N  N   . PRO A  1 232 ? -4.533  -25.369 35.706  1.00 15.58  ? 232  PRO A N   1 
ATOM   1767  C  CA  . PRO A  1 232 ? -5.823  -25.555 36.395  1.00 15.76  ? 232  PRO A CA  1 
ATOM   1768  C  C   . PRO A  1 232 ? -6.320  -24.302 37.120  1.00 16.17  ? 232  PRO A C   1 
ATOM   1769  O  O   . PRO A  1 232 ? -7.517  -24.075 37.243  1.00 16.42  ? 232  PRO A O   1 
ATOM   1770  C  CB  . PRO A  1 232 ? -5.547  -26.679 37.400  1.00 15.56  ? 232  PRO A CB  1 
ATOM   1771  C  CG  . PRO A  1 232 ? -4.062  -26.902 37.386  1.00 20.38  ? 232  PRO A CG  1 
ATOM   1772  C  CD  . PRO A  1 232 ? -3.407  -25.887 36.496  1.00 15.51  ? 232  PRO A CD  1 
ATOM   1773  N  N   . ASN A  1 233 ? -5.399  -23.480 37.595  1.00 25.64  ? 233  ASN A N   1 
ATOM   1774  C  CA  . ASN A  1 233 ? -5.789  -22.206 38.166  1.00 26.44  ? 233  ASN A CA  1 
ATOM   1775  C  C   . ASN A  1 233 ? -6.073  -21.271 37.019  1.00 28.57  ? 233  ASN A C   1 
ATOM   1776  O  O   . ASN A  1 233 ? -5.916  -21.645 35.866  1.00 30.67  ? 233  ASN A O   1 
ATOM   1777  C  CB  . ASN A  1 233 ? -4.677  -21.629 39.037  1.00 28.78  ? 233  ASN A CB  1 
ATOM   1778  C  CG  . ASN A  1 233 ? -3.335  -21.602 38.334  1.00 27.34  ? 233  ASN A CG  1 
ATOM   1779  O  OD1 . ASN A  1 233 ? -2.868  -22.624 37.826  1.00 26.95  ? 233  ASN A OD1 1 
ATOM   1780  N  ND2 . ASN A  1 233 ? -2.703  -20.429 38.305  1.00 24.52  ? 233  ASN A ND2 1 
ATOM   1781  N  N   . GLY A  1 234 ? -6.470  -20.047 37.310  1.00 33.83  ? 234  GLY A N   1 
ATOM   1782  C  CA  . GLY A  1 234 ? -6.785  -19.139 36.230  1.00 34.94  ? 234  GLY A CA  1 
ATOM   1783  C  C   . GLY A  1 234 ? -8.258  -19.145 35.869  1.00 33.02  ? 234  GLY A C   1 
ATOM   1784  O  O   . GLY A  1 234 ? -8.983  -20.092 36.208  1.00 31.88  ? 234  GLY A O   1 
ATOM   1785  N  N   . PRO A  1 235 ? -8.693  -18.094 35.144  1.00 29.66  ? 235  PRO A N   1 
ATOM   1786  C  CA  . PRO A  1 235 ? -10.094 -17.691 34.929  1.00 26.65  ? 235  PRO A CA  1 
ATOM   1787  C  C   . PRO A  1 235 ? -10.969 -18.675 34.165  1.00 24.65  ? 235  PRO A C   1 
ATOM   1788  O  O   . PRO A  1 235 ? -12.149 -18.773 34.473  1.00 25.07  ? 235  PRO A O   1 
ATOM   1789  C  CB  . PRO A  1 235 ? -9.968  -16.392 34.125  1.00 24.18  ? 235  PRO A CB  1 
ATOM   1790  C  CG  . PRO A  1 235 ? -8.603  -16.474 33.462  1.00 23.95  ? 235  PRO A CG  1 
ATOM   1791  C  CD  . PRO A  1 235 ? -7.741  -17.223 34.418  1.00 24.96  ? 235  PRO A CD  1 
ATOM   1792  N  N   . TRP A  1 236 ? -10.426 -19.345 33.156  1.00 18.58  ? 236  TRP A N   1 
ATOM   1793  C  CA  . TRP A  1 236 ? -11.267 -20.122 32.260  1.00 18.57  ? 236  TRP A CA  1 
ATOM   1794  C  C   . TRP A  1 236 ? -11.502 -21.609 32.571  1.00 21.85  ? 236  TRP A C   1 
ATOM   1795  O  O   . TRP A  1 236 ? -12.485 -22.186 32.096  1.00 21.66  ? 236  TRP A O   1 
ATOM   1796  C  CB  . TRP A  1 236 ? -10.771 -19.946 30.817  1.00 23.02  ? 236  TRP A CB  1 
ATOM   1797  C  CG  . TRP A  1 236 ? -9.366  -20.363 30.635  1.00 22.02  ? 236  TRP A CG  1 
ATOM   1798  C  CD1 . TRP A  1 236 ? -8.264  -19.571 30.701  1.00 23.42  ? 236  TRP A CD1 1 
ATOM   1799  C  CD2 . TRP A  1 236 ? -8.897  -21.688 30.375  1.00 22.78  ? 236  TRP A CD2 1 
ATOM   1800  N  NE1 . TRP A  1 236 ? -7.129  -20.318 30.497  1.00 25.16  ? 236  TRP A NE1 1 
ATOM   1801  C  CE2 . TRP A  1 236 ? -7.490  -21.621 30.295  1.00 25.78  ? 236  TRP A CE2 1 
ATOM   1802  C  CE3 . TRP A  1 236 ? -9.529  -22.921 30.204  1.00 22.22  ? 236  TRP A CE3 1 
ATOM   1803  C  CZ2 . TRP A  1 236 ? -6.703  -22.745 30.048  1.00 28.35  ? 236  TRP A CZ2 1 
ATOM   1804  C  CZ3 . TRP A  1 236 ? -8.755  -24.030 29.958  1.00 24.70  ? 236  TRP A CZ3 1 
ATOM   1805  C  CH2 . TRP A  1 236 ? -7.349  -23.938 29.878  1.00 28.27  ? 236  TRP A CH2 1 
ATOM   1806  N  N   . ALA A  1 237 ? -10.664 -22.224 33.395  1.00 18.09  ? 237  ALA A N   1 
ATOM   1807  C  CA  . ALA A  1 237 ? -10.659 -23.690 33.451  1.00 27.40  ? 237  ALA A CA  1 
ATOM   1808  C  C   . ALA A  1 237 ? -11.565 -24.359 34.496  1.00 33.55  ? 237  ALA A C   1 
ATOM   1809  O  O   . ALA A  1 237 ? -11.735 -25.579 34.484  1.00 38.17  ? 237  ALA A O   1 
ATOM   1810  C  CB  . ALA A  1 237 ? -9.246  -24.203 33.573  1.00 16.52  ? 237  ALA A CB  1 
ATOM   1811  N  N   . THR A  1 238 ? -12.146 -23.577 35.396  1.00 33.16  ? 238  THR A N   1 
ATOM   1812  C  CA  . THR A  1 238 ? -13.001 -24.139 36.440  1.00 29.02  ? 238  THR A CA  1 
ATOM   1813  C  C   . THR A  1 238 ? -14.232 -23.273 36.627  1.00 24.62  ? 238  THR A C   1 
ATOM   1814  O  O   . THR A  1 238 ? -14.251 -22.110 36.209  1.00 23.93  ? 238  THR A O   1 
ATOM   1815  C  CB  . THR A  1 238 ? -12.274 -24.269 37.813  1.00 33.68  ? 238  THR A CB  1 
ATOM   1816  O  OG1 . THR A  1 238 ? -10.918 -23.817 37.710  1.00 34.94  ? 238  THR A OG1 1 
ATOM   1817  C  CG2 . THR A  1 238 ? -12.263 -25.693 38.252  1.00 31.55  ? 238  THR A CG2 1 
ATOM   1818  N  N   . VAL A  1 239 ? -15.263 -23.842 37.244  1.00 19.06  ? 239  VAL A N   1 
ATOM   1819  C  CA  . VAL A  1 239 ? -16.439 -23.061 37.603  1.00 20.28  ? 239  VAL A CA  1 
ATOM   1820  C  C   . VAL A  1 239 ? -16.942 -23.358 39.008  1.00 24.07  ? 239  VAL A C   1 
ATOM   1821  O  O   . VAL A  1 239 ? -16.805 -24.483 39.510  1.00 20.09  ? 239  VAL A O   1 
ATOM   1822  C  CB  . VAL A  1 239 ? -17.626 -23.224 36.605  1.00 20.45  ? 239  VAL A CB  1 
ATOM   1823  C  CG1 . VAL A  1 239 ? -17.429 -22.356 35.381  1.00 20.52  ? 239  VAL A CG1 1 
ATOM   1824  C  CG2 . VAL A  1 239 ? -17.826 -24.678 36.237  1.00 20.17  ? 239  VAL A CG2 1 
ATOM   1825  N  N   . SER A  1 240 ? -17.544 -22.323 39.600  1.00 27.12  ? 240  SER A N   1 
ATOM   1826  C  CA  . SER A  1 240 ? -18.304 -22.416 40.830  1.00 28.60  ? 240  SER A CA  1 
ATOM   1827  C  C   . SER A  1 240 ? -19.317 -23.537 40.689  1.00 25.16  ? 240  SER A C   1 
ATOM   1828  O  O   . SER A  1 240 ? -19.849 -23.766 39.605  1.00 25.79  ? 240  SER A O   1 
ATOM   1829  C  CB  . SER A  1 240 ? -19.046 -21.098 41.050  1.00 52.57  ? 240  SER A CB  1 
ATOM   1830  O  OG  . SER A  1 240 ? -19.949 -21.171 42.144  1.00 59.48  ? 240  SER A OG  1 
ATOM   1831  N  N   . ALA A  1 241 ? -19.558 -24.274 41.764  1.00 26.41  ? 241  ALA A N   1 
ATOM   1832  C  CA  . ALA A  1 241 ? -20.540 -25.343 41.697  1.00 27.61  ? 241  ALA A CA  1 
ATOM   1833  C  C   . ALA A  1 241 ? -21.917 -24.745 41.363  1.00 27.50  ? 241  ALA A C   1 
ATOM   1834  O  O   . ALA A  1 241 ? -22.677 -25.265 40.535  1.00 27.86  ? 241  ALA A O   1 
ATOM   1835  C  CB  . ALA A  1 241 ? -20.566 -26.093 43.008  1.00 33.94  ? 241  ALA A CB  1 
ATOM   1836  N  N   . GLY A  1 242 ? -22.211 -23.621 41.997  1.00 24.54  ? 242  GLY A N   1 
ATOM   1837  C  CA  . GLY A  1 242 ? -23.434 -22.900 41.729  1.00 25.62  ? 242  GLY A CA  1 
ATOM   1838  C  C   . GLY A  1 242 ? -23.523 -22.381 40.312  1.00 26.44  ? 242  GLY A C   1 
ATOM   1839  O  O   . GLY A  1 242 ? -24.592 -22.417 39.713  1.00 30.12  ? 242  GLY A O   1 
ATOM   1840  N  N   . GLU A  1 243 ? -22.414 -21.888 39.770  1.00 25.79  ? 243  GLU A N   1 
ATOM   1841  C  CA  . GLU A  1 243 ? -22.409 -21.444 38.378  1.00 29.40  ? 243  GLU A CA  1 
ATOM   1842  C  C   . GLU A  1 243 ? -22.727 -22.604 37.437  1.00 31.48  ? 243  GLU A C   1 
ATOM   1843  O  O   . GLU A  1 243 ? -23.661 -22.520 36.640  1.00 29.88  ? 243  GLU A O   1 
ATOM   1844  C  CB  . GLU A  1 243 ? -21.082 -20.797 37.986  1.00 32.44  ? 243  GLU A CB  1 
ATOM   1845  C  CG  . GLU A  1 243 ? -20.978 -20.486 36.497  1.00 39.11  ? 243  GLU A CG  1 
ATOM   1846  C  CD  . GLU A  1 243 ? -21.961 -19.401 35.997  1.00 50.15  ? 243  GLU A CD  1 
ATOM   1847  O  OE1 . GLU A  1 243 ? -22.680 -18.774 36.817  1.00 55.42  ? 243  GLU A OE1 1 
ATOM   1848  O  OE2 . GLU A  1 243 ? -22.006 -19.170 34.763  1.00 52.25  ? 243  GLU A OE2 1 
ATOM   1849  N  N   . ALA A  1 244 ? -21.958 -23.686 37.551  1.00 40.91  ? 244  ALA A N   1 
ATOM   1850  C  CA  . ALA A  1 244 ? -22.195 -24.891 36.760  1.00 38.14  ? 244  ALA A CA  1 
ATOM   1851  C  C   . ALA A  1 244 ? -23.664 -25.302 36.817  1.00 36.63  ? 244  ALA A C   1 
ATOM   1852  O  O   . ALA A  1 244 ? -24.256 -25.622 35.786  1.00 37.04  ? 244  ALA A O   1 
ATOM   1853  C  CB  . ALA A  1 244 ? -21.301 -26.028 37.234  1.00 26.75  ? 244  ALA A CB  1 
ATOM   1854  N  N   . ARG A  1 245 ? -24.249 -25.251 38.016  1.00 25.00  ? 245  ARG A N   1 
ATOM   1855  C  CA  . ARG A  1 245 ? -25.663 -25.609 38.226  1.00 26.24  ? 245  ARG A CA  1 
ATOM   1856  C  C   . ARG A  1 245 ? -26.624 -24.690 37.485  1.00 27.25  ? 245  ARG A C   1 
ATOM   1857  O  O   . ARG A  1 245 ? -27.590 -25.129 36.843  1.00 28.06  ? 245  ARG A O   1 
ATOM   1858  C  CB  . ARG A  1 245 ? -25.987 -25.579 39.715  1.00 36.17  ? 245  ARG A CB  1 
ATOM   1859  C  CG  . ARG A  1 245 ? -27.463 -25.504 40.015  1.00 39.17  ? 245  ARG A CG  1 
ATOM   1860  C  CD  . ARG A  1 245 ? -27.688 -25.797 41.477  1.00 41.98  ? 245  ARG A CD  1 
ATOM   1861  N  NE  . ARG A  1 245 ? -27.221 -27.136 41.825  1.00 41.07  ? 245  ARG A NE  1 
ATOM   1862  C  CZ  . ARG A  1 245 ? -27.939 -28.243 41.644  1.00 41.37  ? 245  ARG A CZ  1 
ATOM   1863  N  NH1 . ARG A  1 245 ? -29.161 -28.182 41.112  1.00 37.76  ? 245  ARG A NH1 1 
ATOM   1864  N  NH2 . ARG A  1 245 ? -27.429 -29.418 41.989  1.00 43.93  ? 245  ARG A NH2 1 
ATOM   1865  N  N   . ARG A  1 246 ? -26.330 -23.407 37.607  1.00 33.56  ? 246  ARG A N   1 
ATOM   1866  C  CA  . ARG A  1 246 ? -27.021 -22.360 36.897  1.00 38.38  ? 246  ARG A CA  1 
ATOM   1867  C  C   . ARG A  1 246 ? -27.031 -22.661 35.396  1.00 38.00  ? 246  ARG A C   1 
ATOM   1868  O  O   . ARG A  1 246 ? -28.105 -22.666 34.754  1.00 40.80  ? 246  ARG A O   1 
ATOM   1869  C  CB  . ARG A  1 246 ? -26.320 -21.022 37.175  1.00 50.18  ? 246  ARG A CB  1 
ATOM   1870  C  CG  . ARG A  1 246 ? -27.045 -19.793 36.653  1.00 55.44  ? 246  ARG A CG  1 
ATOM   1871  C  CD  . ARG A  1 246 ? -26.129 -18.554 36.618  1.00 57.33  ? 246  ARG A CD  1 
ATOM   1872  N  NE  . ARG A  1 246 ? -25.255 -18.498 35.441  1.00 56.03  ? 246  ARG A NE  1 
ATOM   1873  C  CZ  . ARG A  1 246 ? -25.681 -18.412 34.180  1.00 53.38  ? 246  ARG A CZ  1 
ATOM   1874  N  NH1 . ARG A  1 246 ? -26.981 -18.386 33.896  1.00 53.71  ? 246  ARG A NH1 1 
ATOM   1875  N  NH2 . ARG A  1 246 ? -24.801 -18.374 33.193  1.00 49.81  ? 246  ARG A NH2 1 
ATOM   1876  N  N   . ARG A  1 247 ? -25.840 -22.919 34.845  1.00 35.97  ? 247  ARG A N   1 
ATOM   1877  C  CA  . ARG A  1 247 ? -25.675 -23.124 33.403  1.00 35.33  ? 247  ARG A CA  1 
ATOM   1878  C  C   . ARG A  1 247 ? -26.427 -24.380 32.960  1.00 34.98  ? 247  ARG A C   1 
ATOM   1879  O  O   . ARG A  1 247 ? -26.998 -24.424 31.864  1.00 33.79  ? 247  ARG A O   1 
ATOM   1880  C  CB  . ARG A  1 247 ? -24.193 -23.184 33.002  1.00 25.27  ? 247  ARG A CB  1 
ATOM   1881  C  CG  . ARG A  1 247 ? -23.453 -21.847 33.062  1.00 25.03  ? 247  ARG A CG  1 
ATOM   1882  C  CD  . ARG A  1 247 ? -21.952 -22.049 32.826  1.00 23.76  ? 247  ARG A CD  1 
ATOM   1883  N  NE  . ARG A  1 247 ? -21.147 -20.824 32.916  1.00 23.56  ? 247  ARG A NE  1 
ATOM   1884  C  CZ  . ARG A  1 247 ? -19.833 -20.762 32.661  1.00 22.66  ? 247  ARG A CZ  1 
ATOM   1885  N  NH1 . ARG A  1 247 ? -19.168 -21.857 32.298  1.00 21.85  ? 247  ARG A NH1 1 
ATOM   1886  N  NH2 . ARG A  1 247 ? -19.173 -19.606 32.768  1.00 22.65  ? 247  ARG A NH2 1 
ATOM   1887  N  N   . ALA A  1 248 ? -26.446 -25.385 33.835  1.00 33.61  ? 248  ALA A N   1 
ATOM   1888  C  CA  . ALA A  1 248 ? -27.067 -26.664 33.517  1.00 29.70  ? 248  ALA A CA  1 
ATOM   1889  C  C   . ALA A  1 248 ? -28.552 -26.508 33.421  1.00 28.77  ? 248  ALA A C   1 
ATOM   1890  O  O   . ALA A  1 248 ? -29.150 -26.892 32.422  1.00 29.43  ? 248  ALA A O   1 
ATOM   1891  C  CB  . ALA A  1 248 ? -26.732 -27.686 34.554  1.00 26.69  ? 248  ALA A CB  1 
ATOM   1892  N  N   . THR A  1 249 ? -29.156 -25.943 34.462  1.00 36.26  ? 249  THR A N   1 
ATOM   1893  C  CA  . THR A  1 249 ? -30.615 -25.819 34.478  1.00 40.67  ? 249  THR A CA  1 
ATOM   1894  C  C   . THR A  1 249 ? -31.078 -24.842 33.417  1.00 43.08  ? 249  THR A C   1 
ATOM   1895  O  O   . THR A  1 249 ? -32.191 -24.967 32.909  1.00 47.48  ? 249  THR A O   1 
ATOM   1896  C  CB  . THR A  1 249 ? -31.155 -25.359 35.830  1.00 33.65  ? 249  THR A CB  1 
ATOM   1897  O  OG1 . THR A  1 249 ? -30.515 -24.134 36.188  1.00 35.28  ? 249  THR A OG1 1 
ATOM   1898  C  CG2 . THR A  1 249 ? -30.889 -26.390 36.910  1.00 31.45  ? 249  THR A CG2 1 
ATOM   1899  N  N   . LEU A  1 250 ? -30.228 -23.869 33.086  1.00 32.09  ? 250  LEU A N   1 
ATOM   1900  C  CA  . LEU A  1 250 ? -30.524 -22.974 31.969  1.00 32.81  ? 250  LEU A CA  1 
ATOM   1901  C  C   . LEU A  1 250 ? -30.507 -23.693 30.615  1.00 31.84  ? 250  LEU A C   1 
ATOM   1902  O  O   . LEU A  1 250 ? -31.425 -23.521 29.815  1.00 33.12  ? 250  LEU A O   1 
ATOM   1903  C  CB  . LEU A  1 250 ? -29.576 -21.781 31.934  1.00 31.13  ? 250  LEU A CB  1 
ATOM   1904  C  CG  . LEU A  1 250 ? -29.611 -20.980 30.624  1.00 31.64  ? 250  LEU A CG  1 
ATOM   1905  C  CD1 . LEU A  1 250 ? -30.978 -20.380 30.358  1.00 33.45  ? 250  LEU A CD1 1 
ATOM   1906  C  CD2 . LEU A  1 250 ? -28.571 -19.881 30.639  1.00 57.92  ? 250  LEU A CD2 1 
ATOM   1907  N  N   . LEU A  1 251 ? -29.472 -24.486 30.350  1.00 30.53  ? 251  LEU A N   1 
ATOM   1908  C  CA  . LEU A  1 251 ? -29.425 -25.244 29.103  1.00 30.56  ? 251  LEU A CA  1 
ATOM   1909  C  C   . LEU A  1 251 ? -30.611 -26.178 29.033  1.00 31.75  ? 251  LEU A C   1 
ATOM   1910  O  O   . LEU A  1 251 ? -31.212 -26.340 27.980  1.00 38.71  ? 251  LEU A O   1 
ATOM   1911  C  CB  . LEU A  1 251 ? -28.143 -26.052 28.984  1.00 30.25  ? 251  LEU A CB  1 
ATOM   1912  C  CG  . LEU A  1 251 ? -28.008 -26.786 27.650  1.00 34.01  ? 251  LEU A CG  1 
ATOM   1913  C  CD1 . LEU A  1 251 ? -26.599 -26.622 27.160  1.00 32.67  ? 251  LEU A CD1 1 
ATOM   1914  C  CD2 . LEU A  1 251 ? -28.347 -28.261 27.771  1.00 30.43  ? 251  LEU A CD2 1 
ATOM   1915  N  N   . ALA A  1 252 ? -30.924 -26.797 30.165  1.00 37.90  ? 252  ALA A N   1 
ATOM   1916  C  CA  . ALA A  1 252 ? -32.118 -27.612 30.311  1.00 39.68  ? 252  ALA A CA  1 
ATOM   1917  C  C   . ALA A  1 252 ? -33.358 -26.848 29.840  1.00 40.95  ? 252  ALA A C   1 
ATOM   1918  O  O   . ALA A  1 252 ? -34.107 -27.341 28.998  1.00 40.97  ? 252  ALA A O   1 
ATOM   1919  C  CB  . ALA A  1 252 ? -32.276 -28.036 31.755  1.00 46.00  ? 252  ALA A CB  1 
ATOM   1920  N  N   . ARG A  1 253 ? -33.561 -25.643 30.376  1.00 35.66  ? 253  ARG A N   1 
ATOM   1921  C  CA  . ARG A  1 253 ? -34.657 -24.781 29.938  1.00 39.60  ? 253  ARG A CA  1 
ATOM   1922  C  C   . ARG A  1 253 ? -34.620 -24.547 28.429  1.00 37.94  ? 253  ARG A C   1 
ATOM   1923  O  O   . ARG A  1 253 ? -35.651 -24.604 27.766  1.00 38.86  ? 253  ARG A O   1 
ATOM   1924  C  CB  . ARG A  1 253 ? -34.646 -23.441 30.685  1.00 70.52  ? 253  ARG A CB  1 
ATOM   1925  C  CG  . ARG A  1 253 ? -35.658 -23.337 31.832  1.00 81.42  ? 253  ARG A CG  1 
ATOM   1926  C  CD  . ARG A  1 253 ? -36.415 -21.996 31.813  1.00 91.35  ? 253  ARG A CD  1 
ATOM   1927  N  NE  . ARG A  1 253 ? -37.455 -21.939 30.778  1.00 100.12 ? 253  ARG A NE  1 
ATOM   1928  C  CZ  . ARG A  1 253 ? -37.420 -21.157 29.696  1.00 103.36 ? 253  ARG A CZ  1 
ATOM   1929  N  NH1 . ARG A  1 253 ? -36.391 -20.343 29.487  1.00 103.47 ? 253  ARG A NH1 1 
ATOM   1930  N  NH2 . ARG A  1 253 ? -38.420 -21.189 28.817  1.00 103.49 ? 253  ARG A NH2 1 
ATOM   1931  N  N   . LEU A  1 254 ? -33.429 -24.309 27.891  1.00 54.27  ? 254  LEU A N   1 
ATOM   1932  C  CA  . LEU A  1 254 ? -33.270 -23.979 26.473  1.00 56.11  ? 254  LEU A CA  1 
ATOM   1933  C  C   . LEU A  1 254 ? -33.656 -25.095 25.517  1.00 58.05  ? 254  LEU A C   1 
ATOM   1934  O  O   . LEU A  1 254 ? -34.164 -24.821 24.436  1.00 62.95  ? 254  LEU A O   1 
ATOM   1935  C  CB  . LEU A  1 254 ? -31.841 -23.521 26.169  1.00 47.18  ? 254  LEU A CB  1 
ATOM   1936  C  CG  . LEU A  1 254 ? -31.561 -22.152 26.754  1.00 34.51  ? 254  LEU A CG  1 
ATOM   1937  C  CD1 . LEU A  1 254 ? -30.338 -21.565 26.171  1.00 33.47  ? 254  LEU A CD1 1 
ATOM   1938  C  CD2 . LEU A  1 254 ? -32.746 -21.269 26.481  1.00 62.36  ? 254  LEU A CD2 1 
ATOM   1939  N  N   . VAL A  1 255 ? -33.407 -26.343 25.903  1.00 36.36  ? 255  VAL A N   1 
ATOM   1940  C  CA  . VAL A  1 255 ? -33.710 -27.476 25.039  1.00 36.63  ? 255  VAL A CA  1 
ATOM   1941  C  C   . VAL A  1 255 ? -35.118 -27.961 25.305  1.00 43.62  ? 255  VAL A C   1 
ATOM   1942  O  O   . VAL A  1 255 ? -35.516 -29.031 24.836  1.00 46.17  ? 255  VAL A O   1 
ATOM   1943  C  CB  . VAL A  1 255 ? -32.741 -28.634 25.208  1.00 45.92  ? 255  VAL A CB  1 
ATOM   1944  C  CG1 . VAL A  1 255 ? -31.338 -28.185 24.885  1.00 45.25  ? 255  VAL A CG1 1 
ATOM   1945  C  CG2 . VAL A  1 255 ? -32.822 -29.170 26.615  1.00 49.14  ? 255  VAL A CG2 1 
ATOM   1946  N  N   . GLY A  1 256 ? -35.856 -27.193 26.101  1.00 59.00  ? 256  GLY A N   1 
ATOM   1947  C  CA  . GLY A  1 256 ? -37.258 -27.481 26.336  1.00 64.47  ? 256  GLY A CA  1 
ATOM   1948  C  C   . GLY A  1 256 ? -37.384 -28.594 27.344  1.00 66.93  ? 256  GLY A C   1 
ATOM   1949  O  O   . GLY A  1 256 ? -38.264 -29.448 27.251  1.00 65.88  ? 256  GLY A O   1 
ATOM   1950  N  N   . CYS A  1 257 ? -36.500 -28.566 28.331  1.00 77.09  ? 257  CYS A N   1 
ATOM   1951  C  CA  . CYS A  1 257 ? -36.486 -29.609 29.328  1.00 80.33  ? 257  CYS A CA  1 
ATOM   1952  C  C   . CYS A  1 257 ? -36.644 -29.031 30.724  1.00 86.71  ? 257  CYS A C   1 
ATOM   1953  O  O   . CYS A  1 257 ? -35.795 -29.248 31.590  1.00 85.58  ? 257  CYS A O   1 
ATOM   1954  C  CB  . CYS A  1 257 ? -35.159 -30.376 29.251  1.00 67.26  ? 257  CYS A CB  1 
ATOM   1955  S  SG  . CYS A  1 257 ? -35.377 -32.150 29.070  1.00 108.14 ? 257  CYS A SG  1 
ATOM   1956  N  N   . PRO A  1 258 ? -37.719 -28.260 30.952  1.00 85.99  ? 258  PRO A N   1 
ATOM   1957  C  CA  . PRO A  1 258 ? -38.142 -28.374 32.345  1.00 90.19  ? 258  PRO A CA  1 
ATOM   1958  C  C   . PRO A  1 258 ? -38.799 -29.744 32.624  1.00 93.47  ? 258  PRO A C   1 
ATOM   1959  O  O   . PRO A  1 258 ? -38.379 -30.368 33.605  1.00 90.04  ? 258  PRO A O   1 
ATOM   1960  C  CB  . PRO A  1 258 ? -39.093 -27.181 32.531  1.00 104.74 ? 258  PRO A CB  1 
ATOM   1961  C  CG  . PRO A  1 258 ? -38.686 -26.199 31.461  1.00 103.18 ? 258  PRO A CG  1 
ATOM   1962  C  CD  . PRO A  1 258 ? -38.257 -27.048 30.299  1.00 101.03 ? 258  PRO A CD  1 
ATOM   1963  N  N   . PRO A  1 259 ? -39.753 -30.230 31.765  1.00 117.90 ? 259  PRO A N   1 
ATOM   1964  C  CA  . PRO A  1 259 ? -40.546 -29.611 30.675  1.00 121.99 ? 259  PRO A CA  1 
ATOM   1965  C  C   . PRO A  1 259 ? -41.734 -28.733 31.137  1.00 129.99 ? 259  PRO A C   1 
ATOM   1966  O  O   . PRO A  1 259 ? -42.458 -29.123 32.057  1.00 132.13 ? 259  PRO A O   1 
ATOM   1967  C  CB  . PRO A  1 259 ? -41.069 -30.822 29.892  1.00 88.33  ? 259  PRO A CB  1 
ATOM   1968  C  CG  . PRO A  1 259 ? -41.221 -31.872 30.916  1.00 86.83  ? 259  PRO A CG  1 
ATOM   1969  C  CD  . PRO A  1 259 ? -40.100 -31.659 31.917  1.00 86.62  ? 259  PRO A CD  1 
ATOM   1970  N  N   . GLY A  1 260 ? -41.944 -27.585 30.487  1.00 119.51 ? 260  GLY A N   1 
ATOM   1971  C  CA  . GLY A  1 260 ? -43.131 -26.763 30.715  1.00 124.08 ? 260  GLY A CA  1 
ATOM   1972  C  C   . GLY A  1 260 ? -43.131 -25.646 31.761  1.00 125.46 ? 260  GLY A C   1 
ATOM   1973  O  O   . GLY A  1 260 ? -44.176 -25.027 31.987  1.00 124.18 ? 260  GLY A O   1 
ATOM   1974  N  N   . GLY A  1 261 ? -41.970 -25.353 32.358  1.00 134.89 ? 261  GLY A N   1 
ATOM   1975  C  CA  . GLY A  1 261 ? -41.852 -24.388 33.454  1.00 135.50 ? 261  GLY A CA  1 
ATOM   1976  C  C   . GLY A  1 261 ? -41.530 -24.946 34.843  1.00 134.86 ? 261  GLY A C   1 
ATOM   1977  O  O   . GLY A  1 261 ? -41.438 -24.199 35.821  1.00 134.45 ? 261  GLY A O   1 
ATOM   1978  N  N   . ALA A  1 262 ? -41.357 -26.263 34.911  1.00 130.34 ? 262  ALA A N   1 
ATOM   1979  C  CA  . ALA A  1 262 ? -40.897 -27.010 36.089  1.00 128.77 ? 262  ALA A CA  1 
ATOM   1980  C  C   . ALA A  1 262 ? -39.353 -27.073 36.153  1.00 128.81 ? 262  ALA A C   1 
ATOM   1981  O  O   . ALA A  1 262 ? -38.672 -26.195 35.615  1.00 128.64 ? 262  ALA A O   1 
ATOM   1982  C  CB  . ALA A  1 262 ? -41.519 -28.401 36.124  1.00 115.41 ? 262  ALA A CB  1 
ATOM   1983  N  N   . GLY A  1 263 ? -38.804 -28.084 36.831  1.00 129.22 ? 263  GLY A N   1 
ATOM   1984  C  CA  . GLY A  1 263 ? -37.358 -28.214 36.981  1.00 124.53 ? 263  GLY A CA  1 
ATOM   1985  C  C   . GLY A  1 263 ? -36.704 -28.128 38.356  1.00 121.57 ? 263  GLY A C   1 
ATOM   1986  O  O   . GLY A  1 263 ? -35.487 -27.933 38.447  1.00 118.78 ? 263  GLY A O   1 
ATOM   1987  N  N   . GLY A  1 264 ? -37.502 -28.248 39.420  1.00 126.10 ? 264  GLY A N   1 
ATOM   1988  C  CA  . GLY A  1 264 ? -36.982 -28.417 40.775  1.00 122.15 ? 264  GLY A CA  1 
ATOM   1989  C  C   . GLY A  1 264 ? -36.247 -29.730 41.074  1.00 116.40 ? 264  GLY A C   1 
ATOM   1990  O  O   . GLY A  1 264 ? -35.126 -29.722 41.596  1.00 114.37 ? 264  GLY A O   1 
ATOM   1991  N  N   . ASN A  1 265 ? -36.877 -30.860 40.757  1.00 103.54 ? 265  ASN A N   1 
ATOM   1992  C  CA  . ASN A  1 265 ? -36.272 -32.177 40.972  1.00 96.54  ? 265  ASN A CA  1 
ATOM   1993  C  C   . ASN A  1 265 ? -35.114 -32.412 39.995  1.00 88.20  ? 265  ASN A C   1 
ATOM   1994  O  O   . ASN A  1 265 ? -35.298 -32.351 38.778  1.00 89.35  ? 265  ASN A O   1 
ATOM   1995  C  CB  . ASN A  1 265 ? -37.348 -33.263 40.803  1.00 88.06  ? 265  ASN A CB  1 
ATOM   1996  C  CG  . ASN A  1 265 ? -36.890 -34.647 41.260  1.00 90.78  ? 265  ASN A CG  1 
ATOM   1997  O  OD1 . ASN A  1 265 ? -36.164 -35.342 40.545  1.00 87.67  ? 265  ASN A OD1 1 
ATOM   1998  N  ND2 . ASN A  1 265 ? -37.347 -35.064 42.448  1.00 97.96  ? 265  ASN A ND2 1 
ATOM   1999  N  N   . ASP A  1 266 ? -33.921 -32.670 40.528  1.00 64.47  ? 266  ASP A N   1 
ATOM   2000  C  CA  . ASP A  1 266 ? -32.752 -32.965 39.691  1.00 52.31  ? 266  ASP A CA  1 
ATOM   2001  C  C   . ASP A  1 266 ? -32.935 -34.191 38.794  1.00 44.09  ? 266  ASP A C   1 
ATOM   2002  O  O   . ASP A  1 266 ? -33.036 -34.048 37.577  1.00 40.52  ? 266  ASP A O   1 
ATOM   2003  C  CB  . ASP A  1 266 ? -31.485 -33.127 40.538  1.00 58.01  ? 266  ASP A CB  1 
ATOM   2004  C  CG  . ASP A  1 266 ? -30.679 -31.843 40.644  1.00 56.07  ? 266  ASP A CG  1 
ATOM   2005  O  OD1 . ASP A  1 266 ? -31.279 -30.744 40.627  1.00 57.06  ? 266  ASP A OD1 1 
ATOM   2006  O  OD2 . ASP A  1 266 ? -29.439 -31.943 40.750  1.00 52.71  ? 266  ASP A OD2 1 
ATOM   2007  N  N   . THR A  1 267 ? -33.003 -35.379 39.405  1.00 50.74  ? 267  THR A N   1 
ATOM   2008  C  CA  . THR A  1 267 ? -33.045 -36.660 38.685  1.00 48.39  ? 267  THR A CA  1 
ATOM   2009  C  C   . THR A  1 267 ? -34.032 -36.609 37.544  1.00 49.50  ? 267  THR A C   1 
ATOM   2010  O  O   . THR A  1 267 ? -33.760 -37.117 36.464  1.00 48.25  ? 267  THR A O   1 
ATOM   2011  C  CB  . THR A  1 267 ? -33.505 -37.832 39.586  1.00 43.94  ? 267  THR A CB  1 
ATOM   2012  O  OG1 . THR A  1 267 ? -33.677 -37.382 40.936  1.00 46.11  ? 267  THR A OG1 1 
ATOM   2013  C  CG2 . THR A  1 267 ? -32.512 -38.991 39.535  1.00 41.04  ? 267  THR A CG2 1 
ATOM   2014  N  N   . GLU A  1 268 ? -35.174 -35.983 37.813  1.00 49.01  ? 268  GLU A N   1 
ATOM   2015  C  CA  . GLU A  1 268 ? -36.229 -35.758 36.838  1.00 54.82  ? 268  GLU A CA  1 
ATOM   2016  C  C   . GLU A  1 268 ? -35.768 -34.898 35.652  1.00 48.74  ? 268  GLU A C   1 
ATOM   2017  O  O   . GLU A  1 268 ? -36.116 -35.179 34.485  1.00 45.72  ? 268  GLU A O   1 
ATOM   2018  C  CB  . GLU A  1 268 ? -37.404 -35.097 37.555  1.00 100.45 ? 268  GLU A CB  1 
ATOM   2019  C  CG  . GLU A  1 268 ? -38.250 -34.182 36.701  1.00 112.95 ? 268  GLU A CG  1 
ATOM   2020  C  CD  . GLU A  1 268 ? -39.385 -34.911 36.029  1.00 122.65 ? 268  GLU A CD  1 
ATOM   2021  O  OE1 . GLU A  1 268 ? -39.217 -36.116 35.725  1.00 124.47 ? 268  GLU A OE1 1 
ATOM   2022  O  OE2 . GLU A  1 268 ? -40.445 -34.279 35.817  1.00 126.35 ? 268  GLU A OE2 1 
ATOM   2023  N  N   . LEU A  1 269 ? -34.978 -33.861 35.957  1.00 48.87  ? 269  LEU A N   1 
ATOM   2024  C  CA  . LEU A  1 269 ? -34.477 -32.910 34.949  1.00 45.64  ? 269  LEU A CA  1 
ATOM   2025  C  C   . LEU A  1 269 ? -33.385 -33.506 34.078  1.00 41.61  ? 269  LEU A C   1 
ATOM   2026  O  O   . LEU A  1 269 ? -33.392 -33.345 32.862  1.00 34.20  ? 269  LEU A O   1 
ATOM   2027  C  CB  . LEU A  1 269 ? -33.969 -31.620 35.603  1.00 36.58  ? 269  LEU A CB  1 
ATOM   2028  C  CG  . LEU A  1 269 ? -33.272 -30.608 34.691  1.00 33.92  ? 269  LEU A CG  1 
ATOM   2029  C  CD1 . LEU A  1 269 ? -33.716 -29.209 35.011  1.00 49.16  ? 269  LEU A CD1 1 
ATOM   2030  C  CD2 . LEU A  1 269 ? -31.778 -30.694 34.847  1.00 32.06  ? 269  LEU A CD2 1 
ATOM   2031  N  N   . ILE A  1 270 ? -32.434 -34.176 34.709  1.00 41.94  ? 270  ILE A N   1 
ATOM   2032  C  CA  . ILE A  1 270 ? -31.403 -34.859 33.954  1.00 38.88  ? 270  ILE A CA  1 
ATOM   2033  C  C   . ILE A  1 270 ? -32.069 -35.938 33.122  1.00 38.30  ? 270  ILE A C   1 
ATOM   2034  O  O   . ILE A  1 270 ? -31.840 -36.037 31.922  1.00 37.48  ? 270  ILE A O   1 
ATOM   2035  C  CB  . ILE A  1 270 ? -30.343 -35.480 34.871  1.00 39.17  ? 270  ILE A CB  1 
ATOM   2036  C  CG1 . ILE A  1 270 ? -29.646 -34.380 35.666  1.00 37.35  ? 270  ILE A CG1 1 
ATOM   2037  C  CG2 . ILE A  1 270 ? -29.334 -36.310 34.072  1.00 37.86  ? 270  ILE A CG2 1 
ATOM   2038  C  CD1 . ILE A  1 270 ? -29.831 -34.547 37.161  1.00 38.60  ? 270  ILE A CD1 1 
ATOM   2039  N  N   . ALA A  1 271 ? -32.920 -36.731 33.750  1.00 40.80  ? 271  ALA A N   1 
ATOM   2040  C  CA  . ALA A  1 271 ? -33.580 -37.796 33.017  1.00 46.58  ? 271  ALA A CA  1 
ATOM   2041  C  C   . ALA A  1 271 ? -34.373 -37.273 31.808  1.00 47.86  ? 271  ALA A C   1 
ATOM   2042  O  O   . ALA A  1 271 ? -34.453 -37.949 30.779  1.00 48.76  ? 271  ALA A O   1 
ATOM   2043  C  CB  . ALA A  1 271 ? -34.450 -38.627 33.932  1.00 59.70  ? 271  ALA A CB  1 
ATOM   2044  N  N   . CYS A  1 272 ? -34.937 -36.072 31.905  1.00 53.22  ? 272  CYS A N   1 
ATOM   2045  C  CA  . CYS A  1 272 ? -35.501 -35.473 30.692  1.00 58.00  ? 272  CYS A CA  1 
ATOM   2046  C  C   . CYS A  1 272 ? -34.392 -35.098 29.678  1.00 57.57  ? 272  CYS A C   1 
ATOM   2047  O  O   . CYS A  1 272 ? -34.476 -35.440 28.494  1.00 58.49  ? 272  CYS A O   1 
ATOM   2048  C  CB  . CYS A  1 272 ? -36.435 -34.285 31.008  1.00 58.52  ? 272  CYS A CB  1 
ATOM   2049  S  SG  . CYS A  1 272 ? -36.997 -33.320 29.543  1.00 97.07  ? 272  CYS A SG  1 
ATOM   2050  N  N   . LEU A  1 273 ? -33.362 -34.398 30.147  1.00 51.39  ? 273  LEU A N   1 
ATOM   2051  C  CA  . LEU A  1 273 ? -32.234 -33.999 29.302  1.00 49.53  ? 273  LEU A CA  1 
ATOM   2052  C  C   . LEU A  1 273 ? -31.653 -35.187 28.537  1.00 48.88  ? 273  LEU A C   1 
ATOM   2053  O  O   . LEU A  1 273 ? -31.191 -35.053 27.400  1.00 47.80  ? 273  LEU A O   1 
ATOM   2054  C  CB  . LEU A  1 273 ? -31.126 -33.391 30.169  1.00 38.27  ? 273  LEU A CB  1 
ATOM   2055  C  CG  . LEU A  1 273 ? -30.643 -31.952 29.985  1.00 35.72  ? 273  LEU A CG  1 
ATOM   2056  C  CD1 . LEU A  1 273 ? -29.818 -31.556 31.200  1.00 29.95  ? 273  LEU A CD1 1 
ATOM   2057  C  CD2 . LEU A  1 273 ? -29.837 -31.811 28.708  1.00 32.60  ? 273  LEU A CD2 1 
ATOM   2058  N  N   . ARG A  1 274 ? -31.681 -36.351 29.178  1.00 50.52  ? 274  ARG A N   1 
ATOM   2059  C  CA  . ARG A  1 274 ? -31.080 -37.548 28.614  1.00 48.30  ? 274  ARG A CA  1 
ATOM   2060  C  C   . ARG A  1 274 ? -31.862 -38.054 27.426  1.00 45.39  ? 274  ARG A C   1 
ATOM   2061  O  O   . ARG A  1 274 ? -31.372 -38.892 26.674  1.00 45.82  ? 274  ARG A O   1 
ATOM   2062  C  CB  . ARG A  1 274 ? -30.952 -38.646 29.665  1.00 49.76  ? 274  ARG A CB  1 
ATOM   2063  C  CG  . ARG A  1 274 ? -29.577 -38.707 30.277  1.00 50.37  ? 274  ARG A CG  1 
ATOM   2064  C  CD  . ARG A  1 274 ? -29.297 -40.066 30.850  1.00 53.90  ? 274  ARG A CD  1 
ATOM   2065  N  NE  . ARG A  1 274 ? -30.125 -40.341 32.013  1.00 56.46  ? 274  ARG A NE  1 
ATOM   2066  C  CZ  . ARG A  1 274 ? -29.679 -40.312 33.262  1.00 57.63  ? 274  ARG A CZ  1 
ATOM   2067  N  NH1 . ARG A  1 274 ? -28.405 -40.018 33.523  1.00 53.24  ? 274  ARG A NH1 1 
ATOM   2068  N  NH2 . ARG A  1 274 ? -30.517 -40.581 34.251  1.00 62.09  ? 274  ARG A NH2 1 
ATOM   2069  N  N   . THR A  1 275 ? -33.083 -37.556 27.268  1.00 38.58  ? 275  THR A N   1 
ATOM   2070  C  CA  . THR A  1 275 ? -33.886 -37.906 26.105  1.00 38.85  ? 275  THR A CA  1 
ATOM   2071  C  C   . THR A  1 275 ? -33.542 -37.083 24.857  1.00 38.70  ? 275  THR A C   1 
ATOM   2072  O  O   . THR A  1 275 ? -33.565 -37.610 23.749  1.00 39.45  ? 275  THR A O   1 
ATOM   2073  C  CB  . THR A  1 275 ? -35.394 -37.828 26.395  1.00 44.13  ? 275  THR A CB  1 
ATOM   2074  O  OG1 . THR A  1 275 ? -35.828 -36.467 26.320  1.00 46.11  ? 275  THR A OG1 1 
ATOM   2075  C  CG2 . THR A  1 275 ? -35.695 -38.393 27.778  1.00 42.75  ? 275  THR A CG2 1 
ATOM   2076  N  N   . ARG A  1 276 ? -33.227 -35.802 25.020  1.00 40.64  ? 276  ARG A N   1 
ATOM   2077  C  CA  . ARG A  1 276 ? -32.925 -34.974 23.853  1.00 41.28  ? 276  ARG A CA  1 
ATOM   2078  C  C   . ARG A  1 276 ? -31.718 -35.532 23.079  1.00 40.12  ? 276  ARG A C   1 
ATOM   2079  O  O   . ARG A  1 276 ? -30.738 -35.971 23.693  1.00 38.77  ? 276  ARG A O   1 
ATOM   2080  C  CB  . ARG A  1 276 ? -32.685 -33.513 24.257  1.00 39.85  ? 276  ARG A CB  1 
ATOM   2081  C  CG  . ARG A  1 276 ? -33.852 -32.833 24.953  1.00 46.07  ? 276  ARG A CG  1 
ATOM   2082  C  CD  . ARG A  1 276 ? -35.011 -32.518 24.010  1.00 56.14  ? 276  ARG A CD  1 
ATOM   2083  N  NE  . ARG A  1 276 ? -36.165 -31.973 24.738  1.00 65.60  ? 276  ARG A NE  1 
ATOM   2084  C  CZ  . ARG A  1 276 ? -37.225 -32.684 25.137  1.00 72.70  ? 276  ARG A CZ  1 
ATOM   2085  N  NH1 . ARG A  1 276 ? -37.309 -33.984 24.874  1.00 74.44  ? 276  ARG A NH1 1 
ATOM   2086  N  NH2 . ARG A  1 276 ? -38.216 -32.092 25.799  1.00 75.00  ? 276  ARG A NH2 1 
ATOM   2087  N  N   . PRO A  1 277 ? -31.790 -35.512 21.731  1.00 40.36  ? 277  PRO A N   1 
ATOM   2088  C  CA  . PRO A  1 277 ? -30.724 -35.955 20.818  1.00 40.49  ? 277  PRO A CA  1 
ATOM   2089  C  C   . PRO A  1 277 ? -29.450 -35.161 21.047  1.00 44.63  ? 277  PRO A C   1 
ATOM   2090  O  O   . PRO A  1 277 ? -29.544 -33.950 21.247  1.00 48.86  ? 277  PRO A O   1 
ATOM   2091  C  CB  . PRO A  1 277 ? -31.263 -35.587 19.438  1.00 36.08  ? 277  PRO A CB  1 
ATOM   2092  C  CG  . PRO A  1 277 ? -32.708 -35.342 19.619  1.00 37.78  ? 277  PRO A CG  1 
ATOM   2093  C  CD  . PRO A  1 277 ? -32.900 -34.872 21.009  1.00 37.21  ? 277  PRO A CD  1 
ATOM   2094  N  N   . ALA A  1 278 ? -28.294 -35.816 20.989  1.00 44.36  ? 278  ALA A N   1 
ATOM   2095  C  CA  . ALA A  1 278 ? -27.022 -35.191 21.355  1.00 39.44  ? 278  ALA A CA  1 
ATOM   2096  C  C   . ALA A  1 278 ? -26.801 -33.843 20.683  1.00 39.24  ? 278  ALA A C   1 
ATOM   2097  O  O   . ALA A  1 278 ? -26.460 -32.840 21.332  1.00 40.85  ? 278  ALA A O   1 
ATOM   2098  C  CB  . ALA A  1 278 ? -25.884 -36.118 21.030  1.00 30.06  ? 278  ALA A CB  1 
ATOM   2099  N  N   . GLN A  1 279 ? -27.021 -33.816 19.378  1.00 33.51  ? 279  GLN A N   1 
ATOM   2100  C  CA  . GLN A  1 279 ? -26.799 -32.600 18.618  1.00 34.95  ? 279  GLN A CA  1 
ATOM   2101  C  C   . GLN A  1 279 ? -27.610 -31.380 19.093  1.00 37.27  ? 279  GLN A C   1 
ATOM   2102  O  O   . GLN A  1 279 ? -27.171 -30.263 18.875  1.00 39.94  ? 279  GLN A O   1 
ATOM   2103  C  CB  . GLN A  1 279 ? -26.988 -32.848 17.121  1.00 40.64  ? 279  GLN A CB  1 
ATOM   2104  C  CG  . GLN A  1 279 ? -26.504 -31.716 16.235  1.00 44.34  ? 279  GLN A CG  1 
ATOM   2105  C  CD  . GLN A  1 279 ? -25.002 -31.533 16.286  1.00 49.39  ? 279  GLN A CD  1 
ATOM   2106  O  OE1 . GLN A  1 279 ? -24.236 -32.504 16.207  1.00 50.20  ? 279  GLN A OE1 1 
ATOM   2107  N  NE2 . GLN A  1 279 ? -24.565 -30.280 16.421  1.00 51.91  ? 279  GLN A NE2 1 
ATOM   2108  N  N   . ASP A  1 280 ? -28.761 -31.575 19.747  1.00 36.62  ? 280  ASP A N   1 
ATOM   2109  C  CA  . ASP A  1 280 ? -29.538 -30.438 20.280  1.00 41.28  ? 280  ASP A CA  1 
ATOM   2110  C  C   . ASP A  1 280 ? -28.817 -29.760 21.444  1.00 33.78  ? 280  ASP A C   1 
ATOM   2111  O  O   . ASP A  1 280 ? -28.756 -28.518 21.551  1.00 32.10  ? 280  ASP A O   1 
ATOM   2112  C  CB  . ASP A  1 280 ? -30.930 -30.876 20.729  1.00 71.00  ? 280  ASP A CB  1 
ATOM   2113  C  CG  . ASP A  1 280 ? -31.882 -31.048 19.571  1.00 86.48  ? 280  ASP A CG  1 
ATOM   2114  O  OD1 . ASP A  1 280 ? -31.567 -30.558 18.461  1.00 91.94  ? 280  ASP A OD1 1 
ATOM   2115  O  OD2 . ASP A  1 280 ? -32.950 -31.666 19.773  1.00 91.64  ? 280  ASP A OD2 1 
ATOM   2116  N  N   . LEU A  1 281 ? -28.273 -30.600 22.315  1.00 30.98  ? 281  LEU A N   1 
ATOM   2117  C  CA  . LEU A  1 281 ? -27.441 -30.155 23.408  1.00 29.61  ? 281  LEU A CA  1 
ATOM   2118  C  C   . LEU A  1 281 ? -26.236 -29.413 22.863  1.00 28.69  ? 281  LEU A C   1 
ATOM   2119  O  O   . LEU A  1 281 ? -25.855 -28.360 23.374  1.00 28.21  ? 281  LEU A O   1 
ATOM   2120  C  CB  . LEU A  1 281 ? -26.977 -31.355 24.206  1.00 28.72  ? 281  LEU A CB  1 
ATOM   2121  C  CG  . LEU A  1 281 ? -27.811 -31.635 25.434  1.00 29.13  ? 281  LEU A CG  1 
ATOM   2122  C  CD1 . LEU A  1 281 ? -29.245 -31.859 25.056  1.00 30.84  ? 281  LEU A CD1 1 
ATOM   2123  C  CD2 . LEU A  1 281 ? -27.233 -32.847 26.099  1.00 33.72  ? 281  LEU A CD2 1 
ATOM   2124  N  N   . VAL A  1 282 ? -25.631 -29.965 21.817  1.00 32.40  ? 282  VAL A N   1 
ATOM   2125  C  CA  . VAL A  1 282 ? -24.471 -29.306 21.223  1.00 31.94  ? 282  VAL A CA  1 
ATOM   2126  C  C   . VAL A  1 282 ? -24.836 -27.943 20.643  1.00 33.04  ? 282  VAL A C   1 
ATOM   2127  O  O   . VAL A  1 282 ? -24.094 -26.973 20.818  1.00 34.01  ? 282  VAL A O   1 
ATOM   2128  C  CB  . VAL A  1 282 ? -23.810 -30.168 20.152  1.00 27.68  ? 282  VAL A CB  1 
ATOM   2129  C  CG1 . VAL A  1 282 ? -22.831 -29.352 19.366  1.00 28.58  ? 282  VAL A CG1 1 
ATOM   2130  C  CG2 . VAL A  1 282 ? -23.108 -31.341 20.795  1.00 26.62  ? 282  VAL A CG2 1 
ATOM   2131  N  N   . ASP A  1 283 ? -25.990 -27.871 19.976  1.00 31.35  ? 283  ASP A N   1 
ATOM   2132  C  CA  . ASP A  1 283 ? -26.497 -26.622 19.400  1.00 34.34  ? 283  ASP A CA  1 
ATOM   2133  C  C   . ASP A  1 283 ? -26.751 -25.572 20.465  1.00 32.80  ? 283  ASP A C   1 
ATOM   2134  O  O   . ASP A  1 283 ? -26.647 -24.383 20.195  1.00 34.21  ? 283  ASP A O   1 
ATOM   2135  C  CB  . ASP A  1 283 ? -27.797 -26.838 18.613  1.00 47.51  ? 283  ASP A CB  1 
ATOM   2136  C  CG  . ASP A  1 283 ? -27.628 -27.779 17.425  1.00 52.91  ? 283  ASP A CG  1 
ATOM   2137  O  OD1 . ASP A  1 283 ? -26.487 -27.930 16.914  1.00 53.34  ? 283  ASP A OD1 1 
ATOM   2138  O  OD2 . ASP A  1 283 ? -28.657 -28.369 17.007  1.00 53.91  ? 283  ASP A OD2 1 
ATOM   2139  N  N   . HIS A  1 284 ? -27.110 -25.995 21.670  1.00 30.71  ? 284  HIS A N   1 
ATOM   2140  C  CA  . HIS A  1 284 ? -27.391 -24.997 22.702  1.00 30.71  ? 284  HIS A CA  1 
ATOM   2141  C  C   . HIS A  1 284 ? -26.314 -24.654 23.721  1.00 29.23  ? 284  HIS A C   1 
ATOM   2142  O  O   . HIS A  1 284 ? -26.508 -23.750 24.523  1.00 29.32  ? 284  HIS A O   1 
ATOM   2143  C  CB  . HIS A  1 284 ? -28.686 -25.338 23.414  1.00 42.60  ? 284  HIS A CB  1 
ATOM   2144  C  CG  . HIS A  1 284 ? -29.872 -25.183 22.536  1.00 47.99  ? 284  HIS A CG  1 
ATOM   2145  N  ND1 . HIS A  1 284 ? -29.934 -25.749 21.284  1.00 49.93  ? 284  HIS A ND1 1 
ATOM   2146  C  CD2 . HIS A  1 284 ? -31.018 -24.485 22.697  1.00 53.92  ? 284  HIS A CD2 1 
ATOM   2147  C  CE1 . HIS A  1 284 ? -31.082 -25.428 20.717  1.00 56.14  ? 284  HIS A CE1 1 
ATOM   2148  N  NE2 . HIS A  1 284 ? -31.758 -24.661 21.553  1.00 58.49  ? 284  HIS A NE2 1 
ATOM   2149  N  N   . GLU A  1 285 ? -25.179 -25.332 23.695  1.00 36.56  ? 285  GLU A N   1 
ATOM   2150  C  CA  . GLU A  1 285 ? -24.268 -25.198 24.824  1.00 38.31  ? 285  GLU A CA  1 
ATOM   2151  C  C   . GLU A  1 285 ? -23.658 -23.806 24.969  1.00 35.84  ? 285  GLU A C   1 
ATOM   2152  O  O   . GLU A  1 285 ? -23.181 -23.429 26.032  1.00 34.20  ? 285  GLU A O   1 
ATOM   2153  C  CB  . GLU A  1 285 ? -23.202 -26.290 24.811  1.00 46.90  ? 285  GLU A CB  1 
ATOM   2154  C  CG  . GLU A  1 285 ? -22.158 -26.177 23.752  1.00 52.46  ? 285  GLU A CG  1 
ATOM   2155  C  CD  . GLU A  1 285 ? -21.082 -27.207 23.976  1.00 60.94  ? 285  GLU A CD  1 
ATOM   2156  O  OE1 . GLU A  1 285 ? -21.365 -28.207 24.669  1.00 62.66  ? 285  GLU A OE1 1 
ATOM   2157  O  OE2 . GLU A  1 285 ? -19.953 -27.020 23.483  1.00 65.72  ? 285  GLU A OE2 1 
ATOM   2158  N  N   . TRP A  1 286 ? -23.718 -23.028 23.905  1.00 29.11  ? 286  TRP A N   1 
ATOM   2159  C  CA  . TRP A  1 286 ? -23.105 -21.716 23.915  1.00 35.83  ? 286  TRP A CA  1 
ATOM   2160  C  C   . TRP A  1 286 ? -23.984 -20.587 24.466  1.00 36.80  ? 286  TRP A C   1 
ATOM   2161  O  O   . TRP A  1 286 ? -23.478 -19.515 24.815  1.00 27.88  ? 286  TRP A O   1 
ATOM   2162  C  CB  . TRP A  1 286 ? -22.638 -21.407 22.504  1.00 70.64  ? 286  TRP A CB  1 
ATOM   2163  C  CG  . TRP A  1 286 ? -21.476 -22.245 22.142  1.00 79.37  ? 286  TRP A CG  1 
ATOM   2164  C  CD1 . TRP A  1 286 ? -21.494 -23.480 21.563  1.00 81.05  ? 286  TRP A CD1 1 
ATOM   2165  C  CD2 . TRP A  1 286 ? -20.108 -21.924 22.371  1.00 83.01  ? 286  TRP A CD2 1 
ATOM   2166  N  NE1 . TRP A  1 286 ? -20.213 -23.941 21.401  1.00 81.01  ? 286  TRP A NE1 1 
ATOM   2167  C  CE2 . TRP A  1 286 ? -19.343 -23.002 21.889  1.00 83.76  ? 286  TRP A CE2 1 
ATOM   2168  C  CE3 . TRP A  1 286 ? -19.454 -20.821 22.930  1.00 85.52  ? 286  TRP A CE3 1 
ATOM   2169  C  CZ2 . TRP A  1 286 ? -17.955 -23.012 21.950  1.00 87.50  ? 286  TRP A CZ2 1 
ATOM   2170  C  CZ3 . TRP A  1 286 ? -18.080 -20.828 22.990  1.00 88.36  ? 286  TRP A CZ3 1 
ATOM   2171  C  CH2 . TRP A  1 286 ? -17.342 -21.918 22.504  1.00 89.68  ? 286  TRP A CH2 1 
ATOM   2172  N  N   . HIS A  1 287 ? -25.291 -20.842 24.565  1.00 49.46  ? 287  HIS A N   1 
ATOM   2173  C  CA  . HIS A  1 287 ? -26.268 -19.820 24.942  1.00 45.45  ? 287  HIS A CA  1 
ATOM   2174  C  C   . HIS A  1 287 ? -26.319 -19.617 26.438  1.00 44.83  ? 287  HIS A C   1 
ATOM   2175  O  O   . HIS A  1 287 ? -26.877 -18.646 26.925  1.00 48.92  ? 287  HIS A O   1 
ATOM   2176  C  CB  . HIS A  1 287 ? -27.663 -20.213 24.489  1.00 42.97  ? 287  HIS A CB  1 
ATOM   2177  C  CG  . HIS A  1 287 ? -27.739 -20.676 23.070  1.00 45.38  ? 287  HIS A CG  1 
ATOM   2178  N  ND1 . HIS A  1 287 ? -28.873 -21.263 22.548  1.00 45.49  ? 287  HIS A ND1 1 
ATOM   2179  C  CD2 . HIS A  1 287 ? -26.836 -20.636 22.065  1.00 47.58  ? 287  HIS A CD2 1 
ATOM   2180  C  CE1 . HIS A  1 287 ? -28.660 -21.572 21.281  1.00 47.66  ? 287  HIS A CE1 1 
ATOM   2181  N  NE2 . HIS A  1 287 ? -27.429 -21.201 20.965  1.00 48.87  ? 287  HIS A NE2 1 
ATOM   2182  N  N   . VAL A  1 288 ? -25.737 -20.541 27.178  1.00 42.84  ? 288  VAL A N   1 
ATOM   2183  C  CA  . VAL A  1 288 ? -25.779 -20.452 28.622  1.00 43.41  ? 288  VAL A CA  1 
ATOM   2184  C  C   . VAL A  1 288 ? -24.770 -19.467 29.254  1.00 45.81  ? 288  VAL A C   1 
ATOM   2185  O  O   . VAL A  1 288 ? -24.957 -19.066 30.403  1.00 52.29  ? 288  VAL A O   1 
ATOM   2186  C  CB  . VAL A  1 288 ? -25.641 -21.840 29.245  1.00 33.10  ? 288  VAL A CB  1 
ATOM   2187  C  CG1 . VAL A  1 288 ? -26.680 -22.770 28.653  1.00 28.41  ? 288  VAL A CG1 1 
ATOM   2188  C  CG2 . VAL A  1 288 ? -24.242 -22.381 29.003  1.00 30.06  ? 288  VAL A CG2 1 
ATOM   2189  N  N   . LEU A  1 289 ? -23.726 -19.075 28.515  1.00 37.20  ? 289  LEU A N   1 
ATOM   2190  C  CA  . LEU A  1 289 ? -22.707 -18.119 29.000  1.00 32.49  ? 289  LEU A CA  1 
ATOM   2191  C  C   . LEU A  1 289 ? -23.260 -16.790 29.510  1.00 35.61  ? 289  LEU A C   1 
ATOM   2192  O  O   . LEU A  1 289 ? -24.167 -16.216 28.896  1.00 38.84  ? 289  LEU A O   1 
ATOM   2193  C  CB  . LEU A  1 289 ? -21.695 -17.805 27.906  1.00 29.59  ? 289  LEU A CB  1 
ATOM   2194  C  CG  . LEU A  1 289 ? -20.481 -18.718 27.843  1.00 28.17  ? 289  LEU A CG  1 
ATOM   2195  C  CD1 . LEU A  1 289 ? -19.654 -18.415 26.594  1.00 31.45  ? 289  LEU A CD1 1 
ATOM   2196  C  CD2 . LEU A  1 289 ? -19.666 -18.542 29.087  1.00 24.80  ? 289  LEU A CD2 1 
ATOM   2197  N  N   . PRO A  1 290 ? -22.712 -16.303 30.641  1.00 27.02  ? 290  PRO A N   1 
ATOM   2198  C  CA  . PRO A  1 290 ? -23.108 -15.083 31.350  1.00 27.87  ? 290  PRO A CA  1 
ATOM   2199  C  C   . PRO A  1 290 ? -22.913 -13.821 30.556  1.00 30.18  ? 290  PRO A C   1 
ATOM   2200  O  O   . PRO A  1 290 ? -23.853 -13.030 30.512  1.00 29.82  ? 290  PRO A O   1 
ATOM   2201  C  CB  . PRO A  1 290 ? -22.145 -15.046 32.526  1.00 26.97  ? 290  PRO A CB  1 
ATOM   2202  C  CG  . PRO A  1 290 ? -21.815 -16.440 32.765  1.00 30.94  ? 290  PRO A CG  1 
ATOM   2203  C  CD  . PRO A  1 290 ? -21.713 -17.053 31.409  1.00 25.74  ? 290  PRO A CD  1 
ATOM   2204  N  N   . GLN A  1 291 ? -21.733 -13.652 29.948  1.00 50.69  ? 291  GLN A N   1 
ATOM   2205  C  CA  . GLN A  1 291 ? -21.360 -12.409 29.263  1.00 53.62  ? 291  GLN A CA  1 
ATOM   2206  C  C   . GLN A  1 291 ? -20.835 -12.565 27.841  1.00 54.99  ? 291  GLN A C   1 
ATOM   2207  O  O   . GLN A  1 291 ? -20.391 -13.641 27.421  1.00 55.05  ? 291  GLN A O   1 
ATOM   2208  C  CB  . GLN A  1 291 ? -20.284 -11.659 30.044  1.00 52.46  ? 291  GLN A CB  1 
ATOM   2209  C  CG  . GLN A  1 291 ? -20.668 -11.263 31.435  1.00 53.74  ? 291  GLN A CG  1 
ATOM   2210  C  CD  . GLN A  1 291 ? -20.048 -12.172 32.453  1.00 53.14  ? 291  GLN A CD  1 
ATOM   2211  O  OE1 . GLN A  1 291 ? -19.145 -12.952 32.134  1.00 53.38  ? 291  GLN A OE1 1 
ATOM   2212  N  NE2 . GLN A  1 291 ? -20.520 -12.081 33.691  1.00 53.74  ? 291  GLN A NE2 1 
ATOM   2213  N  N   . GLU A  1 292 ? -20.858 -11.445 27.126  1.00 46.75  ? 292  GLU A N   1 
ATOM   2214  C  CA  . GLU A  1 292 ? -20.188 -11.325 25.852  1.00 44.75  ? 292  GLU A CA  1 
ATOM   2215  C  C   . GLU A  1 292 ? -18.736 -11.398 26.258  1.00 40.61  ? 292  GLU A C   1 
ATOM   2216  O  O   . GLU A  1 292 ? -18.244 -10.554 27.014  1.00 38.76  ? 292  GLU A O   1 
ATOM   2217  C  CB  . GLU A  1 292 ? -20.514 -9.946  25.284  1.00 64.70  ? 292  GLU A CB  1 
ATOM   2218  C  CG  . GLU A  1 292 ? -19.740 -9.481  24.072  1.00 70.01  ? 292  GLU A CG  1 
ATOM   2219  C  CD  . GLU A  1 292 ? -20.198 -8.094  23.613  1.00 77.43  ? 292  GLU A CD  1 
ATOM   2220  O  OE1 . GLU A  1 292 ? -20.858 -7.374  24.405  1.00 76.88  ? 292  GLU A OE1 1 
ATOM   2221  O  OE2 . GLU A  1 292 ? -19.908 -7.727  22.455  1.00 82.74  ? 292  GLU A OE2 1 
ATOM   2222  N  N   . SER A  1 293 ? -18.047 -12.420 25.761  1.00 38.36  ? 293  SER A N   1 
ATOM   2223  C  CA  . SER A  1 293 ? -16.716 -12.737 26.248  1.00 32.87  ? 293  SER A CA  1 
ATOM   2224  C  C   . SER A  1 293 ? -15.972 -13.628 25.277  1.00 28.05  ? 293  SER A C   1 
ATOM   2225  O  O   . SER A  1 293 ? -16.578 -14.271 24.429  1.00 25.86  ? 293  SER A O   1 
ATOM   2226  C  CB  . SER A  1 293 ? -16.841 -13.482 27.562  1.00 33.68  ? 293  SER A CB  1 
ATOM   2227  O  OG  . SER A  1 293 ? -17.413 -14.752 27.310  1.00 34.49  ? 293  SER A OG  1 
ATOM   2228  N  N   . ILE A  1 294 ? -14.653 -13.677 25.435  1.00 24.84  ? 294  ILE A N   1 
ATOM   2229  C  CA  . ILE A  1 294 ? -13.821 -14.675 24.777  1.00 24.10  ? 294  ILE A CA  1 
ATOM   2230  C  C   . ILE A  1 294 ? -12.938 -15.410 25.781  1.00 22.92  ? 294  ILE A C   1 
ATOM   2231  O  O   . ILE A  1 294 ? -12.630 -14.903 26.862  1.00 22.73  ? 294  ILE A O   1 
ATOM   2232  C  CB  . ILE A  1 294 ? -12.930 -14.049 23.700  1.00 24.57  ? 294  ILE A CB  1 
ATOM   2233  C  CG1 . ILE A  1 294 ? -12.125 -12.887 24.267  1.00 24.76  ? 294  ILE A CG1 1 
ATOM   2234  C  CG2 . ILE A  1 294 ? -13.762 -13.557 22.552  1.00 25.77  ? 294  ILE A CG2 1 
ATOM   2235  C  CD1 . ILE A  1 294 ? -11.029 -12.445 23.345  1.00 30.52  ? 294  ILE A CD1 1 
ATOM   2236  N  N   . PHE A  1 295 ? -12.535 -16.614 25.395  1.00 46.36  ? 295  PHE A N   1 
ATOM   2237  C  CA  . PHE A  1 295 ? -11.662 -17.456 26.207  1.00 45.79  ? 295  PHE A CA  1 
ATOM   2238  C  C   . PHE A  1 295 ? -12.400 -17.803 27.491  1.00 46.40  ? 295  PHE A C   1 
ATOM   2239  O  O   . PHE A  1 295 ? -11.809 -17.936 28.558  1.00 45.40  ? 295  PHE A O   1 
ATOM   2240  C  CB  . PHE A  1 295 ? -10.322 -16.767 26.472  1.00 21.03  ? 295  PHE A CB  1 
ATOM   2241  C  CG  . PHE A  1 295 ? -9.149  -17.703 26.565  1.00 20.20  ? 295  PHE A CG  1 
ATOM   2242  C  CD1 . PHE A  1 295 ? -9.299  -18.990 27.019  1.00 19.47  ? 295  PHE A CD1 1 
ATOM   2243  C  CD2 . PHE A  1 295 ? -7.875  -17.274 26.213  1.00 20.25  ? 295  PHE A CD2 1 
ATOM   2244  C  CE1 . PHE A  1 295 ? -8.189  -19.840 27.116  1.00 65.23  ? 295  PHE A CE1 1 
ATOM   2245  C  CE2 . PHE A  1 295 ? -6.766  -18.113 26.312  1.00 19.60  ? 295  PHE A CE2 1 
ATOM   2246  C  CZ  . PHE A  1 295 ? -6.919  -19.390 26.755  1.00 18.88  ? 295  PHE A CZ  1 
ATOM   2247  N  N   . ARG A  1 296 ? -13.715 -17.937 27.353  1.00 37.89  ? 296  ARG A N   1 
ATOM   2248  C  CA  . ARG A  1 296 ? -14.588 -18.424 28.408  1.00 38.03  ? 296  ARG A CA  1 
ATOM   2249  C  C   . ARG A  1 296 ? -15.472 -19.522 27.822  1.00 40.41  ? 296  ARG A C   1 
ATOM   2250  O  O   . ARG A  1 296 ? -16.150 -19.314 26.808  1.00 39.93  ? 296  ARG A O   1 
ATOM   2251  C  CB  . ARG A  1 296 ? -15.464 -17.299 28.969  1.00 25.71  ? 296  ARG A CB  1 
ATOM   2252  C  CG  . ARG A  1 296 ? -14.711 -16.205 29.660  1.00 22.16  ? 296  ARG A CG  1 
ATOM   2253  C  CD  . ARG A  1 296 ? -14.010 -16.712 30.862  1.00 21.37  ? 296  ARG A CD  1 
ATOM   2254  N  NE  . ARG A  1 296 ? -13.335 -15.622 31.551  1.00 28.31  ? 296  ARG A NE  1 
ATOM   2255  C  CZ  . ARG A  1 296 ? -12.057 -15.289 31.356  1.00 25.94  ? 296  ARG A CZ  1 
ATOM   2256  N  NH1 . ARG A  1 296 ? -11.321 -15.980 30.493  1.00 24.36  ? 296  ARG A NH1 1 
ATOM   2257  N  NH2 . ARG A  1 296 ? -11.504 -14.268 32.020  1.00 25.20  ? 296  ARG A NH2 1 
ATOM   2258  N  N   . PHE A  1 297 ? -15.471 -20.682 28.473  1.00 44.44  ? 297  PHE A N   1 
ATOM   2259  C  CA  . PHE A  1 297 ? -16.184 -21.843 27.960  1.00 42.50  ? 297  PHE A CA  1 
ATOM   2260  C  C   . PHE A  1 297 ? -17.348 -22.269 28.866  1.00 35.42  ? 297  PHE A C   1 
ATOM   2261  O  O   . PHE A  1 297 ? -17.297 -22.080 30.084  1.00 32.94  ? 297  PHE A O   1 
ATOM   2262  C  CB  . PHE A  1 297 ? -15.194 -22.976 27.732  1.00 44.61  ? 297  PHE A CB  1 
ATOM   2263  C  CG  . PHE A  1 297 ? -13.903 -22.528 27.090  1.00 47.14  ? 297  PHE A CG  1 
ATOM   2264  C  CD1 . PHE A  1 297 ? -13.821 -22.330 25.725  1.00 50.34  ? 297  PHE A CD1 1 
ATOM   2265  C  CD2 . PHE A  1 297 ? -12.770 -22.306 27.856  1.00 47.74  ? 297  PHE A CD2 1 
ATOM   2266  C  CE1 . PHE A  1 297 ? -12.627 -21.924 25.134  1.00 51.51  ? 297  PHE A CE1 1 
ATOM   2267  C  CE2 . PHE A  1 297 ? -11.569 -21.904 27.271  1.00 49.24  ? 297  PHE A CE2 1 
ATOM   2268  C  CZ  . PHE A  1 297 ? -11.500 -21.715 25.911  1.00 50.89  ? 297  PHE A CZ  1 
ATOM   2269  N  N   . SER A  1 298 ? -18.399 -22.822 28.258  1.00 21.72  ? 298  SER A N   1 
ATOM   2270  C  CA  . SER A  1 298 ? -19.667 -23.060 28.955  1.00 22.33  ? 298  SER A CA  1 
ATOM   2271  C  C   . SER A  1 298 ? -19.628 -24.178 29.972  1.00 21.78  ? 298  SER A C   1 
ATOM   2272  O  O   . SER A  1 298 ? -19.961 -23.970 31.135  1.00 23.77  ? 298  SER A O   1 
ATOM   2273  C  CB  . SER A  1 298 ? -20.798 -23.347 27.969  1.00 32.82  ? 298  SER A CB  1 
ATOM   2274  O  OG  . SER A  1 298 ? -21.393 -22.161 27.472  1.00 38.47  ? 298  SER A OG  1 
ATOM   2275  N  N   . PHE A  1 299 ? -19.225 -25.366 29.539  1.00 21.29  ? 299  PHE A N   1 
ATOM   2276  C  CA  . PHE A  1 299 ? -19.123 -26.489 30.455  1.00 20.82  ? 299  PHE A CA  1 
ATOM   2277  C  C   . PHE A  1 299 ? -17.681 -26.967 30.664  1.00 20.12  ? 299  PHE A C   1 
ATOM   2278  O  O   . PHE A  1 299 ? -17.040 -27.487 29.761  1.00 19.43  ? 299  PHE A O   1 
ATOM   2279  C  CB  . PHE A  1 299 ? -20.044 -27.586 30.003  1.00 21.35  ? 299  PHE A CB  1 
ATOM   2280  C  CG  . PHE A  1 299 ? -21.458 -27.136 29.889  1.00 22.50  ? 299  PHE A CG  1 
ATOM   2281  C  CD1 . PHE A  1 299 ? -21.938 -26.563 28.708  1.00 23.22  ? 299  PHE A CD1 1 
ATOM   2282  C  CD2 . PHE A  1 299 ? -22.325 -27.253 30.966  1.00 39.64  ? 299  PHE A CD2 1 
ATOM   2283  C  CE1 . PHE A  1 299 ? -23.279 -26.133 28.587  1.00 24.45  ? 299  PHE A CE1 1 
ATOM   2284  C  CE2 . PHE A  1 299 ? -23.668 -26.827 30.854  1.00 38.62  ? 299  PHE A CE2 1 
ATOM   2285  C  CZ  . PHE A  1 299 ? -24.134 -26.268 29.655  1.00 24.94  ? 299  PHE A CZ  1 
ATOM   2286  N  N   . VAL A  1 300 ? -17.174 -26.746 31.870  1.00 19.36  ? 300  VAL A N   1 
ATOM   2287  C  CA  . VAL A  1 300 ? -15.797 -27.041 32.187  1.00 18.51  ? 300  VAL A CA  1 
ATOM   2288  C  C   . VAL A  1 300 ? -15.788 -27.760 33.543  1.00 18.32  ? 300  VAL A C   1 
ATOM   2289  O  O   . VAL A  1 300 ? -16.864 -27.907 34.153  1.00 18.90  ? 300  VAL A O   1 
ATOM   2290  C  CB  . VAL A  1 300 ? -14.933 -25.734 32.241  1.00 29.15  ? 300  VAL A CB  1 
ATOM   2291  C  CG1 . VAL A  1 300 ? -15.051 -24.925 30.961  1.00 31.43  ? 300  VAL A CG1 1 
ATOM   2292  C  CG2 . VAL A  1 300 ? -15.292 -24.905 33.444  1.00 28.04  ? 300  VAL A CG2 1 
ATOM   2293  N  N   . PRO A  1 301 ? -14.588 -28.218 34.015  1.00 39.67  ? 301  PRO A N   1 
ATOM   2294  C  CA  . PRO A  1 301 ? -14.525 -28.867 35.326  1.00 35.31  ? 301  PRO A CA  1 
ATOM   2295  C  C   . PRO A  1 301 ? -15.146 -28.003 36.380  1.00 36.82  ? 301  PRO A C   1 
ATOM   2296  O  O   . PRO A  1 301 ? -14.897 -26.805 36.394  1.00 40.93  ? 301  PRO A O   1 
ATOM   2297  C  CB  . PRO A  1 301 ? -13.036 -28.973 35.577  1.00 18.55  ? 301  PRO A CB  1 
ATOM   2298  C  CG  . PRO A  1 301 ? -12.481 -29.187 34.244  1.00 19.49  ? 301  PRO A CG  1 
ATOM   2299  C  CD  . PRO A  1 301 ? -13.299 -28.368 33.305  1.00 22.70  ? 301  PRO A CD  1 
ATOM   2300  N  N   . VAL A  1 302 ? -15.953 -28.612 37.238  1.00 25.19  ? 302  VAL A N   1 
ATOM   2301  C  CA  . VAL A  1 302 ? -16.633 -27.904 38.309  1.00 24.78  ? 302  VAL A CA  1 
ATOM   2302  C  C   . VAL A  1 302 ? -15.868 -28.136 39.610  1.00 25.63  ? 302  VAL A C   1 
ATOM   2303  O  O   . VAL A  1 302 ? -15.230 -29.173 39.773  1.00 24.29  ? 302  VAL A O   1 
ATOM   2304  C  CB  . VAL A  1 302 ? -18.076 -28.403 38.452  1.00 19.95  ? 302  VAL A CB  1 
ATOM   2305  C  CG1 . VAL A  1 302 ? -18.096 -29.846 38.919  1.00 19.93  ? 302  VAL A CG1 1 
ATOM   2306  C  CG2 . VAL A  1 302 ? -18.871 -27.491 39.389  1.00 20.75  ? 302  VAL A CG2 1 
ATOM   2307  N  N   . VAL A  1 303 ? -15.882 -27.171 40.525  1.00 29.80  ? 303  VAL A N   1 
ATOM   2308  C  CA  . VAL A  1 303 ? -15.252 -27.437 41.807  1.00 32.95  ? 303  VAL A CA  1 
ATOM   2309  C  C   . VAL A  1 303 ? -16.326 -28.012 42.737  1.00 40.64  ? 303  VAL A C   1 
ATOM   2310  O  O   . VAL A  1 303 ? -17.116 -27.291 43.350  1.00 44.35  ? 303  VAL A O   1 
ATOM   2311  C  CB  . VAL A  1 303 ? -14.678 -26.141 42.391  1.00 20.77  ? 303  VAL A CB  1 
ATOM   2312  C  CG1 . VAL A  1 303 ? -14.000 -26.397 43.719  1.00 21.02  ? 303  VAL A CG1 1 
ATOM   2313  C  CG2 . VAL A  1 303 ? -13.699 -25.520 41.413  1.00 18.81  ? 303  VAL A CG2 1 
ATOM   2314  N  N   . ASP A  1 304 ? -16.283 -29.335 42.865  1.00 33.09  ? 304  ASP A N   1 
ATOM   2315  C  CA  . ASP A  1 304 ? -17.330 -30.130 43.497  1.00 36.63  ? 304  ASP A CA  1 
ATOM   2316  C  C   . ASP A  1 304 ? -17.005 -30.565 44.932  1.00 38.78  ? 304  ASP A C   1 
ATOM   2317  O  O   . ASP A  1 304 ? -17.796 -31.256 45.584  1.00 37.21  ? 304  ASP A O   1 
ATOM   2318  C  CB  . ASP A  1 304 ? -17.678 -31.349 42.607  1.00 47.57  ? 304  ASP A CB  1 
ATOM   2319  C  CG  . ASP A  1 304 ? -16.434 -32.167 42.153  1.00 52.97  ? 304  ASP A CG  1 
ATOM   2320  O  OD1 . ASP A  1 304 ? -15.276 -31.695 42.299  1.00 49.74  ? 304  ASP A OD1 1 
ATOM   2321  O  OD2 . ASP A  1 304 ? -16.634 -33.292 41.624  1.00 52.54  ? 304  ASP A OD2 1 
ATOM   2322  N  N   . GLY A  1 305 ? -15.820 -30.192 45.405  1.00 60.33  ? 305  GLY A N   1 
ATOM   2323  C  CA  . GLY A  1 305 ? -15.307 -30.728 46.651  1.00 64.88  ? 305  GLY A CA  1 
ATOM   2324  C  C   . GLY A  1 305 ? -15.016 -32.220 46.579  1.00 67.12  ? 305  GLY A C   1 
ATOM   2325  O  O   . GLY A  1 305 ? -14.762 -32.859 47.598  1.00 72.84  ? 305  GLY A O   1 
ATOM   2326  N  N   . ASP A  1 306 ? -15.045 -32.782 45.375  1.00 54.18  ? 306  ASP A N   1 
ATOM   2327  C  CA  . ASP A  1 306 ? -14.808 -34.212 45.190  1.00 51.85  ? 306  ASP A CA  1 
ATOM   2328  C  C   . ASP A  1 306 ? -13.559 -34.467 44.344  1.00 49.52  ? 306  ASP A C   1 
ATOM   2329  O  O   . ASP A  1 306 ? -12.524 -34.866 44.887  1.00 51.91  ? 306  ASP A O   1 
ATOM   2330  C  CB  . ASP A  1 306 ? -16.042 -34.890 44.573  1.00 50.79  ? 306  ASP A CB  1 
ATOM   2331  C  CG  . ASP A  1 306 ? -15.901 -36.411 44.458  1.00 50.01  ? 306  ASP A CG  1 
ATOM   2332  O  OD1 . ASP A  1 306 ? -14.999 -36.999 45.090  1.00 50.75  ? 306  ASP A OD1 1 
ATOM   2333  O  OD2 . ASP A  1 306 ? -16.712 -37.026 43.736  1.00 49.30  ? 306  ASP A OD2 1 
ATOM   2334  N  N   . PHE A  1 307 ? -13.648 -34.247 43.027  1.00 37.75  ? 307  PHE A N   1 
ATOM   2335  C  CA  . PHE A  1 307 ? -12.478 -34.409 42.163  1.00 30.47  ? 307  PHE A CA  1 
ATOM   2336  C  C   . PHE A  1 307 ? -11.498 -33.310 42.514  1.00 27.53  ? 307  PHE A C   1 
ATOM   2337  O  O   . PHE A  1 307 ? -10.334 -33.565 42.830  1.00 24.90  ? 307  PHE A O   1 
ATOM   2338  C  CB  . PHE A  1 307 ? -12.840 -34.328 40.675  1.00 29.44  ? 307  PHE A CB  1 
ATOM   2339  C  CG  . PHE A  1 307 ? -11.713 -34.754 39.754  1.00 29.28  ? 307  PHE A CG  1 
ATOM   2340  C  CD1 . PHE A  1 307 ? -10.558 -33.988 39.630  1.00 26.40  ? 307  PHE A CD1 1 
ATOM   2341  C  CD2 . PHE A  1 307 ? -11.807 -35.927 39.018  1.00 29.84  ? 307  PHE A CD2 1 
ATOM   2342  C  CE1 . PHE A  1 307 ? -9.529  -34.382 38.793  1.00 24.63  ? 307  PHE A CE1 1 
ATOM   2343  C  CE2 . PHE A  1 307 ? -10.772 -36.328 38.174  1.00 27.72  ? 307  PHE A CE2 1 
ATOM   2344  C  CZ  . PHE A  1 307 ? -9.634  -35.554 38.065  1.00 25.04  ? 307  PHE A CZ  1 
ATOM   2345  N  N   . LEU A  1 308 ? -11.985 -32.079 42.437  1.00 34.41  ? 308  LEU A N   1 
ATOM   2346  C  CA  . LEU A  1 308 ? -11.257 -30.951 42.969  1.00 35.78  ? 308  LEU A CA  1 
ATOM   2347  C  C   . LEU A  1 308 ? -11.831 -30.767 44.347  1.00 41.23  ? 308  LEU A C   1 
ATOM   2348  O  O   . LEU A  1 308 ? -13.021 -30.494 44.492  1.00 40.85  ? 308  LEU A O   1 
ATOM   2349  C  CB  . LEU A  1 308 ? -11.470 -29.711 42.106  1.00 26.84  ? 308  LEU A CB  1 
ATOM   2350  C  CG  . LEU A  1 308 ? -10.832 -29.850 40.721  1.00 16.94  ? 308  LEU A CG  1 
ATOM   2351  C  CD1 . LEU A  1 308 ? -11.055 -28.629 39.884  1.00 16.91  ? 308  LEU A CD1 1 
ATOM   2352  C  CD2 . LEU A  1 308 ? -9.358  -30.125 40.859  1.00 16.54  ? 308  LEU A CD2 1 
ATOM   2353  N  N   . SER A  1 309 ? -10.994 -30.968 45.360  1.00 50.59  ? 309  SER A N   1 
ATOM   2354  C  CA  . SER A  1 309 ? -11.448 -30.928 46.743  1.00 50.06  ? 309  SER A CA  1 
ATOM   2355  C  C   . SER A  1 309 ? -11.662 -29.486 47.198  1.00 52.17  ? 309  SER A C   1 
ATOM   2356  O  O   . SER A  1 309 ? -12.600 -29.189 47.935  1.00 52.82  ? 309  SER A O   1 
ATOM   2357  C  CB  . SER A  1 309 ? -10.422 -31.597 47.634  1.00 29.16  ? 309  SER A CB  1 
ATOM   2358  O  OG  . SER A  1 309 ? -9.495  -30.630 48.069  1.00 27.61  ? 309  SER A OG  1 
ATOM   2359  N  N   . ASP A  1 310 ? -10.768 -28.602 46.768  1.00 43.71  ? 310  ASP A N   1 
ATOM   2360  C  CA  . ASP A  1 310 ? -10.974 -27.166 46.883  1.00 42.60  ? 310  ASP A CA  1 
ATOM   2361  C  C   . ASP A  1 310 ? -10.696 -26.534 45.516  1.00 40.95  ? 310  ASP A C   1 
ATOM   2362  O  O   . ASP A  1 310 ? -10.483 -27.244 44.540  1.00 43.85  ? 310  ASP A O   1 
ATOM   2363  C  CB  . ASP A  1 310 ? -10.057 -26.573 47.945  1.00 46.71  ? 310  ASP A CB  1 
ATOM   2364  C  CG  . ASP A  1 310 ? -10.597 -25.277 48.514  1.00 51.77  ? 310  ASP A CG  1 
ATOM   2365  O  OD1 . ASP A  1 310 ? -11.569 -24.733 47.941  1.00 54.95  ? 310  ASP A OD1 1 
ATOM   2366  O  OD2 . ASP A  1 310 ? -10.051 -24.802 49.532  1.00 52.40  ? 310  ASP A OD2 1 
ATOM   2367  N  N   . THR A  1 311 ? -10.714 -25.209 45.429  1.00 30.42  ? 311  THR A N   1 
ATOM   2368  C  CA  . THR A  1 311 ? -10.307 -24.541 44.195  1.00 28.05  ? 311  THR A CA  1 
ATOM   2369  C  C   . THR A  1 311 ? -8.820  -24.768 43.927  1.00 25.32  ? 311  THR A C   1 
ATOM   2370  O  O   . THR A  1 311 ? -8.022  -24.842 44.867  1.00 21.00  ? 311  THR A O   1 
ATOM   2371  C  CB  . THR A  1 311 ? -10.572 -23.031 44.251  1.00 34.52  ? 311  THR A CB  1 
ATOM   2372  O  OG1 . THR A  1 311 ? -9.633  -22.403 45.131  1.00 33.95  ? 311  THR A OG1 1 
ATOM   2373  C  CG2 . THR A  1 311 ? -11.963 -22.781 44.762  1.00 37.75  ? 311  THR A CG2 1 
ATOM   2374  N  N   . PRO A  1 312 ? -8.447  -24.890 42.641  1.00 39.73  ? 312  PRO A N   1 
ATOM   2375  C  CA  . PRO A  1 312 ? -7.058  -25.101 42.247  1.00 42.70  ? 312  PRO A CA  1 
ATOM   2376  C  C   . PRO A  1 312 ? -6.151  -24.052 42.857  1.00 50.43  ? 312  PRO A C   1 
ATOM   2377  O  O   . PRO A  1 312 ? -5.025  -24.377 43.207  1.00 54.88  ? 312  PRO A O   1 
ATOM   2378  C  CB  . PRO A  1 312 ? -7.112  -24.954 40.727  1.00 16.86  ? 312  PRO A CB  1 
ATOM   2379  C  CG  . PRO A  1 312 ? -8.443  -25.453 40.376  1.00 16.88  ? 312  PRO A CG  1 
ATOM   2380  C  CD  . PRO A  1 312 ? -9.340  -24.936 41.471  1.00 17.67  ? 312  PRO A CD  1 
ATOM   2381  N  N   . GLU A  1 313 ? -6.640  -22.823 42.981  1.00 43.81  ? 313  GLU A N   1 
ATOM   2382  C  CA  . GLU A  1 313 ? -5.923  -21.781 43.709  1.00 48.06  ? 313  GLU A CA  1 
ATOM   2383  C  C   . GLU A  1 313 ? -5.472  -22.307 45.063  1.00 42.97  ? 313  GLU A C   1 
ATOM   2384  O  O   . GLU A  1 313 ? -4.277  -22.432 45.334  1.00 43.76  ? 313  GLU A O   1 
ATOM   2385  C  CB  . GLU A  1 313 ? -6.834  -20.572 43.921  1.00 87.37  ? 313  GLU A CB  1 
ATOM   2386  C  CG  . GLU A  1 313 ? -7.485  -20.075 42.653  1.00 96.04  ? 313  GLU A CG  1 
ATOM   2387  C  CD  . GLU A  1 313 ? -6.470  -19.507 41.690  1.00 102.15 ? 313  GLU A CD  1 
ATOM   2388  O  OE1 . GLU A  1 313 ? -5.402  -19.061 42.167  1.00 104.33 ? 313  GLU A OE1 1 
ATOM   2389  O  OE2 . GLU A  1 313 ? -6.735  -19.510 40.465  1.00 103.23 ? 313  GLU A OE2 1 
ATOM   2390  N  N   . ALA A  1 314 ? -6.449  -22.626 45.900  1.00 48.91  ? 314  ALA A N   1 
ATOM   2391  C  CA  . ALA A  1 314 ? -6.205  -23.127 47.239  1.00 47.40  ? 314  ALA A CA  1 
ATOM   2392  C  C   . ALA A  1 314 ? -5.264  -24.320 47.205  1.00 47.91  ? 314  ALA A C   1 
ATOM   2393  O  O   . ALA A  1 314 ? -4.324  -24.424 48.004  1.00 52.72  ? 314  ALA A O   1 
ATOM   2394  C  CB  . ALA A  1 314 ? -7.526  -23.520 47.883  1.00 37.54  ? 314  ALA A CB  1 
ATOM   2395  N  N   . LEU A  1 315 ? -5.514  -25.205 46.250  1.00 40.47  ? 315  LEU A N   1 
ATOM   2396  C  CA  . LEU A  1 315 ? -4.843  -26.487 46.218  1.00 32.83  ? 315  LEU A CA  1 
ATOM   2397  C  C   . LEU A  1 315 ? -3.376  -26.357 45.907  1.00 32.80  ? 315  LEU A C   1 
ATOM   2398  O  O   . LEU A  1 315 ? -2.556  -26.983 46.577  1.00 38.22  ? 315  LEU A O   1 
ATOM   2399  C  CB  . LEU A  1 315 ? -5.534  -27.417 45.234  1.00 22.88  ? 315  LEU A CB  1 
ATOM   2400  C  CG  . LEU A  1 315 ? -6.850  -27.863 45.864  1.00 23.62  ? 315  LEU A CG  1 
ATOM   2401  C  CD1 . LEU A  1 315 ? -7.661  -28.758 44.945  1.00 24.70  ? 315  LEU A CD1 1 
ATOM   2402  C  CD2 . LEU A  1 315 ? -6.533  -28.566 47.164  1.00 24.32  ? 315  LEU A CD2 1 
ATOM   2403  N  N   . ILE A  1 316 ? -3.040  -25.546 44.904  1.00 20.92  ? 316  ILE A N   1 
ATOM   2404  C  CA  . ILE A  1 316 ? -1.638  -25.341 44.545  1.00 19.58  ? 316  ILE A CA  1 
ATOM   2405  C  C   . ILE A  1 316 ? -1.004  -24.447 45.579  1.00 20.57  ? 316  ILE A C   1 
ATOM   2406  O  O   . ILE A  1 316 ? 0.208   -24.414 45.718  1.00 21.34  ? 316  ILE A O   1 
ATOM   2407  C  CB  . ILE A  1 316 ? -1.403  -24.716 43.130  1.00 23.92  ? 316  ILE A CB  1 
ATOM   2408  C  CG1 . ILE A  1 316 ? -1.887  -23.270 43.073  1.00 28.27  ? 316  ILE A CG1 1 
ATOM   2409  C  CG2 . ILE A  1 316 ? -2.042  -25.543 42.031  1.00 21.66  ? 316  ILE A CG2 1 
ATOM   2410  C  CD1 . ILE A  1 316 ? -1.720  -22.635 41.709  1.00 29.80  ? 316  ILE A CD1 1 
ATOM   2411  N  N   . ASN A  1 317 ? -1.815  -23.711 46.317  1.00 29.48  ? 317  ASN A N   1 
ATOM   2412  C  CA  . ASN A  1 317 ? -1.222  -22.866 47.334  1.00 38.63  ? 317  ASN A CA  1 
ATOM   2413  C  C   . ASN A  1 317 ? -0.720  -23.675 48.515  1.00 42.76  ? 317  ASN A C   1 
ATOM   2414  O  O   . ASN A  1 317 ? 0.358   -23.416 49.043  1.00 44.51  ? 317  ASN A O   1 
ATOM   2415  C  CB  . ASN A  1 317 ? -2.179  -21.764 47.771  1.00 52.35  ? 317  ASN A CB  1 
ATOM   2416  C  CG  . ASN A  1 317 ? -1.605  -20.397 47.520  1.00 59.16  ? 317  ASN A CG  1 
ATOM   2417  O  OD1 . ASN A  1 317 ? -1.786  -19.811 46.441  1.00 59.54  ? 317  ASN A OD1 1 
ATOM   2418  N  ND2 . ASN A  1 317 ? -0.858  -19.892 48.500  1.00 63.48  ? 317  ASN A ND2 1 
ATOM   2419  N  N   . THR A  1 318 ? -1.520  -24.651 48.919  1.00 52.21  ? 318  THR A N   1 
ATOM   2420  C  CA  . THR A  1 318 ? -1.254  -25.418 50.122  1.00 54.21  ? 318  THR A CA  1 
ATOM   2421  C  C   . THR A  1 318 ? -0.619  -26.799 49.946  1.00 59.29  ? 318  THR A C   1 
ATOM   2422  O  O   . THR A  1 318 ? -0.372  -27.474 50.944  1.00 66.56  ? 318  THR A O   1 
ATOM   2423  C  CB  . THR A  1 318 ? -2.550  -25.625 50.870  1.00 44.46  ? 318  THR A CB  1 
ATOM   2424  O  OG1 . THR A  1 318 ? -3.391  -26.492 50.096  1.00 44.55  ? 318  THR A OG1 1 
ATOM   2425  C  CG2 . THR A  1 318 ? -3.248  -24.283 51.073  1.00 44.19  ? 318  THR A CG2 1 
ATOM   2426  N  N   . GLY A  1 319 ? -0.372  -27.236 48.711  1.00 42.25  ? 319  GLY A N   1 
ATOM   2427  C  CA  . GLY A  1 319 ? -0.011  -28.631 48.456  1.00 40.25  ? 319  GLY A CA  1 
ATOM   2428  C  C   . GLY A  1 319 ? 1.393   -29.068 48.866  1.00 39.22  ? 319  GLY A C   1 
ATOM   2429  O  O   . GLY A  1 319 ? 2.190   -28.250 49.309  1.00 34.87  ? 319  GLY A O   1 
ATOM   2430  N  N   . ASP A  1 320 ? 1.697   -30.362 48.749  1.00 61.81  ? 320  ASP A N   1 
ATOM   2431  C  CA  . ASP A  1 320 ? 3.089   -30.809 48.871  1.00 69.59  ? 320  ASP A CA  1 
ATOM   2432  C  C   . ASP A  1 320 ? 3.588   -31.489 47.606  1.00 72.58  ? 320  ASP A C   1 
ATOM   2433  O  O   . ASP A  1 320 ? 3.177   -32.604 47.273  1.00 76.11  ? 320  ASP A O   1 
ATOM   2434  C  CB  . ASP A  1 320 ? 3.296   -31.763 50.037  1.00 72.84  ? 320  ASP A CB  1 
ATOM   2435  C  CG  . ASP A  1 320 ? 4.716   -32.296 50.086  1.00 76.84  ? 320  ASP A CG  1 
ATOM   2436  O  OD1 . ASP A  1 320 ? 5.653   -31.471 49.987  1.00 77.55  ? 320  ASP A OD1 1 
ATOM   2437  O  OD2 . ASP A  1 320 ? 4.895   -33.531 50.194  1.00 78.58  ? 320  ASP A OD2 1 
ATOM   2438  N  N   . PHE A  1 321 ? 4.484   -30.800 46.913  1.00 64.36  ? 321  PHE A N   1 
ATOM   2439  C  CA  . PHE A  1 321 ? 4.917   -31.196 45.579  1.00 58.81  ? 321  PHE A CA  1 
ATOM   2440  C  C   . PHE A  1 321 ? 6.288   -31.897 45.371  1.00 68.60  ? 321  PHE A C   1 
ATOM   2441  O  O   . PHE A  1 321 ? 6.736   -32.013 44.231  1.00 72.24  ? 321  PHE A O   1 
ATOM   2442  C  CB  . PHE A  1 321 ? 4.620   -30.067 44.584  1.00 45.04  ? 321  PHE A CB  1 
ATOM   2443  C  CG  . PHE A  1 321 ? 3.167   -29.601 44.613  1.00 39.56  ? 321  PHE A CG  1 
ATOM   2444  C  CD1 . PHE A  1 321 ? 2.119   -30.512 44.506  1.00 37.74  ? 321  PHE A CD1 1 
ATOM   2445  C  CD2 . PHE A  1 321 ? 2.847   -28.260 44.777  1.00 36.07  ? 321  PHE A CD2 1 
ATOM   2446  C  CE1 . PHE A  1 321 ? 0.777   -30.084 44.538  1.00 34.92  ? 321  PHE A CE1 1 
ATOM   2447  C  CE2 . PHE A  1 321 ? 1.515   -27.830 44.809  1.00 33.19  ? 321  PHE A CE2 1 
ATOM   2448  C  CZ  . PHE A  1 321 ? 0.482   -28.740 44.691  1.00 31.97  ? 321  PHE A CZ  1 
ATOM   2449  N  N   . GLN A  1 322 ? 6.974   -32.292 46.448  1.00 40.66  ? 322  GLN A N   1 
ATOM   2450  C  CA  . GLN A  1 322 ? 8.303   -32.944 46.348  1.00 46.10  ? 322  GLN A CA  1 
ATOM   2451  C  C   . GLN A  1 322 ? 8.388   -34.227 45.499  1.00 49.21  ? 322  GLN A C   1 
ATOM   2452  O  O   . GLN A  1 322 ? 9.453   -34.581 44.973  1.00 46.26  ? 322  GLN A O   1 
ATOM   2453  C  CB  . GLN A  1 322 ? 8.872   -33.243 47.733  1.00 80.03  ? 322  GLN A CB  1 
ATOM   2454  C  CG  . GLN A  1 322 ? 9.145   -32.027 48.563  1.00 88.69  ? 322  GLN A CG  1 
ATOM   2455  C  CD  . GLN A  1 322 ? 8.697   -32.220 49.991  1.00 96.43  ? 322  GLN A CD  1 
ATOM   2456  O  OE1 . GLN A  1 322 ? 8.622   -33.351 50.483  1.00 97.74  ? 322  GLN A OE1 1 
ATOM   2457  N  NE2 . GLN A  1 322 ? 8.375   -31.117 50.666  1.00 99.33  ? 322  GLN A NE2 1 
ATOM   2458  N  N   . ASP A  1 323 ? 7.265   -34.926 45.387  1.00 85.00  ? 323  ASP A N   1 
ATOM   2459  C  CA  . ASP A  1 323 ? 7.155   -36.139 44.582  1.00 89.27  ? 323  ASP A CA  1 
ATOM   2460  C  C   . ASP A  1 323 ? 7.506   -35.817 43.128  1.00 78.76  ? 323  ASP A C   1 
ATOM   2461  O  O   . ASP A  1 323 ? 7.953   -36.679 42.368  1.00 78.24  ? 323  ASP A O   1 
ATOM   2462  C  CB  . ASP A  1 323 ? 5.693   -36.632 44.662  1.00 113.76 ? 323  ASP A CB  1 
ATOM   2463  C  CG  . ASP A  1 323 ? 5.533   -38.131 44.378  1.00 122.14 ? 323  ASP A CG  1 
ATOM   2464  O  OD1 . ASP A  1 323 ? 5.565   -38.533 43.190  1.00 125.20 ? 323  ASP A OD1 1 
ATOM   2465  O  OD2 . ASP A  1 323 ? 5.329   -38.901 45.347  1.00 123.24 ? 323  ASP A OD2 1 
ATOM   2466  N  N   . LEU A  1 324 ? 7.354   -34.542 42.781  1.00 63.77  ? 324  LEU A N   1 
ATOM   2467  C  CA  . LEU A  1 324 ? 6.932   -34.140 41.448  1.00 48.86  ? 324  LEU A CA  1 
ATOM   2468  C  C   . LEU A  1 324 ? 7.876   -33.228 40.669  1.00 43.99  ? 324  LEU A C   1 
ATOM   2469  O  O   . LEU A  1 324 ? 8.461   -32.305 41.237  1.00 46.25  ? 324  LEU A O   1 
ATOM   2470  C  CB  . LEU A  1 324 ? 5.578   -33.438 41.579  1.00 21.46  ? 324  LEU A CB  1 
ATOM   2471  C  CG  . LEU A  1 324 ? 4.896   -33.120 40.263  1.00 16.83  ? 324  LEU A CG  1 
ATOM   2472  C  CD1 . LEU A  1 324 ? 4.322   -34.401 39.693  1.00 16.49  ? 324  LEU A CD1 1 
ATOM   2473  C  CD2 . LEU A  1 324 ? 3.852   -32.039 40.452  1.00 16.59  ? 324  LEU A CD2 1 
ATOM   2474  N  N   . GLN A  1 325 ? 7.993   -33.499 39.363  1.00 26.96  ? 325  GLN A N   1 
ATOM   2475  C  CA  . GLN A  1 325 ? 8.631   -32.599 38.401  1.00 22.39  ? 325  GLN A CA  1 
ATOM   2476  C  C   . GLN A  1 325 ? 7.683   -32.209 37.262  1.00 17.83  ? 325  GLN A C   1 
ATOM   2477  O  O   . GLN A  1 325 ? 7.071   -33.077 36.609  1.00 16.79  ? 325  GLN A O   1 
ATOM   2478  C  CB  . GLN A  1 325 ? 9.882   -33.225 37.795  1.00 30.07  ? 325  GLN A CB  1 
ATOM   2479  C  CG  . GLN A  1 325 ? 10.682  -34.073 38.738  1.00 36.36  ? 325  GLN A CG  1 
ATOM   2480  C  CD  . GLN A  1 325 ? 10.493  -35.534 38.449  1.00 42.64  ? 325  GLN A CD  1 
ATOM   2481  O  OE1 . GLN A  1 325 ? 9.433   -36.101 38.725  1.00 45.08  ? 325  GLN A OE1 1 
ATOM   2482  N  NE2 . GLN A  1 325 ? 11.510  -36.156 37.863  1.00 44.79  ? 325  GLN A NE2 1 
ATOM   2483  N  N   . VAL A  1 326 ? 7.573   -30.904 37.019  1.00 17.73  ? 326  VAL A N   1 
ATOM   2484  C  CA  . VAL A  1 326 ? 6.737   -30.391 35.939  1.00 17.69  ? 326  VAL A CA  1 
ATOM   2485  C  C   . VAL A  1 326 ? 7.533   -29.545 34.955  1.00 17.08  ? 326  VAL A C   1 
ATOM   2486  O  O   . VAL A  1 326 ? 8.458   -28.827 35.329  1.00 23.67  ? 326  VAL A O   1 
ATOM   2487  C  CB  . VAL A  1 326 ? 5.570   -29.532 36.467  1.00 18.19  ? 326  VAL A CB  1 
ATOM   2488  C  CG1 . VAL A  1 326 ? 4.619   -30.358 37.313  1.00 16.18  ? 326  VAL A CG1 1 
ATOM   2489  C  CG2 . VAL A  1 326 ? 6.114   -28.407 37.280  1.00 17.77  ? 326  VAL A CG2 1 
ATOM   2490  N  N   . LEU A  1 327 ? 7.157   -29.645 33.690  1.00 21.55  ? 327  LEU A N   1 
ATOM   2491  C  CA  . LEU A  1 327 ? 7.646   -28.774 32.636  1.00 21.17  ? 327  LEU A CA  1 
ATOM   2492  C  C   . LEU A  1 327 ? 6.450   -27.921 32.132  1.00 23.52  ? 327  LEU A C   1 
ATOM   2493  O  O   . LEU A  1 327 ? 5.449   -28.460 31.639  1.00 22.77  ? 327  LEU A O   1 
ATOM   2494  C  CB  . LEU A  1 327 ? 8.264   -29.632 31.527  1.00 17.32  ? 327  LEU A CB  1 
ATOM   2495  C  CG  . LEU A  1 327 ? 8.570   -28.992 30.174  1.00 17.67  ? 327  LEU A CG  1 
ATOM   2496  C  CD1 . LEU A  1 327 ? 9.729   -28.051 30.304  1.00 18.43  ? 327  LEU A CD1 1 
ATOM   2497  C  CD2 . LEU A  1 327 ? 8.837   -30.053 29.120  1.00 17.74  ? 327  LEU A CD2 1 
ATOM   2498  N  N   . VAL A  1 328 ? 6.541   -26.598 32.300  1.00 21.08  ? 328  VAL A N   1 
ATOM   2499  C  CA  . VAL A  1 328 ? 5.455   -25.673 31.956  1.00 19.52  ? 328  VAL A CA  1 
ATOM   2500  C  C   . VAL A  1 328 ? 5.925   -24.532 31.067  1.00 18.38  ? 328  VAL A C   1 
ATOM   2501  O  O   . VAL A  1 328 ? 7.036   -24.008 31.210  1.00 18.16  ? 328  VAL A O   1 
ATOM   2502  C  CB  . VAL A  1 328 ? 4.788   -25.064 33.198  1.00 16.89  ? 328  VAL A CB  1 
ATOM   2503  C  CG1 . VAL A  1 328 ? 4.273   -26.164 34.096  1.00 16.45  ? 328  VAL A CG1 1 
ATOM   2504  C  CG2 . VAL A  1 328 ? 5.756   -24.181 33.941  1.00 17.52  ? 328  VAL A CG2 1 
ATOM   2505  N  N   . GLY A  1 329 ? 5.079   -24.143 30.128  1.00 19.61  ? 329  GLY A N   1 
ATOM   2506  C  CA  . GLY A  1 329 ? 5.479   -23.040 29.274  1.00 20.45  ? 329  GLY A CA  1 
ATOM   2507  C  C   . GLY A  1 329 ? 4.369   -22.435 28.449  1.00 25.98  ? 329  GLY A C   1 
ATOM   2508  O  O   . GLY A  1 329 ? 3.247   -22.928 28.457  1.00 31.42  ? 329  GLY A O   1 
ATOM   2509  N  N   . VAL A  1 330 ? 4.674   -21.359 27.732  1.00 23.98  ? 330  VAL A N   1 
ATOM   2510  C  CA  . VAL A  1 330 ? 3.665   -20.677 26.925  1.00 22.87  ? 330  VAL A CA  1 
ATOM   2511  C  C   . VAL A  1 330 ? 4.235   -20.423 25.541  1.00 23.45  ? 330  VAL A C   1 
ATOM   2512  O  O   . VAL A  1 330 ? 5.421   -20.593 25.347  1.00 20.03  ? 330  VAL A O   1 
ATOM   2513  C  CB  . VAL A  1 330 ? 3.259   -19.345 27.572  1.00 19.30  ? 330  VAL A CB  1 
ATOM   2514  C  CG1 . VAL A  1 330 ? 2.689   -19.596 28.953  1.00 18.73  ? 330  VAL A CG1 1 
ATOM   2515  C  CG2 . VAL A  1 330 ? 4.448   -18.434 27.667  1.00 20.09  ? 330  VAL A CG2 1 
ATOM   2516  N  N   . VAL A  1 331 ? 3.406   -20.050 24.570  1.00 28.79  ? 331  VAL A N   1 
ATOM   2517  C  CA  . VAL A  1 331 ? 3.952   -19.596 23.289  1.00 29.44  ? 331  VAL A CA  1 
ATOM   2518  C  C   . VAL A  1 331 ? 4.008   -18.072 23.238  1.00 31.77  ? 331  VAL A C   1 
ATOM   2519  O  O   . VAL A  1 331 ? 3.510   -17.390 24.142  1.00 33.02  ? 331  VAL A O   1 
ATOM   2520  C  CB  . VAL A  1 331 ? 3.181   -20.151 22.070  1.00 23.06  ? 331  VAL A CB  1 
ATOM   2521  C  CG1 . VAL A  1 331 ? 3.255   -21.667 22.057  1.00 20.16  ? 331  VAL A CG1 1 
ATOM   2522  C  CG2 . VAL A  1 331 ? 1.735   -19.675 22.072  1.00 20.71  ? 331  VAL A CG2 1 
ATOM   2523  N  N   . LYS A  1 332 ? 4.590   -17.537 22.171  1.00 30.37  ? 332  LYS A N   1 
ATOM   2524  C  CA  . LYS A  1 332 ? 4.988   -16.135 22.179  1.00 35.46  ? 332  LYS A CA  1 
ATOM   2525  C  C   . LYS A  1 332 ? 3.800   -15.198 22.178  1.00 35.24  ? 332  LYS A C   1 
ATOM   2526  O  O   . LYS A  1 332 ? 3.806   -14.207 22.907  1.00 36.28  ? 332  LYS A O   1 
ATOM   2527  C  CB  . LYS A  1 332 ? 5.944   -15.798 21.031  1.00 51.17  ? 332  LYS A CB  1 
ATOM   2528  C  CG  . LYS A  1 332 ? 6.664   -14.454 21.190  1.00 53.48  ? 332  LYS A CG  1 
ATOM   2529  C  CD  . LYS A  1 332 ? 7.333   -14.037 19.886  1.00 55.01  ? 332  LYS A CD  1 
ATOM   2530  C  CE  . LYS A  1 332 ? 8.498   -13.094 20.125  1.00 56.93  ? 332  LYS A CE  1 
ATOM   2531  N  NZ  . LYS A  1 332 ? 8.143   -11.951 21.002  1.00 57.88  ? 332  LYS A NZ  1 
ATOM   2532  N  N   . ASP A  1 333 ? 2.794   -15.482 21.356  1.00 41.27  ? 333  ASP A N   1 
ATOM   2533  C  CA  . ASP A  1 333 ? 1.558   -14.722 21.465  1.00 45.24  ? 333  ASP A CA  1 
ATOM   2534  C  C   . ASP A  1 333 ? 0.373   -15.626 21.732  1.00 44.08  ? 333  ASP A C   1 
ATOM   2535  O  O   . ASP A  1 333 ? -0.152  -16.257 20.819  1.00 44.69  ? 333  ASP A O   1 
ATOM   2536  C  CB  . ASP A  1 333 ? 1.335   -13.932 20.188  1.00 48.06  ? 333  ASP A CB  1 
ATOM   2537  C  CG  . ASP A  1 333 ? 2.630   -13.463 19.581  1.00 50.99  ? 333  ASP A CG  1 
ATOM   2538  O  OD1 . ASP A  1 333 ? 3.298   -14.308 18.955  1.00 52.91  ? 333  ASP A OD1 1 
ATOM   2539  O  OD2 . ASP A  1 333 ? 2.987   -12.271 19.738  1.00 51.92  ? 333  ASP A OD2 1 
ATOM   2540  N  N   . GLU A  1 334 ? -0.095  -15.611 22.976  1.00 34.31  ? 334  GLU A N   1 
ATOM   2541  C  CA  . GLU A  1 334 ? -1.162  -16.498 23.408  1.00 28.96  ? 334  GLU A CA  1 
ATOM   2542  C  C   . GLU A  1 334 ? -2.498  -15.927 23.031  1.00 30.90  ? 334  GLU A C   1 
ATOM   2543  O  O   . GLU A  1 334 ? -3.415  -16.662 22.679  1.00 34.42  ? 334  GLU A O   1 
ATOM   2544  C  CB  . GLU A  1 334 ? -1.102  -16.717 24.911  1.00 29.42  ? 334  GLU A CB  1 
ATOM   2545  C  CG  . GLU A  1 334 ? 0.189   -17.376 25.358  1.00 33.54  ? 334  GLU A CG  1 
ATOM   2546  C  CD  . GLU A  1 334 ? 0.137   -18.886 25.262  1.00 37.19  ? 334  GLU A CD  1 
ATOM   2547  O  OE1 . GLU A  1 334 ? -0.986  -19.442 25.278  1.00 40.72  ? 334  GLU A OE1 1 
ATOM   2548  O  OE2 . GLU A  1 334 ? 1.214   -19.518 25.182  1.00 36.01  ? 334  GLU A OE2 1 
ATOM   2549  N  N   . GLY A  1 335 ? -2.599  -14.606 23.094  1.00 31.07  ? 335  GLY A N   1 
ATOM   2550  C  CA  . GLY A  1 335 ? -3.879  -13.944 22.956  1.00 32.85  ? 335  GLY A CA  1 
ATOM   2551  C  C   . GLY A  1 335 ? -4.462  -13.964 21.559  1.00 34.67  ? 335  GLY A C   1 
ATOM   2552  O  O   . GLY A  1 335 ? -5.659  -14.209 21.386  1.00 33.80  ? 335  GLY A O   1 
ATOM   2553  N  N   . SER A  1 336 ? -3.604  -13.735 20.566  1.00 37.94  ? 336  SER A N   1 
ATOM   2554  C  CA  . SER A  1 336 ? -4.045  -13.407 19.205  1.00 35.90  ? 336  SER A CA  1 
ATOM   2555  C  C   . SER A  1 336 ? -5.089  -14.343 18.604  1.00 30.60  ? 336  SER A C   1 
ATOM   2556  O  O   . SER A  1 336 ? -5.971  -13.890 17.894  1.00 29.81  ? 336  SER A O   1 
ATOM   2557  C  CB  . SER A  1 336 ? -2.848  -13.206 18.247  1.00 32.33  ? 336  SER A CB  1 
ATOM   2558  O  OG  . SER A  1 336 ? -1.861  -14.219 18.368  1.00 25.42  ? 336  SER A OG  1 
ATOM   2559  N  N   . TYR A  1 337 ? -5.006  -15.632 18.906  1.00 26.40  ? 337  TYR A N   1 
ATOM   2560  C  CA  . TYR A  1 337 ? -5.966  -16.583 18.364  1.00 32.92  ? 337  TYR A CA  1 
ATOM   2561  C  C   . TYR A  1 337 ? -7.421  -16.218 18.756  1.00 39.29  ? 337  TYR A C   1 
ATOM   2562  O  O   . TYR A  1 337 ? -8.316  -16.186 17.906  1.00 37.65  ? 337  TYR A O   1 
ATOM   2563  C  CB  . TYR A  1 337 ? -5.603  -18.030 18.767  1.00 51.08  ? 337  TYR A CB  1 
ATOM   2564  C  CG  . TYR A  1 337 ? -6.439  -19.104 18.082  1.00 61.42  ? 337  TYR A CG  1 
ATOM   2565  C  CD1 . TYR A  1 337 ? -7.803  -19.229 18.350  1.00 65.43  ? 337  TYR A CD1 1 
ATOM   2566  C  CD2 . TYR A  1 337 ? -5.870  -19.995 17.180  1.00 66.03  ? 337  TYR A CD2 1 
ATOM   2567  C  CE1 . TYR A  1 337 ? -8.582  -20.186 17.732  1.00 68.67  ? 337  TYR A CE1 1 
ATOM   2568  C  CE2 . TYR A  1 337 ? -6.648  -20.973 16.551  1.00 70.29  ? 337  TYR A CE2 1 
ATOM   2569  C  CZ  . TYR A  1 337 ? -8.009  -21.059 16.836  1.00 72.11  ? 337  TYR A CZ  1 
ATOM   2570  O  OH  . TYR A  1 337 ? -8.816  -22.013 16.241  1.00 73.95  ? 337  TYR A OH  1 
ATOM   2571  N  N   . PHE A  1 338 ? -7.653  -15.936 20.035  1.00 48.66  ? 338  PHE A N   1 
ATOM   2572  C  CA  . PHE A  1 338 ? -9.015  -15.791 20.547  1.00 45.95  ? 338  PHE A CA  1 
ATOM   2573  C  C   . PHE A  1 338 ? -9.599  -14.450 20.190  1.00 47.38  ? 338  PHE A C   1 
ATOM   2574  O  O   . PHE A  1 338 ? -10.784 -14.221 20.389  1.00 50.06  ? 338  PHE A O   1 
ATOM   2575  C  CB  . PHE A  1 338 ? -9.042  -15.979 22.061  1.00 36.90  ? 338  PHE A CB  1 
ATOM   2576  C  CG  . PHE A  1 338 ? -8.351  -17.217 22.507  1.00 36.55  ? 338  PHE A CG  1 
ATOM   2577  C  CD1 . PHE A  1 338 ? -6.968  -17.234 22.671  1.00 35.98  ? 338  PHE A CD1 1 
ATOM   2578  C  CD2 . PHE A  1 338 ? -9.068  -18.379 22.733  1.00 36.61  ? 338  PHE A CD2 1 
ATOM   2579  C  CE1 . PHE A  1 338 ? -6.311  -18.394 23.056  1.00 35.61  ? 338  PHE A CE1 1 
ATOM   2580  C  CE2 . PHE A  1 338 ? -8.416  -19.543 23.124  1.00 37.75  ? 338  PHE A CE2 1 
ATOM   2581  C  CZ  . PHE A  1 338 ? -7.035  -19.551 23.286  1.00 36.21  ? 338  PHE A CZ  1 
ATOM   2582  N  N   . LEU A  1 339 ? -8.765  -13.560 19.668  1.00 41.18  ? 339  LEU A N   1 
ATOM   2583  C  CA  . LEU A  1 339 ? -9.224  -12.224 19.326  1.00 40.62  ? 339  LEU A CA  1 
ATOM   2584  C  C   . LEU A  1 339 ? -10.224 -12.245 18.181  1.00 45.43  ? 339  LEU A C   1 
ATOM   2585  O  O   . LEU A  1 339 ? -11.274 -11.614 18.264  1.00 48.09  ? 339  LEU A O   1 
ATOM   2586  C  CB  . LEU A  1 339 ? -8.049  -11.326 18.980  1.00 33.33  ? 339  LEU A CB  1 
ATOM   2587  C  CG  . LEU A  1 339 ? -7.215  -10.951 20.190  1.00 31.20  ? 339  LEU A CG  1 
ATOM   2588  C  CD1 . LEU A  1 339 ? -6.155  -9.976  19.757  1.00 32.53  ? 339  LEU A CD1 1 
ATOM   2589  C  CD2 . LEU A  1 339 ? -8.109  -10.354 21.258  1.00 29.82  ? 339  LEU A CD2 1 
ATOM   2590  N  N   . VAL A  1 340 ? -9.910  -12.994 17.126  1.00 49.88  ? 340  VAL A N   1 
ATOM   2591  C  CA  . VAL A  1 340 ? -10.773 -13.078 15.945  1.00 49.99  ? 340  VAL A CA  1 
ATOM   2592  C  C   . VAL A  1 340 ? -12.119 -13.741 16.296  1.00 46.31  ? 340  VAL A C   1 
ATOM   2593  O  O   . VAL A  1 340 ? -13.087 -13.709 15.529  1.00 45.94  ? 340  VAL A O   1 
ATOM   2594  C  CB  . VAL A  1 340 ? -10.051 -13.815 14.792  1.00 44.56  ? 340  VAL A CB  1 
ATOM   2595  C  CG1 . VAL A  1 340 ? -8.733  -13.118 14.458  1.00 43.14  ? 340  VAL A CG1 1 
ATOM   2596  C  CG2 . VAL A  1 340 ? -9.786  -15.247 15.171  1.00 43.78  ? 340  VAL A CG2 1 
ATOM   2597  N  N   . TYR A  1 341 ? -12.159 -14.274 17.510  1.00 32.46  ? 341  TYR A N   1 
ATOM   2598  C  CA  . TYR A  1 341 ? -13.295 -14.979 18.081  1.00 34.39  ? 341  TYR A CA  1 
ATOM   2599  C  C   . TYR A  1 341 ? -14.321 -14.083 18.785  1.00 37.65  ? 341  TYR A C   1 
ATOM   2600  O  O   . TYR A  1 341 ? -15.131 -14.558 19.592  1.00 36.23  ? 341  TYR A O   1 
ATOM   2601  C  CB  . TYR A  1 341 ? -12.861 -16.185 18.910  1.00 50.64  ? 341  TYR A CB  1 
ATOM   2602  C  CG  . TYR A  1 341 ? -12.747 -17.424 18.051  1.00 56.23  ? 341  TYR A CG  1 
ATOM   2603  C  CD1 . TYR A  1 341 ? -11.785 -17.503 17.057  1.00 59.40  ? 341  TYR A CD1 1 
ATOM   2604  C  CD2 . TYR A  1 341 ? -13.615 -18.501 18.215  1.00 57.97  ? 341  TYR A CD2 1 
ATOM   2605  C  CE1 . TYR A  1 341 ? -11.671 -18.615 16.266  1.00 61.44  ? 341  TYR A CE1 1 
ATOM   2606  C  CE2 . TYR A  1 341 ? -13.515 -19.617 17.417  1.00 59.73  ? 341  TYR A CE2 1 
ATOM   2607  C  CZ  . TYR A  1 341 ? -12.539 -19.663 16.438  1.00 63.20  ? 341  TYR A CZ  1 
ATOM   2608  O  OH  . TYR A  1 341 ? -12.404 -20.767 15.628  1.00 67.90  ? 341  TYR A OH  1 
ATOM   2609  N  N   . GLY A  1 342 ? -14.285 -12.792 18.457  1.00 54.99  ? 342  GLY A N   1 
ATOM   2610  C  CA  . GLY A  1 342 ? -15.212 -11.823 19.021  1.00 54.92  ? 342  GLY A CA  1 
ATOM   2611  C  C   . GLY A  1 342 ? -14.821 -10.585 19.802  1.00 50.69  ? 342  GLY A C   1 
ATOM   2612  O  O   . GLY A  1 342 ? -15.677 -9.957  20.416  1.00 52.15  ? 342  GLY A O   1 
ATOM   2613  N  N   . VAL A  1 343 ? -13.551 -10.211 19.765  1.00 37.66  ? 343  VAL A N   1 
ATOM   2614  C  CA  . VAL A  1 343 ? -13.197 -8.800  19.929  1.00 35.65  ? 343  VAL A CA  1 
ATOM   2615  C  C   . VAL A  1 343 ? -13.255 -8.103  18.554  1.00 36.53  ? 343  VAL A C   1 
ATOM   2616  O  O   . VAL A  1 343 ? -12.576 -8.518  17.605  1.00 37.44  ? 343  VAL A O   1 
ATOM   2617  C  CB  . VAL A  1 343 ? -11.800 -8.623  20.578  1.00 37.49  ? 343  VAL A CB  1 
ATOM   2618  C  CG1 . VAL A  1 343 ? -11.328 -7.167  20.517  1.00 30.72  ? 343  VAL A CG1 1 
ATOM   2619  C  CG2 . VAL A  1 343 ? -11.835 -9.112  22.003  1.00 36.87  ? 343  VAL A CG2 1 
ATOM   2620  N  N   . PRO A  1 344 ? -14.090 -7.056  18.434  1.00 40.15  ? 344  PRO A N   1 
ATOM   2621  C  CA  . PRO A  1 344 ? -14.245 -6.306  17.181  1.00 41.58  ? 344  PRO A CA  1 
ATOM   2622  C  C   . PRO A  1 344 ? -12.976 -5.583  16.751  1.00 44.71  ? 344  PRO A C   1 
ATOM   2623  O  O   . PRO A  1 344 ? -12.217 -5.112  17.590  1.00 43.92  ? 344  PRO A O   1 
ATOM   2624  C  CB  . PRO A  1 344 ? -15.330 -5.286  17.518  1.00 35.99  ? 344  PRO A CB  1 
ATOM   2625  C  CG  . PRO A  1 344 ? -16.087 -5.902  18.615  1.00 35.05  ? 344  PRO A CG  1 
ATOM   2626  C  CD  . PRO A  1 344 ? -15.074 -6.633  19.438  1.00 33.36  ? 344  PRO A CD  1 
ATOM   2627  N  N   . GLY A  1 345 ? -12.765 -5.499  15.443  1.00 55.40  ? 345  GLY A N   1 
ATOM   2628  C  CA  . GLY A  1 345 ? -11.577 -4.884  14.893  1.00 58.73  ? 345  GLY A CA  1 
ATOM   2629  C  C   . GLY A  1 345 ? -10.582 -5.943  14.473  1.00 59.56  ? 345  GLY A C   1 
ATOM   2630  O  O   . GLY A  1 345 ? -9.658  -5.676  13.705  1.00 64.69  ? 345  GLY A O   1 
ATOM   2631  N  N   . PHE A  1 346 ? -10.778 -7.159  14.967  1.00 34.44  ? 346  PHE A N   1 
ATOM   2632  C  CA  . PHE A  1 346 ? -9.791  -8.207  14.758  1.00 34.42  ? 346  PHE A CA  1 
ATOM   2633  C  C   . PHE A  1 346 ? -10.207 -9.290  13.755  1.00 39.22  ? 346  PHE A C   1 
ATOM   2634  O  O   . PHE A  1 346 ? -11.098 -10.099 14.030  1.00 37.81  ? 346  PHE A O   1 
ATOM   2635  C  CB  . PHE A  1 346 ? -9.406  -8.834  16.099  1.00 47.73  ? 346  PHE A CB  1 
ATOM   2636  C  CG  . PHE A  1 346 ? -8.532  -7.953  16.955  1.00 48.60  ? 346  PHE A CG  1 
ATOM   2637  C  CD1 . PHE A  1 346 ? -9.091  -7.026  17.822  1.00 47.97  ? 346  PHE A CD1 1 
ATOM   2638  C  CD2 . PHE A  1 346 ? -7.148  -8.054  16.892  1.00 47.30  ? 346  PHE A CD2 1 
ATOM   2639  C  CE1 . PHE A  1 346 ? -8.285  -6.217  18.604  1.00 45.91  ? 346  PHE A CE1 1 
ATOM   2640  C  CE2 . PHE A  1 346 ? -6.340  -7.247  17.674  1.00 44.84  ? 346  PHE A CE2 1 
ATOM   2641  C  CZ  . PHE A  1 346 ? -6.906  -6.330  18.525  1.00 44.61  ? 346  PHE A CZ  1 
ATOM   2642  N  N   . SER A  1 347 ? -9.533  -9.307  12.602  1.00 69.76  ? 347  SER A N   1 
ATOM   2643  C  CA  . SER A  1 347 ? -9.716  -10.338 11.573  1.00 70.85  ? 347  SER A CA  1 
ATOM   2644  C  C   . SER A  1 347 ? -8.394  -11.033 11.240  1.00 68.62  ? 347  SER A C   1 
ATOM   2645  O  O   . SER A  1 347 ? -7.320  -10.535 11.572  1.00 70.83  ? 347  SER A O   1 
ATOM   2646  C  CB  . SER A  1 347 ? -10.294 -9.718  10.299  1.00 62.28  ? 347  SER A CB  1 
ATOM   2647  O  OG  . SER A  1 347 ? -10.128 -10.589 9.192   1.00 62.28  ? 347  SER A OG  1 
ATOM   2648  N  N   . LYS A  1 348 ? -8.469  -12.188 10.590  1.00 46.72  ? 348  LYS A N   1 
ATOM   2649  C  CA  . LYS A  1 348 ? -7.256  -12.840 10.096  1.00 45.77  ? 348  LYS A CA  1 
ATOM   2650  C  C   . LYS A  1 348 ? -6.894  -12.306 8.703   1.00 48.05  ? 348  LYS A C   1 
ATOM   2651  O  O   . LYS A  1 348 ? -5.783  -12.521 8.198   1.00 44.09  ? 348  LYS A O   1 
ATOM   2652  C  CB  . LYS A  1 348 ? -7.441  -14.363 10.032  1.00 49.26  ? 348  LYS A CB  1 
ATOM   2653  C  CG  . LYS A  1 348 ? -8.303  -14.840 8.849   1.00 49.50  ? 348  LYS A CG  1 
ATOM   2654  C  CD  . LYS A  1 348 ? -8.236  -16.354 8.653   1.00 44.55  ? 348  LYS A CD  1 
ATOM   2655  C  CE  . LYS A  1 348 ? -9.009  -16.822 7.421   1.00 41.61  ? 348  LYS A CE  1 
ATOM   2656  N  NZ  . LYS A  1 348 ? -8.399  -16.387 6.136   1.00 40.53  ? 348  LYS A NZ  1 
ATOM   2657  N  N   . ASP A  1 349 ? -7.844  -11.598 8.095   1.00 69.39  ? 349  ASP A N   1 
ATOM   2658  C  CA  . ASP A  1 349 ? -7.773  -11.244 6.682   1.00 72.17  ? 349  ASP A CA  1 
ATOM   2659  C  C   . ASP A  1 349 ? -7.145  -9.876  6.437   1.00 76.90  ? 349  ASP A C   1 
ATOM   2660  O  O   . ASP A  1 349 ? -6.943  -9.470  5.290   1.00 83.04  ? 349  ASP A O   1 
ATOM   2661  C  CB  . ASP A  1 349 ? -9.172  -11.311 6.071   1.00 57.04  ? 349  ASP A CB  1 
ATOM   2662  C  CG  . ASP A  1 349 ? -9.816  -12.681 6.240   1.00 54.73  ? 349  ASP A CG  1 
ATOM   2663  O  OD1 . ASP A  1 349 ? -9.169  -13.692 5.899   1.00 53.03  ? 349  ASP A OD1 1 
ATOM   2664  O  OD2 . ASP A  1 349 ? -10.966 -12.758 6.726   1.00 55.17  ? 349  ASP A OD2 1 
ATOM   2665  N  N   . ASN A  1 350 ? -6.836  -9.174  7.522   1.00 50.85  ? 350  ASN A N   1 
ATOM   2666  C  CA  . ASN A  1 350 ? -6.226  -7.846  7.457   1.00 49.96  ? 350  ASN A CA  1 
ATOM   2667  C  C   . ASN A  1 350 ? -5.386  -7.568  8.701   1.00 46.93  ? 350  ASN A C   1 
ATOM   2668  O  O   . ASN A  1 350 ? -5.487  -8.274  9.704   1.00 42.28  ? 350  ASN A O   1 
ATOM   2669  C  CB  . ASN A  1 350 ? -7.273  -6.745  7.236   1.00 62.30  ? 350  ASN A CB  1 
ATOM   2670  C  CG  . ASN A  1 350 ? -8.361  -6.744  8.296   1.00 67.13  ? 350  ASN A CG  1 
ATOM   2671  O  OD1 . ASN A  1 350 ? -8.129  -6.360  9.444   1.00 68.78  ? 350  ASN A OD1 1 
ATOM   2672  N  ND2 . ASN A  1 350 ? -9.563  -7.165  7.912   1.00 69.66  ? 350  ASN A ND2 1 
ATOM   2673  N  N   . GLU A  1 351 ? -4.554  -6.535  8.626   1.00 65.11  ? 351  GLU A N   1 
ATOM   2674  C  CA  . GLU A  1 351 ? -3.550  -6.249  9.650   1.00 66.54  ? 351  GLU A CA  1 
ATOM   2675  C  C   . GLU A  1 351 ? -4.130  -6.004  11.035  1.00 61.78  ? 351  GLU A C   1 
ATOM   2676  O  O   . GLU A  1 351 ? -3.398  -5.987  12.020  1.00 61.66  ? 351  GLU A O   1 
ATOM   2677  C  CB  . GLU A  1 351 ? -2.732  -5.031  9.237   1.00 79.56  ? 351  GLU A CB  1 
ATOM   2678  C  CG  . GLU A  1 351 ? -1.256  -5.282  9.155   1.00 83.98  ? 351  GLU A CG  1 
ATOM   2679  C  CD  . GLU A  1 351 ? -0.477  -3.996  9.151   1.00 90.46  ? 351  GLU A CD  1 
ATOM   2680  O  OE1 . GLU A  1 351 ? -0.901  -3.040  8.461   1.00 91.55  ? 351  GLU A OE1 1 
ATOM   2681  O  OE2 . GLU A  1 351 ? 0.547   -3.938  9.860   1.00 94.01  ? 351  GLU A OE2 1 
ATOM   2682  N  N   . SER A  1 352 ? -5.439  -5.803  11.096  1.00 51.15  ? 352  SER A N   1 
ATOM   2683  C  CA  . SER A  1 352 ? -6.133  -5.605  12.357  1.00 48.26  ? 352  SER A CA  1 
ATOM   2684  C  C   . SER A  1 352 ? -5.514  -4.497  13.182  1.00 51.01  ? 352  SER A C   1 
ATOM   2685  O  O   . SER A  1 352 ? -4.959  -4.753  14.245  1.00 47.61  ? 352  SER A O   1 
ATOM   2686  C  CB  . SER A  1 352 ? -6.153  -6.894  13.176  1.00 46.45  ? 352  SER A CB  1 
ATOM   2687  O  OG  . SER A  1 352 ? -6.916  -7.884  12.523  1.00 46.15  ? 352  SER A OG  1 
ATOM   2688  N  N   . LEU A  1 353 ? -5.590  -3.271  12.676  1.00 76.09  ? 353  LEU A N   1 
ATOM   2689  C  CA  . LEU A  1 353 ? -5.268  -2.102  13.479  1.00 74.21  ? 353  LEU A CA  1 
ATOM   2690  C  C   . LEU A  1 353 ? -6.590  -1.630  14.050  1.00 73.96  ? 353  LEU A C   1 
ATOM   2691  O  O   . LEU A  1 353 ? -7.619  -1.734  13.394  1.00 78.49  ? 353  LEU A O   1 
ATOM   2692  C  CB  . LEU A  1 353 ? -4.607  -1.026  12.619  1.00 45.61  ? 353  LEU A CB  1 
ATOM   2693  C  CG  . LEU A  1 353 ? -3.386  -1.567  11.869  1.00 43.41  ? 353  LEU A CG  1 
ATOM   2694  C  CD1 . LEU A  1 353 ? -2.959  -0.649  10.746  1.00 45.42  ? 353  LEU A CD1 1 
ATOM   2695  C  CD2 . LEU A  1 353 ? -2.227  -1.801  12.816  1.00 40.39  ? 353  LEU A CD2 1 
ATOM   2696  N  N   . ILE A  1 354 ? -6.586  -1.160  15.288  1.00 55.77  ? 354  ILE A N   1 
ATOM   2697  C  CA  . ILE A  1 354 ? -7.847  -0.831  15.946  1.00 52.35  ? 354  ILE A CA  1 
ATOM   2698  C  C   . ILE A  1 354 ? -7.836  0.529   16.653  1.00 53.59  ? 354  ILE A C   1 
ATOM   2699  O  O   . ILE A  1 354 ? -6.787  1.016   17.084  1.00 53.33  ? 354  ILE A O   1 
ATOM   2700  C  CB  . ILE A  1 354 ? -8.258  -1.933  16.947  1.00 40.67  ? 354  ILE A CB  1 
ATOM   2701  C  CG1 . ILE A  1 354 ? -7.261  -2.012  18.102  1.00 37.83  ? 354  ILE A CG1 1 
ATOM   2702  C  CG2 . ILE A  1 354 ? -8.349  -3.279  16.251  1.00 36.93  ? 354  ILE A CG2 1 
ATOM   2703  C  CD1 . ILE A  1 354 ? -7.797  -2.732  19.292  1.00 34.75  ? 354  ILE A CD1 1 
ATOM   2704  N  N   . SER A  1 355 ? -9.009  1.139   16.776  1.00 51.99  ? 355  SER A N   1 
ATOM   2705  C  CA  . SER A  1 355 ? -9.098  2.431   17.439  1.00 53.46  ? 355  SER A CA  1 
ATOM   2706  C  C   . SER A  1 355 ? -8.955  2.255   18.935  1.00 52.23  ? 355  SER A C   1 
ATOM   2707  O  O   . SER A  1 355 ? -8.887  1.133   19.438  1.00 51.38  ? 355  SER A O   1 
ATOM   2708  C  CB  . SER A  1 355 ? -10.426 3.134   17.121  1.00 57.18  ? 355  SER A CB  1 
ATOM   2709  O  OG  . SER A  1 355 ? -11.550 2.348   17.477  1.00 56.10  ? 355  SER A OG  1 
ATOM   2710  N  N   . ARG A  1 356 ? -8.936  3.368   19.653  1.00 50.56  ? 356  ARG A N   1 
ATOM   2711  C  CA  . ARG A  1 356 ? -8.808  3.291   21.089  1.00 46.48  ? 356  ARG A CA  1 
ATOM   2712  C  C   . ARG A  1 356 ? -10.091 2.739   21.644  1.00 45.70  ? 356  ARG A C   1 
ATOM   2713  O  O   . ARG A  1 356 ? -10.063 1.798   22.425  1.00 42.81  ? 356  ARG A O   1 
ATOM   2714  C  CB  . ARG A  1 356 ? -8.509  4.652   21.693  1.00 47.95  ? 356  ARG A CB  1 
ATOM   2715  C  CG  . ARG A  1 356 ? -8.275  4.593   23.176  1.00 44.66  ? 356  ARG A CG  1 
ATOM   2716  C  CD  . ARG A  1 356 ? -7.002  5.307   23.571  1.00 44.99  ? 356  ARG A CD  1 
ATOM   2717  N  NE  . ARG A  1 356 ? -6.793  5.160   25.001  1.00 46.47  ? 356  ARG A NE  1 
ATOM   2718  C  CZ  . ARG A  1 356 ? -6.084  4.183   25.554  1.00 46.64  ? 356  ARG A CZ  1 
ATOM   2719  N  NH1 . ARG A  1 356 ? -5.484  3.284   24.785  1.00 47.74  ? 356  ARG A NH1 1 
ATOM   2720  N  NH2 . ARG A  1 356 ? -5.964  4.114   26.875  1.00 44.47  ? 356  ARG A NH2 1 
ATOM   2721  N  N   . ALA A  1 357 ? -11.213 3.307   21.209  1.00 59.15  ? 357  ALA A N   1 
ATOM   2722  C  CA  . ALA A  1 357 ? -12.531 2.872   21.667  1.00 63.69  ? 357  ALA A CA  1 
ATOM   2723  C  C   . ALA A  1 357 ? -12.686 1.370   21.506  1.00 65.62  ? 357  ALA A C   1 
ATOM   2724  O  O   . ALA A  1 357 ? -13.287 0.691   22.357  1.00 68.15  ? 357  ALA A O   1 
ATOM   2725  C  CB  . ALA A  1 357 ? -13.611 3.585   20.901  1.00 58.96  ? 357  ALA A CB  1 
ATOM   2726  N  N   . GLN A  1 358 ? -12.112 0.868   20.414  1.00 62.03  ? 358  GLN A N   1 
ATOM   2727  C  CA  . GLN A  1 358 ? -12.086 -0.555  20.101  1.00 55.75  ? 358  GLN A CA  1 
ATOM   2728  C  C   . GLN A  1 358 ? -11.241 -1.330  21.084  1.00 49.36  ? 358  GLN A C   1 
ATOM   2729  O  O   . GLN A  1 358 ? -11.600 -2.441  21.464  1.00 48.01  ? 358  GLN A O   1 
ATOM   2730  C  CB  . GLN A  1 358 ? -11.531 -0.776  18.702  1.00 43.85  ? 358  GLN A CB  1 
ATOM   2731  C  CG  . GLN A  1 358 ? -12.455 -1.563  17.817  1.00 42.41  ? 358  GLN A CG  1 
ATOM   2732  C  CD  . GLN A  1 358 ? -12.365 -1.128  16.380  1.00 42.35  ? 358  GLN A CD  1 
ATOM   2733  O  OE1 . GLN A  1 358 ? -11.273 -0.898  15.854  1.00 41.61  ? 358  GLN A OE1 1 
ATOM   2734  N  NE2 . GLN A  1 358 ? -13.519 -0.992  15.734  1.00 43.65  ? 358  GLN A NE2 1 
ATOM   2735  N  N   . PHE A  1 359 ? -10.113 -0.747  21.480  1.00 35.97  ? 359  PHE A N   1 
ATOM   2736  C  CA  . PHE A  1 359 ? -9.271  -1.368  22.494  1.00 34.57  ? 359  PHE A CA  1 
ATOM   2737  C  C   . PHE A  1 359 ? -9.989  -1.459  23.849  1.00 33.96  ? 359  PHE A C   1 
ATOM   2738  O  O   . PHE A  1 359 ? -9.965  -2.505  24.504  1.00 32.60  ? 359  PHE A O   1 
ATOM   2739  C  CB  . PHE A  1 359 ? -7.927  -0.639  22.633  1.00 35.00  ? 359  PHE A CB  1 
ATOM   2740  C  CG  . PHE A  1 359 ? -7.128  -1.074  23.834  1.00 42.17  ? 359  PHE A CG  1 
ATOM   2741  C  CD1 . PHE A  1 359 ? -6.488  -2.305  23.849  1.00 32.49  ? 359  PHE A CD1 1 
ATOM   2742  C  CD2 . PHE A  1 359 ? -7.036  -0.263  24.956  1.00 34.19  ? 359  PHE A CD2 1 
ATOM   2743  C  CE1 . PHE A  1 359 ? -5.765  -2.710  24.958  1.00 31.54  ? 359  PHE A CE1 1 
ATOM   2744  C  CE2 . PHE A  1 359 ? -6.320  -0.672  26.062  1.00 33.24  ? 359  PHE A CE2 1 
ATOM   2745  C  CZ  . PHE A  1 359 ? -5.683  -1.894  26.062  1.00 31.93  ? 359  PHE A CZ  1 
ATOM   2746  N  N   . LEU A  1 360 ? -10.622 -0.367  24.264  1.00 38.26  ? 360  LEU A N   1 
ATOM   2747  C  CA  . LEU A  1 360 ? -11.346 -0.334  25.530  1.00 39.92  ? 360  LEU A CA  1 
ATOM   2748  C  C   . LEU A  1 360 ? -12.452 -1.390  25.536  1.00 40.05  ? 360  LEU A C   1 
ATOM   2749  O  O   . LEU A  1 360 ? -12.582 -2.179  26.497  1.00 37.49  ? 360  LEU A O   1 
ATOM   2750  C  CB  . LEU A  1 360 ? -11.939 1.060   25.757  1.00 42.11  ? 360  LEU A CB  1 
ATOM   2751  C  CG  . LEU A  1 360 ? -11.029 2.252   25.429  1.00 42.23  ? 360  LEU A CG  1 
ATOM   2752  C  CD1 . LEU A  1 360 ? -11.743 3.576   25.682  1.00 43.91  ? 360  LEU A CD1 1 
ATOM   2753  C  CD2 . LEU A  1 360 ? -9.706  2.195   26.195  1.00 40.49  ? 360  LEU A CD2 1 
ATOM   2754  N  N   . ALA A  1 361 ? -13.228 -1.400  24.448  1.00 39.04  ? 361  ALA A N   1 
ATOM   2755  C  CA  . ALA A  1 361 ? -14.340 -2.323  24.280  1.00 34.36  ? 361  ALA A CA  1 
ATOM   2756  C  C   . ALA A  1 361 ? -13.816 -3.718  24.374  1.00 32.75  ? 361  ALA A C   1 
ATOM   2757  O  O   . ALA A  1 361 ? -14.404 -4.590  25.018  1.00 37.03  ? 361  ALA A O   1 
ATOM   2758  C  CB  . ALA A  1 361 ? -14.968 -2.119  22.947  1.00 68.13  ? 361  ALA A CB  1 
ATOM   2759  N  N   . GLY A  1 362 ? -12.682 -3.918  23.723  1.00 38.51  ? 362  GLY A N   1 
ATOM   2760  C  CA  . GLY A  1 362 ? -12.001 -5.195  23.739  1.00 36.68  ? 362  GLY A CA  1 
ATOM   2761  C  C   . GLY A  1 362 ? -11.689 -5.643  25.150  1.00 36.91  ? 362  GLY A C   1 
ATOM   2762  O  O   . GLY A  1 362 ? -12.055 -6.740  25.547  1.00 38.93  ? 362  GLY A O   1 
ATOM   2763  N  N   . VAL A  1 363 ? -11.020 -4.788  25.913  1.00 30.13  ? 363  VAL A N   1 
ATOM   2764  C  CA  . VAL A  1 363 ? -10.716 -5.084  27.309  1.00 29.28  ? 363  VAL A CA  1 
ATOM   2765  C  C   . VAL A  1 363 ? -11.966 -5.482  28.101  1.00 29.06  ? 363  VAL A C   1 
ATOM   2766  O  O   . VAL A  1 363 ? -11.895 -6.352  28.955  1.00 28.05  ? 363  VAL A O   1 
ATOM   2767  C  CB  . VAL A  1 363 ? -9.974  -3.904  27.980  1.00 30.90  ? 363  VAL A CB  1 
ATOM   2768  C  CG1 . VAL A  1 363 ? -10.053 -3.999  29.495  1.00 29.49  ? 363  VAL A CG1 1 
ATOM   2769  C  CG2 . VAL A  1 363 ? -8.526  -3.855  27.507  1.00 29.85  ? 363  VAL A CG2 1 
ATOM   2770  N  N   . ARG A  1 364 ? -13.112 -4.868  27.808  1.00 30.10  ? 364  ARG A N   1 
ATOM   2771  C  CA  . ARG A  1 364 ? -14.350 -5.322  28.458  1.00 30.01  ? 364  ARG A CA  1 
ATOM   2772  C  C   . ARG A  1 364 ? -14.694 -6.753  28.048  1.00 35.47  ? 364  ARG A C   1 
ATOM   2773  O  O   . ARG A  1 364 ? -15.225 -7.537  28.850  1.00 28.42  ? 364  ARG A O   1 
ATOM   2774  C  CB  . ARG A  1 364 ? -15.558 -4.419  28.149  1.00 31.46  ? 364  ARG A CB  1 
ATOM   2775  C  CG  . ARG A  1 364 ? -15.472 -2.994  28.659  1.00 41.97  ? 364  ARG A CG  1 
ATOM   2776  C  CD  . ARG A  1 364 ? -14.664 -2.888  29.932  1.00 39.45  ? 364  ARG A CD  1 
ATOM   2777  N  NE  . ARG A  1 364 ? -15.351 -3.452  31.085  1.00 36.78  ? 364  ARG A NE  1 
ATOM   2778  C  CZ  . ARG A  1 364 ? -16.084 -2.733  31.924  1.00 38.80  ? 364  ARG A CZ  1 
ATOM   2779  N  NH1 . ARG A  1 364 ? -16.228 -1.427  31.719  1.00 41.07  ? 364  ARG A NH1 1 
ATOM   2780  N  NH2 . ARG A  1 364 ? -16.679 -3.316  32.959  1.00 38.77  ? 364  ARG A NH2 1 
ATOM   2781  N  N   . ILE A  1 365 ? -14.425 -7.084  26.786  1.00 46.89  ? 365  ILE A N   1 
ATOM   2782  C  CA  . ILE A  1 365 ? -14.809 -8.403  26.278  1.00 44.27  ? 365  ILE A CA  1 
ATOM   2783  C  C   . ILE A  1 365 ? -13.907 -9.511  26.801  1.00 45.81  ? 365  ILE A C   1 
ATOM   2784  O  O   . ILE A  1 365 ? -14.390 -10.557 27.240  1.00 48.83  ? 365  ILE A O   1 
ATOM   2785  C  CB  . ILE A  1 365 ? -14.817 -8.447  24.743  1.00 37.88  ? 365  ILE A CB  1 
ATOM   2786  C  CG1 . ILE A  1 365 ? -15.896 -7.513  24.192  1.00 30.43  ? 365  ILE A CG1 1 
ATOM   2787  C  CG2 . ILE A  1 365 ? -15.007 -9.871  24.267  1.00 28.10  ? 365  ILE A CG2 1 
ATOM   2788  C  CD1 . ILE A  1 365 ? -16.600 -8.020  22.973  1.00 30.96  ? 365  ILE A CD1 1 
ATOM   2789  N  N   . GLY A  1 366 ? -12.599 -9.261  26.755  1.00 32.10  ? 366  GLY A N   1 
ATOM   2790  C  CA  . GLY A  1 366 ? -11.586 -10.207 27.166  1.00 25.38  ? 366  GLY A CA  1 
ATOM   2791  C  C   . GLY A  1 366 ? -11.455 -10.386 28.667  1.00 24.78  ? 366  GLY A C   1 
ATOM   2792  O  O   . GLY A  1 366 ? -11.132 -11.475 29.113  1.00 23.79  ? 366  GLY A O   1 
ATOM   2793  N  N   . VAL A  1 367 ? -11.692 -9.337  29.453  1.00 33.26  ? 367  VAL A N   1 
ATOM   2794  C  CA  . VAL A  1 367 ? -11.701 -9.451  30.920  1.00 33.03  ? 367  VAL A CA  1 
ATOM   2795  C  C   . VAL A  1 367 ? -13.137 -9.141  31.337  1.00 33.70  ? 367  VAL A C   1 
ATOM   2796  O  O   . VAL A  1 367 ? -13.429 -8.061  31.854  1.00 33.64  ? 367  VAL A O   1 
ATOM   2797  C  CB  . VAL A  1 367 ? -10.713 -8.451  31.624  1.00 39.48  ? 367  VAL A CB  1 
ATOM   2798  C  CG1 . VAL A  1 367 ? -10.106 -9.051  32.882  1.00 24.67  ? 367  VAL A CG1 1 
ATOM   2799  C  CG2 . VAL A  1 367 ? -9.609  -8.040  30.698  1.00 25.63  ? 367  VAL A CG2 1 
ATOM   2800  N  N   . PRO A  1 368 ? -14.045 -10.096 31.088  1.00 26.25  ? 368  PRO A N   1 
ATOM   2801  C  CA  . PRO A  1 368 ? -15.505 -9.915  31.126  1.00 31.99  ? 368  PRO A CA  1 
ATOM   2802  C  C   . PRO A  1 368 ? -16.100 -9.773  32.533  1.00 36.13  ? 368  PRO A C   1 
ATOM   2803  O  O   . PRO A  1 368 ? -17.181 -9.198  32.703  1.00 35.79  ? 368  PRO A O   1 
ATOM   2804  C  CB  . PRO A  1 368 ? -16.031 -11.177 30.426  1.00 26.80  ? 368  PRO A CB  1 
ATOM   2805  C  CG  . PRO A  1 368 ? -14.889 -12.178 30.487  1.00 27.28  ? 368  PRO A CG  1 
ATOM   2806  C  CD  . PRO A  1 368 ? -13.675 -11.518 31.073  1.00 24.30  ? 368  PRO A CD  1 
ATOM   2807  N  N   . GLN A  1 369 ? -15.393 -10.315 33.520  1.00 44.13  ? 369  GLN A N   1 
ATOM   2808  C  CA  . GLN A  1 369 ? -15.819 -10.279 34.908  1.00 45.13  ? 369  GLN A CA  1 
ATOM   2809  C  C   . GLN A  1 369 ? -15.191 -9.102  35.627  1.00 45.81  ? 369  GLN A C   1 
ATOM   2810  O  O   . GLN A  1 369 ? -15.354 -8.946  36.829  1.00 49.24  ? 369  GLN A O   1 
ATOM   2811  C  CB  . GLN A  1 369 ? -15.428 -11.576 35.598  1.00 50.35  ? 369  GLN A CB  1 
ATOM   2812  C  CG  . GLN A  1 369 ? -14.361 -12.382 34.845  1.00 55.53  ? 369  GLN A CG  1 
ATOM   2813  C  CD  . GLN A  1 369 ? -12.980 -11.723 34.845  1.00 54.79  ? 369  GLN A CD  1 
ATOM   2814  O  OE1 . GLN A  1 369 ? -12.763 -10.741 34.146  1.00 53.89  ? 369  GLN A OE1 1 
ATOM   2815  N  NE2 . GLN A  1 369 ? -12.040 -12.279 35.620  1.00 53.33  ? 369  GLN A NE2 1 
ATOM   2816  N  N   . ALA A  1 370 ? -14.458 -8.279  34.888  1.00 42.64  ? 370  ALA A N   1 
ATOM   2817  C  CA  . ALA A  1 370 ? -13.812 -7.105  35.466  1.00 40.90  ? 370  ALA A CA  1 
ATOM   2818  C  C   . ALA A  1 370 ? -14.757 -5.930  35.452  1.00 42.39  ? 370  ALA A C   1 
ATOM   2819  O  O   . ALA A  1 370 ? -15.307 -5.593  34.403  1.00 40.44  ? 370  ALA A O   1 
ATOM   2820  C  CB  . ALA A  1 370 ? -12.552 -6.752  34.696  1.00 28.66  ? 370  ALA A CB  1 
ATOM   2821  N  N   . SER A  1 371 ? -14.922 -5.297  36.611  1.00 46.85  ? 371  SER A N   1 
ATOM   2822  C  CA  . SER A  1 371 ? -15.738 -4.095  36.726  1.00 52.95  ? 371  SER A CA  1 
ATOM   2823  C  C   . SER A  1 371 ? -14.997 -2.928  36.106  1.00 55.90  ? 371  SER A C   1 
ATOM   2824  O  O   . SER A  1 371 ? -13.864 -3.075  35.660  1.00 57.99  ? 371  SER A O   1 
ATOM   2825  C  CB  . SER A  1 371 ? -15.986 -3.784  38.194  1.00 60.01  ? 371  SER A CB  1 
ATOM   2826  O  OG  . SER A  1 371 ? -14.750 -3.710  38.885  1.00 62.52  ? 371  SER A OG  1 
ATOM   2827  N  N   . ASP A  1 372 ? -15.622 -1.759  36.082  1.00 54.06  ? 372  ASP A N   1 
ATOM   2828  C  CA  . ASP A  1 372 ? -14.888 -0.556  35.725  1.00 54.41  ? 372  ASP A CA  1 
ATOM   2829  C  C   . ASP A  1 372 ? -13.860 -0.382  36.818  1.00 51.12  ? 372  ASP A C   1 
ATOM   2830  O  O   . ASP A  1 372 ? -14.049 -0.869  37.934  1.00 51.40  ? 372  ASP A O   1 
ATOM   2831  C  CB  . ASP A  1 372 ? -15.809 0.652   35.689  1.00 61.35  ? 372  ASP A CB  1 
ATOM   2832  C  CG  . ASP A  1 372 ? -17.122 0.353   35.024  1.00 62.69  ? 372  ASP A CG  1 
ATOM   2833  O  OD1 . ASP A  1 372 ? -17.568 -0.817  35.081  1.00 61.61  ? 372  ASP A OD1 1 
ATOM   2834  O  OD2 . ASP A  1 372 ? -17.704 1.293   34.449  1.00 63.68  ? 372  ASP A OD2 1 
ATOM   2835  N  N   . LEU A  1 373 ? -12.749 0.252   36.482  1.00 54.83  ? 373  LEU A N   1 
ATOM   2836  C  CA  . LEU A  1 373 ? -11.633 0.454   37.410  1.00 55.59  ? 373  LEU A CA  1 
ATOM   2837  C  C   . LEU A  1 373 ? -10.895 -0.861  37.662  1.00 49.04  ? 373  LEU A C   1 
ATOM   2838  O  O   . LEU A  1 373 ? -9.705  -0.864  37.953  1.00 50.08  ? 373  LEU A O   1 
ATOM   2839  C  CB  . LEU A  1 373 ? -12.078 1.114   38.742  1.00 45.95  ? 373  LEU A CB  1 
ATOM   2840  C  CG  . LEU A  1 373 ? -11.119 1.187   39.950  1.00 41.90  ? 373  LEU A CG  1 
ATOM   2841  C  CD1 . LEU A  1 373 ? -11.242 2.511   40.658  1.00 43.13  ? 373  LEU A CD1 1 
ATOM   2842  C  CD2 . LEU A  1 373 ? -11.354 0.059   40.941  1.00 38.24  ? 373  LEU A CD2 1 
ATOM   2843  N  N   . ALA A  1 374 ? -11.565 -1.984  37.462  1.00 32.58  ? 374  ALA A N   1 
ATOM   2844  C  CA  . ALA A  1 374 ? -10.831 -3.216  37.380  1.00 29.78  ? 374  ALA A CA  1 
ATOM   2845  C  C   . ALA A  1 374 ? -10.310 -3.093  35.974  1.00 30.68  ? 374  ALA A C   1 
ATOM   2846  O  O   . ALA A  1 374 ? -9.128  -3.284  35.722  1.00 31.88  ? 374  ALA A O   1 
ATOM   2847  C  CB  . ALA A  1 374 ? -11.745 -4.423  37.534  1.00 32.32  ? 374  ALA A CB  1 
ATOM   2848  N  N   . ALA A  1 375 ? -11.203 -2.696  35.070  1.00 30.31  ? 375  ALA A N   1 
ATOM   2849  C  CA  . ALA A  1 375 ? -10.882 -2.587  33.657  1.00 30.39  ? 375  ALA A CA  1 
ATOM   2850  C  C   . ALA A  1 375 ? -10.097 -1.327  33.386  1.00 37.14  ? 375  ALA A C   1 
ATOM   2851  O  O   . ALA A  1 375 ? -9.238  -1.316  32.524  1.00 31.38  ? 375  ALA A O   1 
ATOM   2852  C  CB  . ALA A  1 375 ? -12.138 -2.614  32.824  1.00 30.81  ? 375  ALA A CB  1 
ATOM   2853  N  N   . GLU A  1 376 ? -10.388 -0.263  34.121  1.00 42.63  ? 376  GLU A N   1 
ATOM   2854  C  CA  . GLU A  1 376 ? -9.607  0.954   33.977  1.00 46.38  ? 376  GLU A CA  1 
ATOM   2855  C  C   . GLU A  1 376 ? -8.185  0.693   34.478  1.00 41.66  ? 376  GLU A C   1 
ATOM   2856  O  O   . GLU A  1 376 ? -7.223  1.324   34.022  1.00 43.25  ? 376  GLU A O   1 
ATOM   2857  C  CB  . GLU A  1 376 ? -10.258 2.133   34.710  1.00 72.78  ? 376  GLU A CB  1 
ATOM   2858  C  CG  . GLU A  1 376 ? -9.571  3.471   34.463  1.00 83.04  ? 376  GLU A CG  1 
ATOM   2859  C  CD  . GLU A  1 376 ? -10.225 4.629   35.200  1.00 91.62  ? 376  GLU A CD  1 
ATOM   2860  O  OE1 . GLU A  1 376 ? -11.438 4.537   35.507  1.00 93.86  ? 376  GLU A OE1 1 
ATOM   2861  O  OE2 . GLU A  1 376 ? -9.517  5.631   35.470  1.00 94.23  ? 376  GLU A OE2 1 
ATOM   2862  N  N   . ALA A  1 377 ? -8.050  -0.252  35.406  1.00 34.82  ? 377  ALA A N   1 
ATOM   2863  C  CA  . ALA A  1 377 ? -6.731  -0.664  35.860  1.00 32.57  ? 377  ALA A CA  1 
ATOM   2864  C  C   . ALA A  1 377 ? -5.999  -1.365  34.727  1.00 31.81  ? 377  ALA A C   1 
ATOM   2865  O  O   . ALA A  1 377 ? -4.816  -1.115  34.485  1.00 34.94  ? 377  ALA A O   1 
ATOM   2866  C  CB  . ALA A  1 377 ? -6.837  -1.574  37.051  1.00 30.65  ? 377  ALA A CB  1 
ATOM   2867  N  N   . VAL A  1 378 ? -6.713  -2.248  34.036  1.00 32.25  ? 378  VAL A N   1 
ATOM   2868  C  CA  . VAL A  1 378 ? -6.151  -2.968  32.906  1.00 30.67  ? 378  VAL A CA  1 
ATOM   2869  C  C   . VAL A  1 378 ? -5.701  -1.977  31.840  1.00 31.73  ? 378  VAL A C   1 
ATOM   2870  O  O   . VAL A  1 378 ? -4.583  -2.075  31.340  1.00 31.92  ? 378  VAL A O   1 
ATOM   2871  C  CB  . VAL A  1 378 ? -7.145  -4.002  32.316  1.00 28.47  ? 378  VAL A CB  1 
ATOM   2872  C  CG1 . VAL A  1 378 ? -6.586  -4.619  31.050  1.00 28.02  ? 378  VAL A CG1 1 
ATOM   2873  C  CG2 . VAL A  1 378 ? -7.436  -5.087  33.321  1.00 27.41  ? 378  VAL A CG2 1 
ATOM   2874  N  N   . VAL A  1 379 ? -6.555  -1.008  31.522  1.00 31.46  ? 379  VAL A N   1 
ATOM   2875  C  CA  . VAL A  1 379 ? -6.249  -0.035  30.479  1.00 32.64  ? 379  VAL A CA  1 
ATOM   2876  C  C   . VAL A  1 379 ? -5.059  0.827   30.850  1.00 33.45  ? 379  VAL A C   1 
ATOM   2877  O  O   . VAL A  1 379 ? -4.178  1.052   30.020  1.00 33.86  ? 379  VAL A O   1 
ATOM   2878  C  CB  . VAL A  1 379 ? -7.432  0.886   30.178  1.00 33.81  ? 379  VAL A CB  1 
ATOM   2879  C  CG1 . VAL A  1 379 ? -7.095  1.822   29.025  1.00 35.09  ? 379  VAL A CG1 1 
ATOM   2880  C  CG2 . VAL A  1 379 ? -8.651  0.070   29.847  1.00 53.68  ? 379  VAL A CG2 1 
ATOM   2881  N  N   . LEU A  1 380 ? -5.041  1.313   32.092  1.00 44.14  ? 380  LEU A N   1 
ATOM   2882  C  CA  . LEU A  1 380 ? -3.898  2.063   32.602  1.00 43.55  ? 380  LEU A CA  1 
ATOM   2883  C  C   . LEU A  1 380 ? -2.612  1.261   32.450  1.00 42.83  ? 380  LEU A C   1 
ATOM   2884  O  O   . LEU A  1 380 ? -1.588  1.780   32.001  1.00 42.76  ? 380  LEU A O   1 
ATOM   2885  C  CB  . LEU A  1 380 ? -4.076  2.416   34.073  1.00 39.99  ? 380  LEU A CB  1 
ATOM   2886  C  CG  . LEU A  1 380 ? -2.810  3.077   34.623  1.00 35.64  ? 380  LEU A CG  1 
ATOM   2887  C  CD1 . LEU A  1 380 ? -2.902  4.563   34.464  1.00 37.40  ? 380  LEU A CD1 1 
ATOM   2888  C  CD2 . LEU A  1 380 ? -2.553  2.734   36.055  1.00 35.26  ? 380  LEU A CD2 1 
ATOM   2889  N  N   . HIS A  1 381 ? -2.663  -0.011  32.820  1.00 43.29  ? 381  HIS A N   1 
ATOM   2890  C  CA  . HIS A  1 381 ? -1.468  -0.825  32.741  1.00 47.01  ? 381  HIS A CA  1 
ATOM   2891  C  C   . HIS A  1 381 ? -1.014  -1.069  31.291  1.00 49.33  ? 381  HIS A C   1 
ATOM   2892  O  O   . HIS A  1 381 ? 0.179   -0.956  30.984  1.00 53.72  ? 381  HIS A O   1 
ATOM   2893  C  CB  . HIS A  1 381 ? -1.648  -2.138  33.504  1.00 44.52  ? 381  HIS A CB  1 
ATOM   2894  C  CG  . HIS A  1 381 ? -0.361  -2.861  33.769  1.00 48.41  ? 381  HIS A CG  1 
ATOM   2895  N  ND1 . HIS A  1 381 ? 0.216   -2.919  35.021  1.00 48.94  ? 381  HIS A ND1 1 
ATOM   2896  C  CD2 . HIS A  1 381 ? 0.466   -3.545  32.938  1.00 49.00  ? 381  HIS A CD2 1 
ATOM   2897  C  CE1 . HIS A  1 381 ? 1.340   -3.614  34.950  1.00 49.72  ? 381  HIS A CE1 1 
ATOM   2898  N  NE2 . HIS A  1 381 ? 1.514   -4.005  33.698  1.00 49.34  ? 381  HIS A NE2 1 
ATOM   2899  N  N   . TYR A  1 382 ? -1.954  -1.383  30.401  1.00 39.84  ? 382  TYR A N   1 
ATOM   2900  C  CA  . TYR A  1 382 ? -1.600  -1.782  29.034  1.00 35.70  ? 382  TYR A CA  1 
ATOM   2901  C  C   . TYR A  1 382 ? -1.455  -0.675  27.987  1.00 34.07  ? 382  TYR A C   1 
ATOM   2902  O  O   . TYR A  1 382 ? -0.898  -0.910  26.916  1.00 33.26  ? 382  TYR A O   1 
ATOM   2903  C  CB  . TYR A  1 382 ? -2.542  -2.873  28.535  1.00 30.18  ? 382  TYR A CB  1 
ATOM   2904  C  CG  . TYR A  1 382 ? -2.225  -4.207  29.146  1.00 31.34  ? 382  TYR A CG  1 
ATOM   2905  C  CD1 . TYR A  1 382 ? -1.279  -5.043  28.572  1.00 28.50  ? 382  TYR A CD1 1 
ATOM   2906  C  CD2 . TYR A  1 382 ? -2.839  -4.622  30.312  1.00 28.08  ? 382  TYR A CD2 1 
ATOM   2907  C  CE1 . TYR A  1 382 ? -0.960  -6.277  29.133  1.00 28.66  ? 382  TYR A CE1 1 
ATOM   2908  C  CE2 . TYR A  1 382 ? -2.528  -5.852  30.883  1.00 31.67  ? 382  TYR A CE2 1 
ATOM   2909  C  CZ  . TYR A  1 382 ? -1.588  -6.676  30.285  1.00 29.12  ? 382  TYR A CZ  1 
ATOM   2910  O  OH  . TYR A  1 382 ? -1.274  -7.898  30.838  1.00 28.09  ? 382  TYR A OH  1 
ATOM   2911  N  N   . THR A  1 383 ? -1.928  0.529   28.289  1.00 33.86  ? 383  THR A N   1 
ATOM   2912  C  CA  . THR A  1 383 ? -1.800  1.645   27.349  1.00 36.28  ? 383  THR A CA  1 
ATOM   2913  C  C   . THR A  1 383 ? -0.379  2.194   27.314  1.00 39.92  ? 383  THR A C   1 
ATOM   2914  O  O   . THR A  1 383 ? 0.281   2.280   28.352  1.00 38.37  ? 383  THR A O   1 
ATOM   2915  C  CB  . THR A  1 383 ? -2.737  2.810   27.718  1.00 36.55  ? 383  THR A CB  1 
ATOM   2916  O  OG1 . THR A  1 383 ? -4.081  2.331   27.825  1.00 36.15  ? 383  THR A OG1 1 
ATOM   2917  C  CG2 . THR A  1 383 ? -2.671  3.910   26.670  1.00 38.21  ? 383  THR A CG2 1 
ATOM   2918  N  N   . ASP A  1 384 ? 0.088   2.568   26.124  1.00 53.78  ? 384  ASP A N   1 
ATOM   2919  C  CA  . ASP A  1 384 ? 1.299   3.372   26.015  1.00 60.84  ? 384  ASP A CA  1 
ATOM   2920  C  C   . ASP A  1 384 ? 0.833   4.810   26.034  1.00 64.14  ? 384  ASP A C   1 
ATOM   2921  O  O   . ASP A  1 384 ? 0.222   5.272   25.083  1.00 66.03  ? 384  ASP A O   1 
ATOM   2922  C  CB  . ASP A  1 384 ? 2.046   3.089   24.716  1.00 71.76  ? 384  ASP A CB  1 
ATOM   2923  C  CG  . ASP A  1 384 ? 3.261   3.984   24.532  1.00 78.55  ? 384  ASP A CG  1 
ATOM   2924  O  OD1 . ASP A  1 384 ? 3.700   4.614   25.521  1.00 81.56  ? 384  ASP A OD1 1 
ATOM   2925  O  OD2 . ASP A  1 384 ? 3.781   4.050   23.397  1.00 80.47  ? 384  ASP A OD2 1 
ATOM   2926  N  N   . TRP A  1 385 ? 1.141   5.518   27.118  1.00 62.39  ? 385  TRP A N   1 
ATOM   2927  C  CA  . TRP A  1 385 ? 0.528   6.818   27.391  1.00 59.16  ? 385  TRP A CA  1 
ATOM   2928  C  C   . TRP A  1 385 ? 1.234   7.932   26.655  1.00 60.47  ? 385  TRP A C   1 
ATOM   2929  O  O   . TRP A  1 385 ? 0.745   9.060   26.588  1.00 60.19  ? 385  TRP A O   1 
ATOM   2930  C  CB  . TRP A  1 385 ? 0.475   7.092   28.900  1.00 45.59  ? 385  TRP A CB  1 
ATOM   2931  C  CG  . TRP A  1 385 ? -0.501  6.200   29.579  1.00 41.66  ? 385  TRP A CG  1 
ATOM   2932  C  CD1 . TRP A  1 385 ? -0.242  5.014   30.203  1.00 41.23  ? 385  TRP A CD1 1 
ATOM   2933  C  CD2 . TRP A  1 385 ? -1.911  6.393   29.652  1.00 40.49  ? 385  TRP A CD2 1 
ATOM   2934  N  NE1 . TRP A  1 385 ? -1.405  4.469   30.678  1.00 37.93  ? 385  TRP A NE1 1 
ATOM   2935  C  CE2 . TRP A  1 385 ? -2.446  5.296   30.350  1.00 38.89  ? 385  TRP A CE2 1 
ATOM   2936  C  CE3 . TRP A  1 385 ? -2.774  7.392   29.196  1.00 41.81  ? 385  TRP A CE3 1 
ATOM   2937  C  CZ2 . TRP A  1 385 ? -3.805  5.173   30.608  1.00 38.76  ? 385  TRP A CZ2 1 
ATOM   2938  C  CZ3 . TRP A  1 385 ? -4.115  7.269   29.450  1.00 43.22  ? 385  TRP A CZ3 1 
ATOM   2939  C  CH2 . TRP A  1 385 ? -4.621  6.168   30.152  1.00 42.00  ? 385  TRP A CH2 1 
ATOM   2940  N  N   . LEU A  1 386 ? 2.390   7.601   26.101  1.00 63.50  ? 386  LEU A N   1 
ATOM   2941  C  CA  . LEU A  1 386 ? 3.095   8.530   25.249  1.00 66.23  ? 386  LEU A CA  1 
ATOM   2942  C  C   . LEU A  1 386 ? 2.401   8.558   23.890  1.00 68.88  ? 386  LEU A C   1 
ATOM   2943  O  O   . LEU A  1 386 ? 2.358   9.598   23.223  1.00 72.37  ? 386  LEU A O   1 
ATOM   2944  C  CB  . LEU A  1 386 ? 4.558   8.111   25.122  1.00 52.24  ? 386  LEU A CB  1 
ATOM   2945  C  CG  . LEU A  1 386 ? 5.555   9.247   25.354  1.00 54.31  ? 386  LEU A CG  1 
ATOM   2946  C  CD1 . LEU A  1 386 ? 6.975   8.700   25.487  1.00 52.74  ? 386  LEU A CD1 1 
ATOM   2947  C  CD2 . LEU A  1 386 ? 5.442   10.312  24.252  1.00 49.78  ? 386  LEU A CD2 1 
ATOM   2948  N  N   . HIS A  1 387 ? 1.854   7.406   23.496  1.00 50.32  ? 387  HIS A N   1 
ATOM   2949  C  CA  . HIS A  1 387 ? 1.131   7.258   22.232  1.00 51.39  ? 387  HIS A CA  1 
ATOM   2950  C  C   . HIS A  1 387 ? -0.079  6.352   22.429  1.00 44.32  ? 387  HIS A C   1 
ATOM   2951  O  O   . HIS A  1 387 ? -0.065  5.199   21.993  1.00 43.05  ? 387  HIS A O   1 
ATOM   2952  C  CB  . HIS A  1 387 ? 2.049   6.669   21.156  1.00 78.06  ? 387  HIS A CB  1 
ATOM   2953  C  CG  . HIS A  1 387 ? 3.381   7.349   21.059  1.00 85.48  ? 387  HIS A CG  1 
ATOM   2954  N  ND1 . HIS A  1 387 ? 4.554   6.749   21.465  1.00 86.91  ? 387  HIS A ND1 1 
ATOM   2955  C  CD2 . HIS A  1 387 ? 3.721   8.585   20.622  1.00 88.97  ? 387  HIS A CD2 1 
ATOM   2956  C  CE1 . HIS A  1 387 ? 5.561   7.583   21.275  1.00 89.77  ? 387  HIS A CE1 1 
ATOM   2957  N  NE2 . HIS A  1 387 ? 5.082   8.705   20.766  1.00 90.72  ? 387  HIS A NE2 1 
ATOM   2958  N  N   . PRO A  1 388 ? -1.119  6.871   23.113  1.00 52.92  ? 388  PRO A N   1 
ATOM   2959  C  CA  . PRO A  1 388 ? -2.316  6.168   23.605  1.00 50.39  ? 388  PRO A CA  1 
ATOM   2960  C  C   . PRO A  1 388 ? -3.273  5.782   22.502  1.00 49.47  ? 388  PRO A C   1 
ATOM   2961  O  O   . PRO A  1 388 ? -4.121  4.909   22.696  1.00 44.23  ? 388  PRO A O   1 
ATOM   2962  C  CB  . PRO A  1 388 ? -2.994  7.209   24.499  1.00 43.25  ? 388  PRO A CB  1 
ATOM   2963  C  CG  . PRO A  1 388 ? -2.012  8.348   24.620  1.00 44.82  ? 388  PRO A CG  1 
ATOM   2964  C  CD  . PRO A  1 388 ? -1.211  8.312   23.376  1.00 46.66  ? 388  PRO A CD  1 
ATOM   2965  N  N   . GLU A  1 389 ? -3.151  6.476   21.374  1.00 48.42  ? 389  GLU A N   1 
ATOM   2966  C  CA  . GLU A  1 389 ? -4.005  6.262   20.218  1.00 49.52  ? 389  GLU A CA  1 
ATOM   2967  C  C   . GLU A  1 389 ? -3.368  5.373   19.149  1.00 47.35  ? 389  GLU A C   1 
ATOM   2968  O  O   . GLU A  1 389 ? -3.985  5.115   18.117  1.00 46.71  ? 389  GLU A O   1 
ATOM   2969  C  CB  . GLU A  1 389 ? -4.381  7.611   19.613  1.00 69.63  ? 389  GLU A CB  1 
ATOM   2970  C  CG  . GLU A  1 389 ? -5.052  8.562   20.589  1.00 76.31  ? 389  GLU A CG  1 
ATOM   2971  C  CD  . GLU A  1 389 ? -6.561  8.442   20.560  1.00 82.81  ? 389  GLU A CD  1 
ATOM   2972  O  OE1 . GLU A  1 389 ? -7.089  7.948   19.541  1.00 85.71  ? 389  GLU A OE1 1 
ATOM   2973  O  OE2 . GLU A  1 389 ? -7.216  8.836   21.551  1.00 84.56  ? 389  GLU A OE2 1 
ATOM   2974  N  N   . ASP A  1 390 ? -2.138  4.916   19.384  1.00 55.29  ? 390  ASP A N   1 
ATOM   2975  C  CA  . ASP A  1 390 ? -1.415  4.136   18.381  1.00 56.90  ? 390  ASP A CA  1 
ATOM   2976  C  C   . ASP A  1 390 ? -2.116  2.821   18.101  1.00 57.83  ? 390  ASP A C   1 
ATOM   2977  O  O   . ASP A  1 390 ? -2.193  1.969   18.980  1.00 59.36  ? 390  ASP A O   1 
ATOM   2978  C  CB  . ASP A  1 390 ? 0.012   3.840   18.835  1.00 57.31  ? 390  ASP A CB  1 
ATOM   2979  C  CG  . ASP A  1 390 ? 0.929   3.485   17.674  1.00 59.68  ? 390  ASP A CG  1 
ATOM   2980  O  OD1 . ASP A  1 390 ? 0.826   2.359   17.130  1.00 57.34  ? 390  ASP A OD1 1 
ATOM   2981  O  OD2 . ASP A  1 390 ? 1.755   4.348   17.301  1.00 63.30  ? 390  ASP A OD2 1 
ATOM   2982  N  N   . PRO A  1 391 ? -2.601  2.643   16.865  1.00 52.84  ? 391  PRO A N   1 
ATOM   2983  C  CA  . PRO A  1 391 ? -3.404  1.500   16.414  1.00 52.81  ? 391  PRO A CA  1 
ATOM   2984  C  C   . PRO A  1 391 ? -2.643  0.185   16.437  1.00 54.06  ? 391  PRO A C   1 
ATOM   2985  O  O   . PRO A  1 391 ? -3.219  -0.836  16.838  1.00 55.23  ? 391  PRO A O   1 
ATOM   2986  C  CB  . PRO A  1 391 ? -3.738  1.865   14.973  1.00 50.86  ? 391  PRO A CB  1 
ATOM   2987  C  CG  . PRO A  1 391 ? -3.596  3.345   14.925  1.00 52.21  ? 391  PRO A CG  1 
ATOM   2988  C  CD  . PRO A  1 391 ? -2.424  3.624   15.791  1.00 50.74  ? 391  PRO A CD  1 
ATOM   2989  N  N   . THR A  1 392 ? -1.380  0.209   16.008  1.00 51.52  ? 392  THR A N   1 
ATOM   2990  C  CA  . THR A  1 392 ? -0.513  -0.965  16.102  1.00 47.21  ? 392  THR A CA  1 
ATOM   2991  C  C   . THR A  1 392 ? -0.292  -1.354  17.555  1.00 44.47  ? 392  THR A C   1 
ATOM   2992  O  O   . THR A  1 392 ? -0.496  -2.517  17.944  1.00 43.53  ? 392  THR A O   1 
ATOM   2993  C  CB  . THR A  1 392 ? 0.856   -0.713  15.472  1.00 47.89  ? 392  THR A CB  1 
ATOM   2994  O  OG1 . THR A  1 392 ? 0.740   -0.765  14.047  1.00 48.61  ? 392  THR A OG1 1 
ATOM   2995  C  CG2 . THR A  1 392 ? 1.849   -1.777  15.927  1.00 46.52  ? 392  THR A CG2 1 
ATOM   2996  N  N   . HIS A  1 393 ? 0.122   -0.373  18.357  1.00 38.44  ? 393  HIS A N   1 
ATOM   2997  C  CA  . HIS A  1 393 ? 0.348   -0.621  19.768  1.00 38.60  ? 393  HIS A CA  1 
ATOM   2998  C  C   . HIS A  1 393 ? -0.909  -1.102  20.457  1.00 35.61  ? 393  HIS A C   1 
ATOM   2999  O  O   . HIS A  1 393 ? -0.851  -2.055  21.209  1.00 34.18  ? 393  HIS A O   1 
ATOM   3000  C  CB  . HIS A  1 393 ? 0.900   0.587   20.512  1.00 60.97  ? 393  HIS A CB  1 
ATOM   3001  C  CG  . HIS A  1 393 ? 1.274   0.269   21.925  1.00 69.35  ? 393  HIS A CG  1 
ATOM   3002  N  ND1 . HIS A  1 393 ? 0.334   0.048   22.911  1.00 70.74  ? 393  HIS A ND1 1 
ATOM   3003  C  CD2 . HIS A  1 393 ? 2.482   0.077   22.507  1.00 72.69  ? 393  HIS A CD2 1 
ATOM   3004  C  CE1 . HIS A  1 393 ? 0.947   -0.241  24.045  1.00 70.97  ? 393  HIS A CE1 1 
ATOM   3005  N  NE2 . HIS A  1 393 ? 2.251   -0.230  23.827  1.00 72.64  ? 393  HIS A NE2 1 
ATOM   3006  N  N   . LEU A  1 394 ? -2.029  -0.426  20.213  1.00 47.08  ? 394  LEU A N   1 
ATOM   3007  C  CA  . LEU A  1 394 ? -3.337  -0.855  20.710  1.00 45.17  ? 394  LEU A CA  1 
ATOM   3008  C  C   . LEU A  1 394 ? -3.660  -2.311  20.387  1.00 42.03  ? 394  LEU A C   1 
ATOM   3009  O  O   . LEU A  1 394 ? -4.052  -3.068  21.272  1.00 41.87  ? 394  LEU A O   1 
ATOM   3010  C  CB  . LEU A  1 394 ? -4.429  0.040   20.139  1.00 36.84  ? 394  LEU A CB  1 
ATOM   3011  C  CG  . LEU A  1 394 ? -4.490  1.375   20.863  1.00 37.91  ? 394  LEU A CG  1 
ATOM   3012  C  CD1 . LEU A  1 394 ? -5.508  2.314   20.229  1.00 39.41  ? 394  LEU A CD1 1 
ATOM   3013  C  CD2 . LEU A  1 394 ? -4.793  1.114   22.326  1.00 48.50  ? 394  LEU A CD2 1 
ATOM   3014  N  N   . ARG A  1 395 ? -3.500  -2.690  19.120  1.00 34.58  ? 395  ARG A N   1 
ATOM   3015  C  CA  . ARG A  1 395 ? -3.716  -4.067  18.696  1.00 33.47  ? 395  ARG A CA  1 
ATOM   3016  C  C   . ARG A  1 395 ? -2.852  -5.052  19.479  1.00 32.04  ? 395  ARG A C   1 
ATOM   3017  O  O   . ARG A  1 395 ? -3.368  -5.998  20.124  1.00 30.76  ? 395  ARG A O   1 
ATOM   3018  C  CB  . ARG A  1 395 ? -3.407  -4.213  17.208  1.00 37.17  ? 395  ARG A CB  1 
ATOM   3019  C  CG  . ARG A  1 395 ? -3.423  -5.656  16.719  1.00 37.93  ? 395  ARG A CG  1 
ATOM   3020  C  CD  . ARG A  1 395 ? -2.076  -6.080  16.164  1.00 37.87  ? 395  ARG A CD  1 
ATOM   3021  N  NE  . ARG A  1 395 ? -1.780  -5.498  14.857  1.00 38.82  ? 395  ARG A NE  1 
ATOM   3022  C  CZ  . ARG A  1 395 ? -0.553  -5.405  14.347  1.00 38.90  ? 395  ARG A CZ  1 
ATOM   3023  N  NH1 . ARG A  1 395 ? 0.485   -5.843  15.045  1.00 38.26  ? 395  ARG A NH1 1 
ATOM   3024  N  NH2 . ARG A  1 395 ? -0.359  -4.870  13.146  1.00 40.27  ? 395  ARG A NH2 1 
ATOM   3025  N  N   . ASP A  1 396 ? -1.540  -4.826  19.419  1.00 32.38  ? 396  ASP A N   1 
ATOM   3026  C  CA  . ASP A  1 396 ? -0.587  -5.702  20.091  1.00 35.36  ? 396  ASP A CA  1 
ATOM   3027  C  C   . ASP A  1 396 ? -0.904  -5.786  21.593  1.00 32.42  ? 396  ASP A C   1 
ATOM   3028  O  O   . ASP A  1 396 ? -0.853  -6.861  22.209  1.00 30.19  ? 396  ASP A O   1 
ATOM   3029  C  CB  . ASP A  1 396 ? 0.852   -5.222  19.853  1.00 51.64  ? 396  ASP A CB  1 
ATOM   3030  C  CG  . ASP A  1 396 ? 1.409   -5.648  18.493  1.00 57.41  ? 396  ASP A CG  1 
ATOM   3031  O  OD1 . ASP A  1 396 ? 0.864   -6.594  17.889  1.00 62.26  ? 396  ASP A OD1 1 
ATOM   3032  O  OD2 . ASP A  1 396 ? 2.408   -5.049  18.036  1.00 56.36  ? 396  ASP A OD2 1 
ATOM   3033  N  N   . ALA A  1 397 ? -1.247  -4.637  22.164  1.00 31.78  ? 397  ALA A N   1 
ATOM   3034  C  CA  . ALA A  1 397 ? -1.691  -4.536  23.541  1.00 30.43  ? 397  ALA A CA  1 
ATOM   3035  C  C   . ALA A  1 397 ? -2.799  -5.531  23.778  1.00 29.88  ? 397  ALA A C   1 
ATOM   3036  O  O   . ALA A  1 397 ? -2.583  -6.513  24.459  1.00 29.83  ? 397  ALA A O   1 
ATOM   3037  C  CB  . ALA A  1 397 ? -2.180  -3.143  23.837  1.00 34.63  ? 397  ALA A CB  1 
ATOM   3038  N  N   . MET A  1 398 ? -3.959  -5.299  23.167  1.00 33.64  ? 398  MET A N   1 
ATOM   3039  C  CA  . MET A  1 398 ? -5.146  -6.129  23.376  1.00 31.74  ? 398  MET A CA  1 
ATOM   3040  C  C   . MET A  1 398 ? -4.837  -7.618  23.306  1.00 32.00  ? 398  MET A C   1 
ATOM   3041  O  O   . MET A  1 398 ? -5.292  -8.403  24.171  1.00 30.64  ? 398  MET A O   1 
ATOM   3042  C  CB  . MET A  1 398 ? -6.197  -5.792  22.330  1.00 30.35  ? 398  MET A CB  1 
ATOM   3043  C  CG  . MET A  1 398 ? -7.469  -6.609  22.420  1.00 29.50  ? 398  MET A CG  1 
ATOM   3044  S  SD  . MET A  1 398 ? -8.607  -5.972  23.656  1.00 49.82  ? 398  MET A SD  1 
ATOM   3045  C  CE  . MET A  1 398 ? -8.258  -7.088  25.015  1.00 47.36  ? 398  MET A CE  1 
ATOM   3046  N  N   . SER A  1 399 ? -4.051  -7.998  22.294  1.00 27.82  ? 399  SER A N   1 
ATOM   3047  C  CA  . SER A  1 399 ? -3.559  -9.375  22.205  1.00 26.73  ? 399  SER A CA  1 
ATOM   3048  C  C   . SER A  1 399 ? -2.894  -9.772  23.507  1.00 29.09  ? 399  SER A C   1 
ATOM   3049  O  O   . SER A  1 399 ? -3.251  -10.776 24.121  1.00 24.77  ? 399  SER A O   1 
ATOM   3050  C  CB  . SER A  1 399 ? -2.554  -9.538  21.062  1.00 31.31  ? 399  SER A CB  1 
ATOM   3051  O  OG  . SER A  1 399 ? -1.845  -10.769 21.163  1.00 28.85  ? 399  SER A OG  1 
ATOM   3052  N  N   . ALA A  1 400 ? -1.934  -8.962  23.937  1.00 34.39  ? 400  ALA A N   1 
ATOM   3053  C  CA  . ALA A  1 400 ? -1.192  -9.256  25.159  1.00 34.20  ? 400  ALA A CA  1 
ATOM   3054  C  C   . ALA A  1 400 ? -2.090  -9.316  26.400  1.00 32.80  ? 400  ALA A C   1 
ATOM   3055  O  O   . ALA A  1 400 ? -1.807  -10.042 27.343  1.00 30.80  ? 400  ALA A O   1 
ATOM   3056  C  CB  . ALA A  1 400 ? -0.066  -8.241  25.353  1.00 35.73  ? 400  ALA A CB  1 
ATOM   3057  N  N   . VAL A  1 401 ? -3.169  -8.543  26.401  1.00 28.11  ? 401  VAL A N   1 
ATOM   3058  C  CA  . VAL A  1 401 ? -4.061  -8.519  27.539  1.00 26.21  ? 401  VAL A CA  1 
ATOM   3059  C  C   . VAL A  1 401 ? -4.703  -9.882  27.637  1.00 24.23  ? 401  VAL A C   1 
ATOM   3060  O  O   . VAL A  1 401 ? -4.597  -10.538 28.674  1.00 25.55  ? 401  VAL A O   1 
ATOM   3061  C  CB  . VAL A  1 401 ? -5.124  -7.420  27.416  1.00 26.29  ? 401  VAL A CB  1 
ATOM   3062  C  CG1 . VAL A  1 401 ? -6.080  -7.473  28.591  1.00 25.99  ? 401  VAL A CG1 1 
ATOM   3063  C  CG2 . VAL A  1 401 ? -4.457  -6.075  27.357  1.00 27.45  ? 401  VAL A CG2 1 
ATOM   3064  N  N   . VAL A  1 402 ? -5.333  -10.328 26.549  1.00 24.25  ? 402  VAL A N   1 
ATOM   3065  C  CA  . VAL A  1 402 ? -6.004  -11.629 26.583  1.00 23.35  ? 402  VAL A CA  1 
ATOM   3066  C  C   . VAL A  1 402 ? -5.020  -12.731 26.955  1.00 22.39  ? 402  VAL A C   1 
ATOM   3067  O  O   . VAL A  1 402 ? -5.274  -13.554 27.850  1.00 21.61  ? 402  VAL A O   1 
ATOM   3068  C  CB  . VAL A  1 402 ? -6.645  -11.976 25.244  1.00 23.64  ? 402  VAL A CB  1 
ATOM   3069  C  CG1 . VAL A  1 402 ? -6.962  -13.457 25.183  1.00 22.71  ? 402  VAL A CG1 1 
ATOM   3070  C  CG2 . VAL A  1 402 ? -7.886  -11.145 25.016  1.00 24.51  ? 402  VAL A CG2 1 
ATOM   3071  N  N   . GLY A  1 403 ? -3.876  -12.717 26.283  1.00 28.92  ? 403  GLY A N   1 
ATOM   3072  C  CA  . GLY A  1 403 ? -2.856  -13.726 26.497  1.00 21.84  ? 403  GLY A CA  1 
ATOM   3073  C  C   . GLY A  1 403 ? -2.361  -13.793 27.925  1.00 21.42  ? 403  GLY A C   1 
ATOM   3074  O  O   . GLY A  1 403 ? -2.329  -14.866 28.526  1.00 20.60  ? 403  GLY A O   1 
ATOM   3075  N  N   . ASP A  1 404 ? -1.976  -12.644 28.466  1.00 29.30  ? 404  ASP A N   1 
ATOM   3076  C  CA  . ASP A  1 404 ? -1.497  -12.553 29.838  1.00 35.86  ? 404  ASP A CA  1 
ATOM   3077  C  C   . ASP A  1 404 ? -2.548  -12.993 30.855  1.00 34.53  ? 404  ASP A C   1 
ATOM   3078  O  O   . ASP A  1 404 ? -2.238  -13.695 31.822  1.00 33.49  ? 404  ASP A O   1 
ATOM   3079  C  CB  . ASP A  1 404 ? -1.044  -11.126 30.150  1.00 43.86  ? 404  ASP A CB  1 
ATOM   3080  C  CG  . ASP A  1 404 ? 0.262   -10.772 29.468  1.00 46.30  ? 404  ASP A CG  1 
ATOM   3081  O  OD1 . ASP A  1 404 ? 0.966   -11.718 29.053  1.00 46.61  ? 404  ASP A OD1 1 
ATOM   3082  O  OD2 . ASP A  1 404 ? 0.584   -9.560  29.357  1.00 45.37  ? 404  ASP A OD2 1 
ATOM   3083  N  N   . HIS A  1 405 ? -3.793  -12.591 30.640  1.00 28.73  ? 405  HIS A N   1 
ATOM   3084  C  CA  . HIS A  1 405 ? -4.826  -12.875 31.632  1.00 27.41  ? 405  HIS A CA  1 
ATOM   3085  C  C   . HIS A  1 405 ? -5.233  -14.344 31.672  1.00 25.72  ? 405  HIS A C   1 
ATOM   3086  O  O   . HIS A  1 405 ? -5.464  -14.890 32.758  1.00 24.80  ? 405  HIS A O   1 
ATOM   3087  C  CB  . HIS A  1 405 ? -6.046  -11.973 31.425  1.00 29.72  ? 405  HIS A CB  1 
ATOM   3088  C  CG  . HIS A  1 405 ? -7.214  -12.315 32.301  1.00 29.48  ? 405  HIS A CG  1 
ATOM   3089  N  ND1 . HIS A  1 405 ? -7.069  -12.798 33.583  1.00 29.87  ? 405  HIS A ND1 1 
ATOM   3090  C  CD2 . HIS A  1 405 ? -8.550  -12.233 32.076  1.00 30.65  ? 405  HIS A CD2 1 
ATOM   3091  C  CE1 . HIS A  1 405 ? -8.266  -13.001 34.110  1.00 32.19  ? 405  HIS A CE1 1 
ATOM   3092  N  NE2 . HIS A  1 405 ? -9.181  -12.664 33.217  1.00 31.93  ? 405  HIS A NE2 1 
ATOM   3093  N  N   . ASN A  1 406 ? -5.378  -14.977 30.507  1.00 24.49  ? 406  ASN A N   1 
ATOM   3094  C  CA  . ASN A  1 406 ? -5.791  -16.382 30.521  1.00 23.63  ? 406  ASN A CA  1 
ATOM   3095  C  C   . ASN A  1 406 ? -4.675  -17.418 30.520  1.00 21.53  ? 406  ASN A C   1 
ATOM   3096  O  O   . ASN A  1 406 ? -4.898  -18.577 30.862  1.00 18.17  ? 406  ASN A O   1 
ATOM   3097  C  CB  . ASN A  1 406 ? -6.738  -16.664 29.369  1.00 26.27  ? 406  ASN A CB  1 
ATOM   3098  C  CG  . ASN A  1 406 ? -7.760  -15.577 29.195  1.00 35.18  ? 406  ASN A CG  1 
ATOM   3099  O  OD1 . ASN A  1 406 ? -8.737  -15.494 29.941  1.00 39.54  ? 406  ASN A OD1 1 
ATOM   3100  N  ND2 . ASN A  1 406 ? -7.534  -14.716 28.213  1.00 37.96  ? 406  ASN A ND2 1 
ATOM   3101  N  N   . VAL A  1 407 ? -3.467  -17.015 30.153  1.00 29.55  ? 407  VAL A N   1 
ATOM   3102  C  CA  . VAL A  1 407 ? -2.411  -18.004 30.015  1.00 30.94  ? 407  VAL A CA  1 
ATOM   3103  C  C   . VAL A  1 407 ? -1.097  -17.677 30.721  1.00 34.80  ? 407  VAL A C   1 
ATOM   3104  O  O   . VAL A  1 407 ? -0.708  -18.397 31.641  1.00 39.57  ? 407  VAL A O   1 
ATOM   3105  C  CB  . VAL A  1 407 ? -2.163  -18.395 28.559  1.00 18.70  ? 407  VAL A CB  1 
ATOM   3106  C  CG1 . VAL A  1 407 ? -1.070  -19.428 28.501  1.00 18.24  ? 407  VAL A CG1 1 
ATOM   3107  C  CG2 . VAL A  1 407 ? -3.413  -18.974 27.962  1.00 18.47  ? 407  VAL A CG2 1 
ATOM   3108  N  N   . VAL A  1 408 ? -0.407  -16.617 30.304  1.00 27.57  ? 408  VAL A N   1 
ATOM   3109  C  CA  . VAL A  1 408 ? 0.906   -16.349 30.886  1.00 28.86  ? 408  VAL A CA  1 
ATOM   3110  C  C   . VAL A  1 408 ? 0.888   -16.145 32.409  1.00 27.20  ? 408  VAL A C   1 
ATOM   3111  O  O   . VAL A  1 408 ? 1.589   -16.839 33.137  1.00 28.55  ? 408  VAL A O   1 
ATOM   3112  C  CB  . VAL A  1 408 ? 1.671   -15.222 30.186  1.00 20.62  ? 408  VAL A CB  1 
ATOM   3113  C  CG1 . VAL A  1 408 ? 3.171   -15.426 30.395  1.00 20.86  ? 408  VAL A CG1 1 
ATOM   3114  C  CG2 . VAL A  1 408 ? 1.369   -15.243 28.728  1.00 20.81  ? 408  VAL A CG2 1 
ATOM   3115  N  N   . CYS A  1 409 ? 0.080   -15.229 32.912  1.00 33.82  ? 409  CYS A N   1 
ATOM   3116  C  CA  . CYS A  1 409 ? 0.077   -15.024 34.361  1.00 35.93  ? 409  CYS A CA  1 
ATOM   3117  C  C   . CYS A  1 409 ? -0.380  -16.209 35.250  1.00 33.93  ? 409  CYS A C   1 
ATOM   3118  O  O   . CYS A  1 409 ? 0.183   -16.420 36.326  1.00 36.18  ? 409  CYS A O   1 
ATOM   3119  C  CB  . CYS A  1 409 ? -0.575  -13.694 34.714  1.00 32.74  ? 409  CYS A CB  1 
ATOM   3120  S  SG  . CYS A  1 409 ? 0.456   -12.365 34.059  1.00 31.14  ? 409  CYS A SG  1 
ATOM   3121  N  N   . PRO A  1 410 ? -1.392  -16.980 34.811  1.00 19.09  ? 410  PRO A N   1 
ATOM   3122  C  CA  . PRO A  1 410 ? -1.670  -18.255 35.490  1.00 18.22  ? 410  PRO A CA  1 
ATOM   3123  C  C   . PRO A  1 410 ? -0.567  -19.334 35.405  1.00 17.83  ? 410  PRO A C   1 
ATOM   3124  O  O   . PRO A  1 410 ? -0.394  -20.081 36.380  1.00 17.61  ? 410  PRO A O   1 
ATOM   3125  C  CB  . PRO A  1 410 ? -2.973  -18.736 34.825  1.00 21.17  ? 410  PRO A CB  1 
ATOM   3126  C  CG  . PRO A  1 410 ? -3.213  -17.817 33.666  1.00 20.36  ? 410  PRO A CG  1 
ATOM   3127  C  CD  . PRO A  1 410 ? -2.550  -16.532 34.023  1.00 22.07  ? 410  PRO A CD  1 
ATOM   3128  N  N   . VAL A  1 411 ? 0.150   -19.423 34.282  1.00 18.79  ? 411  VAL A N   1 
ATOM   3129  C  CA  . VAL A  1 411 ? 1.325   -20.313 34.178  1.00 26.42  ? 411  VAL A CA  1 
ATOM   3130  C  C   . VAL A  1 411 ? 2.435   -19.884 35.130  1.00 25.55  ? 411  VAL A C   1 
ATOM   3131  O  O   . VAL A  1 411 ? 3.029   -20.703 35.825  1.00 18.95  ? 411  VAL A O   1 
ATOM   3132  C  CB  . VAL A  1 411 ? 1.906   -20.362 32.752  1.00 17.78  ? 411  VAL A CB  1 
ATOM   3133  C  CG1 . VAL A  1 411 ? 3.230   -21.077 32.738  1.00 17.81  ? 411  VAL A CG1 1 
ATOM   3134  C  CG2 . VAL A  1 411 ? 0.932   -21.040 31.829  1.00 17.34  ? 411  VAL A CG2 1 
ATOM   3135  N  N   . ALA A  1 412 ? 2.703   -18.586 35.159  1.00 24.47  ? 412  ALA A N   1 
ATOM   3136  C  CA  . ALA A  1 412 ? 3.669   -18.026 36.084  1.00 25.26  ? 412  ALA A CA  1 
ATOM   3137  C  C   . ALA A  1 412 ? 3.277   -18.322 37.531  1.00 27.57  ? 412  ALA A C   1 
ATOM   3138  O  O   . ALA A  1 412 ? 4.132   -18.638 38.367  1.00 32.47  ? 412  ALA A O   1 
ATOM   3139  C  CB  . ALA A  1 412 ? 3.788   -16.540 35.866  1.00 20.25  ? 412  ALA A CB  1 
ATOM   3140  N  N   . GLN A  1 413 ? 1.987   -18.223 37.832  1.00 19.11  ? 413  GLN A N   1 
ATOM   3141  C  CA  . GLN A  1 413 ? 1.539   -18.439 39.203  1.00 21.56  ? 413  GLN A CA  1 
ATOM   3142  C  C   . GLN A  1 413 ? 1.685   -19.900 39.599  1.00 19.75  ? 413  GLN A C   1 
ATOM   3143  O  O   . GLN A  1 413 ? 2.157   -20.204 40.697  1.00 18.90  ? 413  GLN A O   1 
ATOM   3144  C  CB  . GLN A  1 413 ? 0.099   -17.987 39.385  1.00 43.67  ? 413  GLN A CB  1 
ATOM   3145  C  CG  . GLN A  1 413 ? -0.349  -17.996 40.817  1.00 54.34  ? 413  GLN A CG  1 
ATOM   3146  C  CD  . GLN A  1 413 ? -1.852  -18.065 40.942  1.00 65.32  ? 413  GLN A CD  1 
ATOM   3147  O  OE1 . GLN A  1 413 ? -2.575  -18.046 39.943  1.00 67.86  ? 413  GLN A OE1 1 
ATOM   3148  N  NE2 . GLN A  1 413 ? -2.336  -18.159 42.175  1.00 70.59  ? 413  GLN A NE2 1 
ATOM   3149  N  N   . LEU A  1 414 ? 1.296   -20.805 38.704  1.00 33.35  ? 414  LEU A N   1 
ATOM   3150  C  CA  . LEU A  1 414 ? 1.453   -22.234 38.980  1.00 33.91  ? 414  LEU A CA  1 
ATOM   3151  C  C   . LEU A  1 414 ? 2.929   -22.628 39.116  1.00 34.15  ? 414  LEU A C   1 
ATOM   3152  O  O   . LEU A  1 414 ? 3.291   -23.454 39.955  1.00 34.19  ? 414  LEU A O   1 
ATOM   3153  C  CB  . LEU A  1 414 ? 0.770   -23.081 37.904  1.00 25.72  ? 414  LEU A CB  1 
ATOM   3154  C  CG  . LEU A  1 414 ? 0.949   -24.587 38.033  1.00 16.48  ? 414  LEU A CG  1 
ATOM   3155  C  CD1 . LEU A  1 414 ? 0.288   -25.057 39.293  1.00 16.51  ? 414  LEU A CD1 1 
ATOM   3156  C  CD2 . LEU A  1 414 ? 0.357   -25.259 36.839  1.00 16.00  ? 414  LEU A CD2 1 
ATOM   3157  N  N   . ALA A  1 415 ? 3.781   -22.036 38.289  1.00 27.22  ? 415  ALA A N   1 
ATOM   3158  C  CA  . ALA A  1 415 ? 5.200   -22.319 38.373  1.00 26.85  ? 415  ALA A CA  1 
ATOM   3159  C  C   . ALA A  1 415 ? 5.708   -21.879 39.733  1.00 33.86  ? 415  ALA A C   1 
ATOM   3160  O  O   . ALA A  1 415 ? 6.285   -22.670 40.472  1.00 38.05  ? 415  ALA A O   1 
ATOM   3161  C  CB  . ALA A  1 415 ? 5.948   -21.612 37.277  1.00 18.83  ? 415  ALA A CB  1 
ATOM   3162  N  N   . GLY A  1 416 ? 5.480   -20.613 40.062  1.00 37.87  ? 416  GLY A N   1 
ATOM   3163  C  CA  . GLY A  1 416 ? 5.953   -20.065 41.317  1.00 39.77  ? 416  GLY A CA  1 
ATOM   3164  C  C   . GLY A  1 416 ? 5.520   -20.882 42.516  1.00 38.70  ? 416  GLY A C   1 
ATOM   3165  O  O   . GLY A  1 416 ? 6.328   -21.166 43.397  1.00 42.05  ? 416  GLY A O   1 
ATOM   3166  N  N   . ARG A  1 417 ? 4.250   -21.278 42.539  1.00 25.09  ? 417  ARG A N   1 
ATOM   3167  C  CA  . ARG A  1 417 ? 3.714   -22.031 43.672  1.00 25.58  ? 417  ARG A CA  1 
ATOM   3168  C  C   . ARG A  1 417 ? 4.233   -23.469 43.751  1.00 22.56  ? 417  ARG A C   1 
ATOM   3169  O  O   . ARG A  1 417 ? 4.553   -23.953 44.836  1.00 19.86  ? 417  ARG A O   1 
ATOM   3170  C  CB  . ARG A  1 417 ? 2.188   -22.012 43.652  1.00 48.76  ? 417  ARG A CB  1 
ATOM   3171  C  CG  . ARG A  1 417 ? 1.636   -20.612 43.642  1.00 61.76  ? 417  ARG A CG  1 
ATOM   3172  C  CD  . ARG A  1 417 ? 0.803   -20.319 44.860  1.00 73.26  ? 417  ARG A CD  1 
ATOM   3173  N  NE  . ARG A  1 417 ? 1.425   -20.800 46.092  1.00 80.86  ? 417  ARG A NE  1 
ATOM   3174  C  CZ  . ARG A  1 417 ? 2.066   -20.027 46.962  1.00 83.63  ? 417  ARG A CZ  1 
ATOM   3175  N  NH1 . ARG A  1 417 ? 2.177   -18.723 46.730  1.00 84.72  ? 417  ARG A NH1 1 
ATOM   3176  N  NH2 . ARG A  1 417 ? 2.587   -20.559 48.062  1.00 83.39  ? 417  ARG A NH2 1 
ATOM   3177  N  N   . LEU A  1 418 ? 4.308   -24.152 42.607  1.00 24.87  ? 418  LEU A N   1 
ATOM   3178  C  CA  . LEU A  1 418 ? 4.809   -25.534 42.563  1.00 24.14  ? 418  LEU A CA  1 
ATOM   3179  C  C   . LEU A  1 418 ? 6.267   -25.554 42.985  1.00 24.11  ? 418  LEU A C   1 
ATOM   3180  O  O   . LEU A  1 418 ? 6.722   -26.483 43.639  1.00 19.55  ? 418  LEU A O   1 
ATOM   3181  C  CB  . LEU A  1 418 ? 4.681   -26.142 41.156  1.00 19.60  ? 418  LEU A CB  1 
ATOM   3182  C  CG  . LEU A  1 418 ? 3.328   -26.614 40.635  1.00 17.19  ? 418  LEU A CG  1 
ATOM   3183  C  CD1 . LEU A  1 418 ? 3.475   -27.198 39.262  1.00 16.73  ? 418  LEU A CD1 1 
ATOM   3184  C  CD2 . LEU A  1 418 ? 2.790   -27.642 41.553  1.00 17.13  ? 418  LEU A CD2 1 
ATOM   3185  N  N   . ALA A  1 419 ? 6.997   -24.518 42.591  1.00 28.73  ? 419  ALA A N   1 
ATOM   3186  C  CA  . ALA A  1 419 ? 8.388   -24.396 42.964  1.00 29.61  ? 419  ALA A CA  1 
ATOM   3187  C  C   . ALA A  1 419 ? 8.471   -24.190 44.467  1.00 32.65  ? 419  ALA A C   1 
ATOM   3188  O  O   . ALA A  1 419 ? 9.176   -24.923 45.157  1.00 36.58  ? 419  ALA A O   1 
ATOM   3189  C  CB  . ALA A  1 419 ? 9.042   -23.252 42.220  1.00 26.32  ? 419  ALA A CB  1 
ATOM   3190  N  N   . ALA A  1 420 ? 7.722   -23.211 44.972  1.00 33.17  ? 420  ALA A N   1 
ATOM   3191  C  CA  . ALA A  1 420 ? 7.744   -22.872 46.397  1.00 34.26  ? 420  ALA A CA  1 
ATOM   3192  C  C   . ALA A  1 420 ? 7.315   -24.056 47.241  1.00 29.28  ? 420  ALA A C   1 
ATOM   3193  O  O   . ALA A  1 420 ? 7.718   -24.205 48.388  1.00 29.99  ? 420  ALA A O   1 
ATOM   3194  C  CB  . ALA A  1 420 ? 6.848   -21.667 46.680  1.00 44.95  ? 420  ALA A CB  1 
ATOM   3195  N  N   . GLN A  1 421 ? 6.512   -24.919 46.650  1.00 22.88  ? 421  GLN A N   1 
ATOM   3196  C  CA  . GLN A  1 421 ? 6.023   -26.090 47.347  1.00 29.05  ? 421  GLN A CA  1 
ATOM   3197  C  C   . GLN A  1 421 ? 7.023   -27.236 47.171  1.00 30.98  ? 421  GLN A C   1 
ATOM   3198  O  O   . GLN A  1 421 ? 6.759   -28.389 47.550  1.00 28.33  ? 421  GLN A O   1 
ATOM   3199  C  CB  . GLN A  1 421 ? 4.628   -26.461 46.850  1.00 42.05  ? 421  GLN A CB  1 
ATOM   3200  C  CG  . GLN A  1 421 ? 3.500   -26.159 47.819  1.00 44.78  ? 421  GLN A CG  1 
ATOM   3201  C  CD  . GLN A  1 421 ? 3.544   -24.761 48.384  1.00 49.39  ? 421  GLN A CD  1 
ATOM   3202  O  OE1 . GLN A  1 421 ? 3.208   -23.792 47.704  1.00 49.51  ? 421  GLN A OE1 1 
ATOM   3203  N  NE2 . GLN A  1 421 ? 3.948   -24.647 49.645  1.00 53.03  ? 421  GLN A NE2 1 
ATOM   3204  N  N   . GLY A  1 422 ? 8.174   -26.901 46.590  1.00 51.52  ? 422  GLY A N   1 
ATOM   3205  C  CA  . GLY A  1 422 ? 9.242   -27.862 46.400  1.00 55.15  ? 422  GLY A CA  1 
ATOM   3206  C  C   . GLY A  1 422 ? 9.047   -28.873 45.291  1.00 53.77  ? 422  GLY A C   1 
ATOM   3207  O  O   . GLY A  1 422 ? 9.069   -30.074 45.521  1.00 58.60  ? 422  GLY A O   1 
ATOM   3208  N  N   . ALA A  1 423 ? 8.809   -28.387 44.084  1.00 38.89  ? 423  ALA A N   1 
ATOM   3209  C  CA  . ALA A  1 423 ? 8.844   -29.251 42.917  1.00 32.98  ? 423  ALA A CA  1 
ATOM   3210  C  C   . ALA A  1 423 ? 9.958   -28.812 41.953  1.00 34.93  ? 423  ALA A C   1 
ATOM   3211  O  O   . ALA A  1 423 ? 10.370  -27.648 41.943  1.00 37.42  ? 423  ALA A O   1 
ATOM   3212  C  CB  . ALA A  1 423 ? 7.509   -29.253 42.230  1.00 18.84  ? 423  ALA A CB  1 
ATOM   3213  N  N   . ARG A  1 424 ? 10.469  -29.750 41.162  1.00 27.30  ? 424  ARG A N   1 
ATOM   3214  C  CA  . ARG A  1 424 ? 11.418  -29.395 40.124  1.00 26.92  ? 424  ARG A CA  1 
ATOM   3215  C  C   . ARG A  1 424 ? 10.575  -28.866 38.991  1.00 24.94  ? 424  ARG A C   1 
ATOM   3216  O  O   . ARG A  1 424 ? 9.697   -29.558 38.483  1.00 26.21  ? 424  ARG A O   1 
ATOM   3217  C  CB  . ARG A  1 424 ? 12.224  -30.621 39.679  1.00 35.10  ? 424  ARG A CB  1 
ATOM   3218  C  CG  . ARG A  1 424 ? 13.411  -30.352 38.718  1.00 81.94  ? 424  ARG A CG  1 
ATOM   3219  C  CD  . ARG A  1 424 ? 14.594  -29.568 39.328  1.00 81.54  ? 424  ARG A CD  1 
ATOM   3220  N  NE  . ARG A  1 424 ? 14.729  -29.734 40.773  1.00 82.77  ? 424  ARG A NE  1 
ATOM   3221  C  CZ  . ARG A  1 424 ? 15.097  -30.864 41.375  1.00 84.59  ? 424  ARG A CZ  1 
ATOM   3222  N  NH1 . ARG A  1 424 ? 15.362  -31.948 40.649  1.00 85.31  ? 424  ARG A NH1 1 
ATOM   3223  N  NH2 . ARG A  1 424 ? 15.184  -30.912 42.704  1.00 84.08  ? 424  ARG A NH2 1 
ATOM   3224  N  N   . VAL A  1 425 ? 10.804  -27.623 38.610  1.00 24.66  ? 425  VAL A N   1 
ATOM   3225  C  CA  . VAL A  1 425 ? 9.992   -27.052 37.561  1.00 24.09  ? 425  VAL A CA  1 
ATOM   3226  C  C   . VAL A  1 425 ? 10.919  -26.573 36.481  1.00 25.28  ? 425  VAL A C   1 
ATOM   3227  O  O   . VAL A  1 425 ? 11.904  -25.904 36.770  1.00 29.00  ? 425  VAL A O   1 
ATOM   3228  C  CB  . VAL A  1 425 ? 9.167   -25.851 38.074  1.00 21.88  ? 425  VAL A CB  1 
ATOM   3229  C  CG1 . VAL A  1 425 ? 8.306   -25.287 36.966  1.00 18.61  ? 425  VAL A CG1 1 
ATOM   3230  C  CG2 . VAL A  1 425 ? 8.313   -26.249 39.263  1.00 18.84  ? 425  VAL A CG2 1 
ATOM   3231  N  N   . TYR A  1 426 ? 10.620  -26.923 35.240  1.00 25.10  ? 426  TYR A N   1 
ATOM   3232  C  CA  . TYR A  1 426 ? 11.285  -26.276 34.124  1.00 27.69  ? 426  TYR A CA  1 
ATOM   3233  C  C   . TYR A  1 426 ? 10.279  -25.415 33.366  1.00 32.44  ? 426  TYR A C   1 
ATOM   3234  O  O   . TYR A  1 426 ? 9.109   -25.776 33.265  1.00 33.71  ? 426  TYR A O   1 
ATOM   3235  C  CB  . TYR A  1 426 ? 11.954  -27.305 33.233  1.00 23.38  ? 426  TYR A CB  1 
ATOM   3236  C  CG  . TYR A  1 426 ? 13.032  -28.058 33.970  1.00 25.93  ? 426  TYR A CG  1 
ATOM   3237  C  CD1 . TYR A  1 426 ? 12.726  -29.170 34.743  1.00 26.28  ? 426  TYR A CD1 1 
ATOM   3238  C  CD2 . TYR A  1 426 ? 14.355  -27.643 33.917  1.00 28.40  ? 426  TYR A CD2 1 
ATOM   3239  C  CE1 . TYR A  1 426 ? 13.710  -29.862 35.418  1.00 27.79  ? 426  TYR A CE1 1 
ATOM   3240  C  CE2 . TYR A  1 426 ? 15.348  -28.326 34.595  1.00 30.96  ? 426  TYR A CE2 1 
ATOM   3241  C  CZ  . TYR A  1 426 ? 15.019  -29.434 35.345  1.00 31.97  ? 426  TYR A CZ  1 
ATOM   3242  O  OH  . TYR A  1 426 ? 16.006  -30.109 36.030  1.00 35.58  ? 426  TYR A OH  1 
ATOM   3243  N  N   . ALA A  1 427 ? 10.726  -24.263 32.865  1.00 32.62  ? 427  ALA A N   1 
ATOM   3244  C  CA  . ALA A  1 427 ? 9.823   -23.308 32.222  1.00 30.20  ? 427  ALA A CA  1 
ATOM   3245  C  C   . ALA A  1 427 ? 10.294  -22.881 30.827  1.00 28.76  ? 427  ALA A C   1 
ATOM   3246  O  O   . ALA A  1 427 ? 11.493  -22.731 30.580  1.00 21.09  ? 427  ALA A O   1 
ATOM   3247  C  CB  . ALA A  1 427 ? 9.620   -22.109 33.109  1.00 20.05  ? 427  ALA A CB  1 
ATOM   3248  N  N   . TYR A  1 428 ? 9.347   -22.696 29.910  1.00 24.23  ? 428  TYR A N   1 
ATOM   3249  C  CA  . TYR A  1 428 ? 9.712   -22.299 28.551  1.00 25.34  ? 428  TYR A CA  1 
ATOM   3250  C  C   . TYR A  1 428 ? 8.783   -21.260 27.929  1.00 27.99  ? 428  TYR A C   1 
ATOM   3251  O  O   . TYR A  1 428 ? 7.576   -21.255 28.162  1.00 28.83  ? 428  TYR A O   1 
ATOM   3252  C  CB  . TYR A  1 428 ? 9.765   -23.520 27.631  1.00 27.86  ? 428  TYR A CB  1 
ATOM   3253  C  CG  . TYR A  1 428 ? 8.402   -24.110 27.305  1.00 28.46  ? 428  TYR A CG  1 
ATOM   3254  C  CD1 . TYR A  1 428 ? 7.646   -23.621 26.254  1.00 25.73  ? 428  TYR A CD1 1 
ATOM   3255  C  CD2 . TYR A  1 428 ? 7.887   -25.168 28.037  1.00 30.01  ? 428  TYR A CD2 1 
ATOM   3256  C  CE1 . TYR A  1 428 ? 6.423   -24.141 25.958  1.00 24.35  ? 428  TYR A CE1 1 
ATOM   3257  C  CE2 . TYR A  1 428 ? 6.664   -25.706 27.733  1.00 28.63  ? 428  TYR A CE2 1 
ATOM   3258  C  CZ  . TYR A  1 428 ? 5.933   -25.180 26.693  1.00 27.52  ? 428  TYR A CZ  1 
ATOM   3259  O  OH  . TYR A  1 428 ? 4.695   -25.692 26.379  1.00 30.44  ? 428  TYR A OH  1 
ATOM   3260  N  N   . ILE A  1 429 ? 9.355   -20.386 27.117  1.00 35.71  ? 429  ILE A N   1 
ATOM   3261  C  CA  . ILE A  1 429 ? 8.549   -19.586 26.211  1.00 35.66  ? 429  ILE A CA  1 
ATOM   3262  C  C   . ILE A  1 429 ? 8.913   -20.089 24.806  1.00 36.40  ? 429  ILE A C   1 
ATOM   3263  O  O   . ILE A  1 429 ? 10.087  -20.143 24.448  1.00 37.72  ? 429  ILE A O   1 
ATOM   3264  C  CB  . ILE A  1 429 ? 8.771   -18.047 26.415  1.00 25.32  ? 429  ILE A CB  1 
ATOM   3265  C  CG1 . ILE A  1 429 ? 8.200   -17.250 25.259  1.00 29.81  ? 429  ILE A CG1 1 
ATOM   3266  C  CG2 . ILE A  1 429 ? 10.225  -17.694 26.444  1.00 23.40  ? 429  ILE A CG2 1 
ATOM   3267  C  CD1 . ILE A  1 429 ? 6.758   -17.463 25.064  1.00 34.18  ? 429  ILE A CD1 1 
ATOM   3268  N  N   . PHE A  1 430 ? 7.910   -20.504 24.036  1.00 25.66  ? 430  PHE A N   1 
ATOM   3269  C  CA  . PHE A  1 430 ? 8.118   -21.029 22.692  1.00 25.48  ? 430  PHE A CA  1 
ATOM   3270  C  C   . PHE A  1 430 ? 7.951   -19.915 21.668  1.00 26.62  ? 430  PHE A C   1 
ATOM   3271  O  O   . PHE A  1 430 ? 6.837   -19.467 21.410  1.00 24.55  ? 430  PHE A O   1 
ATOM   3272  C  CB  . PHE A  1 430 ? 7.093   -22.118 22.413  1.00 21.12  ? 430  PHE A CB  1 
ATOM   3273  C  CG  . PHE A  1 430 ? 7.195   -22.701 21.046  1.00 26.12  ? 430  PHE A CG  1 
ATOM   3274  C  CD1 . PHE A  1 430 ? 8.057   -23.759 20.796  1.00 25.19  ? 430  PHE A CD1 1 
ATOM   3275  C  CD2 . PHE A  1 430 ? 6.435   -22.191 19.996  1.00 26.89  ? 430  PHE A CD2 1 
ATOM   3276  C  CE1 . PHE A  1 430 ? 8.159   -24.302 19.519  1.00 26.98  ? 430  PHE A CE1 1 
ATOM   3277  C  CE2 . PHE A  1 430 ? 6.527   -22.731 18.709  1.00 26.37  ? 430  PHE A CE2 1 
ATOM   3278  C  CZ  . PHE A  1 430 ? 7.386   -23.786 18.470  1.00 26.83  ? 430  PHE A CZ  1 
ATOM   3279  N  N   . GLU A  1 431 ? 9.061   -19.479 21.078  1.00 29.49  ? 431  GLU A N   1 
ATOM   3280  C  CA  . GLU A  1 431 ? 9.065   -18.291 20.225  1.00 30.12  ? 431  GLU A CA  1 
ATOM   3281  C  C   . GLU A  1 431 ? 9.067   -18.480 18.716  1.00 29.71  ? 431  GLU A C   1 
ATOM   3282  O  O   . GLU A  1 431 ? 9.101   -17.494 17.987  1.00 29.57  ? 431  GLU A O   1 
ATOM   3283  C  CB  . GLU A  1 431 ? 10.208  -17.367 20.618  1.00 37.79  ? 431  GLU A CB  1 
ATOM   3284  C  CG  . GLU A  1 431 ? 9.894   -16.511 21.812  1.00 41.64  ? 431  GLU A CG  1 
ATOM   3285  C  CD  . GLU A  1 431 ? 11.133  -15.880 22.392  1.00 48.33  ? 431  GLU A CD  1 
ATOM   3286  O  OE1 . GLU A  1 431 ? 12.161  -16.584 22.480  1.00 50.61  ? 431  GLU A OE1 1 
ATOM   3287  O  OE2 . GLU A  1 431 ? 11.085  -14.684 22.751  1.00 50.98  ? 431  GLU A OE2 1 
ATOM   3288  N  N   . HIS A  1 432 ? 9.054   -19.715 18.232  1.00 36.34  ? 432  HIS A N   1 
ATOM   3289  C  CA  . HIS A  1 432 ? 9.159   -19.921 16.785  1.00 38.67  ? 432  HIS A CA  1 
ATOM   3290  C  C   . HIS A  1 432 ? 7.843   -20.013 16.009  1.00 35.99  ? 432  HIS A C   1 
ATOM   3291  O  O   . HIS A  1 432 ? 7.019   -20.902 16.249  1.00 33.56  ? 432  HIS A O   1 
ATOM   3292  C  CB  . HIS A  1 432 ? 9.993   -21.149 16.451  1.00 41.44  ? 432  HIS A CB  1 
ATOM   3293  C  CG  . HIS A  1 432 ? 9.969   -21.494 14.995  1.00 43.02  ? 432  HIS A CG  1 
ATOM   3294  N  ND1 . HIS A  1 432 ? 10.711  -20.809 14.057  1.00 44.01  ? 432  HIS A ND1 1 
ATOM   3295  C  CD2 . HIS A  1 432 ? 9.260   -22.425 14.311  1.00 42.30  ? 432  HIS A CD2 1 
ATOM   3296  C  CE1 . HIS A  1 432 ? 10.485  -21.326 12.863  1.00 45.21  ? 432  HIS A CE1 1 
ATOM   3297  N  NE2 . HIS A  1 432 ? 9.603   -22.303 12.988  1.00 43.46  ? 432  HIS A NE2 1 
ATOM   3298  N  N   . ARG A  1 433 ? 7.690   -19.113 15.041  1.00 33.29  ? 433  ARG A N   1 
ATOM   3299  C  CA  . ARG A  1 433 ? 6.543   -19.127 14.145  1.00 33.10  ? 433  ARG A CA  1 
ATOM   3300  C  C   . ARG A  1 433 ? 6.738   -20.161 13.035  1.00 36.68  ? 433  ARG A C   1 
ATOM   3301  O  O   . ARG A  1 433 ? 7.761   -20.163 12.365  1.00 38.40  ? 433  ARG A O   1 
ATOM   3302  C  CB  . ARG A  1 433 ? 6.346   -17.740 13.538  1.00 33.62  ? 433  ARG A CB  1 
ATOM   3303  C  CG  . ARG A  1 433 ? 5.169   -17.646 12.596  1.00 34.22  ? 433  ARG A CG  1 
ATOM   3304  C  CD  . ARG A  1 433 ? 4.927   -16.217 12.142  1.00 37.82  ? 433  ARG A CD  1 
ATOM   3305  N  NE  . ARG A  1 433 ? 3.996   -16.189 11.019  1.00 42.02  ? 433  ARG A NE  1 
ATOM   3306  C  CZ  . ARG A  1 433 ? 2.683   -16.022 11.139  1.00 46.54  ? 433  ARG A CZ  1 
ATOM   3307  N  NH1 . ARG A  1 433 ? 2.132   -15.852 12.334  1.00 46.87  ? 433  ARG A NH1 1 
ATOM   3308  N  NH2 . ARG A  1 433 ? 1.916   -16.025 10.060  1.00 49.70  ? 433  ARG A NH2 1 
ATOM   3309  N  N   . ALA A  1 434 ? 5.763   -21.044 12.841  1.00 38.50  ? 434  ALA A N   1 
ATOM   3310  C  CA  . ALA A  1 434 ? 5.879   -22.065 11.806  1.00 38.55  ? 434  ALA A CA  1 
ATOM   3311  C  C   . ALA A  1 434 ? 5.915   -21.459 10.409  1.00 40.72  ? 434  ALA A C   1 
ATOM   3312  O  O   . ALA A  1 434 ? 5.185   -20.517 10.098  1.00 41.11  ? 434  ALA A O   1 
ATOM   3313  C  CB  . ALA A  1 434 ? 4.748   -23.070 11.911  1.00 34.88  ? 434  ALA A CB  1 
ATOM   3314  N  N   . SER A  1 435 ? 6.776   -22.011 9.566   1.00 38.40  ? 435  SER A N   1 
ATOM   3315  C  CA  . SER A  1 435 ? 6.848   -21.587 8.183   1.00 38.93  ? 435  SER A CA  1 
ATOM   3316  C  C   . SER A  1 435 ? 5.553   -21.970 7.470   1.00 42.80  ? 435  SER A C   1 
ATOM   3317  O  O   . SER A  1 435 ? 5.125   -21.279 6.554   1.00 44.96  ? 435  SER A O   1 
ATOM   3318  C  CB  . SER A  1 435 ? 8.074   -22.199 7.487   1.00 36.95  ? 435  SER A CB  1 
ATOM   3319  O  OG  . SER A  1 435 ? 7.801   -23.489 6.963   1.00 32.24  ? 435  SER A OG  1 
ATOM   3320  N  N   . THR A  1 436 ? 4.911   -23.045 7.926   1.00 52.09  ? 436  THR A N   1 
ATOM   3321  C  CA  . THR A  1 436 ? 3.688   -23.560 7.300   1.00 58.91  ? 436  THR A CA  1 
ATOM   3322  C  C   . THR A  1 436 ? 2.464   -22.770 7.755   1.00 56.41  ? 436  THR A C   1 
ATOM   3323  O  O   . THR A  1 436 ? 1.333   -23.062 7.347   1.00 56.61  ? 436  THR A O   1 
ATOM   3324  C  CB  . THR A  1 436 ? 3.452   -25.045 7.668   1.00 77.54  ? 436  THR A CB  1 
ATOM   3325  O  OG1 . THR A  1 436 ? 4.713   -25.704 7.808   1.00 83.91  ? 436  THR A OG1 1 
ATOM   3326  C  CG2 . THR A  1 436 ? 2.604   -25.768 6.609   1.00 77.07  ? 436  THR A CG2 1 
ATOM   3327  N  N   . LEU A  1 437 ? 2.693   -21.774 8.607   1.00 50.90  ? 437  LEU A N   1 
ATOM   3328  C  CA  . LEU A  1 437 ? 1.598   -21.091 9.280   1.00 46.47  ? 437  LEU A CA  1 
ATOM   3329  C  C   . LEU A  1 437 ? 0.680   -20.310 8.341   1.00 49.69  ? 437  LEU A C   1 
ATOM   3330  O  O   . LEU A  1 437 ? 1.133   -19.641 7.416   1.00 52.88  ? 437  LEU A O   1 
ATOM   3331  C  CB  . LEU A  1 437 ? 2.115   -20.208 10.413  1.00 35.36  ? 437  LEU A CB  1 
ATOM   3332  C  CG  . LEU A  1 437 ? 1.196   -20.235 11.635  1.00 33.47  ? 437  LEU A CG  1 
ATOM   3333  C  CD1 . LEU A  1 437 ? 1.991   -20.338 12.933  1.00 33.31  ? 437  LEU A CD1 1 
ATOM   3334  C  CD2 . LEU A  1 437 ? 0.291   -19.015 11.650  1.00 33.37  ? 437  LEU A CD2 1 
ATOM   3335  N  N   . THR A  1 438 ? -0.617  -20.418 8.612   1.00 52.51  ? 438  THR A N   1 
ATOM   3336  C  CA  . THR A  1 438 ? -1.695  -19.863 7.794   1.00 52.78  ? 438  THR A CA  1 
ATOM   3337  C  C   . THR A  1 438 ? -2.132  -18.470 8.247   1.00 51.75  ? 438  THR A C   1 
ATOM   3338  O  O   . THR A  1 438 ? -2.128  -17.525 7.446   1.00 52.62  ? 438  THR A O   1 
ATOM   3339  C  CB  . THR A  1 438 ? -2.891  -20.789 7.796   1.00 56.51  ? 438  THR A CB  1 
ATOM   3340  O  OG1 . THR A  1 438 ? -2.573  -21.946 8.583   1.00 57.55  ? 438  THR A OG1 1 
ATOM   3341  C  CG2 . THR A  1 438 ? -3.222  -21.207 6.373   1.00 56.96  ? 438  THR A CG2 1 
ATOM   3342  N  N   . TRP A  1 439 ? -2.542  -18.379 9.520   1.00 37.77  ? 439  TRP A N   1 
ATOM   3343  C  CA  . TRP A  1 439 ? -2.953  -17.129 10.170  1.00 34.43  ? 439  TRP A CA  1 
ATOM   3344  C  C   . TRP A  1 439 ? -1.952  -16.021 9.877   1.00 36.36  ? 439  TRP A C   1 
ATOM   3345  O  O   . TRP A  1 439 ? -0.753  -16.282 9.771   1.00 34.39  ? 439  TRP A O   1 
ATOM   3346  C  CB  . TRP A  1 439 ? -2.944  -17.289 11.685  1.00 36.08  ? 439  TRP A CB  1 
ATOM   3347  C  CG  . TRP A  1 439 ? -3.822  -18.316 12.244  1.00 35.13  ? 439  TRP A CG  1 
ATOM   3348  C  CD1 . TRP A  1 439 ? -3.451  -19.544 12.693  1.00 32.12  ? 439  TRP A CD1 1 
ATOM   3349  C  CD2 . TRP A  1 439 ? -5.228  -18.204 12.479  1.00 37.56  ? 439  TRP A CD2 1 
ATOM   3350  N  NE1 . TRP A  1 439 ? -4.541  -20.217 13.180  1.00 32.44  ? 439  TRP A NE1 1 
ATOM   3351  C  CE2 . TRP A  1 439 ? -5.648  -19.417 13.062  1.00 35.64  ? 439  TRP A CE2 1 
ATOM   3352  C  CE3 . TRP A  1 439 ? -6.177  -17.199 12.249  1.00 39.39  ? 439  TRP A CE3 1 
ATOM   3353  C  CZ2 . TRP A  1 439 ? -6.987  -19.657 13.420  1.00 35.41  ? 439  TRP A CZ2 1 
ATOM   3354  C  CZ3 . TRP A  1 439 ? -7.512  -17.438 12.609  1.00 38.39  ? 439  TRP A CZ3 1 
ATOM   3355  C  CH2 . TRP A  1 439 ? -7.900  -18.658 13.186  1.00 35.29  ? 439  TRP A CH2 1 
ATOM   3356  N  N   . PRO A  1 440 ? -2.443  -14.770 9.764   1.00 41.80  ? 440  PRO A N   1 
ATOM   3357  C  CA  . PRO A  1 440 ? -1.656  -13.632 9.274   1.00 42.77  ? 440  PRO A CA  1 
ATOM   3358  C  C   . PRO A  1 440 ? -0.447  -13.337 10.142  1.00 40.30  ? 440  PRO A C   1 
ATOM   3359  O  O   . PRO A  1 440 ? -0.178  -14.035 11.118  1.00 37.48  ? 440  PRO A O   1 
ATOM   3360  C  CB  . PRO A  1 440 ? -2.640  -12.469 9.370   1.00 60.68  ? 440  PRO A CB  1 
ATOM   3361  C  CG  . PRO A  1 440 ? -3.589  -12.884 10.452  1.00 60.34  ? 440  PRO A CG  1 
ATOM   3362  C  CD  . PRO A  1 440 ? -3.776  -14.343 10.225  1.00 58.45  ? 440  PRO A CD  1 
ATOM   3363  N  N   . LEU A  1 441 ? 0.289   -12.298 9.787   1.00 50.44  ? 441  LEU A N   1 
ATOM   3364  C  CA  . LEU A  1 441 ? 1.554   -12.050 10.458  1.00 52.48  ? 441  LEU A CA  1 
ATOM   3365  C  C   . LEU A  1 441 ? 1.387   -11.460 11.860  1.00 51.80  ? 441  LEU A C   1 
ATOM   3366  O  O   . LEU A  1 441 ? 2.167   -11.779 12.760  1.00 49.61  ? 441  LEU A O   1 
ATOM   3367  C  CB  . LEU A  1 441 ? 2.454   -11.167 9.588   1.00 57.33  ? 441  LEU A CB  1 
ATOM   3368  C  CG  . LEU A  1 441 ? 3.938   -11.171 9.949   1.00 55.36  ? 441  LEU A CG  1 
ATOM   3369  C  CD1 . LEU A  1 441 ? 4.265   -10.057 10.962  1.00 55.46  ? 441  LEU A CD1 1 
ATOM   3370  C  CD2 . LEU A  1 441 ? 4.337   -12.554 10.468  1.00 51.21  ? 441  LEU A CD2 1 
ATOM   3371  N  N   . TRP A  1 442 ? 0.374   -10.615 12.043  1.00 60.97  ? 442  TRP A N   1 
ATOM   3372  C  CA  . TRP A  1 442 ? 0.201   -9.894  13.302  1.00 60.68  ? 442  TRP A CA  1 
ATOM   3373  C  C   . TRP A  1 442 ? -0.108  -10.797 14.488  1.00 59.50  ? 442  TRP A C   1 
ATOM   3374  O  O   . TRP A  1 442 ? 0.068   -10.391 15.640  1.00 62.70  ? 442  TRP A O   1 
ATOM   3375  C  CB  . TRP A  1 442 ? -0.864  -8.798  13.182  1.00 54.47  ? 442  TRP A CB  1 
ATOM   3376  C  CG  . TRP A  1 442 ? -2.277  -9.289  13.041  1.00 53.82  ? 442  TRP A CG  1 
ATOM   3377  C  CD1 . TRP A  1 442 ? -2.991  -9.384  11.883  1.00 55.95  ? 442  TRP A CD1 1 
ATOM   3378  C  CD2 . TRP A  1 442 ? -3.160  -9.725  14.094  1.00 51.37  ? 442  TRP A CD2 1 
ATOM   3379  N  NE1 . TRP A  1 442 ? -4.257  -9.860  12.143  1.00 55.92  ? 442  TRP A NE1 1 
ATOM   3380  C  CE2 . TRP A  1 442 ? -4.387  -10.078 13.492  1.00 52.55  ? 442  TRP A CE2 1 
ATOM   3381  C  CE3 . TRP A  1 442 ? -3.032  -9.853  15.482  1.00 48.34  ? 442  TRP A CE3 1 
ATOM   3382  C  CZ2 . TRP A  1 442 ? -5.478  -10.554 14.226  1.00 49.18  ? 442  TRP A CZ2 1 
ATOM   3383  C  CZ3 . TRP A  1 442 ? -4.114  -10.329 16.209  1.00 47.22  ? 442  TRP A CZ3 1 
ATOM   3384  C  CH2 . TRP A  1 442 ? -5.321  -10.671 15.578  1.00 47.45  ? 442  TRP A CH2 1 
ATOM   3385  N  N   . MET A  1 443 ? -0.561  -12.016 14.205  1.00 46.17  ? 443  MET A N   1 
ATOM   3386  C  CA  . MET A  1 443 ? -0.939  -12.966 15.250  1.00 40.63  ? 443  MET A CA  1 
ATOM   3387  C  C   . MET A  1 443 ? 0.248   -13.704 15.866  1.00 41.25  ? 443  MET A C   1 
ATOM   3388  O  O   . MET A  1 443 ? 0.072   -14.484 16.807  1.00 41.60  ? 443  MET A O   1 
ATOM   3389  C  CB  . MET A  1 443 ? -1.934  -13.979 14.713  1.00 30.84  ? 443  MET A CB  1 
ATOM   3390  C  CG  . MET A  1 443 ? -3.089  -13.344 14.006  1.00 29.14  ? 443  MET A CG  1 
ATOM   3391  S  SD  . MET A  1 443 ? -4.356  -14.571 13.695  1.00 47.26  ? 443  MET A SD  1 
ATOM   3392  C  CE  . MET A  1 443 ? -4.552  -15.249 15.339  1.00 26.88  ? 443  MET A CE  1 
ATOM   3393  N  N   . GLY A  1 444 ? 1.442   -13.470 15.316  1.00 40.20  ? 444  GLY A N   1 
ATOM   3394  C  CA  . GLY A  1 444 ? 2.688   -13.958 15.892  1.00 38.08  ? 444  GLY A CA  1 
ATOM   3395  C  C   . GLY A  1 444 ? 2.872   -15.465 15.927  1.00 34.89  ? 444  GLY A C   1 
ATOM   3396  O  O   . GLY A  1 444 ? 2.835   -16.140 14.903  1.00 34.76  ? 444  GLY A O   1 
ATOM   3397  N  N   . VAL A  1 445 ? 3.086   -15.986 17.126  1.00 29.33  ? 445  VAL A N   1 
ATOM   3398  C  CA  . VAL A  1 445 ? 3.230   -17.414 17.334  1.00 24.91  ? 445  VAL A CA  1 
ATOM   3399  C  C   . VAL A  1 445 ? 2.054   -17.804 18.198  1.00 25.60  ? 445  VAL A C   1 
ATOM   3400  O  O   . VAL A  1 445 ? 2.193   -17.948 19.417  1.00 23.24  ? 445  VAL A O   1 
ATOM   3401  C  CB  . VAL A  1 445 ? 4.516   -17.736 18.106  1.00 27.42  ? 445  VAL A CB  1 
ATOM   3402  C  CG1 . VAL A  1 445 ? 4.774   -19.223 18.116  1.00 27.56  ? 445  VAL A CG1 1 
ATOM   3403  C  CG2 . VAL A  1 445 ? 5.689   -17.010 17.502  1.00 28.70  ? 445  VAL A CG2 1 
ATOM   3404  N  N   . PRO A  1 446 ? 0.881   -17.968 17.563  1.00 33.02  ? 446  PRO A N   1 
ATOM   3405  C  CA  . PRO A  1 446 ? -0.399  -18.114 18.259  1.00 32.66  ? 446  PRO A CA  1 
ATOM   3406  C  C   . PRO A  1 446 ? -0.540  -19.425 19.021  1.00 30.57  ? 446  PRO A C   1 
ATOM   3407  O  O   . PRO A  1 446 ? 0.219   -20.377 18.837  1.00 29.75  ? 446  PRO A O   1 
ATOM   3408  C  CB  . PRO A  1 446 ? -1.429  -18.023 17.133  1.00 23.96  ? 446  PRO A CB  1 
ATOM   3409  C  CG  . PRO A  1 446 ? -0.722  -18.501 15.948  1.00 24.57  ? 446  PRO A CG  1 
ATOM   3410  C  CD  . PRO A  1 446 ? 0.727   -18.107 16.106  1.00 24.84  ? 446  PRO A CD  1 
ATOM   3411  N  N   . HIS A  1 447 ? -1.535  -19.430 19.894  1.00 26.59  ? 447  HIS A N   1 
ATOM   3412  C  CA  . HIS A  1 447 ? -1.796  -20.493 20.838  1.00 23.95  ? 447  HIS A CA  1 
ATOM   3413  C  C   . HIS A  1 447 ? -1.937  -21.807 20.119  1.00 26.51  ? 447  HIS A C   1 
ATOM   3414  O  O   . HIS A  1 447 ? -2.740  -21.924 19.201  1.00 31.25  ? 447  HIS A O   1 
ATOM   3415  C  CB  . HIS A  1 447 ? -3.110  -20.166 21.516  1.00 22.80  ? 447  HIS A CB  1 
ATOM   3416  C  CG  . HIS A  1 447 ? -3.419  -21.030 22.685  1.00 26.21  ? 447  HIS A CG  1 
ATOM   3417  N  ND1 . HIS A  1 447 ? -2.515  -21.257 23.697  1.00 28.42  ? 447  HIS A ND1 1 
ATOM   3418  C  CD2 . HIS A  1 447 ? -4.547  -21.697 23.024  1.00 29.07  ? 447  HIS A CD2 1 
ATOM   3419  C  CE1 . HIS A  1 447 ? -3.068  -22.042 24.606  1.00 30.55  ? 447  HIS A CE1 1 
ATOM   3420  N  NE2 . HIS A  1 447 ? -4.299  -22.326 24.220  1.00 30.95  ? 447  HIS A NE2 1 
ATOM   3421  N  N   . GLY A  1 448 ? -1.154  -22.798 20.527  1.00 24.82  ? 448  GLY A N   1 
ATOM   3422  C  CA  . GLY A  1 448 ? -1.281  -24.143 19.985  1.00 22.99  ? 448  GLY A CA  1 
ATOM   3423  C  C   . GLY A  1 448 ? -0.314  -24.562 18.892  1.00 22.05  ? 448  GLY A C   1 
ATOM   3424  O  O   . GLY A  1 448 ? -0.313  -25.720 18.480  1.00 21.64  ? 448  GLY A O   1 
ATOM   3425  N  N   . TYR A  1 449 ? 0.517   -23.634 18.431  1.00 27.69  ? 449  TYR A N   1 
ATOM   3426  C  CA  . TYR A  1 449 ? 1.359   -23.893 17.270  1.00 32.27  ? 449  TYR A CA  1 
ATOM   3427  C  C   . TYR A  1 449 ? 2.753   -24.398 17.581  1.00 35.76  ? 449  TYR A C   1 
ATOM   3428  O  O   . TYR A  1 449 ? 3.580   -24.531 16.692  1.00 42.29  ? 449  TYR A O   1 
ATOM   3429  C  CB  . TYR A  1 449 ? 1.325   -22.721 16.284  1.00 38.92  ? 449  TYR A CB  1 
ATOM   3430  C  CG  . TYR A  1 449 ? -0.038  -22.685 15.657  1.00 45.48  ? 449  TYR A CG  1 
ATOM   3431  C  CD1 . TYR A  1 449 ? -1.129  -22.209 16.374  1.00 48.54  ? 449  TYR A CD1 1 
ATOM   3432  C  CD2 . TYR A  1 449 ? -0.264  -23.216 14.398  1.00 49.32  ? 449  TYR A CD2 1 
ATOM   3433  C  CE1 . TYR A  1 449 ? -2.402  -22.213 15.842  1.00 51.04  ? 449  TYR A CE1 1 
ATOM   3434  C  CE2 . TYR A  1 449 ? -1.544  -23.224 13.853  1.00 53.35  ? 449  TYR A CE2 1 
ATOM   3435  C  CZ  . TYR A  1 449 ? -2.609  -22.717 14.585  1.00 52.91  ? 449  TYR A CZ  1 
ATOM   3436  O  OH  . TYR A  1 449 ? -3.889  -22.709 14.076  1.00 53.45  ? 449  TYR A OH  1 
ATOM   3437  N  N   . GLU A  1 450 ? 3.018   -24.675 18.848  1.00 31.59  ? 450  GLU A N   1 
ATOM   3438  C  CA  . GLU A  1 450 ? 4.227   -25.396 19.194  1.00 31.94  ? 450  GLU A CA  1 
ATOM   3439  C  C   . GLU A  1 450 ? 3.929   -26.886 19.181  1.00 33.80  ? 450  GLU A C   1 
ATOM   3440  O  O   . GLU A  1 450 ? 4.850   -27.701 19.201  1.00 37.09  ? 450  GLU A O   1 
ATOM   3441  C  CB  . GLU A  1 450 ? 4.721   -24.986 20.582  1.00 27.90  ? 450  GLU A CB  1 
ATOM   3442  C  CG  . GLU A  1 450 ? 4.102   -25.743 21.752  1.00 27.39  ? 450  GLU A CG  1 
ATOM   3443  C  CD  . GLU A  1 450 ? 2.625   -25.449 21.957  1.00 26.73  ? 450  GLU A CD  1 
ATOM   3444  O  OE1 . GLU A  1 450 ? 2.007   -24.811 21.085  1.00 24.96  ? 450  GLU A OE1 1 
ATOM   3445  O  OE2 . GLU A  1 450 ? 2.074   -25.864 22.998  1.00 28.26  ? 450  GLU A OE2 1 
ATOM   3446  N  N   . ILE A  1 451 ? 2.646   -27.247 19.141  1.00 29.84  ? 451  ILE A N   1 
ATOM   3447  C  CA  . ILE A  1 451 ? 2.268   -28.652 19.289  1.00 27.68  ? 451  ILE A CA  1 
ATOM   3448  C  C   . ILE A  1 451 ? 2.885   -29.494 18.197  1.00 28.14  ? 451  ILE A C   1 
ATOM   3449  O  O   . ILE A  1 451 ? 3.556   -30.484 18.479  1.00 29.28  ? 451  ILE A O   1 
ATOM   3450  C  CB  . ILE A  1 451 ? 0.753   -28.882 19.253  1.00 23.33  ? 451  ILE A CB  1 
ATOM   3451  C  CG1 . ILE A  1 451 ? 0.093   -28.360 20.527  1.00 18.19  ? 451  ILE A CG1 1 
ATOM   3452  C  CG2 . ILE A  1 451 ? 0.452   -30.369 19.087  1.00 18.63  ? 451  ILE A CG2 1 
ATOM   3453  C  CD1 . ILE A  1 451 ? -1.283  -28.960 20.763  1.00 17.85  ? 451  ILE A CD1 1 
ATOM   3454  N  N   . GLU A  1 452 ? 2.668   -29.077 16.954  1.00 27.28  ? 452  GLU A N   1 
ATOM   3455  C  CA  . GLU A  1 452 ? 3.157   -29.806 15.789  1.00 29.82  ? 452  GLU A CA  1 
ATOM   3456  C  C   . GLU A  1 452 ? 4.676   -29.928 15.775  1.00 25.79  ? 452  GLU A C   1 
ATOM   3457  O  O   . GLU A  1 452 ? 5.216   -30.838 15.161  1.00 23.82  ? 452  GLU A O   1 
ATOM   3458  C  CB  . GLU A  1 452 ? 2.683   -29.134 14.508  1.00 41.72  ? 452  GLU A CB  1 
ATOM   3459  C  CG  . GLU A  1 452 ? 3.488   -27.919 14.152  1.00 48.84  ? 452  GLU A CG  1 
ATOM   3460  C  CD  . GLU A  1 452 ? 2.694   -26.930 13.349  1.00 55.74  ? 452  GLU A CD  1 
ATOM   3461  O  OE1 . GLU A  1 452 ? 1.446   -26.943 13.450  1.00 54.73  ? 452  GLU A OE1 1 
ATOM   3462  O  OE2 . GLU A  1 452 ? 3.325   -26.137 12.618  1.00 61.88  ? 452  GLU A OE2 1 
ATOM   3463  N  N   . PHE A  1 453 ? 5.363   -29.006 16.440  1.00 27.53  ? 453  PHE A N   1 
ATOM   3464  C  CA  . PHE A  1 453 ? 6.806   -29.112 16.589  1.00 31.46  ? 453  PHE A CA  1 
ATOM   3465  C  C   . PHE A  1 453 ? 7.197   -30.061 17.711  1.00 31.81  ? 453  PHE A C   1 
ATOM   3466  O  O   . PHE A  1 453 ? 8.308   -30.579 17.716  1.00 32.52  ? 453  PHE A O   1 
ATOM   3467  C  CB  . PHE A  1 453 ? 7.451   -27.745 16.815  1.00 38.66  ? 453  PHE A CB  1 
ATOM   3468  C  CG  . PHE A  1 453 ? 7.519   -26.906 15.587  1.00 41.70  ? 453  PHE A CG  1 
ATOM   3469  C  CD1 . PHE A  1 453 ? 6.433   -26.139 15.197  1.00 44.54  ? 453  PHE A CD1 1 
ATOM   3470  C  CD2 . PHE A  1 453 ? 8.662   -26.888 14.813  1.00 42.43  ? 453  PHE A CD2 1 
ATOM   3471  C  CE1 . PHE A  1 453 ? 6.486   -25.362 14.057  1.00 48.07  ? 453  PHE A CE1 1 
ATOM   3472  C  CE2 . PHE A  1 453 ? 8.722   -26.117 13.670  1.00 46.83  ? 453  PHE A CE2 1 
ATOM   3473  C  CZ  . PHE A  1 453 ? 7.632   -25.349 13.291  1.00 49.50  ? 453  PHE A CZ  1 
ATOM   3474  N  N   . ILE A  1 454 ? 6.297   -30.273 18.668  1.00 39.43  ? 454  ILE A N   1 
ATOM   3475  C  CA  . ILE A  1 454 ? 6.566   -31.204 19.759  1.00 36.82  ? 454  ILE A CA  1 
ATOM   3476  C  C   . ILE A  1 454 ? 6.406   -32.639 19.277  1.00 37.46  ? 454  ILE A C   1 
ATOM   3477  O  O   . ILE A  1 454 ? 7.209   -33.510 19.601  1.00 39.69  ? 454  ILE A O   1 
ATOM   3478  C  CB  . ILE A  1 454 ? 5.658   -30.946 20.971  1.00 24.45  ? 454  ILE A CB  1 
ATOM   3479  C  CG1 . ILE A  1 454 ? 6.072   -29.647 21.669  1.00 21.59  ? 454  ILE A CG1 1 
ATOM   3480  C  CG2 . ILE A  1 454 ? 5.738   -32.107 21.956  1.00 22.29  ? 454  ILE A CG2 1 
ATOM   3481  C  CD1 . ILE A  1 454 ? 7.487   -29.694 22.213  1.00 19.40  ? 454  ILE A CD1 1 
ATOM   3482  N  N   . PHE A  1 455 ? 5.387   -32.874 18.461  1.00 28.08  ? 455  PHE A N   1 
ATOM   3483  C  CA  . PHE A  1 455 ? 5.128   -34.208 17.945  1.00 27.79  ? 455  PHE A CA  1 
ATOM   3484  C  C   . PHE A  1 455 ? 6.008   -34.530 16.758  1.00 31.91  ? 455  PHE A C   1 
ATOM   3485  O  O   . PHE A  1 455 ? 5.920   -35.618 16.201  1.00 34.38  ? 455  PHE A O   1 
ATOM   3486  C  CB  . PHE A  1 455 ? 3.665   -34.365 17.544  1.00 28.07  ? 455  PHE A CB  1 
ATOM   3487  C  CG  . PHE A  1 455 ? 2.747   -34.642 18.696  1.00 25.50  ? 455  PHE A CG  1 
ATOM   3488  C  CD1 . PHE A  1 455 ? 2.339   -33.624 19.534  1.00 24.25  ? 455  PHE A CD1 1 
ATOM   3489  C  CD2 . PHE A  1 455 ? 2.281   -35.915 18.930  1.00 24.55  ? 455  PHE A CD2 1 
ATOM   3490  C  CE1 . PHE A  1 455 ? 1.490   -33.877 20.590  1.00 23.82  ? 455  PHE A CE1 1 
ATOM   3491  C  CE2 . PHE A  1 455 ? 1.433   -36.168 19.989  1.00 25.00  ? 455  PHE A CE2 1 
ATOM   3492  C  CZ  . PHE A  1 455 ? 1.036   -35.152 20.820  1.00 23.86  ? 455  PHE A CZ  1 
ATOM   3493  N  N   . GLY A  1 456 ? 6.843   -33.582 16.358  1.00 39.42  ? 456  GLY A N   1 
ATOM   3494  C  CA  . GLY A  1 456 ? 7.820   -33.840 15.316  1.00 42.28  ? 456  GLY A CA  1 
ATOM   3495  C  C   . GLY A  1 456 ? 7.254   -34.045 13.923  1.00 42.29  ? 456  GLY A C   1 
ATOM   3496  O  O   . GLY A  1 456 ? 7.797   -34.813 13.130  1.00 44.31  ? 456  GLY A O   1 
ATOM   3497  N  N   . LEU A  1 457 ? 6.159   -33.357 13.634  1.00 23.13  ? 457  LEU A N   1 
ATOM   3498  C  CA  . LEU A  1 457 ? 5.599   -33.304 12.298  1.00 23.99  ? 457  LEU A CA  1 
ATOM   3499  C  C   . LEU A  1 457 ? 6.522   -32.767 11.196  1.00 25.26  ? 457  LEU A C   1 
ATOM   3500  O  O   . LEU A  1 457 ? 6.364   -33.173 10.038  1.00 26.17  ? 457  LEU A O   1 
ATOM   3501  C  CB  . LEU A  1 457 ? 4.295   -32.533 12.296  1.00 23.70  ? 457  LEU A CB  1 
ATOM   3502  C  CG  . LEU A  1 457 ? 3.083   -33.420 12.495  1.00 23.18  ? 457  LEU A CG  1 
ATOM   3503  C  CD1 . LEU A  1 457 ? 3.102   -33.992 13.887  1.00 22.06  ? 457  LEU A CD1 1 
ATOM   3504  C  CD2 . LEU A  1 457 ? 1.817   -32.628 12.252  1.00 23.22  ? 457  LEU A CD2 1 
ATOM   3505  N  N   . PRO A  1 458 ? 7.432   -31.807 11.514  1.00 41.34  ? 458  PRO A N   1 
ATOM   3506  C  CA  . PRO A  1 458 ? 8.451   -31.403 10.529  1.00 41.75  ? 458  PRO A CA  1 
ATOM   3507  C  C   . PRO A  1 458 ? 9.372   -32.525 10.072  1.00 44.76  ? 458  PRO A C   1 
ATOM   3508  O  O   . PRO A  1 458 ? 10.047  -32.369 9.051   1.00 48.10  ? 458  PRO A O   1 
ATOM   3509  C  CB  . PRO A  1 458 ? 9.274   -30.363 11.286  1.00 26.68  ? 458  PRO A CB  1 
ATOM   3510  C  CG  . PRO A  1 458 ? 8.306   -29.725 12.161  1.00 25.64  ? 458  PRO A CG  1 
ATOM   3511  C  CD  . PRO A  1 458 ? 7.370   -30.828 12.616  1.00 28.05  ? 458  PRO A CD  1 
ATOM   3512  N  N   . LEU A  1 459 ? 9.411   -33.627 10.816  1.00 33.36  ? 459  LEU A N   1 
ATOM   3513  C  CA  . LEU A  1 459 ? 10.203  -34.774 10.418  1.00 33.89  ? 459  LEU A CA  1 
ATOM   3514  C  C   . LEU A  1 459 ? 9.571   -35.499 9.233   1.00 39.38  ? 459  LEU A C   1 
ATOM   3515  O  O   . LEU A  1 459 ? 10.219  -36.331 8.588   1.00 43.44  ? 459  LEU A O   1 
ATOM   3516  C  CB  . LEU A  1 459 ? 10.442  -35.708 11.597  1.00 26.40  ? 459  LEU A CB  1 
ATOM   3517  C  CG  . LEU A  1 459 ? 11.738  -35.326 12.320  1.00 26.53  ? 459  LEU A CG  1 
ATOM   3518  C  CD1 . LEU A  1 459 ? 11.560  -34.087 13.183  1.00 25.83  ? 459  LEU A CD1 1 
ATOM   3519  C  CD2 . LEU A  1 459 ? 12.290  -36.463 13.151  1.00 26.18  ? 459  LEU A CD2 1 
ATOM   3520  N  N   . ASP A  1 460 ? 8.311   -35.170 8.945   1.00 45.21  ? 460  ASP A N   1 
ATOM   3521  C  CA  . ASP A  1 460 ? 7.642   -35.631 7.739   1.00 48.27  ? 460  ASP A CA  1 
ATOM   3522  C  C   . ASP A  1 460 ? 7.968   -34.684 6.596   1.00 56.66  ? 460  ASP A C   1 
ATOM   3523  O  O   . ASP A  1 460 ? 7.544   -33.524 6.609   1.00 62.05  ? 460  ASP A O   1 
ATOM   3524  C  CB  . ASP A  1 460 ? 6.140   -35.643 7.942   1.00 48.13  ? 460  ASP A CB  1 
ATOM   3525  C  CG  . ASP A  1 460 ? 5.410   -36.285 6.788   1.00 53.56  ? 460  ASP A CG  1 
ATOM   3526  O  OD1 . ASP A  1 460 ? 6.047   -36.541 5.744   1.00 54.36  ? 460  ASP A OD1 1 
ATOM   3527  O  OD2 . ASP A  1 460 ? 4.193   -36.544 6.916   1.00 57.10  ? 460  ASP A OD2 1 
ATOM   3528  N  N   . PRO A  1 461 ? 8.698   -35.186 5.588   1.00 61.59  ? 461  PRO A N   1 
ATOM   3529  C  CA  . PRO A  1 461 ? 9.163   -34.425 4.419   1.00 61.90  ? 461  PRO A CA  1 
ATOM   3530  C  C   . PRO A  1 461 ? 8.020   -33.896 3.556   1.00 63.18  ? 461  PRO A C   1 
ATOM   3531  O  O   . PRO A  1 461 ? 8.084   -32.774 3.053   1.00 66.46  ? 461  PRO A O   1 
ATOM   3532  C  CB  . PRO A  1 461 ? 9.959   -35.462 3.631   1.00 56.99  ? 461  PRO A CB  1 
ATOM   3533  C  CG  . PRO A  1 461 ? 9.379   -36.775 4.049   1.00 57.56  ? 461  PRO A CG  1 
ATOM   3534  C  CD  . PRO A  1 461 ? 9.078   -36.605 5.501   1.00 55.77  ? 461  PRO A CD  1 
ATOM   3535  N  N   . SER A  1 462 ? 6.973   -34.698 3.409   1.00 48.47  ? 462  SER A N   1 
ATOM   3536  C  CA  . SER A  1 462 ? 5.815   -34.329 2.605   1.00 48.26  ? 462  SER A CA  1 
ATOM   3537  C  C   . SER A  1 462 ? 5.040   -33.118 3.140   1.00 46.83  ? 462  SER A C   1 
ATOM   3538  O  O   . SER A  1 462 ? 4.084   -32.677 2.508   1.00 46.75  ? 462  SER A O   1 
ATOM   3539  C  CB  . SER A  1 462 ? 4.864   -35.521 2.474   1.00 62.22  ? 462  SER A CB  1 
ATOM   3540  O  OG  . SER A  1 462 ? 4.186   -35.783 3.694   1.00 62.47  ? 462  SER A OG  1 
ATOM   3541  N  N   . LEU A  1 463 ? 5.417   -32.600 4.308   1.00 64.66  ? 463  LEU A N   1 
ATOM   3542  C  CA  . LEU A  1 463 ? 4.637   -31.530 4.934   1.00 65.18  ? 463  LEU A CA  1 
ATOM   3543  C  C   . LEU A  1 463 ? 5.094   -30.093 4.686   1.00 68.06  ? 463  LEU A C   1 
ATOM   3544  O  O   . LEU A  1 463 ? 4.444   -29.151 5.159   1.00 69.80  ? 463  LEU A O   1 
ATOM   3545  C  CB  . LEU A  1 463 ? 4.464   -31.790 6.428   1.00 48.65  ? 463  LEU A CB  1 
ATOM   3546  C  CG  . LEU A  1 463 ? 3.422   -32.880 6.656   1.00 46.76  ? 463  LEU A CG  1 
ATOM   3547  C  CD1 . LEU A  1 463 ? 2.931   -32.851 8.093   1.00 47.22  ? 463  LEU A CD1 1 
ATOM   3548  C  CD2 . LEU A  1 463 ? 2.258   -32.749 5.661   1.00 44.75  ? 463  LEU A CD2 1 
ATOM   3549  N  N   . ASN A  1 464 ? 6.182   -29.936 3.931   1.00 55.01  ? 464  ASN A N   1 
ATOM   3550  C  CA  . ASN A  1 464 ? 6.713   -28.623 3.537   1.00 51.52  ? 464  ASN A CA  1 
ATOM   3551  C  C   . ASN A  1 464 ? 7.320   -27.757 4.667   1.00 47.12  ? 464  ASN A C   1 
ATOM   3552  O  O   . ASN A  1 464 ? 7.328   -26.532 4.576   1.00 46.69  ? 464  ASN A O   1 
ATOM   3553  C  CB  . ASN A  1 464 ? 5.657   -27.803 2.749   1.00 77.35  ? 464  ASN A CB  1 
ATOM   3554  C  CG  . ASN A  1 464 ? 5.161   -28.510 1.479   1.00 78.34  ? 464  ASN A CG  1 
ATOM   3555  O  OD1 . ASN A  1 464 ? 5.874   -29.324 0.886   1.00 81.10  ? 464  ASN A OD1 1 
ATOM   3556  N  ND2 . ASN A  1 464 ? 3.935   -28.186 1.056   1.00 75.28  ? 464  ASN A ND2 1 
ATOM   3557  N  N   . TYR A  1 465 ? 7.823   -28.378 5.731   1.00 40.90  ? 465  TYR A N   1 
ATOM   3558  C  CA  . TYR A  1 465 ? 8.604   -27.631 6.722   1.00 38.67  ? 465  TYR A CA  1 
ATOM   3559  C  C   . TYR A  1 465 ? 10.011  -27.409 6.184   1.00 39.11  ? 465  TYR A C   1 
ATOM   3560  O  O   . TYR A  1 465 ? 10.442  -28.112 5.271   1.00 36.09  ? 465  TYR A O   1 
ATOM   3561  C  CB  . TYR A  1 465 ? 8.665   -28.350 8.074   1.00 41.13  ? 465  TYR A CB  1 
ATOM   3562  C  CG  . TYR A  1 465 ? 7.359   -28.339 8.817   1.00 42.60  ? 465  TYR A CG  1 
ATOM   3563  C  CD1 . TYR A  1 465 ? 6.393   -29.315 8.573   1.00 44.27  ? 465  TYR A CD1 1 
ATOM   3564  C  CD2 . TYR A  1 465 ? 7.079   -27.352 9.756   1.00 43.01  ? 465  TYR A CD2 1 
ATOM   3565  C  CE1 . TYR A  1 465 ? 5.187   -29.311 9.241   1.00 44.05  ? 465  TYR A CE1 1 
ATOM   3566  C  CE2 . TYR A  1 465 ? 5.869   -27.336 10.434  1.00 42.70  ? 465  TYR A CE2 1 
ATOM   3567  C  CZ  . TYR A  1 465 ? 4.932   -28.319 10.166  1.00 44.65  ? 465  TYR A CZ  1 
ATOM   3568  O  OH  . TYR A  1 465 ? 3.730   -28.316 10.819  1.00 47.37  ? 465  TYR A OH  1 
ATOM   3569  N  N   . THR A  1 466 ? 10.707  -26.414 6.730   1.00 48.27  ? 466  THR A N   1 
ATOM   3570  C  CA  . THR A  1 466 ? 12.110  -26.174 6.399   1.00 50.81  ? 466  THR A CA  1 
ATOM   3571  C  C   . THR A  1 466 ? 13.032  -27.050 7.225   1.00 52.55  ? 466  THR A C   1 
ATOM   3572  O  O   . THR A  1 466 ? 12.743  -27.354 8.377   1.00 51.45  ? 466  THR A O   1 
ATOM   3573  C  CB  . THR A  1 466 ? 12.514  -24.727 6.660   1.00 47.79  ? 466  THR A CB  1 
ATOM   3574  O  OG1 . THR A  1 466 ? 12.667  -24.519 8.067   1.00 45.77  ? 466  THR A OG1 1 
ATOM   3575  C  CG2 . THR A  1 466 ? 11.457  -23.799 6.138   1.00 50.27  ? 466  THR A CG2 1 
ATOM   3576  N  N   . THR A  1 467 ? 14.153  -27.431 6.633   1.00 51.96  ? 467  THR A N   1 
ATOM   3577  C  CA  . THR A  1 467 ? 15.136  -28.275 7.295   1.00 56.06  ? 467  THR A CA  1 
ATOM   3578  C  C   . THR A  1 467 ? 15.587  -27.739 8.672   1.00 57.35  ? 467  THR A C   1 
ATOM   3579  O  O   . THR A  1 467 ? 15.902  -28.523 9.576   1.00 59.21  ? 467  THR A O   1 
ATOM   3580  C  CB  . THR A  1 467 ? 16.336  -28.521 6.363   1.00 66.84  ? 467  THR A CB  1 
ATOM   3581  O  OG1 . THR A  1 467 ? 16.761  -27.275 5.794   1.00 70.82  ? 467  THR A OG1 1 
ATOM   3582  C  CG2 . THR A  1 467 ? 15.924  -29.442 5.230   1.00 66.71  ? 467  THR A CG2 1 
ATOM   3583  N  N   . GLU A  1 468 ? 15.589  -26.416 8.839   1.00 54.80  ? 468  GLU A N   1 
ATOM   3584  C  CA  . GLU A  1 468 ? 15.927  -25.805 10.131  1.00 54.84  ? 468  GLU A CA  1 
ATOM   3585  C  C   . GLU A  1 468 ? 14.849  -26.143 11.154  1.00 46.71  ? 468  GLU A C   1 
ATOM   3586  O  O   . GLU A  1 468 ? 15.138  -26.456 12.313  1.00 43.79  ? 468  GLU A O   1 
ATOM   3587  C  CB  . GLU A  1 468 ? 16.096  -24.281 10.014  1.00 81.93  ? 468  GLU A CB  1 
ATOM   3588  C  CG  . GLU A  1 468 ? 17.268  -23.834 9.144   1.00 93.95  ? 468  GLU A CG  1 
ATOM   3589  C  CD  . GLU A  1 468 ? 16.950  -23.875 7.648   1.00 103.68 ? 468  GLU A CD  1 
ATOM   3590  O  OE1 . GLU A  1 468 ? 15.804  -23.532 7.279   1.00 107.59 ? 468  GLU A OE1 1 
ATOM   3591  O  OE2 . GLU A  1 468 ? 17.841  -24.250 6.844   1.00 104.92 ? 468  GLU A OE2 1 
ATOM   3592  N  N   . GLU A  1 469 ? 13.601  -26.084 10.704  1.00 48.38  ? 469  GLU A N   1 
ATOM   3593  C  CA  . GLU A  1 469 ? 12.468  -26.459 11.528  1.00 44.59  ? 469  GLU A CA  1 
ATOM   3594  C  C   . GLU A  1 469 ? 12.497  -27.948 11.834  1.00 44.72  ? 469  GLU A C   1 
ATOM   3595  O  O   . GLU A  1 469 ? 12.039  -28.382 12.885  1.00 44.73  ? 469  GLU A O   1 
ATOM   3596  C  CB  . GLU A  1 469 ? 11.166  -26.111 10.813  1.00 37.98  ? 469  GLU A CB  1 
ATOM   3597  C  CG  . GLU A  1 469 ? 10.906  -24.630 10.716  1.00 37.74  ? 469  GLU A CG  1 
ATOM   3598  C  CD  . GLU A  1 469 ? 9.694   -24.310 9.870   1.00 36.99  ? 469  GLU A CD  1 
ATOM   3599  O  OE1 . GLU A  1 469 ? 9.688   -24.690 8.681   1.00 36.88  ? 469  GLU A OE1 1 
ATOM   3600  O  OE2 . GLU A  1 469 ? 8.752   -23.681 10.401  1.00 36.78  ? 469  GLU A OE2 1 
ATOM   3601  N  N   . ARG A  1 470 ? 13.025  -28.735 10.906  1.00 38.36  ? 470  ARG A N   1 
ATOM   3602  C  CA  . ARG A  1 470 ? 13.073  -30.170 11.100  1.00 36.27  ? 470  ARG A CA  1 
ATOM   3603  C  C   . ARG A  1 470 ? 14.049  -30.456 12.226  1.00 34.27  ? 470  ARG A C   1 
ATOM   3604  O  O   . ARG A  1 470 ? 13.707  -31.159 13.187  1.00 37.02  ? 470  ARG A O   1 
ATOM   3605  C  CB  . ARG A  1 470 ? 13.485  -30.871 9.811   1.00 52.73  ? 470  ARG A CB  1 
ATOM   3606  C  CG  . ARG A  1 470 ? 13.224  -32.353 9.802   1.00 59.28  ? 470  ARG A CG  1 
ATOM   3607  C  CD  . ARG A  1 470 ? 14.502  -33.131 10.026  1.00 66.60  ? 470  ARG A CD  1 
ATOM   3608  N  NE  . ARG A  1 470 ? 15.506  -32.824 9.013   1.00 73.57  ? 470  ARG A NE  1 
ATOM   3609  C  CZ  . ARG A  1 470 ? 16.772  -33.228 9.072   1.00 80.27  ? 470  ARG A CZ  1 
ATOM   3610  N  NH1 . ARG A  1 470 ? 17.192  -33.962 10.097  1.00 80.20  ? 470  ARG A NH1 1 
ATOM   3611  N  NH2 . ARG A  1 470 ? 17.620  -32.895 8.107   1.00 85.78  ? 470  ARG A NH2 1 
ATOM   3612  N  N   . ILE A  1 471 ? 15.249  -29.883 12.127  1.00 36.36  ? 471  ILE A N   1 
ATOM   3613  C  CA  . ILE A  1 471 ? 16.259  -30.031 13.180  1.00 36.03  ? 471  ILE A CA  1 
ATOM   3614  C  C   . ILE A  1 471 ? 15.699  -29.562 14.521  1.00 35.05  ? 471  ILE A C   1 
ATOM   3615  O  O   . ILE A  1 471 ? 15.828  -30.247 15.546  1.00 35.99  ? 471  ILE A O   1 
ATOM   3616  C  CB  . ILE A  1 471 ? 17.539  -29.208 12.870  1.00 39.86  ? 471  ILE A CB  1 
ATOM   3617  C  CG1 . ILE A  1 471 ? 18.190  -29.672 11.568  1.00 40.99  ? 471  ILE A CG1 1 
ATOM   3618  C  CG2 . ILE A  1 471 ? 18.547  -29.293 14.020  1.00 38.77  ? 471  ILE A CG2 1 
ATOM   3619  C  CD1 . ILE A  1 471 ? 19.191  -28.673 11.014  1.00 42.96  ? 471  ILE A CD1 1 
ATOM   3620  N  N   . PHE A  1 472 ? 15.074  -28.389 14.491  1.00 33.88  ? 472  PHE A N   1 
ATOM   3621  C  CA  . PHE A  1 472 ? 14.488  -27.771 15.673  1.00 33.65  ? 472  PHE A CA  1 
ATOM   3622  C  C   . PHE A  1 472 ? 13.520  -28.734 16.343  1.00 32.45  ? 472  PHE A C   1 
ATOM   3623  O  O   . PHE A  1 472 ? 13.593  -28.948 17.560  1.00 32.45  ? 472  PHE A O   1 
ATOM   3624  C  CB  . PHE A  1 472 ? 13.770  -26.487 15.249  1.00 36.78  ? 472  PHE A CB  1 
ATOM   3625  C  CG  . PHE A  1 472 ? 13.027  -25.785 16.357  1.00 36.21  ? 472  PHE A CG  1 
ATOM   3626  C  CD1 . PHE A  1 472 ? 13.656  -25.450 17.534  1.00 35.67  ? 472  PHE A CD1 1 
ATOM   3627  C  CD2 . PHE A  1 472 ? 11.701  -25.417 16.187  1.00 36.54  ? 472  PHE A CD2 1 
ATOM   3628  C  CE1 . PHE A  1 472 ? 12.969  -24.784 18.524  1.00 35.39  ? 472  PHE A CE1 1 
ATOM   3629  C  CE2 . PHE A  1 472 ? 11.009  -24.756 17.177  1.00 35.30  ? 472  PHE A CE2 1 
ATOM   3630  C  CZ  . PHE A  1 472 ? 11.642  -24.436 18.344  1.00 35.18  ? 472  PHE A CZ  1 
ATOM   3631  N  N   . ALA A  1 473 ? 12.637  -29.322 15.527  1.00 27.27  ? 473  ALA A N   1 
ATOM   3632  C  CA  . ALA A  1 473 ? 11.595  -30.248 15.974  1.00 24.98  ? 473  ALA A CA  1 
ATOM   3633  C  C   . ALA A  1 473 ? 12.209  -31.447 16.665  1.00 27.65  ? 473  ALA A C   1 
ATOM   3634  O  O   . ALA A  1 473 ? 11.753  -31.845 17.736  1.00 24.97  ? 473  ALA A O   1 
ATOM   3635  C  CB  . ALA A  1 473 ? 10.755  -30.696 14.809  1.00 24.63  ? 473  ALA A CB  1 
ATOM   3636  N  N   . GLN A  1 474 ? 13.248  -32.018 16.050  1.00 47.99  ? 474  GLN A N   1 
ATOM   3637  C  CA  . GLN A  1 474 ? 14.051  -33.062 16.703  1.00 48.09  ? 474  GLN A CA  1 
ATOM   3638  C  C   . GLN A  1 474 ? 14.516  -32.639 18.087  1.00 44.37  ? 474  GLN A C   1 
ATOM   3639  O  O   . GLN A  1 474 ? 14.371  -33.389 19.056  1.00 43.47  ? 474  GLN A O   1 
ATOM   3640  C  CB  . GLN A  1 474 ? 15.283  -33.396 15.872  1.00 43.14  ? 474  GLN A CB  1 
ATOM   3641  C  CG  . GLN A  1 474 ? 14.972  -34.096 14.586  1.00 47.52  ? 474  GLN A CG  1 
ATOM   3642  C  CD  . GLN A  1 474 ? 16.219  -34.455 13.830  1.00 51.99  ? 474  GLN A CD  1 
ATOM   3643  O  OE1 . GLN A  1 474 ? 17.017  -33.581 13.480  1.00 53.74  ? 474  GLN A OE1 1 
ATOM   3644  N  NE2 . GLN A  1 474 ? 16.409  -35.752 13.580  1.00 53.02  ? 474  GLN A NE2 1 
ATOM   3645  N  N   . ARG A  1 475 ? 15.078  -31.434 18.163  1.00 29.02  ? 475  ARG A N   1 
ATOM   3646  C  CA  . ARG A  1 475 ? 15.599  -30.907 19.419  1.00 26.84  ? 475  ARG A CA  1 
ATOM   3647  C  C   . ARG A  1 475 ? 14.525  -30.811 20.502  1.00 26.07  ? 475  ARG A C   1 
ATOM   3648  O  O   . ARG A  1 475 ? 14.767  -31.164 21.665  1.00 28.01  ? 475  ARG A O   1 
ATOM   3649  C  CB  . ARG A  1 475 ? 16.268  -29.550 19.203  1.00 34.75  ? 475  ARG A CB  1 
ATOM   3650  C  CG  . ARG A  1 475 ? 16.992  -29.025 20.433  1.00 38.19  ? 475  ARG A CG  1 
ATOM   3651  C  CD  . ARG A  1 475 ? 17.918  -27.878 20.064  1.00 43.51  ? 475  ARG A CD  1 
ATOM   3652  N  NE  . ARG A  1 475 ? 17.601  -26.638 20.773  1.00 46.60  ? 475  ARG A NE  1 
ATOM   3653  C  CZ  . ARG A  1 475 ? 17.164  -25.522 20.186  1.00 46.90  ? 475  ARG A CZ  1 
ATOM   3654  N  NH1 . ARG A  1 475 ? 16.985  -25.478 18.865  1.00 46.13  ? 475  ARG A NH1 1 
ATOM   3655  N  NH2 . ARG A  1 475 ? 16.914  -24.444 20.927  1.00 45.36  ? 475  ARG A NH2 1 
ATOM   3656  N  N   . LEU A  1 476 ? 13.341  -30.335 20.129  1.00 26.98  ? 476  LEU A N   1 
ATOM   3657  C  CA  . LEU A  1 476 ? 12.225  -30.325 21.064  1.00 22.92  ? 476  LEU A CA  1 
ATOM   3658  C  C   . LEU A  1 476 ? 11.890  -31.755 21.512  1.00 22.80  ? 476  LEU A C   1 
ATOM   3659  O  O   . LEU A  1 476 ? 11.824  -32.024 22.712  1.00 23.04  ? 476  LEU A O   1 
ATOM   3660  C  CB  . LEU A  1 476 ? 11.004  -29.632 20.459  1.00 21.62  ? 476  LEU A CB  1 
ATOM   3661  C  CG  . LEU A  1 476 ? 11.174  -28.126 20.293  1.00 22.13  ? 476  LEU A CG  1 
ATOM   3662  C  CD1 . LEU A  1 476 ? 9.944   -27.496 19.688  1.00 21.92  ? 476  LEU A CD1 1 
ATOM   3663  C  CD2 . LEU A  1 476 ? 11.483  -27.512 21.629  1.00 21.85  ? 476  LEU A CD2 1 
ATOM   3664  N  N   . MET A  1 477 ? 11.710  -32.671 20.560  1.00 21.53  ? 477  MET A N   1 
ATOM   3665  C  CA  . MET A  1 477 ? 11.397  -34.061 20.894  1.00 21.09  ? 477  MET A CA  1 
ATOM   3666  C  C   . MET A  1 477 ? 12.366  -34.612 21.916  1.00 28.97  ? 477  MET A C   1 
ATOM   3667  O  O   . MET A  1 477 ? 11.946  -35.196 22.909  1.00 20.56  ? 477  MET A O   1 
ATOM   3668  C  CB  . MET A  1 477 ? 11.390  -34.942 19.654  1.00 21.64  ? 477  MET A CB  1 
ATOM   3669  C  CG  . MET A  1 477 ? 10.160  -34.756 18.797  1.00 21.42  ? 477  MET A CG  1 
ATOM   3670  S  SD  . MET A  1 477 ? 10.370  -35.438 17.149  1.00 34.59  ? 477  MET A SD  1 
ATOM   3671  C  CE  . MET A  1 477 ? 10.312  -37.189 17.512  1.00 36.31  ? 477  MET A CE  1 
ATOM   3672  N  N   . LYS A  1 478 ? 13.659  -34.394 21.685  1.00 31.79  ? 478  LYS A N   1 
ATOM   3673  C  CA  . LYS A  1 478 ? 14.677  -34.775 22.666  1.00 34.93  ? 478  LYS A CA  1 
ATOM   3674  C  C   . LYS A  1 478 ? 14.494  -34.111 24.033  1.00 33.74  ? 478  LYS A C   1 
ATOM   3675  O  O   . LYS A  1 478 ? 14.687  -34.773 25.049  1.00 32.72  ? 478  LYS A O   1 
ATOM   3676  C  CB  . LYS A  1 478 ? 16.098  -34.554 22.143  1.00 52.15  ? 478  LYS A CB  1 
ATOM   3677  C  CG  . LYS A  1 478 ? 16.699  -35.779 21.464  1.00 59.51  ? 478  LYS A CG  1 
ATOM   3678  C  CD  . LYS A  1 478 ? 18.215  -35.830 21.625  1.00 64.80  ? 478  LYS A CD  1 
ATOM   3679  C  CE  . LYS A  1 478 ? 18.670  -37.156 22.238  1.00 66.98  ? 478  LYS A CE  1 
ATOM   3680  N  NZ  . LYS A  1 478 ? 18.306  -38.347 21.399  1.00 67.14  ? 478  LYS A NZ  1 
ATOM   3681  N  N   . TYR A  1 479 ? 14.120  -32.827 24.068  1.00 40.80  ? 479  TYR A N   1 
ATOM   3682  C  CA  . TYR A  1 479 ? 13.831  -32.171 25.355  1.00 37.83  ? 479  TYR A CA  1 
ATOM   3683  C  C   . TYR A  1 479 ? 12.717  -32.891 26.088  1.00 34.81  ? 479  TYR A C   1 
ATOM   3684  O  O   . TYR A  1 479 ? 12.860  -33.241 27.260  1.00 37.12  ? 479  TYR A O   1 
ATOM   3685  C  CB  . TYR A  1 479 ? 13.402  -30.712 25.185  1.00 30.52  ? 479  TYR A CB  1 
ATOM   3686  C  CG  . TYR A  1 479 ? 14.507  -29.752 24.836  1.00 30.48  ? 479  TYR A CG  1 
ATOM   3687  C  CD1 . TYR A  1 479 ? 15.767  -29.870 25.404  1.00 30.97  ? 479  TYR A CD1 1 
ATOM   3688  C  CD2 . TYR A  1 479 ? 14.292  -28.722 23.921  1.00 31.57  ? 479  TYR A CD2 1 
ATOM   3689  C  CE1 . TYR A  1 479 ? 16.794  -28.984 25.065  1.00 33.00  ? 479  TYR A CE1 1 
ATOM   3690  C  CE2 . TYR A  1 479 ? 15.306  -27.826 23.585  1.00 32.73  ? 479  TYR A CE2 1 
ATOM   3691  C  CZ  . TYR A  1 479 ? 16.554  -27.963 24.158  1.00 31.66  ? 479  TYR A CZ  1 
ATOM   3692  O  OH  . TYR A  1 479 ? 17.558  -27.084 23.822  1.00 28.67  ? 479  TYR A OH  1 
ATOM   3693  N  N   . TRP A  1 480 ? 11.607  -33.102 25.384  1.00 19.89  ? 480  TRP A N   1 
ATOM   3694  C  CA  . TRP A  1 480 ? 10.388  -33.632 25.991  1.00 18.78  ? 480  TRP A CA  1 
ATOM   3695  C  C   . TRP A  1 480 ? 10.547  -35.061 26.454  1.00 19.54  ? 480  TRP A C   1 
ATOM   3696  O  O   . TRP A  1 480 ? 10.165  -35.399 27.565  1.00 18.29  ? 480  TRP A O   1 
ATOM   3697  C  CB  . TRP A  1 480 ? 9.216   -33.548 25.021  1.00 18.44  ? 480  TRP A CB  1 
ATOM   3698  C  CG  . TRP A  1 480 ? 8.261   -32.461 25.333  1.00 18.42  ? 480  TRP A CG  1 
ATOM   3699  C  CD1 . TRP A  1 480 ? 6.953   -32.604 25.660  1.00 17.33  ? 480  TRP A CD1 1 
ATOM   3700  C  CD2 . TRP A  1 480 ? 8.533   -31.048 25.348  1.00 21.08  ? 480  TRP A CD2 1 
ATOM   3701  N  NE1 . TRP A  1 480 ? 6.387   -31.371 25.880  1.00 19.59  ? 480  TRP A NE1 1 
ATOM   3702  C  CE2 . TRP A  1 480 ? 7.340   -30.401 25.696  1.00 20.69  ? 480  TRP A CE2 1 
ATOM   3703  C  CE3 . TRP A  1 480 ? 9.670   -30.270 25.098  1.00 24.66  ? 480  TRP A CE3 1 
ATOM   3704  C  CZ2 . TRP A  1 480 ? 7.251   -29.006 25.804  1.00 20.63  ? 480  TRP A CZ2 1 
ATOM   3705  C  CZ3 . TRP A  1 480 ? 9.577   -28.884 25.207  1.00 19.16  ? 480  TRP A CZ3 1 
ATOM   3706  C  CH2 . TRP A  1 480 ? 8.381   -28.272 25.558  1.00 19.36  ? 480  TRP A CH2 1 
ATOM   3707  N  N   . THR A  1 481 ? 11.104  -35.909 25.602  1.00 36.96  ? 481  THR A N   1 
ATOM   3708  C  CA  . THR A  1 481 ? 11.315  -37.292 25.991  1.00 37.47  ? 481  THR A CA  1 
ATOM   3709  C  C   . THR A  1 481 ? 12.426  -37.406 27.037  1.00 37.00  ? 481  THR A C   1 
ATOM   3710  O  O   . THR A  1 481 ? 12.433  -38.342 27.839  1.00 38.87  ? 481  THR A O   1 
ATOM   3711  C  CB  . THR A  1 481 ? 11.617  -38.173 24.785  1.00 25.94  ? 481  THR A CB  1 
ATOM   3712  O  OG1 . THR A  1 481 ? 12.892  -37.808 24.236  1.00 24.92  ? 481  THR A OG1 1 
ATOM   3713  C  CG2 . THR A  1 481 ? 10.514  -38.017 23.745  1.00 19.56  ? 481  THR A CG2 1 
ATOM   3714  N  N   . ASN A  1 482 ? 13.357  -36.456 27.039  1.00 20.31  ? 482  ASN A N   1 
ATOM   3715  C  CA  . ASN A  1 482 ? 14.273  -36.353 28.167  1.00 20.74  ? 482  ASN A CA  1 
ATOM   3716  C  C   . ASN A  1 482 ? 13.545  -36.061 29.466  1.00 20.07  ? 482  ASN A C   1 
ATOM   3717  O  O   . ASN A  1 482 ? 13.801  -36.695 30.479  1.00 20.20  ? 482  ASN A O   1 
ATOM   3718  C  CB  . ASN A  1 482 ? 15.355  -35.306 27.941  1.00 27.55  ? 482  ASN A CB  1 
ATOM   3719  C  CG  . ASN A  1 482 ? 16.457  -35.812 27.066  1.00 31.55  ? 482  ASN A CG  1 
ATOM   3720  O  OD1 . ASN A  1 482 ? 16.634  -37.019 26.927  1.00 34.15  ? 482  ASN A OD1 1 
ATOM   3721  N  ND2 . ASN A  1 482 ? 17.195  -34.902 26.448  1.00 33.14  ? 482  ASN A ND2 1 
ATOM   3722  N  N   . PHE A  1 483 ? 12.640  -35.094 29.448  1.00 25.14  ? 483  PHE A N   1 
ATOM   3723  C  CA  . PHE A  1 483 ? 11.905  -34.793 30.659  1.00 26.55  ? 483  PHE A CA  1 
ATOM   3724  C  C   . PHE A  1 483 ? 11.096  -35.997 31.093  1.00 29.84  ? 483  PHE A C   1 
ATOM   3725  O  O   . PHE A  1 483 ? 11.025  -36.312 32.276  1.00 33.95  ? 483  PHE A O   1 
ATOM   3726  C  CB  . PHE A  1 483 ? 10.968  -33.630 30.456  1.00 21.70  ? 483  PHE A CB  1 
ATOM   3727  C  CG  . PHE A  1 483 ? 10.111  -33.359 31.644  1.00 21.63  ? 483  PHE A CG  1 
ATOM   3728  C  CD1 . PHE A  1 483 ? 10.672  -32.868 32.812  1.00 23.00  ? 483  PHE A CD1 1 
ATOM   3729  C  CD2 . PHE A  1 483 ? 8.750   -33.600 31.605  1.00 22.61  ? 483  PHE A CD2 1 
ATOM   3730  C  CE1 . PHE A  1 483 ? 9.883   -32.611 33.917  1.00 25.74  ? 483  PHE A CE1 1 
ATOM   3731  C  CE2 . PHE A  1 483 ? 7.959   -33.344 32.699  1.00 25.65  ? 483  PHE A CE2 1 
ATOM   3732  C  CZ  . PHE A  1 483 ? 8.523   -32.845 33.860  1.00 26.68  ? 483  PHE A CZ  1 
ATOM   3733  N  N   . ALA A  1 484 ? 10.494  -36.660 30.111  1.00 21.72  ? 484  ALA A N   1 
ATOM   3734  C  CA  . ALA A  1 484 ? 9.675   -37.842 30.326  1.00 20.39  ? 484  ALA A CA  1 
ATOM   3735  C  C   . ALA A  1 484 ? 10.461  -38.920 31.045  1.00 22.07  ? 484  ALA A C   1 
ATOM   3736  O  O   . ALA A  1 484 ? 9.994   -39.497 32.034  1.00 21.76  ? 484  ALA A O   1 
ATOM   3737  C  CB  . ALA A  1 484 ? 9.188   -38.367 29.003  1.00 17.77  ? 484  ALA A CB  1 
ATOM   3738  N  N   . ARG A  1 485 ? 11.653  -39.188 30.519  1.00 25.80  ? 485  ARG A N   1 
ATOM   3739  C  CA  . ARG A  1 485 ? 12.523  -40.247 31.017  1.00 28.37  ? 485  ARG A CA  1 
ATOM   3740  C  C   . ARG A  1 485 ? 13.189  -39.919 32.357  1.00 22.62  ? 485  ARG A C   1 
ATOM   3741  O  O   . ARG A  1 485 ? 13.068  -40.669 33.312  1.00 20.47  ? 485  ARG A O   1 
ATOM   3742  C  CB  . ARG A  1 485 ? 13.584  -40.549 29.957  1.00 53.64  ? 485  ARG A CB  1 
ATOM   3743  C  CG  . ARG A  1 485 ? 14.335  -41.844 30.141  1.00 63.39  ? 485  ARG A CG  1 
ATOM   3744  C  CD  . ARG A  1 485 ? 15.353  -42.037 29.021  1.00 71.21  ? 485  ARG A CD  1 
ATOM   3745  N  NE  . ARG A  1 485 ? 16.460  -41.084 29.108  1.00 77.38  ? 485  ARG A NE  1 
ATOM   3746  C  CZ  . ARG A  1 485 ? 16.683  -40.091 28.248  1.00 78.99  ? 485  ARG A CZ  1 
ATOM   3747  N  NH1 . ARG A  1 485 ? 15.872  -39.903 27.206  1.00 78.31  ? 485  ARG A NH1 1 
ATOM   3748  N  NH2 . ARG A  1 485 ? 17.727  -39.286 28.432  1.00 78.93  ? 485  ARG A NH2 1 
ATOM   3749  N  N   . THR A  1 486 ? 13.910  -38.807 32.406  1.00 27.59  ? 486  THR A N   1 
ATOM   3750  C  CA  . THR A  1 486 ? 14.702  -38.432 33.579  1.00 28.86  ? 486  THR A CA  1 
ATOM   3751  C  C   . THR A  1 486 ? 14.136  -37.355 34.515  1.00 27.46  ? 486  THR A C   1 
ATOM   3752  O  O   . THR A  1 486 ? 14.755  -37.053 35.537  1.00 26.91  ? 486  THR A O   1 
ATOM   3753  C  CB  . THR A  1 486 ? 16.119  -38.003 33.150  1.00 34.25  ? 486  THR A CB  1 
ATOM   3754  O  OG1 . THR A  1 486 ? 16.133  -36.612 32.813  1.00 33.20  ? 486  THR A OG1 1 
ATOM   3755  C  CG2 . THR A  1 486 ? 16.549  -38.795 31.934  1.00 38.89  ? 486  THR A CG2 1 
ATOM   3756  N  N   . GLY A  1 487 ? 12.993  -36.762 34.174  1.00 28.89  ? 487  GLY A N   1 
ATOM   3757  C  CA  . GLY A  1 487 ? 12.507  -35.601 34.906  1.00 30.27  ? 487  GLY A CA  1 
ATOM   3758  C  C   . GLY A  1 487 ? 13.253  -34.296 34.628  1.00 34.62  ? 487  GLY A C   1 
ATOM   3759  O  O   . GLY A  1 487 ? 12.987  -33.278 35.258  1.00 38.04  ? 487  GLY A O   1 
ATOM   3760  N  N   . ASP A  1 488 ? 14.190  -34.318 33.687  1.00 31.94  ? 488  ASP A N   1 
ATOM   3761  C  CA  . ASP A  1 488 ? 14.970  -33.136 33.334  1.00 36.70  ? 488  ASP A CA  1 
ATOM   3762  C  C   . ASP A  1 488 ? 14.981  -33.046 31.808  1.00 40.86  ? 488  ASP A C   1 
ATOM   3763  O  O   . ASP A  1 488 ? 15.212  -34.049 31.136  1.00 47.00  ? 488  ASP A O   1 
ATOM   3764  C  CB  . ASP A  1 488 ? 16.395  -33.339 33.875  1.00 46.19  ? 488  ASP A CB  1 
ATOM   3765  C  CG  . ASP A  1 488 ? 17.339  -32.173 33.583  1.00 51.90  ? 488  ASP A CG  1 
ATOM   3766  O  OD1 . ASP A  1 488 ? 17.136  -31.445 32.594  1.00 55.18  ? 488  ASP A OD1 1 
ATOM   3767  O  OD2 . ASP A  1 488 ? 18.321  -32.001 34.346  1.00 51.94  ? 488  ASP A OD2 1 
ATOM   3768  N  N   . PRO A  1 489 ? 14.774  -31.840 31.246  1.00 41.67  ? 489  PRO A N   1 
ATOM   3769  C  CA  . PRO A  1 489 ? 14.743  -31.744 29.784  1.00 40.02  ? 489  PRO A CA  1 
ATOM   3770  C  C   . PRO A  1 489 ? 16.122  -31.903 29.193  1.00 42.40  ? 489  PRO A C   1 
ATOM   3771  O  O   . PRO A  1 489 ? 16.235  -32.137 27.991  1.00 45.28  ? 489  PRO A O   1 
ATOM   3772  C  CB  . PRO A  1 489 ? 14.246  -30.318 29.525  1.00 37.98  ? 489  PRO A CB  1 
ATOM   3773  C  CG  . PRO A  1 489 ? 13.638  -29.872 30.799  1.00 38.72  ? 489  PRO A CG  1 
ATOM   3774  C  CD  . PRO A  1 489 ? 14.404  -30.566 31.882  1.00 39.49  ? 489  PRO A CD  1 
ATOM   3775  N  N   . ASN A  1 490 ? 17.150  -31.753 30.024  1.00 33.43  ? 490  ASN A N   1 
ATOM   3776  C  CA  . ASN A  1 490 ? 18.525  -31.665 29.540  1.00 37.05  ? 490  ASN A CA  1 
ATOM   3777  C  C   . ASN A  1 490 ? 19.072  -32.946 28.972  1.00 42.31  ? 490  ASN A C   1 
ATOM   3778  O  O   . ASN A  1 490 ? 18.714  -34.037 29.428  1.00 43.08  ? 490  ASN A O   1 
ATOM   3779  C  CB  . ASN A  1 490 ? 19.459  -31.178 30.643  1.00 42.49  ? 490  ASN A CB  1 
ATOM   3780  C  CG  . ASN A  1 490 ? 19.467  -29.683 30.759  1.00 41.68  ? 490  ASN A CG  1 
ATOM   3781  O  OD1 . ASN A  1 490 ? 19.581  -28.992 29.756  1.00 42.17  ? 490  ASN A OD1 1 
ATOM   3782  N  ND2 . ASN A  1 490 ? 19.324  -29.169 31.976  1.00 40.54  ? 490  ASN A ND2 1 
ATOM   3783  N  N   . ASP A  1 491 ? 19.937  -32.795 27.970  0.88 35.42  ? 491  ASP A N   1 
ATOM   3784  C  CA  . ASP A  1 491 ? 20.701  -33.912 27.425  0.88 41.37  ? 491  ASP A CA  1 
ATOM   3785  C  C   . ASP A  1 491 ? 21.684  -34.324 28.504  0.88 41.11  ? 491  ASP A C   1 
ATOM   3786  O  O   . ASP A  1 491 ? 22.481  -33.507 28.953  0.88 37.43  ? 491  ASP A O   1 
ATOM   3787  C  CB  . ASP A  1 491 ? 21.393  -33.523 26.112  0.88 79.80  ? 491  ASP A CB  1 
ATOM   3788  C  CG  . ASP A  1 491 ? 20.451  -33.610 24.909  0.88 87.45  ? 491  ASP A CG  1 
ATOM   3789  O  OD1 . ASP A  1 491 ? 20.191  -34.742 24.431  0.88 90.11  ? 491  ASP A OD1 1 
ATOM   3790  O  OD2 . ASP A  1 491 ? 19.960  -32.553 24.448  0.88 89.05  ? 491  ASP A OD2 1 
ATOM   3791  N  N   . PRO A  1 492 ? 21.566  -35.576 28.982  1.00 58.72  ? 492  PRO A N   1 
ATOM   3792  C  CA  . PRO A  1 492 ? 22.246  -36.043 30.201  1.00 65.86  ? 492  PRO A CA  1 
ATOM   3793  C  C   . PRO A  1 492 ? 23.775  -36.150 30.106  1.00 75.09  ? 492  PRO A C   1 
ATOM   3794  O  O   . PRO A  1 492 ? 24.503  -35.660 30.981  1.00 72.27  ? 492  PRO A O   1 
ATOM   3795  C  CB  . PRO A  1 492 ? 21.615  -37.421 30.439  1.00 69.73  ? 492  PRO A CB  1 
ATOM   3796  C  CG  . PRO A  1 492 ? 21.222  -37.895 29.078  1.00 67.84  ? 492  PRO A CG  1 
ATOM   3797  C  CD  . PRO A  1 492 ? 20.876  -36.670 28.272  1.00 65.99  ? 492  PRO A CD  1 
ATOM   3798  N  N   . ARG A  1 493 ? 24.251  -36.764 29.029  1.00 110.92 ? 493  ARG A N   1 
ATOM   3799  C  CA  . ARG A  1 493 ? 25.679  -36.936 28.825  1.00 121.94 ? 493  ARG A CA  1 
ATOM   3800  C  C   . ARG A  1 493 ? 26.284  -35.562 28.578  1.00 127.88 ? 493  ARG A C   1 
ATOM   3801  O  O   . ARG A  1 493 ? 27.195  -35.122 29.283  1.00 131.01 ? 493  ARG A O   1 
ATOM   3802  C  CB  . ARG A  1 493 ? 25.943  -37.868 27.632  1.00 113.41 ? 493  ARG A CB  1 
ATOM   3803  C  CG  . ARG A  1 493 ? 25.453  -39.308 27.818  1.00 113.23 ? 493  ARG A CG  1 
ATOM   3804  C  CD  . ARG A  1 493 ? 25.470  -40.084 26.502  1.00 115.31 ? 493  ARG A CD  1 
ATOM   3805  N  NE  . ARG A  1 493 ? 24.520  -39.535 25.535  1.00 117.67 ? 493  ARG A NE  1 
ATOM   3806  C  CZ  . ARG A  1 493 ? 24.216  -40.104 24.371  1.00 119.82 ? 493  ARG A CZ  1 
ATOM   3807  N  NH1 . ARG A  1 493 ? 24.789  -41.250 24.021  1.00 121.24 ? 493  ARG A NH1 1 
ATOM   3808  N  NH2 . ARG A  1 493 ? 23.336  -39.530 23.555  1.00 118.97 ? 493  ARG A NH2 1 
ATOM   3809  N  N   . ASP A  1 494 ? 25.725  -34.880 27.586  0.94 111.30 ? 494  ASP A N   1 
ATOM   3810  C  CA  . ASP A  1 494 ? 26.224  -33.596 27.125  0.94 113.53 ? 494  ASP A CA  1 
ATOM   3811  C  C   . ASP A  1 494 ? 26.237  -32.533 28.218  0.94 110.94 ? 494  ASP A C   1 
ATOM   3812  O  O   . ASP A  1 494 ? 25.395  -32.538 29.118  0.94 108.15 ? 494  ASP A O   1 
ATOM   3813  C  CB  . ASP A  1 494 ? 25.358  -33.109 25.962  0.94 126.90 ? 494  ASP A CB  1 
ATOM   3814  C  CG  . ASP A  1 494 ? 26.119  -32.228 24.996  0.94 131.48 ? 494  ASP A CG  1 
ATOM   3815  O  OD1 . ASP A  1 494 ? 27.206  -31.720 25.361  0.94 133.21 ? 494  ASP A OD1 1 
ATOM   3816  O  OD2 . ASP A  1 494 ? 25.619  -32.042 23.866  0.94 132.95 ? 494  ASP A OD2 1 
ATOM   3817  N  N   . SER A  1 495 ? 27.233  -31.655 28.157  0.99 116.64 ? 495  SER A N   1 
ATOM   3818  C  CA  . SER A  1 495 ? 27.164  -30.368 28.835  0.99 115.01 ? 495  SER A CA  1 
ATOM   3819  C  C   . SER A  1 495 ? 27.375  -29.264 27.792  0.99 114.05 ? 495  SER A C   1 
ATOM   3820  O  O   . SER A  1 495 ? 28.498  -29.071 27.314  0.99 113.66 ? 495  SER A O   1 
ATOM   3821  C  CB  . SER A  1 495 ? 28.218  -30.291 29.943  0.99 109.01 ? 495  SER A CB  1 
ATOM   3822  O  OG  . SER A  1 495 ? 28.074  -31.366 30.861  0.99 107.68 ? 495  SER A OG  1 
ATOM   3823  N  N   . LYS A  1 496 ? 26.303  -28.531 27.473  0.87 114.42 ? 496  LYS A N   1 
ATOM   3824  C  CA  . LYS A  1 496 ? 26.325  -27.510 26.414  0.87 113.27 ? 496  LYS A CA  1 
ATOM   3825  C  C   . LYS A  1 496 ? 24.993  -26.784 26.141  0.87 116.45 ? 496  LYS A C   1 
ATOM   3826  O  O   . LYS A  1 496 ? 23.945  -27.075 26.726  0.87 115.80 ? 496  LYS A O   1 
ATOM   3827  C  CB  . LYS A  1 496 ? 26.845  -28.083 25.081  0.87 91.07  ? 496  LYS A CB  1 
ATOM   3828  C  CG  . LYS A  1 496 ? 25.847  -28.972 24.344  0.87 84.65  ? 496  LYS A CG  1 
ATOM   3829  C  CD  . LYS A  1 496 ? 25.340  -28.343 23.049  0.87 79.11  ? 496  LYS A CD  1 
ATOM   3830  C  CE  . LYS A  1 496 ? 24.234  -29.180 22.390  0.87 73.08  ? 496  LYS A CE  1 
ATOM   3831  N  NZ  . LYS A  1 496 ? 23.109  -29.525 23.303  0.87 67.75  ? 496  LYS A NZ  1 
ATOM   3832  N  N   . SER A  1 497 ? 25.106  -25.844 25.206  1.00 129.29 ? 497  SER A N   1 
ATOM   3833  C  CA  . SER A  1 497 ? 24.070  -24.983 24.596  1.00 129.26 ? 497  SER A CA  1 
ATOM   3834  C  C   . SER A  1 497 ? 23.138  -24.007 25.337  1.00 129.82 ? 497  SER A C   1 
ATOM   3835  O  O   . SER A  1 497 ? 21.987  -23.857 24.919  1.00 130.18 ? 497  SER A O   1 
ATOM   3836  C  CB  . SER A  1 497 ? 23.109  -25.885 23.808  1.00 110.40 ? 497  SER A CB  1 
ATOM   3837  O  OG  . SER A  1 497 ? 22.177  -26.511 24.682  1.00 107.04 ? 497  SER A OG  1 
ATOM   3838  N  N   . PRO A  1 498 ? 23.591  -23.338 26.419  1.00 138.41 ? 498  PRO A N   1 
ATOM   3839  C  CA  . PRO A  1 498 ? 24.090  -24.025 27.612  1.00 135.20 ? 498  PRO A CA  1 
ATOM   3840  C  C   . PRO A  1 498 ? 22.851  -24.732 28.201  1.00 127.17 ? 498  PRO A C   1 
ATOM   3841  O  O   . PRO A  1 498 ? 21.731  -24.493 27.738  1.00 127.12 ? 498  PRO A O   1 
ATOM   3842  C  CB  . PRO A  1 498 ? 24.581  -22.880 28.507  1.00 107.55 ? 498  PRO A CB  1 
ATOM   3843  C  CG  . PRO A  1 498 ? 24.968  -21.805 27.545  1.00 109.19 ? 498  PRO A CG  1 
ATOM   3844  C  CD  . PRO A  1 498 ? 23.941  -21.902 26.434  1.00 109.76 ? 498  PRO A CD  1 
ATOM   3845  N  N   . GLN A  1 499 ? 23.026  -25.619 29.167  1.00 81.18  ? 499  GLN A N   1 
ATOM   3846  C  CA  . GLN A  1 499 ? 21.890  -26.390 29.654  1.00 68.31  ? 499  GLN A CA  1 
ATOM   3847  C  C   . GLN A  1 499 ? 20.760  -25.524 30.265  1.00 52.63  ? 499  GLN A C   1 
ATOM   3848  O  O   . GLN A  1 499 ? 20.954  -24.363 30.609  1.00 48.18  ? 499  GLN A O   1 
ATOM   3849  C  CB  . GLN A  1 499 ? 22.358  -27.473 30.629  1.00 89.95  ? 499  GLN A CB  1 
ATOM   3850  C  CG  . GLN A  1 499 ? 22.977  -26.933 31.894  1.00 94.46  ? 499  GLN A CG  1 
ATOM   3851  C  CD  . GLN A  1 499 ? 22.740  -27.849 33.066  1.00 97.68  ? 499  GLN A CD  1 
ATOM   3852  O  OE1 . GLN A  1 499 ? 23.022  -29.048 32.995  1.00 100.29 ? 499  GLN A OE1 1 
ATOM   3853  N  NE2 . GLN A  1 499 ? 22.199  -27.296 34.152  1.00 96.32  ? 499  GLN A NE2 1 
ATOM   3854  N  N   . TRP A  1 500 ? 19.573  -26.121 30.335  1.00 60.49  ? 500  TRP A N   1 
ATOM   3855  C  CA  . TRP A  1 500 ? 18.309  -25.501 30.736  1.00 49.87  ? 500  TRP A CA  1 
ATOM   3856  C  C   . TRP A  1 500 ? 18.108  -25.658 32.242  1.00 45.45  ? 500  TRP A C   1 
ATOM   3857  O  O   . TRP A  1 500 ? 17.923  -26.770 32.735  1.00 45.08  ? 500  TRP A O   1 
ATOM   3858  C  CB  . TRP A  1 500 ? 17.218  -26.232 29.951  1.00 35.49  ? 500  TRP A CB  1 
ATOM   3859  C  CG  . TRP A  1 500 ? 15.780  -25.915 30.173  1.00 30.21  ? 500  TRP A CG  1 
ATOM   3860  C  CD1 . TRP A  1 500 ? 15.218  -25.211 31.196  1.00 30.21  ? 500  TRP A CD1 1 
ATOM   3861  C  CD2 . TRP A  1 500 ? 14.694  -26.338 29.330  1.00 27.51  ? 500  TRP A CD2 1 
ATOM   3862  N  NE1 . TRP A  1 500 ? 13.844  -25.164 31.041  1.00 28.46  ? 500  TRP A NE1 1 
ATOM   3863  C  CE2 . TRP A  1 500 ? 13.507  -25.842 29.908  1.00 27.73  ? 500  TRP A CE2 1 
ATOM   3864  C  CE3 . TRP A  1 500 ? 14.622  -27.079 28.148  1.00 25.13  ? 500  TRP A CE3 1 
ATOM   3865  C  CZ2 . TRP A  1 500 ? 12.260  -26.069 29.323  1.00 25.38  ? 500  TRP A CZ2 1 
ATOM   3866  C  CZ3 . TRP A  1 500 ? 13.387  -27.301 27.580  1.00 21.23  ? 500  TRP A CZ3 1 
ATOM   3867  C  CH2 . TRP A  1 500 ? 12.222  -26.798 28.165  1.00 23.31  ? 500  TRP A CH2 1 
ATOM   3868  N  N   . PRO A  1 501 ? 18.167  -24.536 32.975  1.00 30.77  ? 501  PRO A N   1 
ATOM   3869  C  CA  . PRO A  1 501 ? 18.093  -24.402 34.441  1.00 28.43  ? 501  PRO A CA  1 
ATOM   3870  C  C   . PRO A  1 501 ? 16.680  -24.449 35.006  1.00 27.80  ? 501  PRO A C   1 
ATOM   3871  O  O   . PRO A  1 501 ? 15.750  -24.020 34.342  1.00 29.62  ? 501  PRO A O   1 
ATOM   3872  C  CB  . PRO A  1 501 ? 18.656  -23.009 34.675  1.00 31.47  ? 501  PRO A CB  1 
ATOM   3873  C  CG  . PRO A  1 501 ? 18.214  -22.251 33.465  1.00 32.05  ? 501  PRO A CG  1 
ATOM   3874  C  CD  . PRO A  1 501 ? 18.248  -23.225 32.310  1.00 31.42  ? 501  PRO A CD  1 
ATOM   3875  N  N   . PRO A  1 502 ? 16.519  -24.927 36.241  1.00 38.35  ? 502  PRO A N   1 
ATOM   3876  C  CA  . PRO A  1 502 ? 15.178  -24.991 36.820  1.00 40.94  ? 502  PRO A CA  1 
ATOM   3877  C  C   . PRO A  1 502 ? 14.618  -23.622 37.161  1.00 44.06  ? 502  PRO A C   1 
ATOM   3878  O  O   . PRO A  1 502 ? 15.347  -22.757 37.649  1.00 49.38  ? 502  PRO A O   1 
ATOM   3879  C  CB  . PRO A  1 502 ? 15.396  -25.786 38.105  1.00 44.58  ? 502  PRO A CB  1 
ATOM   3880  C  CG  . PRO A  1 502 ? 16.595  -26.596 37.818  1.00 46.73  ? 502  PRO A CG  1 
ATOM   3881  C  CD  . PRO A  1 502 ? 17.484  -25.679 37.046  1.00 46.25  ? 502  PRO A CD  1 
ATOM   3882  N  N   . TYR A  1 503 ? 13.330  -23.434 36.890  1.00 31.04  ? 503  TYR A N   1 
ATOM   3883  C  CA  . TYR A  1 503 ? 12.619  -22.269 37.371  1.00 27.57  ? 503  TYR A CA  1 
ATOM   3884  C  C   . TYR A  1 503 ? 12.520  -22.383 38.885  1.00 27.35  ? 503  TYR A C   1 
ATOM   3885  O  O   . TYR A  1 503 ? 12.069  -23.400 39.420  1.00 28.43  ? 503  TYR A O   1 
ATOM   3886  C  CB  . TYR A  1 503 ? 11.221  -22.209 36.760  1.00 30.47  ? 503  TYR A CB  1 
ATOM   3887  C  CG  . TYR A  1 503 ? 10.433  -20.989 37.169  1.00 30.99  ? 503  TYR A CG  1 
ATOM   3888  C  CD1 . TYR A  1 503 ? 9.635   -21.001 38.304  1.00 30.43  ? 503  TYR A CD1 1 
ATOM   3889  C  CD2 . TYR A  1 503 ? 10.491  -19.826 36.416  1.00 34.44  ? 503  TYR A CD2 1 
ATOM   3890  C  CE1 . TYR A  1 503 ? 8.918   -19.891 38.679  1.00 33.77  ? 503  TYR A CE1 1 
ATOM   3891  C  CE2 . TYR A  1 503 ? 9.780   -18.708 36.778  1.00 37.57  ? 503  TYR A CE2 1 
ATOM   3892  C  CZ  . TYR A  1 503 ? 8.995   -18.744 37.913  1.00 39.26  ? 503  TYR A CZ  1 
ATOM   3893  O  OH  . TYR A  1 503 ? 8.285   -17.619 38.273  1.00 44.23  ? 503  TYR A OH  1 
ATOM   3894  N  N   . THR A  1 504 ? 12.958  -21.335 39.570  1.00 25.74  ? 504  THR A N   1 
ATOM   3895  C  CA  . THR A  1 504 ? 12.943  -21.296 41.024  1.00 28.75  ? 504  THR A CA  1 
ATOM   3896  C  C   . THR A  1 504 ? 12.221  -20.019 41.419  1.00 31.04  ? 504  THR A C   1 
ATOM   3897  O  O   . THR A  1 504 ? 12.034  -19.122 40.582  1.00 28.22  ? 504  THR A O   1 
ATOM   3898  C  CB  . THR A  1 504 ? 14.379  -21.296 41.607  1.00 44.53  ? 504  THR A CB  1 
ATOM   3899  O  OG1 . THR A  1 504 ? 14.989  -20.010 41.432  1.00 46.89  ? 504  THR A OG1 1 
ATOM   3900  C  CG2 . THR A  1 504 ? 15.238  -22.339 40.907  1.00 47.75  ? 504  THR A CG2 1 
ATOM   3901  N  N   . THR A  1 505 ? 11.798  -19.927 42.678  1.00 45.06  ? 505  THR A N   1 
ATOM   3902  C  CA  . THR A  1 505 ? 11.064  -18.739 43.123  1.00 48.16  ? 505  THR A CA  1 
ATOM   3903  C  C   . THR A  1 505 ? 12.004  -17.546 43.191  1.00 44.84  ? 505  THR A C   1 
ATOM   3904  O  O   . THR A  1 505 ? 11.673  -16.455 42.734  1.00 41.21  ? 505  THR A O   1 
ATOM   3905  C  CB  . THR A  1 505 ? 10.342  -18.952 44.474  1.00 58.52  ? 505  THR A CB  1 
ATOM   3906  O  OG1 . THR A  1 505 ? 10.681  -20.243 45.012  1.00 63.17  ? 505  THR A OG1 1 
ATOM   3907  C  CG2 . THR A  1 505 ? 8.818   -18.846 44.284  1.00 55.02  ? 505  THR A CG2 1 
ATOM   3908  N  N   . ALA A  1 506 ? 13.190  -17.787 43.735  1.00 53.39  ? 506  ALA A N   1 
ATOM   3909  C  CA  . ALA A  1 506 ? 14.255  -16.793 43.788  1.00 56.68  ? 506  ALA A CA  1 
ATOM   3910  C  C   . ALA A  1 506 ? 14.652  -16.194 42.419  1.00 53.80  ? 506  ALA A C   1 
ATOM   3911  O  O   . ALA A  1 506 ? 14.377  -15.022 42.122  1.00 54.40  ? 506  ALA A O   1 
ATOM   3912  C  CB  . ALA A  1 506 ? 15.476  -17.414 44.462  1.00 57.44  ? 506  ALA A CB  1 
ATOM   3913  N  N   . ALA A  1 507 ? 15.300  -17.015 41.596  1.00 35.54  ? 507  ALA A N   1 
ATOM   3914  C  CA  . ALA A  1 507 ? 15.891  -16.568 40.338  1.00 34.04  ? 507  ALA A CA  1 
ATOM   3915  C  C   . ALA A  1 507 ? 14.907  -16.426 39.182  1.00 30.31  ? 507  ALA A C   1 
ATOM   3916  O  O   . ALA A  1 507 ? 15.089  -15.566 38.315  1.00 28.13  ? 507  ALA A O   1 
ATOM   3917  C  CB  . ALA A  1 507 ? 17.009  -17.511 39.941  1.00 54.89  ? 507  ALA A CB  1 
ATOM   3918  N  N   . GLN A  1 508 ? 13.886  -17.288 39.179  1.00 31.64  ? 508  GLN A N   1 
ATOM   3919  C  CA  . GLN A  1 508 ? 12.899  -17.429 38.093  1.00 30.74  ? 508  GLN A CA  1 
ATOM   3920  C  C   . GLN A  1 508 ? 13.490  -17.486 36.686  1.00 29.70  ? 508  GLN A C   1 
ATOM   3921  O  O   . GLN A  1 508 ? 13.276  -16.598 35.866  1.00 25.17  ? 508  GLN A O   1 
ATOM   3922  C  CB  . GLN A  1 508 ? 11.844  -16.334 38.144  1.00 38.29  ? 508  GLN A CB  1 
ATOM   3923  C  CG  . GLN A  1 508 ? 11.577  -15.756 39.496  1.00 39.53  ? 508  GLN A CG  1 
ATOM   3924  C  CD  . GLN A  1 508 ? 10.851  -14.453 39.346  1.00 42.47  ? 508  GLN A CD  1 
ATOM   3925  O  OE1 . GLN A  1 508 ? 9.883   -14.371 38.587  1.00 43.36  ? 508  GLN A OE1 1 
ATOM   3926  N  NE2 . GLN A  1 508 ? 11.334  -13.410 40.019  1.00 43.94  ? 508  GLN A NE2 1 
ATOM   3927  N  N   . GLN A  1 509 ? 14.221  -18.542 36.395  1.00 30.29  ? 509  GLN A N   1 
ATOM   3928  C  CA  . GLN A  1 509 ? 14.797  -18.652 35.078  1.00 34.03  ? 509  GLN A CA  1 
ATOM   3929  C  C   . GLN A  1 509 ? 13.960  -19.576 34.228  1.00 35.08  ? 509  GLN A C   1 
ATOM   3930  O  O   . GLN A  1 509 ? 13.572  -20.657 34.664  1.00 35.67  ? 509  GLN A O   1 
ATOM   3931  C  CB  . GLN A  1 509 ? 16.230  -19.167 35.165  1.00 39.96  ? 509  GLN A CB  1 
ATOM   3932  C  CG  . GLN A  1 509 ? 17.144  -18.262 35.920  1.00 43.27  ? 509  GLN A CG  1 
ATOM   3933  C  CD  . GLN A  1 509 ? 18.459  -18.916 36.182  1.00 49.80  ? 509  GLN A CD  1 
ATOM   3934  O  OE1 . GLN A  1 509 ? 18.537  -20.137 36.275  1.00 51.77  ? 509  GLN A OE1 1 
ATOM   3935  N  NE2 . GLN A  1 509 ? 19.516  -18.115 36.293  1.00 53.97  ? 509  GLN A NE2 1 
ATOM   3936  N  N   . TYR A  1 510 ? 13.686  -19.140 33.012  1.00 23.97  ? 510  TYR A N   1 
ATOM   3937  C  CA  . TYR A  1 510 ? 13.060  -19.994 32.020  1.00 24.13  ? 510  TYR A CA  1 
ATOM   3938  C  C   . TYR A  1 510 ? 13.887  -19.824 30.763  1.00 24.06  ? 510  TYR A C   1 
ATOM   3939  O  O   . TYR A  1 510 ? 14.748  -18.964 30.722  1.00 25.37  ? 510  TYR A O   1 
ATOM   3940  C  CB  . TYR A  1 510 ? 11.616  -19.571 31.766  1.00 28.48  ? 510  TYR A CB  1 
ATOM   3941  C  CG  . TYR A  1 510 ? 11.507  -18.162 31.267  1.00 26.93  ? 510  TYR A CG  1 
ATOM   3942  C  CD1 . TYR A  1 510 ? 11.510  -17.107 32.149  1.00 29.87  ? 510  TYR A CD1 1 
ATOM   3943  C  CD2 . TYR A  1 510 ? 11.421  -17.882 29.915  1.00 24.28  ? 510  TYR A CD2 1 
ATOM   3944  C  CE1 . TYR A  1 510 ? 11.426  -15.815 31.705  1.00 31.21  ? 510  TYR A CE1 1 
ATOM   3945  C  CE2 . TYR A  1 510 ? 11.331  -16.588 29.466  1.00 26.26  ? 510  TYR A CE2 1 
ATOM   3946  C  CZ  . TYR A  1 510 ? 11.329  -15.560 30.369  1.00 30.00  ? 510  TYR A CZ  1 
ATOM   3947  O  OH  . TYR A  1 510 ? 11.248  -14.259 29.947  1.00 33.36  ? 510  TYR A OH  1 
ATOM   3948  N  N   . VAL A  1 511 ? 13.648  -20.640 29.743  1.00 32.86  ? 511  VAL A N   1 
ATOM   3949  C  CA  . VAL A  1 511 ? 14.423  -20.517 28.516  1.00 35.36  ? 511  VAL A CA  1 
ATOM   3950  C  C   . VAL A  1 511 ? 13.521  -20.249 27.329  1.00 38.06  ? 511  VAL A C   1 
ATOM   3951  O  O   . VAL A  1 511 ? 12.297  -20.445 27.391  1.00 36.03  ? 511  VAL A O   1 
ATOM   3952  C  CB  . VAL A  1 511 ? 15.268  -21.776 28.220  1.00 35.51  ? 511  VAL A CB  1 
ATOM   3953  C  CG1 . VAL A  1 511 ? 16.218  -22.074 29.373  1.00 36.59  ? 511  VAL A CG1 1 
ATOM   3954  C  CG2 . VAL A  1 511 ? 14.370  -22.974 27.947  1.00 33.29  ? 511  VAL A CG2 1 
ATOM   3955  N  N   . SER A  1 512 ? 14.147  -19.791 26.252  1.00 53.52  ? 512  SER A N   1 
ATOM   3956  C  CA  . SER A  1 512 ? 13.467  -19.534 24.997  1.00 58.14  ? 512  SER A CA  1 
ATOM   3957  C  C   . SER A  1 512 ? 13.635  -20.729 24.070  1.00 60.82  ? 512  SER A C   1 
ATOM   3958  O  O   . SER A  1 512 ? 14.756  -21.193 23.840  1.00 65.69  ? 512  SER A O   1 
ATOM   3959  C  CB  . SER A  1 512 ? 14.096  -18.324 24.329  1.00 55.00  ? 512  SER A CB  1 
ATOM   3960  O  OG  . SER A  1 512 ? 15.408  -18.647 23.899  1.00 56.78  ? 512  SER A OG  1 
ATOM   3961  N  N   . LEU A  1 513 ? 12.525  -21.226 23.535  1.00 40.13  ? 513  LEU A N   1 
ATOM   3962  C  CA  . LEU A  1 513 ? 12.573  -22.293 22.552  1.00 35.61  ? 513  LEU A CA  1 
ATOM   3963  C  C   . LEU A  1 513 ? 12.343  -21.696 21.177  1.00 32.89  ? 513  LEU A C   1 
ATOM   3964  O  O   . LEU A  1 513 ? 11.244  -21.231 20.868  1.00 29.27  ? 513  LEU A O   1 
ATOM   3965  C  CB  . LEU A  1 513 ? 11.527  -23.365 22.857  1.00 37.13  ? 513  LEU A CB  1 
ATOM   3966  C  CG  . LEU A  1 513 ? 11.711  -24.082 24.196  1.00 34.92  ? 513  LEU A CG  1 
ATOM   3967  C  CD1 . LEU A  1 513 ? 10.741  -25.258 24.338  1.00 32.94  ? 513  LEU A CD1 1 
ATOM   3968  C  CD2 . LEU A  1 513 ? 13.153  -24.534 24.354  1.00 33.83  ? 513  LEU A CD2 1 
ATOM   3969  N  N   . ASN A  1 514 ? 13.395  -21.687 20.364  1.00 40.84  ? 514  ASN A N   1 
ATOM   3970  C  CA  . ASN A  1 514 ? 13.331  -21.114 19.025  1.00 43.78  ? 514  ASN A CA  1 
ATOM   3971  C  C   . ASN A  1 514 ? 14.426  -21.682 18.148  1.00 42.13  ? 514  ASN A C   1 
ATOM   3972  O  O   . ASN A  1 514 ? 15.113  -22.623 18.533  1.00 41.34  ? 514  ASN A O   1 
ATOM   3973  C  CB  . ASN A  1 514 ? 13.437  -19.589 19.071  1.00 45.01  ? 514  ASN A CB  1 
ATOM   3974  C  CG  . ASN A  1 514 ? 14.716  -19.120 19.722  1.00 48.99  ? 514  ASN A CG  1 
ATOM   3975  O  OD1 . ASN A  1 514 ? 15.804  -19.554 19.355  1.00 50.66  ? 514  ASN A OD1 1 
ATOM   3976  N  ND2 . ASN A  1 514 ? 14.593  -18.242 20.711  1.00 50.54  ? 514  ASN A ND2 1 
ATOM   3977  N  N   . LEU A  1 515 ? 14.606  -21.084 16.980  1.00 41.69  ? 515  LEU A N   1 
ATOM   3978  C  CA  . LEU A  1 515 ? 15.598  -21.567 16.035  1.00 42.12  ? 515  LEU A CA  1 
ATOM   3979  C  C   . LEU A  1 515 ? 17.044  -21.411 16.529  1.00 49.92  ? 515  LEU A C   1 
ATOM   3980  O  O   . LEU A  1 515 ? 17.877  -22.286 16.290  1.00 52.37  ? 515  LEU A O   1 
ATOM   3981  C  CB  . LEU A  1 515 ? 15.398  -20.899 14.682  1.00 31.05  ? 515  LEU A CB  1 
ATOM   3982  C  CG  . LEU A  1 515 ? 14.771  -21.817 13.646  1.00 30.92  ? 515  LEU A CG  1 
ATOM   3983  C  CD1 . LEU A  1 515 ? 15.669  -23.025 13.476  1.00 31.17  ? 515  LEU A CD1 1 
ATOM   3984  C  CD2 . LEU A  1 515 ? 13.408  -22.244 14.068  1.00 29.44  ? 515  LEU A CD2 1 
ATOM   3985  N  N   . LYS A  1 516 ? 17.338  -20.312 17.225  1.00 55.27  ? 516  LYS A N   1 
ATOM   3986  C  CA  . LYS A  1 516 ? 18.640  -20.134 17.871  1.00 56.97  ? 516  LYS A CA  1 
ATOM   3987  C  C   . LYS A  1 516 ? 18.739  -21.192 18.969  1.00 56.40  ? 516  LYS A C   1 
ATOM   3988  O  O   . LYS A  1 516 ? 17.728  -21.803 19.324  1.00 55.90  ? 516  LYS A O   1 
ATOM   3989  C  CB  . LYS A  1 516 ? 18.743  -18.745 18.519  1.00 58.48  ? 516  LYS A CB  1 
ATOM   3990  C  CG  . LYS A  1 516 ? 18.758  -17.535 17.594  1.00 61.79  ? 516  LYS A CG  1 
ATOM   3991  C  CD  . LYS A  1 516 ? 18.706  -16.243 18.438  1.00 65.75  ? 516  LYS A CD  1 
ATOM   3992  C  CE  . LYS A  1 516 ? 18.743  -14.959 17.591  1.00 70.91  ? 516  LYS A CE  1 
ATOM   3993  N  NZ  . LYS A  1 516 ? 20.104  -14.317 17.470  1.00 74.27  ? 516  LYS A NZ  1 
ATOM   3994  N  N   . PRO A  1 517 ? 19.948  -21.421 19.516  1.00 56.01  ? 517  PRO A N   1 
ATOM   3995  C  CA  . PRO A  1 517 ? 20.058  -22.290 20.699  1.00 55.89  ? 517  PRO A CA  1 
ATOM   3996  C  C   . PRO A  1 517 ? 19.427  -21.649 21.935  1.00 56.95  ? 517  PRO A C   1 
ATOM   3997  O  O   . PRO A  1 517 ? 18.989  -20.501 21.871  1.00 59.61  ? 517  PRO A O   1 
ATOM   3998  C  CB  . PRO A  1 517 ? 21.565  -22.401 20.902  1.00 42.24  ? 517  PRO A CB  1 
ATOM   3999  C  CG  . PRO A  1 517 ? 22.107  -21.134 20.300  1.00 42.15  ? 517  PRO A CG  1 
ATOM   4000  C  CD  . PRO A  1 517 ? 21.264  -20.925 19.082  1.00 41.91  ? 517  PRO A CD  1 
ATOM   4001  N  N   . LEU A  1 518 ? 19.401  -22.367 23.053  1.00 43.93  ? 518  LEU A N   1 
ATOM   4002  C  CA  . LEU A  1 518 ? 18.733  -21.858 24.254  1.00 45.10  ? 518  LEU A CA  1 
ATOM   4003  C  C   . LEU A  1 518 ? 19.410  -20.624 24.820  1.00 48.24  ? 518  LEU A C   1 
ATOM   4004  O  O   . LEU A  1 518 ? 20.633  -20.584 24.943  1.00 49.40  ? 518  LEU A O   1 
ATOM   4005  C  CB  . LEU A  1 518 ? 18.698  -22.905 25.372  1.00 48.37  ? 518  LEU A CB  1 
ATOM   4006  C  CG  . LEU A  1 518 ? 17.917  -24.212 25.273  1.00 47.19  ? 518  LEU A CG  1 
ATOM   4007  C  CD1 . LEU A  1 518 ? 17.512  -24.658 26.675  1.00 43.35  ? 518  LEU A CD1 1 
ATOM   4008  C  CD2 . LEU A  1 518 ? 16.716  -24.080 24.343  1.00 47.61  ? 518  LEU A CD2 1 
ATOM   4009  N  N   . GLU A  1 519 ? 18.609  -19.622 25.171  1.00 56.19  ? 519  GLU A N   1 
ATOM   4010  C  CA  . GLU A  1 519 ? 19.075  -18.533 26.023  1.00 60.40  ? 519  GLU A CA  1 
ATOM   4011  C  C   . GLU A  1 519 ? 18.203  -18.556 27.267  1.00 50.33  ? 519  GLU A C   1 
ATOM   4012  O  O   . GLU A  1 519 ? 17.051  -18.993 27.206  1.00 48.64  ? 519  GLU A O   1 
ATOM   4013  C  CB  . GLU A  1 519 ? 19.028  -17.170 25.304  1.00 95.95  ? 519  GLU A CB  1 
ATOM   4014  C  CG  . GLU A  1 519 ? 17.668  -16.775 24.717  1.00 106.31 ? 519  GLU A CG  1 
ATOM   4015  C  CD  . GLU A  1 519 ? 17.754  -15.681 23.644  1.00 114.65 ? 519  GLU A CD  1 
ATOM   4016  O  OE1 . GLU A  1 519 ? 17.824  -14.485 24.011  1.00 116.34 ? 519  GLU A OE1 1 
ATOM   4017  O  OE2 . GLU A  1 519 ? 17.733  -16.020 22.434  1.00 116.67 ? 519  GLU A OE2 1 
ATOM   4018  N  N   . VAL A  1 520 ? 18.753  -18.132 28.399  1.00 37.17  ? 520  VAL A N   1 
ATOM   4019  C  CA  . VAL A  1 520 ? 17.988  -18.131 29.644  1.00 32.13  ? 520  VAL A CA  1 
ATOM   4020  C  C   . VAL A  1 520 ? 17.498  -16.745 30.038  1.00 30.53  ? 520  VAL A C   1 
ATOM   4021  O  O   . VAL A  1 520 ? 18.288  -15.841 30.290  1.00 32.37  ? 520  VAL A O   1 
ATOM   4022  C  CB  . VAL A  1 520 ? 18.786  -18.713 30.817  1.00 29.02  ? 520  VAL A CB  1 
ATOM   4023  C  CG1 . VAL A  1 520 ? 17.989  -18.560 32.123  1.00 27.80  ? 520  VAL A CG1 1 
ATOM   4024  C  CG2 . VAL A  1 520 ? 19.125  -20.159 30.549  1.00 28.14  ? 520  VAL A CG2 1 
ATOM   4025  N  N   . ARG A  1 521 ? 16.184  -16.596 30.102  1.00 32.41  ? 521  ARG A N   1 
ATOM   4026  C  CA  . ARG A  1 521 ? 15.571  -15.352 30.530  1.00 35.17  ? 521  ARG A CA  1 
ATOM   4027  C  C   . ARG A  1 521 ? 15.092  -15.435 31.986  1.00 36.17  ? 521  ARG A C   1 
ATOM   4028  O  O   . ARG A  1 521 ? 14.540  -16.447 32.422  1.00 32.42  ? 521  ARG A O   1 
ATOM   4029  C  CB  . ARG A  1 521 ? 14.425  -14.993 29.587  1.00 37.28  ? 521  ARG A CB  1 
ATOM   4030  C  CG  . ARG A  1 521 ? 14.673  -15.412 28.153  1.00 37.32  ? 521  ARG A CG  1 
ATOM   4031  C  CD  . ARG A  1 521 ? 14.145  -14.379 27.186  1.00 41.28  ? 521  ARG A CD  1 
ATOM   4032  N  NE  . ARG A  1 521 ? 14.745  -14.531 25.862  1.00 46.31  ? 521  ARG A NE  1 
ATOM   4033  C  CZ  . ARG A  1 521 ? 14.068  -14.896 24.779  1.00 48.25  ? 521  ARG A CZ  1 
ATOM   4034  N  NH1 . ARG A  1 521 ? 12.766  -15.136 24.875  1.00 49.81  ? 521  ARG A NH1 1 
ATOM   4035  N  NH2 . ARG A  1 521 ? 14.684  -15.009 23.606  1.00 47.28  ? 521  ARG A NH2 1 
ATOM   4036  N  N   . ARG A  1 522 ? 15.320  -14.365 32.737  1.00 50.24  ? 522  ARG A N   1 
ATOM   4037  C  CA  . ARG A  1 522 ? 14.968  -14.350 34.147  1.00 55.83  ? 522  ARG A CA  1 
ATOM   4038  C  C   . ARG A  1 522 ? 13.675  -13.585 34.388  1.00 56.90  ? 522  ARG A C   1 
ATOM   4039  O  O   . ARG A  1 522 ? 13.517  -12.440 33.982  1.00 62.02  ? 522  ARG A O   1 
ATOM   4040  C  CB  . ARG A  1 522 ? 16.102  -13.762 34.973  1.00 67.95  ? 522  ARG A CB  1 
ATOM   4041  C  CG  . ARG A  1 522 ? 17.434  -14.450 34.764  1.00 78.23  ? 522  ARG A CG  1 
ATOM   4042  C  CD  . ARG A  1 522 ? 18.471  -13.809 35.650  1.00 89.89  ? 522  ARG A CD  1 
ATOM   4043  N  NE  . ARG A  1 522 ? 17.851  -13.331 36.885  1.00 98.39  ? 522  ARG A NE  1 
ATOM   4044  C  CZ  . ARG A  1 522 ? 17.977  -13.919 38.070  1.00 103.23 ? 522  ARG A CZ  1 
ATOM   4045  N  NH1 . ARG A  1 522 ? 18.725  -15.011 38.197  1.00 104.82 ? 522  ARG A NH1 1 
ATOM   4046  N  NH2 . ARG A  1 522 ? 17.364  -13.405 39.130  1.00 103.64 ? 522  ARG A NH2 1 
ATOM   4047  N  N   . GLY A  1 523 ? 12.723  -14.266 34.994  1.00 50.89  ? 523  GLY A N   1 
ATOM   4048  C  CA  . GLY A  1 523 ? 11.447  -13.689 35.361  1.00 49.24  ? 523  GLY A CA  1 
ATOM   4049  C  C   . GLY A  1 523 ? 10.554  -13.693 34.139  1.00 47.98  ? 523  GLY A C   1 
ATOM   4050  O  O   . GLY A  1 523 ? 10.963  -13.238 33.057  1.00 46.67  ? 523  GLY A O   1 
ATOM   4051  N  N   . LEU A  1 524 ? 9.301   -14.090 34.350  1.00 43.40  ? 524  LEU A N   1 
ATOM   4052  C  CA  . LEU A  1 524 ? 8.382   -14.343 33.258  1.00 39.05  ? 524  LEU A CA  1 
ATOM   4053  C  C   . LEU A  1 524 ? 7.229   -13.368 33.392  1.00 43.72  ? 524  LEU A C   1 
ATOM   4054  O  O   . LEU A  1 524 ? 6.365   -13.558 34.251  1.00 46.89  ? 524  LEU A O   1 
ATOM   4055  C  CB  . LEU A  1 524 ? 7.893   -15.788 33.382  1.00 24.21  ? 524  LEU A CB  1 
ATOM   4056  C  CG  . LEU A  1 524 ? 6.964   -16.470 32.366  1.00 23.68  ? 524  LEU A CG  1 
ATOM   4057  C  CD1 . LEU A  1 524 ? 7.630   -16.615 30.998  1.00 21.79  ? 524  LEU A CD1 1 
ATOM   4058  C  CD2 . LEU A  1 524 ? 6.482   -17.833 32.902  1.00 20.48  ? 524  LEU A CD2 1 
ATOM   4059  N  N   . ARG A  1 525 ? 7.206   -12.348 32.530  1.00 46.99  ? 525  ARG A N   1 
ATOM   4060  C  CA  . ARG A  1 525 ? 6.217   -11.259 32.604  1.00 47.79  ? 525  ARG A CA  1 
ATOM   4061  C  C   . ARG A  1 525 ? 6.012   -10.784 34.052  1.00 46.55  ? 525  ARG A C   1 
ATOM   4062  O  O   . ARG A  1 525 ? 4.883   -10.693 34.533  1.00 47.03  ? 525  ARG A O   1 
ATOM   4063  C  CB  . ARG A  1 525 ? 4.876   -11.644 31.957  1.00 51.57  ? 525  ARG A CB  1 
ATOM   4064  C  CG  . ARG A  1 525 ? 4.940   -12.090 30.480  1.00 55.19  ? 525  ARG A CG  1 
ATOM   4065  C  CD  . ARG A  1 525 ? 5.121   -10.955 29.478  1.00 60.06  ? 525  ARG A CD  1 
ATOM   4066  N  NE  . ARG A  1 525 ? 3.994   -10.031 29.476  1.00 66.65  ? 525  ARG A NE  1 
ATOM   4067  C  CZ  . ARG A  1 525 ? 4.108   -8.707  29.584  1.00 73.91  ? 525  ARG A CZ  1 
ATOM   4068  N  NH1 . ARG A  1 525 ? 5.309   -8.142  29.694  1.00 74.70  ? 525  ARG A NH1 1 
ATOM   4069  N  NH2 . ARG A  1 525 ? 3.017   -7.941  29.576  1.00 76.79  ? 525  ARG A NH2 1 
ATOM   4070  N  N   . ALA A  1 526 ? 7.118   -10.494 34.736  1.00 35.29  ? 526  ALA A N   1 
ATOM   4071  C  CA  . ALA A  1 526 ? 7.118   -10.308 36.186  1.00 29.19  ? 526  ALA A CA  1 
ATOM   4072  C  C   . ALA A  1 526 ? 6.234   -9.193  36.720  1.00 29.59  ? 526  ALA A C   1 
ATOM   4073  O  O   . ALA A  1 526 ? 5.432   -9.431  37.606  1.00 28.15  ? 526  ALA A O   1 
ATOM   4074  C  CB  . ALA A  1 526 ? 8.526   -10.139 36.694  1.00 30.36  ? 526  ALA A CB  1 
ATOM   4075  N  N   . GLN A  1 527 ? 6.386   -7.979  36.212  1.00 53.91  ? 527  GLN A N   1 
ATOM   4076  C  CA  . GLN A  1 527 ? 5.642   -6.855  36.774  1.00 60.08  ? 527  GLN A CA  1 
ATOM   4077  C  C   . GLN A  1 527 ? 4.165   -7.002  36.441  1.00 59.53  ? 527  GLN A C   1 
ATOM   4078  O  O   . GLN A  1 527 ? 3.275   -6.737  37.269  1.00 63.71  ? 527  GLN A O   1 
ATOM   4079  C  CB  . GLN A  1 527 ? 6.186   -5.536  36.230  1.00 54.10  ? 527  GLN A CB  1 
ATOM   4080  C  CG  . GLN A  1 527 ? 7.699   -5.509  36.137  1.00 54.90  ? 527  GLN A CG  1 
ATOM   4081  C  CD  . GLN A  1 527 ? 8.365   -5.581  37.494  1.00 56.00  ? 527  GLN A CD  1 
ATOM   4082  O  OE1 . GLN A  1 527 ? 9.310   -6.348  37.701  1.00 56.95  ? 527  GLN A OE1 1 
ATOM   4083  N  NE2 . GLN A  1 527 ? 7.882   -4.768  38.429  1.00 55.83  ? 527  GLN A NE2 1 
ATOM   4084  N  N   . THR A  1 528 ? 3.920   -7.458  35.220  1.00 33.72  ? 528  THR A N   1 
ATOM   4085  C  CA  . THR A  1 528 ? 2.572   -7.599  34.705  1.00 27.02  ? 528  THR A CA  1 
ATOM   4086  C  C   . THR A  1 528 ? 1.858   -8.707  35.460  1.00 24.93  ? 528  THR A C   1 
ATOM   4087  O  O   . THR A  1 528 ? 0.706   -8.576  35.882  1.00 24.78  ? 528  THR A O   1 
ATOM   4088  C  CB  . THR A  1 528 ? 2.614   -7.881  33.200  1.00 27.87  ? 528  THR A CB  1 
ATOM   4089  O  OG1 . THR A  1 528 ? 2.625   -6.633  32.492  1.00 33.12  ? 528  THR A OG1 1 
ATOM   4090  C  CG2 . THR A  1 528 ? 1.417   -8.698  32.763  1.00 24.87  ? 528  THR A CG2 1 
ATOM   4091  N  N   . CYS A  1 529 ? 2.568   -9.798  35.670  1.00 30.07  ? 529  CYS A N   1 
ATOM   4092  C  CA  . CYS A  1 529 ? 1.975   -10.890 36.397  1.00 30.50  ? 529  CYS A CA  1 
ATOM   4093  C  C   . CYS A  1 529 ? 1.798   -10.537 37.869  1.00 28.62  ? 529  CYS A C   1 
ATOM   4094  O  O   . CYS A  1 529 ? 0.875   -11.000 38.504  1.00 30.32  ? 529  CYS A O   1 
ATOM   4095  C  CB  . CYS A  1 529 ? 2.750   -12.189 36.161  1.00 32.44  ? 529  CYS A CB  1 
ATOM   4096  S  SG  . CYS A  1 529 ? 2.381   -12.885 34.509  1.00 74.19  ? 529  CYS A SG  1 
ATOM   4097  N  N   . ALA A  1 530 ? 2.655   -9.690  38.412  1.00 24.69  ? 530  ALA A N   1 
ATOM   4098  C  CA  . ALA A  1 530 ? 2.414   -9.210  39.764  1.00 25.24  ? 530  ALA A CA  1 
ATOM   4099  C  C   . ALA A  1 530 ? 1.080   -8.467  39.781  1.00 25.47  ? 530  ALA A C   1 
ATOM   4100  O  O   . ALA A  1 530 ? 0.305   -8.589  40.727  1.00 26.62  ? 530  ALA A O   1 
ATOM   4101  C  CB  . ALA A  1 530 ? 3.542   -8.312  40.236  1.00 26.40  ? 530  ALA A CB  1 
ATOM   4102  N  N   . PHE A  1 531 ? 0.797   -7.717  38.722  1.00 30.63  ? 531  PHE A N   1 
ATOM   4103  C  CA  . PHE A  1 531 ? -0.494  -7.037  38.641  1.00 31.94  ? 531  PHE A CA  1 
ATOM   4104  C  C   . PHE A  1 531 ? -1.653  -8.032  38.611  1.00 32.15  ? 531  PHE A C   1 
ATOM   4105  O  O   . PHE A  1 531 ? -2.524  -8.017  39.494  1.00 32.54  ? 531  PHE A O   1 
ATOM   4106  C  CB  . PHE A  1 531 ? -0.526  -6.116  37.427  1.00 26.72  ? 531  PHE A CB  1 
ATOM   4107  C  CG  . PHE A  1 531 ? -1.897  -5.757  36.964  1.00 26.79  ? 531  PHE A CG  1 
ATOM   4108  C  CD1 . PHE A  1 531 ? -2.671  -4.868  37.670  1.00 27.57  ? 531  PHE A CD1 1 
ATOM   4109  C  CD2 . PHE A  1 531 ? -2.400  -6.280  35.790  1.00 36.90  ? 531  PHE A CD2 1 
ATOM   4110  C  CE1 . PHE A  1 531 ? -3.942  -4.520  37.218  1.00 31.65  ? 531  PHE A CE1 1 
ATOM   4111  C  CE2 . PHE A  1 531 ? -3.669  -5.933  35.338  1.00 38.87  ? 531  PHE A CE2 1 
ATOM   4112  C  CZ  . PHE A  1 531 ? -4.439  -5.056  36.052  1.00 27.21  ? 531  PHE A CZ  1 
ATOM   4113  N  N   . TRP A  1 532 ? -1.627  -8.919  37.617  1.00 28.95  ? 532  TRP A N   1 
ATOM   4114  C  CA  . TRP A  1 532 ? -2.726  -9.854  37.367  1.00 28.46  ? 532  TRP A CA  1 
ATOM   4115  C  C   . TRP A  1 532 ? -2.969  -10.829 38.515  1.00 29.14  ? 532  TRP A C   1 
ATOM   4116  O  O   . TRP A  1 532 ? -4.108  -11.100 38.872  1.00 30.23  ? 532  TRP A O   1 
ATOM   4117  C  CB  . TRP A  1 532 ? -2.470  -10.654 36.086  1.00 22.77  ? 532  TRP A CB  1 
ATOM   4118  C  CG  . TRP A  1 532 ? -2.701  -9.899  34.824  1.00 31.84  ? 532  TRP A CG  1 
ATOM   4119  C  CD1 . TRP A  1 532 ? -1.752  -9.431  33.951  1.00 23.70  ? 532  TRP A CD1 1 
ATOM   4120  C  CD2 . TRP A  1 532 ? -3.969  -9.524  34.276  1.00 37.05  ? 532  TRP A CD2 1 
ATOM   4121  N  NE1 . TRP A  1 532 ? -2.355  -8.784  32.898  1.00 24.20  ? 532  TRP A NE1 1 
ATOM   4122  C  CE2 . TRP A  1 532 ? -3.719  -8.828  33.073  1.00 24.09  ? 532  TRP A CE2 1 
ATOM   4123  C  CE3 . TRP A  1 532 ? -5.295  -9.704  34.686  1.00 23.38  ? 532  TRP A CE3 1 
ATOM   4124  C  CZ2 . TRP A  1 532 ? -4.748  -8.315  32.277  1.00 24.57  ? 532  TRP A CZ2 1 
ATOM   4125  C  CZ3 . TRP A  1 532 ? -6.304  -9.195  33.897  1.00 41.96  ? 532  TRP A CZ3 1 
ATOM   4126  C  CH2 . TRP A  1 532 ? -6.027  -8.507  32.707  1.00 24.44  ? 532  TRP A CH2 1 
ATOM   4127  N  N   . ASN A  1 533 ? -1.892  -11.390 39.049  1.00 30.89  ? 533  ASN A N   1 
ATOM   4128  C  CA  . ASN A  1 533 ? -1.964  -12.407 40.092  1.00 32.40  ? 533  ASN A CA  1 
ATOM   4129  C  C   . ASN A  1 533 ? -2.143  -11.810 41.491  1.00 33.56  ? 533  ASN A C   1 
ATOM   4130  O  O   . ASN A  1 533 ? -2.865  -12.361 42.317  1.00 33.33  ? 533  ASN A O   1 
ATOM   4131  C  CB  . ASN A  1 533 ? -0.719  -13.319 40.072  1.00 37.09  ? 533  ASN A CB  1 
ATOM   4132  C  CG  . ASN A  1 533 ? -0.457  -13.971 38.698  1.00 34.90  ? 533  ASN A CG  1 
ATOM   4133  O  OD1 . ASN A  1 533 ? -1.381  -14.237 37.915  1.00 34.26  ? 533  ASN A OD1 1 
ATOM   4134  N  ND2 . ASN A  1 533 ? 0.821   -14.246 38.419  1.00 31.08  ? 533  ASN A ND2 1 
ATOM   4135  N  N   . ARG A  1 534 ? -1.471  -10.694 41.761  1.00 33.52  ? 534  ARG A N   1 
ATOM   4136  C  CA  . ARG A  1 534 ? -1.483  -10.110 43.104  1.00 38.55  ? 534  ARG A CA  1 
ATOM   4137  C  C   . ARG A  1 534 ? -2.502  -8.987  43.269  1.00 36.13  ? 534  ARG A C   1 
ATOM   4138  O  O   . ARG A  1 534 ? -3.355  -9.052  44.152  1.00 35.68  ? 534  ARG A O   1 
ATOM   4139  C  CB  . ARG A  1 534 ? -0.088  -9.668  43.551  1.00 61.18  ? 534  ARG A CB  1 
ATOM   4140  C  CG  . ARG A  1 534 ? 0.902   -10.812 43.659  1.00 69.03  ? 534  ARG A CG  1 
ATOM   4141  C  CD  . ARG A  1 534 ? 2.336   -10.302 43.711  1.00 76.95  ? 534  ARG A CD  1 
ATOM   4142  N  NE  . ARG A  1 534 ? 3.118   -11.004 44.722  1.00 81.64  ? 534  ARG A NE  1 
ATOM   4143  C  CZ  . ARG A  1 534 ? 3.012   -10.781 46.030  1.00 85.60  ? 534  ARG A CZ  1 
ATOM   4144  N  NH1 . ARG A  1 534 ? 2.153   -9.873  46.498  1.00 84.75  ? 534  ARG A NH1 1 
ATOM   4145  N  NH2 . ARG A  1 534 ? 3.767   -11.476 46.873  1.00 87.49  ? 534  ARG A NH2 1 
ATOM   4146  N  N   . PHE A  1 535 ? -2.380  -7.937  42.457  1.00 30.56  ? 535  PHE A N   1 
ATOM   4147  C  CA  . PHE A  1 535 ? -3.200  -6.742  42.645  1.00 30.35  ? 535  PHE A CA  1 
ATOM   4148  C  C   . PHE A  1 535 ? -4.649  -6.915  42.193  1.00 26.64  ? 535  PHE A C   1 
ATOM   4149  O  O   . PHE A  1 535 ? -5.555  -6.852  43.014  1.00 27.17  ? 535  PHE A O   1 
ATOM   4150  C  CB  . PHE A  1 535 ? -2.564  -5.522  41.982  1.00 27.85  ? 535  PHE A CB  1 
ATOM   4151  C  CG  . PHE A  1 535 ? -3.347  -4.271  42.170  1.00 28.95  ? 535  PHE A CG  1 
ATOM   4152  C  CD1 . PHE A  1 535 ? -3.534  -3.746  43.431  1.00 29.80  ? 535  PHE A CD1 1 
ATOM   4153  C  CD2 . PHE A  1 535 ? -3.914  -3.623  41.088  1.00 38.00  ? 535  PHE A CD2 1 
ATOM   4154  C  CE1 . PHE A  1 535 ? -4.276  -2.589  43.612  1.00 30.91  ? 535  PHE A CE1 1 
ATOM   4155  C  CE2 . PHE A  1 535 ? -4.649  -2.467  41.260  1.00 30.34  ? 535  PHE A CE2 1 
ATOM   4156  C  CZ  . PHE A  1 535 ? -4.832  -1.950  42.526  1.00 31.17  ? 535  PHE A CZ  1 
ATOM   4157  N  N   . LEU A  1 536 ? -4.867  -7.149  40.902  1.00 26.67  ? 536  LEU A N   1 
ATOM   4158  C  CA  . LEU A  1 536 ? -6.231  -7.232  40.348  1.00 28.04  ? 536  LEU A CA  1 
ATOM   4159  C  C   . LEU A  1 536 ? -7.233  -8.086  41.129  1.00 29.20  ? 536  LEU A C   1 
ATOM   4160  O  O   . LEU A  1 536 ? -8.417  -7.757  41.145  1.00 30.29  ? 536  LEU A O   1 
ATOM   4161  C  CB  . LEU A  1 536 ? -6.236  -7.657  38.873  1.00 25.83  ? 536  LEU A CB  1 
ATOM   4162  C  CG  . LEU A  1 536 ? -7.070  -6.860  37.856  1.00 25.93  ? 536  LEU A CG  1 
ATOM   4163  C  CD1 . LEU A  1 536 ? -7.515  -7.773  36.747  1.00 25.14  ? 536  LEU A CD1 1 
ATOM   4164  C  CD2 . LEU A  1 536 ? -8.265  -6.164  38.469  1.00 26.74  ? 536  LEU A CD2 1 
ATOM   4165  N  N   . PRO A  1 537 ? -6.788  -9.205  41.730  1.00 38.38  ? 537  PRO A N   1 
ATOM   4166  C  CA  . PRO A  1 537 ? -7.766  -9.880  42.584  1.00 41.10  ? 537  PRO A CA  1 
ATOM   4167  C  C   . PRO A  1 537 ? -8.282  -8.953  43.660  1.00 44.34  ? 537  PRO A C   1 
ATOM   4168  O  O   . PRO A  1 537 ? -9.489  -8.840  43.763  1.00 49.18  ? 537  PRO A O   1 
ATOM   4169  C  CB  . PRO A  1 537 ? -6.955  -11.005 43.221  1.00 49.90  ? 537  PRO A CB  1 
ATOM   4170  C  CG  . PRO A  1 537 ? -5.949  -11.342 42.197  1.00 49.51  ? 537  PRO A CG  1 
ATOM   4171  C  CD  . PRO A  1 537 ? -5.592  -10.039 41.514  1.00 48.95  ? 537  PRO A CD  1 
ATOM   4172  N  N   . LYS A  1 538 ? -7.405  -8.249  44.374  1.00 41.30  ? 538  LYS A N   1 
ATOM   4173  C  CA  . LYS A  1 538 ? -7.824  -7.352  45.456  1.00 42.12  ? 538  LYS A CA  1 
ATOM   4174  C  C   . LYS A  1 538 ? -8.746  -6.224  44.968  1.00 42.76  ? 538  LYS A C   1 
ATOM   4175  O  O   . LYS A  1 538 ? -9.458  -5.585  45.752  1.00 42.30  ? 538  LYS A O   1 
ATOM   4176  C  CB  . LYS A  1 538 ? -6.603  -6.760  46.170  1.00 40.92  ? 538  LYS A CB  1 
ATOM   4177  C  CG  . LYS A  1 538 ? -5.743  -7.772  46.875  1.00 44.42  ? 538  LYS A CG  1 
ATOM   4178  C  CD  . LYS A  1 538 ? -4.477  -7.131  47.399  1.00 52.42  ? 538  LYS A CD  1 
ATOM   4179  C  CE  . LYS A  1 538 ? -3.471  -8.206  47.815  1.00 59.46  ? 538  LYS A CE  1 
ATOM   4180  N  NZ  . LYS A  1 538 ? -2.040  -7.800  47.604  1.00 63.25  ? 538  LYS A NZ  1 
ATOM   4181  N  N   . LEU A  1 539 ? -8.738  -5.993  43.665  1.00 47.79  ? 539  LEU A N   1 
ATOM   4182  C  CA  . LEU A  1 539 ? -9.480  -4.886  43.118  1.00 50.53  ? 539  LEU A CA  1 
ATOM   4183  C  C   . LEU A  1 539 ? -10.934 -5.250  42.936  1.00 60.33  ? 539  LEU A C   1 
ATOM   4184  O  O   . LEU A  1 539 ? -11.754 -4.828  43.730  1.00 69.03  ? 539  LEU A O   1 
ATOM   4185  C  CB  . LEU A  1 539 ? -8.872  -4.428  41.806  1.00 40.57  ? 539  LEU A CB  1 
ATOM   4186  C  CG  . LEU A  1 539 ? -9.132  -2.963  41.492  1.00 38.77  ? 539  LEU A CG  1 
ATOM   4187  C  CD1 . LEU A  1 539 ? -9.103  -2.135  42.758  1.00 37.17  ? 539  LEU A CD1 1 
ATOM   4188  C  CD2 . LEU A  1 539 ? -8.070  -2.486  40.528  1.00 39.90  ? 539  LEU A CD2 1 
ATOM   4189  N  N   . LEU A  1 540 ? -11.256 -6.090  41.954  1.00 61.30  ? 540  LEU A N   1 
ATOM   4190  C  CA  . LEU A  1 540 ? -12.665 -6.382  41.594  1.00 63.79  ? 540  LEU A CA  1 
ATOM   4191  C  C   . LEU A  1 540 ? -13.458 -7.064  42.740  1.00 98.21  ? 540  LEU A C   1 
ATOM   4192  O  O   . LEU A  1 540 ? -14.666 -7.325  42.660  1.00 96.34  ? 540  LEU A O   1 
ATOM   4193  C  CB  . LEU A  1 540 ? -12.770 -7.110  40.232  1.00 56.39  ? 540  LEU A CB  1 
ATOM   4194  C  CG  . LEU A  1 540 ? -12.193 -8.495  39.882  1.00 52.29  ? 540  LEU A CG  1 
ATOM   4195  C  CD1 . LEU A  1 540 ? -11.556 -8.500  38.492  1.00 47.93  ? 540  LEU A CD1 1 
ATOM   4196  C  CD2 . LEU A  1 540 ? -11.227 -9.032  40.927  1.00 52.64  ? 540  LEU A CD2 1 
ATOM   4197  N  N   . SER A  1 541 ? -12.699 -7.303  43.801  1.00 94.59  ? 541  SER A N   1 
ATOM   4198  C  CA  . SER A  1 541 ? -13.008 -7.985  45.057  1.00 98.00  ? 541  SER A CA  1 
ATOM   4199  C  C   . SER A  1 541 ? -13.503 -7.196  46.286  1.00 102.08 ? 541  SER A C   1 
ATOM   4200  O  O   . SER A  1 541 ? -13.142 -7.596  47.401  1.00 103.27 ? 541  SER A O   1 
ATOM   4201  C  CB  . SER A  1 541 ? -11.910 -8.970  45.442  1.00 108.20 ? 541  SER A CB  1 
ATOM   4202  O  OG  . SER A  1 541 ? -11.821 -9.995  44.462  1.00 109.85 ? 541  SER A OG  1 
ATOM   4203  N  N   . ALA A  1 542 ? -14.313 -6.135  46.132  1.00 102.67 ? 542  ALA A N   1 
ATOM   4204  C  CA  . ALA A  1 542 ? -14.221 -4.809  46.792  1.00 102.74 ? 542  ALA A CA  1 
ATOM   4205  C  C   . ALA A  1 542 ? -13.992 -3.683  45.790  1.00 103.39 ? 542  ALA A C   1 
ATOM   4206  O  O   . ALA A  1 542 ? -13.753 -2.540  46.187  1.00 101.47 ? 542  ALA A O   1 
ATOM   4207  C  CB  . ALA A  1 542 ? -13.126 -4.765  47.871  1.00 100.71 ? 542  ALA A CB  1 
ATOM   4208  N  N   . THR A  1 543 ? -14.026 -4.055  44.505  1.00 118.09 ? 543  THR A N   1 
ATOM   4209  C  CA  . THR A  1 543 ? -14.352 -3.185  43.348  1.00 120.82 ? 543  THR A CA  1 
ATOM   4210  C  C   . THR A  1 543 ? -14.401 -1.677  43.565  1.00 124.58 ? 543  THR A C   1 
ATOM   4211  O  O   . THR A  1 543 ? -13.722 -0.953  42.840  1.00 125.94 ? 543  THR A O   1 
ATOM   4212  C  CB  . THR A  1 543 ? -15.707 -3.594  42.688  1.00 120.11 ? 543  THR A CB  1 
ATOM   4213  O  OG1 . THR A  1 543 ? -15.599 -4.900  42.107  1.00 119.52 ? 543  THR A OG1 1 
ATOM   4214  C  CG2 . THR A  1 543 ? -16.113 -2.592  41.607  1.00 119.48 ? 543  THR A CG2 1 
ATOM   4215  O  OXT . THR A  1 543 ? -15.121 -1.147  44.418  1.00 119.59 ? 543  THR A OXT 1 
ATOM   4216  N  N   . ASP B  1 5   ? 26.281  59.699  45.964  1.00 85.84  ? 5    ASP B N   1 
ATOM   4217  C  CA  . ASP B  1 5   ? 26.001  58.782  44.858  1.00 86.02  ? 5    ASP B CA  1 
ATOM   4218  C  C   . ASP B  1 5   ? 24.573  58.952  44.315  1.00 86.35  ? 5    ASP B C   1 
ATOM   4219  O  O   . ASP B  1 5   ? 23.605  58.874  45.066  1.00 83.00  ? 5    ASP B O   1 
ATOM   4220  C  CB  . ASP B  1 5   ? 26.245  57.335  45.290  1.00 96.31  ? 5    ASP B CB  1 
ATOM   4221  C  CG  . ASP B  1 5   ? 26.868  56.492  44.189  1.00 97.50  ? 5    ASP B CG  1 
ATOM   4222  O  OD1 . ASP B  1 5   ? 26.150  56.136  43.226  1.00 97.41  ? 5    ASP B OD1 1 
ATOM   4223  O  OD2 . ASP B  1 5   ? 28.075  56.175  44.295  1.00 98.16  ? 5    ASP B OD2 1 
ATOM   4224  N  N   . PRO B  1 6   ? 24.445  59.199  42.999  1.00 112.95 ? 6    PRO B N   1 
ATOM   4225  C  CA  . PRO B  1 6   ? 23.159  59.571  42.388  1.00 114.88 ? 6    PRO B CA  1 
ATOM   4226  C  C   . PRO B  1 6   ? 22.121  58.457  42.377  1.00 111.51 ? 6    PRO B C   1 
ATOM   4227  O  O   . PRO B  1 6   ? 20.953  58.694  42.692  1.00 109.50 ? 6    PRO B O   1 
ATOM   4228  C  CB  . PRO B  1 6   ? 23.550  59.913  40.943  1.00 126.90 ? 6    PRO B CB  1 
ATOM   4229  C  CG  . PRO B  1 6   ? 24.773  59.084  40.673  1.00 126.96 ? 6    PRO B CG  1 
ATOM   4230  C  CD  . PRO B  1 6   ? 25.509  59.015  41.991  1.00 125.68 ? 6    PRO B CD  1 
ATOM   4231  N  N   . GLN B  1 7   ? 22.565  57.254  42.028  1.00 109.22 ? 7    GLN B N   1 
ATOM   4232  C  CA  . GLN B  1 7   ? 21.676  56.138  41.743  1.00 106.81 ? 7    GLN B CA  1 
ATOM   4233  C  C   . GLN B  1 7   ? 21.107  55.583  43.025  1.00 104.94 ? 7    GLN B C   1 
ATOM   4234  O  O   . GLN B  1 7   ? 19.974  55.104  43.058  1.00 104.64 ? 7    GLN B O   1 
ATOM   4235  C  CB  . GLN B  1 7   ? 22.449  55.037  41.021  1.00 102.10 ? 7    GLN B CB  1 
ATOM   4236  C  CG  . GLN B  1 7   ? 23.160  55.499  39.763  1.00 105.20 ? 7    GLN B CG  1 
ATOM   4237  C  CD  . GLN B  1 7   ? 22.269  55.466  38.540  1.00 106.41 ? 7    GLN B CD  1 
ATOM   4238  O  OE1 . GLN B  1 7   ? 22.438  54.620  37.662  1.00 107.11 ? 7    GLN B OE1 1 
ATOM   4239  N  NE2 . GLN B  1 7   ? 21.316  56.389  38.472  1.00 106.37 ? 7    GLN B NE2 1 
ATOM   4240  N  N   . LEU B  1 8   ? 21.909  55.660  44.080  1.00 99.98  ? 8    LEU B N   1 
ATOM   4241  C  CA  . LEU B  1 8   ? 21.569  55.075  45.369  1.00 95.32  ? 8    LEU B CA  1 
ATOM   4242  C  C   . LEU B  1 8   ? 20.381  55.763  46.053  1.00 95.17  ? 8    LEU B C   1 
ATOM   4243  O  O   . LEU B  1 8   ? 19.946  55.326  47.111  1.00 94.99  ? 8    LEU B O   1 
ATOM   4244  C  CB  . LEU B  1 8   ? 22.793  54.991  46.298  1.00 76.48  ? 8    LEU B CB  1 
ATOM   4245  C  CG  . LEU B  1 8   ? 24.074  54.262  45.834  1.00 77.16  ? 8    LEU B CG  1 
ATOM   4246  C  CD1 . LEU B  1 8   ? 24.818  53.645  47.016  1.00 76.25  ? 8    LEU B CD1 1 
ATOM   4247  C  CD2 . LEU B  1 8   ? 23.851  53.214  44.741  1.00 76.58  ? 8    LEU B CD2 1 
ATOM   4248  N  N   . LEU B  1 9   ? 19.867  56.840  45.463  1.00 104.63 ? 9    LEU B N   1 
ATOM   4249  C  CA  . LEU B  1 9   ? 18.678  57.514  46.000  1.00 102.41 ? 9    LEU B CA  1 
ATOM   4250  C  C   . LEU B  1 9   ? 17.481  57.538  45.020  1.00 99.21  ? 9    LEU B C   1 
ATOM   4251  O  O   . LEU B  1 9   ? 17.563  58.143  43.947  1.00 100.31 ? 9    LEU B O   1 
ATOM   4252  C  CB  . LEU B  1 9   ? 19.048  58.927  46.470  1.00 89.59  ? 9    LEU B CB  1 
ATOM   4253  C  CG  . LEU B  1 9   ? 18.001  59.767  47.203  1.00 87.02  ? 9    LEU B CG  1 
ATOM   4254  C  CD1 . LEU B  1 9   ? 18.664  60.582  48.303  1.00 86.02  ? 9    LEU B CD1 1 
ATOM   4255  C  CD2 . LEU B  1 9   ? 17.261  60.683  46.230  1.00 88.43  ? 9    LEU B CD2 1 
ATOM   4256  N  N   . VAL B  1 10  ? 16.373  56.894  45.406  1.00 74.12  ? 10   VAL B N   1 
ATOM   4257  C  CA  . VAL B  1 10  ? 15.206  56.731  44.520  1.00 73.73  ? 10   VAL B CA  1 
ATOM   4258  C  C   . VAL B  1 10  ? 13.858  57.035  45.210  1.00 73.24  ? 10   VAL B C   1 
ATOM   4259  O  O   . VAL B  1 10  ? 13.734  56.887  46.424  1.00 71.38  ? 10   VAL B O   1 
ATOM   4260  C  CB  . VAL B  1 10  ? 15.202  55.322  43.876  1.00 77.93  ? 10   VAL B CB  1 
ATOM   4261  C  CG1 . VAL B  1 10  ? 15.161  54.256  44.950  1.00 77.54  ? 10   VAL B CG1 1 
ATOM   4262  C  CG2 . VAL B  1 10  ? 14.059  55.156  42.868  1.00 74.03  ? 10   VAL B CG2 1 
ATOM   4263  N  N   . ARG B  1 11  ? 12.855  57.446  44.428  1.00 97.85  ? 11   ARG B N   1 
ATOM   4264  C  CA  . ARG B  1 11  ? 11.649  58.093  44.970  1.00 102.91 ? 11   ARG B CA  1 
ATOM   4265  C  C   . ARG B  1 11  ? 10.508  57.229  45.534  1.00 101.06 ? 11   ARG B C   1 
ATOM   4266  O  O   . ARG B  1 11  ? 10.187  57.394  46.707  1.00 102.47 ? 11   ARG B O   1 
ATOM   4267  C  CB  . ARG B  1 11  ? 11.123  59.202  44.050  1.00 109.14 ? 11   ARG B CB  1 
ATOM   4268  C  CG  . ARG B  1 11  ? 11.412  60.621  44.582  1.00 113.15 ? 11   ARG B CG  1 
ATOM   4269  C  CD  . ARG B  1 11  ? 10.235  61.191  45.382  1.00 112.82 ? 11   ARG B CD  1 
ATOM   4270  N  NE  . ARG B  1 11  ? 10.546  61.487  46.783  1.00 112.22 ? 11   ARG B NE  1 
ATOM   4271  C  CZ  . ARG B  1 11  ? 11.091  62.623  47.213  1.00 113.56 ? 11   ARG B CZ  1 
ATOM   4272  N  NH1 . ARG B  1 11  ? 11.414  63.577  46.346  1.00 116.92 ? 11   ARG B NH1 1 
ATOM   4273  N  NH2 . ARG B  1 11  ? 11.318  62.801  48.511  1.00 110.68 ? 11   ARG B NH2 1 
ATOM   4274  N  N   . VAL B  1 12  ? 9.867   56.363  44.737  1.00 83.10  ? 12   VAL B N   1 
ATOM   4275  C  CA  . VAL B  1 12  ? 8.893   55.405  45.324  1.00 76.83  ? 12   VAL B CA  1 
ATOM   4276  C  C   . VAL B  1 12  ? 7.675   55.966  46.086  1.00 73.17  ? 12   VAL B C   1 
ATOM   4277  O  O   . VAL B  1 12  ? 7.806   56.350  47.242  1.00 70.66  ? 12   VAL B O   1 
ATOM   4278  C  CB  . VAL B  1 12  ? 9.508   54.124  46.024  1.00 71.48  ? 12   VAL B CB  1 
ATOM   4279  C  CG1 . VAL B  1 12  ? 10.480  53.425  45.106  1.00 71.44  ? 12   VAL B CG1 1 
ATOM   4280  C  CG2 . VAL B  1 12  ? 10.150  54.420  47.366  1.00 65.15  ? 12   VAL B CG2 1 
ATOM   4281  N  N   . ARG B  1 13  ? 6.524   56.073  45.425  1.00 83.33  ? 13   ARG B N   1 
ATOM   4282  C  CA  . ARG B  1 13  ? 5.349   56.817  45.919  1.00 88.53  ? 13   ARG B CA  1 
ATOM   4283  C  C   . ARG B  1 13  ? 5.113   56.787  47.456  1.00 98.27  ? 13   ARG B C   1 
ATOM   4284  O  O   . ARG B  1 13  ? 4.399   57.637  47.997  1.00 100.38 ? 13   ARG B O   1 
ATOM   4285  C  CB  . ARG B  1 13  ? 4.091   56.299  45.185  1.00 96.22  ? 13   ARG B CB  1 
ATOM   4286  C  CG  . ARG B  1 13  ? 2.748   56.949  45.570  1.00 100.49 ? 13   ARG B CG  1 
ATOM   4287  C  CD  . ARG B  1 13  ? 1.682   55.895  45.878  1.00 103.01 ? 13   ARG B CD  1 
ATOM   4288  N  NE  . ARG B  1 13  ? 0.600   55.852  44.891  1.00 107.31 ? 13   ARG B NE  1 
ATOM   4289  C  CZ  . ARG B  1 13  ? 0.684   55.264  43.696  1.00 109.55 ? 13   ARG B CZ  1 
ATOM   4290  N  NH1 . ARG B  1 13  ? 1.811   54.679  43.313  1.00 110.57 ? 13   ARG B NH1 1 
ATOM   4291  N  NH2 . ARG B  1 13  ? -0.358  55.271  42.873  1.00 109.07 ? 13   ARG B NH2 1 
ATOM   4292  N  N   . GLY B  1 14  ? 5.693   55.816  48.158  1.00 89.61  ? 14   GLY B N   1 
ATOM   4293  C  CA  . GLY B  1 14  ? 5.802   55.903  49.609  1.00 85.19  ? 14   GLY B CA  1 
ATOM   4294  C  C   . GLY B  1 14  ? 6.826   56.899  50.173  1.00 82.99  ? 14   GLY B C   1 
ATOM   4295  O  O   . GLY B  1 14  ? 6.804   57.187  51.372  1.00 80.28  ? 14   GLY B O   1 
ATOM   4296  N  N   . GLY B  1 15  ? 7.697   57.451  49.321  1.00 85.01  ? 15   GLY B N   1 
ATOM   4297  C  CA  . GLY B  1 15  ? 8.764   58.351  49.760  1.00 84.66  ? 15   GLY B CA  1 
ATOM   4298  C  C   . GLY B  1 15  ? 10.209  57.848  49.699  1.00 84.27  ? 15   GLY B C   1 
ATOM   4299  O  O   . GLY B  1 15  ? 10.464  56.707  49.341  1.00 84.46  ? 15   GLY B O   1 
ATOM   4300  N  N   . GLN B  1 16  ? 11.153  58.710  50.079  1.00 79.24  ? 16   GLN B N   1 
ATOM   4301  C  CA  . GLN B  1 16  ? 12.595  58.560  49.781  1.00 80.09  ? 16   GLN B CA  1 
ATOM   4302  C  C   . GLN B  1 16  ? 13.303  57.265  50.216  1.00 74.92  ? 16   GLN B C   1 
ATOM   4303  O  O   . GLN B  1 16  ? 13.024  56.719  51.280  1.00 74.14  ? 16   GLN B O   1 
ATOM   4304  C  CB  . GLN B  1 16  ? 13.357  59.765  50.344  1.00 100.20 ? 16   GLN B CB  1 
ATOM   4305  C  CG  . GLN B  1 16  ? 14.749  59.969  49.772  1.00 105.67 ? 16   GLN B CG  1 
ATOM   4306  C  CD  . GLN B  1 16  ? 14.940  61.371  49.226  1.00 110.81 ? 16   GLN B CD  1 
ATOM   4307  O  OE1 . GLN B  1 16  ? 15.922  62.052  49.539  1.00 113.95 ? 16   GLN B OE1 1 
ATOM   4308  N  NE2 . GLN B  1 16  ? 13.997  61.813  48.401  1.00 110.73 ? 16   GLN B NE2 1 
ATOM   4309  N  N   . LEU B  1 17  ? 14.242  56.805  49.390  1.00 70.04  ? 17   LEU B N   1 
ATOM   4310  C  CA  . LEU B  1 17  ? 14.971  55.558  49.632  1.00 69.15  ? 17   LEU B CA  1 
ATOM   4311  C  C   . LEU B  1 17  ? 16.473  55.693  49.381  1.00 69.81  ? 17   LEU B C   1 
ATOM   4312  O  O   . LEU B  1 17  ? 16.880  56.297  48.395  1.00 71.55  ? 17   LEU B O   1 
ATOM   4313  C  CB  . LEU B  1 17  ? 14.444  54.453  48.707  1.00 67.24  ? 17   LEU B CB  1 
ATOM   4314  C  CG  . LEU B  1 17  ? 13.285  53.511  49.049  1.00 65.04  ? 17   LEU B CG  1 
ATOM   4315  C  CD1 . LEU B  1 17  ? 13.092  52.556  47.886  1.00 64.56  ? 17   LEU B CD1 1 
ATOM   4316  C  CD2 . LEU B  1 17  ? 13.537  52.737  50.341  1.00 63.48  ? 17   LEU B CD2 1 
ATOM   4317  N  N   . ARG B  1 18  ? 17.294  55.107  50.251  1.00 69.16  ? 18   ARG B N   1 
ATOM   4318  C  CA  . ARG B  1 18  ? 18.741  55.052  50.016  1.00 75.34  ? 18   ARG B CA  1 
ATOM   4319  C  C   . ARG B  1 18  ? 19.281  53.639  49.837  1.00 70.97  ? 18   ARG B C   1 
ATOM   4320  O  O   . ARG B  1 18  ? 19.374  52.884  50.801  1.00 68.66  ? 18   ARG B O   1 
ATOM   4321  C  CB  . ARG B  1 18  ? 19.518  55.746  51.141  1.00 102.94 ? 18   ARG B CB  1 
ATOM   4322  C  CG  . ARG B  1 18  ? 21.036  55.577  51.052  1.00 105.02 ? 18   ARG B CG  1 
ATOM   4323  C  CD  . ARG B  1 18  ? 21.777  56.575  51.937  1.00 107.76 ? 18   ARG B CD  1 
ATOM   4324  N  NE  . ARG B  1 18  ? 21.388  57.963  51.673  1.00 111.69 ? 18   ARG B NE  1 
ATOM   4325  C  CZ  . ARG B  1 18  ? 21.695  58.645  50.567  1.00 114.87 ? 18   ARG B CZ  1 
ATOM   4326  N  NH1 . ARG B  1 18  ? 22.395  58.076  49.588  1.00 114.65 ? 18   ARG B NH1 1 
ATOM   4327  N  NH2 . ARG B  1 18  ? 21.292  59.905  50.435  1.00 116.30 ? 18   ARG B NH2 1 
ATOM   4328  N  N   . GLY B  1 19  ? 19.691  53.309  48.615  1.00 79.18  ? 19   GLY B N   1 
ATOM   4329  C  CA  . GLY B  1 19  ? 20.212  51.989  48.299  1.00 78.32  ? 19   GLY B CA  1 
ATOM   4330  C  C   . GLY B  1 19  ? 21.630  51.758  48.782  1.00 79.69  ? 19   GLY B C   1 
ATOM   4331  O  O   . GLY B  1 19  ? 22.102  52.444  49.682  1.00 79.41  ? 19   GLY B O   1 
ATOM   4332  N  N   . ILE B  1 20  ? 22.297  50.768  48.199  1.00 97.16  ? 20   ILE B N   1 
ATOM   4333  C  CA  . ILE B  1 20  ? 23.700  50.491  48.496  1.00 101.14 ? 20   ILE B CA  1 
ATOM   4334  C  C   . ILE B  1 20  ? 24.378  49.939  47.243  1.00 103.93 ? 20   ILE B C   1 
ATOM   4335  O  O   . ILE B  1 20  ? 23.751  49.201  46.474  1.00 104.90 ? 20   ILE B O   1 
ATOM   4336  C  CB  . ILE B  1 20  ? 23.863  49.489  49.672  1.00 73.03  ? 20   ILE B CB  1 
ATOM   4337  C  CG1 . ILE B  1 20  ? 25.346  49.158  49.902  1.00 73.56  ? 20   ILE B CG1 1 
ATOM   4338  C  CG2 . ILE B  1 20  ? 23.053  48.227  49.417  1.00 72.08  ? 20   ILE B CG2 1 
ATOM   4339  C  CD1 . ILE B  1 20  ? 25.603  47.871  50.670  1.00 68.35  ? 20   ILE B CD1 1 
ATOM   4340  N  N   . ARG B  1 21  ? 25.643  50.310  47.031  1.00 93.91  ? 21   ARG B N   1 
ATOM   4341  C  CA  . ARG B  1 21  ? 26.414  49.805  45.893  1.00 91.62  ? 21   ARG B CA  1 
ATOM   4342  C  C   . ARG B  1 21  ? 27.136  48.495  46.227  1.00 85.18  ? 21   ARG B C   1 
ATOM   4343  O  O   . ARG B  1 21  ? 27.827  48.394  47.250  1.00 81.25  ? 21   ARG B O   1 
ATOM   4344  C  CB  . ARG B  1 21  ? 27.409  50.858  45.396  1.00 101.18 ? 21   ARG B CB  1 
ATOM   4345  C  CG  . ARG B  1 21  ? 27.188  51.293  43.949  1.00 104.72 ? 21   ARG B CG  1 
ATOM   4346  C  CD  . ARG B  1 21  ? 28.230  52.328  43.491  1.00 109.00 ? 21   ARG B CD  1 
ATOM   4347  N  NE  . ARG B  1 21  ? 29.528  51.739  43.155  1.00 109.37 ? 21   ARG B NE  1 
ATOM   4348  C  CZ  . ARG B  1 21  ? 29.931  51.473  41.916  1.00 109.24 ? 21   ARG B CZ  1 
ATOM   4349  N  NH1 . ARG B  1 21  ? 29.140  51.747  40.888  1.00 108.93 ? 21   ARG B NH1 1 
ATOM   4350  N  NH2 . ARG B  1 21  ? 31.126  50.937  41.701  1.00 109.84 ? 21   ARG B NH2 1 
ATOM   4351  N  N   . LEU B  1 22  ? 26.965  47.500  45.353  1.00 81.46  ? 22   LEU B N   1 
ATOM   4352  C  CA  . LEU B  1 22  ? 27.524  46.163  45.576  1.00 81.25  ? 22   LEU B CA  1 
ATOM   4353  C  C   . LEU B  1 22  ? 28.341  45.631  44.399  1.00 81.76  ? 22   LEU B C   1 
ATOM   4354  O  O   . LEU B  1 22  ? 28.075  45.956  43.235  1.00 80.66  ? 22   LEU B O   1 
ATOM   4355  C  CB  . LEU B  1 22  ? 26.410  45.152  45.847  1.00 82.83  ? 22   LEU B CB  1 
ATOM   4356  C  CG  . LEU B  1 22  ? 25.554  45.125  47.104  1.00 78.52  ? 22   LEU B CG  1 
ATOM   4357  C  CD1 . LEU B  1 22  ? 24.630  43.930  46.943  1.00 74.90  ? 22   LEU B CD1 1 
ATOM   4358  C  CD2 . LEU B  1 22  ? 26.412  45.029  48.370  1.00 76.78  ? 22   LEU B CD2 1 
ATOM   4359  N  N   . LYS B  1 23  ? 29.298  44.761  44.714  1.00 81.49  ? 23   LYS B N   1 
ATOM   4360  C  CA  . LYS B  1 23  ? 30.177  44.183  43.702  1.00 86.90  ? 23   LYS B CA  1 
ATOM   4361  C  C   . LYS B  1 23  ? 29.745  42.807  43.161  1.00 84.11  ? 23   LYS B C   1 
ATOM   4362  O  O   . LYS B  1 23  ? 29.790  41.790  43.861  1.00 80.25  ? 23   LYS B O   1 
ATOM   4363  C  CB  . LYS B  1 23  ? 31.622  44.112  44.228  1.00 111.72 ? 23   LYS B CB  1 
ATOM   4364  C  CG  . LYS B  1 23  ? 31.782  43.386  45.567  1.00 113.43 ? 23   LYS B CG  1 
ATOM   4365  C  CD  . LYS B  1 23  ? 33.097  42.614  45.636  1.00 115.49 ? 23   LYS B CD  1 
ATOM   4366  C  CE  . LYS B  1 23  ? 32.876  41.199  46.159  1.00 113.68 ? 23   LYS B CE  1 
ATOM   4367  N  NZ  . LYS B  1 23  ? 32.191  41.193  47.485  1.00 111.41 ? 23   LYS B NZ  1 
ATOM   4368  N  N   . ALA B  1 24  ? 29.328  42.784  41.902  1.00 104.25 ? 24   ALA B N   1 
ATOM   4369  C  CA  . ALA B  1 24  ? 29.243  41.535  41.162  1.00 105.56 ? 24   ALA B CA  1 
ATOM   4370  C  C   . ALA B  1 24  ? 30.585  41.339  40.447  1.00 111.27 ? 24   ALA B C   1 
ATOM   4371  O  O   . ALA B  1 24  ? 31.306  42.318  40.205  1.00 115.71 ? 24   ALA B O   1 
ATOM   4372  C  CB  . ALA B  1 24  ? 28.087  41.584  40.166  1.00 89.16  ? 24   ALA B CB  1 
ATOM   4373  N  N   . PRO B  1 25  ? 30.940  40.081  40.124  1.00 100.06 ? 25   PRO B N   1 
ATOM   4374  C  CA  . PRO B  1 25  ? 32.163  39.780  39.366  1.00 100.93 ? 25   PRO B CA  1 
ATOM   4375  C  C   . PRO B  1 25  ? 32.350  40.639  38.113  1.00 101.43 ? 25   PRO B C   1 
ATOM   4376  O  O   . PRO B  1 25  ? 33.480  41.006  37.796  1.00 101.32 ? 25   PRO B O   1 
ATOM   4377  C  CB  . PRO B  1 25  ? 31.961  38.315  38.968  1.00 89.46  ? 25   PRO B CB  1 
ATOM   4378  C  CG  . PRO B  1 25  ? 31.219  37.746  40.116  1.00 86.30  ? 25   PRO B CG  1 
ATOM   4379  C  CD  . PRO B  1 25  ? 30.301  38.850  40.621  1.00 86.41  ? 25   PRO B CD  1 
ATOM   4380  N  N   . GLY B  1 26  ? 31.259  40.956  37.423  1.00 107.07 ? 26   GLY B N   1 
ATOM   4381  C  CA  . GLY B  1 26  ? 31.341  41.673  36.164  1.00 110.28 ? 26   GLY B CA  1 
ATOM   4382  C  C   . GLY B  1 26  ? 30.912  43.133  36.149  1.00 110.91 ? 26   GLY B C   1 
ATOM   4383  O  O   . GLY B  1 26  ? 30.857  43.751  35.082  1.00 113.71 ? 26   GLY B O   1 
ATOM   4384  N  N   . GLY B  1 27  ? 30.621  43.699  37.316  1.00 96.91  ? 27   GLY B N   1 
ATOM   4385  C  CA  . GLY B  1 27  ? 30.191  45.086  37.376  1.00 97.77  ? 27   GLY B CA  1 
ATOM   4386  C  C   . GLY B  1 27  ? 29.774  45.541  38.762  1.00 97.47  ? 27   GLY B C   1 
ATOM   4387  O  O   . GLY B  1 27  ? 30.096  44.881  39.756  1.00 94.81  ? 27   GLY B O   1 
ATOM   4388  N  N   . PRO B  1 28  ? 29.138  46.725  38.852  1.00 114.83 ? 28   PRO B N   1 
ATOM   4389  C  CA  . PRO B  1 28  ? 28.434  47.065  40.088  1.00 113.90 ? 28   PRO B CA  1 
ATOM   4390  C  C   . PRO B  1 28  ? 26.927  46.803  40.003  1.00 113.36 ? 28   PRO B C   1 
ATOM   4391  O  O   . PRO B  1 28  ? 26.371  46.641  38.903  1.00 114.23 ? 28   PRO B O   1 
ATOM   4392  C  CB  . PRO B  1 28  ? 28.693  48.567  40.207  1.00 100.48 ? 28   PRO B CB  1 
ATOM   4393  C  CG  . PRO B  1 28  ? 28.919  49.040  38.754  1.00 102.63 ? 28   PRO B CG  1 
ATOM   4394  C  CD  . PRO B  1 28  ? 29.053  47.819  37.872  1.00 102.90 ? 28   PRO B CD  1 
ATOM   4395  N  N   . VAL B  1 29  ? 26.254  46.890  41.149  1.00 94.70  ? 29   VAL B N   1 
ATOM   4396  C  CA  . VAL B  1 29  ? 24.793  46.820  41.191  1.00 90.15  ? 29   VAL B CA  1 
ATOM   4397  C  C   . VAL B  1 29  ? 24.238  47.711  42.279  1.00 86.82  ? 29   VAL B C   1 
ATOM   4398  O  O   . VAL B  1 29  ? 24.823  47.838  43.361  1.00 82.73  ? 29   VAL B O   1 
ATOM   4399  C  CB  . VAL B  1 29  ? 24.240  45.394  41.422  1.00 93.02  ? 29   VAL B CB  1 
ATOM   4400  C  CG1 . VAL B  1 29  ? 24.486  44.500  40.210  1.00 92.48  ? 29   VAL B CG1 1 
ATOM   4401  C  CG2 . VAL B  1 29  ? 24.817  44.795  42.689  1.00 92.37  ? 29   VAL B CG2 1 
ATOM   4402  N  N   . SER B  1 30  ? 23.102  48.324  41.966  1.00 110.81 ? 30   SER B N   1 
ATOM   4403  C  CA  . SER B  1 30  ? 22.344  49.108  42.919  1.00 113.93 ? 30   SER B CA  1 
ATOM   4404  C  C   . SER B  1 30  ? 21.387  48.146  43.605  1.00 111.11 ? 30   SER B C   1 
ATOM   4405  O  O   . SER B  1 30  ? 20.477  47.599  42.972  1.00 112.24 ? 30   SER B O   1 
ATOM   4406  C  CB  . SER B  1 30  ? 21.546  50.206  42.207  1.00 101.24 ? 30   SER B CB  1 
ATOM   4407  O  OG  . SER B  1 30  ? 22.360  50.979  41.345  1.00 103.74 ? 30   SER B OG  1 
ATOM   4408  N  N   . ALA B  1 31  ? 21.607  47.945  44.902  1.00 86.65  ? 31   ALA B N   1 
ATOM   4409  C  CA  . ALA B  1 31  ? 20.818  47.019  45.690  1.00 76.38  ? 31   ALA B CA  1 
ATOM   4410  C  C   . ALA B  1 31  ? 19.987  47.826  46.663  1.00 76.42  ? 31   ALA B C   1 
ATOM   4411  O  O   . ALA B  1 31  ? 20.537  48.623  47.411  1.00 77.72  ? 31   ALA B O   1 
ATOM   4412  C  CB  . ALA B  1 31  ? 21.738  46.085  46.444  1.00 65.65  ? 31   ALA B CB  1 
ATOM   4413  N  N   . PHE B  1 32  ? 18.668  47.637  46.651  1.00 84.27  ? 32   PHE B N   1 
ATOM   4414  C  CA  . PHE B  1 32  ? 17.794  48.308  47.619  1.00 86.22  ? 32   PHE B CA  1 
ATOM   4415  C  C   . PHE B  1 32  ? 17.066  47.273  48.472  1.00 81.86  ? 32   PHE B C   1 
ATOM   4416  O  O   . PHE B  1 32  ? 16.160  46.601  47.996  1.00 82.92  ? 32   PHE B O   1 
ATOM   4417  C  CB  . PHE B  1 32  ? 16.770  49.190  46.900  1.00 92.31  ? 32   PHE B CB  1 
ATOM   4418  C  CG  . PHE B  1 32  ? 17.360  50.057  45.825  1.00 96.41  ? 32   PHE B CG  1 
ATOM   4419  C  CD1 . PHE B  1 32  ? 17.531  49.570  44.539  1.00 97.23  ? 32   PHE B CD1 1 
ATOM   4420  C  CD2 . PHE B  1 32  ? 17.736  51.362  46.100  1.00 99.06  ? 32   PHE B CD2 1 
ATOM   4421  C  CE1 . PHE B  1 32  ? 18.071  50.363  43.557  1.00 100.99 ? 32   PHE B CE1 1 
ATOM   4422  C  CE2 . PHE B  1 32  ? 18.281  52.163  45.123  1.00 101.89 ? 32   PHE B CE2 1 
ATOM   4423  C  CZ  . PHE B  1 32  ? 18.449  51.666  43.849  1.00 103.38 ? 32   PHE B CZ  1 
ATOM   4424  N  N   . LEU B  1 33  ? 17.435  47.173  49.743  1.00 71.74  ? 33   LEU B N   1 
ATOM   4425  C  CA  . LEU B  1 33  ? 16.982  46.057  50.567  1.00 67.05  ? 33   LEU B CA  1 
ATOM   4426  C  C   . LEU B  1 33  ? 16.101  46.483  51.752  1.00 66.67  ? 33   LEU B C   1 
ATOM   4427  O  O   . LEU B  1 33  ? 16.502  47.296  52.582  1.00 70.11  ? 33   LEU B O   1 
ATOM   4428  C  CB  . LEU B  1 33  ? 18.190  45.247  51.064  1.00 58.73  ? 33   LEU B CB  1 
ATOM   4429  C  CG  . LEU B  1 33  ? 19.319  44.944  50.068  1.00 60.00  ? 33   LEU B CG  1 
ATOM   4430  C  CD1 . LEU B  1 33  ? 20.385  44.044  50.681  1.00 59.73  ? 33   LEU B CD1 1 
ATOM   4431  C  CD2 . LEU B  1 33  ? 18.786  44.327  48.796  1.00 59.72  ? 33   LEU B CD2 1 
ATOM   4432  N  N   . GLY B  1 34  ? 14.905  45.920  51.849  1.00 56.28  ? 34   GLY B N   1 
ATOM   4433  C  CA  . GLY B  1 34  ? 14.102  46.173  53.025  1.00 55.29  ? 34   GLY B CA  1 
ATOM   4434  C  C   . GLY B  1 34  ? 13.147  47.320  52.846  1.00 55.83  ? 34   GLY B C   1 
ATOM   4435  O  O   . GLY B  1 34  ? 12.744  47.964  53.806  1.00 55.70  ? 34   GLY B O   1 
ATOM   4436  N  N   . ILE B  1 35  ? 12.796  47.583  51.600  1.00 56.53  ? 35   ILE B N   1 
ATOM   4437  C  CA  . ILE B  1 35  ? 11.741  48.537  51.312  1.00 60.53  ? 35   ILE B CA  1 
ATOM   4438  C  C   . ILE B  1 35  ? 10.448  48.016  51.905  1.00 56.08  ? 35   ILE B C   1 
ATOM   4439  O  O   . ILE B  1 35  ? 9.982   46.945  51.521  1.00 53.94  ? 35   ILE B O   1 
ATOM   4440  C  CB  . ILE B  1 35  ? 11.523  48.670  49.795  1.00 57.83  ? 35   ILE B CB  1 
ATOM   4441  C  CG1 . ILE B  1 35  ? 12.856  48.946  49.073  1.00 59.53  ? 35   ILE B CG1 1 
ATOM   4442  C  CG2 . ILE B  1 35  ? 10.415  49.691  49.510  1.00 58.37  ? 35   ILE B CG2 1 
ATOM   4443  C  CD1 . ILE B  1 35  ? 12.785  48.791  47.577  1.00 60.28  ? 35   ILE B CD1 1 
ATOM   4444  N  N   . PRO B  1 36  ? 9.876   48.742  52.868  1.00 55.03  ? 36   PRO B N   1 
ATOM   4445  C  CA  . PRO B  1 36  ? 8.574   48.314  53.393  1.00 69.10  ? 36   PRO B CA  1 
ATOM   4446  C  C   . PRO B  1 36  ? 7.467   48.393  52.346  1.00 65.95  ? 36   PRO B C   1 
ATOM   4447  O  O   . PRO B  1 36  ? 7.262   49.466  51.757  1.00 66.05  ? 36   PRO B O   1 
ATOM   4448  C  CB  . PRO B  1 36  ? 8.302   49.328  54.504  1.00 61.62  ? 36   PRO B CB  1 
ATOM   4449  C  CG  . PRO B  1 36  ? 9.169   50.501  54.169  1.00 65.29  ? 36   PRO B CG  1 
ATOM   4450  C  CD  . PRO B  1 36  ? 10.393  49.928  53.556  1.00 56.29  ? 36   PRO B CD  1 
ATOM   4451  N  N   . PHE B  1 37  ? 6.771   47.281  52.105  1.00 56.58  ? 37   PHE B N   1 
ATOM   4452  C  CA  . PHE B  1 37  ? 5.603   47.327  51.229  1.00 54.24  ? 37   PHE B CA  1 
ATOM   4453  C  C   . PHE B  1 37  ? 4.242   47.281  51.924  1.00 50.96  ? 37   PHE B C   1 
ATOM   4454  O  O   . PHE B  1 37  ? 3.208   47.449  51.272  1.00 50.54  ? 37   PHE B O   1 
ATOM   4455  C  CB  . PHE B  1 37  ? 5.697   46.292  50.108  1.00 51.36  ? 37   PHE B CB  1 
ATOM   4456  C  CG  . PHE B  1 37  ? 5.664   44.871  50.578  1.00 52.89  ? 37   PHE B CG  1 
ATOM   4457  C  CD1 . PHE B  1 37  ? 6.833   44.224  50.960  1.00 52.85  ? 37   PHE B CD1 1 
ATOM   4458  C  CD2 . PHE B  1 37  ? 4.470   44.166  50.606  1.00 48.18  ? 37   PHE B CD2 1 
ATOM   4459  C  CE1 . PHE B  1 37  ? 6.812   42.908  51.370  1.00 47.94  ? 37   PHE B CE1 1 
ATOM   4460  C  CE2 . PHE B  1 37  ? 4.441   42.856  51.020  1.00 46.65  ? 37   PHE B CE2 1 
ATOM   4461  C  CZ  . PHE B  1 37  ? 5.617   42.226  51.403  1.00 69.75  ? 37   PHE B CZ  1 
ATOM   4462  N  N   . ALA B  1 38  ? 4.250   47.075  53.241  1.00 59.16  ? 38   ALA B N   1 
ATOM   4463  C  CA  . ALA B  1 38  ? 3.019   47.053  54.039  1.00 56.00  ? 38   ALA B CA  1 
ATOM   4464  C  C   . ALA B  1 38  ? 3.308   47.471  55.469  1.00 57.30  ? 38   ALA B C   1 
ATOM   4465  O  O   . ALA B  1 38  ? 4.418   47.239  55.973  1.00 58.01  ? 38   ALA B O   1 
ATOM   4466  C  CB  . ALA B  1 38  ? 2.388   45.680  54.024  1.00 46.84  ? 38   ALA B CB  1 
ATOM   4467  N  N   . GLU B  1 39  ? 2.320   48.094  56.116  1.00 59.77  ? 39   GLU B N   1 
ATOM   4468  C  CA  . GLU B  1 39  ? 2.445   48.411  57.537  1.00 59.27  ? 39   GLU B CA  1 
ATOM   4469  C  C   . GLU B  1 39  ? 2.455   47.071  58.260  1.00 60.32  ? 39   GLU B C   1 
ATOM   4470  O  O   . GLU B  1 39  ? 1.670   46.185  57.914  1.00 60.65  ? 39   GLU B O   1 
ATOM   4471  C  CB  . GLU B  1 39  ? 1.321   49.340  58.042  1.00 48.42  ? 39   GLU B CB  1 
ATOM   4472  C  CG  . GLU B  1 39  ? 1.474   50.848  57.678  1.00 50.31  ? 39   GLU B CG  1 
ATOM   4473  C  CD  . GLU B  1 39  ? 2.676   51.571  58.351  1.00 83.19  ? 39   GLU B CD  1 
ATOM   4474  O  OE1 . GLU B  1 39  ? 3.316   51.011  59.267  1.00 82.71  ? 39   GLU B OE1 1 
ATOM   4475  O  OE2 . GLU B  1 39  ? 2.985   52.721  57.962  1.00 83.83  ? 39   GLU B OE2 1 
ATOM   4476  N  N   . PRO B  1 40  ? 3.379   46.903  59.224  1.00 61.19  ? 40   PRO B N   1 
ATOM   4477  C  CA  . PRO B  1 40  ? 3.641   45.609  59.851  1.00 60.75  ? 40   PRO B CA  1 
ATOM   4478  C  C   . PRO B  1 40  ? 2.379   45.021  60.422  1.00 63.77  ? 40   PRO B C   1 
ATOM   4479  O  O   . PRO B  1 40  ? 1.698   45.705  61.193  1.00 66.06  ? 40   PRO B O   1 
ATOM   4480  C  CB  . PRO B  1 40  ? 4.591   45.966  60.987  1.00 56.99  ? 40   PRO B CB  1 
ATOM   4481  C  CG  . PRO B  1 40  ? 5.308   47.137  60.496  1.00 60.99  ? 40   PRO B CG  1 
ATOM   4482  C  CD  . PRO B  1 40  ? 4.296   47.935  59.729  1.00 61.94  ? 40   PRO B CD  1 
ATOM   4483  N  N   . PRO B  1 41  ? 2.082   43.762  60.057  1.00 62.70  ? 41   PRO B N   1 
ATOM   4484  C  CA  . PRO B  1 41  ? 0.903   43.027  60.503  1.00 57.73  ? 41   PRO B CA  1 
ATOM   4485  C  C   . PRO B  1 41  ? 1.199   42.444  61.865  1.00 58.02  ? 41   PRO B C   1 
ATOM   4486  O  O   . PRO B  1 41  ? 1.338   41.230  62.003  1.00 60.89  ? 41   PRO B O   1 
ATOM   4487  C  CB  . PRO B  1 41  ? 0.810   41.905  59.487  1.00 40.21  ? 41   PRO B CB  1 
ATOM   4488  C  CG  . PRO B  1 41  ? 2.243   41.608  59.166  1.00 40.78  ? 41   PRO B CG  1 
ATOM   4489  C  CD  . PRO B  1 41  ? 2.955   42.930  59.209  1.00 43.40  ? 41   PRO B CD  1 
ATOM   4490  N  N   . VAL B  1 42  ? 1.323   43.308  62.863  1.00 40.76  ? 42   VAL B N   1 
ATOM   4491  C  CA  . VAL B  1 42  ? 1.545   42.851  64.219  1.00 40.12  ? 42   VAL B CA  1 
ATOM   4492  C  C   . VAL B  1 42  ? 0.311   43.204  65.020  1.00 39.66  ? 42   VAL B C   1 
ATOM   4493  O  O   . VAL B  1 42  ? -0.607  43.834  64.504  1.00 39.93  ? 42   VAL B O   1 
ATOM   4494  C  CB  . VAL B  1 42  ? 2.759   43.534  64.825  1.00 41.21  ? 42   VAL B CB  1 
ATOM   4495  C  CG1 . VAL B  1 42  ? 3.928   43.446  63.864  1.00 41.98  ? 42   VAL B CG1 1 
ATOM   4496  C  CG2 . VAL B  1 42  ? 2.437   44.972  65.123  1.00 42.31  ? 42   VAL B CG2 1 
ATOM   4497  N  N   . GLY B  1 43  ? 0.287   42.797  66.279  1.00 39.03  ? 43   GLY B N   1 
ATOM   4498  C  CA  . GLY B  1 43  ? -0.846  43.095  67.132  1.00 40.80  ? 43   GLY B CA  1 
ATOM   4499  C  C   . GLY B  1 43  ? -2.194  42.671  66.567  1.00 37.76  ? 43   GLY B C   1 
ATOM   4500  O  O   . GLY B  1 43  ? -2.384  41.517  66.176  1.00 36.73  ? 43   GLY B O   1 
ATOM   4501  N  N   . SER B  1 44  ? -3.131  43.616  66.531  1.00 38.24  ? 44   SER B N   1 
ATOM   4502  C  CA  . SER B  1 44  ? -4.467  43.366  66.014  1.00 39.25  ? 44   SER B CA  1 
ATOM   4503  C  C   . SER B  1 44  ? -4.439  43.078  64.512  1.00 38.47  ? 44   SER B C   1 
ATOM   4504  O  O   . SER B  1 44  ? -5.392  42.528  63.952  1.00 36.90  ? 44   SER B O   1 
ATOM   4505  C  CB  . SER B  1 44  ? -5.392  44.547  66.324  1.00 53.92  ? 44   SER B CB  1 
ATOM   4506  O  OG  . SER B  1 44  ? -4.930  45.751  65.731  1.00 57.48  ? 44   SER B OG  1 
ATOM   4507  N  N   . ARG B  1 45  ? -3.330  43.424  63.867  1.00 47.14  ? 45   ARG B N   1 
ATOM   4508  C  CA  . ARG B  1 45  ? -3.194  43.216  62.434  1.00 52.81  ? 45   ARG B CA  1 
ATOM   4509  C  C   . ARG B  1 45  ? -2.644  41.824  62.076  1.00 51.10  ? 45   ARG B C   1 
ATOM   4510  O  O   . ARG B  1 45  ? -2.387  41.532  60.908  1.00 54.29  ? 45   ARG B O   1 
ATOM   4511  C  CB  . ARG B  1 45  ? -2.333  44.324  61.808  1.00 75.12  ? 45   ARG B CB  1 
ATOM   4512  C  CG  . ARG B  1 45  ? -3.071  45.172  60.762  1.00 83.65  ? 45   ARG B CG  1 
ATOM   4513  C  CD  . ARG B  1 45  ? -3.570  44.294  59.609  1.00 88.26  ? 45   ARG B CD  1 
ATOM   4514  N  NE  . ARG B  1 45  ? -4.635  44.901  58.808  1.00 89.78  ? 45   ARG B NE  1 
ATOM   4515  C  CZ  . ARG B  1 45  ? -5.891  45.058  59.218  1.00 89.40  ? 45   ARG B CZ  1 
ATOM   4516  N  NH1 . ARG B  1 45  ? -6.256  44.681  60.439  1.00 87.65  ? 45   ARG B NH1 1 
ATOM   4517  N  NH2 . ARG B  1 45  ? -6.782  45.608  58.407  1.00 90.21  ? 45   ARG B NH2 1 
ATOM   4518  N  N   . ARG B  1 46  ? -2.453  40.970  63.075  1.00 45.42  ? 46   ARG B N   1 
ATOM   4519  C  CA  . ARG B  1 46  ? -1.981  39.611  62.824  1.00 40.67  ? 46   ARG B CA  1 
ATOM   4520  C  C   . ARG B  1 46  ? -3.133  38.770  62.284  1.00 39.10  ? 46   ARG B C   1 
ATOM   4521  O  O   . ARG B  1 46  ? -4.264  38.926  62.745  1.00 41.11  ? 46   ARG B O   1 
ATOM   4522  C  CB  . ARG B  1 46  ? -1.435  38.994  64.111  1.00 35.40  ? 46   ARG B CB  1 
ATOM   4523  C  CG  . ARG B  1 46  ? -1.103  37.520  63.990  1.00 34.39  ? 46   ARG B CG  1 
ATOM   4524  C  CD  . ARG B  1 46  ? -1.052  36.836  65.341  1.00 33.64  ? 46   ARG B CD  1 
ATOM   4525  N  NE  . ARG B  1 46  ? 0.287   36.832  65.912  1.00 34.19  ? 46   ARG B NE  1 
ATOM   4526  C  CZ  . ARG B  1 46  ? 0.540   36.541  67.179  1.00 33.92  ? 46   ARG B CZ  1 
ATOM   4527  N  NH1 . ARG B  1 46  ? -0.460  36.241  67.995  1.00 33.11  ? 46   ARG B NH1 1 
ATOM   4528  N  NH2 . ARG B  1 46  ? 1.786   36.555  67.629  1.00 34.52  ? 46   ARG B NH2 1 
ATOM   4529  N  N   . PHE B  1 47  ? -2.837  37.896  61.315  1.00 37.30  ? 47   PHE B N   1 
ATOM   4530  C  CA  . PHE B  1 47  ? -3.829  37.036  60.639  1.00 35.50  ? 47   PHE B CA  1 
ATOM   4531  C  C   . PHE B  1 47  ? -4.632  37.777  59.576  1.00 37.44  ? 47   PHE B C   1 
ATOM   4532  O  O   . PHE B  1 47  ? -5.513  37.192  58.940  1.00 38.70  ? 47   PHE B O   1 
ATOM   4533  C  CB  . PHE B  1 47  ? -4.790  36.321  61.603  1.00 32.36  ? 47   PHE B CB  1 
ATOM   4534  C  CG  . PHE B  1 47  ? -4.111  35.419  62.588  1.00 31.72  ? 47   PHE B CG  1 
ATOM   4535  C  CD1 . PHE B  1 47  ? -3.247  34.431  62.163  1.00 31.45  ? 47   PHE B CD1 1 
ATOM   4536  C  CD2 . PHE B  1 47  ? -4.346  35.560  63.949  1.00 31.46  ? 47   PHE B CD2 1 
ATOM   4537  C  CE1 . PHE B  1 47  ? -2.632  33.602  63.086  1.00 49.65  ? 47   PHE B CE1 1 
ATOM   4538  C  CE2 . PHE B  1 47  ? -3.733  34.737  64.869  1.00 30.95  ? 47   PHE B CE2 1 
ATOM   4539  C  CZ  . PHE B  1 47  ? -2.875  33.765  64.444  1.00 30.70  ? 47   PHE B CZ  1 
ATOM   4540  N  N   . MET B  1 48  ? -4.343  39.062  59.394  1.00 43.40  ? 48   MET B N   1 
ATOM   4541  C  CA  . MET B  1 48  ? -5.199  39.910  58.577  1.00 43.94  ? 48   MET B CA  1 
ATOM   4542  C  C   . MET B  1 48  ? -4.505  40.266  57.289  1.00 47.95  ? 48   MET B C   1 
ATOM   4543  O  O   . MET B  1 48  ? -3.275  40.296  57.233  1.00 50.73  ? 48   MET B O   1 
ATOM   4544  C  CB  . MET B  1 48  ? -5.548  41.205  59.315  1.00 36.88  ? 48   MET B CB  1 
ATOM   4545  C  CG  . MET B  1 48  ? -6.235  41.003  60.642  1.00 36.04  ? 48   MET B CG  1 
ATOM   4546  S  SD  . MET B  1 48  ? -7.973  41.478  60.669  1.00 53.25  ? 48   MET B SD  1 
ATOM   4547  C  CE  . MET B  1 48  ? -8.553  40.704  59.176  1.00 35.43  ? 48   MET B CE  1 
ATOM   4548  N  N   . PRO B  1 49  ? -5.300  40.523  56.240  1.00 41.00  ? 49   PRO B N   1 
ATOM   4549  C  CA  . PRO B  1 49  ? -4.772  40.935  54.940  1.00 40.88  ? 49   PRO B CA  1 
ATOM   4550  C  C   . PRO B  1 49  ? -3.913  42.158  55.135  1.00 43.19  ? 49   PRO B C   1 
ATOM   4551  O  O   . PRO B  1 49  ? -4.251  43.012  55.956  1.00 45.93  ? 49   PRO B O   1 
ATOM   4552  C  CB  . PRO B  1 49  ? -6.025  41.315  54.165  1.00 41.04  ? 49   PRO B CB  1 
ATOM   4553  C  CG  . PRO B  1 49  ? -7.131  40.536  54.827  1.00 39.06  ? 49   PRO B CG  1 
ATOM   4554  C  CD  . PRO B  1 49  ? -6.773  40.460  56.252  1.00 37.28  ? 49   PRO B CD  1 
ATOM   4555  N  N   . PRO B  1 50  ? -2.798  42.237  54.417  1.00 51.10  ? 50   PRO B N   1 
ATOM   4556  C  CA  . PRO B  1 50  ? -1.886  43.364  54.590  1.00 56.80  ? 50   PRO B CA  1 
ATOM   4557  C  C   . PRO B  1 50  ? -2.505  44.677  54.103  1.00 65.22  ? 50   PRO B C   1 
ATOM   4558  O  O   . PRO B  1 50  ? -3.099  44.675  53.029  1.00 69.95  ? 50   PRO B O   1 
ATOM   4559  C  CB  . PRO B  1 50  ? -0.699  42.972  53.712  1.00 42.75  ? 50   PRO B CB  1 
ATOM   4560  C  CG  . PRO B  1 50  ? -1.275  42.063  52.698  1.00 42.07  ? 50   PRO B CG  1 
ATOM   4561  C  CD  . PRO B  1 50  ? -2.329  41.294  53.397  1.00 40.54  ? 50   PRO B CD  1 
ATOM   4562  N  N   . GLU B  1 51  ? -2.409  45.750  54.894  1.00 56.94  ? 51   GLU B N   1 
ATOM   4563  C  CA  . GLU B  1 51  ? -2.670  47.112  54.415  1.00 58.32  ? 51   GLU B CA  1 
ATOM   4564  C  C   . GLU B  1 51  ? -1.345  47.694  53.921  1.00 56.86  ? 51   GLU B C   1 
ATOM   4565  O  O   . GLU B  1 51  ? -0.279  47.342  54.438  1.00 55.21  ? 51   GLU B O   1 
ATOM   4566  C  CB  . GLU B  1 51  ? -3.226  47.998  55.528  1.00 75.21  ? 51   GLU B CB  1 
ATOM   4567  C  CG  . GLU B  1 51  ? -4.500  47.510  56.178  1.00 80.27  ? 51   GLU B CG  1 
ATOM   4568  C  CD  . GLU B  1 51  ? -4.804  48.268  57.468  1.00 87.17  ? 51   GLU B CD  1 
ATOM   4569  O  OE1 . GLU B  1 51  ? -3.940  48.290  58.377  1.00 87.73  ? 51   GLU B OE1 1 
ATOM   4570  O  OE2 . GLU B  1 51  ? -5.906  48.854  57.572  1.00 90.67  ? 51   GLU B OE2 1 
ATOM   4571  N  N   . PRO B  1 52  ? -1.397  48.591  52.924  1.00 70.78  ? 52   PRO B N   1 
ATOM   4572  C  CA  . PRO B  1 52  ? -0.124  49.028  52.331  1.00 72.88  ? 52   PRO B CA  1 
ATOM   4573  C  C   . PRO B  1 52  ? 0.672   49.915  53.283  1.00 75.89  ? 52   PRO B C   1 
ATOM   4574  O  O   . PRO B  1 52  ? 0.096   50.464  54.226  1.00 76.96  ? 52   PRO B O   1 
ATOM   4575  C  CB  . PRO B  1 52  ? -0.558  49.807  51.080  1.00 54.58  ? 52   PRO B CB  1 
ATOM   4576  C  CG  . PRO B  1 52  ? -2.020  49.430  50.864  1.00 53.48  ? 52   PRO B CG  1 
ATOM   4577  C  CD  . PRO B  1 52  ? -2.561  49.171  52.237  1.00 52.29  ? 52   PRO B CD  1 
ATOM   4578  N  N   . LYS B  1 53  ? 1.979   50.025  53.050  1.00 63.09  ? 53   LYS B N   1 
ATOM   4579  C  CA  . LYS B  1 53  ? 2.840   50.842  53.896  1.00 61.31  ? 53   LYS B CA  1 
ATOM   4580  C  C   . LYS B  1 53  ? 2.310   52.256  53.851  1.00 64.05  ? 53   LYS B C   1 
ATOM   4581  O  O   . LYS B  1 53  ? 1.977   52.753  52.777  1.00 65.02  ? 53   LYS B O   1 
ATOM   4582  C  CB  . LYS B  1 53  ? 4.289   50.804  53.389  1.00 60.54  ? 53   LYS B CB  1 
ATOM   4583  C  CG  . LYS B  1 53  ? 5.264   51.722  54.135  1.00 62.30  ? 53   LYS B CG  1 
ATOM   4584  C  CD  . LYS B  1 53  ? 5.498   51.262  55.569  1.00 63.00  ? 53   LYS B CD  1 
ATOM   4585  C  CE  . LYS B  1 53  ? 6.473   52.173  56.320  1.00 63.85  ? 53   LYS B CE  1 
ATOM   4586  N  NZ  . LYS B  1 53  ? 6.906   51.612  57.644  1.00 61.29  ? 53   LYS B NZ  1 
ATOM   4587  N  N   . ARG B  1 54  ? 2.188   52.896  55.007  1.00 72.39  ? 54   ARG B N   1 
ATOM   4588  C  CA  . ARG B  1 54  ? 1.847   54.310  55.011  1.00 80.11  ? 54   ARG B CA  1 
ATOM   4589  C  C   . ARG B  1 54  ? 3.125   55.083  54.713  1.00 84.25  ? 54   ARG B C   1 
ATOM   4590  O  O   . ARG B  1 54  ? 4.206   54.704  55.182  1.00 84.51  ? 54   ARG B O   1 
ATOM   4591  C  CB  . ARG B  1 54  ? 1.233   54.745  56.338  1.00 90.25  ? 54   ARG B CB  1 
ATOM   4592  C  CG  . ARG B  1 54  ? -0.049  55.539  56.169  1.00 94.17  ? 54   ARG B CG  1 
ATOM   4593  C  CD  . ARG B  1 54  ? -0.284  56.463  57.344  1.00 97.83  ? 54   ARG B CD  1 
ATOM   4594  N  NE  . ARG B  1 54  ? -0.585  55.738  58.574  1.00 97.03  ? 54   ARG B NE  1 
ATOM   4595  C  CZ  . ARG B  1 54  ? -0.601  56.305  59.775  1.00 98.09  ? 54   ARG B CZ  1 
ATOM   4596  N  NH1 . ARG B  1 54  ? -0.325  57.598  59.901  1.00 101.28 ? 54   ARG B NH1 1 
ATOM   4597  N  NH2 . ARG B  1 54  ? -0.881  55.582  60.846  1.00 95.48  ? 54   ARG B NH2 1 
ATOM   4598  N  N   . PRO B  1 55  ? 3.011   56.165  53.922  1.00 86.33  ? 55   PRO B N   1 
ATOM   4599  C  CA  . PRO B  1 55  ? 4.203   56.807  53.355  1.00 84.92  ? 55   PRO B CA  1 
ATOM   4600  C  C   . PRO B  1 55  ? 5.065   57.423  54.440  1.00 81.37  ? 55   PRO B C   1 
ATOM   4601  O  O   . PRO B  1 55  ? 4.585   57.602  55.559  1.00 78.40  ? 55   PRO B O   1 
ATOM   4602  C  CB  . PRO B  1 55  ? 3.612   57.894  52.452  1.00 82.96  ? 55   PRO B CB  1 
ATOM   4603  C  CG  . PRO B  1 55  ? 2.288   58.208  53.064  1.00 82.46  ? 55   PRO B CG  1 
ATOM   4604  C  CD  . PRO B  1 55  ? 1.778   56.908  53.601  1.00 81.71  ? 55   PRO B CD  1 
ATOM   4605  N  N   . TRP B  1 56  ? 6.318   57.731  54.123  1.00 83.44  ? 56   TRP B N   1 
ATOM   4606  C  CA  . TRP B  1 56  ? 7.204   58.339  55.107  1.00 85.06  ? 56   TRP B CA  1 
ATOM   4607  C  C   . TRP B  1 56  ? 7.983   59.538  54.568  1.00 90.05  ? 56   TRP B C   1 
ATOM   4608  O  O   . TRP B  1 56  ? 8.200   59.670  53.360  1.00 91.24  ? 56   TRP B O   1 
ATOM   4609  C  CB  . TRP B  1 56  ? 8.180   57.299  55.655  1.00 76.88  ? 56   TRP B CB  1 
ATOM   4610  C  CG  . TRP B  1 56  ? 9.128   56.784  54.627  1.00 75.68  ? 56   TRP B CG  1 
ATOM   4611  C  CD1 . TRP B  1 56  ? 10.442  57.128  54.475  1.00 77.03  ? 56   TRP B CD1 1 
ATOM   4612  C  CD2 . TRP B  1 56  ? 8.839   55.835  53.596  1.00 73.87  ? 56   TRP B CD2 1 
ATOM   4613  N  NE1 . TRP B  1 56  ? 10.990  56.445  53.414  1.00 76.41  ? 56   TRP B NE1 1 
ATOM   4614  C  CE2 . TRP B  1 56  ? 10.028  55.643  52.857  1.00 74.13  ? 56   TRP B CE2 1 
ATOM   4615  C  CE3 . TRP B  1 56  ? 7.696   55.119  53.231  1.00 71.55  ? 56   TRP B CE3 1 
ATOM   4616  C  CZ2 . TRP B  1 56  ? 10.103  54.776  51.774  1.00 71.79  ? 56   TRP B CZ2 1 
ATOM   4617  C  CZ3 . TRP B  1 56  ? 7.771   54.263  52.156  1.00 71.02  ? 56   TRP B CZ3 1 
ATOM   4618  C  CH2 . TRP B  1 56  ? 8.969   54.097  51.439  1.00 70.85  ? 56   TRP B CH2 1 
ATOM   4619  N  N   . SER B  1 57  ? 8.394   60.413  55.480  1.00 86.01  ? 57   SER B N   1 
ATOM   4620  C  CA  . SER B  1 57  ? 9.372   61.439  55.157  1.00 88.84  ? 57   SER B CA  1 
ATOM   4621  C  C   . SER B  1 57  ? 10.721  60.993  55.709  1.00 86.10  ? 57   SER B C   1 
ATOM   4622  O  O   . SER B  1 57  ? 10.796  60.276  56.709  1.00 83.32  ? 57   SER B O   1 
ATOM   4623  C  CB  . SER B  1 57  ? 8.973   62.817  55.706  1.00 100.96 ? 57   SER B CB  1 
ATOM   4624  O  OG  . SER B  1 57  ? 9.651   63.874  55.020  1.00 103.44 ? 57   SER B OG  1 
ATOM   4625  N  N   . GLY B  1 58  ? 11.786  61.401  55.035  1.00 92.77  ? 58   GLY B N   1 
ATOM   4626  C  CA  . GLY B  1 58  ? 13.124  61.009  55.423  1.00 93.12  ? 58   GLY B CA  1 
ATOM   4627  C  C   . GLY B  1 58  ? 13.717  60.074  54.398  1.00 92.10  ? 58   GLY B C   1 
ATOM   4628  O  O   . GLY B  1 58  ? 12.989  59.501  53.588  1.00 91.40  ? 58   GLY B O   1 
ATOM   4629  N  N   . VAL B  1 59  ? 15.041  59.942  54.419  1.00 85.17  ? 59   VAL B N   1 
ATOM   4630  C  CA  . VAL B  1 59  ? 15.725  59.053  53.495  1.00 84.61  ? 59   VAL B CA  1 
ATOM   4631  C  C   . VAL B  1 59  ? 15.911  57.704  54.167  1.00 81.41  ? 59   VAL B C   1 
ATOM   4632  O  O   . VAL B  1 59  ? 16.765  57.546  55.044  1.00 79.87  ? 59   VAL B O   1 
ATOM   4633  C  CB  . VAL B  1 59  ? 17.096  59.609  53.115  1.00 93.53  ? 59   VAL B CB  1 
ATOM   4634  C  CG1 . VAL B  1 59  ? 17.811  58.652  52.183  1.00 93.44  ? 59   VAL B CG1 1 
ATOM   4635  C  CG2 . VAL B  1 59  ? 16.947  60.988  52.480  1.00 96.72  ? 59   VAL B CG2 1 
ATOM   4636  N  N   . LEU B  1 60  ? 15.133  56.729  53.699  1.00 79.32  ? 60   LEU B N   1 
ATOM   4637  C  CA  . LEU B  1 60  ? 14.985  55.435  54.353  1.00 76.72  ? 60   LEU B CA  1 
ATOM   4638  C  C   . LEU B  1 60  ? 16.154  54.549  54.004  1.00 74.33  ? 60   LEU B C   1 
ATOM   4639  O  O   . LEU B  1 60  ? 16.676  54.628  52.899  1.00 74.41  ? 60   LEU B O   1 
ATOM   4640  C  CB  . LEU B  1 60  ? 13.688  54.768  53.896  1.00 86.31  ? 60   LEU B CB  1 
ATOM   4641  C  CG  . LEU B  1 60  ? 13.253  53.500  54.629  1.00 85.87  ? 60   LEU B CG  1 
ATOM   4642  C  CD1 . LEU B  1 60  ? 13.120  53.773  56.125  1.00 87.90  ? 60   LEU B CD1 1 
ATOM   4643  C  CD2 . LEU B  1 60  ? 11.947  52.994  54.064  1.00 82.08  ? 60   LEU B CD2 1 
ATOM   4644  N  N   . ASP B  1 61  ? 16.549  53.677  54.919  1.00 64.15  ? 61   ASP B N   1 
ATOM   4645  C  CA  . ASP B  1 61  ? 17.733  52.885  54.668  1.00 71.08  ? 61   ASP B CA  1 
ATOM   4646  C  C   . ASP B  1 61  ? 17.357  51.583  53.950  1.00 69.18  ? 61   ASP B C   1 
ATOM   4647  O  O   . ASP B  1 61  ? 16.739  50.682  54.522  1.00 68.26  ? 61   ASP B O   1 
ATOM   4648  C  CB  . ASP B  1 61  ? 18.456  52.599  55.984  1.00 85.00  ? 61   ASP B CB  1 
ATOM   4649  C  CG  . ASP B  1 61  ? 19.827  51.995  55.773  1.00 89.87  ? 61   ASP B CG  1 
ATOM   4650  O  OD1 . ASP B  1 61  ? 19.905  50.805  55.398  1.00 92.34  ? 61   ASP B OD1 1 
ATOM   4651  O  OD2 . ASP B  1 61  ? 20.830  52.706  55.985  1.00 91.77  ? 61   ASP B OD2 1 
ATOM   4652  N  N   . ALA B  1 62  ? 17.731  51.512  52.676  1.00 75.72  ? 62   ALA B N   1 
ATOM   4653  C  CA  . ALA B  1 62  ? 17.560  50.325  51.842  1.00 70.93  ? 62   ALA B CA  1 
ATOM   4654  C  C   . ALA B  1 62  ? 18.844  49.498  51.787  1.00 69.25  ? 62   ALA B C   1 
ATOM   4655  O  O   . ALA B  1 62  ? 18.983  48.601  50.963  1.00 67.50  ? 62   ALA B O   1 
ATOM   4656  C  CB  . ALA B  1 62  ? 17.079  50.699  50.441  1.00 68.09  ? 62   ALA B CB  1 
ATOM   4657  N  N   . THR B  1 63  ? 19.807  49.851  52.625  1.00 63.86  ? 63   THR B N   1 
ATOM   4658  C  CA  . THR B  1 63  ? 21.145  49.295  52.515  1.00 64.86  ? 63   THR B CA  1 
ATOM   4659  C  C   . THR B  1 63  ? 21.341  47.905  53.135  1.00 64.85  ? 63   THR B C   1 
ATOM   4660  O  O   . THR B  1 63  ? 22.429  47.336  53.033  1.00 63.93  ? 63   THR B O   1 
ATOM   4661  C  CB  . THR B  1 63  ? 22.159  50.255  53.142  1.00 71.51  ? 63   THR B CB  1 
ATOM   4662  O  OG1 . THR B  1 63  ? 22.215  50.046  54.562  1.00 69.05  ? 63   THR B OG1 1 
ATOM   4663  C  CG2 . THR B  1 63  ? 21.748  51.690  52.855  1.00 72.52  ? 63   THR B CG2 1 
ATOM   4664  N  N   . THR B  1 64  ? 20.311  47.348  53.768  1.00 84.46  ? 64   THR B N   1 
ATOM   4665  C  CA  . THR B  1 64  ? 20.443  45.993  54.315  1.00 83.04  ? 64   THR B CA  1 
ATOM   4666  C  C   . THR B  1 64  ? 19.148  45.172  54.385  1.00 84.06  ? 64   THR B C   1 
ATOM   4667  O  O   . THR B  1 64  ? 18.042  45.716  54.332  1.00 85.25  ? 64   THR B O   1 
ATOM   4668  C  CB  . THR B  1 64  ? 21.099  46.008  55.706  1.00 59.56  ? 64   THR B CB  1 
ATOM   4669  O  OG1 . THR B  1 64  ? 21.481  44.672  56.067  1.00 58.50  ? 64   THR B OG1 1 
ATOM   4670  C  CG2 . THR B  1 64  ? 20.137  46.590  56.748  1.00 58.78  ? 64   THR B CG2 1 
ATOM   4671  N  N   . PHE B  1 65  ? 19.308  43.855  54.512  1.00 70.48  ? 65   PHE B N   1 
ATOM   4672  C  CA  . PHE B  1 65  ? 18.180  42.927  54.640  1.00 67.93  ? 65   PHE B CA  1 
ATOM   4673  C  C   . PHE B  1 65  ? 17.393  43.093  55.941  1.00 66.99  ? 65   PHE B C   1 
ATOM   4674  O  O   . PHE B  1 65  ? 17.962  43.144  57.039  1.00 63.55  ? 65   PHE B O   1 
ATOM   4675  C  CB  . PHE B  1 65  ? 18.656  41.477  54.541  1.00 55.99  ? 65   PHE B CB  1 
ATOM   4676  C  CG  . PHE B  1 65  ? 18.848  40.990  53.144  1.00 54.32  ? 65   PHE B CG  1 
ATOM   4677  C  CD1 . PHE B  1 65  ? 18.058  41.464  52.114  1.00 54.57  ? 65   PHE B CD1 1 
ATOM   4678  C  CD2 . PHE B  1 65  ? 19.821  40.045  52.861  1.00 54.53  ? 65   PHE B CD2 1 
ATOM   4679  C  CE1 . PHE B  1 65  ? 18.242  41.008  50.819  1.00 55.02  ? 65   PHE B CE1 1 
ATOM   4680  C  CE2 . PHE B  1 65  ? 20.009  39.577  51.564  1.00 54.98  ? 65   PHE B CE2 1 
ATOM   4681  C  CZ  . PHE B  1 65  ? 19.218  40.059  50.544  1.00 55.22  ? 65   PHE B CZ  1 
ATOM   4682  N  N   . GLN B  1 66  ? 16.073  43.135  55.802  1.00 79.22  ? 66   GLN B N   1 
ATOM   4683  C  CA  . GLN B  1 66  ? 15.178  43.254  56.941  1.00 79.44  ? 66   GLN B CA  1 
ATOM   4684  C  C   . GLN B  1 66  ? 14.945  41.914  57.630  1.00 79.08  ? 66   GLN B C   1 
ATOM   4685  O  O   . GLN B  1 66  ? 15.625  40.921  57.359  1.00 79.98  ? 66   GLN B O   1 
ATOM   4686  C  CB  . GLN B  1 66  ? 13.836  43.860  56.515  1.00 62.54  ? 66   GLN B CB  1 
ATOM   4687  C  CG  . GLN B  1 66  ? 13.651  45.303  56.935  1.00 64.19  ? 66   GLN B CG  1 
ATOM   4688  C  CD  . GLN B  1 66  ? 13.815  45.505  58.430  1.00 66.76  ? 66   GLN B CD  1 
ATOM   4689  O  OE1 . GLN B  1 66  ? 14.915  45.773  58.918  1.00 68.11  ? 66   GLN B OE1 1 
ATOM   4690  N  NE2 . GLN B  1 66  ? 12.721  45.378  59.167  1.00 67.53  ? 66   GLN B NE2 1 
ATOM   4691  N  N   . ASN B  1 67  ? 13.969  41.910  58.529  1.00 69.44  ? 67   ASN B N   1 
ATOM   4692  C  CA  . ASN B  1 67  ? 13.619  40.744  59.320  1.00 64.66  ? 67   ASN B CA  1 
ATOM   4693  C  C   . ASN B  1 67  ? 13.093  39.578  58.519  1.00 63.55  ? 67   ASN B C   1 
ATOM   4694  O  O   . ASN B  1 67  ? 12.554  39.744  57.424  1.00 64.67  ? 67   ASN B O   1 
ATOM   4695  C  CB  . ASN B  1 67  ? 12.540  41.123  60.315  1.00 57.15  ? 67   ASN B CB  1 
ATOM   4696  C  CG  . ASN B  1 67  ? 13.060  41.976  61.420  1.00 56.83  ? 67   ASN B CG  1 
ATOM   4697  O  OD1 . ASN B  1 67  ? 14.071  41.642  62.045  1.00 55.45  ? 67   ASN B OD1 1 
ATOM   4698  N  ND2 . ASN B  1 67  ? 12.380  43.099  61.676  1.00 57.85  ? 67   ASN B ND2 1 
ATOM   4699  N  N   . VAL B  1 68  ? 13.232  38.393  59.098  1.00 52.44  ? 68   VAL B N   1 
ATOM   4700  C  CA  . VAL B  1 68  ? 12.622  37.194  58.551  1.00 50.38  ? 68   VAL B CA  1 
ATOM   4701  C  C   . VAL B  1 68  ? 11.272  36.935  59.234  1.00 47.33  ? 68   VAL B C   1 
ATOM   4702  O  O   . VAL B  1 68  ? 11.120  37.158  60.431  1.00 42.22  ? 68   VAL B O   1 
ATOM   4703  C  CB  . VAL B  1 68  ? 13.572  35.990  58.694  1.00 43.72  ? 68   VAL B CB  1 
ATOM   4704  C  CG1 . VAL B  1 68  ? 12.817  34.697  58.586  1.00 43.10  ? 68   VAL B CG1 1 
ATOM   4705  C  CG2 . VAL B  1 68  ? 14.663  36.053  57.643  1.00 44.98  ? 68   VAL B CG2 1 
ATOM   4706  N  N   . CYS B  1 69  ? 10.286  36.501  58.455  1.00 50.73  ? 69   CYS B N   1 
ATOM   4707  C  CA  . CYS B  1 69  ? 8.977   36.153  58.982  1.00 49.29  ? 69   CYS B CA  1 
ATOM   4708  C  C   . CYS B  1 69  ? 9.046   35.041  60.007  1.00 48.91  ? 69   CYS B C   1 
ATOM   4709  O  O   . CYS B  1 69  ? 9.793   34.077  59.831  1.00 51.60  ? 69   CYS B O   1 
ATOM   4710  C  CB  . CYS B  1 69  ? 8.070   35.722  57.846  1.00 48.74  ? 69   CYS B CB  1 
ATOM   4711  S  SG  . CYS B  1 69  ? 7.588   37.089  56.839  1.00 70.22  ? 69   CYS B SG  1 
ATOM   4712  N  N   . TYR B  1 70  ? 8.248   35.168  61.063  1.00 38.60  ? 70   TYR B N   1 
ATOM   4713  C  CA  . TYR B  1 70  ? 8.346   34.252  62.179  1.00 37.75  ? 70   TYR B CA  1 
ATOM   4714  C  C   . TYR B  1 70  ? 8.105   32.814  61.732  1.00 36.72  ? 70   TYR B C   1 
ATOM   4715  O  O   . TYR B  1 70  ? 7.104   32.511  61.091  1.00 37.24  ? 70   TYR B O   1 
ATOM   4716  C  CB  . TYR B  1 70  ? 7.407   34.666  63.312  1.00 38.96  ? 70   TYR B CB  1 
ATOM   4717  C  CG  . TYR B  1 70  ? 8.041   34.416  64.642  1.00 39.57  ? 70   TYR B CG  1 
ATOM   4718  C  CD1 . TYR B  1 70  ? 8.164   33.129  65.121  1.00 43.41  ? 70   TYR B CD1 1 
ATOM   4719  C  CD2 . TYR B  1 70  ? 8.572   35.450  65.390  1.00 40.37  ? 70   TYR B CD2 1 
ATOM   4720  C  CE1 . TYR B  1 70  ? 8.775   32.865  66.317  1.00 48.19  ? 70   TYR B CE1 1 
ATOM   4721  C  CE2 . TYR B  1 70  ? 9.189   35.204  66.596  1.00 46.05  ? 70   TYR B CE2 1 
ATOM   4722  C  CZ  . TYR B  1 70  ? 9.287   33.899  67.059  1.00 51.70  ? 70   TYR B CZ  1 
ATOM   4723  O  OH  . TYR B  1 70  ? 9.891   33.604  68.270  1.00 56.85  ? 70   TYR B OH  1 
ATOM   4724  N  N   . GLN B  1 71  ? 9.044   31.928  62.045  1.00 36.71  ? 71   GLN B N   1 
ATOM   4725  C  CA  . GLN B  1 71  ? 8.979   30.572  61.519  1.00 35.94  ? 71   GLN B CA  1 
ATOM   4726  C  C   . GLN B  1 71  ? 9.771   29.539  62.319  1.00 43.73  ? 71   GLN B C   1 
ATOM   4727  O  O   . GLN B  1 71  ? 10.663  29.868  63.111  1.00 36.41  ? 71   GLN B O   1 
ATOM   4728  C  CB  . GLN B  1 71  ? 9.480   30.568  60.086  1.00 38.18  ? 71   GLN B CB  1 
ATOM   4729  C  CG  . GLN B  1 71  ? 10.950  30.917  59.998  1.00 38.59  ? 71   GLN B CG  1 
ATOM   4730  C  CD  . GLN B  1 71  ? 11.428  31.102  58.584  1.00 38.79  ? 71   GLN B CD  1 
ATOM   4731  O  OE1 . GLN B  1 71  ? 12.101  30.236  58.028  1.00 38.93  ? 71   GLN B OE1 1 
ATOM   4732  N  NE2 . GLN B  1 71  ? 11.087  32.236  57.993  1.00 39.45  ? 71   GLN B NE2 1 
ATOM   4733  N  N   . TYR B  1 72  ? 9.429   28.276  62.091  1.00 45.91  ? 72   TYR B N   1 
ATOM   4734  C  CA  . TYR B  1 72  ? 10.171  27.160  62.649  1.00 46.28  ? 72   TYR B CA  1 
ATOM   4735  C  C   . TYR B  1 72  ? 11.602  27.174  62.121  1.00 49.36  ? 72   TYR B C   1 
ATOM   4736  O  O   . TYR B  1 72  ? 11.826  27.256  60.910  1.00 51.97  ? 72   TYR B O   1 
ATOM   4737  C  CB  . TYR B  1 72  ? 9.481   25.845  62.277  1.00 54.48  ? 72   TYR B CB  1 
ATOM   4738  C  CG  . TYR B  1 72  ? 10.282  24.609  62.609  1.00 57.83  ? 72   TYR B CG  1 
ATOM   4739  C  CD1 . TYR B  1 72  ? 10.307  24.094  63.905  1.00 58.21  ? 72   TYR B CD1 1 
ATOM   4740  C  CD2 . TYR B  1 72  ? 11.007  23.947  61.623  1.00 61.62  ? 72   TYR B CD2 1 
ATOM   4741  C  CE1 . TYR B  1 72  ? 11.039  22.960  64.215  1.00 60.07  ? 72   TYR B CE1 1 
ATOM   4742  C  CE2 . TYR B  1 72  ? 11.747  22.812  61.919  1.00 64.48  ? 72   TYR B CE2 1 
ATOM   4743  C  CZ  . TYR B  1 72  ? 11.762  22.323  63.218  1.00 64.15  ? 72   TYR B CZ  1 
ATOM   4744  O  OH  . TYR B  1 72  ? 12.502  21.194  63.505  1.00 65.68  ? 72   TYR B OH  1 
ATOM   4745  N  N   . VAL B  1 73  ? 12.574  27.113  63.025  1.00 55.85  ? 73   VAL B N   1 
ATOM   4746  C  CA  . VAL B  1 73  ? 13.974  26.997  62.621  1.00 57.88  ? 73   VAL B CA  1 
ATOM   4747  C  C   . VAL B  1 73  ? 14.403  25.529  62.621  1.00 59.13  ? 73   VAL B C   1 
ATOM   4748  O  O   . VAL B  1 73  ? 14.264  24.843  63.638  1.00 59.97  ? 73   VAL B O   1 
ATOM   4749  C  CB  . VAL B  1 73  ? 14.891  27.810  63.554  1.00 54.08  ? 73   VAL B CB  1 
ATOM   4750  C  CG1 . VAL B  1 73  ? 16.345  27.388  63.392  1.00 54.77  ? 73   VAL B CG1 1 
ATOM   4751  C  CG2 . VAL B  1 73  ? 14.720  29.300  63.299  1.00 53.01  ? 73   VAL B CG2 1 
ATOM   4752  N  N   . ASP B  1 74  ? 14.925  25.041  61.497  1.00 51.55  ? 74   ASP B N   1 
ATOM   4753  C  CA  . ASP B  1 74  ? 15.181  23.608  61.379  1.00 53.56  ? 74   ASP B CA  1 
ATOM   4754  C  C   . ASP B  1 74  ? 16.323  23.153  62.272  1.00 54.72  ? 74   ASP B C   1 
ATOM   4755  O  O   . ASP B  1 74  ? 17.466  23.587  62.117  1.00 54.84  ? 74   ASP B O   1 
ATOM   4756  C  CB  . ASP B  1 74  ? 15.487  23.213  59.937  1.00 66.99  ? 74   ASP B CB  1 
ATOM   4757  C  CG  . ASP B  1 74  ? 15.865  21.754  59.817  1.00 69.35  ? 74   ASP B CG  1 
ATOM   4758  O  OD1 . ASP B  1 74  ? 14.945  20.931  59.652  1.00 68.46  ? 74   ASP B OD1 1 
ATOM   4759  O  OD2 . ASP B  1 74  ? 17.070  21.426  59.914  1.00 71.45  ? 74   ASP B OD2 1 
ATOM   4760  N  N   . THR B  1 75  ? 15.996  22.244  63.182  1.00 59.42  ? 75   THR B N   1 
ATOM   4761  C  CA  . THR B  1 75  ? 16.928  21.767  64.198  1.00 63.19  ? 75   THR B CA  1 
ATOM   4762  C  C   . THR B  1 75  ? 17.565  20.407  63.879  1.00 63.74  ? 75   THR B C   1 
ATOM   4763  O  O   . THR B  1 75  ? 18.351  19.881  64.676  1.00 62.93  ? 75   THR B O   1 
ATOM   4764  C  CB  . THR B  1 75  ? 16.226  21.698  65.565  1.00 69.91  ? 75   THR B CB  1 
ATOM   4765  O  OG1 . THR B  1 75  ? 15.087  20.835  65.468  1.00 70.66  ? 75   THR B OG1 1 
ATOM   4766  C  CG2 . THR B  1 75  ? 15.753  23.086  65.990  1.00 69.48  ? 75   THR B CG2 1 
ATOM   4767  N  N   . LEU B  1 76  ? 17.217  19.849  62.718  1.00 70.87  ? 76   LEU B N   1 
ATOM   4768  C  CA  . LEU B  1 76  ? 17.489  18.442  62.396  1.00 70.10  ? 76   LEU B CA  1 
ATOM   4769  C  C   . LEU B  1 76  ? 18.963  18.067  62.359  1.00 73.43  ? 76   LEU B C   1 
ATOM   4770  O  O   . LEU B  1 76  ? 19.397  17.141  63.044  1.00 72.56  ? 76   LEU B O   1 
ATOM   4771  C  CB  . LEU B  1 76  ? 16.847  18.064  61.054  1.00 58.23  ? 76   LEU B CB  1 
ATOM   4772  C  CG  . LEU B  1 76  ? 17.042  16.605  60.619  1.00 52.87  ? 76   LEU B CG  1 
ATOM   4773  C  CD1 . LEU B  1 76  ? 16.521  15.664  61.699  1.00 49.89  ? 76   LEU B CD1 1 
ATOM   4774  C  CD2 . LEU B  1 76  ? 16.406  16.300  59.252  1.00 49.09  ? 76   LEU B CD2 1 
ATOM   4775  N  N   . TYR B  1 77  ? 19.719  18.774  61.531  1.00 83.23  ? 77   TYR B N   1 
ATOM   4776  C  CA  . TYR B  1 77  ? 21.134  18.492  61.365  1.00 85.85  ? 77   TYR B CA  1 
ATOM   4777  C  C   . TYR B  1 77  ? 21.963  19.738  61.695  1.00 86.35  ? 77   TYR B C   1 
ATOM   4778  O  O   . TYR B  1 77  ? 22.317  20.491  60.787  1.00 90.72  ? 77   TYR B O   1 
ATOM   4779  C  CB  . TYR B  1 77  ? 21.410  18.047  59.923  1.00 79.00  ? 77   TYR B CB  1 
ATOM   4780  C  CG  . TYR B  1 77  ? 21.002  16.619  59.587  1.00 79.48  ? 77   TYR B CG  1 
ATOM   4781  C  CD1 . TYR B  1 77  ? 21.192  15.580  60.494  1.00 79.59  ? 77   TYR B CD1 1 
ATOM   4782  C  CD2 . TYR B  1 77  ? 20.439  16.308  58.349  1.00 79.53  ? 77   TYR B CD2 1 
ATOM   4783  C  CE1 . TYR B  1 77  ? 20.827  14.269  60.176  1.00 78.92  ? 77   TYR B CE1 1 
ATOM   4784  C  CE2 . TYR B  1 77  ? 20.068  15.002  58.025  1.00 78.29  ? 77   TYR B CE2 1 
ATOM   4785  C  CZ  . TYR B  1 77  ? 20.265  13.989  58.942  1.00 76.97  ? 77   TYR B CZ  1 
ATOM   4786  O  OH  . TYR B  1 77  ? 19.900  12.699  58.628  1.00 73.47  ? 77   TYR B OH  1 
ATOM   4787  N  N   . PRO B  1 78  ? 22.275  19.957  62.996  1.00 65.43  ? 78   PRO B N   1 
ATOM   4788  C  CA  . PRO B  1 78  ? 22.994  21.148  63.469  1.00 60.57  ? 78   PRO B CA  1 
ATOM   4789  C  C   . PRO B  1 78  ? 24.270  21.374  62.689  1.00 62.27  ? 78   PRO B C   1 
ATOM   4790  O  O   . PRO B  1 78  ? 25.004  20.414  62.465  1.00 62.39  ? 78   PRO B O   1 
ATOM   4791  C  CB  . PRO B  1 78  ? 23.351  20.785  64.907  1.00 48.04  ? 78   PRO B CB  1 
ATOM   4792  C  CG  . PRO B  1 78  ? 22.274  19.856  65.330  1.00 47.36  ? 78   PRO B CG  1 
ATOM   4793  C  CD  . PRO B  1 78  ? 21.945  19.047  64.110  1.00 50.93  ? 78   PRO B CD  1 
ATOM   4794  N  N   . GLY B  1 79  ? 24.502  22.615  62.263  1.00 69.22  ? 79   GLY B N   1 
ATOM   4795  C  CA  . GLY B  1 79  ? 25.722  23.002  61.571  1.00 72.08  ? 79   GLY B CA  1 
ATOM   4796  C  C   . GLY B  1 79  ? 26.011  22.313  60.244  1.00 74.30  ? 79   GLY B C   1 
ATOM   4797  O  O   . GLY B  1 79  ? 27.128  22.410  59.735  1.00 77.66  ? 79   GLY B O   1 
ATOM   4798  N  N   . PHE B  1 80  ? 25.019  21.620  59.685  1.00 66.84  ? 80   PHE B N   1 
ATOM   4799  C  CA  . PHE B  1 80  ? 25.154  20.981  58.372  1.00 67.11  ? 80   PHE B CA  1 
ATOM   4800  C  C   . PHE B  1 80  ? 24.692  21.922  57.252  1.00 67.13  ? 80   PHE B C   1 
ATOM   4801  O  O   . PHE B  1 80  ? 23.515  22.274  57.181  1.00 65.21  ? 80   PHE B O   1 
ATOM   4802  C  CB  . PHE B  1 80  ? 24.367  19.665  58.324  1.00 70.68  ? 80   PHE B CB  1 
ATOM   4803  C  CG  . PHE B  1 80  ? 24.386  19.004  56.978  1.00 73.65  ? 80   PHE B CG  1 
ATOM   4804  C  CD1 . PHE B  1 80  ? 25.477  18.257  56.577  1.00 76.73  ? 80   PHE B CD1 1 
ATOM   4805  C  CD2 . PHE B  1 80  ? 23.324  19.141  56.108  1.00 74.56  ? 80   PHE B CD2 1 
ATOM   4806  C  CE1 . PHE B  1 80  ? 25.506  17.655  55.340  1.00 78.04  ? 80   PHE B CE1 1 
ATOM   4807  C  CE2 . PHE B  1 80  ? 23.351  18.544  54.870  1.00 75.82  ? 80   PHE B CE2 1 
ATOM   4808  C  CZ  . PHE B  1 80  ? 24.445  17.803  54.485  1.00 77.52  ? 80   PHE B CZ  1 
ATOM   4809  N  N   . GLU B  1 81  ? 25.614  22.308  56.371  1.00 67.92  ? 81   GLU B N   1 
ATOM   4810  C  CA  . GLU B  1 81  ? 25.359  23.362  55.383  1.00 71.77  ? 81   GLU B CA  1 
ATOM   4811  C  C   . GLU B  1 81  ? 24.053  23.166  54.602  1.00 66.66  ? 81   GLU B C   1 
ATOM   4812  O  O   . GLU B  1 81  ? 23.359  24.135  54.283  1.00 61.61  ? 81   GLU B O   1 
ATOM   4813  C  CB  . GLU B  1 81  ? 26.550  23.505  54.417  1.00 102.91 ? 81   GLU B CB  1 
ATOM   4814  C  CG  . GLU B  1 81  ? 26.335  24.535  53.294  1.00 109.45 ? 81   GLU B CG  1 
ATOM   4815  C  CD  . GLU B  1 81  ? 27.463  24.563  52.266  1.00 113.94 ? 81   GLU B CD  1 
ATOM   4816  O  OE1 . GLU B  1 81  ? 28.616  24.268  52.644  1.00 116.82 ? 81   GLU B OE1 1 
ATOM   4817  O  OE2 . GLU B  1 81  ? 27.195  24.880  51.082  1.00 113.20 ? 81   GLU B OE2 1 
ATOM   4818  N  N   . GLY B  1 82  ? 23.713  21.908  54.337  1.00 83.38  ? 82   GLY B N   1 
ATOM   4819  C  CA  . GLY B  1 82  ? 22.556  21.569  53.524  1.00 85.91  ? 82   GLY B CA  1 
ATOM   4820  C  C   . GLY B  1 82  ? 21.195  21.946  54.085  1.00 84.76  ? 82   GLY B C   1 
ATOM   4821  O  O   . GLY B  1 82  ? 20.369  22.512  53.369  1.00 85.45  ? 82   GLY B O   1 
ATOM   4822  N  N   . THR B  1 83  ? 20.944  21.600  55.346  1.00 86.91  ? 83   THR B N   1 
ATOM   4823  C  CA  . THR B  1 83  ? 19.701  21.981  56.016  1.00 79.11  ? 83   THR B CA  1 
ATOM   4824  C  C   . THR B  1 83  ? 19.812  23.409  56.507  1.00 80.21  ? 83   THR B C   1 
ATOM   4825  O  O   . THR B  1 83  ? 18.851  24.177  56.453  1.00 82.20  ? 83   THR B O   1 
ATOM   4826  C  CB  . THR B  1 83  ? 19.405  21.098  57.237  1.00 48.75  ? 83   THR B CB  1 
ATOM   4827  O  OG1 . THR B  1 83  ? 20.119  21.594  58.376  1.00 43.31  ? 83   THR B OG1 1 
ATOM   4828  C  CG2 . THR B  1 83  ? 19.815  19.665  56.970  1.00 49.07  ? 83   THR B CG2 1 
ATOM   4829  N  N   . GLU B  1 84  ? 20.999  23.747  57.000  1.00 55.48  ? 84   GLU B N   1 
ATOM   4830  C  CA  . GLU B  1 84  ? 21.246  25.050  57.590  1.00 52.43  ? 84   GLU B CA  1 
ATOM   4831  C  C   . GLU B  1 84  ? 20.965  26.158  56.578  1.00 46.61  ? 84   GLU B C   1 
ATOM   4832  O  O   . GLU B  1 84  ? 20.413  27.198  56.929  1.00 44.80  ? 84   GLU B O   1 
ATOM   4833  C  CB  . GLU B  1 84  ? 22.685  25.136  58.111  1.00 72.68  ? 84   GLU B CB  1 
ATOM   4834  C  CG  . GLU B  1 84  ? 22.860  25.941  59.401  1.00 78.76  ? 84   GLU B CG  1 
ATOM   4835  C  CD  . GLU B  1 84  ? 22.344  25.219  60.642  1.00 81.87  ? 84   GLU B CD  1 
ATOM   4836  O  OE1 . GLU B  1 84  ? 22.396  23.973  60.685  1.00 80.83  ? 84   GLU B OE1 1 
ATOM   4837  O  OE2 . GLU B  1 84  ? 21.883  25.902  61.582  1.00 84.56  ? 84   GLU B OE2 1 
ATOM   4838  N  N   . MET B  1 85  ? 21.307  25.922  55.315  1.00 56.09  ? 85   MET B N   1 
ATOM   4839  C  CA  . MET B  1 85  ? 21.199  26.974  54.306  1.00 56.92  ? 85   MET B CA  1 
ATOM   4840  C  C   . MET B  1 85  ? 19.790  27.536  54.116  1.00 58.09  ? 85   MET B C   1 
ATOM   4841  O  O   . MET B  1 85  ? 19.645  28.654  53.626  1.00 57.91  ? 85   MET B O   1 
ATOM   4842  C  CB  . MET B  1 85  ? 21.772  26.519  52.961  1.00 51.80  ? 85   MET B CB  1 
ATOM   4843  C  CG  . MET B  1 85  ? 21.014  25.389  52.303  1.00 49.93  ? 85   MET B CG  1 
ATOM   4844  S  SD  . MET B  1 85  ? 21.896  24.696  50.892  1.00 59.92  ? 85   MET B SD  1 
ATOM   4845  C  CE  . MET B  1 85  ? 21.446  25.848  49.597  1.00 48.72  ? 85   MET B CE  1 
ATOM   4846  N  N   . TRP B  1 86  ? 18.762  26.770  54.487  1.00 61.56  ? 86   TRP B N   1 
ATOM   4847  C  CA  . TRP B  1 86  ? 17.375  27.217  54.304  1.00 60.95  ? 86   TRP B CA  1 
ATOM   4848  C  C   . TRP B  1 86  ? 16.797  27.910  55.525  1.00 63.00  ? 86   TRP B C   1 
ATOM   4849  O  O   . TRP B  1 86  ? 15.710  28.478  55.453  1.00 64.05  ? 86   TRP B O   1 
ATOM   4850  C  CB  . TRP B  1 86  ? 16.474  26.058  53.887  1.00 52.07  ? 86   TRP B CB  1 
ATOM   4851  C  CG  . TRP B  1 86  ? 17.081  25.247  52.795  1.00 52.87  ? 86   TRP B CG  1 
ATOM   4852  C  CD1 . TRP B  1 86  ? 17.722  24.050  52.920  1.00 54.26  ? 86   TRP B CD1 1 
ATOM   4853  C  CD2 . TRP B  1 86  ? 17.137  25.587  51.409  1.00 52.87  ? 86   TRP B CD2 1 
ATOM   4854  N  NE1 . TRP B  1 86  ? 18.164  23.615  51.693  1.00 54.81  ? 86   TRP B NE1 1 
ATOM   4855  C  CE2 . TRP B  1 86  ? 17.819  24.545  50.750  1.00 53.83  ? 86   TRP B CE2 1 
ATOM   4856  C  CE3 . TRP B  1 86  ? 16.678  26.670  50.662  1.00 53.82  ? 86   TRP B CE3 1 
ATOM   4857  C  CZ2 . TRP B  1 86  ? 18.049  24.556  49.385  1.00 55.12  ? 86   TRP B CZ2 1 
ATOM   4858  C  CZ3 . TRP B  1 86  ? 16.907  26.678  49.305  1.00 55.85  ? 86   TRP B CZ3 1 
ATOM   4859  C  CH2 . TRP B  1 86  ? 17.586  25.627  48.679  1.00 56.27  ? 86   TRP B CH2 1 
ATOM   4860  N  N   . ASN B  1 87  ? 17.529  27.858  56.637  1.00 61.11  ? 87   ASN B N   1 
ATOM   4861  C  CA  . ASN B  1 87  ? 17.134  28.531  57.875  1.00 59.18  ? 87   ASN B CA  1 
ATOM   4862  C  C   . ASN B  1 87  ? 17.205  30.039  57.697  1.00 57.45  ? 87   ASN B C   1 
ATOM   4863  O  O   . ASN B  1 87  ? 17.828  30.513  56.752  1.00 59.24  ? 87   ASN B O   1 
ATOM   4864  C  CB  . ASN B  1 87  ? 18.039  28.097  59.033  1.00 62.23  ? 87   ASN B CB  1 
ATOM   4865  C  CG  . ASN B  1 87  ? 17.683  26.723  59.570  1.00 64.01  ? 87   ASN B CG  1 
ATOM   4866  O  OD1 . ASN B  1 87  ? 16.531  26.295  59.500  1.00 65.39  ? 87   ASN B OD1 1 
ATOM   4867  N  ND2 . ASN B  1 87  ? 18.672  26.026  60.116  1.00 64.19  ? 87   ASN B ND2 1 
ATOM   4868  N  N   . PRO B  1 88  ? 16.557  30.804  58.590  1.00 56.25  ? 88   PRO B N   1 
ATOM   4869  C  CA  . PRO B  1 88  ? 16.661  32.264  58.487  1.00 56.87  ? 88   PRO B CA  1 
ATOM   4870  C  C   . PRO B  1 88  ? 18.076  32.776  58.773  1.00 57.97  ? 88   PRO B C   1 
ATOM   4871  O  O   . PRO B  1 88  ? 18.715  32.304  59.715  1.00 57.11  ? 88   PRO B O   1 
ATOM   4872  C  CB  . PRO B  1 88  ? 15.675  32.761  59.550  1.00 42.93  ? 88   PRO B CB  1 
ATOM   4873  C  CG  . PRO B  1 88  ? 15.516  31.628  60.480  1.00 41.84  ? 88   PRO B CG  1 
ATOM   4874  C  CD  . PRO B  1 88  ? 15.611  30.403  59.639  1.00 41.40  ? 88   PRO B CD  1 
ATOM   4875  N  N   . ASN B  1 89  ? 18.559  33.692  57.932  1.00 50.29  ? 89   ASN B N   1 
ATOM   4876  C  CA  . ASN B  1 89  ? 19.862  34.337  58.112  1.00 52.47  ? 89   ASN B CA  1 
ATOM   4877  C  C   . ASN B  1 89  ? 19.770  35.723  58.756  1.00 54.67  ? 89   ASN B C   1 
ATOM   4878  O  O   . ASN B  1 89  ? 20.778  36.378  59.026  1.00 54.01  ? 89   ASN B O   1 
ATOM   4879  C  CB  . ASN B  1 89  ? 20.613  34.418  56.780  1.00 49.31  ? 89   ASN B CB  1 
ATOM   4880  C  CG  . ASN B  1 89  ? 19.870  35.234  55.729  1.00 49.59  ? 89   ASN B CG  1 
ATOM   4881  O  OD1 . ASN B  1 89  ? 18.997  36.052  56.041  1.00 49.26  ? 89   ASN B OD1 1 
ATOM   4882  N  ND2 . ASN B  1 89  ? 20.223  35.011  54.465  1.00 50.29  ? 89   ASN B ND2 1 
ATOM   4883  N  N   . ARG B  1 90  ? 18.546  36.174  58.974  1.00 64.01  ? 90   ARG B N   1 
ATOM   4884  C  CA  . ARG B  1 90  ? 18.311  37.387  59.730  1.00 66.54  ? 90   ARG B CA  1 
ATOM   4885  C  C   . ARG B  1 90  ? 17.519  37.013  60.961  1.00 71.14  ? 90   ARG B C   1 
ATOM   4886  O  O   . ARG B  1 90  ? 17.292  35.838  61.238  1.00 70.87  ? 90   ARG B O   1 
ATOM   4887  C  CB  . ARG B  1 90  ? 17.547  38.426  58.912  1.00 58.78  ? 90   ARG B CB  1 
ATOM   4888  C  CG  . ARG B  1 90  ? 18.385  39.138  57.871  1.00 60.32  ? 90   ARG B CG  1 
ATOM   4889  C  CD  . ARG B  1 90  ? 19.389  40.109  58.484  1.00 61.78  ? 90   ARG B CD  1 
ATOM   4890  N  NE  . ARG B  1 90  ? 20.056  40.886  57.443  1.00 62.99  ? 90   ARG B NE  1 
ATOM   4891  C  CZ  . ARG B  1 90  ? 21.068  40.432  56.707  1.00 63.59  ? 90   ARG B CZ  1 
ATOM   4892  N  NH1 . ARG B  1 90  ? 21.543  39.206  56.908  1.00 61.10  ? 90   ARG B NH1 1 
ATOM   4893  N  NH2 . ARG B  1 90  ? 21.607  41.202  55.770  1.00 65.57  ? 90   ARG B NH2 1 
ATOM   4894  N  N   . GLU B  1 91  ? 17.116  38.023  61.711  1.00 85.30  ? 91   GLU B N   1 
ATOM   4895  C  CA  . GLU B  1 91  ? 16.391  37.794  62.938  1.00 84.26  ? 91   GLU B CA  1 
ATOM   4896  C  C   . GLU B  1 91  ? 14.908  37.605  62.654  1.00 77.59  ? 91   GLU B C   1 
ATOM   4897  O  O   . GLU B  1 91  ? 14.364  38.221  61.735  1.00 79.73  ? 91   GLU B O   1 
ATOM   4898  C  CB  . GLU B  1 91  ? 16.604  38.976  63.860  1.00 86.13  ? 91   GLU B CB  1 
ATOM   4899  C  CG  . GLU B  1 91  ? 16.549  38.619  65.304  1.00 88.98  ? 91   GLU B CG  1 
ATOM   4900  C  CD  . GLU B  1 91  ? 16.429  39.844  66.156  1.00 93.63  ? 91   GLU B CD  1 
ATOM   4901  O  OE1 . GLU B  1 91  ? 16.397  40.964  65.587  1.00 93.74  ? 91   GLU B OE1 1 
ATOM   4902  O  OE2 . GLU B  1 91  ? 16.359  39.683  67.392  1.00 96.42  ? 91   GLU B OE2 1 
ATOM   4903  N  N   . LEU B  1 92  ? 14.261  36.752  63.446  1.00 47.19  ? 92   LEU B N   1 
ATOM   4904  C  CA  . LEU B  1 92  ? 12.824  36.508  63.317  1.00 42.25  ? 92   LEU B CA  1 
ATOM   4905  C  C   . LEU B  1 92  ? 11.971  37.619  63.921  1.00 42.30  ? 92   LEU B C   1 
ATOM   4906  O  O   . LEU B  1 92  ? 12.118  37.959  65.090  1.00 42.64  ? 92   LEU B O   1 
ATOM   4907  C  CB  . LEU B  1 92  ? 12.430  35.211  64.023  1.00 40.90  ? 92   LEU B CB  1 
ATOM   4908  C  CG  . LEU B  1 92  ? 13.001  33.860  63.640  1.00 40.51  ? 92   LEU B CG  1 
ATOM   4909  C  CD1 . LEU B  1 92  ? 12.090  32.807  64.216  1.00 39.04  ? 92   LEU B CD1 1 
ATOM   4910  C  CD2 . LEU B  1 92  ? 13.084  33.743  62.151  1.00 40.82  ? 92   LEU B CD2 1 
ATOM   4911  N  N   . SER B  1 93  ? 11.049  38.157  63.145  1.00 42.21  ? 93   SER B N   1 
ATOM   4912  C  CA  . SER B  1 93  ? 10.079  39.065  63.716  1.00 42.10  ? 93   SER B CA  1 
ATOM   4913  C  C   . SER B  1 93  ? 8.777   39.010  62.947  1.00 41.37  ? 93   SER B C   1 
ATOM   4914  O  O   . SER B  1 93  ? 8.755   38.648  61.775  1.00 41.36  ? 93   SER B O   1 
ATOM   4915  C  CB  . SER B  1 93  ? 10.616  40.487  63.741  1.00 43.59  ? 93   SER B CB  1 
ATOM   4916  O  OG  . SER B  1 93  ? 9.649   41.394  63.243  1.00 43.81  ? 93   SER B OG  1 
ATOM   4917  N  N   . GLU B  1 94  ? 7.686   39.365  63.614  1.00 40.78  ? 94   GLU B N   1 
ATOM   4918  C  CA  . GLU B  1 94  ? 6.389   39.373  62.974  1.00 40.13  ? 94   GLU B CA  1 
ATOM   4919  C  C   . GLU B  1 94  ? 6.299   40.581  62.068  1.00 41.30  ? 94   GLU B C   1 
ATOM   4920  O  O   . GLU B  1 94  ? 5.401   40.654  61.235  1.00 58.61  ? 94   GLU B O   1 
ATOM   4921  C  CB  . GLU B  1 94  ? 5.267   39.395  64.006  1.00 52.67  ? 94   GLU B CB  1 
ATOM   4922  C  CG  . GLU B  1 94  ? 4.646   38.035  64.301  1.00 37.74  ? 94   GLU B CG  1 
ATOM   4923  C  CD  . GLU B  1 94  ? 3.309   38.148  65.043  1.00 36.94  ? 94   GLU B CD  1 
ATOM   4924  O  OE1 . GLU B  1 94  ? 3.290   38.623  66.200  1.00 37.09  ? 94   GLU B OE1 1 
ATOM   4925  O  OE2 . GLU B  1 94  ? 2.268   37.762  64.465  1.00 36.18  ? 94   GLU B OE2 1 
ATOM   4926  N  N   . ASP B  1 95  ? 7.246   41.512  62.200  1.00 42.64  ? 95   ASP B N   1 
ATOM   4927  C  CA  . ASP B  1 95  ? 7.281   42.662  61.306  1.00 46.71  ? 95   ASP B CA  1 
ATOM   4928  C  C   . ASP B  1 95  ? 8.314   42.259  60.282  1.00 45.18  ? 95   ASP B C   1 
ATOM   4929  O  O   . ASP B  1 95  ? 9.494   42.612  60.398  1.00 45.57  ? 95   ASP B O   1 
ATOM   4930  C  CB  . ASP B  1 95  ? 7.831   43.844  62.127  1.00 54.28  ? 95   ASP B CB  1 
ATOM   4931  C  CG  . ASP B  1 95  ? 7.965   45.141  61.338  1.00 57.40  ? 95   ASP B CG  1 
ATOM   4932  O  OD1 . ASP B  1 95  ? 8.082   45.109  60.099  1.00 62.03  ? 95   ASP B OD1 1 
ATOM   4933  O  OD2 . ASP B  1 95  ? 7.968   46.213  61.985  1.00 55.41  ? 95   ASP B OD2 1 
ATOM   4934  N  N   . CYS B  1 96  ? 7.846   41.542  59.261  1.00 43.94  ? 96   CYS B N   1 
ATOM   4935  C  CA  . CYS B  1 96  ? 8.696   41.068  58.174  1.00 44.46  ? 96   CYS B CA  1 
ATOM   4936  C  C   . CYS B  1 96  ? 8.462   41.544  56.758  1.00 45.26  ? 96   CYS B C   1 
ATOM   4937  O  O   . CYS B  1 96  ? 9.177   41.104  55.867  1.00 45.70  ? 96   CYS B O   1 
ATOM   4938  C  CB  . CYS B  1 96  ? 8.893   39.551  58.210  1.00 56.16  ? 96   CYS B CB  1 
ATOM   4939  S  SG  . CYS B  1 96  ? 7.398   38.563  58.232  1.00 64.01  ? 96   CYS B SG  1 
ATOM   4940  N  N   . LEU B  1 97  ? 7.461   42.380  56.509  1.00 52.54  ? 97   LEU B N   1 
ATOM   4941  C  CA  . LEU B  1 97  ? 7.087   42.555  55.111  1.00 54.82  ? 97   LEU B CA  1 
ATOM   4942  C  C   . LEU B  1 97  ? 7.871   43.692  54.459  1.00 58.82  ? 97   LEU B C   1 
ATOM   4943  O  O   . LEU B  1 97  ? 7.504   44.870  54.540  1.00 61.82  ? 97   LEU B O   1 
ATOM   4944  C  CB  . LEU B  1 97  ? 5.589   42.828  55.006  1.00 45.37  ? 97   LEU B CB  1 
ATOM   4945  C  CG  . LEU B  1 97  ? 4.710   41.770  55.664  1.00 43.60  ? 97   LEU B CG  1 
ATOM   4946  C  CD1 . LEU B  1 97  ? 3.246   42.067  55.453  1.00 43.13  ? 97   LEU B CD1 1 
ATOM   4947  C  CD2 . LEU B  1 97  ? 5.060   40.428  55.102  1.00 42.82  ? 97   LEU B CD2 1 
ATOM   4948  N  N   . TYR B  1 98  ? 8.896   43.284  53.716  1.00 62.39  ? 98   TYR B N   1 
ATOM   4949  C  CA  . TYR B  1 98  ? 9.861   44.174  53.096  1.00 63.18  ? 98   TYR B CA  1 
ATOM   4950  C  C   . TYR B  1 98  ? 10.304  43.458  51.848  1.00 64.78  ? 98   TYR B C   1 
ATOM   4951  O  O   . TYR B  1 98  ? 10.538  42.248  51.892  1.00 63.78  ? 98   TYR B O   1 
ATOM   4952  C  CB  . TYR B  1 98  ? 11.075  44.360  54.017  1.00 59.32  ? 98   TYR B CB  1 
ATOM   4953  C  CG  . TYR B  1 98  ? 10.723  45.018  55.325  1.00 58.70  ? 98   TYR B CG  1 
ATOM   4954  C  CD1 . TYR B  1 98  ? 10.617  46.395  55.419  1.00 59.94  ? 98   TYR B CD1 1 
ATOM   4955  C  CD2 . TYR B  1 98  ? 10.463  44.266  56.458  1.00 57.74  ? 98   TYR B CD2 1 
ATOM   4956  C  CE1 . TYR B  1 98  ? 10.270  47.007  56.601  1.00 60.23  ? 98   TYR B CE1 1 
ATOM   4957  C  CE2 . TYR B  1 98  ? 10.116  44.871  57.646  1.00 58.64  ? 98   TYR B CE2 1 
ATOM   4958  C  CZ  . TYR B  1 98  ? 10.022  46.243  57.710  1.00 60.74  ? 98   TYR B CZ  1 
ATOM   4959  O  OH  . TYR B  1 98  ? 9.676   46.858  58.889  1.00 63.65  ? 98   TYR B OH  1 
ATOM   4960  N  N   . LEU B  1 99  ? 10.430  44.176  50.735  1.00 61.91  ? 99   LEU B N   1 
ATOM   4961  C  CA  . LEU B  1 99  ? 10.987  43.553  49.540  1.00 60.86  ? 99   LEU B CA  1 
ATOM   4962  C  C   . LEU B  1 99  ? 12.379  44.056  49.222  1.00 54.04  ? 99   LEU B C   1 
ATOM   4963  O  O   . LEU B  1 99  ? 12.914  44.942  49.897  1.00 61.03  ? 99   LEU B O   1 
ATOM   4964  C  CB  . LEU B  1 99  ? 10.048  43.669  48.343  1.00 52.52  ? 99   LEU B CB  1 
ATOM   4965  C  CG  . LEU B  1 99  ? 9.387   45.021  48.193  1.00 53.52  ? 99   LEU B CG  1 
ATOM   4966  C  CD1 . LEU B  1 99  ? 10.282  45.838  47.331  1.00 60.77  ? 99   LEU B CD1 1 
ATOM   4967  C  CD2 . LEU B  1 99  ? 8.003   44.892  47.582  1.00 52.85  ? 99   LEU B CD2 1 
ATOM   4968  N  N   . ASN B  1 100 ? 12.950  43.478  48.178  1.00 64.44  ? 100  ASN B N   1 
ATOM   4969  C  CA  . ASN B  1 100 ? 14.327  43.727  47.801  1.00 69.55  ? 100  ASN B CA  1 
ATOM   4970  C  C   . ASN B  1 100 ? 14.352  43.935  46.308  1.00 75.72  ? 100  ASN B C   1 
ATOM   4971  O  O   . ASN B  1 100 ? 13.765  43.142  45.572  1.00 77.28  ? 100  ASN B O   1 
ATOM   4972  C  CB  . ASN B  1 100 ? 15.220  42.531  48.152  1.00 60.04  ? 100  ASN B CB  1 
ATOM   4973  C  CG  . ASN B  1 100 ? 15.189  42.185  49.627  1.00 54.20  ? 100  ASN B CG  1 
ATOM   4974  O  OD1 . ASN B  1 100 ? 15.024  43.050  50.480  1.00 60.29  ? 100  ASN B OD1 1 
ATOM   4975  N  ND2 . ASN B  1 100 ? 15.343  40.910  49.933  1.00 52.99  ? 100  ASN B ND2 1 
ATOM   4976  N  N   . VAL B  1 101 ? 15.015  44.998  45.856  1.00 72.85  ? 101  VAL B N   1 
ATOM   4977  C  CA  . VAL B  1 101 ? 15.144  45.257  44.424  1.00 76.44  ? 101  VAL B CA  1 
ATOM   4978  C  C   . VAL B  1 101 ? 16.604  45.300  43.998  1.00 62.09  ? 101  VAL B C   1 
ATOM   4979  O  O   . VAL B  1 101 ? 17.446  45.883  44.672  1.00 62.90  ? 101  VAL B O   1 
ATOM   4980  C  CB  . VAL B  1 101 ? 14.436  46.562  43.977  1.00 66.00  ? 101  VAL B CB  1 
ATOM   4981  C  CG1 . VAL B  1 101 ? 14.276  46.567  42.465  1.00 62.69  ? 101  VAL B CG1 1 
ATOM   4982  C  CG2 . VAL B  1 101 ? 13.073  46.710  44.652  1.00 60.28  ? 101  VAL B CG2 1 
ATOM   4983  N  N   . TRP B  1 102 ? 16.896  44.656  42.878  1.00 62.52  ? 102  TRP B N   1 
ATOM   4984  C  CA  . TRP B  1 102 ? 18.220  44.740  42.298  1.00 66.08  ? 102  TRP B CA  1 
ATOM   4985  C  C   . TRP B  1 102 ? 18.166  45.375  40.905  1.00 74.23  ? 102  TRP B C   1 
ATOM   4986  O  O   . TRP B  1 102 ? 17.450  44.882  40.016  1.00 72.65  ? 102  TRP B O   1 
ATOM   4987  C  CB  . TRP B  1 102 ? 18.877  43.363  42.220  1.00 78.44  ? 102  TRP B CB  1 
ATOM   4988  C  CG  . TRP B  1 102 ? 19.463  42.877  43.506  1.00 81.57  ? 102  TRP B CG  1 
ATOM   4989  C  CD1 . TRP B  1 102 ? 20.741  43.060  43.946  1.00 83.49  ? 102  TRP B CD1 1 
ATOM   4990  C  CD2 . TRP B  1 102 ? 18.801  42.097  44.510  1.00 84.74  ? 102  TRP B CD2 1 
ATOM   4991  N  NE1 . TRP B  1 102 ? 20.914  42.452  45.167  1.00 83.98  ? 102  TRP B NE1 1 
ATOM   4992  C  CE2 . TRP B  1 102 ? 19.737  41.852  45.532  1.00 85.14  ? 102  TRP B CE2 1 
ATOM   4993  C  CE3 . TRP B  1 102 ? 17.506  41.581  44.644  1.00 86.10  ? 102  TRP B CE3 1 
ATOM   4994  C  CZ2 . TRP B  1 102 ? 19.417  41.116  46.674  1.00 86.20  ? 102  TRP B CZ2 1 
ATOM   4995  C  CZ3 . TRP B  1 102 ? 17.190  40.855  45.781  1.00 84.53  ? 102  TRP B CZ3 1 
ATOM   4996  C  CH2 . TRP B  1 102 ? 18.140  40.630  46.779  1.00 84.57  ? 102  TRP B CH2 1 
ATOM   4997  N  N   . THR B  1 103 ? 18.911  46.480  40.743  1.00 90.79  ? 103  THR B N   1 
ATOM   4998  C  CA  . THR B  1 103 ? 19.193  47.088  39.437  1.00 90.50  ? 103  THR B CA  1 
ATOM   4999  C  C   . THR B  1 103 ? 20.693  46.960  39.224  1.00 88.24  ? 103  THR B C   1 
ATOM   5000  O  O   . THR B  1 103 ? 21.445  46.827  40.186  1.00 81.07  ? 103  THR B O   1 
ATOM   5001  C  CB  . THR B  1 103 ? 18.821  48.600  39.371  1.00 71.26  ? 103  THR B CB  1 
ATOM   5002  O  OG1 . THR B  1 103 ? 17.776  48.909  40.304  1.00 69.89  ? 103  THR B OG1 1 
ATOM   5003  C  CG2 . THR B  1 103 ? 18.376  48.990  37.965  1.00 72.57  ? 103  THR B CG2 1 
ATOM   5004  N  N   . PRO B  1 104 ? 21.136  46.952  37.962  1.00 106.92 ? 104  PRO B N   1 
ATOM   5005  C  CA  . PRO B  1 104 ? 22.580  47.069  37.737  1.00 114.17 ? 104  PRO B CA  1 
ATOM   5006  C  C   . PRO B  1 104 ? 23.045  48.501  37.995  1.00 121.61 ? 104  PRO B C   1 
ATOM   5007  O  O   . PRO B  1 104 ? 22.201  49.403  38.070  1.00 122.51 ? 104  PRO B O   1 
ATOM   5008  C  CB  . PRO B  1 104 ? 22.724  46.735  36.249  1.00 101.58 ? 104  PRO B CB  1 
ATOM   5009  C  CG  . PRO B  1 104 ? 21.371  47.041  35.658  1.00 99.04  ? 104  PRO B CG  1 
ATOM   5010  C  CD  . PRO B  1 104 ? 20.403  46.648  36.721  1.00 95.25  ? 104  PRO B CD  1 
ATOM   5011  N  N   . TYR B  1 105 ? 24.351  48.713  38.158  1.00 123.35 ? 105  TYR B N   1 
ATOM   5012  C  CA  . TYR B  1 105 ? 24.870  50.082  38.140  1.00 124.70 ? 105  TYR B CA  1 
ATOM   5013  C  C   . TYR B  1 105 ? 25.572  50.288  36.806  1.00 123.74 ? 105  TYR B C   1 
ATOM   5014  O  O   . TYR B  1 105 ? 26.589  49.648  36.526  1.00 123.02 ? 105  TYR B O   1 
ATOM   5015  C  CB  . TYR B  1 105 ? 25.816  50.354  39.311  1.00 117.98 ? 105  TYR B CB  1 
ATOM   5016  C  CG  . TYR B  1 105 ? 25.965  51.819  39.687  1.00 119.98 ? 105  TYR B CG  1 
ATOM   5017  C  CD1 . TYR B  1 105 ? 26.494  52.742  38.792  1.00 122.26 ? 105  TYR B CD1 1 
ATOM   5018  C  CD2 . TYR B  1 105 ? 25.597  52.273  40.949  1.00 119.56 ? 105  TYR B CD2 1 
ATOM   5019  C  CE1 . TYR B  1 105 ? 26.637  54.078  39.140  1.00 123.71 ? 105  TYR B CE1 1 
ATOM   5020  C  CE2 . TYR B  1 105 ? 25.739  53.606  41.306  1.00 120.50 ? 105  TYR B CE2 1 
ATOM   5021  C  CZ  . TYR B  1 105 ? 26.262  54.502  40.399  1.00 122.43 ? 105  TYR B CZ  1 
ATOM   5022  O  OH  . TYR B  1 105 ? 26.402  55.827  40.748  1.00 123.09 ? 105  TYR B OH  1 
ATOM   5023  N  N   . PRO B  1 106 ? 25.044  51.206  35.986  1.00 113.37 ? 106  PRO B N   1 
ATOM   5024  C  CA  . PRO B  1 106 ? 24.027  52.199  36.344  1.00 111.13 ? 106  PRO B CA  1 
ATOM   5025  C  C   . PRO B  1 106 ? 22.586  51.747  36.109  1.00 107.29 ? 106  PRO B C   1 
ATOM   5026  O  O   . PRO B  1 106 ? 22.348  50.628  35.656  1.00 106.19 ? 106  PRO B O   1 
ATOM   5027  C  CB  . PRO B  1 106 ? 24.337  53.326  35.372  1.00 117.28 ? 106  PRO B CB  1 
ATOM   5028  C  CG  . PRO B  1 106 ? 24.713  52.576  34.111  1.00 118.97 ? 106  PRO B CG  1 
ATOM   5029  C  CD  . PRO B  1 106 ? 25.381  51.283  34.555  1.00 117.78 ? 106  PRO B CD  1 
ATOM   5030  N  N   . ARG B  1 107 ? 21.647  52.656  36.377  1.00 104.36 ? 107  ARG B N   1 
ATOM   5031  C  CA  . ARG B  1 107 ? 20.214  52.469  36.127  1.00 101.34 ? 107  ARG B CA  1 
ATOM   5032  C  C   . ARG B  1 107 ? 19.968  52.297  34.603  1.00 127.69 ? 107  ARG B C   1 
ATOM   5033  O  O   . ARG B  1 107 ? 20.934  52.205  33.846  1.00 129.31 ? 107  ARG B O   1 
ATOM   5034  C  CB  . ARG B  1 107 ? 19.434  53.630  36.754  1.00 103.11 ? 107  ARG B CB  1 
ATOM   5035  C  CG  . ARG B  1 107 ? 18.188  53.199  37.510  1.00 102.39 ? 107  ARG B CG  1 
ATOM   5036  C  CD  . ARG B  1 107 ? 17.461  54.384  38.114  1.00 106.40 ? 107  ARG B CD  1 
ATOM   5037  N  NE  . ARG B  1 107 ? 18.098  54.816  39.356  1.00 110.52 ? 107  ARG B NE  1 
ATOM   5038  C  CZ  . ARG B  1 107 ? 17.666  55.821  40.113  1.00 112.59 ? 107  ARG B CZ  1 
ATOM   5039  N  NH1 . ARG B  1 107 ? 16.587  56.504  39.752  1.00 114.49 ? 107  ARG B NH1 1 
ATOM   5040  N  NH2 . ARG B  1 107 ? 18.312  56.144  41.230  1.00 111.38 ? 107  ARG B NH2 1 
ATOM   5041  N  N   . PRO B  1 108 ? 18.698  52.233  34.135  1.00 137.77 ? 108  PRO B N   1 
ATOM   5042  C  CA  . PRO B  1 108 ? 18.620  51.435  32.908  1.00 137.56 ? 108  PRO B CA  1 
ATOM   5043  C  C   . PRO B  1 108 ? 19.043  52.202  31.664  1.00 137.19 ? 108  PRO B C   1 
ATOM   5044  O  O   . PRO B  1 108 ? 19.453  53.356  31.750  1.00 139.87 ? 108  PRO B O   1 
ATOM   5045  C  CB  . PRO B  1 108 ? 17.123  51.197  32.795  1.00 128.65 ? 108  PRO B CB  1 
ATOM   5046  C  CG  . PRO B  1 108 ? 16.567  52.557  33.162  1.00 129.35 ? 108  PRO B CG  1 
ATOM   5047  C  CD  . PRO B  1 108 ? 17.501  53.097  34.245  1.00 129.15 ? 108  PRO B CD  1 
ATOM   5048  N  N   . ALA B  1 109 ? 18.944  51.554  30.510  1.00 112.25 ? 109  ALA B N   1 
ATOM   5049  C  CA  . ALA B  1 109 ? 18.914  52.293  29.266  1.00 109.43 ? 109  ALA B CA  1 
ATOM   5050  C  C   . ALA B  1 109 ? 17.435  52.604  29.027  1.00 107.13 ? 109  ALA B C   1 
ATOM   5051  O  O   . ALA B  1 109 ? 16.960  53.709  29.318  1.00 102.31 ? 109  ALA B O   1 
ATOM   5052  C  CB  . ALA B  1 109 ? 19.485  51.444  28.134  1.00 112.09 ? 109  ALA B CB  1 
ATOM   5053  N  N   . SER B  1 110 ? 16.699  51.592  28.574  1.00 132.93 ? 110  SER B N   1 
ATOM   5054  C  CA  . SER B  1 110 ? 15.248  51.669  28.446  1.00 132.24 ? 110  SER B CA  1 
ATOM   5055  C  C   . SER B  1 110 ? 14.665  50.868  29.612  1.00 129.61 ? 110  SER B C   1 
ATOM   5056  O  O   . SER B  1 110 ? 15.420  50.260  30.380  1.00 126.88 ? 110  SER B O   1 
ATOM   5057  C  CB  . SER B  1 110 ? 14.809  51.073  27.094  1.00 111.17 ? 110  SER B CB  1 
ATOM   5058  O  OG  . SER B  1 110 ? 13.748  51.806  26.493  1.00 108.87 ? 110  SER B OG  1 
ATOM   5059  N  N   . PRO B  1 111 ? 13.329  50.859  29.762  1.00 125.54 ? 111  PRO B N   1 
ATOM   5060  C  CA  . PRO B  1 111 ? 12.819  49.941  30.783  1.00 122.75 ? 111  PRO B CA  1 
ATOM   5061  C  C   . PRO B  1 111 ? 13.145  48.484  30.453  1.00 123.15 ? 111  PRO B C   1 
ATOM   5062  O  O   . PRO B  1 111 ? 12.799  47.986  29.380  1.00 123.24 ? 111  PRO B O   1 
ATOM   5063  C  CB  . PRO B  1 111 ? 11.309  50.176  30.723  1.00 104.17 ? 111  PRO B CB  1 
ATOM   5064  C  CG  . PRO B  1 111 ? 11.183  51.604  30.321  1.00 105.39 ? 111  PRO B CG  1 
ATOM   5065  C  CD  . PRO B  1 111 ? 12.319  51.859  29.364  1.00 109.14 ? 111  PRO B CD  1 
ATOM   5066  N  N   . THR B  1 112 ? 13.803  47.815  31.393  1.00 118.91 ? 112  THR B N   1 
ATOM   5067  C  CA  . THR B  1 112 ? 14.189  46.417  31.238  1.00 116.61 ? 112  THR B CA  1 
ATOM   5068  C  C   . THR B  1 112 ? 13.137  45.474  31.852  1.00 110.59 ? 112  THR B C   1 
ATOM   5069  O  O   . THR B  1 112 ? 12.341  45.900  32.691  1.00 107.46 ? 112  THR B O   1 
ATOM   5070  C  CB  . THR B  1 112 ? 15.620  46.171  31.803  1.00 77.15  ? 112  THR B CB  1 
ATOM   5071  O  OG1 . THR B  1 112 ? 15.544  45.472  33.049  1.00 70.97  ? 112  THR B OG1 1 
ATOM   5072  C  CG2 . THR B  1 112 ? 16.364  47.502  31.991  1.00 75.04  ? 112  THR B CG2 1 
ATOM   5073  N  N   . PRO B  1 113 ? 13.109  44.202  31.409  1.00 97.20  ? 113  PRO B N   1 
ATOM   5074  C  CA  . PRO B  1 113 ? 12.225  43.201  32.021  1.00 91.80  ? 113  PRO B CA  1 
ATOM   5075  C  C   . PRO B  1 113 ? 12.527  42.947  33.501  1.00 87.82  ? 113  PRO B C   1 
ATOM   5076  O  O   . PRO B  1 113 ? 13.682  43.003  33.939  1.00 83.82  ? 113  PRO B O   1 
ATOM   5077  C  CB  . PRO B  1 113 ? 12.506  41.937  31.199  1.00 94.00  ? 113  PRO B CB  1 
ATOM   5078  C  CG  . PRO B  1 113 ? 12.940  42.438  29.881  1.00 97.17  ? 113  PRO B CG  1 
ATOM   5079  C  CD  . PRO B  1 113 ? 13.730  43.690  30.173  1.00 100.25 ? 113  PRO B CD  1 
ATOM   5080  N  N   . VAL B  1 114 ? 11.471  42.649  34.254  1.00 101.32 ? 114  VAL B N   1 
ATOM   5081  C  CA  . VAL B  1 114 ? 11.552  42.469  35.699  1.00 99.38  ? 114  VAL B CA  1 
ATOM   5082  C  C   . VAL B  1 114 ? 11.291  41.024  36.120  1.00 95.25  ? 114  VAL B C   1 
ATOM   5083  O  O   . VAL B  1 114 ? 10.368  40.370  35.619  1.00 93.40  ? 114  VAL B O   1 
ATOM   5084  C  CB  . VAL B  1 114 ? 10.563  43.413  36.422  1.00 94.75  ? 114  VAL B CB  1 
ATOM   5085  C  CG1 . VAL B  1 114 ? 10.117  42.842  37.761  1.00 92.73  ? 114  VAL B CG1 1 
ATOM   5086  C  CG2 . VAL B  1 114 ? 11.179  44.789  36.596  1.00 96.88  ? 114  VAL B CG2 1 
ATOM   5087  N  N   . LEU B  1 115 ? 12.122  40.534  37.037  1.00 97.21  ? 115  LEU B N   1 
ATOM   5088  C  CA  . LEU B  1 115 ? 11.952  39.204  37.608  1.00 92.13  ? 115  LEU B CA  1 
ATOM   5089  C  C   . LEU B  1 115 ? 11.607  39.257  39.101  1.00 91.67  ? 115  LEU B C   1 
ATOM   5090  O  O   . LEU B  1 115 ? 12.450  39.621  39.918  1.00 96.08  ? 115  LEU B O   1 
ATOM   5091  C  CB  . LEU B  1 115 ? 13.223  38.376  37.405  1.00 66.39  ? 115  LEU B CB  1 
ATOM   5092  C  CG  . LEU B  1 115 ? 13.541  37.962  35.969  1.00 63.36  ? 115  LEU B CG  1 
ATOM   5093  C  CD1 . LEU B  1 115 ? 14.761  37.053  35.943  1.00 63.18  ? 115  LEU B CD1 1 
ATOM   5094  C  CD2 . LEU B  1 115 ? 12.342  37.281  35.328  1.00 59.67  ? 115  LEU B CD2 1 
ATOM   5095  N  N   . ILE B  1 116 ? 10.374  38.884  39.448  1.00 74.68  ? 116  ILE B N   1 
ATOM   5096  C  CA  . ILE B  1 116 ? 9.936   38.811  40.843  1.00 63.97  ? 116  ILE B CA  1 
ATOM   5097  C  C   . ILE B  1 116 ? 10.101  37.397  41.366  1.00 59.95  ? 116  ILE B C   1 
ATOM   5098  O  O   . ILE B  1 116 ? 9.613   36.458  40.756  1.00 58.77  ? 116  ILE B O   1 
ATOM   5099  C  CB  . ILE B  1 116 ? 8.464   39.161  40.982  1.00 52.05  ? 116  ILE B CB  1 
ATOM   5100  C  CG1 . ILE B  1 116 ? 8.193   40.551  40.425  1.00 53.62  ? 116  ILE B CG1 1 
ATOM   5101  C  CG2 . ILE B  1 116 ? 8.063   39.100  42.420  1.00 50.66  ? 116  ILE B CG2 1 
ATOM   5102  C  CD1 . ILE B  1 116 ? 6.767   40.996  40.571  1.00 52.98  ? 116  ILE B CD1 1 
ATOM   5103  N  N   . TRP B  1 117 ? 10.782  37.244  42.494  1.00 56.37  ? 117  TRP B N   1 
ATOM   5104  C  CA  . TRP B  1 117 ? 11.033  35.927  43.068  1.00 55.99  ? 117  TRP B CA  1 
ATOM   5105  C  C   . TRP B  1 117 ? 10.133  35.655  44.281  1.00 55.96  ? 117  TRP B C   1 
ATOM   5106  O  O   . TRP B  1 117 ? 9.991   36.504  45.167  1.00 56.77  ? 117  TRP B O   1 
ATOM   5107  C  CB  . TRP B  1 117 ? 12.507  35.815  43.448  1.00 50.34  ? 117  TRP B CB  1 
ATOM   5108  C  CG  . TRP B  1 117 ? 12.891  34.603  44.237  1.00 49.13  ? 117  TRP B CG  1 
ATOM   5109  C  CD1 . TRP B  1 117 ? 13.281  34.566  45.547  1.00 48.59  ? 117  TRP B CD1 1 
ATOM   5110  C  CD2 . TRP B  1 117 ? 12.952  33.249  43.766  1.00 51.72  ? 117  TRP B CD2 1 
ATOM   5111  N  NE1 . TRP B  1 117 ? 13.575  33.273  45.925  1.00 47.60  ? 117  TRP B NE1 1 
ATOM   5112  C  CE2 . TRP B  1 117 ? 13.380  32.447  44.852  1.00 48.67  ? 117  TRP B CE2 1 
ATOM   5113  C  CE3 . TRP B  1 117 ? 12.678  32.634  42.539  1.00 52.85  ? 117  TRP B CE3 1 
ATOM   5114  C  CZ2 . TRP B  1 117 ? 13.542  31.060  44.736  1.00 47.85  ? 117  TRP B CZ2 1 
ATOM   5115  C  CZ3 . TRP B  1 117 ? 12.836  31.254  42.428  1.00 47.86  ? 117  TRP B CZ3 1 
ATOM   5116  C  CH2 . TRP B  1 117 ? 13.270  30.486  43.519  1.00 46.95  ? 117  TRP B CH2 1 
ATOM   5117  N  N   . ILE B  1 118 ? 9.506   34.481  44.309  1.00 46.38  ? 118  ILE B N   1 
ATOM   5118  C  CA  . ILE B  1 118 ? 8.760   34.059  45.482  1.00 44.77  ? 118  ILE B CA  1 
ATOM   5119  C  C   . ILE B  1 118 ? 9.399   32.808  46.044  1.00 43.92  ? 118  ILE B C   1 
ATOM   5120  O  O   . ILE B  1 118 ? 9.420   31.789  45.377  1.00 43.55  ? 118  ILE B O   1 
ATOM   5121  C  CB  . ILE B  1 118 ? 7.309   33.748  45.146  1.00 43.70  ? 118  ILE B CB  1 
ATOM   5122  C  CG1 . ILE B  1 118 ? 6.640   34.951  44.479  1.00 44.64  ? 118  ILE B CG1 1 
ATOM   5123  C  CG2 . ILE B  1 118 ? 6.565   33.367  46.407  1.00 42.15  ? 118  ILE B CG2 1 
ATOM   5124  C  CD1 . ILE B  1 118 ? 5.199   34.700  44.047  1.00 43.75  ? 118  ILE B CD1 1 
ATOM   5125  N  N   . TYR B  1 119 ? 9.916   32.887  47.268  1.00 59.96  ? 119  TYR B N   1 
ATOM   5126  C  CA  . TYR B  1 119 ? 10.643  31.766  47.873  1.00 60.27  ? 119  TYR B CA  1 
ATOM   5127  C  C   . TYR B  1 119 ? 9.804   30.534  48.207  1.00 59.04  ? 119  TYR B C   1 
ATOM   5128  O  O   . TYR B  1 119 ? 8.588   30.622  48.344  1.00 60.52  ? 119  TYR B O   1 
ATOM   5129  C  CB  . TYR B  1 119 ? 11.402  32.204  49.129  1.00 43.85  ? 119  TYR B CB  1 
ATOM   5130  C  CG  . TYR B  1 119 ? 10.589  32.884  50.228  1.00 42.62  ? 119  TYR B CG  1 
ATOM   5131  C  CD1 . TYR B  1 119 ? 9.886   32.152  51.178  1.00 41.12  ? 119  TYR B CD1 1 
ATOM   5132  C  CD2 . TYR B  1 119 ? 10.583  34.264  50.349  1.00 43.59  ? 119  TYR B CD2 1 
ATOM   5133  C  CE1 . TYR B  1 119 ? 9.180   32.788  52.200  1.00 40.61  ? 119  TYR B CE1 1 
ATOM   5134  C  CE2 . TYR B  1 119 ? 9.879   34.899  51.367  1.00 43.07  ? 119  TYR B CE2 1 
ATOM   5135  C  CZ  . TYR B  1 119 ? 9.184   34.162  52.284  1.00 41.59  ? 119  TYR B CZ  1 
ATOM   5136  O  OH  . TYR B  1 119 ? 8.504   34.835  53.269  1.00 41.19  ? 119  TYR B OH  1 
ATOM   5137  N  N   . GLY B  1 120 ? 10.476  29.393  48.350  1.00 41.02  ? 120  GLY B N   1 
ATOM   5138  C  CA  . GLY B  1 120 ? 9.830   28.153  48.735  1.00 39.53  ? 120  GLY B CA  1 
ATOM   5139  C  C   . GLY B  1 120 ? 9.886   28.002  50.238  1.00 39.66  ? 120  GLY B C   1 
ATOM   5140  O  O   . GLY B  1 120 ? 9.901   29.006  50.945  1.00 42.13  ? 120  GLY B O   1 
ATOM   5141  N  N   . GLY B  1 121 ? 9.946   26.768  50.736  1.00 38.79  ? 121  GLY B N   1 
ATOM   5142  C  CA  . GLY B  1 121 ? 9.952   26.536  52.179  1.00 38.56  ? 121  GLY B CA  1 
ATOM   5143  C  C   . GLY B  1 121 ? 8.670   26.009  52.816  1.00 38.82  ? 121  GLY B C   1 
ATOM   5144  O  O   . GLY B  1 121 ? 8.511   26.057  54.036  1.00 35.08  ? 121  GLY B O   1 
ATOM   5145  N  N   . GLY B  1 122 ? 7.750   25.529  51.981  1.00 44.11  ? 122  GLY B N   1 
ATOM   5146  C  CA  . GLY B  1 122 ? 6.598   24.760  52.424  1.00 33.58  ? 122  GLY B CA  1 
ATOM   5147  C  C   . GLY B  1 122 ? 5.493   25.532  53.109  1.00 33.01  ? 122  GLY B C   1 
ATOM   5148  O  O   . GLY B  1 122 ? 4.640   24.947  53.767  1.00 31.90  ? 122  GLY B O   1 
ATOM   5149  N  N   . PHE B  1 123 ? 5.509   26.848  52.974  1.00 33.84  ? 123  PHE B N   1 
ATOM   5150  C  CA  . PHE B  1 123 ? 4.561   27.702  53.684  1.00 35.04  ? 123  PHE B CA  1 
ATOM   5151  C  C   . PHE B  1 123 ? 4.814   27.724  55.194  1.00 35.76  ? 123  PHE B C   1 
ATOM   5152  O  O   . PHE B  1 123 ? 4.235   28.534  55.920  1.00 33.06  ? 123  PHE B O   1 
ATOM   5153  C  CB  . PHE B  1 123 ? 3.113   27.322  53.366  1.00 32.48  ? 123  PHE B CB  1 
ATOM   5154  C  CG  . PHE B  1 123 ? 2.785   27.400  51.915  1.00 32.87  ? 123  PHE B CG  1 
ATOM   5155  C  CD1 . PHE B  1 123 ? 2.529   28.616  51.319  1.00 33.74  ? 123  PHE B CD1 1 
ATOM   5156  C  CD2 . PHE B  1 123 ? 2.736   26.266  51.145  1.00 32.43  ? 123  PHE B CD2 1 
ATOM   5157  C  CE1 . PHE B  1 123 ? 2.224   28.698  49.990  1.00 34.18  ? 123  PHE B CE1 1 
ATOM   5158  C  CE2 . PHE B  1 123 ? 2.429   26.350  49.811  1.00 32.84  ? 123  PHE B CE2 1 
ATOM   5159  C  CZ  . PHE B  1 123 ? 2.173   27.568  49.235  1.00 33.72  ? 123  PHE B CZ  1 
ATOM   5160  N  N   . TYR B  1 124 ? 5.691   26.845  55.663  1.00 33.05  ? 124  TYR B N   1 
ATOM   5161  C  CA  . TYR B  1 124 ? 6.051   26.848  57.062  1.00 32.87  ? 124  TYR B CA  1 
ATOM   5162  C  C   . TYR B  1 124 ? 7.332   27.620  57.325  1.00 34.10  ? 124  TYR B C   1 
ATOM   5163  O  O   . TYR B  1 124 ? 7.746   27.703  58.472  1.00 49.04  ? 124  TYR B O   1 
ATOM   5164  C  CB  . TYR B  1 124 ? 6.146   25.423  57.622  1.00 32.00  ? 124  TYR B CB  1 
ATOM   5165  C  CG  . TYR B  1 124 ? 7.315   24.602  57.123  1.00 32.50  ? 124  TYR B CG  1 
ATOM   5166  C  CD1 . TYR B  1 124 ? 8.543   24.625  57.785  1.00 33.21  ? 124  TYR B CD1 1 
ATOM   5167  C  CD2 . TYR B  1 124 ? 7.188   23.785  56.010  1.00 32.30  ? 124  TYR B CD2 1 
ATOM   5168  C  CE1 . TYR B  1 124 ? 9.619   23.867  57.338  1.00 34.36  ? 124  TYR B CE1 1 
ATOM   5169  C  CE2 . TYR B  1 124 ? 8.251   23.026  55.551  1.00 36.85  ? 124  TYR B CE2 1 
ATOM   5170  C  CZ  . TYR B  1 124 ? 9.464   23.070  56.216  1.00 36.90  ? 124  TYR B CZ  1 
ATOM   5171  O  OH  . TYR B  1 124 ? 10.527  22.325  55.752  1.00 38.42  ? 124  TYR B OH  1 
ATOM   5172  N  N   . SER B  1 125 ? 7.939   28.196  56.280  1.00 35.17  ? 125  SER B N   1 
ATOM   5173  C  CA  . SER B  1 125 ? 9.246   28.862  56.391  1.00 36.47  ? 125  SER B CA  1 
ATOM   5174  C  C   . SER B  1 125 ? 9.739   29.492  55.091  1.00 37.65  ? 125  SER B C   1 
ATOM   5175  O  O   . SER B  1 125 ? 9.242   29.183  54.016  1.00 37.48  ? 125  SER B O   1 
ATOM   5176  C  CB  . SER B  1 125 ? 10.297  27.845  56.807  1.00 36.51  ? 125  SER B CB  1 
ATOM   5177  O  OG  . SER B  1 125 ? 10.452  26.885  55.778  1.00 36.40  ? 125  SER B OG  1 
ATOM   5178  N  N   . GLY B  1 126 ? 10.742  30.360  55.202  1.00 38.90  ? 126  GLY B N   1 
ATOM   5179  C  CA  . GLY B  1 126 ? 11.444  30.903  54.045  1.00 40.22  ? 126  GLY B CA  1 
ATOM   5180  C  C   . GLY B  1 126 ? 11.930  32.324  54.273  1.00 41.46  ? 126  GLY B C   1 
ATOM   5181  O  O   . GLY B  1 126 ? 11.806  32.820  55.382  1.00 41.28  ? 126  GLY B O   1 
ATOM   5182  N  N   . ALA B  1 127 ? 12.487  32.958  53.237  1.00 42.75  ? 127  ALA B N   1 
ATOM   5183  C  CA  . ALA B  1 127 ? 12.829  34.390  53.229  1.00 44.05  ? 127  ALA B CA  1 
ATOM   5184  C  C   . ALA B  1 127 ? 13.483  34.772  51.915  1.00 45.45  ? 127  ALA B C   1 
ATOM   5185  O  O   . ALA B  1 127 ? 14.112  33.940  51.278  1.00 45.64  ? 127  ALA B O   1 
ATOM   5186  C  CB  . ALA B  1 127 ? 13.785  34.728  54.353  1.00 44.57  ? 127  ALA B CB  1 
ATOM   5187  N  N   . ALA B  1 128 ? 13.402  36.050  51.556  1.00 46.53  ? 128  ALA B N   1 
ATOM   5188  C  CA  . ALA B  1 128 ? 14.106  36.574  50.390  1.00 48.09  ? 128  ALA B CA  1 
ATOM   5189  C  C   . ALA B  1 128 ? 15.532  36.909  50.819  1.00 54.53  ? 128  ALA B C   1 
ATOM   5190  O  O   . ALA B  1 128 ? 16.451  37.028  49.997  1.00 55.25  ? 128  ALA B O   1 
ATOM   5191  C  CB  . ALA B  1 128 ? 13.407  37.800  49.859  1.00 48.81  ? 128  ALA B CB  1 
ATOM   5192  N  N   . SER B  1 129 ? 15.698  37.011  52.136  1.00 51.61  ? 129  SER B N   1 
ATOM   5193  C  CA  . SER B  1 129 ? 16.967  37.333  52.784  1.00 53.59  ? 129  SER B CA  1 
ATOM   5194  C  C   . SER B  1 129 ? 18.022  36.252  52.573  1.00 51.54  ? 129  SER B C   1 
ATOM   5195  O  O   . SER B  1 129 ? 19.175  36.420  52.936  1.00 51.04  ? 129  SER B O   1 
ATOM   5196  C  CB  . SER B  1 129 ? 16.738  37.522  54.291  1.00 70.18  ? 129  SER B CB  1 
ATOM   5197  O  OG  . SER B  1 129 ? 15.561  38.274  54.558  1.00 72.14  ? 129  SER B OG  1 
ATOM   5198  N  N   . LEU B  1 130 ? 17.618  35.133  51.997  1.00 59.89  ? 130  LEU B N   1 
ATOM   5199  C  CA  . LEU B  1 130 ? 18.489  33.972  51.916  1.00 60.41  ? 130  LEU B CA  1 
ATOM   5200  C  C   . LEU B  1 130 ? 19.689  34.177  50.998  1.00 63.68  ? 130  LEU B C   1 
ATOM   5201  O  O   . LEU B  1 130 ? 19.685  35.064  50.133  1.00 64.66  ? 130  LEU B O   1 
ATOM   5202  C  CB  . LEU B  1 130 ? 17.697  32.750  51.460  1.00 47.77  ? 130  LEU B CB  1 
ATOM   5203  C  CG  . LEU B  1 130 ? 16.878  31.973  52.474  1.00 46.05  ? 130  LEU B CG  1 
ATOM   5204  C  CD1 . LEU B  1 130 ? 17.448  30.575  52.543  1.00 45.62  ? 130  LEU B CD1 1 
ATOM   5205  C  CD2 . LEU B  1 130 ? 16.881  32.644  53.832  1.00 45.91  ? 130  LEU B CD2 1 
ATOM   5206  N  N   . ASP B  1 131 ? 20.708  33.342  51.204  1.00 57.91  ? 131  ASP B N   1 
ATOM   5207  C  CA  . ASP B  1 131 ? 21.924  33.359  50.392  1.00 62.25  ? 131  ASP B CA  1 
ATOM   5208  C  C   . ASP B  1 131 ? 21.695  33.016  48.912  1.00 56.72  ? 131  ASP B C   1 
ATOM   5209  O  O   . ASP B  1 131 ? 22.013  33.813  48.022  1.00 55.76  ? 131  ASP B O   1 
ATOM   5210  C  CB  . ASP B  1 131 ? 22.979  32.416  50.992  1.00 86.50  ? 131  ASP B CB  1 
ATOM   5211  C  CG  . ASP B  1 131 ? 23.947  33.125  51.941  1.00 92.54  ? 131  ASP B CG  1 
ATOM   5212  O  OD1 . ASP B  1 131 ? 23.699  34.295  52.312  1.00 94.32  ? 131  ASP B OD1 1 
ATOM   5213  O  OD2 . ASP B  1 131 ? 24.960  32.497  52.320  1.00 93.40  ? 131  ASP B OD2 1 
ATOM   5214  N  N   . VAL B  1 132 ? 21.141  31.836  48.649  1.00 56.94  ? 132  VAL B N   1 
ATOM   5215  C  CA  . VAL B  1 132 ? 20.992  31.351  47.275  1.00 57.75  ? 132  VAL B CA  1 
ATOM   5216  C  C   . VAL B  1 132 ? 20.101  32.250  46.415  1.00 59.93  ? 132  VAL B C   1 
ATOM   5217  O  O   . VAL B  1 132 ? 20.068  32.134  45.187  1.00 61.65  ? 132  VAL B O   1 
ATOM   5218  C  CB  . VAL B  1 132 ? 20.447  29.916  47.240  1.00 52.99  ? 132  VAL B CB  1 
ATOM   5219  C  CG1 . VAL B  1 132 ? 21.435  28.967  47.897  1.00 51.17  ? 132  VAL B CG1 1 
ATOM   5220  C  CG2 . VAL B  1 132 ? 19.100  29.855  47.928  1.00 50.72  ? 132  VAL B CG2 1 
ATOM   5221  N  N   . TYR B  1 133 ? 19.382  33.146  47.075  1.00 56.97  ? 133  TYR B N   1 
ATOM   5222  C  CA  . TYR B  1 133 ? 18.486  34.068  46.398  1.00 59.97  ? 133  TYR B CA  1 
ATOM   5223  C  C   . TYR B  1 133 ? 19.213  35.369  46.100  1.00 61.66  ? 133  TYR B C   1 
ATOM   5224  O  O   . TYR B  1 133 ? 18.574  36.376  45.795  1.00 61.43  ? 133  TYR B O   1 
ATOM   5225  C  CB  . TYR B  1 133 ? 17.185  34.302  47.178  1.00 71.92  ? 133  TYR B CB  1 
ATOM   5226  C  CG  . TYR B  1 133 ? 16.424  33.038  47.573  1.00 71.27  ? 133  TYR B CG  1 
ATOM   5227  C  CD1 . TYR B  1 133 ? 16.483  31.880  46.814  1.00 69.60  ? 133  TYR B CD1 1 
ATOM   5228  C  CD2 . TYR B  1 133 ? 15.649  33.018  48.722  1.00 70.05  ? 133  TYR B CD2 1 
ATOM   5229  C  CE1 . TYR B  1 133 ? 15.795  30.744  47.204  1.00 67.32  ? 133  TYR B CE1 1 
ATOM   5230  C  CE2 . TYR B  1 133 ? 14.964  31.896  49.111  1.00 66.78  ? 133  TYR B CE2 1 
ATOM   5231  C  CZ  . TYR B  1 133 ? 15.037  30.767  48.356  1.00 66.45  ? 133  TYR B CZ  1 
ATOM   5232  O  OH  . TYR B  1 133 ? 14.334  29.668  48.777  1.00 66.81  ? 133  TYR B OH  1 
ATOM   5233  N  N   . ASP B  1 134 ? 20.541  35.350  46.248  1.00 79.87  ? 134  ASP B N   1 
ATOM   5234  C  CA  . ASP B  1 134 ? 21.375  36.536  46.037  1.00 82.34  ? 134  ASP B CA  1 
ATOM   5235  C  C   . ASP B  1 134 ? 20.998  37.100  44.676  1.00 82.13  ? 134  ASP B C   1 
ATOM   5236  O  O   . ASP B  1 134 ? 21.182  36.454  43.650  1.00 83.51  ? 134  ASP B O   1 
ATOM   5237  C  CB  . ASP B  1 134 ? 22.854  36.102  46.012  1.00 68.15  ? 134  ASP B CB  1 
ATOM   5238  C  CG  . ASP B  1 134 ? 23.809  37.155  46.588  1.00 66.88  ? 134  ASP B CG  1 
ATOM   5239  O  OD1 . ASP B  1 134 ? 23.505  38.367  46.493  1.00 65.94  ? 134  ASP B OD1 1 
ATOM   5240  O  OD2 . ASP B  1 134 ? 24.873  36.756  47.129  1.00 65.61  ? 134  ASP B OD2 1 
ATOM   5241  N  N   . GLY B  1 135 ? 20.513  38.332  44.663  1.00 66.65  ? 135  GLY B N   1 
ATOM   5242  C  CA  . GLY B  1 135 ? 19.776  38.801  43.510  1.00 70.68  ? 135  GLY B CA  1 
ATOM   5243  C  C   . GLY B  1 135 ? 20.636  39.436  42.441  1.00 78.78  ? 135  GLY B C   1 
ATOM   5244  O  O   . GLY B  1 135 ? 20.169  39.671  41.320  1.00 81.32  ? 135  GLY B O   1 
ATOM   5245  N  N   . ARG B  1 136 ? 21.901  39.684  42.787  1.00 98.06  ? 136  ARG B N   1 
ATOM   5246  C  CA  . ARG B  1 136 ? 22.776  40.582  42.029  1.00 96.70  ? 136  ARG B CA  1 
ATOM   5247  C  C   . ARG B  1 136 ? 23.337  40.029  40.713  1.00 93.71  ? 136  ARG B C   1 
ATOM   5248  O  O   . ARG B  1 136 ? 23.467  40.765  39.737  1.00 95.90  ? 136  ARG B O   1 
ATOM   5249  C  CB  . ARG B  1 136 ? 23.922  41.076  42.921  1.00 84.70  ? 136  ARG B CB  1 
ATOM   5250  C  CG  . ARG B  1 136 ? 25.190  40.239  42.837  1.00 85.96  ? 136  ARG B CG  1 
ATOM   5251  C  CD  . ARG B  1 136 ? 25.474  39.523  44.129  1.00 85.96  ? 136  ARG B CD  1 
ATOM   5252  N  NE  . ARG B  1 136 ? 26.080  40.394  45.127  1.00 88.94  ? 136  ARG B NE  1 
ATOM   5253  C  CZ  . ARG B  1 136 ? 26.950  39.970  46.036  1.00 90.47  ? 136  ARG B CZ  1 
ATOM   5254  N  NH1 . ARG B  1 136 ? 27.303  38.689  46.049  1.00 90.52  ? 136  ARG B NH1 1 
ATOM   5255  N  NH2 . ARG B  1 136 ? 27.465  40.817  46.922  1.00 90.71  ? 136  ARG B NH2 1 
ATOM   5256  N  N   . PHE B  1 137 ? 23.671  38.745  40.685  1.00 65.21  ? 137  PHE B N   1 
ATOM   5257  C  CA  . PHE B  1 137 ? 24.274  38.153  39.503  1.00 66.45  ? 137  PHE B CA  1 
ATOM   5258  C  C   . PHE B  1 137 ? 23.365  38.268  38.277  1.00 66.67  ? 137  PHE B C   1 
ATOM   5259  O  O   . PHE B  1 137 ? 23.823  38.634  37.207  1.00 68.46  ? 137  PHE B O   1 
ATOM   5260  C  CB  . PHE B  1 137 ? 24.662  36.703  39.776  1.00 83.56  ? 137  PHE B CB  1 
ATOM   5261  C  CG  . PHE B  1 137 ? 25.658  36.544  40.893  1.00 88.70  ? 137  PHE B CG  1 
ATOM   5262  C  CD1 . PHE B  1 137 ? 25.251  36.556  42.215  1.00 90.47  ? 137  PHE B CD1 1 
ATOM   5263  C  CD2 . PHE B  1 137 ? 27.002  36.378  40.623  1.00 92.44  ? 137  PHE B CD2 1 
ATOM   5264  C  CE1 . PHE B  1 137 ? 26.168  36.402  43.246  1.00 91.59  ? 137  PHE B CE1 1 
ATOM   5265  C  CE2 . PHE B  1 137 ? 27.919  36.225  41.651  1.00 94.35  ? 137  PHE B CE2 1 
ATOM   5266  C  CZ  . PHE B  1 137 ? 27.499  36.241  42.964  1.00 92.87  ? 137  PHE B CZ  1 
ATOM   5267  N  N   . LEU B  1 138 ? 22.078  37.977  38.440  1.00 74.60  ? 138  LEU B N   1 
ATOM   5268  C  CA  . LEU B  1 138 ? 21.102  38.135  37.353  1.00 76.78  ? 138  LEU B CA  1 
ATOM   5269  C  C   . LEU B  1 138 ? 21.001  39.584  36.883  1.00 77.69  ? 138  LEU B C   1 
ATOM   5270  O  O   . LEU B  1 138 ? 20.935  39.856  35.684  1.00 78.22  ? 138  LEU B O   1 
ATOM   5271  C  CB  . LEU B  1 138 ? 19.705  37.646  37.780  1.00 82.49  ? 138  LEU B CB  1 
ATOM   5272  C  CG  . LEU B  1 138 ? 19.289  36.186  37.550  1.00 79.13  ? 138  LEU B CG  1 
ATOM   5273  C  CD1 . LEU B  1 138 ? 19.510  35.776  36.103  1.00 80.37  ? 138  LEU B CD1 1 
ATOM   5274  C  CD2 . LEU B  1 138 ? 20.036  35.267  38.481  1.00 76.37  ? 138  LEU B CD2 1 
ATOM   5275  N  N   . ALA B  1 139 ? 20.967  40.502  37.843  1.00 80.37  ? 139  ALA B N   1 
ATOM   5276  C  CA  . ALA B  1 139 ? 20.927  41.927  37.553  1.00 84.97  ? 139  ALA B CA  1 
ATOM   5277  C  C   . ALA B  1 139 ? 22.125  42.368  36.703  1.00 93.25  ? 139  ALA B C   1 
ATOM   5278  O  O   . ALA B  1 139 ? 21.964  42.759  35.546  1.00 94.07  ? 139  ALA B O   1 
ATOM   5279  C  CB  . ALA B  1 139 ? 20.856  42.727  38.848  1.00 79.04  ? 139  ALA B CB  1 
ATOM   5280  N  N   . GLN B  1 140 ? 23.323  42.291  37.281  1.00 113.99 ? 140  GLN B N   1 
ATOM   5281  C  CA  . GLN B  1 140 ? 24.547  42.715  36.597  1.00 116.22 ? 140  GLN B CA  1 
ATOM   5282  C  C   . GLN B  1 140 ? 24.750  41.994  35.269  1.00 117.81 ? 140  GLN B C   1 
ATOM   5283  O  O   . GLN B  1 140 ? 24.874  42.632  34.223  1.00 121.10 ? 140  GLN B O   1 
ATOM   5284  C  CB  . GLN B  1 140 ? 25.775  42.515  37.498  1.00 97.55  ? 140  GLN B CB  1 
ATOM   5285  C  CG  . GLN B  1 140 ? 27.111  42.780  36.808  1.00 98.60  ? 140  GLN B CG  1 
ATOM   5286  C  CD  . GLN B  1 140 ? 27.748  41.518  36.249  1.00 97.21  ? 140  GLN B CD  1 
ATOM   5287  O  OE1 . GLN B  1 140 ? 27.953  40.540  36.969  1.00 94.37  ? 140  GLN B OE1 1 
ATOM   5288  N  NE2 . GLN B  1 140 ? 28.061  41.534  34.957  1.00 98.25  ? 140  GLN B NE2 1 
ATOM   5289  N  N   . VAL B  1 141 ? 24.774  40.665  35.320  1.00 90.68  ? 141  VAL B N   1 
ATOM   5290  C  CA  . VAL B  1 141 ? 25.081  39.863  34.146  1.00 73.91  ? 141  VAL B CA  1 
ATOM   5291  C  C   . VAL B  1 141 ? 24.022  39.964  33.055  1.00 73.98  ? 141  VAL B C   1 
ATOM   5292  O  O   . VAL B  1 141 ? 24.343  40.249  31.913  1.00 75.82  ? 141  VAL B O   1 
ATOM   5293  C  CB  . VAL B  1 141 ? 25.374  38.393  34.510  1.00 72.67  ? 141  VAL B CB  1 
ATOM   5294  C  CG1 . VAL B  1 141 ? 25.211  37.491  33.303  1.00 73.05  ? 141  VAL B CG1 1 
ATOM   5295  C  CG2 . VAL B  1 141 ? 26.765  38.272  35.094  1.00 73.57  ? 141  VAL B CG2 1 
ATOM   5296  N  N   . GLU B  1 142 ? 22.762  39.733  33.380  1.00 73.68  ? 142  GLU B N   1 
ATOM   5297  C  CA  . GLU B  1 142 ? 21.754  39.736  32.323  1.00 78.56  ? 142  GLU B CA  1 
ATOM   5298  C  C   . GLU B  1 142 ? 20.969  41.042  32.185  1.00 76.15  ? 142  GLU B C   1 
ATOM   5299  O  O   . GLU B  1 142 ? 20.031  41.127  31.384  1.00 75.47  ? 142  GLU B O   1 
ATOM   5300  C  CB  . GLU B  1 142 ? 20.843  38.504  32.409  1.00 99.21  ? 142  GLU B CB  1 
ATOM   5301  C  CG  . GLU B  1 142 ? 21.557  37.183  32.083  1.00 102.89 ? 142  GLU B CG  1 
ATOM   5302  C  CD  . GLU B  1 142 ? 22.029  37.102  30.635  1.00 106.56 ? 142  GLU B CD  1 
ATOM   5303  O  OE1 . GLU B  1 142 ? 21.300  37.592  29.742  1.00 108.08 ? 142  GLU B OE1 1 
ATOM   5304  O  OE2 . GLU B  1 142 ? 23.126  36.548  30.395  1.00 106.40 ? 142  GLU B OE2 1 
ATOM   5305  N  N   . GLY B  1 143 ? 21.349  42.046  32.973  1.00 75.10  ? 143  GLY B N   1 
ATOM   5306  C  CA  . GLY B  1 143 ? 20.736  43.364  32.889  1.00 76.47  ? 143  GLY B CA  1 
ATOM   5307  C  C   . GLY B  1 143 ? 19.289  43.372  33.339  1.00 74.04  ? 143  GLY B C   1 
ATOM   5308  O  O   . GLY B  1 143 ? 18.427  43.987  32.703  1.00 73.22  ? 143  GLY B O   1 
ATOM   5309  N  N   . ALA B  1 144 ? 19.024  42.690  34.449  1.00 70.96  ? 144  ALA B N   1 
ATOM   5310  C  CA  . ALA B  1 144 ? 17.659  42.458  34.893  1.00 69.73  ? 144  ALA B CA  1 
ATOM   5311  C  C   . ALA B  1 144 ? 17.355  43.175  36.196  1.00 70.84  ? 144  ALA B C   1 
ATOM   5312  O  O   . ALA B  1 144 ? 18.182  43.209  37.103  1.00 66.99  ? 144  ALA B O   1 
ATOM   5313  C  CB  . ALA B  1 144 ? 17.412  40.973  35.043  1.00 66.04  ? 144  ALA B CB  1 
ATOM   5314  N  N   . VAL B  1 145 ? 16.160  43.756  36.279  1.00 97.91  ? 145  VAL B N   1 
ATOM   5315  C  CA  . VAL B  1 145 ? 15.666  44.296  37.540  1.00 102.03 ? 145  VAL B CA  1 
ATOM   5316  C  C   . VAL B  1 145 ? 14.944  43.172  38.266  1.00 100.08 ? 145  VAL B C   1 
ATOM   5317  O  O   . VAL B  1 145 ? 13.946  42.634  37.772  1.00 98.19  ? 145  VAL B O   1 
ATOM   5318  C  CB  . VAL B  1 145 ? 14.705  45.488  37.351  1.00 100.63 ? 145  VAL B CB  1 
ATOM   5319  C  CG1 . VAL B  1 145 ? 14.176  45.950  38.697  1.00 99.42  ? 145  VAL B CG1 1 
ATOM   5320  C  CG2 . VAL B  1 145 ? 15.404  46.636  36.643  1.00 104.78 ? 145  VAL B CG2 1 
ATOM   5321  N  N   . LEU B  1 146 ? 15.458  42.818  39.440  1.00 84.82  ? 146  LEU B N   1 
ATOM   5322  C  CA  . LEU B  1 146 ? 15.033  41.599  40.114  1.00 80.09  ? 146  LEU B CA  1 
ATOM   5323  C  C   . LEU B  1 146 ? 14.499  41.845  41.528  1.00 78.18  ? 146  LEU B C   1 
ATOM   5324  O  O   . LEU B  1 146 ? 15.243  42.255  42.422  1.00 78.58  ? 146  LEU B O   1 
ATOM   5325  C  CB  . LEU B  1 146 ? 16.198  40.616  40.151  1.00 77.41  ? 146  LEU B CB  1 
ATOM   5326  C  CG  . LEU B  1 146 ? 15.865  39.212  40.621  1.00 78.11  ? 146  LEU B CG  1 
ATOM   5327  C  CD1 . LEU B  1 146 ? 16.181  38.203  39.518  1.00 79.11  ? 146  LEU B CD1 1 
ATOM   5328  C  CD2 . LEU B  1 146 ? 16.639  38.923  41.894  1.00 78.69  ? 146  LEU B CD2 1 
ATOM   5329  N  N   . VAL B  1 147 ? 13.205  41.584  41.718  1.00 84.94  ? 147  VAL B N   1 
ATOM   5330  C  CA  . VAL B  1 147 ? 12.542  41.802  43.001  1.00 78.23  ? 147  VAL B CA  1 
ATOM   5331  C  C   . VAL B  1 147 ? 12.346  40.491  43.744  1.00 71.04  ? 147  VAL B C   1 
ATOM   5332  O  O   . VAL B  1 147 ? 11.994  39.476  43.150  1.00 68.36  ? 147  VAL B O   1 
ATOM   5333  C  CB  . VAL B  1 147 ? 11.155  42.473  42.840  1.00 55.82  ? 147  VAL B CB  1 
ATOM   5334  C  CG1 . VAL B  1 147 ? 10.848  43.320  44.049  1.00 55.57  ? 147  VAL B CG1 1 
ATOM   5335  C  CG2 . VAL B  1 147 ? 11.110  43.328  41.602  1.00 57.57  ? 147  VAL B CG2 1 
ATOM   5336  N  N   . SER B  1 148 ? 12.583  40.515  45.047  1.00 53.47  ? 148  SER B N   1 
ATOM   5337  C  CA  . SER B  1 148 ? 12.228  39.389  45.894  1.00 51.61  ? 148  SER B CA  1 
ATOM   5338  C  C   . SER B  1 148 ? 11.603  39.894  47.198  1.00 56.89  ? 148  SER B C   1 
ATOM   5339  O  O   . SER B  1 148 ? 12.184  40.737  47.878  1.00 51.57  ? 148  SER B O   1 
ATOM   5340  C  CB  . SER B  1 148 ? 13.446  38.504  46.160  1.00 51.61  ? 148  SER B CB  1 
ATOM   5341  O  OG  . SER B  1 148 ? 14.401  39.165  46.959  1.00 52.45  ? 148  SER B OG  1 
ATOM   5342  N  N   . MET B  1 149 ? 10.418  39.381  47.540  1.00 56.38  ? 149  MET B N   1 
ATOM   5343  C  CA  . MET B  1 149 ? 9.702   39.828  48.742  1.00 53.07  ? 149  MET B CA  1 
ATOM   5344  C  C   . MET B  1 149 ? 9.565   38.742  49.803  1.00 50.31  ? 149  MET B C   1 
ATOM   5345  O  O   . MET B  1 149 ? 9.642   37.554  49.506  1.00 45.98  ? 149  MET B O   1 
ATOM   5346  C  CB  . MET B  1 149 ? 8.303   40.357  48.401  1.00 51.00  ? 149  MET B CB  1 
ATOM   5347  C  CG  . MET B  1 149 ? 7.199   39.310  48.518  1.00 47.93  ? 149  MET B CG  1 
ATOM   5348  S  SD  . MET B  1 149 ? 7.316   38.059  47.233  1.00 48.69  ? 149  MET B SD  1 
ATOM   5349  C  CE  . MET B  1 149 ? 6.223   38.742  45.994  1.00 46.74  ? 149  MET B CE  1 
ATOM   5350  N  N   . ASN B  1 150 ? 9.389   39.175  51.047  1.00 50.44  ? 150  ASN B N   1 
ATOM   5351  C  CA  . ASN B  1 150 ? 9.022   38.290  52.132  1.00 44.84  ? 150  ASN B CA  1 
ATOM   5352  C  C   . ASN B  1 150 ? 7.515   38.308  52.233  1.00 43.79  ? 150  ASN B C   1 
ATOM   5353  O  O   . ASN B  1 150 ? 6.911   39.373  52.146  1.00 45.05  ? 150  ASN B O   1 
ATOM   5354  C  CB  . ASN B  1 150 ? 9.602   38.795  53.447  1.00 53.82  ? 150  ASN B CB  1 
ATOM   5355  C  CG  . ASN B  1 150 ? 11.096  38.607  53.539  1.00 54.92  ? 150  ASN B CG  1 
ATOM   5356  O  OD1 . ASN B  1 150 ? 11.664  37.738  52.880  1.00 55.84  ? 150  ASN B OD1 1 
ATOM   5357  N  ND2 . ASN B  1 150 ? 11.745  39.415  54.370  1.00 54.26  ? 150  ASN B ND2 1 
ATOM   5358  N  N   . TYR B  1 151 ? 6.903   37.140  52.397  1.00 42.34  ? 151  TYR B N   1 
ATOM   5359  C  CA  . TYR B  1 151 ? 5.483   37.055  52.729  1.00 41.22  ? 151  TYR B CA  1 
ATOM   5360  C  C   . TYR B  1 151 ? 5.383   36.235  54.004  1.00 39.94  ? 151  TYR B C   1 
ATOM   5361  O  O   . TYR B  1 151 ? 6.304   35.492  54.338  1.00 39.80  ? 151  TYR B O   1 
ATOM   5362  C  CB  . TYR B  1 151 ? 4.685   36.391  51.611  1.00 40.69  ? 151  TYR B CB  1 
ATOM   5363  C  CG  . TYR B  1 151 ? 5.179   35.005  51.262  1.00 44.30  ? 151  TYR B CG  1 
ATOM   5364  C  CD1 . TYR B  1 151 ? 6.307   34.833  50.466  1.00 44.91  ? 151  TYR B CD1 1 
ATOM   5365  C  CD2 . TYR B  1 151 ? 4.523   33.869  51.718  1.00 38.54  ? 151  TYR B CD2 1 
ATOM   5366  C  CE1 . TYR B  1 151 ? 6.775   33.578  50.138  1.00 40.49  ? 151  TYR B CE1 1 
ATOM   5367  C  CE2 . TYR B  1 151 ? 4.989   32.604  51.394  1.00 38.02  ? 151  TYR B CE2 1 
ATOM   5368  C  CZ  . TYR B  1 151 ? 6.119   32.476  50.605  1.00 39.01  ? 151  TYR B CZ  1 
ATOM   5369  O  OH  . TYR B  1 151 ? 6.605   31.246  50.270  1.00 38.59  ? 151  TYR B OH  1 
ATOM   5370  N  N   . ARG B  1 152 ? 4.283   36.385  54.727  1.00 39.10  ? 152  ARG B N   1 
ATOM   5371  C  CA  . ARG B  1 152 ? 4.078   35.656  55.969  1.00 37.93  ? 152  ARG B CA  1 
ATOM   5372  C  C   . ARG B  1 152 ? 4.006   34.141  55.754  1.00 36.81  ? 152  ARG B C   1 
ATOM   5373  O  O   . ARG B  1 152 ? 3.506   33.665  54.741  1.00 36.53  ? 152  ARG B O   1 
ATOM   5374  C  CB  . ARG B  1 152 ? 2.808   36.156  56.657  1.00 37.35  ? 152  ARG B CB  1 
ATOM   5375  C  CG  . ARG B  1 152 ? 3.032   37.330  57.580  1.00 40.76  ? 152  ARG B CG  1 
ATOM   5376  C  CD  . ARG B  1 152 ? 1.723   37.913  58.032  1.00 37.70  ? 152  ARG B CD  1 
ATOM   5377  N  NE  . ARG B  1 152 ? 1.055   38.591  56.935  1.00 38.30  ? 152  ARG B NE  1 
ATOM   5378  C  CZ  . ARG B  1 152 ? -0.166  39.103  57.010  1.00 38.10  ? 152  ARG B CZ  1 
ATOM   5379  N  NH1 . ARG B  1 152 ? -0.863  39.004  58.131  1.00 37.29  ? 152  ARG B NH1 1 
ATOM   5380  N  NH2 . ARG B  1 152 ? -0.696  39.711  55.960  1.00 38.77  ? 152  ARG B NH2 1 
ATOM   5381  N  N   . VAL B  1 153 ? 4.522   33.379  56.707  1.00 40.45  ? 153  VAL B N   1 
ATOM   5382  C  CA  . VAL B  1 153 ? 4.405   31.933  56.641  1.00 39.39  ? 153  VAL B CA  1 
ATOM   5383  C  C   . VAL B  1 153 ? 3.819   31.357  57.925  1.00 37.67  ? 153  VAL B C   1 
ATOM   5384  O  O   . VAL B  1 153 ? 3.532   32.078  58.892  1.00 36.35  ? 153  VAL B O   1 
ATOM   5385  C  CB  . VAL B  1 153 ? 5.756   31.260  56.349  1.00 35.64  ? 153  VAL B CB  1 
ATOM   5386  C  CG1 . VAL B  1 153 ? 6.231   31.652  54.983  1.00 36.69  ? 153  VAL B CG1 1 
ATOM   5387  C  CG2 . VAL B  1 153 ? 6.786   31.629  57.410  1.00 36.22  ? 153  VAL B CG2 1 
ATOM   5388  N  N   . GLY B  1 154 ? 3.646   30.042  57.916  1.00 36.32  ? 154  GLY B N   1 
ATOM   5389  C  CA  . GLY B  1 154 ? 3.120   29.337  59.061  1.00 35.97  ? 154  GLY B CA  1 
ATOM   5390  C  C   . GLY B  1 154 ? 1.742   29.832  59.403  1.00 31.48  ? 154  GLY B C   1 
ATOM   5391  O  O   . GLY B  1 154 ? 0.993   30.254  58.528  1.00 31.56  ? 154  GLY B O   1 
ATOM   5392  N  N   . THR B  1 155 ? 1.416   29.789  60.686  1.00 31.04  ? 155  THR B N   1 
ATOM   5393  C  CA  . THR B  1 155 ? 0.105   30.199  61.151  1.00 30.38  ? 155  THR B CA  1 
ATOM   5394  C  C   . THR B  1 155 ? -0.163  31.649  60.753  1.00 31.27  ? 155  THR B C   1 
ATOM   5395  O  O   . THR B  1 155 ? -1.259  32.001  60.320  1.00 37.40  ? 155  THR B O   1 
ATOM   5396  C  CB  . THR B  1 155 ? -0.018  29.998  62.670  1.00 29.89  ? 155  THR B CB  1 
ATOM   5397  O  OG1 . THR B  1 155 ? 0.985   30.759  63.337  1.00 30.78  ? 155  THR B OG1 1 
ATOM   5398  C  CG2 . THR B  1 155 ? 0.202   28.552  63.012  1.00 29.07  ? 155  THR B CG2 1 
ATOM   5399  N  N   . PHE B  1 156 ? 0.870   32.474  60.852  1.00 38.31  ? 156  PHE B N   1 
ATOM   5400  C  CA  . PHE B  1 156 ? 0.746   33.899  60.598  1.00 33.35  ? 156  PHE B CA  1 
ATOM   5401  C  C   . PHE B  1 156 ? 0.318   34.179  59.177  1.00 36.27  ? 156  PHE B C   1 
ATOM   5402  O  O   . PHE B  1 156 ? -0.501  35.059  58.945  1.00 35.92  ? 156  PHE B O   1 
ATOM   5403  C  CB  . PHE B  1 156 ? 2.061   34.592  60.899  1.00 34.47  ? 156  PHE B CB  1 
ATOM   5404  C  CG  . PHE B  1 156 ? 2.688   34.135  62.175  1.00 35.61  ? 156  PHE B CG  1 
ATOM   5405  C  CD1 . PHE B  1 156 ? 2.245   34.625  63.391  1.00 34.04  ? 156  PHE B CD1 1 
ATOM   5406  C  CD2 . PHE B  1 156 ? 3.712   33.192  62.162  1.00 36.22  ? 156  PHE B CD2 1 
ATOM   5407  C  CE1 . PHE B  1 156 ? 2.819   34.201  64.570  1.00 33.84  ? 156  PHE B CE1 1 
ATOM   5408  C  CE2 . PHE B  1 156 ? 4.300   32.759  63.346  1.00 33.94  ? 156  PHE B CE2 1 
ATOM   5409  C  CZ  . PHE B  1 156 ? 3.855   33.268  64.551  1.00 35.21  ? 156  PHE B CZ  1 
ATOM   5410  N  N   . GLY B  1 157 ? 0.887   33.446  58.225  1.00 36.78  ? 157  GLY B N   1 
ATOM   5411  C  CA  . GLY B  1 157 ? 0.469   33.566  56.842  1.00 38.35  ? 157  GLY B CA  1 
ATOM   5412  C  C   . GLY B  1 157 ? -0.822  32.852  56.474  1.00 39.54  ? 157  GLY B C   1 
ATOM   5413  O  O   . GLY B  1 157 ? -1.682  33.403  55.794  1.00 42.34  ? 157  GLY B O   1 
ATOM   5414  N  N   . PHE B  1 158 ? -0.927  31.585  56.837  1.00 36.43  ? 158  PHE B N   1 
ATOM   5415  C  CA  . PHE B  1 158 ? -2.064  30.794  56.376  1.00 33.86  ? 158  PHE B CA  1 
ATOM   5416  C  C   . PHE B  1 158 ? -3.176  30.274  57.317  1.00 35.32  ? 158  PHE B C   1 
ATOM   5417  O  O   . PHE B  1 158 ? -4.116  29.630  56.841  1.00 29.04  ? 158  PHE B O   1 
ATOM   5418  C  CB  . PHE B  1 158 ? -1.563  29.754  55.378  1.00 32.04  ? 158  PHE B CB  1 
ATOM   5419  C  CG  . PHE B  1 158 ? -0.591  30.326  54.379  1.00 32.00  ? 158  PHE B CG  1 
ATOM   5420  C  CD1 . PHE B  1 158 ? 0.757   30.384  54.658  1.00 32.66  ? 158  PHE B CD1 1 
ATOM   5421  C  CD2 . PHE B  1 158 ? -1.033  30.832  53.177  1.00 47.01  ? 158  PHE B CD2 1 
ATOM   5422  C  CE1 . PHE B  1 158 ? 1.626   30.917  53.752  1.00 35.34  ? 158  PHE B CE1 1 
ATOM   5423  C  CE2 . PHE B  1 158 ? -0.155  31.357  52.268  1.00 33.76  ? 158  PHE B CE2 1 
ATOM   5424  C  CZ  . PHE B  1 158 ? 1.168   31.401  52.557  1.00 34.39  ? 158  PHE B CZ  1 
ATOM   5425  N  N   . LEU B  1 159 ? -3.068  30.509  58.624  1.00 29.62  ? 159  LEU B N   1 
ATOM   5426  C  CA  . LEU B  1 159 ? -4.105  30.037  59.549  1.00 28.60  ? 159  LEU B CA  1 
ATOM   5427  C  C   . LEU B  1 159 ? -5.404  30.701  59.183  1.00 28.58  ? 159  LEU B C   1 
ATOM   5428  O  O   . LEU B  1 159 ? -5.476  31.912  59.091  1.00 29.41  ? 159  LEU B O   1 
ATOM   5429  C  CB  . LEU B  1 159 ? -3.768  30.356  61.009  1.00 28.63  ? 159  LEU B CB  1 
ATOM   5430  C  CG  . LEU B  1 159 ? -4.764  29.952  62.096  1.00 27.72  ? 159  LEU B CG  1 
ATOM   5431  C  CD1 . LEU B  1 159 ? -4.042  29.571  63.350  1.00 27.58  ? 159  LEU B CD1 1 
ATOM   5432  C  CD2 . LEU B  1 159 ? -5.721  31.055  62.404  1.00 27.98  ? 159  LEU B CD2 1 
ATOM   5433  N  N   . ALA B  1 160 ? -6.443  29.920  58.971  1.00 28.42  ? 160  ALA B N   1 
ATOM   5434  C  CA  . ALA B  1 160 ? -7.689  30.505  58.528  1.00 27.71  ? 160  ALA B CA  1 
ATOM   5435  C  C   . ALA B  1 160 ? -8.844  29.938  59.305  1.00 26.87  ? 160  ALA B C   1 
ATOM   5436  O  O   . ALA B  1 160 ? -8.873  28.755  59.622  1.00 25.85  ? 160  ALA B O   1 
ATOM   5437  C  CB  . ALA B  1 160 ? -7.898  30.255  57.052  1.00 27.86  ? 160  ALA B CB  1 
ATOM   5438  N  N   . LEU B  1 161 ? -9.804  30.798  59.598  1.00 36.82  ? 161  LEU B N   1 
ATOM   5439  C  CA  . LEU B  1 161 ? -11.102 30.359  60.037  1.00 35.84  ? 161  LEU B CA  1 
ATOM   5440  C  C   . LEU B  1 161 ? -12.010 30.843  58.944  1.00 40.92  ? 161  LEU B C   1 
ATOM   5441  O  O   . LEU B  1 161 ? -12.584 31.912  59.062  1.00 45.02  ? 161  LEU B O   1 
ATOM   5442  C  CB  . LEU B  1 161 ? -11.469 31.034  61.336  1.00 26.16  ? 161  LEU B CB  1 
ATOM   5443  C  CG  . LEU B  1 161 ? -10.857 30.397  62.563  1.00 25.68  ? 161  LEU B CG  1 
ATOM   5444  C  CD1 . LEU B  1 161 ? -11.612 30.911  63.737  1.00 41.39  ? 161  LEU B CD1 1 
ATOM   5445  C  CD2 . LEU B  1 161 ? -11.010 28.912  62.479  1.00 24.68  ? 161  LEU B CD2 1 
ATOM   5446  N  N   . PRO B  1 162 ? -12.108 30.071  57.850  1.00 38.33  ? 162  PRO B N   1 
ATOM   5447  C  CA  . PRO B  1 162 ? -12.734 30.531  56.606  1.00 39.41  ? 162  PRO B CA  1 
ATOM   5448  C  C   . PRO B  1 162 ? -14.141 31.056  56.839  1.00 37.23  ? 162  PRO B C   1 
ATOM   5449  O  O   . PRO B  1 162 ? -14.934 30.411  57.516  1.00 31.15  ? 162  PRO B O   1 
ATOM   5450  C  CB  . PRO B  1 162 ? -12.762 29.266  55.748  1.00 47.82  ? 162  PRO B CB  1 
ATOM   5451  C  CG  . PRO B  1 162 ? -11.631 28.453  56.263  1.00 47.09  ? 162  PRO B CG  1 
ATOM   5452  C  CD  . PRO B  1 162 ? -11.646 28.678  57.741  1.00 45.71  ? 162  PRO B CD  1 
ATOM   5453  N  N   . GLY B  1 163 ? -14.426 32.233  56.294  1.00 50.03  ? 163  GLY B N   1 
ATOM   5454  C  CA  . GLY B  1 163 ? -15.706 32.872  56.499  1.00 53.51  ? 163  GLY B CA  1 
ATOM   5455  C  C   . GLY B  1 163 ? -15.617 33.960  57.543  1.00 55.99  ? 163  GLY B C   1 
ATOM   5456  O  O   . GLY B  1 163 ? -16.557 34.725  57.730  1.00 60.55  ? 163  GLY B O   1 
ATOM   5457  N  N   . SER B  1 164 ? -14.479 34.036  58.220  1.00 31.82  ? 164  SER B N   1 
ATOM   5458  C  CA  . SER B  1 164 ? -14.289 35.026  59.274  1.00 33.12  ? 164  SER B CA  1 
ATOM   5459  C  C   . SER B  1 164 ? -13.654 36.286  58.721  1.00 30.40  ? 164  SER B C   1 
ATOM   5460  O  O   . SER B  1 164 ? -12.850 36.239  57.777  1.00 30.70  ? 164  SER B O   1 
ATOM   5461  C  CB  . SER B  1 164 ? -13.414 34.489  60.402  1.00 66.41  ? 164  SER B CB  1 
ATOM   5462  O  OG  . SER B  1 164 ? -12.045 34.754  60.134  1.00 73.01  ? 164  SER B OG  1 
ATOM   5463  N  N   . ARG B  1 165 ? -14.052 37.416  59.298  1.00 38.07  ? 165  ARG B N   1 
ATOM   5464  C  CA  . ARG B  1 165 ? -13.488 38.709  58.938  1.00 45.72  ? 165  ARG B CA  1 
ATOM   5465  C  C   . ARG B  1 165 ? -12.018 38.783  59.326  1.00 42.59  ? 165  ARG B C   1 
ATOM   5466  O  O   . ARG B  1 165 ? -11.213 39.371  58.605  1.00 33.62  ? 165  ARG B O   1 
ATOM   5467  C  CB  . ARG B  1 165 ? -14.237 39.833  59.660  1.00 86.51  ? 165  ARG B CB  1 
ATOM   5468  C  CG  . ARG B  1 165 ? -15.455 40.396  58.948  1.00 95.12  ? 165  ARG B CG  1 
ATOM   5469  C  CD  . ARG B  1 165 ? -15.829 41.764  59.540  1.00 104.27 ? 165  ARG B CD  1 
ATOM   5470  N  NE  . ARG B  1 165 ? -14.878 42.831  59.192  1.00 110.86 ? 165  ARG B NE  1 
ATOM   5471  C  CZ  . ARG B  1 165 ? -13.928 43.311  59.999  1.00 111.17 ? 165  ARG B CZ  1 
ATOM   5472  N  NH1 . ARG B  1 165 ? -13.777 42.829  61.226  1.00 110.29 ? 165  ARG B NH1 1 
ATOM   5473  N  NH2 . ARG B  1 165 ? -13.125 44.280  59.577  1.00 110.63 ? 165  ARG B NH2 1 
ATOM   5474  N  N   . GLU B  1 166 ? -11.705 38.214  60.493  1.00 46.49  ? 166  GLU B N   1 
ATOM   5475  C  CA  . GLU B  1 166 ? -10.404 38.380  61.137  1.00 47.73  ? 166  GLU B CA  1 
ATOM   5476  C  C   . GLU B  1 166 ? -9.356  37.297  60.906  1.00 45.17  ? 166  GLU B C   1 
ATOM   5477  O  O   . GLU B  1 166 ? -8.203  37.452  61.304  1.00 46.43  ? 166  GLU B O   1 
ATOM   5478  C  CB  . GLU B  1 166 ? -10.587 38.621  62.623  1.00 71.65  ? 166  GLU B CB  1 
ATOM   5479  C  CG  . GLU B  1 166 ? -11.155 39.988  62.928  1.00 82.78  ? 166  GLU B CG  1 
ATOM   5480  C  CD  . GLU B  1 166 ? -12.445 39.895  63.708  1.00 91.37  ? 166  GLU B CD  1 
ATOM   5481  O  OE1 . GLU B  1 166 ? -12.813 38.761  64.091  1.00 91.82  ? 166  GLU B OE1 1 
ATOM   5482  O  OE2 . GLU B  1 166 ? -13.085 40.948  63.933  1.00 95.32  ? 166  GLU B OE2 1 
ATOM   5483  N  N   . ALA B  1 167 ? -9.748  36.191  60.295  1.00 46.60  ? 167  ALA B N   1 
ATOM   5484  C  CA  . ALA B  1 167 ? -8.761  35.234  59.817  1.00 44.48  ? 167  ALA B CA  1 
ATOM   5485  C  C   . ALA B  1 167 ? -9.243  34.600  58.514  1.00 44.18  ? 167  ALA B C   1 
ATOM   5486  O  O   . ALA B  1 167 ? -9.665  33.435  58.493  1.00 41.64  ? 167  ALA B O   1 
ATOM   5487  C  CB  . ALA B  1 167 ? -8.476  34.197  60.864  1.00 43.73  ? 167  ALA B CB  1 
ATOM   5488  N  N   . PRO B  1 168 ? -9.189  35.379  57.421  1.00 45.60  ? 168  PRO B N   1 
ATOM   5489  C  CA  . PRO B  1 168 ? -9.763  35.016  56.119  1.00 44.79  ? 168  PRO B CA  1 
ATOM   5490  C  C   . PRO B  1 168 ? -8.974  33.910  55.444  1.00 41.22  ? 168  PRO B C   1 
ATOM   5491  O  O   . PRO B  1 168 ? -9.538  33.149  54.665  1.00 40.40  ? 168  PRO B O   1 
ATOM   5492  C  CB  . PRO B  1 168 ? -9.622  36.302  55.295  1.00 58.94  ? 168  PRO B CB  1 
ATOM   5493  C  CG  . PRO B  1 168 ? -9.049  37.342  56.230  1.00 60.88  ? 168  PRO B CG  1 
ATOM   5494  C  CD  . PRO B  1 168 ? -8.389  36.609  57.337  1.00 57.46  ? 168  PRO B CD  1 
ATOM   5495  N  N   . GLY B  1 169 ? -7.680  33.842  55.739  1.00 34.93  ? 169  GLY B N   1 
ATOM   5496  C  CA  . GLY B  1 169 ? -6.799  32.875  55.117  1.00 34.23  ? 169  GLY B CA  1 
ATOM   5497  C  C   . GLY B  1 169 ? -6.099  33.404  53.884  1.00 34.85  ? 169  GLY B C   1 
ATOM   5498  O  O   . GLY B  1 169 ? -6.492  34.419  53.317  1.00 32.79  ? 169  GLY B O   1 
ATOM   5499  N  N   . ASN B  1 170 ? -5.047  32.699  53.486  1.00 35.43  ? 170  ASN B N   1 
ATOM   5500  C  CA  . ASN B  1 170 ? -4.220  33.054  52.334  1.00 38.10  ? 170  ASN B CA  1 
ATOM   5501  C  C   . ASN B  1 170 ? -3.600  34.439  52.451  1.00 41.38  ? 170  ASN B C   1 
ATOM   5502  O  O   . ASN B  1 170 ? -3.156  35.011  51.454  1.00 35.46  ? 170  ASN B O   1 
ATOM   5503  C  CB  . ASN B  1 170 ? -5.013  32.985  51.024  1.00 33.20  ? 170  ASN B CB  1 
ATOM   5504  C  CG  . ASN B  1 170 ? -5.792  31.712  50.877  1.00 31.94  ? 170  ASN B CG  1 
ATOM   5505  O  OD1 . ASN B  1 170 ? -5.278  30.619  51.102  1.00 31.24  ? 170  ASN B OD1 1 
ATOM   5506  N  ND2 . ASN B  1 170 ? -7.053  31.844  50.490  1.00 34.18  ? 170  ASN B ND2 1 
ATOM   5507  N  N   . VAL B  1 171 ? -3.518  34.966  53.662  1.00 34.34  ? 171  VAL B N   1 
ATOM   5508  C  CA  . VAL B  1 171 ? -3.026  36.323  53.784  1.00 35.62  ? 171  VAL B CA  1 
ATOM   5509  C  C   . VAL B  1 171 ? -1.548  36.396  53.373  1.00 36.54  ? 171  VAL B C   1 
ATOM   5510  O  O   . VAL B  1 171 ? -1.091  37.430  52.914  1.00 37.83  ? 171  VAL B O   1 
ATOM   5511  C  CB  . VAL B  1 171 ? -3.344  36.976  55.173  1.00 35.49  ? 171  VAL B CB  1 
ATOM   5512  C  CG1 . VAL B  1 171 ? -4.756  36.626  55.622  1.00 34.43  ? 171  VAL B CG1 1 
ATOM   5513  C  CG2 . VAL B  1 171 ? -2.338  36.577  56.224  1.00 35.22  ? 171  VAL B CG2 1 
ATOM   5514  N  N   . GLY B  1 172 ? -0.819  35.290  53.485  1.00 35.94  ? 172  GLY B N   1 
ATOM   5515  C  CA  . GLY B  1 172 ? 0.550   35.239  53.000  1.00 36.80  ? 172  GLY B CA  1 
ATOM   5516  C  C   . GLY B  1 172 ? 0.607   35.461  51.495  1.00 40.65  ? 172  GLY B C   1 
ATOM   5517  O  O   . GLY B  1 172 ? 1.516   36.123  50.950  1.00 42.09  ? 172  GLY B O   1 
ATOM   5518  N  N   . LEU B  1 173 ? -0.387  34.914  50.806  1.00 46.89  ? 173  LEU B N   1 
ATOM   5519  C  CA  . LEU B  1 173 ? -0.489  35.100  49.368  1.00 46.57  ? 173  LEU B CA  1 
ATOM   5520  C  C   . LEU B  1 173 ? -0.794  36.560  49.085  1.00 47.75  ? 173  LEU B C   1 
ATOM   5521  O  O   . LEU B  1 173 ? -0.304  37.125  48.117  1.00 49.78  ? 173  LEU B O   1 
ATOM   5522  C  CB  . LEU B  1 173 ? -1.587  34.217  48.780  1.00 36.81  ? 173  LEU B CB  1 
ATOM   5523  C  CG  . LEU B  1 173 ? -1.339  32.719  48.728  1.00 35.76  ? 173  LEU B CG  1 
ATOM   5524  C  CD1 . LEU B  1 173 ? -2.548  32.085  48.115  1.00 34.96  ? 173  LEU B CD1 1 
ATOM   5525  C  CD2 . LEU B  1 173 ? -0.092  32.410  47.924  1.00 36.56  ? 173  LEU B CD2 1 
ATOM   5526  N  N   . LEU B  1 174 ? -1.607  37.166  49.943  1.00 38.73  ? 174  LEU B N   1 
ATOM   5527  C  CA  . LEU B  1 174 ? -1.950  38.564  49.788  1.00 39.90  ? 174  LEU B CA  1 
ATOM   5528  C  C   . LEU B  1 174 ? -0.739  39.453  50.002  1.00 41.19  ? 174  LEU B C   1 
ATOM   5529  O  O   . LEU B  1 174 ? -0.648  40.521  49.417  1.00 42.54  ? 174  LEU B O   1 
ATOM   5530  C  CB  . LEU B  1 174 ? -3.050  38.942  50.761  1.00 43.79  ? 174  LEU B CB  1 
ATOM   5531  C  CG  . LEU B  1 174 ? -4.348  38.203  50.523  1.00 38.14  ? 174  LEU B CG  1 
ATOM   5532  C  CD1 . LEU B  1 174 ? -5.415  38.873  51.315  1.00 37.94  ? 174  LEU B CD1 1 
ATOM   5533  C  CD2 . LEU B  1 174 ? -4.673  38.243  49.065  1.00 38.77  ? 174  LEU B CD2 1 
ATOM   5534  N  N   . ASP B  1 175 ? 0.177   39.015  50.861  1.00 45.83  ? 175  ASP B N   1 
ATOM   5535  C  CA  . ASP B  1 175 ? 1.446   39.705  51.049  1.00 47.38  ? 175  ASP B CA  1 
ATOM   5536  C  C   . ASP B  1 175 ? 2.177   39.653  49.733  1.00 43.02  ? 175  ASP B C   1 
ATOM   5537  O  O   . ASP B  1 175 ? 2.722   40.659  49.279  1.00 44.50  ? 175  ASP B O   1 
ATOM   5538  C  CB  . ASP B  1 175 ? 2.302   39.051  52.141  1.00 41.35  ? 175  ASP B CB  1 
ATOM   5539  C  CG  . ASP B  1 175 ? 1.689   39.187  53.530  1.00 44.76  ? 175  ASP B CG  1 
ATOM   5540  O  OD1 . ASP B  1 175 ? 0.881   40.115  53.746  1.00 46.65  ? 175  ASP B OD1 1 
ATOM   5541  O  OD2 . ASP B  1 175 ? 2.016   38.363  54.411  1.00 41.18  ? 175  ASP B OD2 1 
ATOM   5542  N  N   . GLN B  1 176 ? 2.177   38.481  49.107  1.00 42.29  ? 176  GLN B N   1 
ATOM   5543  C  CA  . GLN B  1 176 ? 2.781   38.389  47.782  1.00 43.27  ? 176  GLN B CA  1 
ATOM   5544  C  C   . GLN B  1 176 ? 2.127   39.351  46.778  1.00 44.37  ? 176  GLN B C   1 
ATOM   5545  O  O   . GLN B  1 176 ? 2.808   40.089  46.058  1.00 45.88  ? 176  GLN B O   1 
ATOM   5546  C  CB  . GLN B  1 176 ? 2.718   36.960  47.256  1.00 42.26  ? 176  GLN B CB  1 
ATOM   5547  C  CG  . GLN B  1 176 ? 3.667   35.995  47.919  1.00 41.62  ? 176  GLN B CG  1 
ATOM   5548  C  CD  . GLN B  1 176 ? 3.336   34.570  47.562  1.00 40.43  ? 176  GLN B CD  1 
ATOM   5549  O  OE1 . GLN B  1 176 ? 2.583   34.323  46.631  1.00 40.29  ? 176  GLN B OE1 1 
ATOM   5550  N  NE2 . GLN B  1 176 ? 3.880   33.623  48.308  1.00 49.87  ? 176  GLN B NE2 1 
ATOM   5551  N  N   . ARG B  1 177 ? 0.802   39.351  46.741  1.00 51.16  ? 177  ARG B N   1 
ATOM   5552  C  CA  . ARG B  1 177 ? 0.078   40.133  45.756  1.00 54.12  ? 177  ARG B CA  1 
ATOM   5553  C  C   . ARG B  1 177 ? 0.366   41.603  45.959  1.00 58.22  ? 177  ARG B C   1 
ATOM   5554  O  O   . ARG B  1 177 ? 0.657   42.313  45.005  1.00 62.19  ? 177  ARG B O   1 
ATOM   5555  C  CB  . ARG B  1 177 ? -1.424  39.865  45.845  1.00 43.57  ? 177  ARG B CB  1 
ATOM   5556  C  CG  . ARG B  1 177 ? -2.257  40.789  44.998  1.00 44.61  ? 177  ARG B CG  1 
ATOM   5557  C  CD  . ARG B  1 177 ? -3.711  40.544  45.219  1.00 43.57  ? 177  ARG B CD  1 
ATOM   5558  N  NE  . ARG B  1 177 ? -4.127  39.289  44.613  1.00 42.53  ? 177  ARG B NE  1 
ATOM   5559  C  CZ  . ARG B  1 177 ? -5.306  38.713  44.843  1.00 41.58  ? 177  ARG B CZ  1 
ATOM   5560  N  NH1 . ARG B  1 177 ? -6.177  39.278  45.679  1.00 41.02  ? 177  ARG B NH1 1 
ATOM   5561  N  NH2 . ARG B  1 177 ? -5.619  37.567  44.249  1.00 40.47  ? 177  ARG B NH2 1 
ATOM   5562  N  N   . LEU B  1 178 ? 0.296   42.052  47.209  1.00 48.74  ? 178  LEU B N   1 
ATOM   5563  C  CA  . LEU B  1 178 ? 0.591   43.444  47.554  1.00 50.02  ? 178  LEU B CA  1 
ATOM   5564  C  C   . LEU B  1 178 ? 2.007   43.832  47.168  1.00 48.47  ? 178  LEU B C   1 
ATOM   5565  O  O   . LEU B  1 178 ? 2.225   44.927  46.671  1.00 50.04  ? 178  LEU B O   1 
ATOM   5566  C  CB  . LEU B  1 178 ? 0.386   43.712  49.042  1.00 46.41  ? 178  LEU B CB  1 
ATOM   5567  C  CG  . LEU B  1 178 ? 0.776   45.122  49.460  1.00 47.82  ? 178  LEU B CG  1 
ATOM   5568  C  CD1 . LEU B  1 178 ? -0.185  46.106  48.849  1.00 48.76  ? 178  LEU B CD1 1 
ATOM   5569  C  CD2 . LEU B  1 178 ? 0.757   45.210  50.948  1.00 47.09  ? 178  LEU B CD2 1 
ATOM   5570  N  N   . ALA B  1 179 ? 2.967   42.939  47.396  1.00 47.95  ? 179  ALA B N   1 
ATOM   5571  C  CA  . ALA B  1 179 ? 4.320   43.181  46.920  1.00 49.25  ? 179  ALA B CA  1 
ATOM   5572  C  C   . ALA B  1 179 ? 4.271   43.406  45.419  1.00 51.99  ? 179  ALA B C   1 
ATOM   5573  O  O   . ALA B  1 179 ? 4.980   44.257  44.887  1.00 54.18  ? 179  ALA B O   1 
ATOM   5574  C  CB  . ALA B  1 179 ? 5.216   42.020  47.249  1.00 48.43  ? 179  ALA B CB  1 
ATOM   5575  N  N   . LEU B  1 180 ? 3.407   42.660  44.739  1.00 65.08  ? 180  LEU B N   1 
ATOM   5576  C  CA  . LEU B  1 180 ? 3.255   42.821  43.294  1.00 66.24  ? 180  LEU B CA  1 
ATOM   5577  C  C   . LEU B  1 180 ? 2.644   44.168  42.879  1.00 68.92  ? 180  LEU B C   1 
ATOM   5578  O  O   . LEU B  1 180 ? 3.076   44.756  41.897  1.00 72.98  ? 180  LEU B O   1 
ATOM   5579  C  CB  . LEU B  1 180 ? 2.469   41.648  42.691  1.00 54.87  ? 180  LEU B CB  1 
ATOM   5580  C  CG  . LEU B  1 180 ? 3.278   40.447  42.192  1.00 50.93  ? 180  LEU B CG  1 
ATOM   5581  C  CD1 . LEU B  1 180 ? 4.484   40.167  43.078  1.00 48.89  ? 180  LEU B CD1 1 
ATOM   5582  C  CD2 . LEU B  1 180 ? 2.381   39.230  42.112  1.00 47.55  ? 180  LEU B CD2 1 
ATOM   5583  N  N   . GLN B  1 181 ? 1.651   44.661  43.615  1.00 51.50  ? 181  GLN B N   1 
ATOM   5584  C  CA  . GLN B  1 181 ? 1.074   45.966  43.295  1.00 52.85  ? 181  GLN B CA  1 
ATOM   5585  C  C   . GLN B  1 181 ? 2.053   47.081  43.605  1.00 56.12  ? 181  GLN B C   1 
ATOM   5586  O  O   . GLN B  1 181 ? 2.059   48.104  42.925  1.00 61.21  ? 181  GLN B O   1 
ATOM   5587  C  CB  . GLN B  1 181 ? -0.220  46.216  44.049  1.00 76.33  ? 181  GLN B CB  1 
ATOM   5588  C  CG  . GLN B  1 181 ? -1.289  45.196  43.780  1.00 82.23  ? 181  GLN B CG  1 
ATOM   5589  C  CD  . GLN B  1 181 ? -2.463  45.364  44.716  1.00 87.01  ? 181  GLN B CD  1 
ATOM   5590  O  OE1 . GLN B  1 181 ? -2.723  46.467  45.194  1.00 91.85  ? 181  GLN B OE1 1 
ATOM   5591  N  NE2 . GLN B  1 181 ? -3.172  44.272  44.997  1.00 84.09  ? 181  GLN B NE2 1 
ATOM   5592  N  N   . TRP B  1 182 ? 2.873   46.897  44.636  1.00 75.41  ? 182  TRP B N   1 
ATOM   5593  C  CA  . TRP B  1 182 ? 3.949   47.843  44.914  1.00 76.92  ? 182  TRP B CA  1 
ATOM   5594  C  C   . TRP B  1 182 ? 4.932   47.814  43.766  1.00 77.10  ? 182  TRP B C   1 
ATOM   5595  O  O   . TRP B  1 182 ? 5.470   48.842  43.401  1.00 80.70  ? 182  TRP B O   1 
ATOM   5596  C  CB  . TRP B  1 182 ? 4.694   47.501  46.204  1.00 70.70  ? 182  TRP B CB  1 
ATOM   5597  C  CG  . TRP B  1 182 ? 5.838   48.441  46.548  1.00 71.13  ? 182  TRP B CG  1 
ATOM   5598  C  CD1 . TRP B  1 182 ? 5.816   49.448  47.473  1.00 71.63  ? 182  TRP B CD1 1 
ATOM   5599  C  CD2 . TRP B  1 182 ? 7.171   48.446  45.987  1.00 71.36  ? 182  TRP B CD2 1 
ATOM   5600  N  NE1 . TRP B  1 182 ? 7.040   50.078  47.522  1.00 72.98  ? 182  TRP B NE1 1 
ATOM   5601  C  CE2 . TRP B  1 182 ? 7.887   49.488  46.618  1.00 70.95  ? 182  TRP B CE2 1 
ATOM   5602  C  CE3 . TRP B  1 182 ? 7.823   47.676  45.012  1.00 69.69  ? 182  TRP B CE3 1 
ATOM   5603  C  CZ2 . TRP B  1 182 ? 9.217   49.782  46.305  1.00 67.89  ? 182  TRP B CZ2 1 
ATOM   5604  C  CZ3 . TRP B  1 182 ? 9.145   47.975  44.702  1.00 68.23  ? 182  TRP B CZ3 1 
ATOM   5605  C  CH2 . TRP B  1 182 ? 9.826   49.015  45.352  1.00 67.41  ? 182  TRP B CH2 1 
ATOM   5606  N  N   . VAL B  1 183 ? 5.199   46.641  43.206  1.00 62.45  ? 183  VAL B N   1 
ATOM   5607  C  CA  . VAL B  1 183 ? 6.118   46.603  42.078  1.00 64.69  ? 183  VAL B CA  1 
ATOM   5608  C  C   . VAL B  1 183 ? 5.475   47.183  40.819  1.00 67.20  ? 183  VAL B C   1 
ATOM   5609  O  O   . VAL B  1 183 ? 6.168   47.668  39.939  1.00 69.32  ? 183  VAL B O   1 
ATOM   5610  C  CB  . VAL B  1 183 ? 6.696   45.197  41.806  1.00 71.14  ? 183  VAL B CB  1 
ATOM   5611  C  CG1 . VAL B  1 183 ? 5.971   44.522  40.659  1.00 70.39  ? 183  VAL B CG1 1 
ATOM   5612  C  CG2 . VAL B  1 183 ? 8.173   45.307  41.485  1.00 72.96  ? 183  VAL B CG2 1 
ATOM   5613  N  N   . GLN B  1 184 ? 4.149   47.158  40.746  1.00 71.02  ? 184  GLN B N   1 
ATOM   5614  C  CA  . GLN B  1 184 ? 3.444   47.706  39.589  1.00 70.17  ? 184  GLN B CA  1 
ATOM   5615  C  C   . GLN B  1 184 ? 3.400   49.237  39.624  1.00 70.08  ? 184  GLN B C   1 
ATOM   5616  O  O   . GLN B  1 184 ? 3.409   49.887  38.572  1.00 68.28  ? 184  GLN B O   1 
ATOM   5617  C  CB  . GLN B  1 184 ? 2.030   47.126  39.495  1.00 61.52  ? 184  GLN B CB  1 
ATOM   5618  C  CG  . GLN B  1 184 ? 1.356   47.297  38.145  1.00 61.49  ? 184  GLN B CG  1 
ATOM   5619  C  CD  . GLN B  1 184 ? 1.908   46.350  37.093  1.00 61.79  ? 184  GLN B CD  1 
ATOM   5620  O  OE1 . GLN B  1 184 ? 3.061   45.921  37.166  1.00 59.93  ? 184  GLN B OE1 1 
ATOM   5621  N  NE2 . GLN B  1 184 ? 1.079   46.013  36.109  1.00 63.15  ? 184  GLN B NE2 1 
ATOM   5622  N  N   . GLU B  1 185 ? 3.318   49.802  40.831  1.00 62.86  ? 185  GLU B N   1 
ATOM   5623  C  CA  . GLU B  1 185 ? 3.412   51.249  41.011  1.00 65.56  ? 185  GLU B CA  1 
ATOM   5624  C  C   . GLU B  1 185 ? 4.846   51.758  40.993  1.00 66.40  ? 185  GLU B C   1 
ATOM   5625  O  O   . GLU B  1 185 ? 5.156   52.708  40.297  1.00 70.32  ? 185  GLU B O   1 
ATOM   5626  C  CB  . GLU B  1 185 ? 2.761   51.677  42.329  1.00 83.61  ? 185  GLU B CB  1 
ATOM   5627  C  CG  . GLU B  1 185 ? 1.249   51.512  42.393  1.00 89.10  ? 185  GLU B CG  1 
ATOM   5628  C  CD  . GLU B  1 185 ? 0.719   51.519  43.824  1.00 94.11  ? 185  GLU B CD  1 
ATOM   5629  O  OE1 . GLU B  1 185 ? 1.527   51.706  44.762  1.00 96.89  ? 185  GLU B OE1 1 
ATOM   5630  O  OE2 . GLU B  1 185 ? -0.504  51.328  44.013  1.00 94.28  ? 185  GLU B OE2 1 
ATOM   5631  N  N   . ASN B  1 186 ? 5.713   51.138  41.781  1.00 62.58  ? 186  ASN B N   1 
ATOM   5632  C  CA  . ASN B  1 186 ? 7.042   51.696  42.050  1.00 63.84  ? 186  ASN B CA  1 
ATOM   5633  C  C   . ASN B  1 186 ? 8.297   51.160  41.333  1.00 64.56  ? 186  ASN B C   1 
ATOM   5634  O  O   . ASN B  1 186 ? 9.391   51.696  41.542  1.00 65.75  ? 186  ASN B O   1 
ATOM   5635  C  CB  . ASN B  1 186 ? 7.292   51.726  43.562  1.00 83.69  ? 186  ASN B CB  1 
ATOM   5636  C  CG  . ASN B  1 186 ? 6.223   52.497  44.308  1.00 86.90  ? 186  ASN B CG  1 
ATOM   5637  O  OD1 . ASN B  1 186 ? 6.223   53.731  44.309  1.00 91.27  ? 186  ASN B OD1 1 
ATOM   5638  N  ND2 . ASN B  1 186 ? 5.299   51.774  44.946  1.00 84.35  ? 186  ASN B ND2 1 
ATOM   5639  N  N   . ILE B  1 187 ? 8.174   50.119  40.510  1.00 83.30  ? 187  ILE B N   1 
ATOM   5640  C  CA  . ILE B  1 187 ? 9.383   49.509  39.941  1.00 83.59  ? 187  ILE B CA  1 
ATOM   5641  C  C   . ILE B  1 187 ? 9.974   50.398  38.854  1.00 85.62  ? 187  ILE B C   1 
ATOM   5642  O  O   . ILE B  1 187 ? 11.186  50.376  38.624  1.00 85.85  ? 187  ILE B O   1 
ATOM   5643  C  CB  . ILE B  1 187 ? 9.161   48.058  39.419  1.00 63.08  ? 187  ILE B CB  1 
ATOM   5644  C  CG1 . ILE B  1 187 ? 10.494  47.334  39.232  1.00 63.35  ? 187  ILE B CG1 1 
ATOM   5645  C  CG2 . ILE B  1 187 ? 8.434   48.055  38.094  1.00 63.73  ? 187  ILE B CG2 1 
ATOM   5646  C  CD1 . ILE B  1 187 ? 11.513  47.631  40.285  1.00 63.53  ? 187  ILE B CD1 1 
ATOM   5647  N  N   . ALA B  1 188 ? 9.110   51.191  38.215  1.00 80.26  ? 188  ALA B N   1 
ATOM   5648  C  CA  . ALA B  1 188 ? 9.492   52.088  37.123  1.00 81.06  ? 188  ALA B CA  1 
ATOM   5649  C  C   . ALA B  1 188 ? 10.704  52.934  37.501  1.00 83.62  ? 188  ALA B C   1 
ATOM   5650  O  O   . ALA B  1 188 ? 11.679  52.995  36.758  1.00 73.19  ? 188  ALA B O   1 
ATOM   5651  C  CB  . ALA B  1 188 ? 8.311   52.977  36.731  1.00 73.60  ? 188  ALA B CB  1 
ATOM   5652  N  N   . ALA B  1 189 ? 10.647  53.534  38.686  1.00 71.35  ? 189  ALA B N   1 
ATOM   5653  C  CA  . ALA B  1 189 ? 11.727  54.366  39.208  1.00 74.97  ? 189  ALA B CA  1 
ATOM   5654  C  C   . ALA B  1 189 ? 13.080  53.638  39.364  1.00 74.96  ? 189  ALA B C   1 
ATOM   5655  O  O   . ALA B  1 189 ? 14.122  54.272  39.566  1.00 74.89  ? 189  ALA B O   1 
ATOM   5656  C  CB  . ALA B  1 189 ? 11.302  54.981  40.534  1.00 72.00  ? 189  ALA B CB  1 
ATOM   5657  N  N   . PHE B  1 190 ? 13.059  52.312  39.299  1.00 72.47  ? 190  PHE B N   1 
ATOM   5658  C  CA  . PHE B  1 190 ? 14.288  51.524  39.351  1.00 73.28  ? 190  PHE B CA  1 
ATOM   5659  C  C   . PHE B  1 190 ? 14.715  51.143  37.952  1.00 74.38  ? 190  PHE B C   1 
ATOM   5660  O  O   . PHE B  1 190 ? 15.693  50.427  37.757  1.00 72.17  ? 190  PHE B O   1 
ATOM   5661  C  CB  . PHE B  1 190 ? 14.094  50.281  40.220  1.00 69.93  ? 190  PHE B CB  1 
ATOM   5662  C  CG  . PHE B  1 190 ? 13.793  50.601  41.651  1.00 71.18  ? 190  PHE B CG  1 
ATOM   5663  C  CD1 . PHE B  1 190 ? 12.507  50.935  42.039  1.00 66.60  ? 190  PHE B CD1 1 
ATOM   5664  C  CD2 . PHE B  1 190 ? 14.803  50.595  42.605  1.00 72.00  ? 190  PHE B CD2 1 
ATOM   5665  C  CE1 . PHE B  1 190 ? 12.231  51.244  43.348  1.00 65.73  ? 190  PHE B CE1 1 
ATOM   5666  C  CE2 . PHE B  1 190 ? 14.534  50.907  43.922  1.00 66.59  ? 190  PHE B CE2 1 
ATOM   5667  C  CZ  . PHE B  1 190 ? 13.247  51.235  44.295  1.00 65.72  ? 190  PHE B CZ  1 
ATOM   5668  N  N   . GLY B  1 191 ? 13.951  51.614  36.977  1.00 82.59  ? 191  GLY B N   1 
ATOM   5669  C  CA  . GLY B  1 191 ? 14.254  51.339  35.592  1.00 86.00  ? 191  GLY B CA  1 
ATOM   5670  C  C   . GLY B  1 191 ? 13.815  49.951  35.193  1.00 86.09  ? 191  GLY B C   1 
ATOM   5671  O  O   . GLY B  1 191 ? 14.348  49.365  34.250  1.00 87.88  ? 191  GLY B O   1 
ATOM   5672  N  N   . GLY B  1 192 ? 12.854  49.414  35.934  1.00 88.68  ? 192  GLY B N   1 
ATOM   5673  C  CA  . GLY B  1 192 ? 12.204  48.178  35.550  1.00 87.34  ? 192  GLY B CA  1 
ATOM   5674  C  C   . GLY B  1 192 ? 10.966  48.495  34.734  1.00 87.17  ? 192  GLY B C   1 
ATOM   5675  O  O   . GLY B  1 192 ? 10.382  49.575  34.876  1.00 87.34  ? 192  GLY B O   1 
ATOM   5676  N  N   . ASP B  1 193 ? 10.568  47.562  33.874  1.00 77.83  ? 193  ASP B N   1 
ATOM   5677  C  CA  . ASP B  1 193 ? 9.376   47.748  33.059  1.00 76.54  ? 193  ASP B CA  1 
ATOM   5678  C  C   . ASP B  1 193 ? 8.176   47.147  33.776  1.00 69.68  ? 193  ASP B C   1 
ATOM   5679  O  O   . ASP B  1 193 ? 8.138   45.943  34.005  1.00 66.20  ? 193  ASP B O   1 
ATOM   5680  C  CB  . ASP B  1 193 ? 9.553   47.092  31.685  1.00 94.18  ? 193  ASP B CB  1 
ATOM   5681  C  CG  . ASP B  1 193 ? 8.470   47.503  30.687  1.00 98.85  ? 193  ASP B CG  1 
ATOM   5682  O  OD1 . ASP B  1 193 ? 7.415   48.022  31.108  1.00 98.35  ? 193  ASP B OD1 1 
ATOM   5683  O  OD2 . ASP B  1 193 ? 8.673   47.301  29.471  1.00 102.34 ? 193  ASP B OD2 1 
ATOM   5684  N  N   . PRO B  1 194 ? 7.198   47.991  34.142  1.00 67.14  ? 194  PRO B N   1 
ATOM   5685  C  CA  . PRO B  1 194 ? 5.930   47.531  34.721  1.00 67.57  ? 194  PRO B CA  1 
ATOM   5686  C  C   . PRO B  1 194 ? 5.119   46.631  33.784  1.00 69.83  ? 194  PRO B C   1 
ATOM   5687  O  O   . PRO B  1 194 ? 4.196   45.961  34.259  1.00 67.30  ? 194  PRO B O   1 
ATOM   5688  C  CB  . PRO B  1 194 ? 5.173   48.835  34.986  1.00 65.42  ? 194  PRO B CB  1 
ATOM   5689  C  CG  . PRO B  1 194 ? 6.238   49.844  35.168  1.00 67.14  ? 194  PRO B CG  1 
ATOM   5690  C  CD  . PRO B  1 194 ? 7.321   49.457  34.203  1.00 68.29  ? 194  PRO B CD  1 
ATOM   5691  N  N   . MET B  1 195 ? 5.428   46.638  32.486  1.00 84.00  ? 195  MET B N   1 
ATOM   5692  C  CA  . MET B  1 195 ? 4.741   45.764  31.524  1.00 85.22  ? 195  MET B CA  1 
ATOM   5693  C  C   . MET B  1 195 ? 5.494   44.469  31.159  1.00 85.59  ? 195  MET B C   1 
ATOM   5694  O  O   . MET B  1 195 ? 4.973   43.628  30.413  1.00 83.45  ? 195  MET B O   1 
ATOM   5695  C  CB  . MET B  1 195 ? 4.330   46.542  30.270  1.00 79.46  ? 195  MET B CB  1 
ATOM   5696  C  CG  . MET B  1 195 ? 3.106   47.436  30.463  1.00 77.62  ? 195  MET B CG  1 
ATOM   5697  S  SD  . MET B  1 195 ? 3.099   48.903  29.391  1.00 138.90 ? 195  MET B SD  1 
ATOM   5698  C  CE  . MET B  1 195 ? 4.711   48.816  28.593  1.00 71.73  ? 195  MET B CE  1 
ATOM   5699  N  N   . SER B  1 196 ? 6.715   44.315  31.669  1.00 87.62  ? 196  SER B N   1 
ATOM   5700  C  CA  . SER B  1 196 ? 7.354   43.002  31.688  1.00 89.32  ? 196  SER B CA  1 
ATOM   5701  C  C   . SER B  1 196 ? 7.595   42.560  33.126  1.00 89.90  ? 196  SER B C   1 
ATOM   5702  O  O   . SER B  1 196 ? 8.521   43.032  33.784  1.00 90.60  ? 196  SER B O   1 
ATOM   5703  C  CB  . SER B  1 196 ? 8.680   43.018  30.926  1.00 87.49  ? 196  SER B CB  1 
ATOM   5704  O  OG  . SER B  1 196 ? 9.328   41.758  31.002  1.00 86.46  ? 196  SER B OG  1 
ATOM   5705  N  N   . VAL B  1 197 ? 6.779   41.620  33.589  1.00 89.40  ? 197  VAL B N   1 
ATOM   5706  C  CA  . VAL B  1 197 ? 6.922   41.062  34.926  1.00 87.21  ? 197  VAL B CA  1 
ATOM   5707  C  C   . VAL B  1 197 ? 6.797   39.546  34.853  1.00 83.88  ? 197  VAL B C   1 
ATOM   5708  O  O   . VAL B  1 197 ? 5.746   38.999  34.494  1.00 80.19  ? 197  VAL B O   1 
ATOM   5709  C  CB  . VAL B  1 197 ? 5.897   41.681  35.928  1.00 65.79  ? 197  VAL B CB  1 
ATOM   5710  C  CG1 . VAL B  1 197 ? 5.486   40.683  36.997  1.00 63.09  ? 197  VAL B CG1 1 
ATOM   5711  C  CG2 . VAL B  1 197 ? 6.471   42.937  36.575  1.00 65.73  ? 197  VAL B CG2 1 
ATOM   5712  N  N   . THR B  1 198 ? 7.889   38.872  35.182  1.00 90.09  ? 198  THR B N   1 
ATOM   5713  C  CA  . THR B  1 198 ? 7.887   37.423  35.200  1.00 89.70  ? 198  THR B CA  1 
ATOM   5714  C  C   . THR B  1 198 ? 8.101   36.878  36.608  1.00 90.46  ? 198  THR B C   1 
ATOM   5715  O  O   . THR B  1 198 ? 9.195   36.989  37.168  1.00 92.26  ? 198  THR B O   1 
ATOM   5716  C  CB  . THR B  1 198 ? 8.935   36.863  34.241  1.00 73.58  ? 198  THR B CB  1 
ATOM   5717  O  OG1 . THR B  1 198 ? 8.549   37.186  32.902  1.00 74.91  ? 198  THR B OG1 1 
ATOM   5718  C  CG2 . THR B  1 198 ? 9.039   35.349  34.379  1.00 70.27  ? 198  THR B CG2 1 
ATOM   5719  N  N   . LEU B  1 199 ? 7.048   36.283  37.171  1.00 67.38  ? 199  LEU B N   1 
ATOM   5720  C  CA  . LEU B  1 199 ? 7.127   35.696  38.506  1.00 62.45  ? 199  LEU B CA  1 
ATOM   5721  C  C   . LEU B  1 199 ? 7.812   34.355  38.428  1.00 60.84  ? 199  LEU B C   1 
ATOM   5722  O  O   . LEU B  1 199 ? 7.372   33.491  37.688  1.00 48.77  ? 199  LEU B O   1 
ATOM   5723  C  CB  . LEU B  1 199 ? 5.732   35.444  39.051  1.00 48.21  ? 199  LEU B CB  1 
ATOM   5724  C  CG  . LEU B  1 199 ? 4.776   36.616  39.087  1.00 48.62  ? 199  LEU B CG  1 
ATOM   5725  C  CD1 . LEU B  1 199 ? 3.389   36.106  39.390  1.00 62.11  ? 199  LEU B CD1 1 
ATOM   5726  C  CD2 . LEU B  1 199 ? 5.226   37.589  40.143  1.00 49.01  ? 199  LEU B CD2 1 
ATOM   5727  N  N   . PHE B  1 200 ? 8.879   34.159  39.185  1.00 49.22  ? 200  PHE B N   1 
ATOM   5728  C  CA  . PHE B  1 200 ? 9.418   32.816  39.296  1.00 48.95  ? 200  PHE B CA  1 
ATOM   5729  C  C   . PHE B  1 200 ? 9.576   32.342  40.738  1.00 47.12  ? 200  PHE B C   1 
ATOM   5730  O  O   . PHE B  1 200 ? 9.978   33.095  41.619  1.00 47.40  ? 200  PHE B O   1 
ATOM   5731  C  CB  . PHE B  1 200 ? 10.690  32.620  38.464  1.00 50.14  ? 200  PHE B CB  1 
ATOM   5732  C  CG  . PHE B  1 200 ? 11.921  33.229  39.046  1.00 51.12  ? 200  PHE B CG  1 
ATOM   5733  C  CD1 . PHE B  1 200 ? 11.934  34.542  39.485  1.00 51.71  ? 200  PHE B CD1 1 
ATOM   5734  C  CD2 . PHE B  1 200 ? 13.096  32.487  39.113  1.00 51.58  ? 200  PHE B CD2 1 
ATOM   5735  C  CE1 . PHE B  1 200 ? 13.095  35.104  40.003  1.00 52.70  ? 200  PHE B CE1 1 
ATOM   5736  C  CE2 . PHE B  1 200 ? 14.269  33.040  39.626  1.00 52.58  ? 200  PHE B CE2 1 
ATOM   5737  C  CZ  . PHE B  1 200 ? 14.269  34.349  40.074  1.00 53.13  ? 200  PHE B CZ  1 
ATOM   5738  N  N   . GLY B  1 201 ? 9.233   31.082  40.974  1.00 51.44  ? 201  GLY B N   1 
ATOM   5739  C  CA  . GLY B  1 201 ? 9.311   30.548  42.317  1.00 51.28  ? 201  GLY B CA  1 
ATOM   5740  C  C   . GLY B  1 201 ? 9.689   29.087  42.361  1.00 51.00  ? 201  GLY B C   1 
ATOM   5741  O  O   . GLY B  1 201 ? 9.626   28.361  41.369  1.00 51.75  ? 201  GLY B O   1 
ATOM   5742  N  N   . GLU B  1 202 ? 10.099  28.648  43.536  1.00 43.07  ? 202  GLU B N   1 
ATOM   5743  C  CA  . GLU B  1 202 ? 10.471  27.270  43.699  1.00 42.49  ? 202  GLU B CA  1 
ATOM   5744  C  C   . GLU B  1 202 ? 9.688   26.641  44.850  1.00 42.57  ? 202  GLU B C   1 
ATOM   5745  O  O   . GLU B  1 202 ? 9.385   27.310  45.836  1.00 40.17  ? 202  GLU B O   1 
ATOM   5746  C  CB  . GLU B  1 202 ? 11.973  27.149  43.904  1.00 43.59  ? 202  GLU B CB  1 
ATOM   5747  C  CG  . GLU B  1 202 ? 12.487  25.738  43.708  1.00 49.07  ? 202  GLU B CG  1 
ATOM   5748  C  CD  . GLU B  1 202 ? 12.496  24.939  44.995  1.00 45.28  ? 202  GLU B CD  1 
ATOM   5749  O  OE1 . GLU B  1 202 ? 12.355  25.561  46.068  1.00 44.16  ? 202  GLU B OE1 1 
ATOM   5750  O  OE2 . GLU B  1 202 ? 12.645  23.699  44.936  1.00 43.72  ? 202  GLU B OE2 1 
ATOM   5751  N  N   . SER B  1 203 ? 9.343   25.361  44.684  1.00 49.57  ? 203  SER B N   1 
ATOM   5752  C  CA  . SER B  1 203 ? 8.622   24.585  45.687  1.00 44.59  ? 203  SER B CA  1 
ATOM   5753  C  C   . SER B  1 203 ? 7.288   25.230  46.050  1.00 43.32  ? 203  SER B C   1 
ATOM   5754  O  O   . SER B  1 203 ? 6.430   25.416  45.190  1.00 42.57  ? 203  SER B O   1 
ATOM   5755  C  CB  . SER B  1 203 ? 9.488   24.386  46.933  1.00 43.10  ? 203  SER B CB  1 
ATOM   5756  O  OG  . SER B  1 203 ? 9.022   23.299  47.709  1.00 42.18  ? 203  SER B OG  1 
ATOM   5757  N  N   . ALA B  1 204 ? 7.117   25.552  47.329  1.00 38.56  ? 204  ALA B N   1 
ATOM   5758  C  CA  . ALA B  1 204 ? 5.955   26.303  47.786  1.00 36.01  ? 204  ALA B CA  1 
ATOM   5759  C  C   . ALA B  1 204 ? 5.840   27.610  47.018  1.00 40.20  ? 204  ALA B C   1 
ATOM   5760  O  O   . ALA B  1 204 ? 4.739   28.066  46.715  1.00 36.88  ? 204  ALA B O   1 
ATOM   5761  C  CB  . ALA B  1 204 ? 6.061   26.582  49.261  1.00 35.57  ? 204  ALA B CB  1 
ATOM   5762  N  N   . GLY B  1 205 ? 6.989   28.211  46.714  1.00 47.63  ? 205  GLY B N   1 
ATOM   5763  C  CA  . GLY B  1 205 ? 7.038   29.413  45.903  1.00 47.73  ? 205  GLY B CA  1 
ATOM   5764  C  C   . GLY B  1 205 ? 6.394   29.186  44.553  1.00 47.10  ? 205  GLY B C   1 
ATOM   5765  O  O   . GLY B  1 205 ? 5.530   29.953  44.137  1.00 46.04  ? 205  GLY B O   1 
ATOM   5766  N  N   . ALA B  1 206 ? 6.816   28.124  43.872  1.00 41.47  ? 206  ALA B N   1 
ATOM   5767  C  CA  . ALA B  1 206 ? 6.231   27.736  42.595  1.00 42.39  ? 206  ALA B CA  1 
ATOM   5768  C  C   . ALA B  1 206 ? 4.721   27.624  42.729  1.00 38.79  ? 206  ALA B C   1 
ATOM   5769  O  O   . ALA B  1 206 ? 3.954   28.144  41.908  1.00 39.15  ? 206  ALA B O   1 
ATOM   5770  C  CB  . ALA B  1 206 ? 6.817   26.409  42.139  1.00 40.11  ? 206  ALA B CB  1 
ATOM   5771  N  N   . ALA B  1 207 ? 4.306   26.952  43.795  1.00 37.42  ? 207  ALA B N   1 
ATOM   5772  C  CA  . ALA B  1 207 ? 2.900   26.758  44.073  1.00 38.75  ? 207  ALA B CA  1 
ATOM   5773  C  C   . ALA B  1 207 ? 2.211   28.107  44.203  1.00 38.35  ? 207  ALA B C   1 
ATOM   5774  O  O   . ALA B  1 207 ? 1.046   28.258  43.839  1.00 37.04  ? 207  ALA B O   1 
ATOM   5775  C  CB  . ALA B  1 207 ? 2.726   25.947  45.338  1.00 34.88  ? 207  ALA B CB  1 
ATOM   5776  N  N   . SER B  1 208 ? 2.939   29.091  44.713  1.00 47.00  ? 208  SER B N   1 
ATOM   5777  C  CA  . SER B  1 208 ? 2.373   30.415  44.891  1.00 48.39  ? 208  SER B CA  1 
ATOM   5778  C  C   . SER B  1 208 ? 2.262   31.097  43.533  1.00 50.18  ? 208  SER B C   1 
ATOM   5779  O  O   . SER B  1 208 ? 1.331   31.850  43.275  1.00 51.58  ? 208  SER B O   1 
ATOM   5780  C  CB  . SER B  1 208 ? 3.237   31.241  45.843  1.00 38.68  ? 208  SER B CB  1 
ATOM   5781  O  OG  . SER B  1 208 ? 3.792   30.427  46.855  1.00 37.87  ? 208  SER B OG  1 
ATOM   5782  N  N   . VAL B  1 209 ? 3.222   30.826  42.662  1.00 40.23  ? 209  VAL B N   1 
ATOM   5783  C  CA  . VAL B  1 209 ? 3.227   31.420  41.340  1.00 41.55  ? 209  VAL B CA  1 
ATOM   5784  C  C   . VAL B  1 209 ? 1.987   30.963  40.590  1.00 40.92  ? 209  VAL B C   1 
ATOM   5785  O  O   . VAL B  1 209 ? 1.194   31.782  40.099  1.00 41.44  ? 209  VAL B O   1 
ATOM   5786  C  CB  . VAL B  1 209 ? 4.475   30.990  40.573  1.00 50.25  ? 209  VAL B CB  1 
ATOM   5787  C  CG1 . VAL B  1 209 ? 4.348   31.373  39.127  1.00 51.73  ? 209  VAL B CG1 1 
ATOM   5788  C  CG2 . VAL B  1 209 ? 5.724   31.600  41.206  1.00 51.18  ? 209  VAL B CG2 1 
ATOM   5789  N  N   . GLY B  1 210 ? 1.813   29.645  40.532  1.00 39.81  ? 210  GLY B N   1 
ATOM   5790  C  CA  . GLY B  1 210 ? 0.625   29.065  39.938  1.00 39.04  ? 210  GLY B CA  1 
ATOM   5791  C  C   . GLY B  1 210 ? -0.627  29.533  40.659  1.00 43.88  ? 210  GLY B C   1 
ATOM   5792  O  O   . GLY B  1 210 ? -1.713  29.641  40.071  1.00 38.08  ? 210  GLY B O   1 
ATOM   5793  N  N   . MET B  1 211 ? -0.467  29.826  41.944  1.00 37.71  ? 211  MET B N   1 
ATOM   5794  C  CA  . MET B  1 211 ? -1.570  30.284  42.761  1.00 36.97  ? 211  MET B CA  1 
ATOM   5795  C  C   . MET B  1 211 ? -2.031  31.660  42.273  1.00 41.23  ? 211  MET B C   1 
ATOM   5796  O  O   . MET B  1 211 ? -3.220  31.960  42.265  1.00 42.44  ? 211  MET B O   1 
ATOM   5797  C  CB  . MET B  1 211 ? -1.156  30.326  44.224  1.00 36.36  ? 211  MET B CB  1 
ATOM   5798  C  CG  . MET B  1 211 ? -2.276  30.097  45.194  1.00 35.07  ? 211  MET B CG  1 
ATOM   5799  S  SD  . MET B  1 211 ? -2.658  28.355  45.488  1.00 37.54  ? 211  MET B SD  1 
ATOM   5800  C  CE  . MET B  1 211 ? -1.169  27.717  46.260  1.00 33.34  ? 211  MET B CE  1 
ATOM   5801  N  N   . HIS B  1 212 ? -1.095  32.498  41.846  1.00 43.79  ? 212  HIS B N   1 
ATOM   5802  C  CA  . HIS B  1 212 ? -1.471  33.806  41.319  1.00 47.52  ? 212  HIS B CA  1 
ATOM   5803  C  C   . HIS B  1 212 ? -2.092  33.631  39.950  1.00 46.27  ? 212  HIS B C   1 
ATOM   5804  O  O   . HIS B  1 212 ? -3.118  34.244  39.658  1.00 46.37  ? 212  HIS B O   1 
ATOM   5805  C  CB  . HIS B  1 212 ? -0.272  34.763  41.259  1.00 46.30  ? 212  HIS B CB  1 
ATOM   5806  C  CG  . HIS B  1 212 ? 0.216   35.196  42.607  1.00 48.84  ? 212  HIS B CG  1 
ATOM   5807  N  ND1 . HIS B  1 212 ? -0.580  35.886  43.498  1.00 49.22  ? 212  HIS B ND1 1 
ATOM   5808  C  CD2 . HIS B  1 212 ? 1.408   35.020  43.221  1.00 42.24  ? 212  HIS B CD2 1 
ATOM   5809  C  CE1 . HIS B  1 212 ? 0.102   36.116  44.604  1.00 41.62  ? 212  HIS B CE1 1 
ATOM   5810  N  NE2 . HIS B  1 212 ? 1.311   35.602  44.460  1.00 41.92  ? 212  HIS B NE2 1 
ATOM   5811  N  N   . ILE B  1 213 ? -1.469  32.778  39.132  1.00 41.47  ? 213  ILE B N   1 
ATOM   5812  C  CA  . ILE B  1 213 ? -2.000  32.430  37.812  1.00 42.69  ? 213  ILE B CA  1 
ATOM   5813  C  C   . ILE B  1 213 ? -3.484  32.073  37.904  1.00 43.13  ? 213  ILE B C   1 
ATOM   5814  O  O   . ILE B  1 213 ? -4.295  32.450  37.049  1.00 41.26  ? 213  ILE B O   1 
ATOM   5815  C  CB  . ILE B  1 213 ? -1.244  31.228  37.205  1.00 41.66  ? 213  ILE B CB  1 
ATOM   5816  C  CG1 . ILE B  1 213 ? 0.194   31.602  36.864  1.00 43.06  ? 213  ILE B CG1 1 
ATOM   5817  C  CG2 . ILE B  1 213 ? -1.959  30.712  35.982  1.00 41.82  ? 213  ILE B CG2 1 
ATOM   5818  C  CD1 . ILE B  1 213 ? 1.017   30.442  36.376  1.00 43.14  ? 213  ILE B CD1 1 
ATOM   5819  N  N   . LEU B  1 214 ? -3.845  31.354  38.959  1.00 39.15  ? 214  LEU B N   1 
ATOM   5820  C  CA  . LEU B  1 214 ? -5.219  30.898  39.078  1.00 45.28  ? 214  LEU B CA  1 
ATOM   5821  C  C   . LEU B  1 214 ? -6.148  31.916  39.717  1.00 44.78  ? 214  LEU B C   1 
ATOM   5822  O  O   . LEU B  1 214 ? -7.369  31.786  39.620  1.00 43.26  ? 214  LEU B O   1 
ATOM   5823  C  CB  . LEU B  1 214 ? -5.293  29.565  39.816  1.00 36.39  ? 214  LEU B CB  1 
ATOM   5824  C  CG  . LEU B  1 214 ? -5.245  28.328  38.927  1.00 36.01  ? 214  LEU B CG  1 
ATOM   5825  C  CD1 . LEU B  1 214 ? -3.927  28.221  38.203  1.00 37.06  ? 214  LEU B CD1 1 
ATOM   5826  C  CD2 . LEU B  1 214 ? -5.422  27.138  39.787  1.00 42.78  ? 214  LEU B CD2 1 
ATOM   5827  N  N   . SER B  1 215 ? -5.579  32.930  40.361  1.00 54.52  ? 215  SER B N   1 
ATOM   5828  C  CA  . SER B  1 215 ? -6.387  33.903  41.095  1.00 58.81  ? 215  SER B CA  1 
ATOM   5829  C  C   . SER B  1 215 ? -6.647  35.134  40.246  1.00 64.09  ? 215  SER B C   1 
ATOM   5830  O  O   . SER B  1 215 ? -5.709  35.730  39.708  1.00 66.28  ? 215  SER B O   1 
ATOM   5831  C  CB  . SER B  1 215 ? -5.689  34.306  42.389  1.00 61.28  ? 215  SER B CB  1 
ATOM   5832  O  OG  . SER B  1 215 ? -6.555  35.060  43.216  1.00 61.21  ? 215  SER B OG  1 
ATOM   5833  N  N   . LEU B  1 216 ? -7.912  35.529  40.130  1.00 70.59  ? 216  LEU B N   1 
ATOM   5834  C  CA  . LEU B  1 216 ? -8.257  36.553  39.143  1.00 73.60  ? 216  LEU B CA  1 
ATOM   5835  C  C   . LEU B  1 216 ? -7.579  37.924  39.349  1.00 71.12  ? 216  LEU B C   1 
ATOM   5836  O  O   . LEU B  1 216 ? -6.901  38.408  38.441  1.00 70.98  ? 216  LEU B O   1 
ATOM   5837  C  CB  . LEU B  1 216 ? -9.778  36.669  38.926  1.00 74.44  ? 216  LEU B CB  1 
ATOM   5838  C  CG  . LEU B  1 216 ? -10.181 37.080  37.500  1.00 77.31  ? 216  LEU B CG  1 
ATOM   5839  C  CD1 . LEU B  1 216 ? -10.076 38.593  37.245  1.00 78.59  ? 216  LEU B CD1 1 
ATOM   5840  C  CD2 . LEU B  1 216 ? -9.338  36.315  36.479  1.00 77.92  ? 216  LEU B CD2 1 
ATOM   5841  N  N   . PRO B  1 217 ? -7.749  38.549  40.532  1.00 63.12  ? 217  PRO B N   1 
ATOM   5842  C  CA  . PRO B  1 217 ? -7.110  39.859  40.707  1.00 63.12  ? 217  PRO B CA  1 
ATOM   5843  C  C   . PRO B  1 217 ? -5.587  39.844  40.552  1.00 65.61  ? 217  PRO B C   1 
ATOM   5844  O  O   . PRO B  1 217 ? -4.975  40.883  40.294  1.00 68.61  ? 217  PRO B O   1 
ATOM   5845  C  CB  . PRO B  1 217 ? -7.502  40.244  42.137  1.00 45.15  ? 217  PRO B CB  1 
ATOM   5846  C  CG  . PRO B  1 217 ? -8.793  39.560  42.353  1.00 43.26  ? 217  PRO B CG  1 
ATOM   5847  C  CD  . PRO B  1 217 ? -8.645  38.234  41.661  1.00 44.53  ? 217  PRO B CD  1 
ATOM   5848  N  N   . SER B  1 218 ? -4.976  38.678  40.696  1.00 59.99  ? 218  SER B N   1 
ATOM   5849  C  CA  . SER B  1 218 ? -3.532  38.602  40.561  1.00 60.81  ? 218  SER B CA  1 
ATOM   5850  C  C   . SER B  1 218 ? -3.131  38.736  39.093  1.00 63.35  ? 218  SER B C   1 
ATOM   5851  O  O   . SER B  1 218 ? -2.040  39.226  38.784  1.00 62.09  ? 218  SER B O   1 
ATOM   5852  C  CB  . SER B  1 218 ? -2.986  37.314  41.197  1.00 55.41  ? 218  SER B CB  1 
ATOM   5853  O  OG  . SER B  1 218 ? -2.845  37.459  42.610  1.00 52.88  ? 218  SER B OG  1 
ATOM   5854  N  N   . ARG B  1 219 ? -4.048  38.339  38.207  1.00 75.57  ? 219  ARG B N   1 
ATOM   5855  C  CA  . ARG B  1 219 ? -3.800  38.234  36.765  1.00 80.87  ? 219  ARG B CA  1 
ATOM   5856  C  C   . ARG B  1 219 ? -3.210  39.478  36.091  1.00 83.94  ? 219  ARG B C   1 
ATOM   5857  O  O   . ARG B  1 219 ? -2.367  39.370  35.193  1.00 86.34  ? 219  ARG B O   1 
ATOM   5858  C  CB  . ARG B  1 219 ? -5.081  37.833  36.024  1.00 77.54  ? 219  ARG B CB  1 
ATOM   5859  C  CG  . ARG B  1 219 ? -5.487  36.364  36.142  1.00 78.89  ? 219  ARG B CG  1 
ATOM   5860  C  CD  . ARG B  1 219 ? -4.314  35.376  35.948  1.00 81.48  ? 219  ARG B CD  1 
ATOM   5861  N  NE  . ARG B  1 219 ? -3.471  35.596  34.764  1.00 81.46  ? 219  ARG B NE  1 
ATOM   5862  C  CZ  . ARG B  1 219 ? -3.519  34.873  33.645  1.00 77.14  ? 219  ARG B CZ  1 
ATOM   5863  N  NH1 . ARG B  1 219 ? -4.391  33.873  33.518  1.00 71.29  ? 219  ARG B NH1 1 
ATOM   5864  N  NH2 . ARG B  1 219 ? -2.694  35.163  32.646  1.00 78.05  ? 219  ARG B NH2 1 
ATOM   5865  N  N   . SER B  1 220 ? -3.655  40.654  36.521  1.00 72.91  ? 220  SER B N   1 
ATOM   5866  C  CA  . SER B  1 220 ? -3.225  41.900  35.893  1.00 70.78  ? 220  SER B CA  1 
ATOM   5867  C  C   . SER B  1 220 ? -1.864  42.388  36.400  1.00 69.42  ? 220  SER B C   1 
ATOM   5868  O  O   . SER B  1 220 ? -1.361  43.417  35.953  1.00 70.18  ? 220  SER B O   1 
ATOM   5869  C  CB  . SER B  1 220 ? -4.274  42.991  36.121  1.00 69.89  ? 220  SER B CB  1 
ATOM   5870  O  OG  . SER B  1 220 ? -4.268  43.437  37.469  1.00 68.58  ? 220  SER B OG  1 
ATOM   5871  N  N   . LEU B  1 221 ? -1.284  41.668  37.353  1.00 70.62  ? 221  LEU B N   1 
ATOM   5872  C  CA  . LEU B  1 221 ? -0.041  42.112  37.977  1.00 68.11  ? 221  LEU B CA  1 
ATOM   5873  C  C   . LEU B  1 221 ? 1.195   41.444  37.391  1.00 63.73  ? 221  LEU B C   1 
ATOM   5874  O  O   . LEU B  1 221 ? 2.316   41.723  37.809  1.00 62.63  ? 221  LEU B O   1 
ATOM   5875  C  CB  . LEU B  1 221 ? -0.106  41.911  39.494  1.00 64.93  ? 221  LEU B CB  1 
ATOM   5876  C  CG  . LEU B  1 221 ? -1.276  42.633  40.164  1.00 62.29  ? 221  LEU B CG  1 
ATOM   5877  C  CD1 . LEU B  1 221 ? -1.391  42.240  41.612  1.00 60.25  ? 221  LEU B CD1 1 
ATOM   5878  C  CD2 . LEU B  1 221 ? -1.094  44.129  40.034  1.00 63.68  ? 221  LEU B CD2 1 
ATOM   5879  N  N   . PHE B  1 222 ? 0.997   40.553  36.430  1.00 54.66  ? 222  PHE B N   1 
ATOM   5880  C  CA  . PHE B  1 222 ? 2.136   39.868  35.832  1.00 60.48  ? 222  PHE B CA  1 
ATOM   5881  C  C   . PHE B  1 222 ? 1.869   39.382  34.416  1.00 60.46  ? 222  PHE B C   1 
ATOM   5882  O  O   . PHE B  1 222 ? 0.757   39.514  33.891  1.00 60.69  ? 222  PHE B O   1 
ATOM   5883  C  CB  . PHE B  1 222 ? 2.626   38.707  36.717  1.00 81.48  ? 222  PHE B CB  1 
ATOM   5884  C  CG  . PHE B  1 222 ? 1.647   37.564  36.847  1.00 81.98  ? 222  PHE B CG  1 
ATOM   5885  C  CD1 . PHE B  1 222 ? 0.537   37.670  37.671  1.00 81.34  ? 222  PHE B CD1 1 
ATOM   5886  C  CD2 . PHE B  1 222 ? 1.865   36.372  36.177  1.00 80.58  ? 222  PHE B CD2 1 
ATOM   5887  C  CE1 . PHE B  1 222 ? -0.348  36.626  37.797  1.00 80.70  ? 222  PHE B CE1 1 
ATOM   5888  C  CE2 . PHE B  1 222 ? 0.981   35.330  36.300  1.00 80.24  ? 222  PHE B CE2 1 
ATOM   5889  C  CZ  . PHE B  1 222 ? -0.127  35.455  37.110  1.00 80.26  ? 222  PHE B CZ  1 
ATOM   5890  N  N   . HIS B  1 223 ? 2.908   38.810  33.812  1.00 57.31  ? 223  HIS B N   1 
ATOM   5891  C  CA  . HIS B  1 223 ? 2.906   38.471  32.393  1.00 60.18  ? 223  HIS B CA  1 
ATOM   5892  C  C   . HIS B  1 223 ? 3.346   37.023  32.100  1.00 57.80  ? 223  HIS B C   1 
ATOM   5893  O  O   . HIS B  1 223 ? 2.625   36.262  31.451  1.00 53.63  ? 223  HIS B O   1 
ATOM   5894  C  CB  . HIS B  1 223 ? 3.686   39.530  31.609  1.00 84.02  ? 223  HIS B CB  1 
ATOM   5895  C  CG  . HIS B  1 223 ? 3.214   40.931  31.871  1.00 86.21  ? 223  HIS B CG  1 
ATOM   5896  N  ND1 . HIS B  1 223 ? 3.906   41.816  32.670  1.00 85.15  ? 223  HIS B ND1 1 
ATOM   5897  C  CD2 . HIS B  1 223 ? 2.100   41.588  31.463  1.00 86.19  ? 223  HIS B CD2 1 
ATOM   5898  C  CE1 . HIS B  1 223 ? 3.245   42.958  32.735  1.00 84.80  ? 223  HIS B CE1 1 
ATOM   5899  N  NE2 . HIS B  1 223 ? 2.150   42.849  32.007  1.00 85.13  ? 223  HIS B NE2 1 
ATOM   5900  N  N   . ARG B  1 224 ? 4.552   36.670  32.533  1.00 67.80  ? 224  ARG B N   1 
ATOM   5901  C  CA  . ARG B  1 224 ? 5.043   35.300  32.410  1.00 67.89  ? 224  ARG B CA  1 
ATOM   5902  C  C   . ARG B  1 224 ? 5.323   34.652  33.779  1.00 67.72  ? 224  ARG B C   1 
ATOM   5903  O  O   . ARG B  1 224 ? 5.437   35.345  34.805  1.00 68.91  ? 224  ARG B O   1 
ATOM   5904  C  CB  . ARG B  1 224 ? 6.288   35.278  31.527  1.00 72.26  ? 224  ARG B CB  1 
ATOM   5905  C  CG  . ARG B  1 224 ? 5.991   35.672  30.089  1.00 77.90  ? 224  ARG B CG  1 
ATOM   5906  C  CD  . ARG B  1 224 ? 7.164   36.387  29.415  1.00 84.41  ? 224  ARG B CD  1 
ATOM   5907  N  NE  . ARG B  1 224 ? 7.160   37.836  29.628  1.00 87.19  ? 224  ARG B NE  1 
ATOM   5908  C  CZ  . ARG B  1 224 ? 6.391   38.695  28.960  1.00 87.05  ? 224  ARG B CZ  1 
ATOM   5909  N  NH1 . ARG B  1 224 ? 5.544   38.255  28.035  1.00 86.04  ? 224  ARG B NH1 1 
ATOM   5910  N  NH2 . ARG B  1 224 ? 6.460   39.996  29.227  1.00 86.95  ? 224  ARG B NH2 1 
ATOM   5911  N  N   . ALA B  1 225 ? 5.391   33.323  33.817  1.00 65.86  ? 225  ALA B N   1 
ATOM   5912  C  CA  . ALA B  1 225 ? 5.702   32.669  35.090  1.00 62.66  ? 225  ALA B CA  1 
ATOM   5913  C  C   . ALA B  1 225 ? 6.537   31.365  35.050  1.00 59.32  ? 225  ALA B C   1 
ATOM   5914  O  O   . ALA B  1 225 ? 6.260   30.451  34.266  1.00 60.02  ? 225  ALA B O   1 
ATOM   5915  C  CB  . ALA B  1 225 ? 4.425   32.465  35.866  1.00 66.73  ? 225  ALA B CB  1 
ATOM   5916  N  N   . VAL B  1 226 ? 7.536   31.277  35.926  1.00 53.22  ? 226  VAL B N   1 
ATOM   5917  C  CA  . VAL B  1 226 ? 8.360   30.074  36.070  1.00 54.19  ? 226  VAL B CA  1 
ATOM   5918  C  C   . VAL B  1 226 ? 8.056   29.281  37.360  1.00 55.77  ? 226  VAL B C   1 
ATOM   5919  O  O   . VAL B  1 226 ? 8.140   29.813  38.478  1.00 58.59  ? 226  VAL B O   1 
ATOM   5920  C  CB  . VAL B  1 226 ? 9.861   30.418  36.035  1.00 50.08  ? 226  VAL B CB  1 
ATOM   5921  C  CG1 . VAL B  1 226 ? 10.702  29.168  36.127  1.00 49.90  ? 226  VAL B CG1 1 
ATOM   5922  C  CG2 . VAL B  1 226 ? 10.191  31.193  34.793  1.00 52.05  ? 226  VAL B CG2 1 
ATOM   5923  N  N   . LEU B  1 227 ? 7.712   28.005  37.196  1.00 55.20  ? 227  LEU B N   1 
ATOM   5924  C  CA  . LEU B  1 227 ? 7.415   27.121  38.321  1.00 53.65  ? 227  LEU B CA  1 
ATOM   5925  C  C   . LEU B  1 227 ? 8.452   26.021  38.453  1.00 44.09  ? 227  LEU B C   1 
ATOM   5926  O  O   . LEU B  1 227 ? 8.536   25.087  37.635  1.00 44.33  ? 227  LEU B O   1 
ATOM   5927  C  CB  . LEU B  1 227 ? 6.029   26.511  38.184  1.00 42.63  ? 227  LEU B CB  1 
ATOM   5928  C  CG  . LEU B  1 227 ? 4.900   27.525  38.267  1.00 42.31  ? 227  LEU B CG  1 
ATOM   5929  C  CD1 . LEU B  1 227 ? 4.552   28.077  36.908  1.00 43.55  ? 227  LEU B CD1 1 
ATOM   5930  C  CD2 . LEU B  1 227 ? 3.704   26.867  38.884  1.00 53.55  ? 227  LEU B CD2 1 
ATOM   5931  N  N   . GLN B  1 228 ? 9.240   26.128  39.505  1.00 43.95  ? 228  GLN B N   1 
ATOM   5932  C  CA  . GLN B  1 228 ? 10.331  25.207  39.687  1.00 55.81  ? 228  GLN B CA  1 
ATOM   5933  C  C   . GLN B  1 228 ? 10.028  24.220  40.803  1.00 54.25  ? 228  GLN B C   1 
ATOM   5934  O  O   . GLN B  1 228 ? 10.005  24.593  41.965  1.00 55.28  ? 228  GLN B O   1 
ATOM   5935  C  CB  . GLN B  1 228 ? 11.582  26.006  40.003  1.00 52.50  ? 228  GLN B CB  1 
ATOM   5936  C  CG  . GLN B  1 228 ? 11.681  27.264  39.178  1.00 54.18  ? 228  GLN B CG  1 
ATOM   5937  C  CD  . GLN B  1 228 ? 13.043  27.911  39.283  1.00 60.08  ? 228  GLN B CD  1 
ATOM   5938  O  OE1 . GLN B  1 228 ? 13.226  29.076  38.911  1.00 64.29  ? 228  GLN B OE1 1 
ATOM   5939  N  NE2 . GLN B  1 228 ? 14.019  27.153  39.784  1.00 59.72  ? 228  GLN B NE2 1 
ATOM   5940  N  N   . SER B  1 229 ? 9.800   22.961  40.443  1.00 46.27  ? 229  SER B N   1 
ATOM   5941  C  CA  . SER B  1 229 ? 9.539   21.900  41.423  1.00 43.42  ? 229  SER B CA  1 
ATOM   5942  C  C   . SER B  1 229 ? 8.381   22.190  42.375  1.00 44.37  ? 229  SER B C   1 
ATOM   5943  O  O   . SER B  1 229 ? 8.480   21.909  43.557  1.00 38.25  ? 229  SER B O   1 
ATOM   5944  C  CB  . SER B  1 229 ? 10.802  21.571  42.235  1.00 45.76  ? 229  SER B CB  1 
ATOM   5945  O  OG  . SER B  1 229 ? 11.783  20.934  41.433  1.00 42.25  ? 229  SER B OG  1 
ATOM   5946  N  N   . GLY B  1 230 ? 7.297   22.751  41.855  1.00 38.82  ? 230  GLY B N   1 
ATOM   5947  C  CA  . GLY B  1 230 ? 6.107   22.981  42.647  1.00 37.41  ? 230  GLY B CA  1 
ATOM   5948  C  C   . GLY B  1 230 ? 4.940   23.384  41.767  1.00 46.47  ? 230  GLY B C   1 
ATOM   5949  O  O   . GLY B  1 230 ? 5.140   23.881  40.664  1.00 38.54  ? 230  GLY B O   1 
ATOM   5950  N  N   . THR B  1 231 ? 3.719   23.174  42.248  1.00 35.95  ? 231  THR B N   1 
ATOM   5951  C  CA  . THR B  1 231 ? 2.519   23.466  41.471  1.00 35.78  ? 231  THR B CA  1 
ATOM   5952  C  C   . THR B  1 231 ? 1.408   23.905  42.393  1.00 34.57  ? 231  THR B C   1 
ATOM   5953  O  O   . THR B  1 231 ? 1.406   23.530  43.563  1.00 33.58  ? 231  THR B O   1 
ATOM   5954  C  CB  . THR B  1 231 ? 2.009   22.204  40.836  1.00 38.57  ? 231  THR B CB  1 
ATOM   5955  O  OG1 . THR B  1 231 ? 2.100   21.145  41.799  1.00 41.61  ? 231  THR B OG1 1 
ATOM   5956  C  CG2 . THR B  1 231 ? 2.816   21.863  39.606  1.00 36.58  ? 231  THR B CG2 1 
ATOM   5957  N  N   . PRO B  1 232 ? 0.436   24.675  41.875  1.00 38.94  ? 232  PRO B N   1 
ATOM   5958  C  CA  . PRO B  1 232 ? -0.727  25.057  42.682  1.00 37.02  ? 232  PRO B CA  1 
ATOM   5959  C  C   . PRO B  1 232 ? -1.649  23.875  42.915  1.00 38.15  ? 232  PRO B C   1 
ATOM   5960  O  O   . PRO B  1 232 ? -2.408  23.879  43.879  1.00 39.78  ? 232  PRO B O   1 
ATOM   5961  C  CB  . PRO B  1 232 ? -1.436  26.088  41.807  1.00 41.27  ? 232  PRO B CB  1 
ATOM   5962  C  CG  . PRO B  1 232 ? -1.103  25.689  40.435  1.00 43.36  ? 232  PRO B CG  1 
ATOM   5963  C  CD  . PRO B  1 232 ? 0.321   25.170  40.495  1.00 45.12  ? 232  PRO B CD  1 
ATOM   5964  N  N   . ASN B  1 233 ? -1.599  22.888  42.026  1.00 40.52  ? 233  ASN B N   1 
ATOM   5965  C  CA  . ASN B  1 233 ? -2.435  21.703  42.147  1.00 42.33  ? 233  ASN B CA  1 
ATOM   5966  C  C   . ASN B  1 233 ? -1.713  20.655  42.962  1.00 46.07  ? 233  ASN B C   1 
ATOM   5967  O  O   . ASN B  1 233 ? -0.574  20.854  43.378  1.00 48.44  ? 233  ASN B O   1 
ATOM   5968  C  CB  . ASN B  1 233 ? -2.743  21.136  40.764  1.00 37.33  ? 233  ASN B CB  1 
ATOM   5969  C  CG  . ASN B  1 233 ? -1.479  20.807  39.974  1.00 37.86  ? 233  ASN B CG  1 
ATOM   5970  O  OD1 . ASN B  1 233 ? -0.700  21.697  39.640  1.00 39.07  ? 233  ASN B OD1 1 
ATOM   5971  N  ND2 . ASN B  1 233 ? -1.278  19.529  39.664  1.00 36.22  ? 233  ASN B ND2 1 
ATOM   5972  N  N   . GLY B  1 234 ? -2.362  19.524  43.181  1.00 56.66  ? 234  GLY B N   1 
ATOM   5973  C  CA  . GLY B  1 234 ? -1.680  18.428  43.830  1.00 57.11  ? 234  GLY B CA  1 
ATOM   5974  C  C   . GLY B  1 234 ? -2.050  18.191  45.279  1.00 55.49  ? 234  GLY B C   1 
ATOM   5975  O  O   . GLY B  1 234 ? -2.966  18.817  45.818  1.00 59.31  ? 234  GLY B O   1 
ATOM   5976  N  N   . PRO B  1 235 ? -1.332  17.257  45.912  1.00 34.60  ? 235  PRO B N   1 
ATOM   5977  C  CA  . PRO B  1 235 ? -1.584  16.780  47.268  1.00 29.22  ? 235  PRO B CA  1 
ATOM   5978  C  C   . PRO B  1 235 ? -1.336  17.797  48.368  1.00 28.00  ? 235  PRO B C   1 
ATOM   5979  O  O   . PRO B  1 235 ? -2.163  17.878  49.277  1.00 26.21  ? 235  PRO B O   1 
ATOM   5980  C  CB  . PRO B  1 235 ? -0.575  15.646  47.413  1.00 26.71  ? 235  PRO B CB  1 
ATOM   5981  C  CG  . PRO B  1 235 ? 0.518   16.010  46.506  1.00 28.06  ? 235  PRO B CG  1 
ATOM   5982  C  CD  . PRO B  1 235 ? -0.156  16.602  45.323  1.00 28.45  ? 235  PRO B CD  1 
ATOM   5983  N  N   . TRP B  1 236 ? -0.219  18.522  48.307  1.00 27.54  ? 236  TRP B N   1 
ATOM   5984  C  CA  . TRP B  1 236 ? 0.235   19.330  49.446  1.00 31.32  ? 236  TRP B CA  1 
ATOM   5985  C  C   . TRP B  1 236 ? -0.004  20.848  49.458  1.00 32.98  ? 236  TRP B C   1 
ATOM   5986  O  O   . TRP B  1 236 ? 0.262   21.495  50.476  1.00 32.30  ? 236  TRP B O   1 
ATOM   5987  C  CB  . TRP B  1 236 ? 1.730   19.103  49.645  1.00 31.20  ? 236  TRP B CB  1 
ATOM   5988  C  CG  . TRP B  1 236 ? 2.548   19.521  48.448  1.00 34.37  ? 236  TRP B CG  1 
ATOM   5989  C  CD1 . TRP B  1 236 ? 3.043   18.707  47.463  1.00 36.24  ? 236  TRP B CD1 1 
ATOM   5990  C  CD2 . TRP B  1 236 ? 2.958   20.849  48.107  1.00 34.85  ? 236  TRP B CD2 1 
ATOM   5991  N  NE1 . TRP B  1 236 ? 3.734   19.448  46.540  1.00 37.45  ? 236  TRP B NE1 1 
ATOM   5992  C  CE2 . TRP B  1 236 ? 3.698   20.765  46.915  1.00 38.20  ? 236  TRP B CE2 1 
ATOM   5993  C  CE3 . TRP B  1 236 ? 2.778   22.098  48.700  1.00 35.29  ? 236  TRP B CE3 1 
ATOM   5994  C  CZ2 . TRP B  1 236 ? 4.251   21.883  46.304  1.00 42.01  ? 236  TRP B CZ2 1 
ATOM   5995  C  CZ3 . TRP B  1 236 ? 3.316   23.202  48.087  1.00 38.84  ? 236  TRP B CZ3 1 
ATOM   5996  C  CH2 . TRP B  1 236 ? 4.054   23.090  46.905  1.00 41.16  ? 236  TRP B CH2 1 
ATOM   5997  N  N   . ALA B  1 237 ? -0.480  21.423  48.356  1.00 29.39  ? 237  ALA B N   1 
ATOM   5998  C  CA  . ALA B  1 237 ? -0.426  22.880  48.218  1.00 30.55  ? 237  ALA B CA  1 
ATOM   5999  C  C   . ALA B  1 237 ? -1.644  23.647  48.688  1.00 29.34  ? 237  ALA B C   1 
ATOM   6000  O  O   . ALA B  1 237 ? -1.571  24.855  48.834  1.00 39.26  ? 237  ALA B O   1 
ATOM   6001  C  CB  . ALA B  1 237 ? -0.049  23.287  46.792  1.00 30.84  ? 237  ALA B CB  1 
ATOM   6002  N  N   . THR B  1 238 ? -2.757  22.966  48.922  1.00 28.26  ? 238  THR B N   1 
ATOM   6003  C  CA  . THR B  1 238 ? -3.970  23.633  49.395  1.00 27.86  ? 238  THR B CA  1 
ATOM   6004  C  C   . THR B  1 238 ? -4.690  22.766  50.424  1.00 26.62  ? 238  THR B C   1 
ATOM   6005  O  O   . THR B  1 238 ? -4.498  21.552  50.454  1.00 26.03  ? 238  THR B O   1 
ATOM   6006  C  CB  . THR B  1 238 ? -4.973  23.954  48.243  1.00 28.05  ? 238  THR B CB  1 
ATOM   6007  O  OG1 . THR B  1 238 ? -5.586  22.753  47.769  1.00 27.23  ? 238  THR B OG1 1 
ATOM   6008  C  CG2 . THR B  1 238 ? -4.295  24.638  47.083  1.00 29.30  ? 238  THR B CG2 1 
ATOM   6009  N  N   . VAL B  1 239 ? -5.505  23.375  51.279  1.00 26.30  ? 239  VAL B N   1 
ATOM   6010  C  CA  . VAL B  1 239 ? -6.465  22.591  52.055  1.00 25.17  ? 239  VAL B CA  1 
ATOM   6011  C  C   . VAL B  1 239 ? -7.853  23.113  51.800  1.00 24.97  ? 239  VAL B C   1 
ATOM   6012  O  O   . VAL B  1 239 ? -8.045  24.206  51.250  1.00 25.73  ? 239  VAL B O   1 
ATOM   6013  C  CB  . VAL B  1 239 ? -6.224  22.577  53.587  1.00 24.79  ? 239  VAL B CB  1 
ATOM   6014  C  CG1 . VAL B  1 239 ? -4.958  21.864  53.917  1.00 31.95  ? 239  VAL B CG1 1 
ATOM   6015  C  CG2 . VAL B  1 239 ? -6.217  23.975  54.150  1.00 25.41  ? 239  VAL B CG2 1 
ATOM   6016  N  N   . SER B  1 240 ? -8.822  22.300  52.185  1.00 33.97  ? 240  SER B N   1 
ATOM   6017  C  CA  . SER B  1 240 ? -10.213 22.675  52.093  1.00 34.75  ? 240  SER B CA  1 
ATOM   6018  C  C   . SER B  1 240 ? -10.507 23.717  53.146  1.00 36.03  ? 240  SER B C   1 
ATOM   6019  O  O   . SER B  1 240 ? -9.782  23.831  54.136  1.00 36.78  ? 240  SER B O   1 
ATOM   6020  C  CB  . SER B  1 240 ? -11.057 21.461  52.388  1.00 31.50  ? 240  SER B CB  1 
ATOM   6021  O  OG  . SER B  1 240 ? -10.616 20.920  53.608  1.00 32.19  ? 240  SER B OG  1 
ATOM   6022  N  N   . ALA B  1 241 ? -11.575 24.475  52.937  1.00 29.40  ? 241  ALA B N   1 
ATOM   6023  C  CA  . ALA B  1 241 ? -12.071 25.351  53.979  1.00 28.39  ? 241  ALA B CA  1 
ATOM   6024  C  C   . ALA B  1 241 ? -12.312 24.529  55.247  1.00 25.10  ? 241  ALA B C   1 
ATOM   6025  O  O   . ALA B  1 241 ? -11.975 24.940  56.359  1.00 24.07  ? 241  ALA B O   1 
ATOM   6026  C  CB  . ALA B  1 241 ? -13.343 26.007  53.529  1.00 36.73  ? 241  ALA B CB  1 
ATOM   6027  N  N   . GLY B  1 242 ? -12.875 23.346  55.067  1.00 28.51  ? 242  GLY B N   1 
ATOM   6028  C  CA  . GLY B  1 242 ? -13.157 22.492  56.198  1.00 29.97  ? 242  GLY B CA  1 
ATOM   6029  C  C   . GLY B  1 242 ? -11.930 22.180  57.026  1.00 31.26  ? 242  GLY B C   1 
ATOM   6030  O  O   . GLY B  1 242 ? -11.908 22.421  58.232  1.00 32.86  ? 242  GLY B O   1 
ATOM   6031  N  N   . GLU B  1 243 ? -10.902 21.652  56.377  1.00 28.58  ? 243  GLU B N   1 
ATOM   6032  C  CA  . GLU B  1 243 ? -9.719  21.220  57.088  1.00 27.61  ? 243  GLU B CA  1 
ATOM   6033  C  C   . GLU B  1 243 ? -8.951  22.426  57.624  1.00 30.82  ? 243  GLU B C   1 
ATOM   6034  O  O   . GLU B  1 243 ? -8.299  22.351  58.679  1.00 30.02  ? 243  GLU B O   1 
ATOM   6035  C  CB  . GLU B  1 243 ? -8.843  20.372  56.180  1.00 26.58  ? 243  GLU B CB  1 
ATOM   6036  C  CG  . GLU B  1 243 ? -7.613  19.802  56.852  1.00 31.10  ? 243  GLU B CG  1 
ATOM   6037  C  CD  . GLU B  1 243 ? -7.898  18.625  57.781  1.00 34.77  ? 243  GLU B CD  1 
ATOM   6038  O  OE1 . GLU B  1 243 ? -9.085  18.314  58.075  1.00 35.85  ? 243  GLU B OE1 1 
ATOM   6039  O  OE2 . GLU B  1 243 ? -6.902  18.007  58.217  1.00 35.93  ? 243  GLU B OE2 1 
ATOM   6040  N  N   . ALA B  1 244 ? -9.032  23.545  56.909  1.00 24.42  ? 244  ALA B N   1 
ATOM   6041  C  CA  . ALA B  1 244 ? -8.423  24.764  57.402  1.00 24.11  ? 244  ALA B CA  1 
ATOM   6042  C  C   . ALA B  1 244 ? -9.036  25.049  58.762  1.00 23.73  ? 244  ALA B C   1 
ATOM   6043  O  O   . ALA B  1 244 ? -8.324  25.088  59.765  1.00 23.81  ? 244  ALA B O   1 
ATOM   6044  C  CB  . ALA B  1 244 ? -8.672  25.899  56.456  1.00 24.91  ? 244  ALA B CB  1 
ATOM   6045  N  N   . ARG B  1 245 ? -10.363 25.177  58.797  1.00 23.33  ? 245  ARG B N   1 
ATOM   6046  C  CA  . ARG B  1 245 ? -11.075 25.483  60.034  1.00 23.02  ? 245  ARG B CA  1 
ATOM   6047  C  C   . ARG B  1 245 ? -10.764 24.482  61.124  1.00 22.37  ? 245  ARG B C   1 
ATOM   6048  O  O   . ARG B  1 245 ? -10.561 24.856  62.272  1.00 22.46  ? 245  ARG B O   1 
ATOM   6049  C  CB  . ARG B  1 245 ? -12.582 25.556  59.799  1.00 27.88  ? 245  ARG B CB  1 
ATOM   6050  C  CG  . ARG B  1 245 ? -13.414 25.436  61.076  1.00 30.07  ? 245  ARG B CG  1 
ATOM   6051  C  CD  . ARG B  1 245 ? -14.807 26.042  60.934  1.00 33.75  ? 245  ARG B CD  1 
ATOM   6052  N  NE  . ARG B  1 245 ? -14.978 27.180  61.831  1.00 42.33  ? 245  ARG B NE  1 
ATOM   6053  C  CZ  . ARG B  1 245 ? -15.283 27.074  63.125  1.00 50.60  ? 245  ARG B CZ  1 
ATOM   6054  N  NH1 . ARG B  1 245 ? -15.461 25.876  63.676  1.00 51.42  ? 245  ARG B NH1 1 
ATOM   6055  N  NH2 . ARG B  1 245 ? -15.411 28.167  63.876  1.00 53.31  ? 245  ARG B NH2 1 
ATOM   6056  N  N   . ARG B  1 246 ? -10.709 23.213  60.745  1.00 21.78  ? 246  ARG B N   1 
ATOM   6057  C  CA  . ARG B  1 246 ? -10.399 22.127  61.667  1.00 21.20  ? 246  ARG B CA  1 
ATOM   6058  C  C   . ARG B  1 246 ? -9.047  22.346  62.362  1.00 24.93  ? 246  ARG B C   1 
ATOM   6059  O  O   . ARG B  1 246 ? -8.942  22.255  63.600  1.00 23.38  ? 246  ARG B O   1 
ATOM   6060  C  CB  . ARG B  1 246 ? -10.405 20.798  60.902  1.00 31.26  ? 246  ARG B CB  1 
ATOM   6061  C  CG  . ARG B  1 246 ? -10.705 19.548  61.733  1.00 33.73  ? 246  ARG B CG  1 
ATOM   6062  C  CD  . ARG B  1 246 ? -9.471  18.946  62.423  1.00 36.74  ? 246  ARG B CD  1 
ATOM   6063  N  NE  . ARG B  1 246 ? -8.550  18.331  61.469  1.00 37.79  ? 246  ARG B NE  1 
ATOM   6064  C  CZ  . ARG B  1 246 ? -7.381  17.783  61.790  1.00 36.56  ? 246  ARG B CZ  1 
ATOM   6065  N  NH1 . ARG B  1 246 ? -6.960  17.744  63.050  1.00 33.38  ? 246  ARG B NH1 1 
ATOM   6066  N  NH2 . ARG B  1 246 ? -6.628  17.268  60.837  1.00 38.29  ? 246  ARG B NH2 1 
ATOM   6067  N  N   . ARG B  1 247 ? -8.029  22.659  61.562  1.00 22.35  ? 247  ARG B N   1 
ATOM   6068  C  CA  . ARG B  1 247 ? -6.675  22.825  62.060  1.00 22.90  ? 247  ARG B CA  1 
ATOM   6069  C  C   . ARG B  1 247 ? -6.495  24.094  62.858  1.00 23.50  ? 247  ARG B C   1 
ATOM   6070  O  O   . ARG B  1 247 ? -5.763  24.117  63.840  1.00 23.71  ? 247  ARG B O   1 
ATOM   6071  C  CB  . ARG B  1 247 ? -5.699  22.849  60.899  1.00 32.15  ? 247  ARG B CB  1 
ATOM   6072  C  CG  . ARG B  1 247 ? -5.609  21.550  60.191  1.00 30.70  ? 247  ARG B CG  1 
ATOM   6073  C  CD  . ARG B  1 247 ? -4.575  21.589  59.101  1.00 31.75  ? 247  ARG B CD  1 
ATOM   6074  N  NE  . ARG B  1 247 ? -4.785  20.440  58.232  1.00 34.66  ? 247  ARG B NE  1 
ATOM   6075  C  CZ  . ARG B  1 247 ? -4.059  20.155  57.161  1.00 34.88  ? 247  ARG B CZ  1 
ATOM   6076  N  NH1 . ARG B  1 247 ? -3.039  20.940  56.820  1.00 34.26  ? 247  ARG B NH1 1 
ATOM   6077  N  NH2 . ARG B  1 247 ? -4.359  19.075  56.439  1.00 34.79  ? 247  ARG B NH2 1 
ATOM   6078  N  N   . ALA B  1 248 ? -7.132  25.164  62.411  1.00 23.87  ? 248  ALA B N   1 
ATOM   6079  C  CA  . ALA B  1 248 ? -7.062  26.422  63.127  1.00 24.48  ? 248  ALA B CA  1 
ATOM   6080  C  C   . ALA B  1 248 ? -7.681  26.246  64.504  1.00 23.97  ? 248  ALA B C   1 
ATOM   6081  O  O   . ALA B  1 248 ? -7.114  26.648  65.517  1.00 24.31  ? 248  ALA B O   1 
ATOM   6082  C  CB  . ALA B  1 248 ? -7.788  27.482  62.366  1.00 24.93  ? 248  ALA B CB  1 
ATOM   6083  N  N   . THR B  1 249 ? -8.854  25.627  64.524  1.00 28.28  ? 249  THR B N   1 
ATOM   6084  C  CA  . THR B  1 249 ? -9.570  25.348  65.756  1.00 30.18  ? 249  THR B CA  1 
ATOM   6085  C  C   . THR B  1 249 ? -8.737  24.513  66.717  1.00 22.48  ? 249  THR B C   1 
ATOM   6086  O  O   . THR B  1 249 ? -8.633  24.847  67.901  1.00 22.63  ? 249  THR B O   1 
ATOM   6087  C  CB  . THR B  1 249 ? -10.881 24.632  65.450  1.00 40.78  ? 249  THR B CB  1 
ATOM   6088  O  OG1 . THR B  1 249 ? -11.729 25.525  64.723  1.00 39.88  ? 249  THR B OG1 1 
ATOM   6089  C  CG2 . THR B  1 249 ? -11.577 24.215  66.729  1.00 45.49  ? 249  THR B CG2 1 
ATOM   6090  N  N   . LEU B  1 250 ? -8.145  23.436  66.208  1.00 28.14  ? 250  LEU B N   1 
ATOM   6091  C  CA  . LEU B  1 250 ? -7.254  22.602  67.025  1.00 26.92  ? 250  LEU B CA  1 
ATOM   6092  C  C   . LEU B  1 250 ? -6.008  23.335  67.563  1.00 24.88  ? 250  LEU B C   1 
ATOM   6093  O  O   . LEU B  1 250 ? -5.637  23.168  68.729  1.00 23.02  ? 250  LEU B O   1 
ATOM   6094  C  CB  . LEU B  1 250 ? -6.846  21.323  66.277  1.00 21.77  ? 250  LEU B CB  1 
ATOM   6095  C  CG  . LEU B  1 250 ? -5.685  20.550  66.884  1.00 21.92  ? 250  LEU B CG  1 
ATOM   6096  C  CD1 . LEU B  1 250 ? -6.096  19.960  68.192  1.00 21.50  ? 250  LEU B CD1 1 
ATOM   6097  C  CD2 . LEU B  1 250 ? -5.271  19.494  65.946  1.00 21.72  ? 250  LEU B CD2 1 
ATOM   6098  N  N   . LEU B  1 251 ? -5.357  24.137  66.725  1.00 23.65  ? 251  LEU B N   1 
ATOM   6099  C  CA  . LEU B  1 251 ? -4.163  24.833  67.183  1.00 27.83  ? 251  LEU B CA  1 
ATOM   6100  C  C   . LEU B  1 251 ? -4.529  25.852  68.247  1.00 28.76  ? 251  LEU B C   1 
ATOM   6101  O  O   . LEU B  1 251 ? -3.858  25.948  69.266  1.00 27.72  ? 251  LEU B O   1 
ATOM   6102  C  CB  . LEU B  1 251 ? -3.407  25.512  66.046  1.00 25.25  ? 251  LEU B CB  1 
ATOM   6103  C  CG  . LEU B  1 251 ? -2.169  26.255  66.546  1.00 26.19  ? 251  LEU B CG  1 
ATOM   6104  C  CD1 . LEU B  1 251 ? -0.910  25.596  66.058  1.00 26.52  ? 251  LEU B CD1 1 
ATOM   6105  C  CD2 . LEU B  1 251 ? -2.236  27.675  66.101  1.00 26.95  ? 251  LEU B CD2 1 
ATOM   6106  N  N   . ALA B  1 252 ? -5.593  26.612  68.007  1.00 32.58  ? 252  ALA B N   1 
ATOM   6107  C  CA  . ALA B  1 252 ? -6.132  27.486  69.037  1.00 33.38  ? 252  ALA B CA  1 
ATOM   6108  C  C   . ALA B  1 252 ? -6.288  26.665  70.305  1.00 32.48  ? 252  ALA B C   1 
ATOM   6109  O  O   . ALA B  1 252 ? -5.825  27.058  71.362  1.00 34.06  ? 252  ALA B O   1 
ATOM   6110  C  CB  . ALA B  1 252 ? -7.479  28.054  68.608  1.00 32.84  ? 252  ALA B CB  1 
ATOM   6111  N  N   . ARG B  1 253 ? -6.906  25.495  70.179  1.00 24.62  ? 253  ARG B N   1 
ATOM   6112  C  CA  . ARG B  1 253 ? -7.242  24.675  71.341  1.00 24.89  ? 253  ARG B CA  1 
ATOM   6113  C  C   . ARG B  1 253 ? -6.014  24.175  72.092  1.00 23.38  ? 253  ARG B C   1 
ATOM   6114  O  O   . ARG B  1 253 ? -6.097  23.900  73.280  1.00 23.31  ? 253  ARG B O   1 
ATOM   6115  C  CB  . ARG B  1 253 ? -8.182  23.521  70.932  1.00 28.94  ? 253  ARG B CB  1 
ATOM   6116  C  CG  . ARG B  1 253 ? -8.905  22.793  72.086  1.00 27.23  ? 253  ARG B CG  1 
ATOM   6117  C  CD  . ARG B  1 253 ? -10.334 22.384  71.699  1.00 26.99  ? 253  ARG B CD  1 
ATOM   6118  N  NE  . ARG B  1 253 ? -10.488 22.251  70.254  1.00 29.88  ? 253  ARG B NE  1 
ATOM   6119  C  CZ  . ARG B  1 253 ? -10.105 21.177  69.568  1.00 36.25  ? 253  ARG B CZ  1 
ATOM   6120  N  NH1 . ARG B  1 253 ? -9.539  20.156  70.203  1.00 37.62  ? 253  ARG B NH1 1 
ATOM   6121  N  NH2 . ARG B  1 253 ? -10.264 21.120  68.248  1.00 38.71  ? 253  ARG B NH2 1 
ATOM   6122  N  N   . LEU B  1 254 ? -4.883  24.083  71.396  1.00 23.80  ? 254  LEU B N   1 
ATOM   6123  C  CA  . LEU B  1 254 ? -3.619  23.631  71.999  1.00 24.20  ? 254  LEU B CA  1 
ATOM   6124  C  C   . LEU B  1 254 ? -2.910  24.687  72.849  1.00 25.05  ? 254  LEU B C   1 
ATOM   6125  O  O   . LEU B  1 254 ? -2.306  24.365  73.872  1.00 25.28  ? 254  LEU B O   1 
ATOM   6126  C  CB  . LEU B  1 254 ? -2.663  23.101  70.935  1.00 24.38  ? 254  LEU B CB  1 
ATOM   6127  C  CG  . LEU B  1 254 ? -3.055  21.695  70.543  1.00 23.60  ? 254  LEU B CG  1 
ATOM   6128  C  CD1 . LEU B  1 254 ? -2.165  21.165  69.456  1.00 23.80  ? 254  LEU B CD1 1 
ATOM   6129  C  CD2 . LEU B  1 254 ? -2.960  20.857  71.779  1.00 23.40  ? 254  LEU B CD2 1 
ATOM   6130  N  N   . VAL B  1 255 ? -2.961  25.937  72.403  1.00 30.53  ? 255  VAL B N   1 
ATOM   6131  C  CA  . VAL B  1 255 ? -2.667  27.074  73.260  1.00 34.53  ? 255  VAL B CA  1 
ATOM   6132  C  C   . VAL B  1 255 ? -3.990  27.393  73.955  1.00 41.83  ? 255  VAL B C   1 
ATOM   6133  O  O   . VAL B  1 255 ? -4.941  26.616  73.836  1.00 46.35  ? 255  VAL B O   1 
ATOM   6134  C  CB  . VAL B  1 255 ? -2.165  28.237  72.438  1.00 27.11  ? 255  VAL B CB  1 
ATOM   6135  C  CG1 . VAL B  1 255 ? -1.151  27.727  71.425  1.00 27.31  ? 255  VAL B CG1 1 
ATOM   6136  C  CG2 . VAL B  1 255 ? -3.314  28.914  71.720  1.00 26.92  ? 255  VAL B CG2 1 
ATOM   6137  N  N   . GLY B  1 256 ? -4.086  28.496  74.683  1.00 41.60  ? 256  GLY B N   1 
ATOM   6138  C  CA  . GLY B  1 256 ? -5.294  28.720  75.475  1.00 44.37  ? 256  GLY B CA  1 
ATOM   6139  C  C   . GLY B  1 256 ? -6.688  28.684  74.826  1.00 41.55  ? 256  GLY B C   1 
ATOM   6140  O  O   . GLY B  1 256 ? -7.672  28.319  75.469  1.00 40.27  ? 256  GLY B O   1 
ATOM   6141  N  N   . CYS B  1 257 ? -6.761  29.025  73.545  1.00 34.71  ? 257  CYS B N   1 
ATOM   6142  C  CA  . CYS B  1 257 ? -7.970  29.603  72.951  1.00 36.41  ? 257  CYS B CA  1 
ATOM   6143  C  C   . CYS B  1 257 ? -9.023  28.654  72.358  1.00 43.20  ? 257  CYS B C   1 
ATOM   6144  O  O   . CYS B  1 257 ? -8.686  27.638  71.770  1.00 43.95  ? 257  CYS B O   1 
ATOM   6145  C  CB  . CYS B  1 257 ? -7.549  30.638  71.904  1.00 35.75  ? 257  CYS B CB  1 
ATOM   6146  S  SG  . CYS B  1 257 ? -6.207  31.737  72.464  1.00 61.75  ? 257  CYS B SG  1 
ATOM   6147  N  N   . PRO B  1 258 ? -10.314 28.999  72.506  1.00 55.56  ? 258  PRO B N   1 
ATOM   6148  C  CA  . PRO B  1 258 ? -10.827 30.117  73.297  1.00 61.98  ? 258  PRO B CA  1 
ATOM   6149  C  C   . PRO B  1 258 ? -10.750 29.684  74.749  1.00 67.35  ? 258  PRO B C   1 
ATOM   6150  O  O   . PRO B  1 258 ? -10.622 28.475  74.980  1.00 66.40  ? 258  PRO B O   1 
ATOM   6151  C  CB  . PRO B  1 258 ? -12.276 30.240  72.822  1.00 70.26  ? 258  PRO B CB  1 
ATOM   6152  C  CG  . PRO B  1 258 ? -12.650 28.873  72.458  1.00 69.22  ? 258  PRO B CG  1 
ATOM   6153  C  CD  . PRO B  1 258 ? -11.407 28.230  71.890  1.00 67.83  ? 258  PRO B CD  1 
ATOM   6154  N  N   . PRO B  1 259 ? -10.798 30.636  75.702  1.00 90.21  ? 259  PRO B N   1 
ATOM   6155  C  CA  . PRO B  1 259 ? -10.397 30.291  77.076  1.00 93.76  ? 259  PRO B CA  1 
ATOM   6156  C  C   . PRO B  1 259 ? -11.294 29.235  77.739  1.00 97.50  ? 259  PRO B C   1 
ATOM   6157  O  O   . PRO B  1 259 ? -12.512 29.425  77.812  1.00 98.84  ? 259  PRO B O   1 
ATOM   6158  C  CB  . PRO B  1 259 ? -10.502 31.633  77.819  1.00 60.48  ? 259  PRO B CB  1 
ATOM   6159  C  CG  . PRO B  1 259 ? -10.617 32.694  76.740  1.00 58.71  ? 259  PRO B CG  1 
ATOM   6160  C  CD  . PRO B  1 259 ? -11.278 32.026  75.589  1.00 57.26  ? 259  PRO B CD  1 
ATOM   6161  N  N   . GLY B  1 260 ? -10.685 28.153  78.229  1.00 74.19  ? 260  GLY B N   1 
ATOM   6162  C  CA  . GLY B  1 260 ? -11.404 27.082  78.900  1.00 76.26  ? 260  GLY B CA  1 
ATOM   6163  C  C   . GLY B  1 260 ? -12.534 26.418  78.118  1.00 81.60  ? 260  GLY B C   1 
ATOM   6164  O  O   . GLY B  1 260 ? -13.351 25.704  78.703  1.00 81.77  ? 260  GLY B O   1 
ATOM   6165  N  N   . GLY B  1 261 ? -12.595 26.652  76.806  1.00 102.49 ? 261  GLY B N   1 
ATOM   6166  C  CA  . GLY B  1 261 ? -13.590 26.029  75.935  1.00 100.67 ? 261  GLY B CA  1 
ATOM   6167  C  C   . GLY B  1 261 ? -15.029 26.536  75.961  1.00 96.34  ? 261  GLY B C   1 
ATOM   6168  O  O   . GLY B  1 261 ? -15.970 25.744  75.988  1.00 93.76  ? 261  GLY B O   1 
ATOM   6169  N  N   . ALA B  1 262 ? -15.206 27.852  75.928  1.00 87.15  ? 262  ALA B N   1 
ATOM   6170  C  CA  . ALA B  1 262 ? -16.539 28.450  75.893  1.00 86.14  ? 262  ALA B CA  1 
ATOM   6171  C  C   . ALA B  1 262 ? -17.199 28.290  74.532  1.00 84.18  ? 262  ALA B C   1 
ATOM   6172  O  O   . ALA B  1 262 ? -18.397 28.526  74.392  1.00 84.36  ? 262  ALA B O   1 
ATOM   6173  C  CB  . ALA B  1 262 ? -16.475 29.931  76.259  1.00 86.08  ? 262  ALA B CB  1 
ATOM   6174  N  N   . GLY B  1 263 ? -16.410 27.916  73.529  1.00 78.59  ? 263  GLY B N   1 
ATOM   6175  C  CA  . GLY B  1 263 ? -16.899 27.785  72.166  1.00 77.14  ? 263  GLY B CA  1 
ATOM   6176  C  C   . GLY B  1 263 ? -17.424 29.096  71.610  1.00 77.73  ? 263  GLY B C   1 
ATOM   6177  O  O   . GLY B  1 263 ? -17.186 30.161  72.190  1.00 79.18  ? 263  GLY B O   1 
ATOM   6178  N  N   . GLY B  1 264 ? -18.148 29.019  70.494  1.00 79.14  ? 264  GLY B N   1 
ATOM   6179  C  CA  . GLY B  1 264 ? -18.791 30.188  69.914  1.00 78.81  ? 264  GLY B CA  1 
ATOM   6180  C  C   . GLY B  1 264 ? -17.950 30.993  68.935  1.00 78.81  ? 264  GLY B C   1 
ATOM   6181  O  O   . GLY B  1 264 ? -17.095 30.440  68.238  1.00 78.90  ? 264  GLY B O   1 
ATOM   6182  N  N   . ASN B  1 265 ? -18.185 32.308  68.912  1.00 69.33  ? 265  ASN B N   1 
ATOM   6183  C  CA  . ASN B  1 265 ? -17.719 33.191  67.832  1.00 65.21  ? 265  ASN B CA  1 
ATOM   6184  C  C   . ASN B  1 265 ? -16.251 33.105  67.492  1.00 53.69  ? 265  ASN B C   1 
ATOM   6185  O  O   . ASN B  1 265 ? -15.394 33.085  68.362  1.00 49.61  ? 265  ASN B O   1 
ATOM   6186  C  CB  . ASN B  1 265 ? -18.161 34.664  68.020  1.00 86.77  ? 265  ASN B CB  1 
ATOM   6187  C  CG  . ASN B  1 265 ? -17.879 35.212  69.416  1.00 91.67  ? 265  ASN B CG  1 
ATOM   6188  O  OD1 . ASN B  1 265 ? -16.764 35.099  69.912  1.00 91.30  ? 265  ASN B OD1 1 
ATOM   6189  N  ND2 . ASN B  1 265 ? -18.910 35.796  70.063  1.00 95.42  ? 265  ASN B ND2 1 
ATOM   6190  N  N   . ASP B  1 266 ? -15.990 33.025  66.196  1.00 45.74  ? 266  ASP B N   1 
ATOM   6191  C  CA  . ASP B  1 266 ? -14.636 32.931  65.693  1.00 46.37  ? 266  ASP B CA  1 
ATOM   6192  C  C   . ASP B  1 266 ? -13.884 34.192  66.065  1.00 39.45  ? 266  ASP B C   1 
ATOM   6193  O  O   . ASP B  1 266 ? -12.687 34.142  66.297  1.00 36.19  ? 266  ASP B O   1 
ATOM   6194  C  CB  . ASP B  1 266 ? -14.633 32.734  64.169  1.00 79.22  ? 266  ASP B CB  1 
ATOM   6195  C  CG  . ASP B  1 266 ? -15.180 31.368  63.745  1.00 82.97  ? 266  ASP B CG  1 
ATOM   6196  O  OD1 . ASP B  1 266 ? -15.266 30.457  64.601  1.00 81.06  ? 266  ASP B OD1 1 
ATOM   6197  O  OD2 . ASP B  1 266 ? -15.513 31.207  62.548  1.00 84.89  ? 266  ASP B OD2 1 
ATOM   6198  N  N   . THR B  1 267 ? -14.601 35.314  66.128  1.00 43.18  ? 267  THR B N   1 
ATOM   6199  C  CA  . THR B  1 267 ? -14.019 36.620  66.470  1.00 44.56  ? 267  THR B CA  1 
ATOM   6200  C  C   . THR B  1 267 ? -13.243 36.595  67.790  1.00 37.59  ? 267  THR B C   1 
ATOM   6201  O  O   . THR B  1 267 ? -12.135 37.114  67.872  1.00 33.31  ? 267  THR B O   1 
ATOM   6202  C  CB  . THR B  1 267 ? -15.108 37.695  66.556  1.00 69.28  ? 267  THR B CB  1 
ATOM   6203  O  OG1 . THR B  1 267 ? -16.254 37.142  67.218  1.00 74.03  ? 267  THR B OG1 1 
ATOM   6204  C  CG2 . THR B  1 267 ? -15.528 38.139  65.173  1.00 69.78  ? 267  THR B CG2 1 
ATOM   6205  N  N   . GLU B  1 268 ? -13.824 35.983  68.817  1.00 43.84  ? 268  GLU B N   1 
ATOM   6206  C  CA  . GLU B  1 268 ? -13.140 35.851  70.093  1.00 46.18  ? 268  GLU B CA  1 
ATOM   6207  C  C   . GLU B  1 268 ? -12.024 34.828  70.019  1.00 44.71  ? 268  GLU B C   1 
ATOM   6208  O  O   . GLU B  1 268 ? -11.019 34.991  70.680  1.00 48.81  ? 268  GLU B O   1 
ATOM   6209  C  CB  . GLU B  1 268 ? -14.106 35.481  71.218  1.00 72.25  ? 268  GLU B CB  1 
ATOM   6210  C  CG  . GLU B  1 268 ? -14.090 36.441  72.401  1.00 82.14  ? 268  GLU B CG  1 
ATOM   6211  C  CD  . GLU B  1 268 ? -15.199 36.153  73.406  1.00 89.39  ? 268  GLU B CD  1 
ATOM   6212  O  OE1 . GLU B  1 268 ? -15.734 35.019  73.398  1.00 88.34  ? 268  GLU B OE1 1 
ATOM   6213  O  OE2 . GLU B  1 268 ? -15.539 37.062  74.201  1.00 94.22  ? 268  GLU B OE2 1 
ATOM   6214  N  N   . LEU B  1 269 ? -12.185 33.770  69.232  1.00 45.56  ? 269  LEU B N   1 
ATOM   6215  C  CA  . LEU B  1 269 ? -11.104 32.792  69.111  1.00 39.35  ? 269  LEU B CA  1 
ATOM   6216  C  C   . LEU B  1 269 ? -9.868  33.429  68.459  1.00 37.90  ? 269  LEU B C   1 
ATOM   6217  O  O   . LEU B  1 269 ? -8.746  33.250  68.928  1.00 38.98  ? 269  LEU B O   1 
ATOM   6218  C  CB  . LEU B  1 269 ? -11.549 31.526  68.362  1.00 34.03  ? 269  LEU B CB  1 
ATOM   6219  C  CG  . LEU B  1 269 ? -10.523 30.380  68.264  1.00 30.19  ? 269  LEU B CG  1 
ATOM   6220  C  CD1 . LEU B  1 269 ? -11.167 29.021  68.439  1.00 29.34  ? 269  LEU B CD1 1 
ATOM   6221  C  CD2 . LEU B  1 269 ? -9.779  30.401  66.952  1.00 28.47  ? 269  LEU B CD2 1 
ATOM   6222  N  N   . ILE B  1 270 ? -10.074 34.190  67.394  1.00 27.88  ? 270  ILE B N   1 
ATOM   6223  C  CA  . ILE B  1 270 ? -8.969  34.866  66.741  1.00 28.80  ? 270  ILE B CA  1 
ATOM   6224  C  C   . ILE B  1 270 ? -8.416  35.969  67.634  1.00 40.42  ? 270  ILE B C   1 
ATOM   6225  O  O   . ILE B  1 270 ? -7.209  36.247  67.640  1.00 30.33  ? 270  ILE B O   1 
ATOM   6226  C  CB  . ILE B  1 270 ? -9.393  35.445  65.397  1.00 29.28  ? 270  ILE B CB  1 
ATOM   6227  C  CG1 . ILE B  1 270 ? -10.019 34.343  64.545  1.00 28.39  ? 270  ILE B CG1 1 
ATOM   6228  C  CG2 . ILE B  1 270 ? -8.195  36.070  64.691  1.00 30.27  ? 270  ILE B CG2 1 
ATOM   6229  C  CD1 . ILE B  1 270 ? -9.097  33.183  64.297  1.00 27.88  ? 270  ILE B CD1 1 
ATOM   6230  N  N   . ALA B  1 271 ? -9.309  36.585  68.402  1.00 49.87  ? 271  ALA B N   1 
ATOM   6231  C  CA  . ALA B  1 271 ? -8.925  37.660  69.304  1.00 47.83  ? 271  ALA B CA  1 
ATOM   6232  C  C   . ALA B  1 271 ? -8.000  37.113  70.361  1.00 42.34  ? 271  ALA B C   1 
ATOM   6233  O  O   . ALA B  1 271 ? -7.044  37.757  70.763  1.00 43.83  ? 271  ALA B O   1 
ATOM   6234  C  CB  . ALA B  1 271 ? -10.137 38.244  69.953  1.00 50.43  ? 271  ALA B CB  1 
ATOM   6235  N  N   . CYS B  1 272 ? -8.302  35.907  70.806  1.00 38.75  ? 272  CYS B N   1 
ATOM   6236  C  CA  . CYS B  1 272 ? -7.514  35.250  71.825  1.00 37.23  ? 272  CYS B CA  1 
ATOM   6237  C  C   . CYS B  1 272 ? -6.174  34.807  71.225  1.00 40.42  ? 272  CYS B C   1 
ATOM   6238  O  O   . CYS B  1 272 ? -5.111  34.999  71.837  1.00 40.90  ? 272  CYS B O   1 
ATOM   6239  C  CB  . CYS B  1 272 ? -8.304  34.067  72.400  1.00 28.11  ? 272  CYS B CB  1 
ATOM   6240  S  SG  . CYS B  1 272 ? -7.403  33.014  73.530  1.00 57.38  ? 272  CYS B SG  1 
ATOM   6241  N  N   . LEU B  1 273 ? -6.227  34.231  70.022  1.00 40.08  ? 273  LEU B N   1 
ATOM   6242  C  CA  . LEU B  1 273 ? -5.024  33.762  69.336  1.00 37.69  ? 273  LEU B CA  1 
ATOM   6243  C  C   . LEU B  1 273 ? -4.049  34.903  69.152  1.00 40.01  ? 273  LEU B C   1 
ATOM   6244  O  O   . LEU B  1 273 ? -2.834  34.713  69.184  1.00 40.73  ? 273  LEU B O   1 
ATOM   6245  C  CB  . LEU B  1 273 ? -5.363  33.191  67.962  1.00 28.80  ? 273  LEU B CB  1 
ATOM   6246  C  CG  . LEU B  1 273 ? -5.411  31.681  67.805  1.00 27.79  ? 273  LEU B CG  1 
ATOM   6247  C  CD1 . LEU B  1 273 ? -5.632  31.381  66.358  1.00 27.65  ? 273  LEU B CD1 1 
ATOM   6248  C  CD2 . LEU B  1 273 ? -4.134  31.050  68.302  1.00 27.89  ? 273  LEU B CD2 1 
ATOM   6249  N  N   . ARG B  1 274 ? -4.591  36.099  68.957  1.00 32.45  ? 274  ARG B N   1 
ATOM   6250  C  CA  . ARG B  1 274 ? -3.752  37.243  68.668  1.00 32.31  ? 274  ARG B CA  1 
ATOM   6251  C  C   . ARG B  1 274 ? -2.849  37.589  69.822  1.00 33.33  ? 274  ARG B C   1 
ATOM   6252  O  O   . ARG B  1 274 ? -1.806  38.205  69.617  1.00 36.38  ? 274  ARG B O   1 
ATOM   6253  C  CB  . ARG B  1 274 ? -4.588  38.446  68.279  1.00 42.24  ? 274  ARG B CB  1 
ATOM   6254  C  CG  . ARG B  1 274 ? -4.770  38.558  66.797  1.00 47.98  ? 274  ARG B CG  1 
ATOM   6255  C  CD  . ARG B  1 274 ? -5.265  39.917  66.439  1.00 54.96  ? 274  ARG B CD  1 
ATOM   6256  N  NE  . ARG B  1 274 ? -6.673  39.914  66.078  1.00 58.28  ? 274  ARG B NE  1 
ATOM   6257  C  CZ  . ARG B  1 274 ? -7.101  39.805  64.830  1.00 61.21  ? 274  ARG B CZ  1 
ATOM   6258  N  NH1 . ARG B  1 274 ? -6.231  39.675  63.841  1.00 61.52  ? 274  ARG B NH1 1 
ATOM   6259  N  NH2 . ARG B  1 274 ? -8.393  39.827  64.570  1.00 63.60  ? 274  ARG B NH2 1 
ATOM   6260  N  N   . THR B  1 275 ? -3.243  37.183  71.028  1.00 39.70  ? 275  THR B N   1 
ATOM   6261  C  CA  . THR B  1 275 ? -2.502  37.537  72.240  1.00 41.61  ? 275  THR B CA  1 
ATOM   6262  C  C   . THR B  1 275 ? -1.495  36.493  72.714  1.00 38.04  ? 275  THR B C   1 
ATOM   6263  O  O   . THR B  1 275 ? -0.953  36.615  73.805  1.00 37.30  ? 275  THR B O   1 
ATOM   6264  C  CB  . THR B  1 275 ? -3.430  37.819  73.411  1.00 43.84  ? 275  THR B CB  1 
ATOM   6265  O  OG1 . THR B  1 275 ? -3.562  36.627  74.189  1.00 44.66  ? 275  THR B OG1 1 
ATOM   6266  C  CG2 . THR B  1 275 ? -4.786  38.274  72.918  1.00 42.83  ? 275  THR B CG2 1 
ATOM   6267  N  N   . ARG B  1 276 ? -1.290  35.440  71.938  1.00 31.90  ? 276  ARG B N   1 
ATOM   6268  C  CA  . ARG B  1 276 ? -0.274  34.463  72.278  1.00 31.73  ? 276  ARG B CA  1 
ATOM   6269  C  C   . ARG B  1 276 ? 1.050   34.870  71.649  1.00 40.52  ? 276  ARG B C   1 
ATOM   6270  O  O   . ARG B  1 276 ? 1.073   35.408  70.547  1.00 33.09  ? 276  ARG B O   1 
ATOM   6271  C  CB  . ARG B  1 276 ? -0.698  33.087  71.796  1.00 30.63  ? 276  ARG B CB  1 
ATOM   6272  C  CG  . ARG B  1 276 ? -2.026  32.676  72.362  1.00 45.27  ? 276  ARG B CG  1 
ATOM   6273  C  CD  . ARG B  1 276 ? -1.840  32.042  73.712  1.00 45.32  ? 276  ARG B CD  1 
ATOM   6274  N  NE  . ARG B  1 276 ? -3.107  31.781  74.388  1.00 46.85  ? 276  ARG B NE  1 
ATOM   6275  C  CZ  . ARG B  1 276 ? -3.593  32.562  75.346  1.00 50.91  ? 276  ARG B CZ  1 
ATOM   6276  N  NH1 . ARG B  1 276 ? -2.908  33.636  75.713  1.00 54.81  ? 276  ARG B NH1 1 
ATOM   6277  N  NH2 . ARG B  1 276 ? -4.746  32.277  75.946  1.00 50.31  ? 276  ARG B NH2 1 
ATOM   6278  N  N   . PRO B  1 277 ? 2.159   34.632  72.360  1.00 33.09  ? 277  PRO B N   1 
ATOM   6279  C  CA  . PRO B  1 277 ? 3.513   34.815  71.839  1.00 40.07  ? 277  PRO B CA  1 
ATOM   6280  C  C   . PRO B  1 277 ? 3.724   34.090  70.505  1.00 36.20  ? 277  PRO B C   1 
ATOM   6281  O  O   . PRO B  1 277 ? 3.365   32.922  70.413  1.00 32.70  ? 277  PRO B O   1 
ATOM   6282  C  CB  . PRO B  1 277 ? 4.366   34.154  72.922  1.00 39.32  ? 277  PRO B CB  1 
ATOM   6283  C  CG  . PRO B  1 277 ? 3.607   34.377  74.162  1.00 33.75  ? 277  PRO B CG  1 
ATOM   6284  C  CD  . PRO B  1 277 ? 2.173   34.235  73.776  1.00 32.86  ? 277  PRO B CD  1 
ATOM   6285  N  N   . ALA B  1 278 ? 4.309   34.759  69.513  1.00 34.48  ? 278  ALA B N   1 
ATOM   6286  C  CA  . ALA B  1 278 ? 4.518   34.166  68.186  1.00 37.39  ? 278  ALA B CA  1 
ATOM   6287  C  C   . ALA B  1 278 ? 5.172   32.793  68.241  1.00 34.43  ? 278  ALA B C   1 
ATOM   6288  O  O   . ALA B  1 278 ? 4.795   31.857  67.504  1.00 33.07  ? 278  ALA B O   1 
ATOM   6289  C  CB  . ALA B  1 278 ? 5.353   35.096  67.315  1.00 47.51  ? 278  ALA B CB  1 
ATOM   6290  N  N   . GLN B  1 279 ? 6.155   32.670  69.124  1.00 41.74  ? 279  GLN B N   1 
ATOM   6291  C  CA  . GLN B  1 279 ? 6.871   31.415  69.245  1.00 44.83  ? 279  GLN B CA  1 
ATOM   6292  C  C   . GLN B  1 279 ? 5.967   30.292  69.757  1.00 44.34  ? 279  GLN B C   1 
ATOM   6293  O  O   . GLN B  1 279 ? 6.254   29.128  69.520  1.00 46.24  ? 279  GLN B O   1 
ATOM   6294  C  CB  . GLN B  1 279 ? 8.147   31.567  70.086  1.00 53.10  ? 279  GLN B CB  1 
ATOM   6295  C  CG  . GLN B  1 279 ? 8.979   30.280  70.242  1.00 53.98  ? 279  GLN B CG  1 
ATOM   6296  C  CD  . GLN B  1 279 ? 9.280   29.570  68.919  1.00 52.79  ? 279  GLN B CD  1 
ATOM   6297  O  OE1 . GLN B  1 279 ? 9.540   30.211  67.892  1.00 53.30  ? 279  GLN B OE1 1 
ATOM   6298  N  NE2 . GLN B  1 279 ? 9.251   28.235  68.947  1.00 49.08  ? 279  GLN B NE2 1 
ATOM   6299  N  N   . ASP B  1 280 ? 4.863   30.626  70.422  1.00 37.00  ? 280  ASP B N   1 
ATOM   6300  C  CA  . ASP B  1 280 ? 3.942   29.587  70.897  1.00 37.92  ? 280  ASP B CA  1 
ATOM   6301  C  C   . ASP B  1 280 ? 3.205   28.937  69.730  1.00 34.70  ? 280  ASP B C   1 
ATOM   6302  O  O   . ASP B  1 280 ? 3.071   27.699  69.659  1.00 33.22  ? 280  ASP B O   1 
ATOM   6303  C  CB  . ASP B  1 280 ? 2.962   30.140  71.939  1.00 50.95  ? 280  ASP B CB  1 
ATOM   6304  C  CG  . ASP B  1 280 ? 3.625   30.395  73.279  1.00 54.31  ? 280  ASP B CG  1 
ATOM   6305  O  OD1 . ASP B  1 280 ? 4.628   29.709  73.569  1.00 57.39  ? 280  ASP B OD1 1 
ATOM   6306  O  OD2 . ASP B  1 280 ? 3.155   31.270  74.038  1.00 52.31  ? 280  ASP B OD2 1 
ATOM   6307  N  N   . LEU B  1 281 ? 2.748   29.781  68.812  1.00 30.55  ? 281  LEU B N   1 
ATOM   6308  C  CA  . LEU B  1 281 ? 2.090   29.312  67.617  1.00 29.99  ? 281  LEU B CA  1 
ATOM   6309  C  C   . LEU B  1 281 ? 3.059   28.441  66.885  1.00 30.12  ? 281  LEU B C   1 
ATOM   6310  O  O   . LEU B  1 281 ? 2.727   27.330  66.502  1.00 29.36  ? 281  LEU B O   1 
ATOM   6311  C  CB  . LEU B  1 281 ? 1.687   30.473  66.737  1.00 30.52  ? 281  LEU B CB  1 
ATOM   6312  C  CG  . LEU B  1 281 ? 0.799   31.499  67.419  1.00 30.60  ? 281  LEU B CG  1 
ATOM   6313  C  CD1 . LEU B  1 281 ? 0.307   32.480  66.393  1.00 31.08  ? 281  LEU B CD1 1 
ATOM   6314  C  CD2 . LEU B  1 281 ? -0.365  30.826  68.105  1.00 29.54  ? 281  LEU B CD2 1 
ATOM   6315  N  N   . VAL B  1 282 ? 4.282   28.923  66.722  1.00 31.12  ? 282  VAL B N   1 
ATOM   6316  C  CA  . VAL B  1 282 ? 5.284   28.095  66.051  1.00 31.35  ? 282  VAL B CA  1 
ATOM   6317  C  C   . VAL B  1 282 ? 5.536   26.736  66.738  1.00 30.74  ? 282  VAL B C   1 
ATOM   6318  O  O   . VAL B  1 282 ? 5.626   25.703  66.066  1.00 30.34  ? 282  VAL B O   1 
ATOM   6319  C  CB  . VAL B  1 282 ? 6.587   28.849  65.870  1.00 32.61  ? 282  VAL B CB  1 
ATOM   6320  C  CG1 . VAL B  1 282 ? 7.562   28.007  65.111  1.00 32.89  ? 282  VAL B CG1 1 
ATOM   6321  C  CG2 . VAL B  1 282 ? 6.311   30.123  65.124  1.00 33.25  ? 282  VAL B CG2 1 
ATOM   6322  N  N   . ASP B  1 283 ? 5.624   26.738  68.067  1.00 32.01  ? 283  ASP B N   1 
ATOM   6323  C  CA  . ASP B  1 283 ? 5.832   25.514  68.842  1.00 37.89  ? 283  ASP B CA  1 
ATOM   6324  C  C   . ASP B  1 283 ? 4.752   24.474  68.575  1.00 43.14  ? 283  ASP B C   1 
ATOM   6325  O  O   . ASP B  1 283 ? 5.052   23.314  68.264  1.00 46.29  ? 283  ASP B O   1 
ATOM   6326  C  CB  . ASP B  1 283 ? 5.872   25.814  70.343  1.00 48.85  ? 283  ASP B CB  1 
ATOM   6327  C  CG  . ASP B  1 283 ? 7.168   26.470  70.776  1.00 55.65  ? 283  ASP B CG  1 
ATOM   6328  O  OD1 . ASP B  1 283 ? 8.176   26.360  70.037  1.00 59.68  ? 283  ASP B OD1 1 
ATOM   6329  O  OD2 . ASP B  1 283 ? 7.178   27.094  71.863  1.00 55.97  ? 283  ASP B OD2 1 
ATOM   6330  N  N   . HIS B  1 284 ? 3.490   24.878  68.693  1.00 38.94  ? 284  HIS B N   1 
ATOM   6331  C  CA  . HIS B  1 284 ? 2.417   23.902  68.522  1.00 35.76  ? 284  HIS B CA  1 
ATOM   6332  C  C   . HIS B  1 284 ? 2.035   23.703  67.074  1.00 32.90  ? 284  HIS B C   1 
ATOM   6333  O  O   . HIS B  1 284 ? 1.123   22.947  66.779  1.00 31.31  ? 284  HIS B O   1 
ATOM   6334  C  CB  . HIS B  1 284 ? 1.190   24.278  69.339  1.00 43.80  ? 284  HIS B CB  1 
ATOM   6335  C  CG  . HIS B  1 284 ? 1.428   24.235  70.809  1.00 48.83  ? 284  HIS B CG  1 
ATOM   6336  N  ND1 . HIS B  1 284 ? 1.626   23.055  71.492  1.00 51.76  ? 284  HIS B ND1 1 
ATOM   6337  C  CD2 . HIS B  1 284 ? 1.529   25.226  71.726  1.00 50.86  ? 284  HIS B CD2 1 
ATOM   6338  C  CE1 . HIS B  1 284 ? 1.831   23.320  72.770  1.00 54.03  ? 284  HIS B CE1 1 
ATOM   6339  N  NE2 . HIS B  1 284 ? 1.774   24.630  72.939  1.00 53.24  ? 284  HIS B NE2 1 
ATOM   6340  N  N   . GLU B  1 285 ? 2.732   24.378  66.168  1.00 27.92  ? 285  GLU B N   1 
ATOM   6341  C  CA  . GLU B  1 285 ? 2.344   24.360  64.756  1.00 31.94  ? 285  GLU B CA  1 
ATOM   6342  C  C   . GLU B  1 285 ? 2.335   22.968  64.151  1.00 35.08  ? 285  GLU B C   1 
ATOM   6343  O  O   . GLU B  1 285 ? 1.481   22.642  63.329  1.00 26.67  ? 285  GLU B O   1 
ATOM   6344  C  CB  . GLU B  1 285 ? 3.256   25.267  63.923  1.00 68.61  ? 285  GLU B CB  1 
ATOM   6345  C  CG  . GLU B  1 285 ? 2.613   25.746  62.636  1.00 72.36  ? 285  GLU B CG  1 
ATOM   6346  C  CD  . GLU B  1 285 ? 3.611   25.897  61.524  1.00 76.30  ? 285  GLU B CD  1 
ATOM   6347  O  OE1 . GLU B  1 285 ? 4.824   25.912  61.826  1.00 78.23  ? 285  GLU B OE1 1 
ATOM   6348  O  OE2 . GLU B  1 285 ? 3.181   25.983  60.352  1.00 76.81  ? 285  GLU B OE2 1 
ATOM   6349  N  N   . TRP B  1 286 ? 3.283   22.143  64.567  1.00 65.20  ? 286  TRP B N   1 
ATOM   6350  C  CA  . TRP B  1 286 ? 3.495   20.884  63.882  1.00 70.51  ? 286  TRP B CA  1 
ATOM   6351  C  C   . TRP B  1 286 ? 2.565   19.762  64.341  1.00 69.71  ? 286  TRP B C   1 
ATOM   6352  O  O   . TRP B  1 286 ? 2.593   18.672  63.775  1.00 71.07  ? 286  TRP B O   1 
ATOM   6353  C  CB  . TRP B  1 286 ? 4.980   20.499  63.930  1.00 82.99  ? 286  TRP B CB  1 
ATOM   6354  C  CG  . TRP B  1 286 ? 5.763   21.259  62.887  1.00 88.59  ? 286  TRP B CG  1 
ATOM   6355  C  CD1 . TRP B  1 286 ? 6.631   22.299  63.089  1.00 86.87  ? 286  TRP B CD1 1 
ATOM   6356  C  CD2 . TRP B  1 286 ? 5.695   21.064  61.463  1.00 92.59  ? 286  TRP B CD2 1 
ATOM   6357  N  NE1 . TRP B  1 286 ? 7.119   22.746  61.882  1.00 86.21  ? 286  TRP B NE1 1 
ATOM   6358  C  CE2 . TRP B  1 286 ? 6.562   22.005  60.870  1.00 89.80  ? 286  TRP B CE2 1 
ATOM   6359  C  CE3 . TRP B  1 286 ? 4.988   20.173  60.631  1.00 94.13  ? 286  TRP B CE3 1 
ATOM   6360  C  CZ2 . TRP B  1 286 ? 6.745   22.080  59.487  1.00 91.69  ? 286  TRP B CZ2 1 
ATOM   6361  C  CZ3 . TRP B  1 286 ? 5.170   20.251  59.253  1.00 92.57  ? 286  TRP B CZ3 1 
ATOM   6362  C  CH2 . TRP B  1 286 ? 6.041   21.196  58.699  1.00 92.21  ? 286  TRP B CH2 1 
ATOM   6363  N  N   . HIS B  1 287 ? 1.714   20.053  65.327  1.00 56.71  ? 287  HIS B N   1 
ATOM   6364  C  CA  . HIS B  1 287 ? 0.826   19.048  65.921  1.00 52.73  ? 287  HIS B CA  1 
ATOM   6365  C  C   . HIS B  1 287 ? -0.518  18.836  65.232  1.00 43.97  ? 287  HIS B C   1 
ATOM   6366  O  O   . HIS B  1 287 ? -1.199  17.848  65.497  1.00 42.60  ? 287  HIS B O   1 
ATOM   6367  C  CB  . HIS B  1 287 ? 0.555   19.371  67.386  1.00 76.20  ? 287  HIS B CB  1 
ATOM   6368  C  CG  . HIS B  1 287 ? 1.757   19.223  68.259  1.00 86.34  ? 287  HIS B CG  1 
ATOM   6369  N  ND1 . HIS B  1 287 ? 3.040   19.267  67.768  1.00 89.67  ? 287  HIS B ND1 1 
ATOM   6370  C  CD2 . HIS B  1 287 ? 1.862   19.024  69.597  1.00 91.46  ? 287  HIS B CD2 1 
ATOM   6371  C  CE1 . HIS B  1 287 ? 3.894   19.108  68.765  1.00 93.61  ? 287  HIS B CE1 1 
ATOM   6372  N  NE2 . HIS B  1 287 ? 3.206   18.959  69.881  1.00 95.34  ? 287  HIS B NE2 1 
ATOM   6373  N  N   . VAL B  1 288 ? -0.912  19.739  64.350  1.00 41.74  ? 288  VAL B N   1 
ATOM   6374  C  CA  . VAL B  1 288 ? -2.279  19.682  63.838  1.00 42.23  ? 288  VAL B CA  1 
ATOM   6375  C  C   . VAL B  1 288 ? -2.446  18.791  62.593  1.00 43.94  ? 288  VAL B C   1 
ATOM   6376  O  O   . VAL B  1 288 ? -3.537  18.701  62.015  1.00 43.11  ? 288  VAL B O   1 
ATOM   6377  C  CB  . VAL B  1 288 ? -2.911  21.106  63.647  1.00 23.63  ? 288  VAL B CB  1 
ATOM   6378  C  CG1 . VAL B  1 288 ? -2.501  22.036  64.782  1.00 24.14  ? 288  VAL B CG1 1 
ATOM   6379  C  CG2 . VAL B  1 288 ? -2.539  21.706  62.313  1.00 35.88  ? 288  VAL B CG2 1 
ATOM   6380  N  N   . LEU B  1 289 ? -1.375  18.118  62.191  1.00 57.95  ? 289  LEU B N   1 
ATOM   6381  C  CA  . LEU B  1 289 ? -1.440  17.282  60.999  1.00 61.29  ? 289  LEU B CA  1 
ATOM   6382  C  C   . LEU B  1 289 ? -2.172  15.967  61.259  1.00 71.42  ? 289  LEU B C   1 
ATOM   6383  O  O   . LEU B  1 289 ? -1.949  15.328  62.287  1.00 75.19  ? 289  LEU B O   1 
ATOM   6384  C  CB  . LEU B  1 289 ? -0.041  17.032  60.448  1.00 42.26  ? 289  LEU B CB  1 
ATOM   6385  C  CG  . LEU B  1 289 ? 0.453   18.217  59.624  1.00 38.24  ? 289  LEU B CG  1 
ATOM   6386  C  CD1 . LEU B  1 289 ? 1.937   18.098  59.268  1.00 40.48  ? 289  LEU B CD1 1 
ATOM   6387  C  CD2 . LEU B  1 289 ? -0.399  18.330  58.382  1.00 34.32  ? 289  LEU B CD2 1 
ATOM   6388  N  N   . PRO B  1 290 ? -3.053  15.564  60.321  1.00 74.77  ? 290  PRO B N   1 
ATOM   6389  C  CA  . PRO B  1 290 ? -3.909  14.371  60.453  1.00 76.51  ? 290  PRO B CA  1 
ATOM   6390  C  C   . PRO B  1 290 ? -3.146  13.051  60.611  1.00 80.41  ? 290  PRO B C   1 
ATOM   6391  O  O   . PRO B  1 290 ? -3.487  12.261  61.493  1.00 80.81  ? 290  PRO B O   1 
ATOM   6392  C  CB  . PRO B  1 290 ? -4.708  14.358  59.141  1.00 69.26  ? 290  PRO B CB  1 
ATOM   6393  C  CG  . PRO B  1 290 ? -4.636  15.758  58.631  1.00 69.76  ? 290  PRO B CG  1 
ATOM   6394  C  CD  . PRO B  1 290 ? -3.303  16.285  59.062  1.00 69.62  ? 290  PRO B CD  1 
ATOM   6395  N  N   . GLN B  1 291 ? -2.131  12.824  59.777  1.00 79.55  ? 291  GLN B N   1 
ATOM   6396  C  CA  . GLN B  1 291 ? -1.355  11.584  59.824  1.00 81.33  ? 291  GLN B CA  1 
ATOM   6397  C  C   . GLN B  1 291 ? 0.145   11.861  59.939  1.00 80.41  ? 291  GLN B C   1 
ATOM   6398  O  O   . GLN B  1 291 ? 0.578   13.019  59.962  1.00 76.80  ? 291  GLN B O   1 
ATOM   6399  C  CB  . GLN B  1 291 ? -1.630  10.724  58.580  1.00 89.55  ? 291  GLN B CB  1 
ATOM   6400  C  CG  . GLN B  1 291 ? -3.108  10.563  58.217  1.00 90.74  ? 291  GLN B CG  1 
ATOM   6401  C  CD  . GLN B  1 291 ? -3.529  11.450  57.052  1.00 93.43  ? 291  GLN B CD  1 
ATOM   6402  O  OE1 . GLN B  1 291 ? -2.689  11.953  56.304  1.00 94.52  ? 291  GLN B OE1 1 
ATOM   6403  N  NE2 . GLN B  1 291 ? -4.837  11.648  56.896  1.00 94.30  ? 291  GLN B NE2 1 
ATOM   6404  N  N   . GLU B  1 292 ? 0.933   10.792  60.019  1.00 96.16  ? 292  GLU B N   1 
ATOM   6405  C  CA  . GLU B  1 292 ? 2.385   10.919  59.965  1.00 99.72  ? 292  GLU B CA  1 
ATOM   6406  C  C   . GLU B  1 292 ? 2.760   11.163  58.509  1.00 97.20  ? 292  GLU B C   1 
ATOM   6407  O  O   . GLU B  1 292 ? 2.339   10.412  57.627  1.00 97.44  ? 292  GLU B O   1 
ATOM   6408  C  CB  . GLU B  1 292 ? 3.071   9.661   60.519  1.00 91.75  ? 292  GLU B CB  1 
ATOM   6409  C  CG  . GLU B  1 292 ? 4.199   9.960   61.496  1.00 93.36  ? 292  GLU B CG  1 
ATOM   6410  C  CD  . GLU B  1 292 ? 3.833   11.074  62.480  1.00 95.43  ? 292  GLU B CD  1 
ATOM   6411  O  OE1 . GLU B  1 292 ? 3.085   10.801  63.450  1.00 94.60  ? 292  GLU B OE1 1 
ATOM   6412  O  OE2 . GLU B  1 292 ? 4.286   12.228  62.275  1.00 96.02  ? 292  GLU B OE2 1 
ATOM   6413  N  N   . SER B  1 293 ? 3.523   12.223  58.248  1.00 71.86  ? 293  SER B N   1 
ATOM   6414  C  CA  . SER B  1 293 ? 3.771   12.620  56.861  1.00 68.25  ? 293  SER B CA  1 
ATOM   6415  C  C   . SER B  1 293 ? 5.148   13.226  56.519  1.00 68.38  ? 293  SER B C   1 
ATOM   6416  O  O   . SER B  1 293 ? 5.914   13.649  57.394  1.00 65.46  ? 293  SER B O   1 
ATOM   6417  C  CB  . SER B  1 293 ? 2.629   13.507  56.345  1.00 69.28  ? 293  SER B CB  1 
ATOM   6418  O  OG  . SER B  1 293 ? 2.351   14.562  57.247  1.00 68.45  ? 293  SER B OG  1 
ATOM   6419  N  N   . ILE B  1 294 ? 5.425   13.257  55.217  1.00 96.66  ? 294  ILE B N   1 
ATOM   6420  C  CA  . ILE B  1 294 ? 6.723   13.634  54.669  1.00 100.54 ? 294  ILE B CA  1 
ATOM   6421  C  C   . ILE B  1 294 ? 6.675   15.004  53.970  1.00 98.95  ? 294  ILE B C   1 
ATOM   6422  O  O   . ILE B  1 294 ? 7.318   15.965  54.412  1.00 103.96 ? 294  ILE B O   1 
ATOM   6423  C  CB  . ILE B  1 294 ? 7.238   12.520  53.739  1.00 92.97  ? 294  ILE B CB  1 
ATOM   6424  C  CG1 . ILE B  1 294 ? 7.757   11.365  54.587  1.00 94.55  ? 294  ILE B CG1 1 
ATOM   6425  C  CG2 . ILE B  1 294 ? 8.350   13.007  52.852  1.00 94.66  ? 294  ILE B CG2 1 
ATOM   6426  C  CD1 . ILE B  1 294 ? 8.633   11.810  55.764  1.00 94.98  ? 294  ILE B CD1 1 
ATOM   6427  N  N   . PHE B  1 295 ? 5.894   15.092  52.897  1.00 55.74  ? 295  PHE B N   1 
ATOM   6428  C  CA  . PHE B  1 295 ? 5.394   16.369  52.392  1.00 53.53  ? 295  PHE B CA  1 
ATOM   6429  C  C   . PHE B  1 295 ? 4.218   16.636  53.331  1.00 56.47  ? 295  PHE B C   1 
ATOM   6430  O  O   . PHE B  1 295 ? 4.278   16.183  54.470  1.00 58.39  ? 295  PHE B O   1 
ATOM   6431  C  CB  . PHE B  1 295 ? 5.001   16.299  50.916  1.00 77.27  ? 295  PHE B CB  1 
ATOM   6432  C  CG  . PHE B  1 295 ? 5.984   17.012  49.960  1.00 79.74  ? 295  PHE B CG  1 
ATOM   6433  C  CD1 . PHE B  1 295 ? 5.867   18.380  49.695  1.00 79.29  ? 295  PHE B CD1 1 
ATOM   6434  C  CD2 . PHE B  1 295 ? 6.996   16.308  49.311  1.00 76.42  ? 295  PHE B CD2 1 
ATOM   6435  C  CE1 . PHE B  1 295 ? 6.734   19.025  48.826  1.00 74.71  ? 295  PHE B CE1 1 
ATOM   6436  C  CE2 . PHE B  1 295 ? 7.844   16.945  48.432  1.00 72.39  ? 295  PHE B CE2 1 
ATOM   6437  C  CZ  . PHE B  1 295 ? 7.713   18.302  48.195  1.00 72.71  ? 295  PHE B CZ  1 
ATOM   6438  N  N   . ARG B  1 296 ? 3.205   17.414  52.951  1.00 102.19 ? 296  ARG B N   1 
ATOM   6439  C  CA  . ARG B  1 296 ? 2.079   17.645  53.884  1.00 106.37 ? 296  ARG B CA  1 
ATOM   6440  C  C   . ARG B  1 296 ? 2.417   18.490  55.126  1.00 110.74 ? 296  ARG B C   1 
ATOM   6441  O  O   . ARG B  1 296 ? 2.705   17.960  56.203  1.00 114.62 ? 296  ARG B O   1 
ATOM   6442  C  CB  . ARG B  1 296 ? 1.430   16.311  54.330  1.00 79.22  ? 296  ARG B CB  1 
ATOM   6443  C  CG  . ARG B  1 296 ? 0.051   16.015  53.779  1.00 75.03  ? 296  ARG B CG  1 
ATOM   6444  C  CD  . ARG B  1 296 ? -0.044  16.412  52.320  1.00 74.03  ? 296  ARG B CD  1 
ATOM   6445  N  NE  . ARG B  1 296 ? 0.903   15.714  51.453  1.00 70.14  ? 296  ARG B NE  1 
ATOM   6446  C  CZ  . ARG B  1 296 ? 0.594   14.634  50.745  1.00 66.58  ? 296  ARG B CZ  1 
ATOM   6447  N  NH1 . ARG B  1 296 ? -0.631  14.123  50.816  1.00 61.98  ? 296  ARG B NH1 1 
ATOM   6448  N  NH2 . ARG B  1 296 ? 1.510   14.062  49.974  1.00 68.77  ? 296  ARG B NH2 1 
ATOM   6449  N  N   . PHE B  1 297 ? 2.439   19.806  54.933  1.00 83.02  ? 297  PHE B N   1 
ATOM   6450  C  CA  . PHE B  1 297 ? 2.649   20.778  56.004  1.00 76.85  ? 297  PHE B CA  1 
ATOM   6451  C  C   . PHE B  1 297 ? 1.320   21.378  56.517  1.00 68.26  ? 297  PHE B C   1 
ATOM   6452  O  O   . PHE B  1 297 ? 0.347   21.472  55.761  1.00 65.63  ? 297  PHE B O   1 
ATOM   6453  C  CB  . PHE B  1 297 ? 3.543   21.879  55.481  1.00 82.71  ? 297  PHE B CB  1 
ATOM   6454  C  CG  . PHE B  1 297 ? 4.254   21.520  54.205  1.00 86.53  ? 297  PHE B CG  1 
ATOM   6455  C  CD1 . PHE B  1 297 ? 5.468   20.856  54.233  1.00 89.11  ? 297  PHE B CD1 1 
ATOM   6456  C  CD2 . PHE B  1 297 ? 3.716   21.856  52.976  1.00 88.24  ? 297  PHE B CD2 1 
ATOM   6457  C  CE1 . PHE B  1 297 ? 6.139   20.541  53.055  1.00 90.20  ? 297  PHE B CE1 1 
ATOM   6458  C  CE2 . PHE B  1 297 ? 4.381   21.539  51.798  1.00 89.58  ? 297  PHE B CE2 1 
ATOM   6459  C  CZ  . PHE B  1 297 ? 5.597   20.885  51.841  1.00 89.62  ? 297  PHE B CZ  1 
ATOM   6460  N  N   . SER B  1 298 ? 1.290   21.750  57.805  1.00 33.56  ? 298  SER B N   1 
ATOM   6461  C  CA  . SER B  1 298 ? 0.069   22.167  58.544  1.00 26.43  ? 298  SER B CA  1 
ATOM   6462  C  C   . SER B  1 298 ? -0.811  23.294  57.980  1.00 40.16  ? 298  SER B C   1 
ATOM   6463  O  O   . SER B  1 298 ? -2.011  23.108  57.754  1.00 25.96  ? 298  SER B O   1 
ATOM   6464  C  CB  . SER B  1 298 ? 0.445   22.586  59.970  1.00 26.56  ? 298  SER B CB  1 
ATOM   6465  O  OG  . SER B  1 298 ? 0.666   21.468  60.801  1.00 26.03  ? 298  SER B OG  1 
ATOM   6466  N  N   . PHE B  1 299 ? -0.227  24.471  57.803  1.00 27.60  ? 299  PHE B N   1 
ATOM   6467  C  CA  . PHE B  1 299 ? -0.987  25.613  57.331  1.00 27.94  ? 299  PHE B CA  1 
ATOM   6468  C  C   . PHE B  1 299 ? -0.541  26.058  55.947  1.00 29.76  ? 299  PHE B C   1 
ATOM   6469  O  O   . PHE B  1 299 ? 0.631   26.389  55.735  1.00 29.80  ? 299  PHE B O   1 
ATOM   6470  C  CB  . PHE B  1 299 ? -0.880  26.747  58.334  1.00 28.40  ? 299  PHE B CB  1 
ATOM   6471  C  CG  . PHE B  1 299 ? -1.467  26.409  59.668  1.00 27.60  ? 299  PHE B CG  1 
ATOM   6472  C  CD1 . PHE B  1 299 ? -0.715  25.741  60.620  1.00 27.43  ? 299  PHE B CD1 1 
ATOM   6473  C  CD2 . PHE B  1 299 ? -2.784  26.733  59.960  1.00 28.07  ? 299  PHE B CD2 1 
ATOM   6474  C  CE1 . PHE B  1 299 ? -1.259  25.422  61.837  1.00 26.76  ? 299  PHE B CE1 1 
ATOM   6475  C  CE2 . PHE B  1 299 ? -3.335  26.411  61.170  1.00 26.40  ? 299  PHE B CE2 1 
ATOM   6476  C  CZ  . PHE B  1 299 ? -2.575  25.756  62.108  1.00 43.30  ? 299  PHE B CZ  1 
ATOM   6477  N  N   . VAL B  1 300 ? -1.477  26.045  55.001  1.00 28.59  ? 300  VAL B N   1 
ATOM   6478  C  CA  . VAL B  1 300 ? -1.169  26.333  53.605  1.00 29.37  ? 300  VAL B CA  1 
ATOM   6479  C  C   . VAL B  1 300 ? -2.294  27.168  53.023  1.00 31.17  ? 300  VAL B C   1 
ATOM   6480  O  O   . VAL B  1 300 ? -3.241  27.490  53.758  1.00 32.31  ? 300  VAL B O   1 
ATOM   6481  C  CB  . VAL B  1 300 ? -1.034  25.046  52.793  1.00 28.94  ? 300  VAL B CB  1 
ATOM   6482  C  CG1 . VAL B  1 300 ? 0.249   24.307  53.166  1.00 29.09  ? 300  VAL B CG1 1 
ATOM   6483  C  CG2 . VAL B  1 300 ? -2.284  24.209  52.943  1.00 27.76  ? 300  VAL B CG2 1 
ATOM   6484  N  N   . PRO B  1 301 ? -2.188  27.550  51.721  1.00 30.29  ? 301  PRO B N   1 
ATOM   6485  C  CA  . PRO B  1 301 ? -3.332  28.199  51.078  1.00 34.01  ? 301  PRO B CA  1 
ATOM   6486  C  C   . PRO B  1 301 ? -4.615  27.385  51.243  1.00 32.91  ? 301  PRO B C   1 
ATOM   6487  O  O   . PRO B  1 301 ? -4.573  26.153  51.263  1.00 31.89  ? 301  PRO B O   1 
ATOM   6488  C  CB  . PRO B  1 301 ? -2.915  28.239  49.609  1.00 31.25  ? 301  PRO B CB  1 
ATOM   6489  C  CG  . PRO B  1 301 ? -1.460  28.343  49.647  1.00 32.04  ? 301  PRO B CG  1 
ATOM   6490  C  CD  . PRO B  1 301 ? -0.997  27.594  50.844  1.00 31.28  ? 301  PRO B CD  1 
ATOM   6491  N  N   . VAL B  1 302 ? -5.743  28.063  51.385  1.00 29.11  ? 302  VAL B N   1 
ATOM   6492  C  CA  . VAL B  1 302 ? -7.004  27.368  51.565  1.00 28.05  ? 302  VAL B CA  1 
ATOM   6493  C  C   . VAL B  1 302 ? -7.938  27.730  50.420  1.00 28.36  ? 302  VAL B C   1 
ATOM   6494  O  O   . VAL B  1 302 ? -7.928  28.868  49.955  1.00 29.36  ? 302  VAL B O   1 
ATOM   6495  C  CB  . VAL B  1 302 ? -7.631  27.746  52.912  1.00 27.57  ? 302  VAL B CB  1 
ATOM   6496  C  CG1 . VAL B  1 302 ? -7.508  29.221  53.122  1.00 28.55  ? 302  VAL B CG1 1 
ATOM   6497  C  CG2 . VAL B  1 302 ? -9.085  27.310  53.007  1.00 26.70  ? 302  VAL B CG2 1 
ATOM   6498  N  N   . VAL B  1 303 ? -8.765  26.785  49.969  1.00 29.23  ? 303  VAL B N   1 
ATOM   6499  C  CA  . VAL B  1 303 ? -9.709  27.124  48.918  1.00 31.35  ? 303  VAL B CA  1 
ATOM   6500  C  C   . VAL B  1 303 ? -10.919 27.657  49.645  1.00 35.23  ? 303  VAL B C   1 
ATOM   6501  O  O   . VAL B  1 303 ? -11.716 26.897  50.211  1.00 30.38  ? 303  VAL B O   1 
ATOM   6502  C  CB  . VAL B  1 303 ? -10.122 25.870  48.164  1.00 27.20  ? 303  VAL B CB  1 
ATOM   6503  C  CG1 . VAL B  1 303 ? -11.170 26.189  47.117  1.00 29.37  ? 303  VAL B CG1 1 
ATOM   6504  C  CG2 . VAL B  1 303 ? -8.900  25.235  47.538  1.00 38.13  ? 303  VAL B CG2 1 
ATOM   6505  N  N   . ASP B  1 304 ? -11.029 28.985  49.613  1.00 55.93  ? 304  ASP B N   1 
ATOM   6506  C  CA  . ASP B  1 304 ? -11.985 29.736  50.424  1.00 63.73  ? 304  ASP B CA  1 
ATOM   6507  C  C   . ASP B  1 304 ? -13.257 30.123  49.683  1.00 63.86  ? 304  ASP B C   1 
ATOM   6508  O  O   . ASP B  1 304 ? -14.261 30.487  50.296  1.00 62.10  ? 304  ASP B O   1 
ATOM   6509  C  CB  . ASP B  1 304 ? -11.298 31.003  50.964  1.00 74.10  ? 304  ASP B CB  1 
ATOM   6510  C  CG  . ASP B  1 304 ? -10.367 31.664  49.925  1.00 76.94  ? 304  ASP B CG  1 
ATOM   6511  O  OD1 . ASP B  1 304 ? -10.075 31.029  48.883  1.00 77.94  ? 304  ASP B OD1 1 
ATOM   6512  O  OD2 . ASP B  1 304 ? -9.918  32.812  50.158  1.00 75.31  ? 304  ASP B OD2 1 
ATOM   6513  N  N   . GLY B  1 305 ? -13.215 30.002  48.363  1.00 69.26  ? 305  GLY B N   1 
ATOM   6514  C  CA  . GLY B  1 305 ? -14.221 30.621  47.524  1.00 71.11  ? 305  GLY B CA  1 
ATOM   6515  C  C   . GLY B  1 305 ? -13.916 32.084  47.235  1.00 72.01  ? 305  GLY B C   1 
ATOM   6516  O  O   . GLY B  1 305 ? -14.736 32.780  46.644  1.00 75.16  ? 305  GLY B O   1 
ATOM   6517  N  N   . ASP B  1 306 ? -12.742 32.556  47.646  1.00 53.52  ? 306  ASP B N   1 
ATOM   6518  C  CA  . ASP B  1 306 ? -12.353 33.940  47.378  1.00 55.47  ? 306  ASP B CA  1 
ATOM   6519  C  C   . ASP B  1 306 ? -11.060 34.052  46.558  1.00 52.35  ? 306  ASP B C   1 
ATOM   6520  O  O   . ASP B  1 306 ? -11.114 34.330  45.360  1.00 52.12  ? 306  ASP B O   1 
ATOM   6521  C  CB  . ASP B  1 306 ? -12.242 34.744  48.678  1.00 79.15  ? 306  ASP B CB  1 
ATOM   6522  C  CG  . ASP B  1 306 ? -11.782 36.181  48.445  1.00 88.07  ? 306  ASP B CG  1 
ATOM   6523  O  OD1 . ASP B  1 306 ? -12.081 36.749  47.372  1.00 90.86  ? 306  ASP B OD1 1 
ATOM   6524  O  OD2 . ASP B  1 306 ? -11.120 36.747  49.342  1.00 91.27  ? 306  ASP B OD2 1 
ATOM   6525  N  N   . PHE B  1 307 ? -9.905  33.826  47.186  1.00 53.11  ? 307  PHE B N   1 
ATOM   6526  C  CA  . PHE B  1 307 ? -8.629  33.955  46.475  1.00 49.17  ? 307  PHE B CA  1 
ATOM   6527  C  C   . PHE B  1 307 ? -8.552  32.899  45.390  1.00 49.40  ? 307  PHE B C   1 
ATOM   6528  O  O   . PHE B  1 307 ? -8.072  33.163  44.296  1.00 50.24  ? 307  PHE B O   1 
ATOM   6529  C  CB  . PHE B  1 307 ? -7.444  33.823  47.426  1.00 37.28  ? 307  PHE B CB  1 
ATOM   6530  C  CG  . PHE B  1 307 ? -6.113  34.151  46.797  1.00 37.05  ? 307  PHE B CG  1 
ATOM   6531  C  CD1 . PHE B  1 307 ? -5.454  33.233  46.000  1.00 37.94  ? 307  PHE B CD1 1 
ATOM   6532  C  CD2 . PHE B  1 307 ? -5.508  35.362  47.029  1.00 36.90  ? 307  PHE B CD2 1 
ATOM   6533  C  CE1 . PHE B  1 307 ? -4.234  33.528  45.439  1.00 36.75  ? 307  PHE B CE1 1 
ATOM   6534  C  CE2 . PHE B  1 307 ? -4.285  35.656  46.468  1.00 37.99  ? 307  PHE B CE2 1 
ATOM   6535  C  CZ  . PHE B  1 307 ? -3.651  34.739  45.673  1.00 37.92  ? 307  PHE B CZ  1 
ATOM   6536  N  N   . LEU B  1 308 ? -9.013  31.698  45.713  1.00 54.70  ? 308  LEU B N   1 
ATOM   6537  C  CA  . LEU B  1 308 ? -9.253  30.671  44.713  1.00 52.85  ? 308  LEU B CA  1 
ATOM   6538  C  C   . LEU B  1 308 ? -10.762 30.459  44.671  1.00 53.62  ? 308  LEU B C   1 
ATOM   6539  O  O   . LEU B  1 308 ? -11.377 30.180  45.704  1.00 50.33  ? 308  LEU B O   1 
ATOM   6540  C  CB  . LEU B  1 308 ? -8.532  29.373  45.083  1.00 31.78  ? 308  LEU B CB  1 
ATOM   6541  C  CG  . LEU B  1 308 ? -7.029  29.463  45.373  1.00 32.30  ? 308  LEU B CG  1 
ATOM   6542  C  CD1 . LEU B  1 308 ? -6.536  28.183  46.013  1.00 31.22  ? 308  LEU B CD1 1 
ATOM   6543  C  CD2 . LEU B  1 308 ? -6.230  29.771  44.117  1.00 33.55  ? 308  LEU B CD2 1 
ATOM   6544  N  N   . SER B  1 309 ? -11.355 30.618  43.489  1.00 56.64  ? 309  SER B N   1 
ATOM   6545  C  CA  . SER B  1 309 ? -12.806 30.499  43.320  1.00 58.02  ? 309  SER B CA  1 
ATOM   6546  C  C   . SER B  1 309 ? -13.286 29.049  43.425  1.00 57.03  ? 309  SER B C   1 
ATOM   6547  O  O   . SER B  1 309 ? -14.411 28.776  43.864  1.00 55.54  ? 309  SER B O   1 
ATOM   6548  C  CB  . SER B  1 309 ? -13.243 31.100  41.981  1.00 54.42  ? 309  SER B CB  1 
ATOM   6549  O  OG  . SER B  1 309 ? -12.706 30.377  40.887  1.00 53.29  ? 309  SER B OG  1 
ATOM   6550  N  N   . ASP B  1 310 ? -12.422 28.134  42.996  1.00 51.02  ? 310  ASP B N   1 
ATOM   6551  C  CA  . ASP B  1 310 ? -12.633 26.702  43.158  1.00 50.00  ? 310  ASP B CA  1 
ATOM   6552  C  C   . ASP B  1 310 ? -11.260 26.089  43.395  1.00 44.85  ? 310  ASP B C   1 
ATOM   6553  O  O   . ASP B  1 310 ? -10.241 26.787  43.364  1.00 45.56  ? 310  ASP B O   1 
ATOM   6554  C  CB  . ASP B  1 310 ? -13.281 26.100  41.900  1.00 64.33  ? 310  ASP B CB  1 
ATOM   6555  C  CG  . ASP B  1 310 ? -13.893 24.724  42.144  1.00 68.07  ? 310  ASP B CG  1 
ATOM   6556  O  OD1 . ASP B  1 310 ? -13.543 24.091  43.161  1.00 70.51  ? 310  ASP B OD1 1 
ATOM   6557  O  OD2 . ASP B  1 310 ? -14.718 24.271  41.317  1.00 67.57  ? 310  ASP B OD2 1 
ATOM   6558  N  N   . THR B  1 311 ? -11.230 24.785  43.624  1.00 41.97  ? 311  THR B N   1 
ATOM   6559  C  CA  . THR B  1 311 ? -9.979  24.075  43.820  1.00 39.35  ? 311  THR B CA  1 
ATOM   6560  C  C   . THR B  1 311 ? -9.103  24.178  42.586  1.00 39.09  ? 311  THR B C   1 
ATOM   6561  O  O   . THR B  1 311 ? -9.607  24.163  41.464  1.00 40.43  ? 311  THR B O   1 
ATOM   6562  C  CB  . THR B  1 311 ? -10.247 22.606  44.083  1.00 38.21  ? 311  THR B CB  1 
ATOM   6563  O  OG1 . THR B  1 311 ? -10.630 21.967  42.858  1.00 33.60  ? 311  THR B OG1 1 
ATOM   6564  C  CG2 . THR B  1 311 ? -11.365 22.471  45.110  1.00 40.93  ? 311  THR B CG2 1 
ATOM   6565  N  N   . PRO B  1 312 ? -7.785  24.268  42.789  1.00 37.95  ? 312  PRO B N   1 
ATOM   6566  C  CA  . PRO B  1 312 ? -6.819  24.380  41.699  1.00 41.42  ? 312  PRO B CA  1 
ATOM   6567  C  C   . PRO B  1 312 ? -7.050  23.346  40.605  1.00 45.93  ? 312  PRO B C   1 
ATOM   6568  O  O   . PRO B  1 312 ? -6.834  23.656  39.433  1.00 50.10  ? 312  PRO B O   1 
ATOM   6569  C  CB  . PRO B  1 312 ? -5.491  24.112  42.399  1.00 33.70  ? 312  PRO B CB  1 
ATOM   6570  C  CG  . PRO B  1 312 ? -5.700  24.625  43.752  1.00 30.93  ? 312  PRO B CG  1 
ATOM   6571  C  CD  . PRO B  1 312 ? -7.117  24.256  44.099  1.00 29.66  ? 312  PRO B CD  1 
ATOM   6572  N  N   . GLU B  1 313 ? -7.487  22.147  40.976  1.00 41.45  ? 313  GLU B N   1 
ATOM   6573  C  CA  . GLU B  1 313 ? -7.841  21.146  39.980  1.00 49.80  ? 313  GLU B CA  1 
ATOM   6574  C  C   . GLU B  1 313 ? -8.861  21.722  39.014  1.00 47.91  ? 313  GLU B C   1 
ATOM   6575  O  O   . GLU B  1 313 ? -8.645  21.739  37.799  1.00 49.39  ? 313  GLU B O   1 
ATOM   6576  C  CB  . GLU B  1 313 ? -8.404  19.891  40.643  1.00 95.08  ? 313  GLU B CB  1 
ATOM   6577  C  CG  . GLU B  1 313 ? -7.386  19.132  41.464  1.00 108.69 ? 313  GLU B CG  1 
ATOM   6578  C  CD  . GLU B  1 313 ? -6.230  18.617  40.627  1.00 120.27 ? 313  GLU B CD  1 
ATOM   6579  O  OE1 . GLU B  1 313 ? -6.484  18.150  39.495  1.00 124.46 ? 313  GLU B OE1 1 
ATOM   6580  O  OE2 . GLU B  1 313 ? -5.071  18.682  41.099  1.00 123.31 ? 313  GLU B OE2 1 
ATOM   6581  N  N   . ALA B  1 314 ? -9.960  22.225  39.563  1.00 55.47  ? 314  ALA B N   1 
ATOM   6582  C  CA  . ALA B  1 314 ? -11.054 22.713  38.742  1.00 57.11  ? 314  ALA B CA  1 
ATOM   6583  C  C   . ALA B  1 314 ? -10.618 23.912  37.933  1.00 62.47  ? 314  ALA B C   1 
ATOM   6584  O  O   . ALA B  1 314 ? -11.100 24.121  36.820  1.00 67.80  ? 314  ALA B O   1 
ATOM   6585  C  CB  . ALA B  1 314 ? -12.241 23.069  39.598  1.00 50.90  ? 314  ALA B CB  1 
ATOM   6586  N  N   . LEU B  1 315 ? -9.697  24.695  38.482  1.00 73.46  ? 315  LEU B N   1 
ATOM   6587  C  CA  . LEU B  1 315 ? -9.300  25.937  37.833  1.00 70.41  ? 315  LEU B CA  1 
ATOM   6588  C  C   . LEU B  1 315 ? -8.336  25.718  36.683  1.00 72.86  ? 315  LEU B C   1 
ATOM   6589  O  O   . LEU B  1 315 ? -8.408  26.427  35.680  1.00 78.15  ? 315  LEU B O   1 
ATOM   6590  C  CB  . LEU B  1 315 ? -8.711  26.922  38.835  1.00 40.84  ? 315  LEU B CB  1 
ATOM   6591  C  CG  . LEU B  1 315 ? -9.638  27.274  39.993  1.00 34.09  ? 315  LEU B CG  1 
ATOM   6592  C  CD1 . LEU B  1 315 ? -9.158  28.542  40.673  1.00 34.02  ? 315  LEU B CD1 1 
ATOM   6593  C  CD2 . LEU B  1 315 ? -11.078 27.415  39.512  1.00 32.48  ? 315  LEU B CD2 1 
ATOM   6594  N  N   . ILE B  1 316 ? -7.432  24.750  36.824  1.00 42.87  ? 316  ILE B N   1 
ATOM   6595  C  CA  . ILE B  1 316 ? -6.534  24.420  35.719  1.00 42.83  ? 316  ILE B CA  1 
ATOM   6596  C  C   . ILE B  1 316 ? -7.213  23.479  34.719  1.00 47.08  ? 316  ILE B C   1 
ATOM   6597  O  O   . ILE B  1 316 ? -6.708  23.253  33.611  1.00 43.74  ? 316  ILE B O   1 
ATOM   6598  C  CB  . ILE B  1 316 ? -5.185  23.834  36.185  1.00 43.82  ? 316  ILE B CB  1 
ATOM   6599  C  CG1 . ILE B  1 316 ? -5.362  22.421  36.730  1.00 44.35  ? 316  ILE B CG1 1 
ATOM   6600  C  CG2 . ILE B  1 316 ? -4.555  24.723  37.222  1.00 42.13  ? 316  ILE B CG2 1 
ATOM   6601  C  CD1 . ILE B  1 316 ? -4.050  21.717  36.993  1.00 45.33  ? 316  ILE B CD1 1 
ATOM   6602  N  N   . ASN B  1 317 ? -8.350  22.914  35.120  1.00 74.36  ? 317  ASN B N   1 
ATOM   6603  C  CA  . ASN B  1 317 ? -9.172  22.171  34.172  1.00 80.22  ? 317  ASN B CA  1 
ATOM   6604  C  C   . ASN B  1 317 ? -10.108 23.018  33.302  1.00 83.86  ? 317  ASN B C   1 
ATOM   6605  O  O   . ASN B  1 317 ? -10.229 22.763  32.103  1.00 86.31  ? 317  ASN B O   1 
ATOM   6606  C  CB  . ASN B  1 317 ? -9.915  21.017  34.847  1.00 72.43  ? 317  ASN B CB  1 
ATOM   6607  C  CG  . ASN B  1 317 ? -9.355  19.664  34.443  1.00 74.86  ? 317  ASN B CG  1 
ATOM   6608  O  OD1 . ASN B  1 317 ? -9.642  19.165  33.349  1.00 75.49  ? 317  ASN B OD1 1 
ATOM   6609  N  ND2 . ASN B  1 317 ? -8.534  19.070  35.315  1.00 74.67  ? 317  ASN B ND2 1 
ATOM   6610  N  N   . THR B  1 318 ? -10.782 24.005  33.894  1.00 70.20  ? 318  THR B N   1 
ATOM   6611  C  CA  . THR B  1 318 ? -11.664 24.867  33.104  1.00 69.87  ? 318  THR B CA  1 
ATOM   6612  C  C   . THR B  1 318 ? -11.043 26.193  32.696  1.00 71.49  ? 318  THR B C   1 
ATOM   6613  O  O   . THR B  1 318 ? -11.646 26.925  31.921  1.00 73.76  ? 318  THR B O   1 
ATOM   6614  C  CB  . THR B  1 318 ? -12.988 25.213  33.837  1.00 76.72  ? 318  THR B CB  1 
ATOM   6615  O  OG1 . THR B  1 318 ? -12.736 26.212  34.833  1.00 78.27  ? 318  THR B OG1 1 
ATOM   6616  C  CG2 . THR B  1 318 ? -13.611 23.984  34.485  1.00 74.32  ? 318  THR B CG2 1 
ATOM   6617  N  N   . GLY B  1 319 ? -9.847  26.499  33.188  1.00 74.29  ? 319  GLY B N   1 
ATOM   6618  C  CA  . GLY B  1 319 ? -9.304  27.845  33.046  1.00 79.08  ? 319  GLY B CA  1 
ATOM   6619  C  C   . GLY B  1 319 ? -8.961  28.230  31.621  1.00 83.03  ? 319  GLY B C   1 
ATOM   6620  O  O   . GLY B  1 319 ? -8.500  27.390  30.875  1.00 83.30  ? 319  GLY B O   1 
ATOM   6621  N  N   . ASP B  1 320 ? -9.180  29.485  31.229  1.00 93.43  ? 320  ASP B N   1 
ATOM   6622  C  CA  . ASP B  1 320 ? -8.770  29.904  29.886  1.00 97.25  ? 320  ASP B CA  1 
ATOM   6623  C  C   . ASP B  1 320 ? -7.377  30.529  29.887  1.00 96.42  ? 320  ASP B C   1 
ATOM   6624  O  O   . ASP B  1 320 ? -7.159  31.629  30.392  1.00 98.91  ? 320  ASP B O   1 
ATOM   6625  C  CB  . ASP B  1 320 ? -9.767  30.872  29.253  1.00 105.40 ? 320  ASP B CB  1 
ATOM   6626  C  CG  . ASP B  1 320 ? -9.337  31.306  27.859  1.00 111.47 ? 320  ASP B CG  1 
ATOM   6627  O  OD1 . ASP B  1 320 ? -8.993  30.423  27.042  1.00 113.17 ? 320  ASP B OD1 1 
ATOM   6628  O  OD2 . ASP B  1 320 ? -9.319  32.527  27.587  1.00 113.76 ? 320  ASP B OD2 1 
ATOM   6629  N  N   . PHE B  1 321 ? -6.439  29.803  29.303  1.00 81.18  ? 321  PHE B N   1 
ATOM   6630  C  CA  . PHE B  1 321 ? -5.022  30.139  29.376  1.00 79.46  ? 321  PHE B CA  1 
ATOM   6631  C  C   . PHE B  1 321 ? -4.393  30.877  28.192  1.00 81.10  ? 321  PHE B C   1 
ATOM   6632  O  O   . PHE B  1 321 ? -3.167  30.890  28.043  1.00 81.41  ? 321  PHE B O   1 
ATOM   6633  C  CB  . PHE B  1 321 ? -4.207  28.983  29.949  1.00 80.49  ? 321  PHE B CB  1 
ATOM   6634  C  CG  . PHE B  1 321 ? -4.604  28.650  31.356  1.00 76.32  ? 321  PHE B CG  1 
ATOM   6635  C  CD1 . PHE B  1 321 ? -4.296  29.513  32.390  1.00 75.16  ? 321  PHE B CD1 1 
ATOM   6636  C  CD2 . PHE B  1 321 ? -5.341  27.516  31.637  1.00 74.39  ? 321  PHE B CD2 1 
ATOM   6637  C  CE1 . PHE B  1 321 ? -4.681  29.233  33.682  1.00 73.84  ? 321  PHE B CE1 1 
ATOM   6638  C  CE2 . PHE B  1 321 ? -5.730  27.232  32.928  1.00 72.48  ? 321  PHE B CE2 1 
ATOM   6639  C  CZ  . PHE B  1 321 ? -5.399  28.091  33.951  1.00 72.10  ? 321  PHE B CZ  1 
ATOM   6640  N  N   . GLN B  1 322 ? -5.253  31.453  27.351  1.00 86.01  ? 322  GLN B N   1 
ATOM   6641  C  CA  . GLN B  1 322 ? -4.886  31.971  26.034  1.00 88.35  ? 322  GLN B CA  1 
ATOM   6642  C  C   . GLN B  1 322 ? -3.537  32.675  25.999  1.00 88.67  ? 322  GLN B C   1 
ATOM   6643  O  O   . GLN B  1 322 ? -2.589  32.160  25.407  1.00 87.76  ? 322  GLN B O   1 
ATOM   6644  C  CB  . GLN B  1 322 ? -5.958  32.955  25.560  1.00 94.15  ? 322  GLN B CB  1 
ATOM   6645  C  CG  . GLN B  1 322 ? -7.151  32.299  24.920  1.00 94.67  ? 322  GLN B CG  1 
ATOM   6646  C  CD  . GLN B  1 322 ? -6.769  31.547  23.668  1.00 97.93  ? 322  GLN B CD  1 
ATOM   6647  O  OE1 . GLN B  1 322 ? -6.491  30.345  23.711  1.00 97.07  ? 322  GLN B OE1 1 
ATOM   6648  N  NE2 . GLN B  1 322 ? -6.739  32.252  22.541  1.00 101.22 ? 322  GLN B NE2 1 
ATOM   6649  N  N   . ASP B  1 323 ? -3.408  33.824  26.643  1.00 90.03  ? 323  ASP B N   1 
ATOM   6650  C  CA  . ASP B  1 323 ? -2.084  34.408  26.657  1.00 91.65  ? 323  ASP B CA  1 
ATOM   6651  C  C   . ASP B  1 323 ? -1.458  34.119  28.001  1.00 85.14  ? 323  ASP B C   1 
ATOM   6652  O  O   . ASP B  1 323 ? -1.679  34.827  28.986  1.00 82.33  ? 323  ASP B O   1 
ATOM   6653  C  CB  . ASP B  1 323 ? -2.171  35.911  26.415  1.00 109.48 ? 323  ASP B CB  1 
ATOM   6654  C  CG  . ASP B  1 323 ? -2.795  36.247  25.073  1.00 114.80 ? 323  ASP B CG  1 
ATOM   6655  O  OD1 . ASP B  1 323 ? -3.609  35.443  24.561  1.00 114.84 ? 323  ASP B OD1 1 
ATOM   6656  O  OD2 . ASP B  1 323 ? -2.466  37.319  24.528  1.00 118.25 ? 323  ASP B OD2 1 
ATOM   6657  N  N   . LEU B  1 324 ? -0.636  33.078  28.008  1.00 82.98  ? 324  LEU B N   1 
ATOM   6658  C  CA  . LEU B  1 324 ? 0.143   32.714  29.171  1.00 79.21  ? 324  LEU B CA  1 
ATOM   6659  C  C   . LEU B  1 324 ? 1.420   32.068  28.696  1.00 75.99  ? 324  LEU B C   1 
ATOM   6660  O  O   . LEU B  1 324 ? 1.384   31.181  27.850  1.00 76.58  ? 324  LEU B O   1 
ATOM   6661  C  CB  . LEU B  1 324 ? -0.629  31.722  30.033  1.00 76.43  ? 324  LEU B CB  1 
ATOM   6662  C  CG  . LEU B  1 324 ? -0.122  31.604  31.467  1.00 75.30  ? 324  LEU B CG  1 
ATOM   6663  C  CD1 . LEU B  1 324 ? -0.340  32.924  32.192  1.00 76.56  ? 324  LEU B CD1 1 
ATOM   6664  C  CD2 . LEU B  1 324 ? -0.812  30.463  32.189  1.00 71.53  ? 324  LEU B CD2 1 
ATOM   6665  N  N   . GLN B  1 325 ? 2.545   32.474  29.260  1.00 74.87  ? 325  GLN B N   1 
ATOM   6666  C  CA  . GLN B  1 325 ? 3.785   31.766  29.002  1.00 75.19  ? 325  GLN B CA  1 
ATOM   6667  C  C   . GLN B  1 325 ? 4.330   31.237  30.320  1.00 70.55  ? 325  GLN B C   1 
ATOM   6668  O  O   . GLN B  1 325 ? 4.465   31.978  31.311  1.00 72.93  ? 325  GLN B O   1 
ATOM   6669  C  CB  . GLN B  1 325 ? 4.809   32.641  28.271  1.00 88.86  ? 325  GLN B CB  1 
ATOM   6670  C  CG  . GLN B  1 325 ? 4.474   32.921  26.803  1.00 92.96  ? 325  GLN B CG  1 
ATOM   6671  C  CD  . GLN B  1 325 ? 3.742   34.240  26.602  1.00 95.10  ? 325  GLN B CD  1 
ATOM   6672  O  OE1 . GLN B  1 325 ? 4.339   35.315  26.689  1.00 96.77  ? 325  GLN B OE1 1 
ATOM   6673  N  NE2 . GLN B  1 325 ? 2.443   34.161  26.333  1.00 94.22  ? 325  GLN B NE2 1 
ATOM   6674  N  N   . VAL B  1 326 ? 4.617   29.941  30.337  1.00 56.48  ? 326  VAL B N   1 
ATOM   6675  C  CA  . VAL B  1 326 ? 5.034   29.282  31.561  1.00 49.99  ? 326  VAL B CA  1 
ATOM   6676  C  C   . VAL B  1 326 ? 6.282   28.455  31.346  1.00 50.39  ? 326  VAL B C   1 
ATOM   6677  O  O   . VAL B  1 326 ? 6.379   27.707  30.385  1.00 50.97  ? 326  VAL B O   1 
ATOM   6678  C  CB  . VAL B  1 326 ? 3.942   28.345  32.077  1.00 50.75  ? 326  VAL B CB  1 
ATOM   6679  C  CG1 . VAL B  1 326 ? 4.381   27.728  33.373  1.00 48.95  ? 326  VAL B CG1 1 
ATOM   6680  C  CG2 . VAL B  1 326 ? 2.627   29.094  32.254  1.00 51.05  ? 326  VAL B CG2 1 
ATOM   6681  N  N   . LEU B  1 327 ? 7.246   28.584  32.237  1.00 64.69  ? 327  LEU B N   1 
ATOM   6682  C  CA  . LEU B  1 327 ? 8.389   27.693  32.185  1.00 67.87  ? 327  LEU B CA  1 
ATOM   6683  C  C   . LEU B  1 327 ? 8.364   26.835  33.443  1.00 68.03  ? 327  LEU B C   1 
ATOM   6684  O  O   . LEU B  1 327 ? 8.646   27.328  34.528  1.00 71.70  ? 327  LEU B O   1 
ATOM   6685  C  CB  . LEU B  1 327 ? 9.680   28.507  32.081  1.00 54.54  ? 327  LEU B CB  1 
ATOM   6686  C  CG  . LEU B  1 327 ? 11.011  27.836  32.411  1.00 52.89  ? 327  LEU B CG  1 
ATOM   6687  C  CD1 . LEU B  1 327 ? 11.267  26.697  31.463  1.00 53.39  ? 327  LEU B CD1 1 
ATOM   6688  C  CD2 . LEU B  1 327 ? 12.129  28.857  32.358  1.00 54.60  ? 327  LEU B CD2 1 
ATOM   6689  N  N   . VAL B  1 328 ? 8.028   25.554  33.292  1.00 54.45  ? 328  VAL B N   1 
ATOM   6690  C  CA  . VAL B  1 328 ? 7.892   24.638  34.427  1.00 50.39  ? 328  VAL B CA  1 
ATOM   6691  C  C   . VAL B  1 328 ? 8.906   23.515  34.394  1.00 49.97  ? 328  VAL B C   1 
ATOM   6692  O  O   . VAL B  1 328 ? 9.406   23.127  33.332  1.00 47.91  ? 328  VAL B O   1 
ATOM   6693  C  CB  . VAL B  1 328 ? 6.510   23.989  34.472  1.00 44.84  ? 328  VAL B CB  1 
ATOM   6694  C  CG1 . VAL B  1 328 ? 5.509   24.950  35.033  1.00 44.06  ? 328  VAL B CG1 1 
ATOM   6695  C  CG2 . VAL B  1 328 ? 6.103   23.535  33.093  1.00 45.56  ? 328  VAL B CG2 1 
ATOM   6696  N  N   . GLY B  1 329 ? 9.220   22.973  35.557  1.00 45.62  ? 329  GLY B N   1 
ATOM   6697  C  CA  . GLY B  1 329 ? 10.094  21.823  35.525  1.00 45.88  ? 329  GLY B CA  1 
ATOM   6698  C  C   . GLY B  1 329 ? 10.425  21.213  36.852  1.00 44.75  ? 329  GLY B C   1 
ATOM   6699  O  O   . GLY B  1 329 ? 10.018  21.718  37.895  1.00 43.73  ? 329  GLY B O   1 
ATOM   6700  N  N   . VAL B  1 330 ? 11.170  20.113  36.820  1.00 44.99  ? 330  VAL B N   1 
ATOM   6701  C  CA  . VAL B  1 330 ? 11.546  19.442  38.064  1.00 47.46  ? 330  VAL B CA  1 
ATOM   6702  C  C   . VAL B  1 330 ? 13.056  19.186  38.153  1.00 45.32  ? 330  VAL B C   1 
ATOM   6703  O  O   . VAL B  1 330 ? 13.768  19.319  37.163  1.00 50.95  ? 330  VAL B O   1 
ATOM   6704  C  CB  . VAL B  1 330 ? 10.761  18.121  38.246  1.00 43.12  ? 330  VAL B CB  1 
ATOM   6705  C  CG1 . VAL B  1 330 ? 9.317   18.303  37.827  1.00 41.77  ? 330  VAL B CG1 1 
ATOM   6706  C  CG2 . VAL B  1 330 ? 11.393  17.009  37.445  1.00 43.54  ? 330  VAL B CG2 1 
ATOM   6707  N  N   . VAL B  1 331 ? 13.555  18.855  39.338  1.00 44.74  ? 331  VAL B N   1 
ATOM   6708  C  CA  . VAL B  1 331 ? 14.929  18.369  39.429  1.00 48.66  ? 331  VAL B CA  1 
ATOM   6709  C  C   . VAL B  1 331 ? 14.942  16.847  39.368  1.00 52.22  ? 331  VAL B C   1 
ATOM   6710  O  O   . VAL B  1 331 ? 13.881  16.209  39.355  1.00 52.42  ? 331  VAL B O   1 
ATOM   6711  C  CB  . VAL B  1 331 ? 15.660  18.855  40.691  1.00 58.38  ? 331  VAL B CB  1 
ATOM   6712  C  CG1 . VAL B  1 331 ? 15.746  20.361  40.686  1.00 61.00  ? 331  VAL B CG1 1 
ATOM   6713  C  CG2 . VAL B  1 331 ? 14.961  18.367  41.943  1.00 57.56  ? 331  VAL B CG2 1 
ATOM   6714  N  N   . LYS B  1 332 ? 16.138  16.261  39.355  1.00 55.06  ? 332  LYS B N   1 
ATOM   6715  C  CA  . LYS B  1 332 ? 16.261  14.854  38.973  1.00 55.92  ? 332  LYS B CA  1 
ATOM   6716  C  C   . LYS B  1 332 ? 15.680  13.900  40.006  1.00 53.03  ? 332  LYS B C   1 
ATOM   6717  O  O   . LYS B  1 332 ? 14.788  13.115  39.690  1.00 48.68  ? 332  LYS B O   1 
ATOM   6718  C  CB  . LYS B  1 332 ? 17.709  14.487  38.642  1.00 65.20  ? 332  LYS B CB  1 
ATOM   6719  C  CG  . LYS B  1 332 ? 17.849  13.144  37.942  1.00 67.38  ? 332  LYS B CG  1 
ATOM   6720  C  CD  . LYS B  1 332 ? 19.298  12.795  37.645  1.00 69.47  ? 332  LYS B CD  1 
ATOM   6721  C  CE  . LYS B  1 332 ? 19.553  11.311  37.871  1.00 69.53  ? 332  LYS B CE  1 
ATOM   6722  N  NZ  . LYS B  1 332 ? 19.485  10.958  39.324  1.00 68.79  ? 332  LYS B NZ  1 
ATOM   6723  N  N   . ASP B  1 333 ? 16.161  13.973  41.239  1.00 55.52  ? 333  ASP B N   1 
ATOM   6724  C  CA  . ASP B  1 333 ? 15.551  13.181  42.288  1.00 60.53  ? 333  ASP B CA  1 
ATOM   6725  C  C   . ASP B  1 333 ? 14.910  14.148  43.257  1.00 60.00  ? 333  ASP B C   1 
ATOM   6726  O  O   . ASP B  1 333 ? 15.600  14.775  44.055  1.00 63.06  ? 333  ASP B O   1 
ATOM   6727  C  CB  . ASP B  1 333 ? 16.594  12.325  43.013  1.00 79.63  ? 333  ASP B CB  1 
ATOM   6728  C  CG  . ASP B  1 333 ? 17.801  12.004  42.142  1.00 87.62  ? 333  ASP B CG  1 
ATOM   6729  O  OD1 . ASP B  1 333 ? 18.275  12.908  41.420  1.00 91.24  ? 333  ASP B OD1 1 
ATOM   6730  O  OD2 . ASP B  1 333 ? 18.282  10.848  42.182  1.00 89.08  ? 333  ASP B OD2 1 
ATOM   6731  N  N   . GLU B  1 334 ? 13.586  14.243  43.206  1.00 53.72  ? 334  GLU B N   1 
ATOM   6732  C  CA  . GLU B  1 334 ? 12.851  15.170  44.059  1.00 49.63  ? 334  GLU B CA  1 
ATOM   6733  C  C   . GLU B  1 334 ? 12.737  14.670  45.491  1.00 47.94  ? 334  GLU B C   1 
ATOM   6734  O  O   . GLU B  1 334 ? 13.083  15.381  46.438  1.00 38.46  ? 334  GLU B O   1 
ATOM   6735  C  CB  . GLU B  1 334 ? 11.457  15.397  43.487  1.00 54.86  ? 334  GLU B CB  1 
ATOM   6736  C  CG  . GLU B  1 334 ? 11.444  16.258  42.255  1.00 59.17  ? 334  GLU B CG  1 
ATOM   6737  C  CD  . GLU B  1 334 ? 11.426  17.725  42.606  1.00 64.03  ? 334  GLU B CD  1 
ATOM   6738  O  OE1 . GLU B  1 334 ? 11.117  18.035  43.776  1.00 64.67  ? 334  GLU B OE1 1 
ATOM   6739  O  OE2 . GLU B  1 334 ? 11.717  18.564  41.723  1.00 66.81  ? 334  GLU B OE2 1 
ATOM   6740  N  N   . GLY B  1 335 ? 12.288  13.426  45.629  1.00 51.82  ? 335  GLY B N   1 
ATOM   6741  C  CA  . GLY B  1 335 ? 11.832  12.909  46.904  1.00 51.74  ? 335  GLY B CA  1 
ATOM   6742  C  C   . GLY B  1 335 ? 12.892  12.735  47.967  1.00 54.67  ? 335  GLY B C   1 
ATOM   6743  O  O   . GLY B  1 335 ? 12.598  12.823  49.163  1.00 56.80  ? 335  GLY B O   1 
ATOM   6744  N  N   . SER B  1 336 ? 14.126  12.524  47.520  1.00 54.90  ? 336  SER B N   1 
ATOM   6745  C  CA  . SER B  1 336 ? 15.256  12.149  48.369  1.00 50.43  ? 336  SER B CA  1 
ATOM   6746  C  C   . SER B  1 336 ? 15.400  13.008  49.619  1.00 50.34  ? 336  SER B C   1 
ATOM   6747  O  O   . SER B  1 336 ? 15.400  12.491  50.745  1.00 50.25  ? 336  SER B O   1 
ATOM   6748  C  CB  . SER B  1 336 ? 16.514  12.326  47.548  1.00 49.24  ? 336  SER B CB  1 
ATOM   6749  O  OG  . SER B  1 336 ? 16.469  13.593  46.909  1.00 48.94  ? 336  SER B OG  1 
ATOM   6750  N  N   . TYR B  1 337 ? 15.487  14.321  49.402  1.00 55.89  ? 337  TYR B N   1 
ATOM   6751  C  CA  . TYR B  1 337 ? 15.661  15.304  50.467  1.00 58.44  ? 337  TYR B CA  1 
ATOM   6752  C  C   . TYR B  1 337 ? 14.697  15.050  51.621  1.00 57.68  ? 337  TYR B C   1 
ATOM   6753  O  O   . TYR B  1 337 ? 15.063  15.163  52.790  1.00 58.64  ? 337  TYR B O   1 
ATOM   6754  C  CB  . TYR B  1 337 ? 15.440  16.721  49.910  1.00 64.69  ? 337  TYR B CB  1 
ATOM   6755  C  CG  . TYR B  1 337 ? 15.614  17.832  50.930  1.00 68.65  ? 337  TYR B CG  1 
ATOM   6756  C  CD1 . TYR B  1 337 ? 14.557  18.241  51.737  1.00 67.94  ? 337  TYR B CD1 1 
ATOM   6757  C  CD2 . TYR B  1 337 ? 16.838  18.476  51.081  1.00 73.61  ? 337  TYR B CD2 1 
ATOM   6758  C  CE1 . TYR B  1 337 ? 14.716  19.247  52.668  1.00 70.70  ? 337  TYR B CE1 1 
ATOM   6759  C  CE2 . TYR B  1 337 ? 17.010  19.489  52.009  1.00 75.69  ? 337  TYR B CE2 1 
ATOM   6760  C  CZ  . TYR B  1 337 ? 15.946  19.872  52.800  1.00 75.32  ? 337  TYR B CZ  1 
ATOM   6761  O  OH  . TYR B  1 337 ? 16.113  20.880  53.728  1.00 76.90  ? 337  TYR B OH  1 
ATOM   6762  N  N   . PHE B  1 338 ? 13.464  14.687  51.280  1.00 54.52  ? 338  PHE B N   1 
ATOM   6763  C  CA  . PHE B  1 338 ? 12.399  14.602  52.262  1.00 49.17  ? 338  PHE B CA  1 
ATOM   6764  C  C   . PHE B  1 338 ? 12.463  13.351  53.096  1.00 48.14  ? 338  PHE B C   1 
ATOM   6765  O  O   . PHE B  1 338 ? 12.024  13.357  54.237  1.00 49.96  ? 338  PHE B O   1 
ATOM   6766  C  CB  . PHE B  1 338 ? 11.047  14.715  51.576  1.00 46.67  ? 338  PHE B CB  1 
ATOM   6767  C  CG  . PHE B  1 338 ? 10.823  16.044  50.957  1.00 50.49  ? 338  PHE B CG  1 
ATOM   6768  C  CD1 . PHE B  1 338 ? 10.404  17.112  51.730  1.00 53.40  ? 338  PHE B CD1 1 
ATOM   6769  C  CD2 . PHE B  1 338 ? 11.077  16.248  49.615  1.00 52.81  ? 338  PHE B CD2 1 
ATOM   6770  C  CE1 . PHE B  1 338 ? 10.216  18.361  51.168  1.00 56.18  ? 338  PHE B CE1 1 
ATOM   6771  C  CE2 . PHE B  1 338 ? 10.903  17.493  49.047  1.00 55.42  ? 338  PHE B CE2 1 
ATOM   6772  C  CZ  . PHE B  1 338 ? 10.470  18.554  49.825  1.00 56.89  ? 338  PHE B CZ  1 
ATOM   6773  N  N   . LEU B  1 339 ? 13.029  12.286  52.545  1.00 41.56  ? 339  LEU B N   1 
ATOM   6774  C  CA  . LEU B  1 339 ? 12.972  10.996  53.225  1.00 41.31  ? 339  LEU B CA  1 
ATOM   6775  C  C   . LEU B  1 339 ? 13.646  11.001  54.601  1.00 44.49  ? 339  LEU B C   1 
ATOM   6776  O  O   . LEU B  1 339 ? 13.222  10.286  55.509  1.00 42.22  ? 339  LEU B O   1 
ATOM   6777  C  CB  . LEU B  1 339 ? 13.582  9.912   52.352  1.00 39.29  ? 339  LEU B CB  1 
ATOM   6778  C  CG  . LEU B  1 339 ? 12.911  9.734   51.003  1.00 39.00  ? 339  LEU B CG  1 
ATOM   6779  C  CD1 . LEU B  1 339 ? 13.928  9.180   50.032  1.00 41.65  ? 339  LEU B CD1 1 
ATOM   6780  C  CD2 . LEU B  1 339 ? 11.740  8.805   51.149  1.00 33.89  ? 339  LEU B CD2 1 
ATOM   6781  N  N   . VAL B  1 340 ? 14.683  11.816  54.762  1.00 59.75  ? 340  VAL B N   1 
ATOM   6782  C  CA  . VAL B  1 340 ? 15.434  11.844  56.013  1.00 63.51  ? 340  VAL B CA  1 
ATOM   6783  C  C   . VAL B  1 340 ? 14.669  12.556  57.117  1.00 67.13  ? 340  VAL B C   1 
ATOM   6784  O  O   . VAL B  1 340 ? 15.032  12.510  58.290  1.00 71.20  ? 340  VAL B O   1 
ATOM   6785  C  CB  . VAL B  1 340 ? 16.771  12.527  55.819  1.00 57.88  ? 340  VAL B CB  1 
ATOM   6786  C  CG1 . VAL B  1 340 ? 17.634  11.678  54.914  1.00 58.52  ? 340  VAL B CG1 1 
ATOM   6787  C  CG2 . VAL B  1 340 ? 16.563  13.917  55.245  1.00 57.03  ? 340  VAL B CG2 1 
ATOM   6788  N  N   . TYR B  1 341 ? 13.571  13.172  56.724  1.00 58.74  ? 341  TYR B N   1 
ATOM   6789  C  CA  . TYR B  1 341 ? 12.712  13.903  57.630  1.00 55.04  ? 341  TYR B CA  1 
ATOM   6790  C  C   . TYR B  1 341 ? 11.698  12.988  58.310  1.00 56.59  ? 341  TYR B C   1 
ATOM   6791  O  O   . TYR B  1 341 ? 10.640  13.432  58.730  1.00 59.13  ? 341  TYR B O   1 
ATOM   6792  C  CB  . TYR B  1 341 ? 12.088  15.125  56.975  1.00 48.47  ? 341  TYR B CB  1 
ATOM   6793  C  CG  . TYR B  1 341 ? 13.006  16.332  56.997  1.00 49.03  ? 341  TYR B CG  1 
ATOM   6794  C  CD1 . TYR B  1 341 ? 12.990  17.218  58.063  1.00 46.90  ? 341  TYR B CD1 1 
ATOM   6795  C  CD2 . TYR B  1 341 ? 13.888  16.584  55.954  1.00 50.90  ? 341  TYR B CD2 1 
ATOM   6796  C  CE1 . TYR B  1 341 ? 13.820  18.322  58.093  1.00 45.95  ? 341  TYR B CE1 1 
ATOM   6797  C  CE2 . TYR B  1 341 ? 14.722  17.690  55.975  1.00 50.86  ? 341  TYR B CE2 1 
ATOM   6798  C  CZ  . TYR B  1 341 ? 14.684  18.554  57.053  1.00 48.54  ? 341  TYR B CZ  1 
ATOM   6799  O  OH  . TYR B  1 341 ? 15.508  19.660  57.090  1.00 50.25  ? 341  TYR B OH  1 
ATOM   6800  N  N   . GLY B  1 342 ? 12.015  11.696  58.367  1.00 58.45  ? 342  GLY B N   1 
ATOM   6801  C  CA  . GLY B  1 342 ? 11.180  10.740  59.072  1.00 57.20  ? 342  GLY B CA  1 
ATOM   6802  C  C   . GLY B  1 342 ? 10.568  9.517   58.417  1.00 57.13  ? 342  GLY B C   1 
ATOM   6803  O  O   . GLY B  1 342 ? 9.795   8.816   59.058  1.00 58.36  ? 342  GLY B O   1 
ATOM   6804  N  N   . VAL B  1 343 ? 10.905  9.220   57.171  1.00 56.90  ? 343  VAL B N   1 
ATOM   6805  C  CA  . VAL B  1 343 ? 10.814  7.826   56.755  1.00 55.18  ? 343  VAL B CA  1 
ATOM   6806  C  C   . VAL B  1 343 ? 11.940  7.106   57.483  1.00 56.79  ? 343  VAL B C   1 
ATOM   6807  O  O   . VAL B  1 343 ? 13.098  7.497   57.361  1.00 61.78  ? 343  VAL B O   1 
ATOM   6808  C  CB  . VAL B  1 343 ? 11.078  7.640   55.266  1.00 47.29  ? 343  VAL B CB  1 
ATOM   6809  C  CG1 . VAL B  1 343 ? 10.785  6.196   54.861  1.00 45.67  ? 343  VAL B CG1 1 
ATOM   6810  C  CG2 . VAL B  1 343 ? 10.264  8.619   54.458  1.00 46.97  ? 343  VAL B CG2 1 
ATOM   6811  N  N   . PRO B  1 344 ? 11.616  6.069   58.260  1.00 56.10  ? 344  PRO B N   1 
ATOM   6812  C  CA  . PRO B  1 344 ? 12.669  5.315   58.937  1.00 56.34  ? 344  PRO B CA  1 
ATOM   6813  C  C   . PRO B  1 344 ? 13.656  4.697   57.970  1.00 60.82  ? 344  PRO B C   1 
ATOM   6814  O  O   . PRO B  1 344 ? 13.250  4.128   56.955  1.00 63.45  ? 344  PRO B O   1 
ATOM   6815  C  CB  . PRO B  1 344 ? 11.896  4.209   59.642  1.00 35.02  ? 344  PRO B CB  1 
ATOM   6816  C  CG  . PRO B  1 344 ? 10.634  4.846   59.967  1.00 35.51  ? 344  PRO B CG  1 
ATOM   6817  C  CD  . PRO B  1 344 ? 10.294  5.697   58.766  1.00 37.50  ? 344  PRO B CD  1 
ATOM   6818  N  N   . GLY B  1 345 ? 14.940  4.833   58.293  1.00 51.01  ? 345  GLY B N   1 
ATOM   6819  C  CA  . GLY B  1 345 ? 15.987  4.125   57.598  1.00 48.21  ? 345  GLY B CA  1 
ATOM   6820  C  C   . GLY B  1 345 ? 16.720  5.035   56.661  1.00 48.17  ? 345  GLY B C   1 
ATOM   6821  O  O   . GLY B  1 345 ? 17.642  4.605   55.968  1.00 51.69  ? 345  GLY B O   1 
ATOM   6822  N  N   . PHE B  1 346 ? 16.316  6.297   56.634  1.00 51.43  ? 346  PHE B N   1 
ATOM   6823  C  CA  . PHE B  1 346 ? 16.965  7.244   55.744  1.00 56.46  ? 346  PHE B CA  1 
ATOM   6824  C  C   . PHE B  1 346 ? 17.716  8.297   56.535  1.00 62.99  ? 346  PHE B C   1 
ATOM   6825  O  O   . PHE B  1 346 ? 17.113  9.071   57.277  1.00 65.50  ? 346  PHE B O   1 
ATOM   6826  C  CB  . PHE B  1 346 ? 15.958  7.899   54.802  1.00 43.78  ? 346  PHE B CB  1 
ATOM   6827  C  CG  . PHE B  1 346 ? 15.305  6.936   53.845  1.00 42.85  ? 346  PHE B CG  1 
ATOM   6828  C  CD1 . PHE B  1 346 ? 14.385  5.987   54.300  1.00 40.37  ? 346  PHE B CD1 1 
ATOM   6829  C  CD2 . PHE B  1 346 ? 15.592  6.987   52.488  1.00 42.67  ? 346  PHE B CD2 1 
ATOM   6830  C  CE1 . PHE B  1 346 ? 13.776  5.102   53.422  1.00 37.87  ? 346  PHE B CE1 1 
ATOM   6831  C  CE2 . PHE B  1 346 ? 14.980  6.100   51.602  1.00 41.93  ? 346  PHE B CE2 1 
ATOM   6832  C  CZ  . PHE B  1 346 ? 14.070  5.159   52.073  1.00 39.39  ? 346  PHE B CZ  1 
ATOM   6833  N  N   . SER B  1 347 ? 19.037  8.302   56.381  1.00 61.09  ? 347  SER B N   1 
ATOM   6834  C  CA  . SER B  1 347 ? 19.903  9.300   56.996  1.00 62.53  ? 347  SER B CA  1 
ATOM   6835  C  C   . SER B  1 347 ? 20.720  9.961   55.894  1.00 64.17  ? 347  SER B C   1 
ATOM   6836  O  O   . SER B  1 347 ? 20.730  9.480   54.762  1.00 64.86  ? 347  SER B O   1 
ATOM   6837  C  CB  . SER B  1 347 ? 20.825  8.656   58.036  1.00 61.80  ? 347  SER B CB  1 
ATOM   6838  O  OG  . SER B  1 347 ? 21.902  9.514   58.388  1.00 62.77  ? 347  SER B OG  1 
ATOM   6839  N  N   . LYS B  1 348 ? 21.360  11.084  56.199  1.00 56.68  ? 348  LYS B N   1 
ATOM   6840  C  CA  . LYS B  1 348 ? 22.317  11.661  55.268  1.00 60.70  ? 348  LYS B CA  1 
ATOM   6841  C  C   . LYS B  1 348 ? 23.657  10.953  55.446  1.00 63.57  ? 348  LYS B C   1 
ATOM   6842  O  O   . LYS B  1 348 ? 24.535  11.033  54.584  1.00 65.53  ? 348  LYS B O   1 
ATOM   6843  C  CB  . LYS B  1 348 ? 22.480  13.169  55.495  1.00 77.65  ? 348  LYS B CB  1 
ATOM   6844  C  CG  . LYS B  1 348 ? 23.109  13.553  56.842  1.00 80.76  ? 348  LYS B CG  1 
ATOM   6845  C  CD  . LYS B  1 348 ? 24.101  14.718  56.718  1.00 80.47  ? 348  LYS B CD  1 
ATOM   6846  C  CE  . LYS B  1 348 ? 24.338  15.397  58.063  1.00 78.14  ? 348  LYS B CE  1 
ATOM   6847  N  NZ  . LYS B  1 348 ? 24.813  14.458  59.120  1.00 77.25  ? 348  LYS B NZ  1 
ATOM   6848  N  N   . ASP B  1 349 ? 23.795  10.247  56.569  1.00 70.37  ? 349  ASP B N   1 
ATOM   6849  C  CA  . ASP B  1 349 ? 25.064  9.632   56.958  1.00 72.51  ? 349  ASP B CA  1 
ATOM   6850  C  C   . ASP B  1 349 ? 25.259  8.245   56.369  1.00 74.30  ? 349  ASP B C   1 
ATOM   6851  O  O   . ASP B  1 349 ? 26.073  8.075   55.455  1.00 73.90  ? 349  ASP B O   1 
ATOM   6852  C  CB  . ASP B  1 349 ? 25.186  9.598   58.474  1.00 74.95  ? 349  ASP B CB  1 
ATOM   6853  C  CG  . ASP B  1 349 ? 25.171  10.982  59.070  1.00 76.27  ? 349  ASP B CG  1 
ATOM   6854  O  OD1 . ASP B  1 349 ? 25.802  11.889  58.479  1.00 75.36  ? 349  ASP B OD1 1 
ATOM   6855  O  OD2 . ASP B  1 349 ? 24.508  11.171  60.108  1.00 77.97  ? 349  ASP B OD2 1 
ATOM   6856  N  N   . ASN B  1 350 ? 24.518  7.256   56.872  1.00 78.16  ? 350  ASN B N   1 
ATOM   6857  C  CA  . ASN B  1 350 ? 24.523  5.958   56.202  1.00 78.28  ? 350  ASN B CA  1 
ATOM   6858  C  C   . ASN B  1 350 ? 23.916  6.123   54.813  1.00 77.81  ? 350  ASN B C   1 
ATOM   6859  O  O   . ASN B  1 350 ? 23.204  7.081   54.561  1.00 79.62  ? 350  ASN B O   1 
ATOM   6860  C  CB  . ASN B  1 350 ? 23.921  4.799   57.044  1.00 74.66  ? 350  ASN B CB  1 
ATOM   6861  C  CG  . ASN B  1 350 ? 22.459  5.009   57.451  1.00 75.49  ? 350  ASN B CG  1 
ATOM   6862  O  OD1 . ASN B  1 350 ? 21.755  5.854   56.902  1.00 73.35  ? 350  ASN B OD1 1 
ATOM   6863  N  ND2 . ASN B  1 350 ? 21.994  4.183   58.416  1.00 80.86  ? 350  ASN B ND2 1 
ATOM   6864  N  N   . GLU B  1 351 ? 24.229  5.235   53.888  1.00 64.28  ? 351  GLU B N   1 
ATOM   6865  C  CA  . GLU B  1 351 ? 23.769  5.451   52.525  1.00 66.51  ? 351  GLU B CA  1 
ATOM   6866  C  C   . GLU B  1 351 ? 22.362  4.861   52.295  1.00 62.67  ? 351  GLU B C   1 
ATOM   6867  O  O   . GLU B  1 351 ? 21.873  4.760   51.163  1.00 59.88  ? 351  GLU B O   1 
ATOM   6868  C  CB  . GLU B  1 351 ? 24.822  5.056   51.484  1.00 100.65 ? 351  GLU B CB  1 
ATOM   6869  C  CG  . GLU B  1 351 ? 24.852  3.613   51.072  1.00 107.32 ? 351  GLU B CG  1 
ATOM   6870  C  CD  . GLU B  1 351 ? 25.291  3.473   49.630  1.00 112.71 ? 351  GLU B CD  1 
ATOM   6871  O  OE1 . GLU B  1 351 ? 25.918  4.423   49.098  1.00 110.55 ? 351  GLU B OE1 1 
ATOM   6872  O  OE2 . GLU B  1 351 ? 24.994  2.421   49.026  1.00 117.08 ? 351  GLU B OE2 1 
ATOM   6873  N  N   . SER B  1 352 ? 21.747  4.449   53.401  1.00 83.06  ? 352  SER B N   1 
ATOM   6874  C  CA  . SER B  1 352 ? 20.297  4.275   53.491  1.00 81.10  ? 352  SER B CA  1 
ATOM   6875  C  C   . SER B  1 352 ? 19.725  3.135   52.669  1.00 79.44  ? 352  SER B C   1 
ATOM   6876  O  O   . SER B  1 352 ? 18.640  3.261   52.102  1.00 80.55  ? 352  SER B O   1 
ATOM   6877  C  CB  . SER B  1 352 ? 19.575  5.578   53.106  1.00 72.30  ? 352  SER B CB  1 
ATOM   6878  O  OG  . SER B  1 352 ? 19.779  6.605   54.060  1.00 71.42  ? 352  SER B OG  1 
ATOM   6879  N  N   . LEU B  1 353 ? 20.445  2.026   52.600  1.00 65.60  ? 353  LEU B N   1 
ATOM   6880  C  CA  . LEU B  1 353 ? 19.876  0.810   52.040  1.00 62.17  ? 353  LEU B CA  1 
ATOM   6881  C  C   . LEU B  1 353 ? 18.846  0.333   53.046  1.00 59.49  ? 353  LEU B C   1 
ATOM   6882  O  O   . LEU B  1 353 ? 19.101  0.335   54.245  1.00 59.14  ? 353  LEU B O   1 
ATOM   6883  C  CB  . LEU B  1 353 ? 20.964  -0.231  51.800  1.00 68.63  ? 353  LEU B CB  1 
ATOM   6884  C  CG  . LEU B  1 353 ? 22.073  0.380   50.933  1.00 72.82  ? 353  LEU B CG  1 
ATOM   6885  C  CD1 . LEU B  1 353 ? 23.439  -0.261  51.184  1.00 76.22  ? 353  LEU B CD1 1 
ATOM   6886  C  CD2 . LEU B  1 353 ? 21.699  0.305   49.460  1.00 72.80  ? 353  LEU B CD2 1 
ATOM   6887  N  N   . ILE B  1 354 ? 17.665  -0.032  52.573  1.00 59.27  ? 354  ILE B N   1 
ATOM   6888  C  CA  . ILE B  1 354 ? 16.569  -0.304  53.489  1.00 57.52  ? 354  ILE B CA  1 
ATOM   6889  C  C   . ILE B  1 354 ? 15.981  -1.704  53.320  1.00 57.68  ? 354  ILE B C   1 
ATOM   6890  O  O   . ILE B  1 354 ? 16.243  -2.380  52.317  1.00 58.52  ? 354  ILE B O   1 
ATOM   6891  C  CB  . ILE B  1 354 ? 15.471  0.769   53.369  1.00 52.74  ? 354  ILE B CB  1 
ATOM   6892  C  CG1 . ILE B  1 354 ? 14.964  0.873   51.929  1.00 52.92  ? 354  ILE B CG1 1 
ATOM   6893  C  CG2 . ILE B  1 354 ? 16.010  2.109   53.808  1.00 52.89  ? 354  ILE B CG2 1 
ATOM   6894  C  CD1 . ILE B  1 354 ? 13.643  1.613   51.798  1.00 49.98  ? 354  ILE B CD1 1 
ATOM   6895  N  N   . SER B  1 355 ? 15.208  -2.147  54.312  1.00 52.93  ? 355  SER B N   1 
ATOM   6896  C  CA  . SER B  1 355 ? 14.549  -3.451  54.232  1.00 52.33  ? 355  SER B CA  1 
ATOM   6897  C  C   . SER B  1 355 ? 13.351  -3.342  53.302  1.00 47.32  ? 355  SER B C   1 
ATOM   6898  O  O   . SER B  1 355 ? 13.040  -2.249  52.832  1.00 45.65  ? 355  SER B O   1 
ATOM   6899  C  CB  . SER B  1 355 ? 14.106  -3.930  55.623  1.00 61.09  ? 355  SER B CB  1 
ATOM   6900  O  OG  . SER B  1 355 ? 12.992  -3.197  56.106  1.00 61.24  ? 355  SER B OG  1 
ATOM   6901  N  N   . ARG B  1 356 ? 12.667  -4.452  53.037  1.00 49.66  ? 356  ARG B N   1 
ATOM   6902  C  CA  . ARG B  1 356 ? 11.443  -4.358  52.244  1.00 49.22  ? 356  ARG B CA  1 
ATOM   6903  C  C   . ARG B  1 356 ? 10.324  -3.781  53.088  1.00 44.17  ? 356  ARG B C   1 
ATOM   6904  O  O   . ARG B  1 356 ? 9.567   -2.929  52.624  1.00 40.62  ? 356  ARG B O   1 
ATOM   6905  C  CB  . ARG B  1 356 ? 11.012  -5.702  51.664  1.00 57.66  ? 356  ARG B CB  1 
ATOM   6906  C  CG  . ARG B  1 356 ? 9.633   -5.643  51.006  1.00 57.38  ? 356  ARG B CG  1 
ATOM   6907  C  CD  . ARG B  1 356 ? 9.508   -6.632  49.860  1.00 60.85  ? 356  ARG B CD  1 
ATOM   6908  N  NE  . ARG B  1 356 ? 8.345   -6.365  49.012  1.00 61.08  ? 356  ARG B NE  1 
ATOM   6909  C  CZ  . ARG B  1 356 ? 8.308   -5.437  48.056  1.00 59.01  ? 356  ARG B CZ  1 
ATOM   6910  N  NH1 . ARG B  1 356 ? 9.371   -4.672  47.830  1.00 60.53  ? 356  ARG B NH1 1 
ATOM   6911  N  NH2 . ARG B  1 356 ? 7.206   -5.267  47.331  1.00 53.81  ? 356  ARG B NH2 1 
ATOM   6912  N  N   . ALA B  1 357 ? 10.239  -4.245  54.333  1.00 41.29  ? 357  ALA B N   1 
ATOM   6913  C  CA  . ALA B  1 357 ? 9.213   -3.786  55.257  1.00 42.15  ? 357  ALA B CA  1 
ATOM   6914  C  C   . ALA B  1 357 ? 9.368   -2.294  55.528  1.00 43.95  ? 357  ALA B C   1 
ATOM   6915  O  O   . ALA B  1 357 ? 8.375   -1.566  55.700  1.00 43.50  ? 357  ALA B O   1 
ATOM   6916  C  CB  . ALA B  1 357 ? 9.273   -4.578  56.542  1.00 52.34  ? 357  ALA B CB  1 
ATOM   6917  N  N   . GLN B  1 358 ? 10.617  -1.842  55.555  1.00 61.77  ? 358  GLN B N   1 
ATOM   6918  C  CA  . GLN B  1 358 ? 10.898  -0.420  55.666  1.00 66.49  ? 358  GLN B CA  1 
ATOM   6919  C  C   . GLN B  1 358 ? 10.224  0.343   54.541  1.00 68.69  ? 358  GLN B C   1 
ATOM   6920  O  O   . GLN B  1 358 ? 9.509   1.308   54.794  1.00 71.21  ? 358  GLN B O   1 
ATOM   6921  C  CB  . GLN B  1 358 ? 12.399  -0.153  55.659  1.00 60.54  ? 358  GLN B CB  1 
ATOM   6922  C  CG  . GLN B  1 358 ? 12.971  0.000   57.047  1.00 62.70  ? 358  GLN B CG  1 
ATOM   6923  C  CD  . GLN B  1 358 ? 14.468  0.123   57.037  1.00 67.62  ? 358  GLN B CD  1 
ATOM   6924  O  OE1 . GLN B  1 358 ? 15.154  -0.559  56.274  1.00 70.11  ? 358  GLN B OE1 1 
ATOM   6925  N  NE2 . GLN B  1 358 ? 14.993  0.998   57.886  1.00 69.09  ? 358  GLN B NE2 1 
ATOM   6926  N  N   . PHE B  1 359 ? 10.450  -0.104  53.308  1.00 59.64  ? 359  PHE B N   1 
ATOM   6927  C  CA  . PHE B  1 359 ? 9.835   0.499   52.129  1.00 53.29  ? 359  PHE B CA  1 
ATOM   6928  C  C   . PHE B  1 359 ? 8.327   0.493   52.245  1.00 48.88  ? 359  PHE B C   1 
ATOM   6929  O  O   . PHE B  1 359 ? 7.677   1.509   52.005  1.00 48.79  ? 359  PHE B O   1 
ATOM   6930  C  CB  . PHE B  1 359 ? 10.247  -0.258  50.871  1.00 39.23  ? 359  PHE B CB  1 
ATOM   6931  C  CG  . PHE B  1 359 ? 9.460   0.116   49.645  1.00 37.46  ? 359  PHE B CG  1 
ATOM   6932  C  CD1 . PHE B  1 359 ? 9.692   1.308   48.995  1.00 32.97  ? 359  PHE B CD1 1 
ATOM   6933  C  CD2 . PHE B  1 359 ? 8.505   -0.740  49.130  1.00 32.02  ? 359  PHE B CD2 1 
ATOM   6934  C  CE1 . PHE B  1 359 ? 8.975   1.636   47.862  1.00 46.72  ? 359  PHE B CE1 1 
ATOM   6935  C  CE2 . PHE B  1 359 ? 7.790   -0.410  47.999  1.00 31.78  ? 359  PHE B CE2 1 
ATOM   6936  C  CZ  . PHE B  1 359 ? 8.025   0.773   47.366  1.00 32.15  ? 359  PHE B CZ  1 
ATOM   6937  N  N   . LEU B  1 360 ? 7.782   -0.660  52.618  1.00 45.96  ? 360  LEU B N   1 
ATOM   6938  C  CA  . LEU B  1 360 ? 6.338   -0.837  52.756  1.00 44.37  ? 360  LEU B CA  1 
ATOM   6939  C  C   . LEU B  1 360 ? 5.706   0.191   53.677  1.00 42.16  ? 360  LEU B C   1 
ATOM   6940  O  O   . LEU B  1 360 ? 4.630   0.722   53.370  1.00 41.96  ? 360  LEU B O   1 
ATOM   6941  C  CB  . LEU B  1 360 ? 6.009   -2.238  53.274  1.00 42.08  ? 360  LEU B CB  1 
ATOM   6942  C  CG  . LEU B  1 360 ? 6.368   -3.358  52.306  1.00 42.27  ? 360  LEU B CG  1 
ATOM   6943  C  CD1 . LEU B  1 360 ? 5.909   -4.728  52.819  1.00 41.69  ? 360  LEU B CD1 1 
ATOM   6944  C  CD2 . LEU B  1 360 ? 5.781   -3.030  50.942  1.00 41.43  ? 360  LEU B CD2 1 
ATOM   6945  N  N   . ALA B  1 361 ? 6.365   0.458   54.805  1.00 34.88  ? 361  ALA B N   1 
ATOM   6946  C  CA  . ALA B  1 361 ? 5.840   1.422   55.773  1.00 31.51  ? 361  ALA B CA  1 
ATOM   6947  C  C   . ALA B  1 361 ? 6.124   2.863   55.342  1.00 31.01  ? 361  ALA B C   1 
ATOM   6948  O  O   . ALA B  1 361 ? 5.355   3.798   55.624  1.00 26.57  ? 361  ALA B O   1 
ATOM   6949  C  CB  . ALA B  1 361 ? 6.399   1.144   57.144  1.00 34.24  ? 361  ALA B CB  1 
ATOM   6950  N  N   . GLY B  1 362 ? 7.240   3.029   54.649  1.00 37.95  ? 362  GLY B N   1 
ATOM   6951  C  CA  . GLY B  1 362 ? 7.626   4.319   54.124  1.00 37.73  ? 362  GLY B CA  1 
ATOM   6952  C  C   . GLY B  1 362 ? 6.588   4.798   53.137  1.00 33.30  ? 362  GLY B C   1 
ATOM   6953  O  O   . GLY B  1 362 ? 6.300   5.984   53.080  1.00 31.42  ? 362  GLY B O   1 
ATOM   6954  N  N   . VAL B  1 363 ? 6.030   3.872   52.362  1.00 30.21  ? 363  VAL B N   1 
ATOM   6955  C  CA  . VAL B  1 363 ? 4.961   4.218   51.438  1.00 32.28  ? 363  VAL B CA  1 
ATOM   6956  C  C   . VAL B  1 363 ? 3.778   4.767   52.222  1.00 32.75  ? 363  VAL B C   1 
ATOM   6957  O  O   . VAL B  1 363 ? 3.231   5.818   51.868  1.00 31.59  ? 363  VAL B O   1 
ATOM   6958  C  CB  . VAL B  1 363 ? 4.520   3.018   50.585  1.00 30.89  ? 363  VAL B CB  1 
ATOM   6959  C  CG1 . VAL B  1 363 ? 3.293   3.367   49.750  1.00 26.77  ? 363  VAL B CG1 1 
ATOM   6960  C  CG2 . VAL B  1 363 ? 5.653   2.586   49.688  1.00 31.44  ? 363  VAL B CG2 1 
ATOM   6961  N  N   . ARG B  1 364 ? 3.408   4.073   53.300  1.00 33.51  ? 364  ARG B N   1 
ATOM   6962  C  CA  . ARG B  1 364 ? 2.324   4.537   54.168  1.00 33.71  ? 364  ARG B CA  1 
ATOM   6963  C  C   . ARG B  1 364 ? 2.596   5.950   54.652  1.00 34.10  ? 364  ARG B C   1 
ATOM   6964  O  O   . ARG B  1 364 ? 1.683   6.766   54.781  1.00 35.26  ? 364  ARG B O   1 
ATOM   6965  C  CB  . ARG B  1 364 ? 2.128   3.620   55.376  1.00 33.01  ? 364  ARG B CB  1 
ATOM   6966  C  CG  . ARG B  1 364 ? 1.694   2.213   55.040  1.00 37.97  ? 364  ARG B CG  1 
ATOM   6967  C  CD  . ARG B  1 364 ? 0.844   2.201   53.792  1.00 40.70  ? 364  ARG B CD  1 
ATOM   6968  N  NE  . ARG B  1 364 ? -0.498  2.725   54.012  1.00 39.20  ? 364  ARG B NE  1 
ATOM   6969  C  CZ  . ARG B  1 364 ? -1.542  1.960   54.306  1.00 39.37  ? 364  ARG B CZ  1 
ATOM   6970  N  NH1 . ARG B  1 364 ? -1.382  0.645   54.419  1.00 36.54  ? 364  ARG B NH1 1 
ATOM   6971  N  NH2 . ARG B  1 364 ? -2.741  2.506   54.480  1.00 41.65  ? 364  ARG B NH2 1 
ATOM   6972  N  N   . ILE B  1 365 ? 3.860   6.239   54.921  1.00 33.32  ? 365  ILE B N   1 
ATOM   6973  C  CA  . ILE B  1 365 ? 4.209   7.572   55.369  1.00 34.29  ? 365  ILE B CA  1 
ATOM   6974  C  C   . ILE B  1 365 ? 4.114   8.641   54.278  1.00 34.68  ? 365  ILE B C   1 
ATOM   6975  O  O   . ILE B  1 365 ? 3.439   9.638   54.450  1.00 38.58  ? 365  ILE B O   1 
ATOM   6976  C  CB  . ILE B  1 365 ? 5.595   7.596   55.987  1.00 35.79  ? 365  ILE B CB  1 
ATOM   6977  C  CG1 . ILE B  1 365 ? 5.640   6.638   57.181  1.00 37.66  ? 365  ILE B CG1 1 
ATOM   6978  C  CG2 . ILE B  1 365 ? 5.944   9.007   56.398  1.00 34.98  ? 365  ILE B CG2 1 
ATOM   6979  C  CD1 . ILE B  1 365 ? 6.885   6.785   58.033  1.00 40.15  ? 365  ILE B CD1 1 
ATOM   6980  N  N   . GLY B  1 366 ? 4.775   8.434   53.151  1.00 29.35  ? 366  GLY B N   1 
ATOM   6981  C  CA  . GLY B  1 366 ? 4.866   9.468   52.135  1.00 28.72  ? 366  GLY B CA  1 
ATOM   6982  C  C   . GLY B  1 366 ? 3.620   9.643   51.286  1.00 29.03  ? 366  GLY B C   1 
ATOM   6983  O  O   . GLY B  1 366 ? 3.492   10.644  50.570  1.00 29.09  ? 366  GLY B O   1 
ATOM   6984  N  N   . VAL B  1 367 ? 2.720   8.662   51.329  1.00 25.91  ? 367  VAL B N   1 
ATOM   6985  C  CA  . VAL B  1 367 ? 1.412   8.806   50.700  1.00 29.34  ? 367  VAL B CA  1 
ATOM   6986  C  C   . VAL B  1 367 ? 0.403   8.546   51.789  1.00 27.58  ? 367  VAL B C   1 
ATOM   6987  O  O   . VAL B  1 367 ? -0.279  7.525   51.773  1.00 25.52  ? 367  VAL B O   1 
ATOM   6988  C  CB  . VAL B  1 367 ? 1.160   7.799   49.566  1.00 25.33  ? 367  VAL B CB  1 
ATOM   6989  C  CG1 . VAL B  1 367 ? 0.081   8.314   48.650  1.00 24.98  ? 367  VAL B CG1 1 
ATOM   6990  C  CG2 . VAL B  1 367 ? 2.418   7.553   48.780  1.00 38.23  ? 367  VAL B CG2 1 
ATOM   6991  N  N   . PRO B  1 368 ? 0.288   9.485   52.735  1.00 27.61  ? 368  PRO B N   1 
ATOM   6992  C  CA  . PRO B  1 368 ? -0.462  9.239   53.968  1.00 30.52  ? 368  PRO B CA  1 
ATOM   6993  C  C   . PRO B  1 368 ? -1.967  9.148   53.741  1.00 33.37  ? 368  PRO B C   1 
ATOM   6994  O  O   . PRO B  1 368 ? -2.647  8.466   54.505  1.00 32.79  ? 368  PRO B O   1 
ATOM   6995  C  CB  . PRO B  1 368 ? -0.112  10.453  54.834  1.00 24.48  ? 368  PRO B CB  1 
ATOM   6996  C  CG  . PRO B  1 368 ? 0.292   11.533  53.858  1.00 24.92  ? 368  PRO B CG  1 
ATOM   6997  C  CD  . PRO B  1 368 ? 0.479   10.922  52.494  1.00 24.10  ? 368  PRO B CD  1 
ATOM   6998  N  N   . GLN B  1 369 ? -2.469  9.802   52.698  1.00 39.92  ? 369  GLN B N   1 
ATOM   6999  C  CA  . GLN B  1 369 ? -3.896  9.810   52.435  1.00 49.31  ? 369  GLN B CA  1 
ATOM   7000  C  C   . GLN B  1 369 ? -4.330  8.534   51.731  1.00 48.07  ? 369  GLN B C   1 
ATOM   7001  O  O   . GLN B  1 369 ? -5.516  8.326   51.475  1.00 49.39  ? 369  GLN B O   1 
ATOM   7002  C  CB  . GLN B  1 369 ? -4.300  11.042  51.620  1.00 90.02  ? 369  GLN B CB  1 
ATOM   7003  C  CG  . GLN B  1 369 ? -4.465  12.319  52.453  1.00 104.24 ? 369  GLN B CG  1 
ATOM   7004  C  CD  . GLN B  1 369 ? -3.140  12.970  52.838  1.00 115.10 ? 369  GLN B CD  1 
ATOM   7005  O  OE1 . GLN B  1 369 ? -2.124  12.783  52.166  1.00 119.17 ? 369  GLN B OE1 1 
ATOM   7006  N  NE2 . GLN B  1 369 ? -3.151  13.744  53.922  1.00 117.16 ? 369  GLN B NE2 1 
ATOM   7007  N  N   . ALA B  1 370 ? -3.372  7.665   51.439  1.00 44.02  ? 370  ALA B N   1 
ATOM   7008  C  CA  . ALA B  1 370 ? -3.681  6.425   50.743  1.00 40.16  ? 370  ALA B CA  1 
ATOM   7009  C  C   . ALA B  1 370 ? -4.344  5.397   51.653  1.00 36.06  ? 370  ALA B C   1 
ATOM   7010  O  O   . ALA B  1 370 ? -3.936  5.215   52.799  1.00 33.02  ? 370  ALA B O   1 
ATOM   7011  C  CB  . ALA B  1 370 ? -2.431  5.847   50.129  1.00 46.15  ? 370  ALA B CB  1 
ATOM   7012  N  N   . SER B  1 371 ? -5.364  4.720   51.132  1.00 37.13  ? 371  SER B N   1 
ATOM   7013  C  CA  . SER B  1 371 ? -5.966  3.597   51.839  1.00 42.20  ? 371  SER B CA  1 
ATOM   7014  C  C   . SER B  1 371 ? -5.050  2.401   51.684  1.00 44.33  ? 371  SER B C   1 
ATOM   7015  O  O   . SER B  1 371 ? -4.046  2.487   50.980  1.00 46.19  ? 371  SER B O   1 
ATOM   7016  C  CB  . SER B  1 371 ? -7.339  3.266   51.257  1.00 59.25  ? 371  SER B CB  1 
ATOM   7017  O  OG  . SER B  1 371 ? -7.238  2.851   49.906  1.00 61.19  ? 371  SER B OG  1 
ATOM   7018  N  N   . ASP B  1 372 ? -5.404  1.283   52.313  1.00 46.71  ? 372  ASP B N   1 
ATOM   7019  C  CA  . ASP B  1 372 ? -4.606  0.062   52.210  1.00 49.37  ? 372  ASP B CA  1 
ATOM   7020  C  C   . ASP B  1 372 ? -4.427  -0.373  50.760  1.00 45.83  ? 372  ASP B C   1 
ATOM   7021  O  O   . ASP B  1 372 ? -3.338  -0.806  50.354  1.00 44.27  ? 372  ASP B O   1 
ATOM   7022  C  CB  . ASP B  1 372 ? -5.252  -1.070  53.001  1.00 66.45  ? 372  ASP B CB  1 
ATOM   7023  C  CG  . ASP B  1 372 ? -5.149  -0.868  54.485  1.00 71.99  ? 372  ASP B CG  1 
ATOM   7024  O  OD1 . ASP B  1 372 ? -5.225  0.298   54.927  1.00 74.15  ? 372  ASP B OD1 1 
ATOM   7025  O  OD2 . ASP B  1 372 ? -4.988  -1.876  55.205  1.00 73.72  ? 372  ASP B OD2 1 
ATOM   7026  N  N   . LEU B  1 373 ? -5.505  -0.252  49.988  1.00 49.70  ? 373  LEU B N   1 
ATOM   7027  C  CA  . LEU B  1 373 ? -5.502  -0.655  48.588  1.00 44.68  ? 373  LEU B CA  1 
ATOM   7028  C  C   . LEU B  1 373 ? -4.644  0.278   47.723  1.00 46.02  ? 373  LEU B C   1 
ATOM   7029  O  O   . LEU B  1 373 ? -3.789  -0.185  46.976  1.00 46.37  ? 373  LEU B O   1 
ATOM   7030  C  CB  . LEU B  1 373 ? -6.932  -0.753  48.056  1.00 25.63  ? 373  LEU B CB  1 
ATOM   7031  C  CG  . LEU B  1 373 ? -7.079  -1.324  46.645  1.00 23.37  ? 373  LEU B CG  1 
ATOM   7032  C  CD1 . LEU B  1 373 ? -6.331  -2.629  46.505  1.00 21.29  ? 373  LEU B CD1 1 
ATOM   7033  C  CD2 . LEU B  1 373 ? -8.536  -1.535  46.295  1.00 21.75  ? 373  LEU B CD2 1 
ATOM   7034  N  N   . ALA B  1 374 ? -4.867  1.585   47.833  1.00 42.52  ? 374  ALA B N   1 
ATOM   7035  C  CA  . ALA B  1 374 ? -4.058  2.561   47.110  1.00 39.11  ? 374  ALA B CA  1 
ATOM   7036  C  C   . ALA B  1 374 ? -2.602  2.343   47.426  1.00 37.75  ? 374  ALA B C   1 
ATOM   7037  O  O   . ALA B  1 374 ? -1.759  2.440   46.543  1.00 41.85  ? 374  ALA B O   1 
ATOM   7038  C  CB  . ALA B  1 374 ? -4.454  3.967   47.475  1.00 34.95  ? 374  ALA B CB  1 
ATOM   7039  N  N   . ALA B  1 375 ? -2.309  2.042   48.688  1.00 30.58  ? 375  ALA B N   1 
ATOM   7040  C  CA  . ALA B  1 375 ? -0.949  1.698   49.095  1.00 31.47  ? 375  ALA B CA  1 
ATOM   7041  C  C   . ALA B  1 375 ? -0.448  0.453   48.352  1.00 38.53  ? 375  ALA B C   1 
ATOM   7042  O  O   . ALA B  1 375 ? 0.658   0.451   47.802  1.00 37.72  ? 375  ALA B O   1 
ATOM   7043  C  CB  . ALA B  1 375 ? -0.881  1.490   50.586  1.00 23.23  ? 375  ALA B CB  1 
ATOM   7044  N  N   . GLU B  1 376 ? -1.277  -0.590  48.323  1.00 50.07  ? 376  GLU B N   1 
ATOM   7045  C  CA  . GLU B  1 376 ? -0.943  -1.835  47.630  1.00 54.75  ? 376  GLU B CA  1 
ATOM   7046  C  C   . GLU B  1 376 ? -0.632  -1.560  46.163  1.00 50.54  ? 376  GLU B C   1 
ATOM   7047  O  O   . GLU B  1 376 ? 0.211   -2.213  45.547  1.00 52.12  ? 376  GLU B O   1 
ATOM   7048  C  CB  . GLU B  1 376 ? -2.107  -2.824  47.739  1.00 65.85  ? 376  GLU B CB  1 
ATOM   7049  C  CG  . GLU B  1 376 ? -1.704  -4.274  48.005  1.00 74.73  ? 376  GLU B CG  1 
ATOM   7050  C  CD  . GLU B  1 376 ? -1.900  -4.689  49.462  1.00 82.38  ? 376  GLU B CD  1 
ATOM   7051  O  OE1 . GLU B  1 376 ? -2.310  -3.840  50.290  1.00 83.13  ? 376  GLU B OE1 1 
ATOM   7052  O  OE2 . GLU B  1 376 ? -1.642  -5.870  49.780  1.00 86.24  ? 376  GLU B OE2 1 
ATOM   7053  N  N   . ALA B  1 377 ? -1.325  -0.570  45.622  1.00 40.67  ? 377  ALA B N   1 
ATOM   7054  C  CA  . ALA B  1 377 ? -1.170  -0.151  44.245  1.00 38.09  ? 377  ALA B CA  1 
ATOM   7055  C  C   . ALA B  1 377 ? 0.169   0.555   44.050  1.00 39.14  ? 377  ALA B C   1 
ATOM   7056  O  O   . ALA B  1 377 ? 0.878   0.324   43.066  1.00 40.59  ? 377  ALA B O   1 
ATOM   7057  C  CB  . ALA B  1 377 ? -2.330  0.771   43.856  1.00 25.18  ? 377  ALA B CB  1 
ATOM   7058  N  N   . VAL B  1 378 ? 0.511   1.423   44.993  1.00 35.11  ? 378  VAL B N   1 
ATOM   7059  C  CA  . VAL B  1 378 ? 1.755   2.163   44.901  1.00 36.55  ? 378  VAL B CA  1 
ATOM   7060  C  C   . VAL B  1 378 ? 2.923   1.182   45.005  1.00 40.66  ? 378  VAL B C   1 
ATOM   7061  O  O   . VAL B  1 378 ? 3.892   1.263   44.238  1.00 43.98  ? 378  VAL B O   1 
ATOM   7062  C  CB  . VAL B  1 378 ? 1.836   3.261   45.983  1.00 29.29  ? 378  VAL B CB  1 
ATOM   7063  C  CG1 . VAL B  1 378 ? 3.215   3.902   46.002  1.00 29.71  ? 378  VAL B CG1 1 
ATOM   7064  C  CG2 . VAL B  1 378 ? 0.780   4.314   45.730  1.00 26.59  ? 378  VAL B CG2 1 
ATOM   7065  N  N   . VAL B  1 379 ? 2.806   0.231   45.928  1.00 39.88  ? 379  VAL B N   1 
ATOM   7066  C  CA  . VAL B  1 379 ? 3.860   -0.753  46.135  1.00 38.41  ? 379  VAL B CA  1 
ATOM   7067  C  C   . VAL B  1 379 ? 4.017   -1.636  44.911  1.00 36.57  ? 379  VAL B C   1 
ATOM   7068  O  O   . VAL B  1 379 ? 5.121   -1.787  44.399  1.00 37.12  ? 379  VAL B O   1 
ATOM   7069  C  CB  . VAL B  1 379 ? 3.616   -1.629  47.374  1.00 36.12  ? 379  VAL B CB  1 
ATOM   7070  C  CG1 . VAL B  1 379 ? 4.710   -2.681  47.483  1.00 38.31  ? 379  VAL B CG1 1 
ATOM   7071  C  CG2 . VAL B  1 379 ? 3.569   -0.776  48.630  1.00 33.92  ? 379  VAL B CG2 1 
ATOM   7072  N  N   . LEU B  1 380 ? 2.909   -2.210  44.445  1.00 29.94  ? 380  LEU B N   1 
ATOM   7073  C  CA  . LEU B  1 380 ? 2.909   -3.006  43.221  1.00 30.62  ? 380  LEU B CA  1 
ATOM   7074  C  C   . LEU B  1 380 ? 3.584   -2.254  42.085  1.00 31.18  ? 380  LEU B C   1 
ATOM   7075  O  O   . LEU B  1 380 ? 4.374   -2.825  41.335  1.00 42.15  ? 380  LEU B O   1 
ATOM   7076  C  CB  . LEU B  1 380 ? 1.482   -3.367  42.802  1.00 35.54  ? 380  LEU B CB  1 
ATOM   7077  C  CG  . LEU B  1 380 ? 1.330   -3.648  41.302  1.00 29.87  ? 380  LEU B CG  1 
ATOM   7078  C  CD1 . LEU B  1 380 ? 1.452   -5.132  41.007  1.00 30.38  ? 380  LEU B CD1 1 
ATOM   7079  C  CD2 . LEU B  1 380 ? 0.030   -3.101  40.769  1.00 29.03  ? 380  LEU B CD2 1 
ATOM   7080  N  N   . HIS B  1 381 ? 3.287   -0.963  41.975  1.00 35.44  ? 381  HIS B N   1 
ATOM   7081  C  CA  . HIS B  1 381 ? 3.838   -0.159  40.892  1.00 37.75  ? 381  HIS B CA  1 
ATOM   7082  C  C   . HIS B  1 381 ? 5.348   0.053   41.005  1.00 38.13  ? 381  HIS B C   1 
ATOM   7083  O  O   . HIS B  1 381 ? 6.057   -0.080  40.006  1.00 39.13  ? 381  HIS B O   1 
ATOM   7084  C  CB  . HIS B  1 381 ? 3.122   1.188   40.788  1.00 52.05  ? 381  HIS B CB  1 
ATOM   7085  C  CG  . HIS B  1 381 ? 3.214   1.813   39.431  1.00 56.77  ? 381  HIS B CG  1 
ATOM   7086  N  ND1 . HIS B  1 381 ? 2.222   1.678   38.480  1.00 58.23  ? 381  HIS B ND1 1 
ATOM   7087  C  CD2 . HIS B  1 381 ? 4.186   2.562   38.860  1.00 58.21  ? 381  HIS B CD2 1 
ATOM   7088  C  CE1 . HIS B  1 381 ? 2.577   2.323   37.384  1.00 59.32  ? 381  HIS B CE1 1 
ATOM   7089  N  NE2 . HIS B  1 381 ? 3.766   2.865   37.588  1.00 60.18  ? 381  HIS B NE2 1 
ATOM   7090  N  N   . TYR B  1 382 ? 5.833   0.380   42.209  1.00 44.56  ? 382  TYR B N   1 
ATOM   7091  C  CA  . TYR B  1 382 ? 7.245   0.748   42.406  1.00 44.61  ? 382  TYR B CA  1 
ATOM   7092  C  C   . TYR B  1 382 ? 8.192   -0.395  42.777  1.00 47.69  ? 382  TYR B C   1 
ATOM   7093  O  O   . TYR B  1 382 ? 9.411   -0.212  42.782  1.00 49.27  ? 382  TYR B O   1 
ATOM   7094  C  CB  . TYR B  1 382 ? 7.372   1.885   43.422  1.00 34.49  ? 382  TYR B CB  1 
ATOM   7095  C  CG  . TYR B  1 382 ? 6.906   3.216   42.877  1.00 35.14  ? 382  TYR B CG  1 
ATOM   7096  C  CD1 . TYR B  1 382 ? 5.557   3.468   42.692  1.00 35.10  ? 382  TYR B CD1 1 
ATOM   7097  C  CD2 . TYR B  1 382 ? 7.809   4.212   42.538  1.00 34.38  ? 382  TYR B CD2 1 
ATOM   7098  C  CE1 . TYR B  1 382 ? 5.116   4.665   42.188  1.00 36.37  ? 382  TYR B CE1 1 
ATOM   7099  C  CE2 . TYR B  1 382 ? 7.377   5.417   42.038  1.00 41.62  ? 382  TYR B CE2 1 
ATOM   7100  C  CZ  . TYR B  1 382 ? 6.023   5.636   41.862  1.00 40.14  ? 382  TYR B CZ  1 
ATOM   7101  O  OH  . TYR B  1 382 ? 5.552   6.828   41.357  1.00 42.63  ? 382  TYR B OH  1 
ATOM   7102  N  N   . THR B  1 383 ? 7.630   -1.566  43.077  1.00 48.21  ? 383  THR B N   1 
ATOM   7103  C  CA  . THR B  1 383 ? 8.410   -2.761  43.400  1.00 47.04  ? 383  THR B CA  1 
ATOM   7104  C  C   . THR B  1 383 ? 9.007   -3.327  42.127  1.00 48.37  ? 383  THR B C   1 
ATOM   7105  O  O   . THR B  1 383 ? 8.298   -3.431  41.126  1.00 50.18  ? 383  THR B O   1 
ATOM   7106  C  CB  . THR B  1 383 ? 7.495   -3.858  44.021  1.00 33.97  ? 383  THR B CB  1 
ATOM   7107  O  OG1 . THR B  1 383 ? 7.143   -3.504  45.363  1.00 46.38  ? 383  THR B OG1 1 
ATOM   7108  C  CG2 . THR B  1 383 ? 8.181   -5.196  44.056  1.00 34.91  ? 383  THR B CG2 1 
ATOM   7109  N  N   . ASP B  1 384 ? 10.287  -3.704  42.142  1.00 51.34  ? 384  ASP B N   1 
ATOM   7110  C  CA  . ASP B  1 384 ? 10.792  -4.558  41.059  1.00 56.83  ? 384  ASP B CA  1 
ATOM   7111  C  C   . ASP B  1 384 ? 10.631  -6.026  41.450  1.00 59.98  ? 384  ASP B C   1 
ATOM   7112  O  O   . ASP B  1 384 ? 11.339  -6.530  42.327  1.00 63.70  ? 384  ASP B O   1 
ATOM   7113  C  CB  . ASP B  1 384 ? 12.257  -4.282  40.731  1.00 58.63  ? 384  ASP B CB  1 
ATOM   7114  C  CG  . ASP B  1 384 ? 12.878  -5.380  39.856  1.00 60.42  ? 384  ASP B CG  1 
ATOM   7115  O  OD1 . ASP B  1 384 ? 12.158  -5.968  39.016  1.00 61.81  ? 384  ASP B OD1 1 
ATOM   7116  O  OD2 . ASP B  1 384 ? 14.089  -5.656  40.012  1.00 60.48  ? 384  ASP B OD2 1 
ATOM   7117  N  N   . TRP B  1 385 ? 9.727   -6.716  40.761  1.00 57.77  ? 385  TRP B N   1 
ATOM   7118  C  CA  . TRP B  1 385 ? 9.250   -8.008  41.229  1.00 56.07  ? 385  TRP B CA  1 
ATOM   7119  C  C   . TRP B  1 385 ? 10.220  -9.130  40.961  1.00 62.30  ? 385  TRP B C   1 
ATOM   7120  O  O   . TRP B  1 385 ? 10.074  -10.235 41.496  1.00 65.70  ? 385  TRP B O   1 
ATOM   7121  C  CB  . TRP B  1 385 ? 7.892   -8.314  40.628  1.00 43.55  ? 385  TRP B CB  1 
ATOM   7122  C  CG  . TRP B  1 385 ? 6.876   -7.393  41.157  1.00 41.76  ? 385  TRP B CG  1 
ATOM   7123  C  CD1 . TRP B  1 385 ? 6.406   -6.265  40.563  1.00 43.00  ? 385  TRP B CD1 1 
ATOM   7124  C  CD2 . TRP B  1 385 ? 6.218   -7.486  42.425  1.00 39.52  ? 385  TRP B CD2 1 
ATOM   7125  N  NE1 . TRP B  1 385 ? 5.479   -5.653  41.373  1.00 40.95  ? 385  TRP B NE1 1 
ATOM   7126  C  CE2 . TRP B  1 385 ? 5.344   -6.386  42.522  1.00 38.10  ? 385  TRP B CE2 1 
ATOM   7127  C  CE3 . TRP B  1 385 ? 6.273   -8.397  43.481  1.00 37.69  ? 385  TRP B CE3 1 
ATOM   7128  C  CZ2 . TRP B  1 385 ? 4.531   -6.175  43.632  1.00 34.55  ? 385  TRP B CZ2 1 
ATOM   7129  C  CZ3 . TRP B  1 385 ? 5.468   -8.185  44.577  1.00 34.98  ? 385  TRP B CZ3 1 
ATOM   7130  C  CH2 . TRP B  1 385 ? 4.607   -7.084  44.645  1.00 33.63  ? 385  TRP B CH2 1 
ATOM   7131  N  N   . LEU B  1 386 ? 11.214  -8.843  40.134  1.00 51.41  ? 386  LEU B N   1 
ATOM   7132  C  CA  . LEU B  1 386 ? 12.223  -9.832  39.843  1.00 53.85  ? 386  LEU B CA  1 
ATOM   7133  C  C   . LEU B  1 386 ? 13.180  -9.908  41.029  1.00 58.97  ? 386  LEU B C   1 
ATOM   7134  O  O   . LEU B  1 386 ? 13.651  -10.995 41.377  1.00 60.72  ? 386  LEU B O   1 
ATOM   7135  C  CB  . LEU B  1 386 ? 12.942  -9.483  38.547  1.00 52.30  ? 386  LEU B CB  1 
ATOM   7136  C  CG  . LEU B  1 386 ? 13.247  -10.677 37.646  1.00 55.26  ? 386  LEU B CG  1 
ATOM   7137  C  CD1 . LEU B  1 386 ? 13.527  -10.204 36.228  1.00 56.29  ? 386  LEU B CD1 1 
ATOM   7138  C  CD2 . LEU B  1 386 ? 14.422  -11.475 38.198  1.00 57.77  ? 386  LEU B CD2 1 
ATOM   7139  N  N   . HIS B  1 387 ? 13.439  -8.755  41.656  1.00 67.87  ? 387  HIS B N   1 
ATOM   7140  C  CA  . HIS B  1 387 ? 14.235  -8.678  42.887  1.00 69.10  ? 387  HIS B CA  1 
ATOM   7141  C  C   . HIS B  1 387 ? 13.559  -7.813  43.961  1.00 64.18  ? 387  HIS B C   1 
ATOM   7142  O  O   . HIS B  1 387 ? 14.015  -6.706  44.250  1.00 65.05  ? 387  HIS B O   1 
ATOM   7143  C  CB  . HIS B  1 387 ? 15.623  -8.112  42.597  1.00 77.34  ? 387  HIS B CB  1 
ATOM   7144  C  CG  . HIS B  1 387 ? 16.316  -8.770  41.449  1.00 85.96  ? 387  HIS B CG  1 
ATOM   7145  N  ND1 . HIS B  1 387 ? 15.995  -8.503  40.136  1.00 89.98  ? 387  HIS B ND1 1 
ATOM   7146  C  CD2 . HIS B  1 387 ? 17.319  -9.678  41.415  1.00 92.18  ? 387  HIS B CD2 1 
ATOM   7147  C  CE1 . HIS B  1 387 ? 16.768  -9.222  39.342  1.00 94.66  ? 387  HIS B CE1 1 
ATOM   7148  N  NE2 . HIS B  1 387 ? 17.580  -9.945  40.092  1.00 96.26  ? 387  HIS B NE2 1 
ATOM   7149  N  N   . PRO B  1 388 ? 12.476  -8.324  44.565  1.00 46.91  ? 388  PRO B N   1 
ATOM   7150  C  CA  . PRO B  1 388 ? 11.655  -7.587  45.537  1.00 44.16  ? 388  PRO B CA  1 
ATOM   7151  C  C   . PRO B  1 388 ? 12.384  -7.126  46.810  1.00 46.73  ? 388  PRO B C   1 
ATOM   7152  O  O   . PRO B  1 388 ? 11.890  -6.226  47.488  1.00 43.10  ? 388  PRO B O   1 
ATOM   7153  C  CB  . PRO B  1 388 ? 10.572  -8.606  45.918  1.00 48.83  ? 388  PRO B CB  1 
ATOM   7154  C  CG  . PRO B  1 388 ? 10.539  -9.588  44.794  1.00 49.45  ? 388  PRO B CG  1 
ATOM   7155  C  CD  . PRO B  1 388 ? 11.953  -9.681  44.324  1.00 52.59  ? 388  PRO B CD  1 
ATOM   7156  N  N   . GLU B  1 389 ? 13.503  -7.759  47.155  1.00 63.55  ? 389  GLU B N   1 
ATOM   7157  C  CA  . GLU B  1 389 ? 14.219  -7.438  48.393  1.00 66.32  ? 389  GLU B CA  1 
ATOM   7158  C  C   . GLU B  1 389 ? 15.438  -6.509  48.260  1.00 65.15  ? 389  GLU B C   1 
ATOM   7159  O  O   . GLU B  1 389 ? 16.016  -6.100  49.269  1.00 62.00  ? 389  GLU B O   1 
ATOM   7160  C  CB  . GLU B  1 389 ? 14.656  -8.735  49.079  1.00 74.40  ? 389  GLU B CB  1 
ATOM   7161  C  CG  . GLU B  1 389 ? 13.530  -9.700  49.370  1.00 75.57  ? 389  GLU B CG  1 
ATOM   7162  C  CD  . GLU B  1 389 ? 12.782  -9.345  50.631  1.00 76.13  ? 389  GLU B CD  1 
ATOM   7163  O  OE1 . GLU B  1 389 ? 13.007  -8.237  51.170  1.00 76.15  ? 389  GLU B OE1 1 
ATOM   7164  O  OE2 . GLU B  1 389 ? 11.978  -10.182 51.088  1.00 75.98  ? 389  GLU B OE2 1 
ATOM   7165  N  N   . ASP B  1 390 ? 15.813  -6.167  47.031  1.00 69.40  ? 390  ASP B N   1 
ATOM   7166  C  CA  . ASP B  1 390 ? 17.047  -5.422  46.791  1.00 75.65  ? 390  ASP B CA  1 
ATOM   7167  C  C   . ASP B  1 390 ? 16.995  -4.022  47.419  1.00 78.62  ? 390  ASP B C   1 
ATOM   7168  O  O   . ASP B  1 390 ? 16.229  -3.167  46.974  1.00 81.43  ? 390  ASP B O   1 
ATOM   7169  C  CB  . ASP B  1 390 ? 17.314  -5.354  45.279  1.00 82.03  ? 390  ASP B CB  1 
ATOM   7170  C  CG  . ASP B  1 390 ? 18.272  -4.231  44.882  1.00 86.87  ? 390  ASP B CG  1 
ATOM   7171  O  OD1 . ASP B  1 390 ? 19.220  -3.919  45.643  1.00 90.09  ? 390  ASP B OD1 1 
ATOM   7172  O  OD2 . ASP B  1 390 ? 18.077  -3.667  43.782  1.00 86.70  ? 390  ASP B OD2 1 
ATOM   7173  N  N   . PRO B  1 391 ? 17.840  -3.779  48.440  1.00 79.53  ? 391  PRO B N   1 
ATOM   7174  C  CA  . PRO B  1 391 ? 17.820  -2.562  49.259  1.00 77.43  ? 391  PRO B CA  1 
ATOM   7175  C  C   . PRO B  1 391 ? 18.107  -1.296  48.473  1.00 74.72  ? 391  PRO B C   1 
ATOM   7176  O  O   . PRO B  1 391 ? 17.458  -0.279  48.708  1.00 76.02  ? 391  PRO B O   1 
ATOM   7177  C  CB  . PRO B  1 391 ? 18.941  -2.807  50.267  1.00 73.71  ? 391  PRO B CB  1 
ATOM   7178  C  CG  . PRO B  1 391 ? 19.039  -4.271  50.352  1.00 74.01  ? 391  PRO B CG  1 
ATOM   7179  C  CD  . PRO B  1 391 ? 18.832  -4.736  48.948  1.00 74.81  ? 391  PRO B CD  1 
ATOM   7180  N  N   . THR B  1 392 ? 19.067  -1.355  47.562  1.00 64.52  ? 392  THR B N   1 
ATOM   7181  C  CA  . THR B  1 392 ? 19.382  -0.205  46.727  1.00 63.09  ? 392  THR B CA  1 
ATOM   7182  C  C   . THR B  1 392 ? 18.154  0.244   45.935  1.00 66.34  ? 392  THR B C   1 
ATOM   7183  O  O   . THR B  1 392 ? 17.809  1.440   45.928  1.00 68.24  ? 392  THR B O   1 
ATOM   7184  C  CB  . THR B  1 392 ? 20.519  -0.532  45.761  1.00 54.87  ? 392  THR B CB  1 
ATOM   7185  O  OG1 . THR B  1 392 ? 21.412  -1.461  46.388  1.00 54.16  ? 392  THR B OG1 1 
ATOM   7186  C  CG2 . THR B  1 392 ? 21.273  0.724   45.374  1.00 47.55  ? 392  THR B CG2 1 
ATOM   7187  N  N   . HIS B  1 393 ? 17.486  -0.711  45.284  1.00 71.58  ? 393  HIS B N   1 
ATOM   7188  C  CA  . HIS B  1 393 ? 16.273  -0.385  44.544  1.00 69.00  ? 393  HIS B CA  1 
ATOM   7189  C  C   . HIS B  1 393 ? 15.204  0.137   45.474  1.00 61.37  ? 393  HIS B C   1 
ATOM   7190  O  O   . HIS B  1 393 ? 14.694  1.207   45.235  1.00 62.19  ? 393  HIS B O   1 
ATOM   7191  C  CB  . HIS B  1 393 ? 15.711  -1.551  43.733  1.00 75.13  ? 393  HIS B CB  1 
ATOM   7192  C  CG  . HIS B  1 393 ? 14.458  -1.204  42.978  1.00 78.61  ? 393  HIS B CG  1 
ATOM   7193  N  ND1 . HIS B  1 393 ? 14.423  -0.240  41.992  1.00 80.31  ? 393  HIS B ND1 1 
ATOM   7194  C  CD2 . HIS B  1 393 ? 13.193  -1.684  43.074  1.00 79.31  ? 393  HIS B CD2 1 
ATOM   7195  C  CE1 . HIS B  1 393 ? 13.197  -0.147  41.509  1.00 79.56  ? 393  HIS B CE1 1 
ATOM   7196  N  NE2 . HIS B  1 393 ? 12.431  -1.012  42.148  1.00 79.19  ? 393  HIS B NE2 1 
ATOM   7197  N  N   . LEU B  1 394 ? 14.874  -0.602  46.530  1.00 49.76  ? 394  LEU B N   1 
ATOM   7198  C  CA  . LEU B  1 394 ? 13.852  -0.151  47.474  1.00 45.98  ? 394  LEU B CA  1 
ATOM   7199  C  C   . LEU B  1 394 ? 14.070  1.290   47.916  1.00 43.75  ? 394  LEU B C   1 
ATOM   7200  O  O   . LEU B  1 394 ? 13.117  2.064   48.008  1.00 45.81  ? 394  LEU B O   1 
ATOM   7201  C  CB  . LEU B  1 394 ? 13.825  -1.037  48.705  1.00 37.66  ? 394  LEU B CB  1 
ATOM   7202  C  CG  . LEU B  1 394 ? 13.364  -2.468  48.498  1.00 37.54  ? 394  LEU B CG  1 
ATOM   7203  C  CD1 . LEU B  1 394 ? 13.714  -3.269  49.732  1.00 62.80  ? 394  LEU B CD1 1 
ATOM   7204  C  CD2 . LEU B  1 394 ? 11.878  -2.515  48.243  1.00 36.09  ? 394  LEU B CD2 1 
ATOM   7205  N  N   . ARG B  1 395 ? 15.323  1.650   48.176  1.00 39.11  ? 395  ARG B N   1 
ATOM   7206  C  CA  . ARG B  1 395 ? 15.650  3.017   48.556  1.00 39.14  ? 395  ARG B CA  1 
ATOM   7207  C  C   . ARG B  1 395 ? 15.343  3.984   47.426  1.00 39.27  ? 395  ARG B C   1 
ATOM   7208  O  O   . ARG B  1 395 ? 14.548  4.926   47.590  1.00 38.30  ? 395  ARG B O   1 
ATOM   7209  C  CB  . ARG B  1 395 ? 17.115  3.133   48.979  1.00 40.56  ? 395  ARG B CB  1 
ATOM   7210  C  CG  . ARG B  1 395 ? 17.570  4.539   49.261  1.00 40.82  ? 395  ARG B CG  1 
ATOM   7211  C  CD  . ARG B  1 395 ? 18.580  4.974   48.216  1.00 56.63  ? 395  ARG B CD  1 
ATOM   7212  N  NE  . ARG B  1 395 ? 19.908  4.422   48.482  1.00 58.85  ? 395  ARG B NE  1 
ATOM   7213  C  CZ  . ARG B  1 395 ? 20.902  4.360   47.594  1.00 60.85  ? 395  ARG B CZ  1 
ATOM   7214  N  NH1 . ARG B  1 395 ? 20.728  4.806   46.351  1.00 61.79  ? 395  ARG B NH1 1 
ATOM   7215  N  NH2 . ARG B  1 395 ? 22.074  3.837   47.946  1.00 61.44  ? 395  ARG B NH2 1 
ATOM   7216  N  N   . ASP B  1 396 ? 15.950  3.743   46.271  1.00 40.54  ? 396  ASP B N   1 
ATOM   7217  C  CA  . ASP B  1 396 ? 15.810  4.690   45.168  1.00 46.66  ? 396  ASP B CA  1 
ATOM   7218  C  C   . ASP B  1 396 ? 14.348  4.847   44.774  1.00 41.45  ? 396  ASP B C   1 
ATOM   7219  O  O   . ASP B  1 396 ? 13.889  5.935   44.397  1.00 39.31  ? 396  ASP B O   1 
ATOM   7220  C  CB  . ASP B  1 396 ? 16.674  4.270   43.981  1.00 63.86  ? 396  ASP B CB  1 
ATOM   7221  C  CG  . ASP B  1 396 ? 18.149  4.568   44.209  1.00 71.05  ? 396  ASP B CG  1 
ATOM   7222  O  OD1 . ASP B  1 396 ? 18.460  5.515   44.973  1.00 72.18  ? 396  ASP B OD1 1 
ATOM   7223  O  OD2 . ASP B  1 396 ? 18.995  3.860   43.625  1.00 74.58  ? 396  ASP B OD2 1 
ATOM   7224  N  N   . ALA B  1 397 ? 13.621  3.748   44.925  1.00 46.81  ? 397  ALA B N   1 
ATOM   7225  C  CA  . ALA B  1 397 ? 12.217  3.658   44.577  1.00 43.07  ? 397  ALA B CA  1 
ATOM   7226  C  C   . ALA B  1 397 ? 11.387  4.425   45.578  1.00 39.91  ? 397  ALA B C   1 
ATOM   7227  O  O   . ALA B  1 397 ? 10.471  5.104   45.186  1.00 39.73  ? 397  ALA B O   1 
ATOM   7228  C  CB  . ALA B  1 397 ? 11.760  2.199   44.492  1.00 37.17  ? 397  ALA B CB  1 
ATOM   7229  N  N   . MET B  1 398 ? 11.701  4.332   46.862  1.00 35.74  ? 398  MET B N   1 
ATOM   7230  C  CA  . MET B  1 398 ? 11.002  5.154   47.845  1.00 34.55  ? 398  MET B CA  1 
ATOM   7231  C  C   . MET B  1 398 ? 11.208  6.670   47.595  1.00 35.58  ? 398  MET B C   1 
ATOM   7232  O  O   . MET B  1 398 ? 10.246  7.473   47.677  1.00 33.95  ? 398  MET B O   1 
ATOM   7233  C  CB  . MET B  1 398 ? 11.427  4.768   49.253  1.00 34.33  ? 398  MET B CB  1 
ATOM   7234  C  CG  . MET B  1 398 ? 10.772  5.579   50.345  1.00 33.21  ? 398  MET B CG  1 
ATOM   7235  S  SD  . MET B  1 398 ? 9.193   4.905   50.890  1.00 40.56  ? 398  MET B SD  1 
ATOM   7236  C  CE  . MET B  1 398 ? 8.035   5.771   49.840  1.00 67.24  ? 398  MET B CE  1 
ATOM   7237  N  N   . SER B  1 399 ? 12.445  7.062   47.272  1.00 36.29  ? 399  SER B N   1 
ATOM   7238  C  CA  . SER B  1 399 ? 12.698  8.442   46.825  1.00 37.62  ? 399  SER B CA  1 
ATOM   7239  C  C   . SER B  1 399 ? 11.819  8.810   45.625  1.00 36.73  ? 399  SER B C   1 
ATOM   7240  O  O   . SER B  1 399 ? 11.264  9.920   45.534  1.00 36.26  ? 399  SER B O   1 
ATOM   7241  C  CB  . SER B  1 399 ? 14.178  8.646   46.467  1.00 46.39  ? 399  SER B CB  1 
ATOM   7242  O  OG  . SER B  1 399 ? 14.365  9.762   45.598  1.00 47.05  ? 399  SER B OG  1 
ATOM   7243  N  N   . ALA B  1 400 ? 11.695  7.869   44.700  1.00 36.97  ? 400  ALA B N   1 
ATOM   7244  C  CA  . ALA B  1 400 ? 10.860  8.094   43.538  1.00 40.76  ? 400  ALA B CA  1 
ATOM   7245  C  C   . ALA B  1 400 ? 9.370   8.198   43.890  1.00 37.23  ? 400  ALA B C   1 
ATOM   7246  O  O   . ALA B  1 400 ? 8.644   8.947   43.250  1.00 35.77  ? 400  ALA B O   1 
ATOM   7247  C  CB  . ALA B  1 400 ? 11.090  7.014   42.504  1.00 52.31  ? 400  ALA B CB  1 
ATOM   7248  N  N   . VAL B  1 401 ? 8.909   7.447   44.891  1.00 42.84  ? 401  VAL B N   1 
ATOM   7249  C  CA  . VAL B  1 401 ? 7.495   7.461   45.250  1.00 39.35  ? 401  VAL B CA  1 
ATOM   7250  C  C   . VAL B  1 401 ? 7.172   8.837   45.773  1.00 38.09  ? 401  VAL B C   1 
ATOM   7251  O  O   . VAL B  1 401 ? 6.286   9.520   45.241  1.00 33.09  ? 401  VAL B O   1 
ATOM   7252  C  CB  . VAL B  1 401 ? 7.123   6.415   46.315  1.00 31.69  ? 401  VAL B CB  1 
ATOM   7253  C  CG1 . VAL B  1 401 ? 5.655   6.543   46.671  1.00 30.22  ? 401  VAL B CG1 1 
ATOM   7254  C  CG2 . VAL B  1 401 ? 7.397   5.033   45.815  1.00 32.16  ? 401  VAL B CG2 1 
ATOM   7255  N  N   . VAL B  1 402 ? 7.924   9.268   46.783  1.00 32.40  ? 402  VAL B N   1 
ATOM   7256  C  CA  . VAL B  1 402 ? 7.658   10.579  47.351  1.00 32.03  ? 402  VAL B CA  1 
ATOM   7257  C  C   . VAL B  1 402 ? 7.785   11.713  46.328  1.00 32.87  ? 402  VAL B C   1 
ATOM   7258  O  O   . VAL B  1 402 ? 6.929   12.610  46.270  1.00 32.32  ? 402  VAL B O   1 
ATOM   7259  C  CB  . VAL B  1 402 ? 8.533   10.845  48.527  1.00 32.27  ? 402  VAL B CB  1 
ATOM   7260  C  CG1 . VAL B  1 402 ? 8.352   12.256  48.954  1.00 32.12  ? 402  VAL B CG1 1 
ATOM   7261  C  CG2 . VAL B  1 402 ? 8.154   9.918   49.635  1.00 31.30  ? 402  VAL B CG2 1 
ATOM   7262  N  N   . GLY B  1 403 ? 8.820   11.650  45.493  1.00 34.25  ? 403  GLY B N   1 
ATOM   7263  C  CA  . GLY B  1 403 ? 9.010   12.649  44.447  1.00 39.83  ? 403  GLY B CA  1 
ATOM   7264  C  C   . GLY B  1 403 ? 7.925   12.710  43.374  1.00 40.22  ? 403  GLY B C   1 
ATOM   7265  O  O   . GLY B  1 403 ? 7.402   13.781  43.047  1.00 34.91  ? 403  GLY B O   1 
ATOM   7266  N  N   . ASP B  1 404 ? 7.598   11.552  42.811  1.00 57.26  ? 404  ASP B N   1 
ATOM   7267  C  CA  . ASP B  1 404 ? 6.599   11.463  41.762  1.00 55.26  ? 404  ASP B CA  1 
ATOM   7268  C  C   . ASP B  1 404 ? 5.278   11.959  42.303  1.00 53.25  ? 404  ASP B C   1 
ATOM   7269  O  O   . ASP B  1 404 ? 4.603   12.746  41.646  1.00 56.06  ? 404  ASP B O   1 
ATOM   7270  C  CB  . ASP B  1 404 ? 6.443   10.024  41.256  1.00 46.78  ? 404  ASP B CB  1 
ATOM   7271  C  CG  . ASP B  1 404 ? 7.692   9.498   40.561  1.00 48.90  ? 404  ASP B CG  1 
ATOM   7272  O  OD1 . ASP B  1 404 ? 8.639   10.280  40.340  1.00 51.05  ? 404  ASP B OD1 1 
ATOM   7273  O  OD2 . ASP B  1 404 ? 7.731   8.293   40.228  1.00 49.17  ? 404  ASP B OD2 1 
ATOM   7274  N  N   . HIS B  1 405 ? 4.918   11.513  43.507  1.00 39.60  ? 405  HIS B N   1 
ATOM   7275  C  CA  . HIS B  1 405 ? 3.627   11.884  44.097  1.00 35.35  ? 405  HIS B CA  1 
ATOM   7276  C  C   . HIS B  1 405 ? 3.501   13.373  44.374  1.00 31.99  ? 405  HIS B C   1 
ATOM   7277  O  O   . HIS B  1 405 ? 2.549   13.997  43.915  1.00 30.45  ? 405  HIS B O   1 
ATOM   7278  C  CB  . HIS B  1 405 ? 3.360   11.104  45.386  1.00 37.41  ? 405  HIS B CB  1 
ATOM   7279  C  CG  . HIS B  1 405 ? 2.060   11.449  46.061  1.00 35.46  ? 405  HIS B CG  1 
ATOM   7280  N  ND1 . HIS B  1 405 ? 0.912   11.763  45.363  1.00 35.41  ? 405  HIS B ND1 1 
ATOM   7281  C  CD2 . HIS B  1 405 ? 1.727   11.492  47.376  1.00 31.36  ? 405  HIS B CD2 1 
ATOM   7282  C  CE1 . HIS B  1 405 ? -0.068  11.998  46.220  1.00 32.96  ? 405  HIS B CE1 1 
ATOM   7283  N  NE2 . HIS B  1 405 ? 0.400   11.837  47.446  1.00 30.38  ? 405  HIS B NE2 1 
ATOM   7284  N  N   . ASN B  1 406 ? 4.444   13.940  45.128  1.00 31.20  ? 406  ASN B N   1 
ATOM   7285  C  CA  . ASN B  1 406 ? 4.315   15.344  45.532  1.00 31.25  ? 406  ASN B CA  1 
ATOM   7286  C  C   . ASN B  1 406 ? 4.736   16.420  44.524  1.00 32.53  ? 406  ASN B C   1 
ATOM   7287  O  O   . ASN B  1 406 ? 4.191   17.531  44.522  1.00 32.44  ? 406  ASN B O   1 
ATOM   7288  C  CB  . ASN B  1 406 ? 5.001   15.566  46.860  1.00 31.11  ? 406  ASN B CB  1 
ATOM   7289  C  CG  . ASN B  1 406 ? 4.393   14.731  47.958  1.00 35.94  ? 406  ASN B CG  1 
ATOM   7290  O  OD1 . ASN B  1 406 ? 3.320   15.053  48.463  1.00 33.80  ? 406  ASN B OD1 1 
ATOM   7291  N  ND2 . ASN B  1 406 ? 5.070   13.651  48.339  1.00 29.91  ? 406  ASN B ND2 1 
ATOM   7292  N  N   . VAL B  1 407 ? 5.702   16.098  43.668  1.00 34.59  ? 407  VAL B N   1 
ATOM   7293  C  CA  . VAL B  1 407 ? 6.149   17.062  42.669  1.00 39.53  ? 407  VAL B CA  1 
ATOM   7294  C  C   . VAL B  1 407 ? 5.994   16.643  41.199  1.00 39.94  ? 407  VAL B C   1 
ATOM   7295  O  O   . VAL B  1 407 ? 5.251   17.285  40.457  1.00 39.87  ? 407  VAL B O   1 
ATOM   7296  C  CB  . VAL B  1 407 ? 7.576   17.530  42.932  1.00 36.22  ? 407  VAL B CB  1 
ATOM   7297  C  CG1 . VAL B  1 407 ? 8.079   18.361  41.761  1.00 37.73  ? 407  VAL B CG1 1 
ATOM   7298  C  CG2 . VAL B  1 407 ? 7.613   18.328  44.204  1.00 35.70  ? 407  VAL B CG2 1 
ATOM   7299  N  N   . VAL B  1 408 ? 6.684   15.588  40.769  1.00 36.32  ? 408  VAL B N   1 
ATOM   7300  C  CA  . VAL B  1 408 ? 6.803   15.348  39.329  1.00 37.40  ? 408  VAL B CA  1 
ATOM   7301  C  C   . VAL B  1 408 ? 5.475   15.213  38.601  1.00 40.44  ? 408  VAL B C   1 
ATOM   7302  O  O   . VAL B  1 408 ? 5.195   15.968  37.680  1.00 37.51  ? 408  VAL B O   1 
ATOM   7303  C  CB  . VAL B  1 408 ? 7.713   14.168  38.967  1.00 38.65  ? 408  VAL B CB  1 
ATOM   7304  C  CG1 . VAL B  1 408 ? 7.683   13.969  37.477  1.00 39.19  ? 408  VAL B CG1 1 
ATOM   7305  C  CG2 . VAL B  1 408 ? 9.152   14.442  39.413  1.00 39.16  ? 408  VAL B CG2 1 
ATOM   7306  N  N   . CYS B  1 409 ? 4.645   14.274  39.028  1.00 47.14  ? 409  CYS B N   1 
ATOM   7307  C  CA  . CYS B  1 409 ? 3.332   14.098  38.402  1.00 45.68  ? 409  CYS B CA  1 
ATOM   7308  C  C   . CYS B  1 409 ? 2.373   15.301  38.489  1.00 42.63  ? 409  CYS B C   1 
ATOM   7309  O  O   . CYS B  1 409 ? 1.656   15.573  37.525  1.00 40.02  ? 409  CYS B O   1 
ATOM   7310  C  CB  . CYS B  1 409 ? 2.684   12.808  38.890  1.00 42.95  ? 409  CYS B CB  1 
ATOM   7311  S  SG  . CYS B  1 409 ? 3.767   11.404  38.583  1.00 83.40  ? 409  CYS B SG  1 
ATOM   7312  N  N   . PRO B  1 410 ? 2.342   16.006  39.641  1.00 42.63  ? 410  PRO B N   1 
ATOM   7313  C  CA  . PRO B  1 410 ? 1.684   17.313  39.660  1.00 41.29  ? 410  PRO B CA  1 
ATOM   7314  C  C   . PRO B  1 410 ? 2.194   18.247  38.569  1.00 41.46  ? 410  PRO B C   1 
ATOM   7315  O  O   . PRO B  1 410 ? 1.381   18.832  37.855  1.00 40.60  ? 410  PRO B O   1 
ATOM   7316  C  CB  . PRO B  1 410 ? 2.089   17.866  41.025  1.00 33.27  ? 410  PRO B CB  1 
ATOM   7317  C  CG  . PRO B  1 410 ? 2.163   16.690  41.880  1.00 32.30  ? 410  PRO B CG  1 
ATOM   7318  C  CD  . PRO B  1 410 ? 2.583   15.524  41.014  1.00 33.18  ? 410  PRO B CD  1 
ATOM   7319  N  N   . VAL B  1 411 ? 3.516   18.357  38.438  1.00 36.46  ? 411  VAL B N   1 
ATOM   7320  C  CA  . VAL B  1 411 ? 4.145   19.260  37.478  1.00 38.08  ? 411  VAL B CA  1 
ATOM   7321  C  C   . VAL B  1 411 ? 3.695   18.900  36.083  1.00 38.73  ? 411  VAL B C   1 
ATOM   7322  O  O   . VAL B  1 411 ? 3.253   19.751  35.325  1.00 39.41  ? 411  VAL B O   1 
ATOM   7323  C  CB  . VAL B  1 411 ? 5.675   19.166  37.545  1.00 39.21  ? 411  VAL B CB  1 
ATOM   7324  C  CG1 . VAL B  1 411 ? 6.302   19.715  36.282  1.00 41.00  ? 411  VAL B CG1 1 
ATOM   7325  C  CG2 . VAL B  1 411 ? 6.192   19.888  38.765  1.00 38.96  ? 411  VAL B CG2 1 
ATOM   7326  N  N   . ALA B  1 412 ? 3.793   17.619  35.764  1.00 41.92  ? 412  ALA B N   1 
ATOM   7327  C  CA  . ALA B  1 412 ? 3.355   17.121  34.477  1.00 44.88  ? 412  ALA B CA  1 
ATOM   7328  C  C   . ALA B  1 412 ? 1.875   17.418  34.241  1.00 47.12  ? 412  ALA B C   1 
ATOM   7329  O  O   . ALA B  1 412 ? 1.508   17.881  33.154  1.00 51.66  ? 412  ALA B O   1 
ATOM   7330  C  CB  . ALA B  1 412 ? 3.635   15.633  34.361  1.00 46.05  ? 412  ALA B CB  1 
ATOM   7331  N  N   . GLN B  1 413 ? 1.029   17.172  35.244  1.00 36.70  ? 413  GLN B N   1 
ATOM   7332  C  CA  . GLN B  1 413 ? -0.391  17.464  35.085  1.00 37.09  ? 413  GLN B CA  1 
ATOM   7333  C  C   . GLN B  1 413 ? -0.656  18.942  34.790  1.00 38.27  ? 413  GLN B C   1 
ATOM   7334  O  O   . GLN B  1 413 ? -1.377  19.256  33.850  1.00 39.32  ? 413  GLN B O   1 
ATOM   7335  C  CB  . GLN B  1 413 ? -1.231  17.020  36.272  1.00 52.21  ? 413  GLN B CB  1 
ATOM   7336  C  CG  . GLN B  1 413 ? -2.683  17.484  36.117  1.00 60.20  ? 413  GLN B CG  1 
ATOM   7337  C  CD  . GLN B  1 413 ? -3.653  16.807  37.068  1.00 65.85  ? 413  GLN B CD  1 
ATOM   7338  O  OE1 . GLN B  1 413 ? -3.908  17.296  38.175  1.00 65.20  ? 413  GLN B OE1 1 
ATOM   7339  N  NE2 . GLN B  1 413 ? -4.216  15.681  36.633  1.00 68.12  ? 413  GLN B NE2 1 
ATOM   7340  N  N   . LEU B  1 414 ? -0.075  19.847  35.574  1.00 40.85  ? 414  LEU B N   1 
ATOM   7341  C  CA  . LEU B  1 414 ? -0.211  21.275  35.286  1.00 37.65  ? 414  LEU B CA  1 
ATOM   7342  C  C   . LEU B  1 414 ? 0.270   21.590  33.874  1.00 43.61  ? 414  LEU B C   1 
ATOM   7343  O  O   . LEU B  1 414 ? -0.411  22.291  33.142  1.00 44.89  ? 414  LEU B O   1 
ATOM   7344  C  CB  . LEU B  1 414 ? 0.557   22.133  36.293  1.00 56.97  ? 414  LEU B CB  1 
ATOM   7345  C  CG  . LEU B  1 414 ? 0.413   23.642  36.109  1.00 38.63  ? 414  LEU B CG  1 
ATOM   7346  C  CD1 . LEU B  1 414 ? -0.968  24.052  36.501  1.00 37.60  ? 414  LEU B CD1 1 
ATOM   7347  C  CD2 . LEU B  1 414 ? 1.426   24.389  36.920  1.00 39.06  ? 414  LEU B CD2 1 
ATOM   7348  N  N   . ALA B  1 415 ? 1.435   21.063  33.498  1.00 40.30  ? 415  ALA B N   1 
ATOM   7349  C  CA  . ALA B  1 415 ? 2.001   21.288  32.168  1.00 42.08  ? 415  ALA B CA  1 
ATOM   7350  C  C   . ALA B  1 415 ? 0.987   20.971  31.089  1.00 42.35  ? 415  ALA B C   1 
ATOM   7351  O  O   . ALA B  1 415 ? 0.551   21.853  30.354  1.00 44.42  ? 415  ALA B O   1 
ATOM   7352  C  CB  . ALA B  1 415 ? 3.228   20.454  31.974  1.00 42.78  ? 415  ALA B CB  1 
ATOM   7353  N  N   . GLY B  1 416 ? 0.599   19.706  31.015  1.00 51.47  ? 416  GLY B N   1 
ATOM   7354  C  CA  . GLY B  1 416 ? -0.408  19.275  30.064  1.00 54.07  ? 416  GLY B CA  1 
ATOM   7355  C  C   . GLY B  1 416 ? -1.737  20.018  30.100  1.00 55.46  ? 416  GLY B C   1 
ATOM   7356  O  O   . GLY B  1 416 ? -2.328  20.255  29.044  1.00 60.33  ? 416  GLY B O   1 
ATOM   7357  N  N   . ARG B  1 417 ? -2.217  20.382  31.292  1.00 46.12  ? 417  ARG B N   1 
ATOM   7358  C  CA  . ARG B  1 417 ? -3.503  21.079  31.403  1.00 48.01  ? 417  ARG B CA  1 
ATOM   7359  C  C   . ARG B  1 417 ? -3.369  22.493  30.850  1.00 46.28  ? 417  ARG B C   1 
ATOM   7360  O  O   . ARG B  1 417 ? -4.285  23.017  30.213  1.00 45.03  ? 417  ARG B O   1 
ATOM   7361  C  CB  . ARG B  1 417 ? -4.022  21.151  32.853  1.00 75.70  ? 417  ARG B CB  1 
ATOM   7362  C  CG  . ARG B  1 417 ? -4.299  19.826  33.569  1.00 80.91  ? 417  ARG B CG  1 
ATOM   7363  C  CD  . ARG B  1 417 ? -5.340  18.971  32.887  1.00 87.04  ? 417  ARG B CD  1 
ATOM   7364  N  NE  . ARG B  1 417 ? -6.516  19.740  32.513  1.00 94.63  ? 417  ARG B NE  1 
ATOM   7365  C  CZ  . ARG B  1 417 ? -6.900  19.941  31.258  1.00 102.15 ? 417  ARG B CZ  1 
ATOM   7366  N  NH1 . ARG B  1 417 ? -6.200  19.418  30.258  1.00 105.74 ? 417  ARG B NH1 1 
ATOM   7367  N  NH2 . ARG B  1 417 ? -7.988  20.655  31.000  1.00 103.40 ? 417  ARG B NH2 1 
ATOM   7368  N  N   . LEU B  1 418 ? -2.225  23.116  31.103  1.00 56.56  ? 418  LEU B N   1 
ATOM   7369  C  CA  . LEU B  1 418 ? -2.007  24.472  30.639  1.00 59.67  ? 418  LEU B CA  1 
ATOM   7370  C  C   . LEU B  1 418 ? -1.855  24.460  29.134  1.00 65.68  ? 418  LEU B C   1 
ATOM   7371  O  O   . LEU B  1 418 ? -2.359  25.354  28.458  1.00 71.72  ? 418  LEU B O   1 
ATOM   7372  C  CB  . LEU B  1 418 ? -0.779  25.103  31.296  1.00 43.14  ? 418  LEU B CB  1 
ATOM   7373  C  CG  . LEU B  1 418 ? -0.954  25.623  32.726  1.00 42.11  ? 418  LEU B CG  1 
ATOM   7374  C  CD1 . LEU B  1 418 ? 0.277   26.422  33.164  1.00 42.87  ? 418  LEU B CD1 1 
ATOM   7375  C  CD2 . LEU B  1 418 ? -2.245  26.436  32.873  1.00 41.52  ? 418  LEU B CD2 1 
ATOM   7376  N  N   . ALA B  1 419 ? -1.172  23.443  28.608  1.00 59.44  ? 419  ALA B N   1 
ATOM   7377  C  CA  . ALA B  1 419 ? -1.012  23.310  27.161  1.00 57.00  ? 419  ALA B CA  1 
ATOM   7378  C  C   . ALA B  1 419 ? -2.358  23.117  26.478  1.00 59.49  ? 419  ALA B C   1 
ATOM   7379  O  O   . ALA B  1 419 ? -2.635  23.759  25.473  1.00 63.07  ? 419  ALA B O   1 
ATOM   7380  C  CB  . ALA B  1 419 ? -0.077  22.174  26.817  1.00 48.28  ? 419  ALA B CB  1 
ATOM   7381  N  N   . ALA B  1 420 ? -3.198  22.248  27.035  1.00 64.56  ? 420  ALA B N   1 
ATOM   7382  C  CA  . ALA B  1 420 ? -4.521  21.973  26.463  1.00 67.19  ? 420  ALA B CA  1 
ATOM   7383  C  C   . ALA B  1 420 ? -5.438  23.200  26.426  1.00 68.91  ? 420  ALA B C   1 
ATOM   7384  O  O   . ALA B  1 420 ? -6.393  23.256  25.648  1.00 68.97  ? 420  ALA B O   1 
ATOM   7385  C  CB  . ALA B  1 420 ? -5.201  20.827  27.212  1.00 66.51  ? 420  ALA B CB  1 
ATOM   7386  N  N   . GLN B  1 421 ? -5.156  24.172  27.284  1.00 73.27  ? 421  GLN B N   1 
ATOM   7387  C  CA  . GLN B  1 421 ? -5.926  25.416  27.309  1.00 77.85  ? 421  GLN B CA  1 
ATOM   7388  C  C   . GLN B  1 421 ? -5.355  26.592  26.504  1.00 81.92  ? 421  GLN B C   1 
ATOM   7389  O  O   . GLN B  1 421 ? -5.797  27.737  26.648  1.00 82.11  ? 421  GLN B O   1 
ATOM   7390  C  CB  . GLN B  1 421 ? -6.339  25.810  28.720  1.00 77.76  ? 421  GLN B CB  1 
ATOM   7391  C  CG  . GLN B  1 421 ? -7.760  25.399  29.006  1.00 76.43  ? 421  GLN B CG  1 
ATOM   7392  C  CD  . GLN B  1 421 ? -7.874  23.972  29.447  1.00 76.16  ? 421  GLN B CD  1 
ATOM   7393  O  OE1 . GLN B  1 421 ? -6.908  23.216  29.393  1.00 76.85  ? 421  GLN B OE1 1 
ATOM   7394  N  NE2 . GLN B  1 421 ? -9.062  23.588  29.897  1.00 75.56  ? 421  GLN B NE2 1 
ATOM   7395  N  N   . GLY B  1 422 ? -4.346  26.311  25.690  1.00 93.31  ? 422  GLY B N   1 
ATOM   7396  C  CA  . GLY B  1 422 ? -3.785  27.334  24.838  1.00 94.13  ? 422  GLY B CA  1 
ATOM   7397  C  C   . GLY B  1 422 ? -2.807  28.214  25.574  1.00 91.91  ? 422  GLY B C   1 
ATOM   7398  O  O   . GLY B  1 422 ? -2.860  29.436  25.489  1.00 97.65  ? 422  GLY B O   1 
ATOM   7399  N  N   . ALA B  1 423 ? -1.927  27.584  26.336  1.00 60.25  ? 423  ALA B N   1 
ATOM   7400  C  CA  . ALA B  1 423 ? -0.789  28.295  26.888  1.00 57.68  ? 423  ALA B CA  1 
ATOM   7401  C  C   . ALA B  1 423 ? 0.492   27.770  26.253  1.00 56.11  ? 423  ALA B C   1 
ATOM   7402  O  O   . ALA B  1 423 ? 0.567   26.600  25.854  1.00 53.32  ? 423  ALA B O   1 
ATOM   7403  C  CB  . ALA B  1 423 ? -0.741  28.138  28.392  1.00 67.43  ? 423  ALA B CB  1 
ATOM   7404  N  N   . ARG B  1 424 ? 1.487   28.645  26.142  1.00 62.41  ? 424  ARG B N   1 
ATOM   7405  C  CA  . ARG B  1 424 ? 2.816   28.245  25.700  1.00 67.94  ? 424  ARG B CA  1 
ATOM   7406  C  C   . ARG B  1 424 ? 3.601   27.786  26.913  1.00 62.60  ? 424  ARG B C   1 
ATOM   7407  O  O   . ARG B  1 424 ? 3.737   28.519  27.890  1.00 65.41  ? 424  ARG B O   1 
ATOM   7408  C  CB  . ARG B  1 424 ? 3.533   29.410  25.026  1.00 103.93 ? 424  ARG B CB  1 
ATOM   7409  C  CG  . ARG B  1 424 ? 4.940   29.088  24.556  1.00 112.00 ? 424  ARG B CG  1 
ATOM   7410  C  CD  . ARG B  1 424 ? 5.489   30.193  23.661  1.00 118.19 ? 424  ARG B CD  1 
ATOM   7411  N  NE  . ARG B  1 424 ? 4.551   30.534  22.596  1.00 121.68 ? 424  ARG B NE  1 
ATOM   7412  C  CZ  . ARG B  1 424 ? 4.318   29.776  21.529  1.00 122.81 ? 424  ARG B CZ  1 
ATOM   7413  N  NH1 . ARG B  1 424 ? 4.957   28.624  21.375  1.00 121.43 ? 424  ARG B NH1 1 
ATOM   7414  N  NH2 . ARG B  1 424 ? 3.442   30.170  20.616  1.00 124.53 ? 424  ARG B NH2 1 
ATOM   7415  N  N   . VAL B  1 425 ? 4.111   26.566  26.858  1.00 57.21  ? 425  VAL B N   1 
ATOM   7416  C  CA  . VAL B  1 425 ? 4.699   25.954  28.035  1.00 55.72  ? 425  VAL B CA  1 
ATOM   7417  C  C   . VAL B  1 425 ? 6.039   25.335  27.705  1.00 57.13  ? 425  VAL B C   1 
ATOM   7418  O  O   . VAL B  1 425 ? 6.153   24.612  26.725  1.00 60.52  ? 425  VAL B O   1 
ATOM   7419  C  CB  . VAL B  1 425 ? 3.791   24.834  28.566  1.00 62.69  ? 425  VAL B CB  1 
ATOM   7420  C  CG1 . VAL B  1 425 ? 4.469   24.117  29.727  1.00 62.72  ? 425  VAL B CG1 1 
ATOM   7421  C  CG2 . VAL B  1 425 ? 2.411   25.381  28.956  1.00 61.04  ? 425  VAL B CG2 1 
ATOM   7422  N  N   . TYR B  1 426 ? 7.055   25.602  28.515  1.00 69.92  ? 426  TYR B N   1 
ATOM   7423  C  CA  . TYR B  1 426 ? 8.353   24.973  28.303  1.00 75.01  ? 426  TYR B CA  1 
ATOM   7424  C  C   . TYR B  1 426 ? 8.725   24.140  29.524  1.00 74.59  ? 426  TYR B C   1 
ATOM   7425  O  O   . TYR B  1 426 ? 8.772   24.656  30.638  1.00 77.23  ? 426  TYR B O   1 
ATOM   7426  C  CB  . TYR B  1 426 ? 9.428   26.023  28.008  1.00 81.30  ? 426  TYR B CB  1 
ATOM   7427  C  CG  . TYR B  1 426 ? 9.160   26.848  26.765  1.00 85.42  ? 426  TYR B CG  1 
ATOM   7428  C  CD1 . TYR B  1 426 ? 8.395   28.007  26.830  1.00 86.19  ? 426  TYR B CD1 1 
ATOM   7429  C  CD2 . TYR B  1 426 ? 9.670   26.470  25.529  1.00 87.54  ? 426  TYR B CD2 1 
ATOM   7430  C  CE1 . TYR B  1 426 ? 8.145   28.767  25.700  1.00 87.30  ? 426  TYR B CE1 1 
ATOM   7431  C  CE2 . TYR B  1 426 ? 9.420   27.226  24.389  1.00 89.01  ? 426  TYR B CE2 1 
ATOM   7432  C  CZ  . TYR B  1 426 ? 8.656   28.373  24.483  1.00 88.02  ? 426  TYR B CZ  1 
ATOM   7433  O  OH  . TYR B  1 426 ? 8.402   29.132  23.364  1.00 87.77  ? 426  TYR B OH  1 
ATOM   7434  N  N   . ALA B  1 427 ? 8.982   22.852  29.309  1.00 64.84  ? 427  ALA B N   1 
ATOM   7435  C  CA  . ALA B  1 427 ? 9.283   21.925  30.399  1.00 57.52  ? 427  ALA B CA  1 
ATOM   7436  C  C   . ALA B  1 427 ? 10.769  21.614  30.480  1.00 57.83  ? 427  ALA B C   1 
ATOM   7437  O  O   . ALA B  1 427 ? 11.454  21.569  29.466  1.00 52.88  ? 427  ALA B O   1 
ATOM   7438  C  CB  . ALA B  1 427 ? 8.491   20.650  30.237  1.00 48.94  ? 427  ALA B CB  1 
ATOM   7439  N  N   . TYR B  1 428 ? 11.270  21.414  31.691  1.00 50.37  ? 428  TYR B N   1 
ATOM   7440  C  CA  . TYR B  1 428 ? 12.685  21.103  31.855  1.00 51.41  ? 428  TYR B CA  1 
ATOM   7441  C  C   . TYR B  1 428 ? 12.914  20.152  33.008  1.00 50.10  ? 428  TYR B C   1 
ATOM   7442  O  O   . TYR B  1 428 ? 12.239  20.238  34.037  1.00 53.80  ? 428  TYR B O   1 
ATOM   7443  C  CB  . TYR B  1 428 ? 13.475  22.382  32.128  1.00 64.00  ? 428  TYR B CB  1 
ATOM   7444  C  CG  . TYR B  1 428 ? 13.253  22.963  33.517  1.00 61.09  ? 428  TYR B CG  1 
ATOM   7445  C  CD1 . TYR B  1 428 ? 14.019  22.540  34.605  1.00 60.84  ? 428  TYR B CD1 1 
ATOM   7446  C  CD2 . TYR B  1 428 ? 12.287  23.937  33.738  1.00 58.41  ? 428  TYR B CD2 1 
ATOM   7447  C  CE1 . TYR B  1 428 ? 13.813  23.052  35.863  1.00 59.98  ? 428  TYR B CE1 1 
ATOM   7448  C  CE2 . TYR B  1 428 ? 12.080  24.463  34.994  1.00 57.24  ? 428  TYR B CE2 1 
ATOM   7449  C  CZ  . TYR B  1 428 ? 12.844  24.013  36.054  1.00 58.42  ? 428  TYR B CZ  1 
ATOM   7450  O  OH  . TYR B  1 428 ? 12.649  24.527  37.316  1.00 57.32  ? 428  TYR B OH  1 
ATOM   7451  N  N   . ILE B  1 429 ? 13.892  19.270  32.868  1.00 50.84  ? 429  ILE B N   1 
ATOM   7452  C  CA  . ILE B  1 429 ? 14.290  18.423  33.984  1.00 50.89  ? 429  ILE B CA  1 
ATOM   7453  C  C   . ILE B  1 429 ? 15.763  18.624  34.261  1.00 55.26  ? 429  ILE B C   1 
ATOM   7454  O  O   . ILE B  1 429 ? 16.579  18.565  33.355  1.00 59.62  ? 429  ILE B O   1 
ATOM   7455  C  CB  . ILE B  1 429 ? 13.981  16.940  33.731  1.00 54.59  ? 429  ILE B CB  1 
ATOM   7456  C  CG1 . ILE B  1 429 ? 14.472  16.088  34.900  1.00 53.69  ? 429  ILE B CG1 1 
ATOM   7457  C  CG2 . ILE B  1 429 ? 14.606  16.474  32.435  1.00 56.79  ? 429  ILE B CG2 1 
ATOM   7458  C  CD1 . ILE B  1 429 ? 13.785  14.742  34.985  1.00 53.01  ? 429  ILE B CD1 1 
ATOM   7459  N  N   . PHE B  1 430 ? 16.101  18.875  35.517  1.00 69.51  ? 430  PHE B N   1 
ATOM   7460  C  CA  . PHE B  1 430 ? 17.435  19.339  35.879  1.00 73.37  ? 430  PHE B CA  1 
ATOM   7461  C  C   . PHE B  1 430 ? 18.300  18.163  36.342  1.00 77.45  ? 430  PHE B C   1 
ATOM   7462  O  O   . PHE B  1 430 ? 18.092  17.628  37.425  1.00 79.67  ? 430  PHE B O   1 
ATOM   7463  C  CB  . PHE B  1 430 ? 17.250  20.361  36.991  1.00 67.86  ? 430  PHE B CB  1 
ATOM   7464  C  CG  . PHE B  1 430 ? 18.481  21.114  37.363  1.00 65.18  ? 430  PHE B CG  1 
ATOM   7465  C  CD1 . PHE B  1 430 ? 19.402  20.572  38.247  1.00 65.40  ? 430  PHE B CD1 1 
ATOM   7466  C  CD2 . PHE B  1 430 ? 18.681  22.397  36.890  1.00 64.09  ? 430  PHE B CD2 1 
ATOM   7467  C  CE1 . PHE B  1 430 ? 20.520  21.284  38.627  1.00 67.70  ? 430  PHE B CE1 1 
ATOM   7468  C  CE2 . PHE B  1 430 ? 19.794  23.114  37.263  1.00 67.37  ? 430  PHE B CE2 1 
ATOM   7469  C  CZ  . PHE B  1 430 ? 20.718  22.558  38.136  1.00 69.33  ? 430  PHE B CZ  1 
ATOM   7470  N  N   . GLU B  1 431 ? 19.277  17.776  35.526  1.00 68.45  ? 431  GLU B N   1 
ATOM   7471  C  CA  . GLU B  1 431 ? 20.012  16.526  35.746  1.00 68.74  ? 431  GLU B CA  1 
ATOM   7472  C  C   . GLU B  1 431 ? 21.305  16.671  36.541  1.00 67.30  ? 431  GLU B C   1 
ATOM   7473  O  O   . GLU B  1 431 ? 21.885  15.664  36.964  1.00 64.76  ? 431  GLU B O   1 
ATOM   7474  C  CB  . GLU B  1 431 ? 20.345  15.849  34.406  1.00 82.56  ? 431  GLU B CB  1 
ATOM   7475  C  CG  . GLU B  1 431 ? 19.199  15.786  33.404  1.00 85.25  ? 431  GLU B CG  1 
ATOM   7476  C  CD  . GLU B  1 431 ? 18.316  14.558  33.574  1.00 85.98  ? 431  GLU B CD  1 
ATOM   7477  O  OE1 . GLU B  1 431 ? 17.706  14.394  34.657  1.00 84.80  ? 431  GLU B OE1 1 
ATOM   7478  O  OE2 . GLU B  1 431 ? 18.234  13.758  32.615  1.00 86.34  ? 431  GLU B OE2 1 
ATOM   7479  N  N   . HIS B  1 432 ? 21.755  17.906  36.751  1.00 76.53  ? 432  HIS B N   1 
ATOM   7480  C  CA  . HIS B  1 432 ? 23.116  18.122  37.250  1.00 79.39  ? 432  HIS B CA  1 
ATOM   7481  C  C   . HIS B  1 432 ? 23.249  18.344  38.760  1.00 75.07  ? 432  HIS B C   1 
ATOM   7482  O  O   . HIS B  1 432 ? 22.661  19.266  39.332  1.00 73.01  ? 432  HIS B O   1 
ATOM   7483  C  CB  . HIS B  1 432 ? 23.820  19.252  36.490  1.00 87.58  ? 432  HIS B CB  1 
ATOM   7484  C  CG  . HIS B  1 432 ? 25.118  19.670  37.113  1.00 91.94  ? 432  HIS B CG  1 
ATOM   7485  N  ND1 . HIS B  1 432 ? 25.276  20.867  37.779  1.00 92.11  ? 432  HIS B ND1 1 
ATOM   7486  C  CD2 . HIS B  1 432 ? 26.313  19.036  37.193  1.00 93.95  ? 432  HIS B CD2 1 
ATOM   7487  C  CE1 . HIS B  1 432 ? 26.512  20.957  38.234  1.00 92.97  ? 432  HIS B CE1 1 
ATOM   7488  N  NE2 . HIS B  1 432 ? 27.162  19.859  37.892  1.00 94.41  ? 432  HIS B NE2 1 
ATOM   7489  N  N   . ARG B  1 433 ? 24.056  17.493  39.386  1.00 62.81  ? 433  ARG B N   1 
ATOM   7490  C  CA  . ARG B  1 433 ? 24.321  17.565  40.817  1.00 60.71  ? 433  ARG B CA  1 
ATOM   7491  C  C   . ARG B  1 433 ? 25.540  18.433  41.078  1.00 66.21  ? 433  ARG B C   1 
ATOM   7492  O  O   . ARG B  1 433 ? 26.625  18.151  40.573  1.00 67.50  ? 433  ARG B O   1 
ATOM   7493  C  CB  . ARG B  1 433 ? 24.551  16.155  41.351  1.00 60.54  ? 433  ARG B CB  1 
ATOM   7494  C  CG  . ARG B  1 433 ? 25.190  16.066  42.710  1.00 58.52  ? 433  ARG B CG  1 
ATOM   7495  C  CD  . ARG B  1 433 ? 25.368  14.601  43.079  1.00 59.31  ? 433  ARG B CD  1 
ATOM   7496  N  NE  . ARG B  1 433 ? 26.079  14.440  44.339  1.00 62.66  ? 433  ARG B NE  1 
ATOM   7497  C  CZ  . ARG B  1 433 ? 25.502  14.153  45.504  1.00 64.01  ? 433  ARG B CZ  1 
ATOM   7498  N  NH1 . ARG B  1 433 ? 24.187  13.973  45.587  1.00 61.89  ? 433  ARG B NH1 1 
ATOM   7499  N  NH2 . ARG B  1 433 ? 26.248  14.039  46.594  1.00 66.87  ? 433  ARG B NH2 1 
ATOM   7500  N  N   . ALA B  1 434 ? 25.364  19.495  41.855  1.00 88.07  ? 434  ALA B N   1 
ATOM   7501  C  CA  . ALA B  1 434 ? 26.474  20.396  42.139  1.00 93.90  ? 434  ALA B CA  1 
ATOM   7502  C  C   . ALA B  1 434 ? 27.577  19.679  42.908  1.00 100.05 ? 434  ALA B C   1 
ATOM   7503  O  O   . ALA B  1 434 ? 27.319  18.742  43.676  1.00 99.79  ? 434  ALA B O   1 
ATOM   7504  C  CB  . ALA B  1 434 ? 26.003  21.619  42.901  1.00 74.80  ? 434  ALA B CB  1 
ATOM   7505  N  N   . SER B  1 435 ? 28.808  20.128  42.677  1.00 94.48  ? 435  SER B N   1 
ATOM   7506  C  CA  . SER B  1 435 ? 29.992  19.583  43.327  1.00 93.54  ? 435  SER B CA  1 
ATOM   7507  C  C   . SER B  1 435 ? 30.084  20.108  44.751  1.00 95.24  ? 435  SER B C   1 
ATOM   7508  O  O   . SER B  1 435 ? 30.749  19.525  45.610  1.00 93.15  ? 435  SER B O   1 
ATOM   7509  C  CB  . SER B  1 435 ? 31.217  20.032  42.555  1.00 77.68  ? 435  SER B CB  1 
ATOM   7510  O  OG  . SER B  1 435 ? 31.176  21.439  42.404  1.00 75.26  ? 435  SER B OG  1 
ATOM   7511  N  N   . THR B  1 436 ? 29.400  21.221  44.982  1.00 108.11 ? 436  THR B N   1 
ATOM   7512  C  CA  . THR B  1 436 ? 29.384  21.890  46.274  1.00 109.79 ? 436  THR B CA  1 
ATOM   7513  C  C   . THR B  1 436 ? 28.313  21.281  47.191  1.00 108.30 ? 436  THR B C   1 
ATOM   7514  O  O   . THR B  1 436 ? 28.079  21.759  48.302  1.00 108.67 ? 436  THR B O   1 
ATOM   7515  C  CB  . THR B  1 436 ? 29.158  23.415  46.104  1.00 73.65  ? 436  THR B CB  1 
ATOM   7516  O  OG1 . THR B  1 436 ? 27.849  23.655  45.566  1.00 75.47  ? 436  THR B OG1 1 
ATOM   7517  C  CG2 . THR B  1 436 ? 30.205  24.011  45.168  1.00 71.32  ? 436  THR B CG2 1 
ATOM   7518  N  N   . LEU B  1 437 ? 27.661  20.225  46.712  1.00 94.48  ? 437  LEU B N   1 
ATOM   7519  C  CA  . LEU B  1 437 ? 26.593  19.568  47.464  1.00 91.16  ? 437  LEU B CA  1 
ATOM   7520  C  C   . LEU B  1 437 ? 27.098  18.815  48.695  1.00 83.79  ? 437  LEU B C   1 
ATOM   7521  O  O   . LEU B  1 437 ? 27.931  17.906  48.597  1.00 81.23  ? 437  LEU B O   1 
ATOM   7522  C  CB  . LEU B  1 437 ? 25.819  18.605  46.557  1.00 104.41 ? 437  LEU B CB  1 
ATOM   7523  C  CG  . LEU B  1 437 ? 24.303  18.812  46.479  1.00 104.48 ? 437  LEU B CG  1 
ATOM   7524  C  CD1 . LEU B  1 437 ? 23.662  17.719  45.649  1.00 104.05 ? 437  LEU B CD1 1 
ATOM   7525  C  CD2 . LEU B  1 437 ? 23.689  18.870  47.865  1.00 102.80 ? 437  LEU B CD2 1 
ATOM   7526  N  N   . THR B  1 438 ? 26.552  19.183  49.850  1.00 76.39  ? 438  THR B N   1 
ATOM   7527  C  CA  . THR B  1 438 ? 26.974  18.616  51.123  1.00 74.75  ? 438  THR B CA  1 
ATOM   7528  C  C   . THR B  1 438 ? 26.191  17.358  51.453  1.00 73.70  ? 438  THR B C   1 
ATOM   7529  O  O   . THR B  1 438 ? 26.533  16.632  52.393  1.00 71.95  ? 438  THR B O   1 
ATOM   7530  C  CB  . THR B  1 438 ? 26.771  19.616  52.269  1.00 75.49  ? 438  THR B CB  1 
ATOM   7531  O  OG1 . THR B  1 438 ? 26.928  20.953  51.772  1.00 75.73  ? 438  THR B OG1 1 
ATOM   7532  C  CG2 . THR B  1 438 ? 27.777  19.355  53.385  1.00 75.91  ? 438  THR B CG2 1 
ATOM   7533  N  N   . TRP B  1 439 ? 25.133  17.115  50.679  1.00 82.89  ? 439  TRP B N   1 
ATOM   7534  C  CA  . TRP B  1 439 ? 24.269  15.955  50.873  1.00 79.71  ? 439  TRP B CA  1 
ATOM   7535  C  C   . TRP B  1 439 ? 24.895  14.753  50.208  1.00 80.43  ? 439  TRP B C   1 
ATOM   7536  O  O   . TRP B  1 439 ? 25.513  14.891  49.155  1.00 82.36  ? 439  TRP B O   1 
ATOM   7537  C  CB  . TRP B  1 439 ? 22.898  16.190  50.249  1.00 63.96  ? 439  TRP B CB  1 
ATOM   7538  C  CG  . TRP B  1 439 ? 22.047  17.172  50.965  1.00 45.93  ? 439  TRP B CG  1 
ATOM   7539  C  CD1 . TRP B  1 439 ? 21.769  18.455  50.581  1.00 64.28  ? 439  TRP B CD1 1 
ATOM   7540  C  CD2 . TRP B  1 439 ? 21.345  16.959  52.186  1.00 44.53  ? 439  TRP B CD2 1 
ATOM   7541  N  NE1 . TRP B  1 439 ? 20.934  19.057  51.494  1.00 44.86  ? 439  TRP B NE1 1 
ATOM   7542  C  CE2 . TRP B  1 439 ? 20.660  18.162  52.489  1.00 44.62  ? 439  TRP B CE2 1 
ATOM   7543  C  CE3 . TRP B  1 439 ? 21.230  15.877  53.054  1.00 43.83  ? 439  TRP B CE3 1 
ATOM   7544  C  CZ2 . TRP B  1 439 ? 19.867  18.302  53.626  1.00 42.57  ? 439  TRP B CZ2 1 
ATOM   7545  C  CZ3 . TRP B  1 439 ? 20.440  16.018  54.183  1.00 43.67  ? 439  TRP B CZ3 1 
ATOM   7546  C  CH2 . TRP B  1 439 ? 19.768  17.224  54.458  1.00 42.30  ? 439  TRP B CH2 1 
ATOM   7547  N  N   . PRO B  1 440 ? 24.694  13.562  50.794  1.00 72.91  ? 440  PRO B N   1 
ATOM   7548  C  CA  . PRO B  1 440 ? 25.271  12.315  50.281  1.00 74.30  ? 440  PRO B CA  1 
ATOM   7549  C  C   . PRO B  1 440 ? 24.862  12.078  48.825  1.00 72.75  ? 440  PRO B C   1 
ATOM   7550  O  O   . PRO B  1 440 ? 23.910  12.691  48.348  1.00 70.51  ? 440  PRO B O   1 
ATOM   7551  C  CB  . PRO B  1 440 ? 24.652  11.249  51.193  1.00 77.90  ? 440  PRO B CB  1 
ATOM   7552  C  CG  . PRO B  1 440 ? 23.403  11.883  51.739  1.00 74.51  ? 440  PRO B CG  1 
ATOM   7553  C  CD  . PRO B  1 440 ? 23.781  13.316  51.925  1.00 74.32  ? 440  PRO B CD  1 
ATOM   7554  N  N   . LEU B  1 441 ? 25.587  11.233  48.106  1.00 82.81  ? 441  LEU B N   1 
ATOM   7555  C  CA  . LEU B  1 441 ? 25.290  11.086  46.689  1.00 84.17  ? 441  LEU B CA  1 
ATOM   7556  C  C   . LEU B  1 441 ? 23.998  10.320  46.404  1.00 83.73  ? 441  LEU B C   1 
ATOM   7557  O  O   . LEU B  1 441 ? 23.400  10.491  45.341  1.00 86.28  ? 441  LEU B O   1 
ATOM   7558  C  CB  . LEU B  1 441 ? 26.483  10.519  45.915  1.00 76.88  ? 441  LEU B CB  1 
ATOM   7559  C  CG  . LEU B  1 441 ? 26.807  9.043   46.110  1.00 78.11  ? 441  LEU B CG  1 
ATOM   7560  C  CD1 . LEU B  1 441 ? 26.315  8.209   44.916  1.00 77.91  ? 441  LEU B CD1 1 
ATOM   7561  C  CD2 . LEU B  1 441 ? 28.300  8.872   46.335  1.00 80.17  ? 441  LEU B CD2 1 
ATOM   7562  N  N   . TRP B  1 442 ? 23.542  9.505   47.352  1.00 67.93  ? 442  TRP B N   1 
ATOM   7563  C  CA  . TRP B  1 442 ? 22.338  8.717   47.108  1.00 65.41  ? 442  TRP B CA  1 
ATOM   7564  C  C   . TRP B  1 442 ? 21.098  9.597   46.927  1.00 60.92  ? 442  TRP B C   1 
ATOM   7565  O  O   . TRP B  1 442 ? 20.053  9.136   46.440  1.00 60.62  ? 442  TRP B O   1 
ATOM   7566  C  CB  . TRP B  1 442 ? 22.116  7.654   48.194  1.00 76.05  ? 442  TRP B CB  1 
ATOM   7567  C  CG  . TRP B  1 442 ? 21.693  8.175   49.524  1.00 79.67  ? 442  TRP B CG  1 
ATOM   7568  C  CD1 . TRP B  1 442 ? 22.479  8.326   50.623  1.00 82.99  ? 442  TRP B CD1 1 
ATOM   7569  C  CD2 . TRP B  1 442 ? 20.379  8.598   49.909  1.00 79.39  ? 442  TRP B CD2 1 
ATOM   7570  N  NE1 . TRP B  1 442 ? 21.742  8.825   51.668  1.00 82.42  ? 442  TRP B NE1 1 
ATOM   7571  C  CE2 . TRP B  1 442 ? 20.449  9.001   51.254  1.00 79.96  ? 442  TRP B CE2 1 
ATOM   7572  C  CE3 . TRP B  1 442 ? 19.153  8.681   49.246  1.00 79.18  ? 442  TRP B CE3 1 
ATOM   7573  C  CZ2 . TRP B  1 442 ? 19.345  9.478   51.947  1.00 79.54  ? 442  TRP B CZ2 1 
ATOM   7574  C  CZ3 . TRP B  1 442 ? 18.059  9.162   49.934  1.00 79.12  ? 442  TRP B CZ3 1 
ATOM   7575  C  CH2 . TRP B  1 442 ? 18.160  9.551   51.271  1.00 79.50  ? 442  TRP B CH2 1 
ATOM   7576  N  N   . MET B  1 443 ? 21.222  10.861  47.322  1.00 59.63  ? 443  MET B N   1 
ATOM   7577  C  CA  . MET B  1 443 ? 20.145  11.827  47.155  1.00 53.77  ? 443  MET B CA  1 
ATOM   7578  C  C   . MET B  1 443 ? 20.196  12.501  45.808  1.00 50.17  ? 443  MET B C   1 
ATOM   7579  O  O   . MET B  1 443 ? 19.401  13.398  45.550  1.00 48.80  ? 443  MET B O   1 
ATOM   7580  C  CB  . MET B  1 443 ? 20.191  12.904  48.225  1.00 44.50  ? 443  MET B CB  1 
ATOM   7581  C  CG  . MET B  1 443 ? 19.897  12.407  49.605  1.00 51.46  ? 443  MET B CG  1 
ATOM   7582  S  SD  . MET B  1 443 ? 19.877  13.805  50.728  1.00 52.16  ? 443  MET B SD  1 
ATOM   7583  C  CE  . MET B  1 443 ? 19.379  12.989  52.234  1.00 42.86  ? 443  MET B CE  1 
ATOM   7584  N  N   . GLY B  1 444 ? 21.152  12.110  44.971  1.00 53.88  ? 444  GLY B N   1 
ATOM   7585  C  CA  . GLY B  1 444 ? 21.170  12.585  43.600  1.00 56.50  ? 444  GLY B CA  1 
ATOM   7586  C  C   . GLY B  1 444 ? 21.166  14.100  43.508  1.00 56.39  ? 444  GLY B C   1 
ATOM   7587  O  O   . GLY B  1 444 ? 22.049  14.774  44.040  1.00 58.01  ? 444  GLY B O   1 
ATOM   7588  N  N   . VAL B  1 445 ? 20.141  14.627  42.848  1.00 47.97  ? 445  VAL B N   1 
ATOM   7589  C  CA  . VAL B  1 445 ? 20.005  16.053  42.614  1.00 48.28  ? 445  VAL B CA  1 
ATOM   7590  C  C   . VAL B  1 445 ? 18.778  16.530  43.372  1.00 50.54  ? 445  VAL B C   1 
ATOM   7591  O  O   . VAL B  1 445 ? 17.718  16.733  42.774  1.00 50.13  ? 445  VAL B O   1 
ATOM   7592  C  CB  . VAL B  1 445 ? 19.774  16.316  41.124  1.00 49.15  ? 445  VAL B CB  1 
ATOM   7593  C  CG1 . VAL B  1 445 ? 20.016  17.775  40.779  1.00 50.06  ? 445  VAL B CG1 1 
ATOM   7594  C  CG2 . VAL B  1 445 ? 20.676  15.426  40.310  1.00 73.24  ? 445  VAL B CG2 1 
ATOM   7595  N  N   . PRO B  1 446 ? 18.922  16.727  44.695  1.00 53.57  ? 446  PRO B N   1 
ATOM   7596  C  CA  . PRO B  1 446 ? 17.782  16.874  45.598  1.00 54.55  ? 446  PRO B CA  1 
ATOM   7597  C  C   . PRO B  1 446 ? 16.960  18.115  45.327  1.00 58.01  ? 446  PRO B C   1 
ATOM   7598  O  O   . PRO B  1 446 ? 17.412  19.036  44.644  1.00 57.90  ? 446  PRO B O   1 
ATOM   7599  C  CB  . PRO B  1 446 ? 18.439  16.973  46.978  1.00 44.01  ? 446  PRO B CB  1 
ATOM   7600  C  CG  . PRO B  1 446 ? 19.767  16.380  46.803  1.00 45.42  ? 446  PRO B CG  1 
ATOM   7601  C  CD  . PRO B  1 446 ? 20.184  16.808  45.437  1.00 46.80  ? 446  PRO B CD  1 
ATOM   7602  N  N   . HIS B  1 447 ? 15.750  18.107  45.878  1.00 65.99  ? 447  HIS B N   1 
ATOM   7603  C  CA  . HIS B  1 447 ? 14.794  19.185  45.730  1.00 65.12  ? 447  HIS B CA  1 
ATOM   7604  C  C   . HIS B  1 447 ? 15.461  20.516  46.070  1.00 67.32  ? 447  HIS B C   1 
ATOM   7605  O  O   . HIS B  1 447 ? 16.211  20.618  47.041  1.00 69.31  ? 447  HIS B O   1 
ATOM   7606  C  CB  . HIS B  1 447 ? 13.625  18.907  46.676  1.00 53.57  ? 447  HIS B CB  1 
ATOM   7607  C  CG  . HIS B  1 447 ? 12.503  19.895  46.582  1.00 53.11  ? 447  HIS B CG  1 
ATOM   7608  N  ND1 . HIS B  1 447 ? 11.717  20.028  45.457  1.00 52.92  ? 447  HIS B ND1 1 
ATOM   7609  C  CD2 . HIS B  1 447 ? 12.015  20.776  47.488  1.00 52.65  ? 447  HIS B CD2 1 
ATOM   7610  C  CE1 . HIS B  1 447 ? 10.806  20.961  45.667  1.00 52.26  ? 447  HIS B CE1 1 
ATOM   7611  N  NE2 . HIS B  1 447 ? 10.965  21.430  46.892  1.00 52.24  ? 447  HIS B NE2 1 
ATOM   7612  N  N   . GLY B  1 448 ? 15.230  21.521  45.235  1.00 55.02  ? 448  GLY B N   1 
ATOM   7613  C  CA  . GLY B  1 448 ? 15.679  22.866  45.541  1.00 54.49  ? 448  GLY B CA  1 
ATOM   7614  C  C   . GLY B  1 448 ? 17.114  23.233  45.206  1.00 57.70  ? 448  GLY B C   1 
ATOM   7615  O  O   . GLY B  1 448 ? 17.503  24.382  45.420  1.00 59.45  ? 448  GLY B O   1 
ATOM   7616  N  N   . TYR B  1 449 ? 17.900  22.291  44.680  1.00 65.68  ? 449  TYR B N   1 
ATOM   7617  C  CA  . TYR B  1 449 ? 19.313  22.568  44.354  1.00 63.53  ? 449  TYR B CA  1 
ATOM   7618  C  C   . TYR B  1 449 ? 19.608  23.068  42.940  1.00 58.33  ? 449  TYR B C   1 
ATOM   7619  O  O   . TYR B  1 449 ? 20.763  23.198  42.554  1.00 57.64  ? 449  TYR B O   1 
ATOM   7620  C  CB  . TYR B  1 449 ? 20.239  21.419  44.764  1.00 61.07  ? 449  TYR B CB  1 
ATOM   7621  C  CG  . TYR B  1 449 ? 20.373  21.381  46.254  1.00 64.16  ? 449  TYR B CG  1 
ATOM   7622  C  CD1 . TYR B  1 449 ? 20.875  22.478  46.945  1.00 66.56  ? 449  TYR B CD1 1 
ATOM   7623  C  CD2 . TYR B  1 449 ? 19.952  20.283  46.981  1.00 66.76  ? 449  TYR B CD2 1 
ATOM   7624  C  CE1 . TYR B  1 449 ? 20.979  22.476  48.327  1.00 68.50  ? 449  TYR B CE1 1 
ATOM   7625  C  CE2 . TYR B  1 449 ? 20.052  20.266  48.369  1.00 69.30  ? 449  TYR B CE2 1 
ATOM   7626  C  CZ  . TYR B  1 449 ? 20.567  21.365  49.040  1.00 69.04  ? 449  TYR B CZ  1 
ATOM   7627  O  OH  . TYR B  1 449 ? 20.661  21.349  50.422  1.00 66.87  ? 449  TYR B OH  1 
ATOM   7628  N  N   . GLU B  1 450 ? 18.562  23.340  42.173  1.00 49.40  ? 450  GLU B N   1 
ATOM   7629  C  CA  . GLU B  1 450 ? 18.736  24.011  40.898  1.00 53.58  ? 450  GLU B CA  1 
ATOM   7630  C  C   . GLU B  1 450 ? 18.679  25.534  41.082  1.00 59.43  ? 450  GLU B C   1 
ATOM   7631  O  O   . GLU B  1 450 ? 18.885  26.295  40.131  1.00 62.01  ? 450  GLU B O   1 
ATOM   7632  C  CB  . GLU B  1 450 ? 17.664  23.556  39.912  1.00 59.67  ? 450  GLU B CB  1 
ATOM   7633  C  CG  . GLU B  1 450 ? 16.466  24.489  39.787  1.00 62.39  ? 450  GLU B CG  1 
ATOM   7634  C  CD  . GLU B  1 450 ? 15.511  24.399  40.956  1.00 62.43  ? 450  GLU B CD  1 
ATOM   7635  O  OE1 . GLU B  1 450 ? 15.897  23.861  42.018  1.00 63.07  ? 450  GLU B OE1 1 
ATOM   7636  O  OE2 . GLU B  1 450 ? 14.360  24.859  40.801  1.00 61.00  ? 450  GLU B OE2 1 
ATOM   7637  N  N   . ILE B  1 451 ? 18.403  25.982  42.304  1.00 69.22  ? 451  ILE B N   1 
ATOM   7638  C  CA  . ILE B  1 451 ? 18.351  27.417  42.586  1.00 71.61  ? 451  ILE B CA  1 
ATOM   7639  C  C   . ILE B  1 451 ? 19.744  28.054  42.594  1.00 76.38  ? 451  ILE B C   1 
ATOM   7640  O  O   . ILE B  1 451 ? 19.915  29.170  42.099  1.00 78.05  ? 451  ILE B O   1 
ATOM   7641  C  CB  . ILE B  1 451 ? 17.623  27.719  43.917  1.00 63.87  ? 451  ILE B CB  1 
ATOM   7642  C  CG1 . ILE B  1 451 ? 16.217  27.128  43.901  1.00 59.66  ? 451  ILE B CG1 1 
ATOM   7643  C  CG2 . ILE B  1 451 ? 17.560  29.224  44.187  1.00 64.05  ? 451  ILE B CG2 1 
ATOM   7644  C  CD1 . ILE B  1 451 ? 15.506  27.230  45.235  1.00 57.14  ? 451  ILE B CD1 1 
ATOM   7645  N  N   . GLU B  1 452 ? 20.731  27.340  43.143  1.00 82.57  ? 452  GLU B N   1 
ATOM   7646  C  CA  . GLU B  1 452 ? 22.120  27.808  43.161  1.00 81.16  ? 452  GLU B CA  1 
ATOM   7647  C  C   . GLU B  1 452 ? 22.529  28.288  41.776  1.00 83.77  ? 452  GLU B C   1 
ATOM   7648  O  O   . GLU B  1 452 ? 23.147  29.337  41.618  1.00 86.24  ? 452  GLU B O   1 
ATOM   7649  C  CB  . GLU B  1 452 ? 23.064  26.685  43.605  1.00 60.87  ? 452  GLU B CB  1 
ATOM   7650  C  CG  . GLU B  1 452 ? 22.925  26.302  45.067  1.00 58.06  ? 452  GLU B CG  1 
ATOM   7651  C  CD  . GLU B  1 452 ? 23.698  25.048  45.445  1.00 55.78  ? 452  GLU B CD  1 
ATOM   7652  O  OE1 . GLU B  1 452 ? 24.566  24.615  44.655  1.00 55.79  ? 452  GLU B OE1 1 
ATOM   7653  O  OE2 . GLU B  1 452 ? 23.437  24.501  46.542  1.00 53.28  ? 452  GLU B OE2 1 
ATOM   7654  N  N   . PHE B  1 453 ? 22.139  27.511  40.775  1.00 56.27  ? 453  PHE B N   1 
ATOM   7655  C  CA  . PHE B  1 453 ? 22.537  27.736  39.400  1.00 57.96  ? 453  PHE B CA  1 
ATOM   7656  C  C   . PHE B  1 453 ? 21.705  28.782  38.671  1.00 58.22  ? 453  PHE B C   1 
ATOM   7657  O  O   . PHE B  1 453 ? 22.254  29.593  37.955  1.00 59.91  ? 453  PHE B O   1 
ATOM   7658  C  CB  . PHE B  1 453 ? 22.576  26.405  38.657  1.00 69.59  ? 453  PHE B CB  1 
ATOM   7659  C  CG  . PHE B  1 453 ? 23.635  25.474  39.170  1.00 73.02  ? 453  PHE B CG  1 
ATOM   7660  C  CD1 . PHE B  1 453 ? 23.602  25.009  40.475  1.00 72.28  ? 453  PHE B CD1 1 
ATOM   7661  C  CD2 . PHE B  1 453 ? 24.675  25.075  38.357  1.00 77.42  ? 453  PHE B CD2 1 
ATOM   7662  C  CE1 . PHE B  1 453 ? 24.583  24.166  40.958  1.00 72.94  ? 453  PHE B CE1 1 
ATOM   7663  C  CE2 . PHE B  1 453 ? 25.657  24.224  38.834  1.00 78.44  ? 453  PHE B CE2 1 
ATOM   7664  C  CZ  . PHE B  1 453 ? 25.610  23.769  40.138  1.00 75.42  ? 453  PHE B CZ  1 
ATOM   7665  N  N   . ILE B  1 454 ? 20.392  28.788  38.853  1.00 56.65  ? 454  ILE B N   1 
ATOM   7666  C  CA  . ILE B  1 454 ? 19.567  29.815  38.206  1.00 62.77  ? 454  ILE B CA  1 
ATOM   7667  C  C   . ILE B  1 454 ? 19.969  31.226  38.670  1.00 63.26  ? 454  ILE B C   1 
ATOM   7668  O  O   . ILE B  1 454 ? 19.918  32.189  37.896  1.00 60.76  ? 454  ILE B O   1 
ATOM   7669  C  CB  . ILE B  1 454 ? 18.042  29.595  38.446  1.00 60.23  ? 454  ILE B CB  1 
ATOM   7670  C  CG1 . ILE B  1 454 ? 17.565  28.281  37.820  1.00 56.74  ? 454  ILE B CG1 1 
ATOM   7671  C  CG2 . ILE B  1 454 ? 17.224  30.753  37.882  1.00 55.40  ? 454  ILE B CG2 1 
ATOM   7672  C  CD1 . ILE B  1 454 ? 17.732  28.234  36.328  1.00 57.01  ? 454  ILE B CD1 1 
ATOM   7673  N  N   . PHE B  1 455 ? 20.388  31.339  39.931  1.00 69.69  ? 455  PHE B N   1 
ATOM   7674  C  CA  . PHE B  1 455 ? 20.700  32.647  40.517  1.00 69.06  ? 455  PHE B CA  1 
ATOM   7675  C  C   . PHE B  1 455 ? 22.120  33.109  40.213  1.00 70.31  ? 455  PHE B C   1 
ATOM   7676  O  O   . PHE B  1 455 ? 22.529  34.202  40.596  1.00 67.99  ? 455  PHE B O   1 
ATOM   7677  C  CB  . PHE B  1 455 ? 20.367  32.700  42.019  1.00 62.02  ? 455  PHE B CB  1 
ATOM   7678  C  CG  . PHE B  1 455 ? 18.961  33.184  42.308  1.00 61.23  ? 455  PHE B CG  1 
ATOM   7679  C  CD1 . PHE B  1 455 ? 17.890  32.303  42.310  1.00 59.71  ? 455  PHE B CD1 1 
ATOM   7680  C  CD2 . PHE B  1 455 ? 18.705  34.524  42.548  1.00 62.06  ? 455  PHE B CD2 1 
ATOM   7681  C  CE1 . PHE B  1 455 ? 16.599  32.747  42.559  1.00 56.91  ? 455  PHE B CE1 1 
ATOM   7682  C  CE2 . PHE B  1 455 ? 17.416  34.968  42.797  1.00 59.61  ? 455  PHE B CE2 1 
ATOM   7683  C  CZ  . PHE B  1 455 ? 16.366  34.076  42.801  1.00 56.60  ? 455  PHE B CZ  1 
ATOM   7684  N  N   . GLY B  1 456 ? 22.856  32.266  39.502  1.00 77.52  ? 456  GLY B N   1 
ATOM   7685  C  CA  . GLY B  1 456 ? 24.169  32.621  39.004  1.00 82.22  ? 456  GLY B CA  1 
ATOM   7686  C  C   . GLY B  1 456 ? 25.241  32.591  40.063  1.00 83.97  ? 456  GLY B C   1 
ATOM   7687  O  O   . GLY B  1 456 ? 26.255  33.260  39.948  1.00 89.16  ? 456  GLY B O   1 
ATOM   7688  N  N   . LEU B  1 457 ? 25.005  31.814  41.106  1.00 73.47  ? 457  LEU B N   1 
ATOM   7689  C  CA  . LEU B  1 457 ? 25.983  31.625  42.176  1.00 73.21  ? 457  LEU B CA  1 
ATOM   7690  C  C   . LEU B  1 457 ? 27.370  31.034  41.823  1.00 73.40  ? 457  LEU B C   1 
ATOM   7691  O  O   . LEU B  1 457 ? 28.333  31.295  42.540  1.00 74.87  ? 457  LEU B O   1 
ATOM   7692  C  CB  . LEU B  1 457 ? 25.359  30.957  43.407  1.00 78.03  ? 457  LEU B CB  1 
ATOM   7693  C  CG  . LEU B  1 457 ? 24.891  31.996  44.431  1.00 78.06  ? 457  LEU B CG  1 
ATOM   7694  C  CD1 . LEU B  1 457 ? 23.805  32.906  43.858  1.00 77.42  ? 457  LEU B CD1 1 
ATOM   7695  C  CD2 . LEU B  1 457 ? 24.426  31.325  45.708  1.00 76.71  ? 457  LEU B CD2 1 
ATOM   7696  N  N   . PRO B  1 458 ? 27.471  30.177  40.788  1.00 80.52  ? 458  PRO B N   1 
ATOM   7697  C  CA  . PRO B  1 458 ? 28.841  29.773  40.425  1.00 83.82  ? 458  PRO B CA  1 
ATOM   7698  C  C   . PRO B  1 458 ? 29.740  30.899  39.854  1.00 97.54  ? 458  PRO B C   1 
ATOM   7699  O  O   . PRO B  1 458 ? 30.970  30.767  39.875  1.00 98.69  ? 458  PRO B O   1 
ATOM   7700  C  CB  . PRO B  1 458 ? 28.617  28.670  39.382  1.00 86.19  ? 458  PRO B CB  1 
ATOM   7701  C  CG  . PRO B  1 458 ? 27.243  28.164  39.646  1.00 83.57  ? 458  PRO B CG  1 
ATOM   7702  C  CD  . PRO B  1 458 ? 26.465  29.372  40.075  1.00 82.13  ? 458  PRO B CD  1 
ATOM   7703  N  N   . LEU B  1 459 ? 29.139  31.985  39.365  1.00 95.06  ? 459  LEU B N   1 
ATOM   7704  C  CA  . LEU B  1 459 ? 29.892  33.148  38.890  1.00 91.45  ? 459  LEU B CA  1 
ATOM   7705  C  C   . LEU B  1 459 ? 30.691  33.796  40.018  1.00 93.89  ? 459  LEU B C   1 
ATOM   7706  O  O   . LEU B  1 459 ? 31.634  34.547  39.767  1.00 97.30  ? 459  LEU B O   1 
ATOM   7707  C  CB  . LEU B  1 459 ? 28.964  34.188  38.252  1.00 70.22  ? 459  LEU B CB  1 
ATOM   7708  C  CG  . LEU B  1 459 ? 28.457  33.923  36.834  1.00 70.76  ? 459  LEU B CG  1 
ATOM   7709  C  CD1 . LEU B  1 459 ? 27.380  32.860  36.824  1.00 68.80  ? 459  LEU B CD1 1 
ATOM   7710  C  CD2 . LEU B  1 459 ? 27.937  35.195  36.198  1.00 71.60  ? 459  LEU B CD2 1 
ATOM   7711  N  N   . ASP B  1 460 ? 30.301  33.520  41.260  1.00 97.90  ? 460  ASP B N   1 
ATOM   7712  C  CA  . ASP B  1 460 ? 31.098  33.922  42.415  1.00 99.92  ? 460  ASP B CA  1 
ATOM   7713  C  C   . ASP B  1 460 ? 32.315  33.003  42.514  1.00 102.52 ? 460  ASP B C   1 
ATOM   7714  O  O   . ASP B  1 460 ? 32.183  31.792  42.738  1.00 101.29 ? 460  ASP B O   1 
ATOM   7715  C  CB  . ASP B  1 460 ? 30.270  33.870  43.705  1.00 85.62  ? 460  ASP B CB  1 
ATOM   7716  C  CG  . ASP B  1 460 ? 31.031  34.397  44.914  1.00 83.99  ? 460  ASP B CG  1 
ATOM   7717  O  OD1 . ASP B  1 460 ? 31.959  33.703  45.388  1.00 85.00  ? 460  ASP B OD1 1 
ATOM   7718  O  OD2 . ASP B  1 460 ? 30.692  35.500  45.398  1.00 81.13  ? 460  ASP B OD2 1 
ATOM   7719  N  N   . PRO B  1 461 ? 33.511  33.578  42.331  1.00 100.98 ? 461  PRO B N   1 
ATOM   7720  C  CA  . PRO B  1 461 ? 34.722  32.760  42.232  1.00 102.67 ? 461  PRO B CA  1 
ATOM   7721  C  C   . PRO B  1 461 ? 35.044  32.063  43.551  1.00 101.45 ? 461  PRO B C   1 
ATOM   7722  O  O   . PRO B  1 461 ? 35.367  30.871  43.573  1.00 101.11 ? 461  PRO B O   1 
ATOM   7723  C  CB  . PRO B  1 461 ? 35.810  33.787  41.882  1.00 98.76  ? 461  PRO B CB  1 
ATOM   7724  C  CG  . PRO B  1 461 ? 35.066  35.046  41.472  1.00 98.12  ? 461  PRO B CG  1 
ATOM   7725  C  CD  . PRO B  1 461 ? 33.805  35.018  42.258  1.00 95.12  ? 461  PRO B CD  1 
ATOM   7726  N  N   . SER B  1 462 ? 34.908  32.804  44.645  1.00 99.69  ? 462  SER B N   1 
ATOM   7727  C  CA  . SER B  1 462 ? 35.324  32.337  45.963  1.00 99.42  ? 462  SER B CA  1 
ATOM   7728  C  C   . SER B  1 462 ? 34.486  31.175  46.493  1.00 103.77 ? 462  SER B C   1 
ATOM   7729  O  O   . SER B  1 462 ? 34.779  30.626  47.560  1.00 104.96 ? 462  SER B O   1 
ATOM   7730  C  CB  . SER B  1 462 ? 35.321  33.493  46.961  1.00 82.45  ? 462  SER B CB  1 
ATOM   7731  O  OG  . SER B  1 462 ? 34.087  34.181  46.917  1.00 78.86  ? 462  SER B OG  1 
ATOM   7732  N  N   . LEU B  1 463 ? 33.434  30.821  45.757  1.00 116.24 ? 463  LEU B N   1 
ATOM   7733  C  CA  . LEU B  1 463 ? 32.524  29.755  46.172  1.00 114.70 ? 463  LEU B CA  1 
ATOM   7734  C  C   . LEU B  1 463 ? 32.990  28.332  45.821  1.00 117.37 ? 463  LEU B C   1 
ATOM   7735  O  O   . LEU B  1 463 ? 32.381  27.360  46.270  1.00 117.90 ? 463  LEU B O   1 
ATOM   7736  C  CB  . LEU B  1 463 ? 31.118  30.007  45.615  1.00 87.90  ? 463  LEU B CB  1 
ATOM   7737  C  CG  . LEU B  1 463 ? 30.191  30.942  46.396  1.00 80.44  ? 463  LEU B CG  1 
ATOM   7738  C  CD1 . LEU B  1 463 ? 28.835  31.027  45.709  1.00 77.18  ? 463  LEU B CD1 1 
ATOM   7739  C  CD2 . LEU B  1 463 ? 30.037  30.476  47.842  1.00 76.48  ? 463  LEU B CD2 1 
ATOM   7740  N  N   . ASN B  1 464 ? 34.066  28.219  45.043  1.00 100.34 ? 464  ASN B N   1 
ATOM   7741  C  CA  . ASN B  1 464 ? 34.642  26.924  44.644  1.00 99.56  ? 464  ASN B CA  1 
ATOM   7742  C  C   . ASN B  1 464 ? 33.801  26.064  43.692  1.00 96.69  ? 464  ASN B C   1 
ATOM   7743  O  O   . ASN B  1 464 ? 33.796  24.834  43.801  1.00 92.66  ? 464  ASN B O   1 
ATOM   7744  C  CB  . ASN B  1 464 ? 35.029  26.076  45.870  1.00 105.19 ? 464  ASN B CB  1 
ATOM   7745  C  CG  . ASN B  1 464 ? 35.989  26.790  46.800  1.00 108.26 ? 464  ASN B CG  1 
ATOM   7746  O  OD1 . ASN B  1 464 ? 36.701  27.713  46.393  1.00 110.73 ? 464  ASN B OD1 1 
ATOM   7747  N  ND2 . ASN B  1 464 ? 36.020  26.360  48.060  1.00 107.30 ? 464  ASN B ND2 1 
ATOM   7748  N  N   . TYR B  1 465 ? 33.103  26.702  42.758  1.00 110.22 ? 465  TYR B N   1 
ATOM   7749  C  CA  . TYR B  1 465 ? 32.418  25.960  41.702  1.00 112.85 ? 465  TYR B CA  1 
ATOM   7750  C  C   . TYR B  1 465 ? 33.413  25.586  40.603  1.00 114.37 ? 465  TYR B C   1 
ATOM   7751  O  O   . TYR B  1 465 ? 34.422  26.267  40.423  1.00 118.17 ? 465  TYR B O   1 
ATOM   7752  C  CB  . TYR B  1 465 ? 31.250  26.771  41.119  1.00 107.31 ? 465  TYR B CB  1 
ATOM   7753  C  CG  . TYR B  1 465 ? 30.017  26.835  42.002  1.00 105.23 ? 465  TYR B CG  1 
ATOM   7754  C  CD1 . TYR B  1 465 ? 29.858  27.850  42.938  1.00 105.33 ? 465  TYR B CD1 1 
ATOM   7755  C  CD2 . TYR B  1 465 ? 29.012  25.885  41.897  1.00 103.51 ? 465  TYR B CD2 1 
ATOM   7756  C  CE1 . TYR B  1 465 ? 28.731  27.915  43.743  1.00 103.85 ? 465  TYR B CE1 1 
ATOM   7757  C  CE2 . TYR B  1 465 ? 27.888  25.938  42.699  1.00 102.71 ? 465  TYR B CE2 1 
ATOM   7758  C  CZ  . TYR B  1 465 ? 27.752  26.955  43.622  1.00 102.73 ? 465  TYR B CZ  1 
ATOM   7759  O  OH  . TYR B  1 465 ? 26.631  27.014  44.422  1.00 100.90 ? 465  TYR B OH  1 
ATOM   7760  N  N   . THR B  1 466 ? 33.138  24.508  39.874  1.00 97.73  ? 466  THR B N   1 
ATOM   7761  C  CA  . THR B  1 466 ? 33.943  24.170  38.700  1.00 97.41  ? 466  THR B CA  1 
ATOM   7762  C  C   . THR B  1 466 ? 33.672  25.188  37.579  1.00 96.56  ? 466  THR B C   1 
ATOM   7763  O  O   . THR B  1 466 ? 32.689  25.928  37.637  1.00 94.27  ? 466  THR B O   1 
ATOM   7764  C  CB  . THR B  1 466 ? 33.729  22.698  38.240  1.00 76.69  ? 466  THR B CB  1 
ATOM   7765  O  OG1 . THR B  1 466 ? 32.632  22.602  37.321  1.00 76.53  ? 466  THR B OG1 1 
ATOM   7766  C  CG2 . THR B  1 466 ? 33.478  21.795  39.444  1.00 73.55  ? 466  THR B CG2 1 
ATOM   7767  N  N   . THR B  1 467 ? 34.558  25.272  36.591  1.00 105.45 ? 467  THR B N   1 
ATOM   7768  C  CA  . THR B  1 467 ? 34.416  26.308  35.566  1.00 106.80 ? 467  THR B CA  1 
ATOM   7769  C  C   . THR B  1 467 ? 33.256  26.034  34.606  1.00 108.41 ? 467  THR B C   1 
ATOM   7770  O  O   . THR B  1 467 ? 32.452  26.931  34.292  1.00 108.54 ? 467  THR B O   1 
ATOM   7771  C  CB  . THR B  1 467 ? 35.716  26.518  34.777  1.00 99.71  ? 467  THR B CB  1 
ATOM   7772  O  OG1 . THR B  1 467 ? 36.811  26.634  35.693  1.00 100.25 ? 467  THR B OG1 1 
ATOM   7773  C  CG2 . THR B  1 467 ? 35.625  27.788  33.940  1.00 99.14  ? 467  THR B CG2 1 
ATOM   7774  N  N   . GLU B  1 468 ? 33.160  24.789  34.149  1.00 111.90 ? 468  GLU B N   1 
ATOM   7775  C  CA  . GLU B  1 468 ? 32.024  24.377  33.333  1.00 111.34 ? 468  GLU B CA  1 
ATOM   7776  C  C   . GLU B  1 468 ? 30.717  24.591  34.098  1.00 106.90 ? 468  GLU B C   1 
ATOM   7777  O  O   . GLU B  1 468 ? 29.662  24.792  33.501  1.00 105.59 ? 468  GLU B O   1 
ATOM   7778  C  CB  . GLU B  1 468 ? 32.170  22.923  32.868  1.00 109.58 ? 468  GLU B CB  1 
ATOM   7779  C  CG  . GLU B  1 468 ? 32.577  21.943  33.961  1.00 109.68 ? 468  GLU B CG  1 
ATOM   7780  C  CD  . GLU B  1 468 ? 32.777  20.530  33.431  1.00 110.24 ? 468  GLU B CD  1 
ATOM   7781  O  OE1 . GLU B  1 468 ? 32.291  20.232  32.315  1.00 109.56 ? 468  GLU B OE1 1 
ATOM   7782  O  OE2 . GLU B  1 468 ? 33.424  19.719  34.131  1.00 110.39 ? 468  GLU B OE2 1 
ATOM   7783  N  N   . GLU B  1 469 ? 30.798  24.571  35.424  1.00 106.18 ? 469  GLU B N   1 
ATOM   7784  C  CA  . GLU B  1 469 ? 29.646  24.881  36.254  1.00 102.53 ? 469  GLU B CA  1 
ATOM   7785  C  C   . GLU B  1 469 ? 29.211  26.342  36.137  1.00 104.60 ? 469  GLU B C   1 
ATOM   7786  O  O   . GLU B  1 469 ? 28.013  26.630  36.176  1.00 105.86 ? 469  GLU B O   1 
ATOM   7787  C  CB  . GLU B  1 469 ? 29.905  24.521  37.717  1.00 81.28  ? 469  GLU B CB  1 
ATOM   7788  C  CG  . GLU B  1 469 ? 29.738  23.050  38.031  1.00 65.73  ? 469  GLU B CG  1 
ATOM   7789  C  CD  . GLU B  1 469 ? 29.792  22.775  39.521  1.00 66.93  ? 469  GLU B CD  1 
ATOM   7790  O  OE1 . GLU B  1 469 ? 30.135  23.718  40.267  1.00 66.96  ? 469  GLU B OE1 1 
ATOM   7791  O  OE2 . GLU B  1 469 ? 29.487  21.633  39.949  1.00 64.71  ? 469  GLU B OE2 1 
ATOM   7792  N  N   . ARG B  1 470 ? 30.159  27.272  36.012  1.00 91.83  ? 470  ARG B N   1 
ATOM   7793  C  CA  . ARG B  1 470 ? 29.764  28.676  35.857  1.00 91.30  ? 470  ARG B CA  1 
ATOM   7794  C  C   . ARG B  1 470 ? 29.355  28.996  34.420  1.00 90.39  ? 470  ARG B C   1 
ATOM   7795  O  O   . ARG B  1 470 ? 28.545  29.898  34.186  1.00 88.98  ? 470  ARG B O   1 
ATOM   7796  C  CB  . ARG B  1 470 ? 30.802  29.676  36.405  1.00 105.46 ? 470  ARG B CB  1 
ATOM   7797  C  CG  . ARG B  1 470 ? 32.026  29.888  35.540  1.00 111.35 ? 470  ARG B CG  1 
ATOM   7798  C  CD  . ARG B  1 470 ? 32.519  31.339  35.581  1.00 113.05 ? 470  ARG B CD  1 
ATOM   7799  N  NE  . ARG B  1 470 ? 33.902  31.452  35.116  1.00 114.39 ? 470  ARG B NE  1 
ATOM   7800  C  CZ  . ARG B  1 470 ? 34.274  31.418  33.839  1.00 113.90 ? 470  ARG B CZ  1 
ATOM   7801  N  NH1 . ARG B  1 470 ? 33.363  31.278  32.882  1.00 112.34 ? 470  ARG B NH1 1 
ATOM   7802  N  NH2 . ARG B  1 470 ? 35.559  31.522  33.520  1.00 114.84 ? 470  ARG B NH2 1 
ATOM   7803  N  N   . ILE B  1 471 ? 29.892  28.251  33.457  1.00 100.93 ? 471  ILE B N   1 
ATOM   7804  C  CA  . ILE B  1 471 ? 29.416  28.427  32.085  1.00 101.56 ? 471  ILE B CA  1 
ATOM   7805  C  C   . ILE B  1 471 ? 27.985  27.868  31.970  1.00 97.66  ? 471  ILE B C   1 
ATOM   7806  O  O   . ILE B  1 471 ? 27.138  28.402  31.242  1.00 99.50  ? 471  ILE B O   1 
ATOM   7807  C  CB  . ILE B  1 471 ? 30.412  27.857  31.024  1.00 90.17  ? 471  ILE B CB  1 
ATOM   7808  C  CG1 . ILE B  1 471 ? 30.304  26.333  30.886  1.00 89.66  ? 471  ILE B CG1 1 
ATOM   7809  C  CG2 . ILE B  1 471 ? 31.847  28.284  31.356  1.00 90.07  ? 471  ILE B CG2 1 
ATOM   7810  C  CD1 . ILE B  1 471 ? 31.244  25.726  29.838  1.00 89.80  ? 471  ILE B CD1 1 
ATOM   7811  N  N   . PHE B  1 472 ? 27.729  26.811  32.737  1.00 75.67  ? 472  PHE B N   1 
ATOM   7812  C  CA  . PHE B  1 472 ? 26.394  26.259  32.939  1.00 72.25  ? 472  PHE B CA  1 
ATOM   7813  C  C   . PHE B  1 472 ? 25.481  27.326  33.549  1.00 67.78  ? 472  PHE B C   1 
ATOM   7814  O  O   . PHE B  1 472 ? 24.372  27.566  33.059  1.00 65.86  ? 472  PHE B O   1 
ATOM   7815  C  CB  . PHE B  1 472 ? 26.507  25.052  33.881  1.00 97.83  ? 472  PHE B CB  1 
ATOM   7816  C  CG  . PHE B  1 472 ? 25.223  24.294  34.094  1.00 99.35  ? 472  PHE B CG  1 
ATOM   7817  C  CD1 . PHE B  1 472 ? 24.110  24.510  33.293  1.00 101.16 ? 472  PHE B CD1 1 
ATOM   7818  C  CD2 . PHE B  1 472 ? 25.139  23.355  35.108  1.00 98.29  ? 472  PHE B CD2 1 
ATOM   7819  C  CE1 . PHE B  1 472 ? 22.938  23.808  33.500  1.00 99.90  ? 472  PHE B CE1 1 
ATOM   7820  C  CE2 . PHE B  1 472 ? 23.974  22.651  35.322  1.00 98.37  ? 472  PHE B CE2 1 
ATOM   7821  C  CZ  . PHE B  1 472 ? 22.869  22.876  34.514  1.00 98.98  ? 472  PHE B CZ  1 
ATOM   7822  N  N   . ALA B  1 473 ? 25.951  27.951  34.628  1.00 73.48  ? 473  ALA B N   1 
ATOM   7823  C  CA  . ALA B  1 473 ? 25.192  28.997  35.308  1.00 72.09  ? 473  ALA B CA  1 
ATOM   7824  C  C   . ALA B  1 473 ? 24.772  30.088  34.327  1.00 73.61  ? 473  ALA B C   1 
ATOM   7825  O  O   . ALA B  1 473 ? 23.581  30.434  34.237  1.00 70.04  ? 473  ALA B O   1 
ATOM   7826  C  CB  . ALA B  1 473 ? 25.995  29.584  36.457  1.00 65.55  ? 473  ALA B CB  1 
ATOM   7827  N  N   . GLN B  1 474 ? 25.751  30.603  33.580  1.00 85.63  ? 474  GLN B N   1 
ATOM   7828  C  CA  . GLN B  1 474 ? 25.492  31.619  32.558  1.00 88.13  ? 474  GLN B CA  1 
ATOM   7829  C  C   . GLN B  1 474 ? 24.437  31.122  31.559  1.00 89.87  ? 474  GLN B C   1 
ATOM   7830  O  O   . GLN B  1 474 ? 23.519  31.874  31.190  1.00 89.80  ? 474  GLN B O   1 
ATOM   7831  C  CB  . GLN B  1 474 ? 26.794  32.044  31.855  1.00 87.38  ? 474  GLN B CB  1 
ATOM   7832  C  CG  . GLN B  1 474 ? 27.817  32.732  32.782  1.00 89.60  ? 474  GLN B CG  1 
ATOM   7833  C  CD  . GLN B  1 474 ? 29.172  33.010  32.114  1.00 93.23  ? 474  GLN B CD  1 
ATOM   7834  O  OE1 . GLN B  1 474 ? 30.233  32.875  32.738  1.00 92.42  ? 474  GLN B OE1 1 
ATOM   7835  N  NE2 . GLN B  1 474 ? 29.136  33.411  30.847  1.00 95.93  ? 474  GLN B NE2 1 
ATOM   7836  N  N   . ARG B  1 475 ? 24.555  29.852  31.155  1.00 87.03  ? 475  ARG B N   1 
ATOM   7837  C  CA  . ARG B  1 475 ? 23.560  29.233  30.278  1.00 83.71  ? 475  ARG B CA  1 
ATOM   7838  C  C   . ARG B  1 475 ? 22.174  29.433  30.856  1.00 80.87  ? 475  ARG B C   1 
ATOM   7839  O  O   . ARG B  1 475 ? 21.286  29.976  30.192  1.00 80.67  ? 475  ARG B O   1 
ATOM   7840  C  CB  . ARG B  1 475 ? 23.801  27.727  30.123  1.00 80.74  ? 475  ARG B CB  1 
ATOM   7841  C  CG  . ARG B  1 475 ? 24.897  27.308  29.149  1.00 83.03  ? 475  ARG B CG  1 
ATOM   7842  C  CD  . ARG B  1 475 ? 24.881  25.785  28.957  1.00 81.31  ? 475  ARG B CD  1 
ATOM   7843  N  NE  . ARG B  1 475 ? 23.551  25.305  28.571  1.00 78.26  ? 475  ARG B NE  1 
ATOM   7844  C  CZ  . ARG B  1 475 ? 23.179  24.027  28.560  1.00 74.90  ? 475  ARG B CZ  1 
ATOM   7845  N  NH1 . ARG B  1 475 ? 24.031  23.076  28.920  1.00 73.81  ? 475  ARG B NH1 1 
ATOM   7846  N  NH2 . ARG B  1 475 ? 21.947  23.702  28.191  1.00 73.28  ? 475  ARG B NH2 1 
ATOM   7847  N  N   . LEU B  1 476 ? 22.009  29.011  32.109  1.00 83.34  ? 476  LEU B N   1 
ATOM   7848  C  CA  . LEU B  1 476 ? 20.697  29.013  32.764  1.00 81.14  ? 476  LEU B CA  1 
ATOM   7849  C  C   . LEU B  1 476 ? 20.110  30.410  32.924  1.00 76.20  ? 476  LEU B C   1 
ATOM   7850  O  O   . LEU B  1 476 ? 18.905  30.605  32.708  1.00 72.05  ? 476  LEU B O   1 
ATOM   7851  C  CB  . LEU B  1 476 ? 20.749  28.296  34.120  1.00 81.33  ? 476  LEU B CB  1 
ATOM   7852  C  CG  . LEU B  1 476 ? 21.074  26.796  34.092  1.00 80.49  ? 476  LEU B CG  1 
ATOM   7853  C  CD1 . LEU B  1 476 ? 21.160  26.234  35.498  1.00 78.12  ? 476  LEU B CD1 1 
ATOM   7854  C  CD2 . LEU B  1 476 ? 20.056  26.020  33.266  1.00 78.79  ? 476  LEU B CD2 1 
ATOM   7855  N  N   . MET B  1 477 ? 20.958  31.373  33.296  1.00 64.03  ? 477  MET B N   1 
ATOM   7856  C  CA  . MET B  1 477 ? 20.515  32.763  33.437  1.00 64.97  ? 477  MET B CA  1 
ATOM   7857  C  C   . MET B  1 477 ? 20.040  33.313  32.102  1.00 69.06  ? 477  MET B C   1 
ATOM   7858  O  O   . MET B  1 477 ? 19.007  33.997  32.033  1.00 65.76  ? 477  MET B O   1 
ATOM   7859  C  CB  . MET B  1 477 ? 21.619  33.640  34.016  1.00 65.52  ? 477  MET B CB  1 
ATOM   7860  C  CG  . MET B  1 477 ? 22.066  33.165  35.371  1.00 64.33  ? 477  MET B CG  1 
ATOM   7861  S  SD  . MET B  1 477 ? 23.689  33.760  35.854  1.00 107.42 ? 477  MET B SD  1 
ATOM   7862  C  CE  . MET B  1 477 ? 23.300  35.435  36.353  1.00 66.30  ? 477  MET B CE  1 
ATOM   7863  N  N   . LYS B  1 478 ? 20.789  32.995  31.043  1.00 89.68  ? 478  LYS B N   1 
ATOM   7864  C  CA  . LYS B  1 478 ? 20.376  33.346  29.683  1.00 93.06  ? 478  LYS B CA  1 
ATOM   7865  C  C   . LYS B  1 478 ? 18.999  32.763  29.381  1.00 91.22  ? 478  LYS B C   1 
ATOM   7866  O  O   . LYS B  1 478 ? 18.129  33.455  28.859  1.00 88.87  ? 478  LYS B O   1 
ATOM   7867  C  CB  . LYS B  1 478 ? 21.402  32.869  28.647  1.00 93.62  ? 478  LYS B CB  1 
ATOM   7868  C  CG  . LYS B  1 478 ? 22.064  34.006  27.862  1.00 97.43  ? 478  LYS B CG  1 
ATOM   7869  C  CD  . LYS B  1 478 ? 21.525  34.113  26.441  1.00 98.63  ? 478  LYS B CD  1 
ATOM   7870  C  CE  . LYS B  1 478 ? 21.810  35.482  25.852  1.00 99.71  ? 478  LYS B CE  1 
ATOM   7871  N  NZ  . LYS B  1 478 ? 21.089  36.540  26.607  1.00 98.02  ? 478  LYS B NZ  1 
ATOM   7872  N  N   . TYR B  1 479 ? 18.811  31.495  29.741  1.00 91.80  ? 479  TYR B N   1 
ATOM   7873  C  CA  . TYR B  1 479 ? 17.538  30.809  29.536  1.00 89.25  ? 479  TYR B CA  1 
ATOM   7874  C  C   . TYR B  1 479 ? 16.382  31.557  30.200  1.00 86.88  ? 479  TYR B C   1 
ATOM   7875  O  O   . TYR B  1 479 ? 15.403  31.967  29.541  1.00 88.35  ? 479  TYR B O   1 
ATOM   7876  C  CB  . TYR B  1 479 ? 17.623  29.377  30.080  1.00 82.35  ? 479  TYR B CB  1 
ATOM   7877  C  CG  . TYR B  1 479 ? 18.353  28.408  29.171  1.00 83.98  ? 479  TYR B CG  1 
ATOM   7878  C  CD1 . TYR B  1 479 ? 17.992  28.270  27.837  1.00 85.08  ? 479  TYR B CD1 1 
ATOM   7879  C  CD2 . TYR B  1 479 ? 19.408  27.633  29.647  1.00 85.73  ? 479  TYR B CD2 1 
ATOM   7880  C  CE1 . TYR B  1 479 ? 18.665  27.387  26.996  1.00 88.17  ? 479  TYR B CE1 1 
ATOM   7881  C  CE2 . TYR B  1 479 ? 20.088  26.745  28.814  1.00 88.41  ? 479  TYR B CE2 1 
ATOM   7882  C  CZ  . TYR B  1 479 ? 19.712  26.625  27.487  1.00 89.65  ? 479  TYR B CZ  1 
ATOM   7883  O  OH  . TYR B  1 479 ? 20.379  25.748  26.648  1.00 90.87  ? 479  TYR B OH  1 
ATOM   7884  N  N   . TRP B  1 480 ? 16.516  31.748  31.508  1.00 66.97  ? 480  TRP B N   1 
ATOM   7885  C  CA  . TRP B  1 480 ? 15.449  32.338  32.308  1.00 63.26  ? 480  TRP B CA  1 
ATOM   7886  C  C   . TRP B  1 480 ? 15.130  33.763  31.853  1.00 63.70  ? 480  TRP B C   1 
ATOM   7887  O  O   . TRP B  1 480 ? 13.965  34.131  31.707  1.00 60.64  ? 480  TRP B O   1 
ATOM   7888  C  CB  . TRP B  1 480 ? 15.823  32.309  33.791  1.00 63.04  ? 480  TRP B CB  1 
ATOM   7889  C  CG  . TRP B  1 480 ? 15.216  31.180  34.616  1.00 56.75  ? 480  TRP B CG  1 
ATOM   7890  C  CD1 . TRP B  1 480 ? 14.578  31.310  35.815  1.00 55.09  ? 480  TRP B CD1 1 
ATOM   7891  C  CD2 . TRP B  1 480 ? 15.211  29.770  34.319  1.00 56.12  ? 480  TRP B CD2 1 
ATOM   7892  N  NE1 . TRP B  1 480 ? 14.177  30.081  36.281  1.00 53.48  ? 480  TRP B NE1 1 
ATOM   7893  C  CE2 . TRP B  1 480 ? 14.554  29.118  35.379  1.00 54.07  ? 480  TRP B CE2 1 
ATOM   7894  C  CE3 . TRP B  1 480 ? 15.703  28.994  33.265  1.00 57.15  ? 480  TRP B CE3 1 
ATOM   7895  C  CZ2 . TRP B  1 480 ? 14.369  27.732  35.410  1.00 53.85  ? 480  TRP B CZ2 1 
ATOM   7896  C  CZ3 . TRP B  1 480 ? 15.510  27.608  33.300  1.00 56.09  ? 480  TRP B CZ3 1 
ATOM   7897  C  CH2 . TRP B  1 480 ? 14.850  27.000  34.359  1.00 54.07  ? 480  TRP B CH2 1 
ATOM   7898  N  N   . THR B  1 481 ? 16.165  34.558  31.603  1.00 74.17  ? 481  THR B N   1 
ATOM   7899  C  CA  . THR B  1 481 ? 15.955  35.949  31.204  1.00 81.33  ? 481  THR B CA  1 
ATOM   7900  C  C   . THR B  1 481 ? 15.381  36.087  29.789  1.00 82.91  ? 481  THR B C   1 
ATOM   7901  O  O   . THR B  1 481 ? 14.546  36.972  29.530  1.00 81.14  ? 481  THR B O   1 
ATOM   7902  C  CB  . THR B  1 481 ? 17.246  36.760  31.324  1.00 104.30 ? 481  THR B CB  1 
ATOM   7903  O  OG1 . THR B  1 481 ? 18.330  36.003  30.771  1.00 109.35 ? 481  THR B OG1 1 
ATOM   7904  C  CG2 . THR B  1 481 ? 17.539  37.060  32.785  1.00 102.46 ? 481  THR B CG2 1 
ATOM   7905  N  N   . ASN B  1 482 ? 15.837  35.219  28.881  1.00 93.83  ? 482  ASN B N   1 
ATOM   7906  C  CA  . ASN B  1 482 ? 15.262  35.135  27.539  1.00 96.99  ? 482  ASN B CA  1 
ATOM   7907  C  C   . ASN B  1 482 ? 13.771  34.846  27.626  1.00 93.30  ? 482  ASN B C   1 
ATOM   7908  O  O   . ASN B  1 482 ? 12.979  35.415  26.866  1.00 93.15  ? 482  ASN B O   1 
ATOM   7909  C  CB  . ASN B  1 482 ? 15.943  34.055  26.689  1.00 107.53 ? 482  ASN B CB  1 
ATOM   7910  C  CG  . ASN B  1 482 ? 17.294  34.492  26.147  1.00 113.38 ? 482  ASN B CG  1 
ATOM   7911  O  OD1 . ASN B  1 482 ? 18.257  33.723  26.161  1.00 114.26 ? 482  ASN B OD1 1 
ATOM   7912  N  ND2 . ASN B  1 482 ? 17.370  35.726  25.657  1.00 116.75 ? 482  ASN B ND2 1 
ATOM   7913  N  N   . PHE B  1 483 ? 13.390  33.963  28.553  1.00 76.98  ? 483  PHE B N   1 
ATOM   7914  C  CA  . PHE B  1 483 ? 11.966  33.707  28.782  1.00 73.43  ? 483  PHE B CA  1 
ATOM   7915  C  C   . PHE B  1 483 ? 11.240  34.923  29.364  1.00 71.56  ? 483  PHE B C   1 
ATOM   7916  O  O   . PHE B  1 483 ? 10.103  35.220  28.986  1.00 61.08  ? 483  PHE B O   1 
ATOM   7917  C  CB  . PHE B  1 483 ? 11.737  32.488  29.679  1.00 80.20  ? 483  PHE B CB  1 
ATOM   7918  C  CG  . PHE B  1 483 ? 10.284  32.240  29.982  1.00 78.06  ? 483  PHE B CG  1 
ATOM   7919  C  CD1 . PHE B  1 483 ? 9.425   31.787  28.992  1.00 79.13  ? 483  PHE B CD1 1 
ATOM   7920  C  CD2 . PHE B  1 483 ? 9.771   32.484  31.242  1.00 74.77  ? 483  PHE B CD2 1 
ATOM   7921  C  CE1 . PHE B  1 483 ? 8.089   31.570  29.260  1.00 77.05  ? 483  PHE B CE1 1 
ATOM   7922  C  CE2 . PHE B  1 483 ? 8.439   32.274  31.511  1.00 73.20  ? 483  PHE B CE2 1 
ATOM   7923  C  CZ  . PHE B  1 483 ? 7.598   31.813  30.521  1.00 74.33  ? 483  PHE B CZ  1 
ATOM   7924  N  N   . ALA B  1 484 ? 11.903  35.610  30.292  1.00 75.18  ? 484  ALA B N   1 
ATOM   7925  C  CA  . ALA B  1 484 ? 11.354  36.814  30.906  1.00 74.37  ? 484  ALA B CA  1 
ATOM   7926  C  C   . ALA B  1 484 ? 10.946  37.834  29.847  1.00 78.61  ? 484  ALA B C   1 
ATOM   7927  O  O   . ALA B  1 484 ? 9.790   38.265  29.803  1.00 75.23  ? 484  ALA B O   1 
ATOM   7928  C  CB  . ALA B  1 484 ? 12.361  37.423  31.869  1.00 68.87  ? 484  ALA B CB  1 
ATOM   7929  N  N   . ARG B  1 485 ? 11.896  38.198  28.983  1.00 90.66  ? 485  ARG B N   1 
ATOM   7930  C  CA  . ARG B  1 485 ? 11.628  39.167  27.915  1.00 93.07  ? 485  ARG B CA  1 
ATOM   7931  C  C   . ARG B  1 485 ? 10.677  38.639  26.813  1.00 89.21  ? 485  ARG B C   1 
ATOM   7932  O  O   . ARG B  1 485 ? 9.673   39.280  26.488  1.00 85.23  ? 485  ARG B O   1 
ATOM   7933  C  CB  . ARG B  1 485 ? 12.947  39.713  27.327  1.00 102.44 ? 485  ARG B CB  1 
ATOM   7934  C  CG  . ARG B  1 485 ? 13.961  38.650  26.882  1.00 105.88 ? 485  ARG B CG  1 
ATOM   7935  C  CD  . ARG B  1 485 ? 15.307  39.259  26.445  1.00 111.13 ? 485  ARG B CD  1 
ATOM   7936  N  NE  . ARG B  1 485 ? 16.157  39.672  27.571  1.00 113.18 ? 485  ARG B NE  1 
ATOM   7937  C  CZ  . ARG B  1 485 ? 17.385  39.204  27.812  1.00 112.83 ? 485  ARG B CZ  1 
ATOM   7938  N  NH1 . ARG B  1 485 ? 17.928  38.298  27.006  1.00 114.00 ? 485  ARG B NH1 1 
ATOM   7939  N  NH2 . ARG B  1 485 ? 18.078  39.643  28.862  1.00 109.94 ? 485  ARG B NH2 1 
ATOM   7940  N  N   . THR B  1 486 ? 10.983  37.467  26.259  1.00 92.70  ? 486  THR B N   1 
ATOM   7941  C  CA  . THR B  1 486 ? 10.232  36.940  25.117  1.00 93.58  ? 486  THR B CA  1 
ATOM   7942  C  C   . THR B  1 486 ? 8.903   36.280  25.465  1.00 91.27  ? 486  THR B C   1 
ATOM   7943  O  O   . THR B  1 486 ? 7.897   36.511  24.794  1.00 92.37  ? 486  THR B O   1 
ATOM   7944  C  CB  . THR B  1 486 ? 11.041  35.871  24.347  1.00 94.02  ? 486  THR B CB  1 
ATOM   7945  O  OG1 . THR B  1 486 ? 12.445  36.148  24.444  1.00 97.33  ? 486  THR B OG1 1 
ATOM   7946  C  CG2 . THR B  1 486 ? 10.599  35.805  22.877  1.00 94.07  ? 486  THR B CG2 1 
ATOM   7947  N  N   . GLY B  1 487 ? 8.900   35.476  26.526  1.00 83.32  ? 487  GLY B N   1 
ATOM   7948  C  CA  . GLY B  1 487 ? 7.915   34.419  26.672  1.00 77.80  ? 487  GLY B CA  1 
ATOM   7949  C  C   . GLY B  1 487 ? 8.371   33.232  25.845  1.00 76.32  ? 487  GLY B C   1 
ATOM   7950  O  O   . GLY B  1 487 ? 7.578   32.582  25.157  1.00 75.75  ? 487  GLY B O   1 
ATOM   7951  N  N   . ASP B  1 488 ? 9.670   32.953  25.943  1.00 70.85  ? 488  ASP B N   1 
ATOM   7952  C  CA  . ASP B  1 488 ? 10.343  31.913  25.172  1.00 72.78  ? 488  ASP B CA  1 
ATOM   7953  C  C   . ASP B  1 488 ? 11.791  31.892  25.667  1.00 72.00  ? 488  ASP B C   1 
ATOM   7954  O  O   . ASP B  1 488 ? 12.458  32.929  25.689  1.00 72.71  ? 488  ASP B O   1 
ATOM   7955  C  CB  . ASP B  1 488 ? 10.296  32.293  23.677  1.00 87.29  ? 488  ASP B CB  1 
ATOM   7956  C  CG  . ASP B  1 488 ? 10.883  31.223  22.747  1.00 89.26  ? 488  ASP B CG  1 
ATOM   7957  O  OD1 . ASP B  1 488 ? 11.991  30.706  23.012  1.00 90.96  ? 488  ASP B OD1 1 
ATOM   7958  O  OD2 . ASP B  1 488 ? 10.233  30.920  21.721  1.00 88.12  ? 488  ASP B OD2 1 
ATOM   7959  N  N   . PRO B  1 489 ? 12.294  30.693  26.018  1.00 69.40  ? 489  PRO B N   1 
ATOM   7960  C  CA  . PRO B  1 489 ? 13.611  30.449  26.623  1.00 69.46  ? 489  PRO B CA  1 
ATOM   7961  C  C   . PRO B  1 489 ? 14.776  30.600  25.674  1.00 73.56  ? 489  PRO B C   1 
ATOM   7962  O  O   . PRO B  1 489 ? 15.897  30.668  26.158  1.00 75.19  ? 489  PRO B O   1 
ATOM   7963  C  CB  . PRO B  1 489 ? 13.525  28.993  27.085  1.00 81.22  ? 489  PRO B CB  1 
ATOM   7964  C  CG  . PRO B  1 489 ? 12.530  28.376  26.172  1.00 81.77  ? 489  PRO B CG  1 
ATOM   7965  C  CD  . PRO B  1 489 ? 11.513  29.449  25.909  1.00 81.19  ? 489  PRO B CD  1 
ATOM   7966  N  N   . ASN B  1 490 ? 14.530  30.605  24.366  1.00 80.65  ? 490  ASN B N   1 
ATOM   7967  C  CA  . ASN B  1 490 ? 15.621  30.528  23.396  1.00 86.52  ? 490  ASN B CA  1 
ATOM   7968  C  C   . ASN B  1 490 ? 16.283  31.850  23.029  1.00 95.55  ? 490  ASN B C   1 
ATOM   7969  O  O   . ASN B  1 490 ? 15.837  32.927  23.440  1.00 93.70  ? 490  ASN B O   1 
ATOM   7970  C  CB  . ASN B  1 490 ? 15.134  29.861  22.112  1.00 77.58  ? 490  ASN B CB  1 
ATOM   7971  C  CG  . ASN B  1 490 ? 14.743  28.423  22.319  1.00 74.38  ? 490  ASN B CG  1 
ATOM   7972  O  OD1 . ASN B  1 490 ? 15.601  27.537  22.358  1.00 68.55  ? 490  ASN B OD1 1 
ATOM   7973  N  ND2 . ASN B  1 490 ? 13.442  28.174  22.444  1.00 71.54  ? 490  ASN B ND2 1 
ATOM   7974  N  N   . ASP B  1 491 ? 17.341  31.748  22.226  1.00 116.33 ? 491  ASP B N   1 
ATOM   7975  C  CA  . ASP B  1 491 ? 17.982  32.917  21.647  1.00 125.96 ? 491  ASP B CA  1 
ATOM   7976  C  C   . ASP B  1 491 ? 17.103  33.383  20.500  1.00 131.19 ? 491  ASP B C   1 
ATOM   7977  O  O   . ASP B  1 491 ? 16.518  32.559  19.788  1.00 130.18 ? 491  ASP B O   1 
ATOM   7978  C  CB  . ASP B  1 491 ? 19.389  32.591  21.120  1.00 126.21 ? 491  ASP B CB  1 
ATOM   7979  C  CG  . ASP B  1 491 ? 20.359  32.184  22.221  1.00 125.63 ? 491  ASP B CG  1 
ATOM   7980  O  OD1 . ASP B  1 491 ? 20.050  31.237  22.980  1.00 123.79 ? 491  ASP B OD1 1 
ATOM   7981  O  OD2 . ASP B  1 491 ? 21.436  32.813  22.321  1.00 126.36 ? 491  ASP B OD2 1 
ATOM   7982  N  N   . PRO B  1 492 ? 16.994  34.707  20.327  1.00 134.22 ? 492  PRO B N   1 
ATOM   7983  C  CA  . PRO B  1 492 ? 16.253  35.297  19.206  1.00 138.16 ? 492  PRO B CA  1 
ATOM   7984  C  C   . PRO B  1 492 ? 16.802  34.805  17.867  1.00 142.46 ? 492  PRO B C   1 
ATOM   7985  O  O   . PRO B  1 492 ? 16.042  34.458  16.957  1.00 141.26 ? 492  PRO B O   1 
ATOM   7986  C  CB  . PRO B  1 492 ? 16.533  36.798  19.360  1.00 133.98 ? 492  PRO B CB  1 
ATOM   7987  C  CG  . PRO B  1 492 ? 16.840  36.981  20.809  1.00 131.50 ? 492  PRO B CG  1 
ATOM   7988  C  CD  . PRO B  1 492 ? 17.553  35.731  21.228  1.00 129.86 ? 492  PRO B CD  1 
ATOM   7989  N  N   . ARG B  1 493 ? 18.130  34.762  17.782  1.00 150.20 ? 493  ARG B N   1 
ATOM   7990  C  CA  . ARG B  1 493 ? 18.854  34.454  16.552  1.00 153.12 ? 493  ARG B CA  1 
ATOM   7991  C  C   . ARG B  1 493 ? 19.541  33.080  16.583  1.00 154.51 ? 493  ARG B C   1 
ATOM   7992  O  O   . ARG B  1 493 ? 19.245  32.200  15.771  1.00 154.34 ? 493  ARG B O   1 
ATOM   7993  C  CB  . ARG B  1 493 ? 19.876  35.564  16.262  1.00 142.09 ? 493  ARG B CB  1 
ATOM   7994  C  CG  . ARG B  1 493 ? 20.587  36.107  17.508  1.00 140.03 ? 493  ARG B CG  1 
ATOM   7995  C  CD  . ARG B  1 493 ? 22.050  35.656  17.574  1.00 140.19 ? 493  ARG B CD  1 
ATOM   7996  N  NE  . ARG B  1 493 ? 22.595  35.709  18.931  1.00 137.25 ? 493  ARG B NE  1 
ATOM   7997  C  CZ  . ARG B  1 493 ? 23.827  35.328  19.260  1.00 135.71 ? 493  ARG B CZ  1 
ATOM   7998  N  NH1 . ARG B  1 493 ? 24.652  34.863  18.330  1.00 137.14 ? 493  ARG B NH1 1 
ATOM   7999  N  NH2 . ARG B  1 493 ? 24.234  35.412  20.521  1.00 133.08 ? 493  ARG B NH2 1 
ATOM   8000  N  N   . ASP B  1 494 ? 20.456  32.924  17.534  1.00 155.69 ? 494  ASP B N   1 
ATOM   8001  C  CA  . ASP B  1 494 ? 21.412  31.821  17.586  1.00 155.58 ? 494  ASP B CA  1 
ATOM   8002  C  C   . ASP B  1 494 ? 20.805  30.419  17.471  1.00 152.64 ? 494  ASP B C   1 
ATOM   8003  O  O   . ASP B  1 494 ? 19.843  30.081  18.166  1.00 151.43 ? 494  ASP B O   1 
ATOM   8004  C  CB  . ASP B  1 494 ? 22.221  31.937  18.883  1.00 148.94 ? 494  ASP B CB  1 
ATOM   8005  C  CG  . ASP B  1 494 ? 23.339  30.926  18.967  1.00 149.50 ? 494  ASP B CG  1 
ATOM   8006  O  OD1 . ASP B  1 494 ? 23.808  30.464  17.904  1.00 151.23 ? 494  ASP B OD1 1 
ATOM   8007  O  OD2 . ASP B  1 494 ? 23.750  30.599  20.100  1.00 147.89 ? 494  ASP B OD2 1 
ATOM   8008  N  N   . SER B  1 495 ? 21.367  29.622  16.564  1.00 149.98 ? 495  SER B N   1 
ATOM   8009  C  CA  . SER B  1 495 ? 21.009  28.212  16.425  1.00 145.93 ? 495  SER B CA  1 
ATOM   8010  C  C   . SER B  1 495 ? 22.258  27.346  16.179  1.00 145.24 ? 495  SER B C   1 
ATOM   8011  O  O   . SER B  1 495 ? 22.905  27.545  15.151  1.00 148.29 ? 495  SER B O   1 
ATOM   8012  C  CB  . SER B  1 495 ? 20.030  28.054  15.253  1.00 132.46 ? 495  SER B CB  1 
ATOM   8013  O  OG  . SER B  1 495 ? 19.663  26.700  15.050  1.00 130.34 ? 495  SER B OG  1 
ATOM   8014  N  N   . LYS B  1 496 ? 22.638  26.392  17.046  1.00 135.84 ? 496  LYS B N   1 
ATOM   8015  C  CA  . LYS B  1 496 ? 22.137  26.072  18.402  1.00 130.46 ? 496  LYS B CA  1 
ATOM   8016  C  C   . LYS B  1 496 ? 20.600  25.804  18.519  1.00 148.09 ? 496  LYS B C   1 
ATOM   8017  O  O   . LYS B  1 496 ? 20.001  25.404  17.517  1.00 149.12 ? 496  LYS B O   1 
ATOM   8018  C  CB  . LYS B  1 496 ? 22.631  27.196  19.335  1.00 119.37 ? 496  LYS B CB  1 
ATOM   8019  C  CG  . LYS B  1 496 ? 24.022  26.982  19.919  1.00 116.91 ? 496  LYS B CG  1 
ATOM   8020  C  CD  . LYS B  1 496 ? 23.976  26.941  21.447  1.00 112.48 ? 496  LYS B CD  1 
ATOM   8021  C  CE  . LYS B  1 496 ? 23.321  28.195  22.031  1.00 109.73 ? 496  LYS B CE  1 
ATOM   8022  N  NZ  . LYS B  1 496 ? 23.011  28.083  23.489  1.00 106.09 ? 496  LYS B NZ  1 
ATOM   8023  N  N   . SER B  1 497 ? 19.935  25.987  19.674  1.00 149.11 ? 497  SER B N   1 
ATOM   8024  C  CA  . SER B  1 497 ? 20.464  25.728  21.036  1.00 147.22 ? 497  SER B CA  1 
ATOM   8025  C  C   . SER B  1 497 ? 21.063  24.309  21.287  1.00 143.30 ? 497  SER B C   1 
ATOM   8026  O  O   . SER B  1 497 ? 22.061  24.191  22.003  1.00 143.75 ? 497  SER B O   1 
ATOM   8027  C  CB  . SER B  1 497 ? 19.436  26.120  22.126  1.00 130.09 ? 497  SER B CB  1 
ATOM   8028  O  OG  . SER B  1 497 ? 20.043  26.333  23.397  1.00 127.02 ? 497  SER B OG  1 
ATOM   8029  N  N   . PRO B  1 498 ? 20.482  23.229  20.707  1.00 142.94 ? 498  PRO B N   1 
ATOM   8030  C  CA  . PRO B  1 498 ? 19.321  23.027  19.824  1.00 141.73 ? 498  PRO B CA  1 
ATOM   8031  C  C   . PRO B  1 498 ? 18.020  23.568  20.414  1.00 138.14 ? 498  PRO B C   1 
ATOM   8032  O  O   . PRO B  1 498 ? 17.858  23.587  21.636  1.00 136.74 ? 498  PRO B O   1 
ATOM   8033  C  CB  . PRO B  1 498 ? 19.256  21.500  19.666  1.00 129.96 ? 498  PRO B CB  1 
ATOM   8034  C  CG  . PRO B  1 498 ? 20.646  21.053  19.861  1.00 130.94 ? 498  PRO B CG  1 
ATOM   8035  C  CD  . PRO B  1 498 ? 21.198  21.959  20.932  1.00 131.41 ? 498  PRO B CD  1 
ATOM   8036  N  N   . GLN B  1 499 ? 17.109  23.983  19.539  1.00 139.65 ? 499  GLN B N   1 
ATOM   8037  C  CA  . GLN B  1 499 ? 15.885  24.677  19.932  1.00 133.47 ? 499  GLN B CA  1 
ATOM   8038  C  C   . GLN B  1 499 ? 15.093  23.975  21.041  1.00 126.79 ? 499  GLN B C   1 
ATOM   8039  O  O   . GLN B  1 499 ? 14.832  22.771  20.977  1.00 126.86 ? 499  GLN B O   1 
ATOM   8040  C  CB  . GLN B  1 499 ? 14.992  24.898  18.705  1.00 114.50 ? 499  GLN B CB  1 
ATOM   8041  C  CG  . GLN B  1 499 ? 15.374  26.110  17.873  1.00 115.28 ? 499  GLN B CG  1 
ATOM   8042  C  CD  . GLN B  1 499 ? 14.795  27.395  18.431  1.00 113.48 ? 499  GLN B CD  1 
ATOM   8043  O  OE1 . GLN B  1 499 ? 13.676  27.408  18.950  1.00 110.32 ? 499  GLN B OE1 1 
ATOM   8044  N  NE2 . GLN B  1 499 ? 15.556  28.483  18.335  1.00 115.23 ? 499  GLN B NE2 1 
ATOM   8045  N  N   . TRP B  1 500 ? 14.715  24.754  22.054  1.00 103.77 ? 500  TRP B N   1 
ATOM   8046  C  CA  . TRP B  1 500 ? 13.907  24.270  23.164  1.00 91.26  ? 500  TRP B CA  1 
ATOM   8047  C  C   . TRP B  1 500 ? 12.466  24.361  22.701  1.00 79.38  ? 500  TRP B C   1 
ATOM   8048  O  O   . TRP B  1 500 ? 11.897  25.451  22.600  1.00 77.72  ? 500  TRP B O   1 
ATOM   8049  C  CB  . TRP B  1 500 ? 14.141  25.166  24.383  1.00 98.88  ? 500  TRP B CB  1 
ATOM   8050  C  CG  . TRP B  1 500 ? 13.376  24.839  25.652  1.00 98.69  ? 500  TRP B CG  1 
ATOM   8051  C  CD1 . TRP B  1 500 ? 12.121  24.306  25.761  1.00 98.31  ? 500  TRP B CD1 1 
ATOM   8052  C  CD2 . TRP B  1 500 ? 13.832  25.058  26.994  1.00 97.64  ? 500  TRP B CD2 1 
ATOM   8053  N  NE1 . TRP B  1 500 ? 11.776  24.168  27.086  1.00 95.06  ? 500  TRP B NE1 1 
ATOM   8054  C  CE2 . TRP B  1 500 ? 12.808  24.626  27.859  1.00 95.75  ? 500  TRP B CE2 1 
ATOM   8055  C  CE3 . TRP B  1 500 ? 15.009  25.577  27.544  1.00 97.38  ? 500  TRP B CE3 1 
ATOM   8056  C  CZ2 . TRP B  1 500 ? 12.932  24.693  29.239  1.00 94.65  ? 500  TRP B CZ2 1 
ATOM   8057  C  CZ3 . TRP B  1 500 ? 15.127  25.644  28.912  1.00 95.30  ? 500  TRP B CZ3 1 
ATOM   8058  C  CH2 . TRP B  1 500 ? 14.097  25.206  29.745  1.00 94.52  ? 500  TRP B CH2 1 
ATOM   8059  N  N   . PRO B  1 501 ? 11.871  23.198  22.425  1.00 62.21  ? 501  PRO B N   1 
ATOM   8060  C  CA  . PRO B  1 501 ? 10.529  23.046  21.858  1.00 61.57  ? 501  PRO B CA  1 
ATOM   8061  C  C   . PRO B  1 501 ? 9.425   23.257  22.876  1.00 59.41  ? 501  PRO B C   1 
ATOM   8062  O  O   . PRO B  1 501 ? 9.572   22.845  24.017  1.00 57.93  ? 501  PRO B O   1 
ATOM   8063  C  CB  . PRO B  1 501 ? 10.520  21.593  21.382  1.00 62.82  ? 501  PRO B CB  1 
ATOM   8064  C  CG  . PRO B  1 501 ? 11.645  20.907  22.126  1.00 61.29  ? 501  PRO B CG  1 
ATOM   8065  C  CD  . PRO B  1 501 ? 12.448  21.917  22.859  1.00 61.55  ? 501  PRO B CD  1 
ATOM   8066  N  N   . PRO B  1 502 ? 8.317   23.878  22.471  1.00 84.49  ? 502  PRO B N   1 
ATOM   8067  C  CA  . PRO B  1 502 ? 7.203   23.997  23.412  1.00 86.52  ? 502  PRO B CA  1 
ATOM   8068  C  C   . PRO B  1 502 ? 6.587   22.644  23.752  1.00 86.91  ? 502  PRO B C   1 
ATOM   8069  O  O   . PRO B  1 502 ? 6.314   21.854  22.847  1.00 92.14  ? 502  PRO B O   1 
ATOM   8070  C  CB  . PRO B  1 502 ? 6.202   24.857  22.644  1.00 84.41  ? 502  PRO B CB  1 
ATOM   8071  C  CG  . PRO B  1 502 ? 7.059   25.692  21.766  1.00 86.42  ? 502  PRO B CG  1 
ATOM   8072  C  CD  . PRO B  1 502 ? 8.154   24.771  21.316  1.00 86.04  ? 502  PRO B CD  1 
ATOM   8073  N  N   . TYR B  1 503 ? 6.389   22.389  25.044  1.00 63.48  ? 503  TYR B N   1 
ATOM   8074  C  CA  . TYR B  1 503 ? 5.683   21.202  25.507  1.00 59.75  ? 503  TYR B CA  1 
ATOM   8075  C  C   . TYR B  1 503 ? 4.262   21.298  24.971  1.00 59.44  ? 503  TYR B C   1 
ATOM   8076  O  O   . TYR B  1 503 ? 3.598   22.318  25.162  1.00 59.11  ? 503  TYR B O   1 
ATOM   8077  C  CB  . TYR B  1 503 ? 5.681   21.157  27.049  1.00 62.76  ? 503  TYR B CB  1 
ATOM   8078  C  CG  . TYR B  1 503 ? 4.984   19.961  27.681  1.00 59.70  ? 503  TYR B CG  1 
ATOM   8079  C  CD1 . TYR B  1 503 ? 5.659   18.763  27.880  1.00 60.52  ? 503  TYR B CD1 1 
ATOM   8080  C  CD2 . TYR B  1 503 ? 3.660   20.040  28.103  1.00 57.87  ? 503  TYR B CD2 1 
ATOM   8081  C  CE1 . TYR B  1 503 ? 5.026   17.660  28.462  1.00 59.83  ? 503  TYR B CE1 1 
ATOM   8082  C  CE2 . TYR B  1 503 ? 3.016   18.943  28.688  1.00 56.93  ? 503  TYR B CE2 1 
ATOM   8083  C  CZ  . TYR B  1 503 ? 3.704   17.752  28.863  1.00 56.52  ? 503  TYR B CZ  1 
ATOM   8084  O  OH  . TYR B  1 503 ? 3.077   16.656  29.437  1.00 51.07  ? 503  TYR B OH  1 
ATOM   8085  N  N   . THR B  1 504 ? 3.815   20.255  24.271  1.00 66.32  ? 504  THR B N   1 
ATOM   8086  C  CA  . THR B  1 504 ? 2.430   20.156  23.814  1.00 65.53  ? 504  THR B CA  1 
ATOM   8087  C  C   . THR B  1 504 ? 1.838   18.855  24.335  1.00 64.56  ? 504  THR B C   1 
ATOM   8088  O  O   . THR B  1 504 ? 2.564   17.957  24.758  1.00 64.77  ? 504  THR B O   1 
ATOM   8089  C  CB  . THR B  1 504 ? 2.304   20.175  22.275  1.00 68.60  ? 504  THR B CB  1 
ATOM   8090  O  OG1 . THR B  1 504 ? 2.605   18.878  21.745  1.00 68.38  ? 504  THR B OG1 1 
ATOM   8091  C  CG2 . THR B  1 504 ? 3.235   21.218  21.660  1.00 71.73  ? 504  THR B CG2 1 
ATOM   8092  N  N   . THR B  1 505 ? 0.517   18.754  24.309  1.00 58.80  ? 505  THR B N   1 
ATOM   8093  C  CA  . THR B  1 505 ? -0.154  17.572  24.830  1.00 58.62  ? 505  THR B CA  1 
ATOM   8094  C  C   . THR B  1 505 ? 0.127   16.338  23.971  1.00 59.10  ? 505  THR B C   1 
ATOM   8095  O  O   . THR B  1 505 ? 0.057   15.203  24.444  1.00 56.10  ? 505  THR B O   1 
ATOM   8096  C  CB  . THR B  1 505 ? -1.662  17.814  24.922  1.00 71.83  ? 505  THR B CB  1 
ATOM   8097  O  OG1 . THR B  1 505 ? -1.969  19.093  24.345  1.00 74.38  ? 505  THR B OG1 1 
ATOM   8098  C  CG2 . THR B  1 505 ? -2.106  17.801  26.376  1.00 70.84  ? 505  THR B CG2 1 
ATOM   8099  N  N   . ALA B  1 506 ? 0.456   16.569  22.704  1.00 71.21  ? 506  ALA B N   1 
ATOM   8100  C  CA  . ALA B  1 506 ? 0.732   15.478  21.782  1.00 73.34  ? 506  ALA B CA  1 
ATOM   8101  C  C   . ALA B  1 506 ? 2.197   15.052  21.841  1.00 78.58  ? 506  ALA B C   1 
ATOM   8102  O  O   . ALA B  1 506 ? 2.509   13.933  22.241  1.00 80.02  ? 506  ALA B O   1 
ATOM   8103  C  CB  . ALA B  1 506 ? 0.347   15.876  20.375  1.00 67.67  ? 506  ALA B CB  1 
ATOM   8104  N  N   . ALA B  1 507 ? 3.093   15.950  21.443  1.00 84.30  ? 507  ALA B N   1 
ATOM   8105  C  CA  . ALA B  1 507 ? 4.526   15.654  21.407  1.00 86.33  ? 507  ALA B CA  1 
ATOM   8106  C  C   . ALA B  1 507 ? 5.097   15.356  22.792  1.00 83.67  ? 507  ALA B C   1 
ATOM   8107  O  O   . ALA B  1 507 ? 5.872   14.409  22.959  1.00 84.15  ? 507  ALA B O   1 
ATOM   8108  C  CB  . ALA B  1 507 ? 5.294   16.814  20.752  1.00 87.42  ? 507  ALA B CB  1 
ATOM   8109  N  N   . GLN B  1 508 ? 4.700   16.178  23.767  1.00 69.35  ? 508  GLN B N   1 
ATOM   8110  C  CA  . GLN B  1 508 ? 5.187   16.118  25.151  1.00 62.21  ? 508  GLN B CA  1 
ATOM   8111  C  C   . GLN B  1 508 ? 6.690   16.299  25.258  1.00 58.79  ? 508  GLN B C   1 
ATOM   8112  O  O   . GLN B  1 508 ? 7.351   15.614  26.035  1.00 55.09  ? 508  GLN B O   1 
ATOM   8113  C  CB  . GLN B  1 508 ? 4.767   14.820  25.837  1.00 66.33  ? 508  GLN B CB  1 
ATOM   8114  C  CG  . GLN B  1 508 ? 3.296   14.750  26.149  1.00 66.08  ? 508  GLN B CG  1 
ATOM   8115  C  CD  . GLN B  1 508 ? 2.950   13.499  26.907  1.00 66.18  ? 508  GLN B CD  1 
ATOM   8116  O  OE1 . GLN B  1 508 ? 2.637   13.544  28.098  1.00 66.25  ? 508  GLN B OE1 1 
ATOM   8117  N  NE2 . GLN B  1 508 ? 3.013   12.365  26.226  1.00 65.86  ? 508  GLN B NE2 1 
ATOM   8118  N  N   . GLN B  1 509 ? 7.229   17.225  24.477  1.00 69.17  ? 509  GLN B N   1 
ATOM   8119  C  CA  . GLN B  1 509 ? 8.661   17.459  24.509  1.00 71.92  ? 509  GLN B CA  1 
ATOM   8120  C  C   . GLN B  1 509 ? 9.035   18.262  25.751  1.00 70.46  ? 509  GLN B C   1 
ATOM   8121  O  O   . GLN B  1 509 ? 8.433   19.301  26.039  1.00 68.07  ? 509  GLN B O   1 
ATOM   8122  C  CB  . GLN B  1 509 ? 9.144   18.165  23.230  1.00 76.02  ? 509  GLN B CB  1 
ATOM   8123  C  CG  . GLN B  1 509 ? 8.820   17.429  21.927  1.00 76.80  ? 509  GLN B CG  1 
ATOM   8124  C  CD  . GLN B  1 509 ? 10.002  17.380  20.958  1.00 79.69  ? 509  GLN B CD  1 
ATOM   8125  O  OE1 . GLN B  1 509 ? 10.547  18.415  20.575  1.00 80.60  ? 509  GLN B OE1 1 
ATOM   8126  N  NE2 . GLN B  1 509 ? 10.401  16.167  20.561  1.00 79.69  ? 509  GLN B NE2 1 
ATOM   8127  N  N   . TYR B  1 510 ? 10.012  17.753  26.494  1.00 63.29  ? 510  TYR B N   1 
ATOM   8128  C  CA  . TYR B  1 510 ? 10.644  18.508  27.572  1.00 62.04  ? 510  TYR B CA  1 
ATOM   8129  C  C   . TYR B  1 510 ? 12.157  18.439  27.388  1.00 64.54  ? 510  TYR B C   1 
ATOM   8130  O  O   . TYR B  1 510 ? 12.650  17.569  26.682  1.00 65.97  ? 510  TYR B O   1 
ATOM   8131  C  CB  . TYR B  1 510 ? 10.224  17.977  28.948  1.00 57.74  ? 510  TYR B CB  1 
ATOM   8132  C  CG  . TYR B  1 510 ? 10.697  16.578  29.293  1.00 55.95  ? 510  TYR B CG  1 
ATOM   8133  C  CD1 . TYR B  1 510 ? 10.177  15.473  28.644  1.00 54.81  ? 510  TYR B CD1 1 
ATOM   8134  C  CD2 . TYR B  1 510 ? 11.639  16.363  30.296  1.00 56.30  ? 510  TYR B CD2 1 
ATOM   8135  C  CE1 . TYR B  1 510 ? 10.592  14.193  28.968  1.00 54.81  ? 510  TYR B CE1 1 
ATOM   8136  C  CE2 . TYR B  1 510 ? 12.060  15.088  30.629  1.00 49.72  ? 510  TYR B CE2 1 
ATOM   8137  C  CZ  . TYR B  1 510 ? 11.533  14.006  29.959  1.00 54.82  ? 510  TYR B CZ  1 
ATOM   8138  O  OH  . TYR B  1 510 ? 11.934  12.724  30.265  1.00 54.05  ? 510  TYR B OH  1 
ATOM   8139  N  N   . VAL B  1 511 ? 12.898  19.349  28.009  1.00 74.30  ? 511  VAL B N   1 
ATOM   8140  C  CA  . VAL B  1 511 ? 14.344  19.398  27.788  1.00 77.11  ? 511  VAL B CA  1 
ATOM   8141  C  C   . VAL B  1 511 ? 15.146  18.996  29.017  1.00 76.22  ? 511  VAL B C   1 
ATOM   8142  O  O   . VAL B  1 511 ? 14.676  19.118  30.144  1.00 76.09  ? 511  VAL B O   1 
ATOM   8143  C  CB  . VAL B  1 511 ? 14.811  20.785  27.271  1.00 67.85  ? 511  VAL B CB  1 
ATOM   8144  C  CG1 . VAL B  1 511 ? 13.648  21.528  26.659  1.00 68.03  ? 511  VAL B CG1 1 
ATOM   8145  C  CG2 . VAL B  1 511 ? 15.447  21.610  28.379  1.00 66.56  ? 511  VAL B CG2 1 
ATOM   8146  N  N   . SER B  1 512 ? 16.349  18.488  28.782  1.00 64.57  ? 512  SER B N   1 
ATOM   8147  C  CA  . SER B  1 512 ? 17.253  18.120  29.858  1.00 64.24  ? 512  SER B CA  1 
ATOM   8148  C  C   . SER B  1 512 ? 18.224  19.267  30.104  1.00 67.94  ? 512  SER B C   1 
ATOM   8149  O  O   . SER B  1 512 ? 18.861  19.735  29.163  1.00 71.22  ? 512  SER B O   1 
ATOM   8150  C  CB  . SER B  1 512 ? 18.018  16.853  29.473  1.00 69.67  ? 512  SER B CB  1 
ATOM   8151  O  OG  . SER B  1 512 ? 19.213  16.710  30.222  1.00 71.56  ? 512  SER B OG  1 
ATOM   8152  N  N   . LEU B  1 513 ? 18.335  19.730  31.353  1.00 69.84  ? 513  LEU B N   1 
ATOM   8153  C  CA  . LEU B  1 513 ? 19.315  20.772  31.689  1.00 70.32  ? 513  LEU B CA  1 
ATOM   8154  C  C   . LEU B  1 513 ? 20.548  20.177  32.388  1.00 70.56  ? 513  LEU B C   1 
ATOM   8155  O  O   . LEU B  1 513 ? 20.547  19.880  33.581  1.00 66.49  ? 513  LEU B O   1 
ATOM   8156  C  CB  . LEU B  1 513 ? 18.675  21.876  32.548  1.00 63.67  ? 513  LEU B CB  1 
ATOM   8157  C  CG  . LEU B  1 513 ? 17.454  22.622  31.985  1.00 56.79  ? 513  LEU B CG  1 
ATOM   8158  C  CD1 . LEU B  1 513 ? 16.958  23.699  32.933  1.00 55.83  ? 513  LEU B CD1 1 
ATOM   8159  C  CD2 . LEU B  1 513 ? 17.754  23.241  30.642  1.00 58.77  ? 513  LEU B CD2 1 
ATOM   8160  N  N   . ASN B  1 514 ? 21.631  20.082  31.635  1.00 89.09  ? 514  ASN B N   1 
ATOM   8161  C  CA  . ASN B  1 514 ? 22.777  19.307  32.054  1.00 95.15  ? 514  ASN B CA  1 
ATOM   8162  C  C   . ASN B  1 514 ? 24.020  20.125  31.765  1.00 101.22 ? 514  ASN B C   1 
ATOM   8163  O  O   . ASN B  1 514 ? 23.919  21.209  31.189  1.00 103.81 ? 514  ASN B O   1 
ATOM   8164  C  CB  . ASN B  1 514 ? 22.803  18.015  31.242  1.00 92.38  ? 514  ASN B CB  1 
ATOM   8165  C  CG  . ASN B  1 514 ? 23.349  16.850  32.020  1.00 94.15  ? 514  ASN B CG  1 
ATOM   8166  O  OD1 . ASN B  1 514 ? 24.360  16.970  32.718  1.00 94.71  ? 514  ASN B OD1 1 
ATOM   8167  N  ND2 . ASN B  1 514 ? 22.675  15.707  31.917  1.00 93.81  ? 514  ASN B ND2 1 
ATOM   8168  N  N   . LEU B  1 515 ? 25.194  19.625  32.141  1.00 100.89 ? 515  LEU B N   1 
ATOM   8169  C  CA  . LEU B  1 515 ? 26.415  20.307  31.732  1.00 102.26 ? 515  LEU B CA  1 
ATOM   8170  C  C   . LEU B  1 515 ? 26.578  20.032  30.245  1.00 104.81 ? 515  LEU B C   1 
ATOM   8171  O  O   . LEU B  1 515 ? 26.789  20.954  29.455  1.00 106.41 ? 515  LEU B O   1 
ATOM   8172  C  CB  . LEU B  1 515 ? 27.653  19.838  32.508  1.00 90.43  ? 515  LEU B CB  1 
ATOM   8173  C  CG  . LEU B  1 515 ? 27.544  19.174  33.880  1.00 86.74  ? 515  LEU B CG  1 
ATOM   8174  C  CD1 . LEU B  1 515 ? 27.288  17.668  33.726  1.00 87.04  ? 515  LEU B CD1 1 
ATOM   8175  C  CD2 . LEU B  1 515 ? 28.802  19.441  34.696  1.00 84.07  ? 515  LEU B CD2 1 
ATOM   8176  N  N   . LYS B  1 516 ? 26.457  18.758  29.870  1.00 107.27 ? 516  LYS B N   1 
ATOM   8177  C  CA  . LYS B  1 516 ? 26.429  18.376  28.464  1.00 106.61 ? 516  LYS B CA  1 
ATOM   8178  C  C   . LYS B  1 516 ? 25.216  19.075  27.846  1.00 105.94 ? 516  LYS B C   1 
ATOM   8179  O  O   . LYS B  1 516 ? 24.222  19.309  28.533  1.00 105.89 ? 516  LYS B O   1 
ATOM   8180  C  CB  . LYS B  1 516 ? 26.393  16.847  28.303  1.00 92.99  ? 516  LYS B CB  1 
ATOM   8181  C  CG  . LYS B  1 516 ? 25.102  16.167  28.723  1.00 93.59  ? 516  LYS B CG  1 
ATOM   8182  C  CD  . LYS B  1 516 ? 25.262  14.637  28.768  1.00 95.66  ? 516  LYS B CD  1 
ATOM   8183  C  CE  . LYS B  1 516 ? 23.936  13.879  28.517  1.00 94.55  ? 516  LYS B CE  1 
ATOM   8184  N  NZ  . LYS B  1 516 ? 22.808  14.210  29.461  1.00 91.19  ? 516  LYS B NZ  1 
ATOM   8185  N  N   . PRO B  1 517 ? 25.301  19.432  26.556  1.00 98.14  ? 517  PRO B N   1 
ATOM   8186  C  CA  . PRO B  1 517 ? 24.360  20.377  25.942  1.00 95.83  ? 517  PRO B CA  1 
ATOM   8187  C  C   . PRO B  1 517 ? 22.922  19.883  25.861  1.00 94.27  ? 517  PRO B C   1 
ATOM   8188  O  O   . PRO B  1 517 ? 22.628  18.701  26.071  1.00 92.48  ? 517  PRO B O   1 
ATOM   8189  C  CB  . PRO B  1 517 ? 24.925  20.566  24.541  1.00 90.65  ? 517  PRO B CB  1 
ATOM   8190  C  CG  . PRO B  1 517 ? 25.596  19.278  24.252  1.00 92.67  ? 517  PRO B CG  1 
ATOM   8191  C  CD  . PRO B  1 517 ? 26.213  18.854  25.554  1.00 93.58  ? 517  PRO B CD  1 
ATOM   8192  N  N   . LEU B  1 518 ? 22.042  20.823  25.535  1.00 89.26  ? 518  LEU B N   1 
ATOM   8193  C  CA  . LEU B  1 518 ? 20.597  20.643  25.562  1.00 86.82  ? 518  LEU B CA  1 
ATOM   8194  C  C   . LEU B  1 518 ? 20.167  19.355  24.863  1.00 87.85  ? 518  LEU B C   1 
ATOM   8195  O  O   . LEU B  1 518 ? 20.583  19.074  23.739  1.00 86.88  ? 518  LEU B O   1 
ATOM   8196  C  CB  . LEU B  1 518 ? 19.965  21.844  24.844  1.00 87.67  ? 518  LEU B CB  1 
ATOM   8197  C  CG  . LEU B  1 518 ? 18.637  22.510  25.223  1.00 84.02  ? 518  LEU B CG  1 
ATOM   8198  C  CD1 . LEU B  1 518 ? 17.453  21.624  24.868  1.00 83.26  ? 518  LEU B CD1 1 
ATOM   8199  C  CD2 . LEU B  1 518 ? 18.619  22.916  26.691  1.00 80.76  ? 518  LEU B CD2 1 
ATOM   8200  N  N   . GLU B  1 519 ? 19.347  18.570  25.561  1.00 108.33 ? 519  GLU B N   1 
ATOM   8201  C  CA  . GLU B  1 519 ? 18.723  17.364  25.012  1.00 110.57 ? 519  GLU B CA  1 
ATOM   8202  C  C   . GLU B  1 519 ? 17.208  17.475  25.093  1.00 105.74 ? 519  GLU B C   1 
ATOM   8203  O  O   . GLU B  1 519 ? 16.676  18.064  26.031  1.00 105.66 ? 519  GLU B O   1 
ATOM   8204  C  CB  . GLU B  1 519 ? 19.145  16.122  25.795  1.00 107.28 ? 519  GLU B CB  1 
ATOM   8205  C  CG  . GLU B  1 519 ? 20.444  15.494  25.360  1.00 110.94 ? 519  GLU B CG  1 
ATOM   8206  C  CD  . GLU B  1 519 ? 20.559  14.062  25.842  1.00 112.26 ? 519  GLU B CD  1 
ATOM   8207  O  OE1 . GLU B  1 519 ? 19.536  13.508  26.308  1.00 109.40 ? 519  GLU B OE1 1 
ATOM   8208  O  OE2 . GLU B  1 519 ? 21.669  13.494  25.755  1.00 115.76 ? 519  GLU B OE2 1 
ATOM   8209  N  N   . VAL B  1 520 ? 16.511  16.898  24.122  1.00 83.50  ? 520  VAL B N   1 
ATOM   8210  C  CA  . VAL B  1 520 ? 15.057  16.876  24.169  1.00 81.28  ? 520  VAL B CA  1 
ATOM   8211  C  C   . VAL B  1 520 ? 14.558  15.457  24.389  1.00 81.67  ? 520  VAL B C   1 
ATOM   8212  O  O   . VAL B  1 520 ? 14.824  14.575  23.575  1.00 84.71  ? 520  VAL B O   1 
ATOM   8213  C  CB  . VAL B  1 520 ? 14.418  17.454  22.886  1.00 61.48  ? 520  VAL B CB  1 
ATOM   8214  C  CG1 . VAL B  1 520 ? 12.920  17.191  22.871  1.00 59.86  ? 520  VAL B CG1 1 
ATOM   8215  C  CG2 . VAL B  1 520 ? 14.695  18.942  22.780  1.00 62.51  ? 520  VAL B CG2 1 
ATOM   8216  N  N   . ARG B  1 521 ? 13.862  15.232  25.502  1.00 74.10  ? 521  ARG B N   1 
ATOM   8217  C  CA  . ARG B  1 521 ? 13.139  13.979  25.696  1.00 71.11  ? 521  ARG B CA  1 
ATOM   8218  C  C   . ARG B  1 521 ? 11.630  14.212  25.486  1.00 67.77  ? 521  ARG B C   1 
ATOM   8219  O  O   . ARG B  1 521 ? 11.182  15.354  25.309  1.00 63.69  ? 521  ARG B O   1 
ATOM   8220  C  CB  . ARG B  1 521 ? 13.429  13.390  27.085  1.00 79.86  ? 521  ARG B CB  1 
ATOM   8221  C  CG  . ARG B  1 521 ? 14.792  13.778  27.680  1.00 82.83  ? 521  ARG B CG  1 
ATOM   8222  C  CD  . ARG B  1 521 ? 15.162  12.905  28.891  1.00 84.28  ? 521  ARG B CD  1 
ATOM   8223  N  NE  . ARG B  1 521 ? 16.269  13.449  29.689  1.00 86.93  ? 521  ARG B NE  1 
ATOM   8224  C  CZ  . ARG B  1 521 ? 17.564  13.220  29.461  1.00 89.41  ? 521  ARG B CZ  1 
ATOM   8225  N  NH1 . ARG B  1 521 ? 17.947  12.458  28.443  1.00 91.13  ? 521  ARG B NH1 1 
ATOM   8226  N  NH2 . ARG B  1 521 ? 18.486  13.758  30.252  1.00 89.03  ? 521  ARG B NH2 1 
ATOM   8227  N  N   . ARG B  1 522 ? 10.852  13.133  25.515  1.00 80.82  ? 522  ARG B N   1 
ATOM   8228  C  CA  . ARG B  1 522 ? 9.402   13.230  25.396  1.00 82.29  ? 522  ARG B CA  1 
ATOM   8229  C  C   . ARG B  1 522 ? 8.809   12.407  26.514  1.00 80.01  ? 522  ARG B C   1 
ATOM   8230  O  O   . ARG B  1 522 ? 9.476   11.502  27.024  1.00 80.97  ? 522  ARG B O   1 
ATOM   8231  C  CB  . ARG B  1 522 ? 8.908   12.684  24.057  1.00 87.85  ? 522  ARG B CB  1 
ATOM   8232  C  CG  . ARG B  1 522 ? 9.219   13.555  22.857  1.00 95.14  ? 522  ARG B CG  1 
ATOM   8233  C  CD  . ARG B  1 522 ? 8.422   13.133  21.619  1.00 101.02 ? 522  ARG B CD  1 
ATOM   8234  N  NE  . ARG B  1 522 ? 8.613   11.724  21.272  1.00 106.33 ? 522  ARG B NE  1 
ATOM   8235  C  CZ  . ARG B  1 522 ? 7.621   10.856  21.078  1.00 108.17 ? 522  ARG B CZ  1 
ATOM   8236  N  NH1 . ARG B  1 522 ? 6.358   11.257  21.194  1.00 108.57 ? 522  ARG B NH1 1 
ATOM   8237  N  NH2 . ARG B  1 522 ? 7.891   9.590   20.768  1.00 107.30 ? 522  ARG B NH2 1 
ATOM   8238  N  N   . GLY B  1 523 ? 7.570   12.711  26.902  1.00 73.65  ? 523  GLY B N   1 
ATOM   8239  C  CA  . GLY B  1 523 ? 6.898   11.900  27.900  1.00 69.76  ? 523  GLY B CA  1 
ATOM   8240  C  C   . GLY B  1 523 ? 7.490   11.941  29.300  1.00 68.04  ? 523  GLY B C   1 
ATOM   8241  O  O   . GLY B  1 523 ? 8.006   10.925  29.779  1.00 68.81  ? 523  GLY B O   1 
ATOM   8242  N  N   . LEU B  1 524 ? 7.494   13.117  29.924  1.00 63.48  ? 524  LEU B N   1 
ATOM   8243  C  CA  . LEU B  1 524 ? 7.884   13.244  31.328  1.00 60.93  ? 524  LEU B CA  1 
ATOM   8244  C  C   . LEU B  1 524 ? 6.988   12.315  32.126  1.00 61.71  ? 524  LEU B C   1 
ATOM   8245  O  O   . LEU B  1 524 ? 5.786   12.584  32.254  1.00 61.61  ? 524  LEU B O   1 
ATOM   8246  C  CB  . LEU B  1 524 ? 7.532   14.665  31.763  1.00 44.42  ? 524  LEU B CB  1 
ATOM   8247  C  CG  . LEU B  1 524 ? 8.359   15.552  32.684  1.00 44.40  ? 524  LEU B CG  1 
ATOM   8248  C  CD1 . LEU B  1 524 ? 7.626   16.861  32.822  1.00 44.08  ? 524  LEU B CD1 1 
ATOM   8249  C  CD2 . LEU B  1 524 ? 8.560   14.913  34.027  1.00 43.16  ? 524  LEU B CD2 1 
ATOM   8250  N  N   . ARG B  1 525 ? 7.559   11.290  32.756  1.00 66.32  ? 525  ARG B N   1 
ATOM   8251  C  CA  . ARG B  1 525 ? 6.694   10.251  33.336  1.00 65.11  ? 525  ARG B CA  1 
ATOM   8252  C  C   . ARG B  1 525 ? 5.714   9.591   32.330  1.00 62.80  ? 525  ARG B C   1 
ATOM   8253  O  O   . ARG B  1 525 ? 6.108   8.641   31.642  1.00 64.27  ? 525  ARG B O   1 
ATOM   8254  C  CB  . ARG B  1 525 ? 6.093   10.648  34.673  1.00 59.66  ? 525  ARG B CB  1 
ATOM   8255  C  CG  . ARG B  1 525 ? 7.173   10.937  35.724  1.00 62.26  ? 525  ARG B CG  1 
ATOM   8256  C  CD  . ARG B  1 525 ? 8.555   10.293  35.423  1.00 76.53  ? 525  ARG B CD  1 
ATOM   8257  N  NE  . ARG B  1 525 ? 8.681   8.930   35.938  1.00 76.82  ? 525  ARG B NE  1 
ATOM   8258  C  CZ  . ARG B  1 525 ? 9.457   8.579   36.962  1.00 74.20  ? 525  ARG B CZ  1 
ATOM   8259  N  NH1 . ARG B  1 525 ? 10.196  9.496   37.583  1.00 72.78  ? 525  ARG B NH1 1 
ATOM   8260  N  NH2 . ARG B  1 525 ? 9.496   7.308   37.360  1.00 71.77  ? 525  ARG B NH2 1 
ATOM   8261  N  N   . ALA B  1 526 ? 4.455   10.051  32.281  1.00 53.12  ? 526  ALA B N   1 
ATOM   8262  C  CA  . ALA B  1 526 ? 3.370   9.379   31.530  1.00 51.48  ? 526  ALA B CA  1 
ATOM   8263  C  C   . ALA B  1 526 ? 2.931   8.078   32.190  1.00 57.76  ? 526  ALA B C   1 
ATOM   8264  O  O   . ALA B  1 526 ? 2.111   8.118   33.109  1.00 58.91  ? 526  ALA B O   1 
ATOM   8265  C  CB  . ALA B  1 526 ? 3.728   9.179   30.066  1.00 41.06  ? 526  ALA B CB  1 
ATOM   8266  N  N   . GLN B  1 527 ? 3.328   6.924   31.677  1.00 79.12  ? 527  GLN B N   1 
ATOM   8267  C  CA  . GLN B  1 527 ? 3.246   5.767   32.553  1.00 81.44  ? 527  GLN B CA  1 
ATOM   8268  C  C   . GLN B  1 527 ? 3.924   6.217   33.840  1.00 82.64  ? 527  GLN B C   1 
ATOM   8269  O  O   . GLN B  1 527 ? 4.929   6.928   33.798  1.00 87.68  ? 527  GLN B O   1 
ATOM   8270  C  CB  . GLN B  1 527 ? 3.951   4.544   31.976  1.00 72.64  ? 527  GLN B CB  1 
ATOM   8271  C  CG  . GLN B  1 527 ? 3.128   3.766   30.980  1.00 73.56  ? 527  GLN B CG  1 
ATOM   8272  C  CD  . GLN B  1 527 ? 3.358   4.227   29.554  1.00 76.02  ? 527  GLN B CD  1 
ATOM   8273  O  OE1 . GLN B  1 527 ? 2.784   3.678   28.621  1.00 76.93  ? 527  GLN B OE1 1 
ATOM   8274  N  NE2 . GLN B  1 527 ? 4.215   5.231   29.379  1.00 76.39  ? 527  GLN B NE2 1 
ATOM   8275  N  N   . THR B  1 528 ? 3.336   5.819   34.963  1.00 65.25  ? 528  THR B N   1 
ATOM   8276  C  CA  . THR B  1 528 ? 3.638   6.296   36.322  1.00 61.96  ? 528  THR B CA  1 
ATOM   8277  C  C   . THR B  1 528 ? 2.963   7.630   36.644  1.00 58.53  ? 528  THR B C   1 
ATOM   8278  O  O   . THR B  1 528 ? 2.560   7.848   37.779  1.00 59.29  ? 528  THR B O   1 
ATOM   8279  C  CB  . THR B  1 528 ? 5.224   6.421   36.610  1.00 43.17  ? 528  THR B CB  1 
ATOM   8280  O  OG1 . THR B  1 528 ? 5.766   5.179   37.078  1.00 44.15  ? 528  THR B OG1 1 
ATOM   8281  C  CG2 . THR B  1 528 ? 5.558   7.480   37.635  1.00 35.89  ? 528  THR B CG2 1 
ATOM   8282  N  N   . CYS B  1 529 ? 2.710   8.485   35.667  1.00 51.62  ? 529  CYS B N   1 
ATOM   8283  C  CA  . CYS B  1 529 ? 1.969   9.697   36.017  1.00 47.38  ? 529  CYS B CA  1 
ATOM   8284  C  C   . CYS B  1 529 ? 0.508   9.574   35.675  1.00 44.89  ? 529  CYS B C   1 
ATOM   8285  O  O   . CYS B  1 529 ? -0.320  10.353  36.133  1.00 42.32  ? 529  CYS B O   1 
ATOM   8286  C  CB  . CYS B  1 529 ? 2.586   10.959  35.409  1.00 46.11  ? 529  CYS B CB  1 
ATOM   8287  S  SG  . CYS B  1 529 ? 3.537   11.910  36.622  1.00 50.95  ? 529  CYS B SG  1 
ATOM   8288  N  N   . ALA B  1 530 ? 0.196   8.567   34.873  1.00 45.05  ? 530  ALA B N   1 
ATOM   8289  C  CA  . ALA B  1 530 ? -1.175  8.326   34.504  1.00 43.36  ? 530  ALA B CA  1 
ATOM   8290  C  C   . ALA B  1 530 ? -1.723  7.561   35.675  1.00 44.62  ? 530  ALA B C   1 
ATOM   8291  O  O   . ALA B  1 530 ? -2.898  7.642   35.990  1.00 44.35  ? 530  ALA B O   1 
ATOM   8292  C  CB  . ALA B  1 530 ? -1.254  7.527   33.224  1.00 37.04  ? 530  ALA B CB  1 
ATOM   8293  N  N   . PHE B  1 531 ? -0.836  6.820   36.328  1.00 64.16  ? 531  PHE B N   1 
ATOM   8294  C  CA  . PHE B  1 531 ? -1.174  6.123   37.551  1.00 62.82  ? 531  PHE B CA  1 
ATOM   8295  C  C   . PHE B  1 531 ? -1.678  7.163   38.517  1.00 62.21  ? 531  PHE B C   1 
ATOM   8296  O  O   . PHE B  1 531 ? -2.871  7.193   38.848  1.00 66.09  ? 531  PHE B O   1 
ATOM   8297  C  CB  . PHE B  1 531 ? 0.066   5.441   38.115  1.00 36.26  ? 531  PHE B CB  1 
ATOM   8298  C  CG  . PHE B  1 531 ? -0.107  4.921   39.502  1.00 29.62  ? 531  PHE B CG  1 
ATOM   8299  C  CD1 . PHE B  1 531 ? -0.902  3.829   39.750  1.00 30.82  ? 531  PHE B CD1 1 
ATOM   8300  C  CD2 . PHE B  1 531 ? 0.542   5.514   40.562  1.00 34.59  ? 531  PHE B CD2 1 
ATOM   8301  C  CE1 . PHE B  1 531 ? -1.060  3.337   41.042  1.00 29.13  ? 531  PHE B CE1 1 
ATOM   8302  C  CE2 . PHE B  1 531 ? 0.393   5.029   41.857  1.00 31.19  ? 531  PHE B CE2 1 
ATOM   8303  C  CZ  . PHE B  1 531 ? -0.408  3.940   42.095  1.00 29.00  ? 531  PHE B CZ  1 
ATOM   8304  N  N   . TRP B  1 532 ? -0.766  8.049   38.910  1.00 34.85  ? 532  TRP B N   1 
ATOM   8305  C  CA  . TRP B  1 532 ? -1.030  9.054   39.928  1.00 31.09  ? 532  TRP B CA  1 
ATOM   8306  C  C   . TRP B  1 532 ? -2.172  10.011  39.566  1.00 31.33  ? 532  TRP B C   1 
ATOM   8307  O  O   . TRP B  1 532 ? -3.044  10.272  40.395  1.00 30.42  ? 532  TRP B O   1 
ATOM   8308  C  CB  . TRP B  1 532 ? 0.244   9.848   40.253  1.00 30.08  ? 532  TRP B CB  1 
ATOM   8309  C  CG  . TRP B  1 532 ? 1.294   9.083   41.000  1.00 30.24  ? 532  TRP B CG  1 
ATOM   8310  C  CD1 . TRP B  1 532 ? 2.453   8.589   40.494  1.00 31.41  ? 532  TRP B CD1 1 
ATOM   8311  C  CD2 . TRP B  1 532 ? 1.290   8.741   42.393  1.00 29.29  ? 532  TRP B CD2 1 
ATOM   8312  N  NE1 . TRP B  1 532 ? 3.165   7.945   41.474  1.00 31.25  ? 532  TRP B NE1 1 
ATOM   8313  C  CE2 . TRP B  1 532 ? 2.471   8.026   42.650  1.00 29.96  ? 532  TRP B CE2 1 
ATOM   8314  C  CE3 . TRP B  1 532 ? 0.401   8.966   43.444  1.00 30.65  ? 532  TRP B CE3 1 
ATOM   8315  C  CZ2 . TRP B  1 532 ? 2.782   7.535   43.910  1.00 29.40  ? 532  TRP B CZ2 1 
ATOM   8316  C  CZ3 . TRP B  1 532 ? 0.716   8.474   44.693  1.00 27.46  ? 532  TRP B CZ3 1 
ATOM   8317  C  CH2 . TRP B  1 532 ? 1.891   7.768   44.914  1.00 28.15  ? 532  TRP B CH2 1 
ATOM   8318  N  N   . ASN B  1 533 ? -2.162  10.546  38.349  1.00 29.83  ? 533  ASN B N   1 
ATOM   8319  C  CA  . ASN B  1 533 ? -3.158  11.538  37.959  1.00 29.69  ? 533  ASN B CA  1 
ATOM   8320  C  C   . ASN B  1 533 ? -4.509  10.993  37.505  1.00 30.84  ? 533  ASN B C   1 
ATOM   8321  O  O   . ASN B  1 533 ? -5.554  11.532  37.863  1.00 30.80  ? 533  ASN B O   1 
ATOM   8322  C  CB  . ASN B  1 533 ? -2.590  12.460  36.898  1.00 36.41  ? 533  ASN B CB  1 
ATOM   8323  C  CG  . ASN B  1 533 ? -1.359  13.168  37.367  1.00 36.43  ? 533  ASN B CG  1 
ATOM   8324  O  OD1 . ASN B  1 533 ? -1.152  13.334  38.574  1.00 35.79  ? 533  ASN B OD1 1 
ATOM   8325  N  ND2 . ASN B  1 533 ? -0.524  13.600  36.423  1.00 37.69  ? 533  ASN B ND2 1 
ATOM   8326  N  N   . ARG B  1 534 ? -4.497  9.942   36.700  1.00 35.82  ? 534  ARG B N   1 
ATOM   8327  C  CA  . ARG B  1 534 ? -5.745  9.346   36.238  1.00 41.15  ? 534  ARG B CA  1 
ATOM   8328  C  C   . ARG B  1 534 ? -6.307  8.334   37.241  1.00 39.39  ? 534  ARG B C   1 
ATOM   8329  O  O   . ARG B  1 534 ? -7.420  8.496   37.740  1.00 40.06  ? 534  ARG B O   1 
ATOM   8330  C  CB  . ARG B  1 534 ? -5.585  8.698   34.856  1.00 67.00  ? 534  ARG B CB  1 
ATOM   8331  C  CG  . ARG B  1 534 ? -5.702  9.659   33.697  1.00 73.69  ? 534  ARG B CG  1 
ATOM   8332  C  CD  . ARG B  1 534 ? -5.451  8.944   32.384  1.00 80.42  ? 534  ARG B CD  1 
ATOM   8333  N  NE  . ARG B  1 534 ? -5.244  9.886   31.287  1.00 89.37  ? 534  ARG B NE  1 
ATOM   8334  C  CZ  . ARG B  1 534 ? -4.147  10.628  31.125  1.00 95.63  ? 534  ARG B CZ  1 
ATOM   8335  N  NH1 . ARG B  1 534 ? -3.145  10.549  31.993  1.00 96.32  ? 534  ARG B NH1 1 
ATOM   8336  N  NH2 . ARG B  1 534 ? -4.050  11.458  30.092  1.00 98.44  ? 534  ARG B NH2 1 
ATOM   8337  N  N   . PHE B  1 535 ? -5.536  7.285   37.515  1.00 35.80  ? 535  PHE B N   1 
ATOM   8338  C  CA  . PHE B  1 535 ? -6.069  6.096   38.165  1.00 31.82  ? 535  PHE B CA  1 
ATOM   8339  C  C   . PHE B  1 535 ? -6.205  6.161   39.687  1.00 29.90  ? 535  PHE B C   1 
ATOM   8340  O  O   . PHE B  1 535 ? -7.294  5.974   40.215  1.00 25.75  ? 535  PHE B O   1 
ATOM   8341  C  CB  . PHE B  1 535 ? -5.289  4.862   37.755  1.00 27.09  ? 535  PHE B CB  1 
ATOM   8342  C  CG  . PHE B  1 535 ? -5.802  3.621   38.374  1.00 26.21  ? 535  PHE B CG  1 
ATOM   8343  C  CD1 . PHE B  1 535 ? -6.939  3.023   37.887  1.00 25.72  ? 535  PHE B CD1 1 
ATOM   8344  C  CD2 . PHE B  1 535 ? -5.163  3.062   39.466  1.00 25.83  ? 535  PHE B CD2 1 
ATOM   8345  C  CE1 . PHE B  1 535 ? -7.428  1.882   38.469  1.00 24.93  ? 535  PHE B CE1 1 
ATOM   8346  C  CE2 . PHE B  1 535 ? -5.645  1.919   40.054  1.00 25.07  ? 535  PHE B CE2 1 
ATOM   8347  C  CZ  . PHE B  1 535 ? -6.783  1.328   39.557  1.00 24.61  ? 535  PHE B CZ  1 
ATOM   8348  N  N   . LEU B  1 536 ? -5.099  6.365   40.394  1.00 51.31  ? 536  LEU B N   1 
ATOM   8349  C  CA  . LEU B  1 536 ? -5.131  6.398   41.861  1.00 54.61  ? 536  LEU B CA  1 
ATOM   8350  C  C   . LEU B  1 536 ? -6.282  7.187   42.516  1.00 60.09  ? 536  LEU B C   1 
ATOM   8351  O  O   . LEU B  1 536 ? -6.826  6.739   43.510  1.00 64.70  ? 536  LEU B O   1 
ATOM   8352  C  CB  . LEU B  1 536 ? -3.788  6.843   42.444  1.00 37.55  ? 536  LEU B CB  1 
ATOM   8353  C  CG  . LEU B  1 536 ? -3.576  6.291   43.853  1.00 33.49  ? 536  LEU B CG  1 
ATOM   8354  C  CD1 . LEU B  1 536 ? -3.594  4.777   43.804  1.00 35.46  ? 536  LEU B CD1 1 
ATOM   8355  C  CD2 . LEU B  1 536 ? -2.278  6.763   44.423  1.00 31.35  ? 536  LEU B CD2 1 
ATOM   8356  N  N   . PRO B  1 537 ? -6.645  8.365   41.979  1.00 51.93  ? 537  PRO B N   1 
ATOM   8357  C  CA  . PRO B  1 537 ? -7.865  9.041   42.444  1.00 50.48  ? 537  PRO B CA  1 
ATOM   8358  C  C   . PRO B  1 537 ? -9.154  8.209   42.382  1.00 52.38  ? 537  PRO B C   1 
ATOM   8359  O  O   . PRO B  1 537 ? -9.925  8.253   43.343  1.00 54.06  ? 537  PRO B O   1 
ATOM   8360  C  CB  . PRO B  1 537 ? -7.989  10.235  41.487  1.00 34.25  ? 537  PRO B CB  1 
ATOM   8361  C  CG  . PRO B  1 537 ? -6.950  10.016  40.421  1.00 34.89  ? 537  PRO B CG  1 
ATOM   8362  C  CD  . PRO B  1 537 ? -5.876  9.243   41.088  1.00 36.03  ? 537  PRO B CD  1 
ATOM   8363  N  N   . LYS B  1 538 ? -9.393  7.499   41.276  1.00 43.62  ? 538  LYS B N   1 
ATOM   8364  C  CA  . LYS B  1 538 ? -10.545 6.598   41.153  1.00 41.46  ? 538  LYS B CA  1 
ATOM   8365  C  C   . LYS B  1 538 ? -10.487 5.575   42.275  1.00 40.28  ? 538  LYS B C   1 
ATOM   8366  O  O   . LYS B  1 538 ? -11.507 5.158   42.816  1.00 39.35  ? 538  LYS B O   1 
ATOM   8367  C  CB  . LYS B  1 538 ? -10.540 5.860   39.803  1.00 44.35  ? 538  LYS B CB  1 
ATOM   8368  C  CG  . LYS B  1 538 ? -11.449 6.431   38.726  1.00 46.57  ? 538  LYS B CG  1 
ATOM   8369  C  CD  . LYS B  1 538 ? -10.822 7.653   38.055  1.00 50.82  ? 538  LYS B CD  1 
ATOM   8370  C  CE  . LYS B  1 538 ? -11.742 8.285   36.998  1.00 53.59  ? 538  LYS B CE  1 
ATOM   8371  N  NZ  . LYS B  1 538 ? -11.806 7.511   35.713  1.00 55.04  ? 538  LYS B NZ  1 
ATOM   8372  N  N   . LEU B  1 539 ? -9.266  5.181   42.609  1.00 52.97  ? 539  LEU B N   1 
ATOM   8373  C  CA  . LEU B  1 539 ? -9.009  4.162   43.612  1.00 56.15  ? 539  LEU B CA  1 
ATOM   8374  C  C   . LEU B  1 539 ? -9.034  4.712   45.046  1.00 64.44  ? 539  LEU B C   1 
ATOM   8375  O  O   . LEU B  1 539 ? -9.166  3.953   46.003  1.00 65.44  ? 539  LEU B O   1 
ATOM   8376  C  CB  . LEU B  1 539 ? -7.664  3.497   43.312  1.00 40.83  ? 539  LEU B CB  1 
ATOM   8377  C  CG  . LEU B  1 539 ? -7.320  2.259   44.126  1.00 37.20  ? 539  LEU B CG  1 
ATOM   8378  C  CD1 . LEU B  1 539 ? -8.430  1.258   43.966  1.00 37.27  ? 539  LEU B CD1 1 
ATOM   8379  C  CD2 . LEU B  1 539 ? -6.004  1.680   43.660  1.00 37.43  ? 539  LEU B CD2 1 
ATOM   8380  N  N   . LEU B  1 540 ? -8.883  6.026   45.196  1.00 74.12  ? 540  LEU B N   1 
ATOM   8381  C  CA  . LEU B  1 540 ? -8.947  6.648   46.517  1.00 76.24  ? 540  LEU B CA  1 
ATOM   8382  C  C   . LEU B  1 540 ? -10.402 6.821   46.934  1.00 88.01  ? 540  LEU B C   1 
ATOM   8383  O  O   . LEU B  1 540 ? -10.722 6.829   48.128  1.00 90.95  ? 540  LEU B O   1 
ATOM   8384  C  CB  . LEU B  1 540 ? -8.194  7.983   46.545  1.00 47.93  ? 540  LEU B CB  1 
ATOM   8385  C  CG  . LEU B  1 540 ? -6.785  7.982   47.171  1.00 39.56  ? 540  LEU B CG  1 
ATOM   8386  C  CD1 . LEU B  1 540 ? -6.593  6.720   48.014  1.00 38.96  ? 540  LEU B CD1 1 
ATOM   8387  C  CD2 . LEU B  1 540 ? -5.641  8.174   46.149  1.00 33.42  ? 540  LEU B CD2 1 
ATOM   8388  N  N   . SER B  1 541 ? -11.270 6.988   45.935  1.00 83.59  ? 541  SER B N   1 
ATOM   8389  C  CA  . SER B  1 541 ? -12.706 6.765   46.090  1.00 85.53  ? 541  SER B CA  1 
ATOM   8390  C  C   . SER B  1 541 ? -12.948 5.259   45.979  1.00 91.12  ? 541  SER B C   1 
ATOM   8391  O  O   . SER B  1 541 ? -12.132 4.549   45.392  1.00 90.45  ? 541  SER B O   1 
ATOM   8392  C  CB  . SER B  1 541 ? -13.488 7.514   45.012  1.00 74.15  ? 541  SER B CB  1 
ATOM   8393  O  OG  . SER B  1 541 ? -13.065 8.865   44.926  1.00 73.18  ? 541  SER B OG  1 
ATOM   8394  N  N   . ALA B  1 542 ? -14.046 4.778   46.559  1.00 96.78  ? 542  ALA B N   1 
ATOM   8395  C  CA  . ALA B  1 542 ? -14.376 3.345   46.599  1.00 103.55 ? 542  ALA B CA  1 
ATOM   8396  C  C   . ALA B  1 542 ? -13.510 2.528   47.567  1.00 109.31 ? 542  ALA B C   1 
ATOM   8397  O  O   . ALA B  1 542 ? -13.754 1.335   47.760  1.00 109.34 ? 542  ALA B O   1 
ATOM   8398  C  CB  . ALA B  1 542 ? -14.390 2.700   45.174  1.00 17.27  ? 542  ALA B CB  1 
ATOM   8399  N  N   . THR B  1 543 ? -12.505 3.164   48.169  1.00 125.44 ? 543  THR B N   1 
ATOM   8400  C  CA  . THR B  1 543 ? -11.642 2.493   49.153  1.00 129.97 ? 543  THR B CA  1 
ATOM   8401  C  C   . THR B  1 543 ? -11.437 3.313   50.433  1.00 132.32 ? 543  THR B C   1 
ATOM   8402  O  O   . THR B  1 543 ? -11.402 4.547   50.410  1.00 132.86 ? 543  THR B O   1 
ATOM   8403  C  CB  . THR B  1 543 ? -10.247 2.116   48.570  1.00 86.02  ? 543  THR B CB  1 
ATOM   8404  O  OG1 . THR B  1 543 ? -9.469  3.300   48.342  1.00 87.63  ? 543  THR B OG1 1 
ATOM   8405  C  CG2 . THR B  1 543 ? -10.390 1.336   47.273  1.00 84.74  ? 543  THR B CG2 1 
ATOM   8406  O  OXT . THR B  1 543 ? -11.290 2.752   51.525  1.00 121.96 ? 543  THR B OXT 1 
ATOM   8407  N  N   . GLU C  1 4   ? -24.118 18.405  123.840 1.00 49.16  ? 4    GLU C N   1 
ATOM   8408  C  CA  . GLU C  1 4   ? -24.970 17.710  124.801 1.00 48.47  ? 4    GLU C CA  1 
ATOM   8409  C  C   . GLU C  1 4   ? -25.981 16.794  124.147 1.00 47.58  ? 4    GLU C C   1 
ATOM   8410  O  O   . GLU C  1 4   ? -26.217 15.690  124.643 1.00 49.61  ? 4    GLU C O   1 
ATOM   8411  C  CB  . GLU C  1 4   ? -25.717 18.704  125.684 1.00 46.59  ? 4    GLU C CB  1 
ATOM   8412  C  CG  . GLU C  1 4   ? -24.825 19.490  126.591 1.00 49.88  ? 4    GLU C CG  1 
ATOM   8413  C  CD  . GLU C  1 4   ? -24.299 18.665  127.743 1.00 55.32  ? 4    GLU C CD  1 
ATOM   8414  O  OE1 . GLU C  1 4   ? -23.761 17.550  127.525 1.00 57.46  ? 4    GLU C OE1 1 
ATOM   8415  O  OE2 . GLU C  1 4   ? -24.432 19.143  128.886 1.00 57.90  ? 4    GLU C OE2 1 
ATOM   8416  N  N   . ASP C  1 5   ? -26.561 17.253  123.036 1.00 33.96  ? 5    ASP C N   1 
ATOM   8417  C  CA  . ASP C  1 5   ? -27.711 16.593  122.430 1.00 31.35  ? 5    ASP C CA  1 
ATOM   8418  C  C   . ASP C  1 5   ? -27.396 15.133  122.139 1.00 30.77  ? 5    ASP C C   1 
ATOM   8419  O  O   . ASP C  1 5   ? -26.532 14.821  121.327 1.00 29.71  ? 5    ASP C O   1 
ATOM   8420  C  CB  . ASP C  1 5   ? -28.108 17.325  121.146 1.00 36.36  ? 5    ASP C CB  1 
ATOM   8421  C  CG  . ASP C  1 5   ? -29.358 16.743  120.481 1.00 35.33  ? 5    ASP C CG  1 
ATOM   8422  O  OD1 . ASP C  1 5   ? -29.930 15.750  120.983 1.00 37.06  ? 5    ASP C OD1 1 
ATOM   8423  O  OD2 . ASP C  1 5   ? -29.765 17.286  119.431 1.00 32.28  ? 5    ASP C OD2 1 
ATOM   8424  N  N   . PRO C  1 6   ? -28.111 14.227  122.811 1.00 37.22  ? 6    PRO C N   1 
ATOM   8425  C  CA  . PRO C  1 6   ? -27.826 12.795  122.721 1.00 38.50  ? 6    PRO C CA  1 
ATOM   8426  C  C   . PRO C  1 6   ? -28.162 12.192  121.365 1.00 39.02  ? 6    PRO C C   1 
ATOM   8427  O  O   . PRO C  1 6   ? -27.669 11.117  121.044 1.00 40.84  ? 6    PRO C O   1 
ATOM   8428  C  CB  . PRO C  1 6   ? -28.719 12.196  123.804 1.00 40.02  ? 6    PRO C CB  1 
ATOM   8429  C  CG  . PRO C  1 6   ? -29.809 13.186  123.983 1.00 39.74  ? 6    PRO C CG  1 
ATOM   8430  C  CD  . PRO C  1 6   ? -29.179 14.514  123.781 1.00 37.91  ? 6    PRO C CD  1 
ATOM   8431  N  N   . GLN C  1 7   ? -28.985 12.859  120.573 1.00 35.12  ? 7    GLN C N   1 
ATOM   8432  C  CA  . GLN C  1 7   ? -29.314 12.306  119.275 1.00 38.00  ? 7    GLN C CA  1 
ATOM   8433  C  C   . GLN C  1 7   ? -28.197 12.537  118.247 1.00 36.13  ? 7    GLN C C   1 
ATOM   8434  O  O   . GLN C  1 7   ? -28.096 11.825  117.244 1.00 36.39  ? 7    GLN C O   1 
ATOM   8435  C  CB  . GLN C  1 7   ? -30.640 12.873  118.775 1.00 61.39  ? 7    GLN C CB  1 
ATOM   8436  C  CG  . GLN C  1 7   ? -31.362 11.962  117.793 1.00 68.42  ? 7    GLN C CG  1 
ATOM   8437  C  CD  . GLN C  1 7   ? -31.900 10.698  118.444 1.00 75.33  ? 7    GLN C CD  1 
ATOM   8438  O  OE1 . GLN C  1 7   ? -32.134 9.685   117.772 1.00 74.65  ? 7    GLN C OE1 1 
ATOM   8439  N  NE2 . GLN C  1 7   ? -32.112 10.754  119.760 1.00 80.25  ? 7    GLN C NE2 1 
ATOM   8440  N  N   . LEU C  1 8   ? -27.359 13.537  118.485 1.00 34.92  ? 8    LEU C N   1 
ATOM   8441  C  CA  . LEU C  1 8   ? -26.373 13.903  117.478 1.00 32.71  ? 8    LEU C CA  1 
ATOM   8442  C  C   . LEU C  1 8   ? -24.995 13.253  117.600 1.00 32.18  ? 8    LEU C C   1 
ATOM   8443  O  O   . LEU C  1 8   ? -24.204 13.346  116.668 1.00 33.33  ? 8    LEU C O   1 
ATOM   8444  C  CB  . LEU C  1 8   ? -26.227 15.415  117.411 1.00 39.27  ? 8    LEU C CB  1 
ATOM   8445  C  CG  . LEU C  1 8   ? -27.553 16.120  117.192 1.00 43.02  ? 8    LEU C CG  1 
ATOM   8446  C  CD1 . LEU C  1 8   ? -27.314 17.615  116.979 1.00 46.27  ? 8    LEU C CD1 1 
ATOM   8447  C  CD2 . LEU C  1 8   ? -28.279 15.481  116.016 1.00 42.37  ? 8    LEU C CD2 1 
ATOM   8448  N  N   . LEU C  1 9   ? -24.688 12.591  118.713 1.00 29.22  ? 9    LEU C N   1 
ATOM   8449  C  CA  . LEU C  1 9   ? -23.435 11.834  118.761 1.00 27.91  ? 9    LEU C CA  1 
ATOM   8450  C  C   . LEU C  1 9   ? -23.644 10.367  118.344 1.00 28.79  ? 9    LEU C C   1 
ATOM   8451  O  O   . LEU C  1 9   ? -24.558 9.680   118.845 1.00 26.89  ? 9    LEU C O   1 
ATOM   8452  C  CB  . LEU C  1 9   ? -22.741 11.943  120.117 1.00 27.58  ? 9    LEU C CB  1 
ATOM   8453  C  CG  . LEU C  1 9   ? -21.562 10.971  120.221 1.00 29.26  ? 9    LEU C CG  1 
ATOM   8454  C  CD1 . LEU C  1 9   ? -20.252 11.672  120.501 1.00 27.63  ? 9    LEU C CD1 1 
ATOM   8455  C  CD2 . LEU C  1 9   ? -21.862 9.908   121.280 1.00 31.97  ? 9    LEU C CD2 1 
ATOM   8456  N  N   . VAL C  1 10  ? -22.800 9.922   117.402 1.00 31.98  ? 10   VAL C N   1 
ATOM   8457  C  CA  . VAL C  1 10  ? -22.874 8.601   116.762 1.00 31.12  ? 10   VAL C CA  1 
ATOM   8458  C  C   . VAL C  1 10  ? -21.462 8.068   116.589 1.00 30.38  ? 10   VAL C C   1 
ATOM   8459  O  O   . VAL C  1 10  ? -20.551 8.816   116.235 1.00 29.56  ? 10   VAL C O   1 
ATOM   8460  C  CB  . VAL C  1 10  ? -23.500 8.679   115.343 1.00 23.88  ? 10   VAL C CB  1 
ATOM   8461  C  CG1 . VAL C  1 10  ? -23.579 7.315   114.718 1.00 23.59  ? 10   VAL C CG1 1 
ATOM   8462  C  CG2 . VAL C  1 10  ? -24.875 9.285   115.390 1.00 34.36  ? 10   VAL C CG2 1 
ATOM   8463  N  N   . ARG C  1 11  ? -21.263 6.781   116.833 1.00 35.31  ? 11   ARG C N   1 
ATOM   8464  C  CA  . ARG C  1 11  ? -19.947 6.208   116.595 1.00 35.88  ? 11   ARG C CA  1 
ATOM   8465  C  C   . ARG C  1 11  ? -19.950 5.336   115.352 1.00 31.63  ? 11   ARG C C   1 
ATOM   8466  O  O   . ARG C  1 11  ? -20.847 4.518   115.183 1.00 33.26  ? 11   ARG C O   1 
ATOM   8467  C  CB  . ARG C  1 11  ? -19.473 5.391   117.798 1.00 38.59  ? 11   ARG C CB  1 
ATOM   8468  C  CG  . ARG C  1 11  ? -18.527 4.276   117.410 1.00 40.40  ? 11   ARG C CG  1 
ATOM   8469  C  CD  . ARG C  1 11  ? -17.944 3.562   118.594 1.00 41.63  ? 11   ARG C CD  1 
ATOM   8470  N  NE  . ARG C  1 11  ? -16.572 3.977   118.838 1.00 38.75  ? 11   ARG C NE  1 
ATOM   8471  C  CZ  . ARG C  1 11  ? -16.223 4.748   119.856 1.00 37.03  ? 11   ARG C CZ  1 
ATOM   8472  N  NH1 . ARG C  1 11  ? -17.159 5.167   120.699 1.00 37.48  ? 11   ARG C NH1 1 
ATOM   8473  N  NH2 . ARG C  1 11  ? -14.951 5.090   120.030 1.00 35.43  ? 11   ARG C NH2 1 
ATOM   8474  N  N   . VAL C  1 12  ? -18.948 5.528   114.494 1.00 23.17  ? 12   VAL C N   1 
ATOM   8475  C  CA  . VAL C  1 12  ? -18.670 4.650   113.355 1.00 22.50  ? 12   VAL C CA  1 
ATOM   8476  C  C   . VAL C  1 12  ? -17.308 3.925   113.514 1.00 37.24  ? 12   VAL C C   1 
ATOM   8477  O  O   . VAL C  1 12  ? -16.675 3.993   114.572 1.00 41.15  ? 12   VAL C O   1 
ATOM   8478  C  CB  . VAL C  1 12  ? -18.679 5.432   112.046 1.00 22.59  ? 12   VAL C CB  1 
ATOM   8479  C  CG1 . VAL C  1 12  ? -20.012 6.124   111.854 1.00 21.21  ? 12   VAL C CG1 1 
ATOM   8480  C  CG2 . VAL C  1 12  ? -17.538 6.438   112.032 1.00 21.17  ? 12   VAL C CG2 1 
ATOM   8481  N  N   . ARG C  1 13  ? -16.872 3.209   112.480 1.00 32.73  ? 13   ARG C N   1 
ATOM   8482  C  CA  . ARG C  1 13  ? -15.616 2.451   112.553 1.00 32.14  ? 13   ARG C CA  1 
ATOM   8483  C  C   . ARG C  1 13  ? -14.387 3.331   112.758 1.00 34.92  ? 13   ARG C C   1 
ATOM   8484  O  O   . ARG C  1 13  ? -13.453 2.959   113.471 1.00 35.65  ? 13   ARG C O   1 
ATOM   8485  C  CB  . ARG C  1 13  ? -15.416 1.595   111.304 1.00 30.49  ? 13   ARG C CB  1 
ATOM   8486  C  CG  . ARG C  1 13  ? -14.057 0.913   111.214 1.00 30.08  ? 13   ARG C CG  1 
ATOM   8487  C  CD  . ARG C  1 13  ? -13.969 -0.337  112.069 1.00 23.40  ? 13   ARG C CD  1 
ATOM   8488  N  NE  . ARG C  1 13  ? -12.908 -0.234  113.077 1.00 31.12  ? 13   ARG C NE  1 
ATOM   8489  C  CZ  . ARG C  1 13  ? -11.646 -0.637  112.920 1.00 27.95  ? 13   ARG C CZ  1 
ATOM   8490  N  NH1 . ARG C  1 13  ? -11.258 -1.179  111.772 1.00 27.47  ? 13   ARG C NH1 1 
ATOM   8491  N  NH2 . ARG C  1 13  ? -10.765 -0.495  113.914 1.00 26.18  ? 13   ARG C NH2 1 
ATOM   8492  N  N   . GLY C  1 14  ? -14.384 4.499   112.130 1.00 36.83  ? 14   GLY C N   1 
ATOM   8493  C  CA  . GLY C  1 14  ? -13.252 5.405   112.245 1.00 35.88  ? 14   GLY C CA  1 
ATOM   8494  C  C   . GLY C  1 14  ? -13.182 6.154   113.563 1.00 34.70  ? 14   GLY C C   1 
ATOM   8495  O  O   . GLY C  1 14  ? -12.141 6.679   113.940 1.00 23.06  ? 14   GLY C O   1 
ATOM   8496  N  N   . GLY C  1 15  ? -14.299 6.210   114.271 1.00 37.95  ? 15   GLY C N   1 
ATOM   8497  C  CA  . GLY C  1 15  ? -14.322 6.913   115.533 1.00 38.82  ? 15   GLY C CA  1 
ATOM   8498  C  C   . GLY C  1 15  ? -15.665 7.542   115.830 1.00 37.55  ? 15   GLY C C   1 
ATOM   8499  O  O   . GLY C  1 15  ? -16.679 7.187   115.228 1.00 36.61  ? 15   GLY C O   1 
ATOM   8500  N  N   . GLN C  1 16  ? -15.662 8.475   116.777 1.00 37.64  ? 16   GLN C N   1 
ATOM   8501  C  CA  . GLN C  1 16  ? -16.871 9.169   117.175 1.00 37.02  ? 16   GLN C CA  1 
ATOM   8502  C  C   . GLN C  1 16  ? -17.110 10.419  116.324 1.00 37.72  ? 16   GLN C C   1 
ATOM   8503  O  O   . GLN C  1 16  ? -16.167 11.114  115.940 1.00 39.90  ? 16   GLN C O   1 
ATOM   8504  C  CB  . GLN C  1 16  ? -16.775 9.550   118.649 1.00 36.89  ? 16   GLN C CB  1 
ATOM   8505  C  CG  . GLN C  1 16  ? -16.947 8.387   119.599 1.00 39.40  ? 16   GLN C CG  1 
ATOM   8506  C  CD  . GLN C  1 16  ? -17.732 8.759   120.847 1.00 41.34  ? 16   GLN C CD  1 
ATOM   8507  O  OE1 . GLN C  1 16  ? -18.856 8.289   121.044 1.00 40.24  ? 16   GLN C OE1 1 
ATOM   8508  N  NE2 . GLN C  1 16  ? -17.142 9.599   121.701 1.00 42.32  ? 16   GLN C NE2 1 
ATOM   8509  N  N   . LEU C  1 17  ? -18.370 10.707  116.017 1.00 28.08  ? 17   LEU C N   1 
ATOM   8510  C  CA  . LEU C  1 17  ? -18.694 11.991  115.407 1.00 26.48  ? 17   LEU C CA  1 
ATOM   8511  C  C   . LEU C  1 17  ? -20.020 12.591  115.910 1.00 28.72  ? 17   LEU C C   1 
ATOM   8512  O  O   . LEU C  1 17  ? -20.879 11.885  116.456 1.00 30.10  ? 17   LEU C O   1 
ATOM   8513  C  CB  . LEU C  1 17  ? -18.627 11.903  113.884 1.00 22.08  ? 17   LEU C CB  1 
ATOM   8514  C  CG  . LEU C  1 17  ? -19.362 10.768  113.182 1.00 21.61  ? 17   LEU C CG  1 
ATOM   8515  C  CD1 . LEU C  1 17  ? -20.837 11.092  113.049 1.00 29.80  ? 17   LEU C CD1 1 
ATOM   8516  C  CD2 . LEU C  1 17  ? -18.748 10.521  111.826 1.00 20.64  ? 17   LEU C CD2 1 
ATOM   8517  N  N   . ARG C  1 18  ? -20.157 13.906  115.757 1.00 23.69  ? 18   ARG C N   1 
ATOM   8518  C  CA  . ARG C  1 18  ? -21.309 14.628  116.282 1.00 24.28  ? 18   ARG C CA  1 
ATOM   8519  C  C   . ARG C  1 18  ? -21.845 15.549  115.222 1.00 23.64  ? 18   ARG C C   1 
ATOM   8520  O  O   . ARG C  1 18  ? -21.143 16.439  114.767 1.00 23.34  ? 18   ARG C O   1 
ATOM   8521  C  CB  . ARG C  1 18  ? -20.912 15.448  117.494 1.00 40.05  ? 18   ARG C CB  1 
ATOM   8522  C  CG  . ARG C  1 18  ? -21.801 16.628  117.760 1.00 44.77  ? 18   ARG C CG  1 
ATOM   8523  C  CD  . ARG C  1 18  ? -21.008 17.725  118.432 1.00 53.88  ? 18   ARG C CD  1 
ATOM   8524  N  NE  . ARG C  1 18  ? -20.262 17.241  119.601 1.00 62.81  ? 18   ARG C NE  1 
ATOM   8525  C  CZ  . ARG C  1 18  ? -18.943 17.392  119.773 1.00 66.44  ? 18   ARG C CZ  1 
ATOM   8526  N  NH1 . ARG C  1 18  ? -18.204 18.016  118.848 1.00 65.01  ? 18   ARG C NH1 1 
ATOM   8527  N  NH2 . ARG C  1 18  ? -18.360 16.921  120.877 1.00 66.95  ? 18   ARG C NH2 1 
ATOM   8528  N  N   . GLY C  1 19  ? -23.092 15.320  114.826 1.00 48.35  ? 19   GLY C N   1 
ATOM   8529  C  CA  . GLY C  1 19  ? -23.719 16.069  113.755 1.00 22.94  ? 19   GLY C CA  1 
ATOM   8530  C  C   . GLY C  1 19  ? -24.555 17.225  114.257 1.00 23.70  ? 19   GLY C C   1 
ATOM   8531  O  O   . GLY C  1 19  ? -24.505 17.600  115.429 1.00 27.52  ? 19   GLY C O   1 
ATOM   8532  N  N   . ILE C  1 20  ? -25.336 17.787  113.347 1.00 24.93  ? 20   ILE C N   1 
ATOM   8533  C  CA  . ILE C  1 20  ? -26.120 18.977  113.617 1.00 27.58  ? 20   ILE C CA  1 
ATOM   8534  C  C   . ILE C  1 20  ? -27.617 18.717  113.334 1.00 29.06  ? 20   ILE C C   1 
ATOM   8535  O  O   . ILE C  1 20  ? -27.983 18.014  112.386 1.00 23.55  ? 20   ILE C O   1 
ATOM   8536  C  CB  . ILE C  1 20  ? -25.525 20.189  112.824 1.00 23.66  ? 20   ILE C CB  1 
ATOM   8537  C  CG1 . ILE C  1 20  ? -25.990 21.534  113.397 1.00 31.32  ? 20   ILE C CG1 1 
ATOM   8538  C  CG2 . ILE C  1 20  ? -25.784 20.057  111.355 1.00 26.11  ? 20   ILE C CG2 1 
ATOM   8539  C  CD1 . ILE C  1 20  ? -27.310 22.061  112.872 1.00 30.45  ? 20   ILE C CD1 1 
ATOM   8540  N  N   . ARG C  1 21  ? -28.473 19.267  114.189 1.00 25.30  ? 21   ARG C N   1 
ATOM   8541  C  CA  . ARG C  1 21  ? -29.911 19.119  114.050 1.00 32.51  ? 21   ARG C CA  1 
ATOM   8542  C  C   . ARG C  1 21  ? -30.409 20.270  113.195 1.00 31.60  ? 21   ARG C C   1 
ATOM   8543  O  O   . ARG C  1 21  ? -30.391 21.407  113.645 1.00 37.09  ? 21   ARG C O   1 
ATOM   8544  C  CB  . ARG C  1 21  ? -30.544 19.233  115.436 1.00 46.95  ? 21   ARG C CB  1 
ATOM   8545  C  CG  . ARG C  1 21  ? -32.021 18.896  115.521 1.00 53.26  ? 21   ARG C CG  1 
ATOM   8546  C  CD  . ARG C  1 21  ? -32.548 19.206  116.908 1.00 60.00  ? 21   ARG C CD  1 
ATOM   8547  N  NE  . ARG C  1 21  ? -32.958 20.598  117.004 1.00 66.71  ? 21   ARG C NE  1 
ATOM   8548  C  CZ  . ARG C  1 21  ? -34.218 21.003  116.896 1.00 72.34  ? 21   ARG C CZ  1 
ATOM   8549  N  NH1 . ARG C  1 21  ? -35.183 20.111  116.711 1.00 73.50  ? 21   ARG C NH1 1 
ATOM   8550  N  NH2 . ARG C  1 21  ? -34.519 22.292  116.984 1.00 74.73  ? 21   ARG C NH2 1 
ATOM   8551  N  N   . LEU C  1 22  ? -30.883 19.998  111.982 1.00 27.79  ? 22   LEU C N   1 
ATOM   8552  C  CA  . LEU C  1 22  ? -31.293 21.082  111.088 1.00 26.85  ? 22   LEU C CA  1 
ATOM   8553  C  C   . LEU C  1 22  ? -32.792 21.040  111.012 1.00 28.26  ? 22   LEU C C   1 
ATOM   8554  O  O   . LEU C  1 22  ? -33.369 19.973  111.213 1.00 25.71  ? 22   LEU C O   1 
ATOM   8555  C  CB  . LEU C  1 22  ? -30.779 20.867  109.681 1.00 23.76  ? 22   LEU C CB  1 
ATOM   8556  C  CG  . LEU C  1 22  ? -29.381 20.352  109.425 1.00 22.84  ? 22   LEU C CG  1 
ATOM   8557  C  CD1 . LEU C  1 22  ? -29.393 19.821  108.016 1.00 22.79  ? 22   LEU C CD1 1 
ATOM   8558  C  CD2 . LEU C  1 22  ? -28.386 21.472  109.544 1.00 22.89  ? 22   LEU C CD2 1 
ATOM   8559  N  N   . LYS C  1 23  ? -33.432 22.184  110.741 1.00 32.97  ? 23   LYS C N   1 
ATOM   8560  C  CA  . LYS C  1 23  ? -34.887 22.185  110.561 1.00 34.87  ? 23   LYS C CA  1 
ATOM   8561  C  C   . LYS C  1 23  ? -35.315 22.096  109.098 1.00 30.30  ? 23   LYS C C   1 
ATOM   8562  O  O   . LYS C  1 23  ? -34.886 22.874  108.251 1.00 26.78  ? 23   LYS C O   1 
ATOM   8563  C  CB  . LYS C  1 23  ? -35.587 23.333  111.306 1.00 57.27  ? 23   LYS C CB  1 
ATOM   8564  C  CG  . LYS C  1 23  ? -35.098 24.731  110.981 1.00 65.81  ? 23   LYS C CG  1 
ATOM   8565  C  CD  . LYS C  1 23  ? -35.945 25.790  111.709 1.00 73.83  ? 23   LYS C CD  1 
ATOM   8566  C  CE  . LYS C  1 23  ? -35.728 25.762  113.226 1.00 78.11  ? 23   LYS C CE  1 
ATOM   8567  N  NZ  . LYS C  1 23  ? -36.661 26.673  113.961 1.00 81.08  ? 23   LYS C NZ  1 
ATOM   8568  N  N   . ALA C  1 24  ? -36.105 21.067  108.819 1.00 39.80  ? 24   ALA C N   1 
ATOM   8569  C  CA  . ALA C  1 24  ? -36.836 20.921  107.573 1.00 42.93  ? 24   ALA C CA  1 
ATOM   8570  C  C   . ALA C  1 24  ? -38.161 21.637  107.795 1.00 43.36  ? 24   ALA C C   1 
ATOM   8571  O  O   . ALA C  1 24  ? -38.518 21.915  108.950 1.00 40.60  ? 24   ALA C O   1 
ATOM   8572  C  CB  . ALA C  1 24  ? -37.056 19.448  107.262 1.00 39.67  ? 24   ALA C CB  1 
ATOM   8573  N  N   . PRO C  1 25  ? -38.889 21.954  106.708 1.00 40.05  ? 25   PRO C N   1 
ATOM   8574  C  CA  . PRO C  1 25  ? -40.067 22.791  106.896 1.00 40.48  ? 25   PRO C CA  1 
ATOM   8575  C  C   . PRO C  1 25  ? -41.059 22.127  107.826 1.00 38.78  ? 25   PRO C C   1 
ATOM   8576  O  O   . PRO C  1 25  ? -41.744 22.819  108.572 1.00 37.78  ? 25   PRO C O   1 
ATOM   8577  C  CB  . PRO C  1 25  ? -40.645 22.890  105.483 1.00 38.58  ? 25   PRO C CB  1 
ATOM   8578  C  CG  . PRO C  1 25  ? -39.494 22.679  104.599 1.00 36.33  ? 25   PRO C CG  1 
ATOM   8579  C  CD  . PRO C  1 25  ? -38.732 21.591  105.293 1.00 36.91  ? 25   PRO C CD  1 
ATOM   8580  N  N   . GLY C  1 26  ? -41.105 20.803  107.814 1.00 38.66  ? 26   GLY C N   1 
ATOM   8581  C  CA  . GLY C  1 26  ? -42.107 20.118  108.607 1.00 41.89  ? 26   GLY C CA  1 
ATOM   8582  C  C   . GLY C  1 26  ? -41.672 19.448  109.894 1.00 42.59  ? 26   GLY C C   1 
ATOM   8583  O  O   . GLY C  1 26  ? -42.453 18.715  110.498 1.00 42.82  ? 26   GLY C O   1 
ATOM   8584  N  N   . GLY C  1 27  ? -40.444 19.699  110.325 1.00 55.27  ? 27   GLY C N   1 
ATOM   8585  C  CA  . GLY C  1 27  ? -39.892 18.997  111.470 1.00 57.77  ? 27   GLY C CA  1 
ATOM   8586  C  C   . GLY C  1 27  ? -38.388 19.081  111.397 1.00 56.94  ? 27   GLY C C   1 
ATOM   8587  O  O   . GLY C  1 27  ? -37.863 19.675  110.462 1.00 61.39  ? 27   GLY C O   1 
ATOM   8588  N  N   . PRO C  1 28  ? -37.678 18.536  112.391 1.00 39.32  ? 28   PRO C N   1 
ATOM   8589  C  CA  . PRO C  1 28  ? -36.234 18.600  112.209 1.00 34.45  ? 28   PRO C CA  1 
ATOM   8590  C  C   . PRO C  1 28  ? -35.704 17.328  111.556 1.00 33.28  ? 28   PRO C C   1 
ATOM   8591  O  O   . PRO C  1 28  ? -36.444 16.346  111.410 1.00 35.12  ? 28   PRO C O   1 
ATOM   8592  C  CB  . PRO C  1 28  ? -35.725 18.712  113.640 1.00 29.52  ? 28   PRO C CB  1 
ATOM   8593  C  CG  . PRO C  1 28  ? -36.782 18.034  114.471 1.00 29.48  ? 28   PRO C CG  1 
ATOM   8594  C  CD  . PRO C  1 28  ? -38.028 17.847  113.635 1.00 35.61  ? 28   PRO C CD  1 
ATOM   8595  N  N   . VAL C  1 29  ? -34.417 17.348  111.221 1.00 25.66  ? 29   VAL C N   1 
ATOM   8596  C  CA  . VAL C  1 29  ? -33.702 16.209  110.675 1.00 25.19  ? 29   VAL C CA  1 
ATOM   8597  C  C   . VAL C  1 29  ? -32.366 16.221  111.376 1.00 26.17  ? 29   VAL C C   1 
ATOM   8598  O  O   . VAL C  1 29  ? -31.961 17.257  111.922 1.00 24.77  ? 29   VAL C O   1 
ATOM   8599  C  CB  . VAL C  1 29  ? -33.451 16.326  109.159 1.00 23.67  ? 29   VAL C CB  1 
ATOM   8600  C  CG1 . VAL C  1 29  ? -34.705 16.074  108.396 1.00 25.56  ? 29   VAL C CG1 1 
ATOM   8601  C  CG2 . VAL C  1 29  ? -32.911 17.688  108.820 1.00 23.44  ? 29   VAL C CG2 1 
ATOM   8602  N  N   . SER C  1 30  ? -31.708 15.063  111.386 1.00 40.64  ? 30   SER C N   1 
ATOM   8603  C  CA  . SER C  1 30  ? -30.347 14.920  111.876 1.00 43.12  ? 30   SER C CA  1 
ATOM   8604  C  C   . SER C  1 30  ? -29.445 14.929  110.658 1.00 41.29  ? 30   SER C C   1 
ATOM   8605  O  O   . SER C  1 30  ? -29.763 14.304  109.643 1.00 44.03  ? 30   SER C O   1 
ATOM   8606  C  CB  . SER C  1 30  ? -30.165 13.591  112.617 1.00 39.20  ? 30   SER C CB  1 
ATOM   8607  O  OG  . SER C  1 30  ? -31.023 13.471  113.733 1.00 40.95  ? 30   SER C OG  1 
ATOM   8608  N  N   . ALA C  1 31  ? -28.324 15.632  110.748 1.00 25.93  ? 31   ALA C N   1 
ATOM   8609  C  CA  . ALA C  1 31  ? -27.392 15.674  109.636 1.00 24.20  ? 31   ALA C CA  1 
ATOM   8610  C  C   . ALA C  1 31  ? -25.957 15.509  110.097 1.00 27.68  ? 31   ALA C C   1 
ATOM   8611  O  O   . ALA C  1 31  ? -25.507 16.159  111.032 1.00 31.26  ? 31   ALA C O   1 
ATOM   8612  C  CB  . ALA C  1 31  ? -27.542 16.961  108.877 1.00 21.59  ? 31   ALA C CB  1 
ATOM   8613  N  N   . PHE C  1 32  ? -25.231 14.635  109.423 1.00 23.39  ? 32   PHE C N   1 
ATOM   8614  C  CA  . PHE C  1 32  ? -23.820 14.470  109.692 1.00 20.35  ? 32   PHE C CA  1 
ATOM   8615  C  C   . PHE C  1 32  ? -23.103 14.761  108.395 1.00 19.16  ? 32   PHE C C   1 
ATOM   8616  O  O   . PHE C  1 32  ? -23.217 14.010  107.440 1.00 18.56  ? 32   PHE C O   1 
ATOM   8617  C  CB  . PHE C  1 32  ? -23.561 13.052  110.176 1.00 22.93  ? 32   PHE C CB  1 
ATOM   8618  C  CG  . PHE C  1 32  ? -24.435 12.656  111.326 1.00 24.64  ? 32   PHE C CG  1 
ATOM   8619  C  CD1 . PHE C  1 32  ? -25.735 12.219  111.106 1.00 23.64  ? 32   PHE C CD1 1 
ATOM   8620  C  CD2 . PHE C  1 32  ? -23.970 12.747  112.622 1.00 24.74  ? 32   PHE C CD2 1 
ATOM   8621  C  CE1 . PHE C  1 32  ? -26.545 11.870  112.145 1.00 22.18  ? 32   PHE C CE1 1 
ATOM   8622  C  CE2 . PHE C  1 32  ? -24.773 12.399  113.670 1.00 22.77  ? 32   PHE C CE2 1 
ATOM   8623  C  CZ  . PHE C  1 32  ? -26.068 11.958  113.432 1.00 23.17  ? 32   PHE C CZ  1 
ATOM   8624  N  N   . LEU C  1 33  ? -22.376 15.869  108.363 1.00 19.36  ? 33   LEU C N   1 
ATOM   8625  C  CA  . LEU C  1 33  ? -21.793 16.342  107.125 1.00 19.32  ? 33   LEU C CA  1 
ATOM   8626  C  C   . LEU C  1 33  ? -20.276 16.352  107.203 1.00 22.80  ? 33   LEU C C   1 
ATOM   8627  O  O   . LEU C  1 33  ? -19.687 16.780  108.203 1.00 24.21  ? 33   LEU C O   1 
ATOM   8628  C  CB  . LEU C  1 33  ? -22.302 17.740  106.833 1.00 18.68  ? 33   LEU C CB  1 
ATOM   8629  C  CG  . LEU C  1 33  ? -23.792 17.873  107.078 1.00 19.12  ? 33   LEU C CG  1 
ATOM   8630  C  CD1 . LEU C  1 33  ? -24.105 19.284  107.392 1.00 19.71  ? 33   LEU C CD1 1 
ATOM   8631  C  CD2 . LEU C  1 33  ? -24.531 17.457  105.855 1.00 18.56  ? 33   LEU C CD2 1 
ATOM   8632  N  N   . GLY C  1 34  ? -19.643 15.874  106.137 1.00 22.57  ? 34   GLY C N   1 
ATOM   8633  C  CA  . GLY C  1 34  ? -18.200 15.958  106.025 1.00 23.85  ? 34   GLY C CA  1 
ATOM   8634  C  C   . GLY C  1 34  ? -17.491 14.902  106.834 1.00 17.79  ? 34   GLY C C   1 
ATOM   8635  O  O   . GLY C  1 34  ? -16.436 15.161  107.404 1.00 18.16  ? 34   GLY C O   1 
ATOM   8636  N  N   . ILE C  1 35  ? -18.090 13.718  106.895 1.00 17.69  ? 35   ILE C N   1 
ATOM   8637  C  CA  . ILE C  1 35  ? -17.453 12.559  107.490 1.00 17.94  ? 35   ILE C CA  1 
ATOM   8638  C  C   . ILE C  1 35  ? -16.416 12.064  106.515 1.00 17.41  ? 35   ILE C C   1 
ATOM   8639  O  O   . ILE C  1 35  ? -16.759 11.774  105.371 1.00 16.79  ? 35   ILE C O   1 
ATOM   8640  C  CB  . ILE C  1 35  ? -18.445 11.445  107.685 1.00 18.03  ? 35   ILE C CB  1 
ATOM   8641  C  CG1 . ILE C  1 35  ? -19.600 11.944  108.529 1.00 18.58  ? 35   ILE C CG1 1 
ATOM   8642  C  CG2 . ILE C  1 35  ? -17.769 10.279  108.332 1.00 18.41  ? 35   ILE C CG2 1 
ATOM   8643  C  CD1 . ILE C  1 35  ? -20.730 10.999  108.566 1.00 18.70  ? 35   ILE C CD1 1 
ATOM   8644  N  N   . PRO C  1 36  ? -15.138 12.014  106.941 1.00 17.72  ? 36   PRO C N   1 
ATOM   8645  C  CA  . PRO C  1 36  ? -14.074 11.572  106.034 1.00 17.33  ? 36   PRO C CA  1 
ATOM   8646  C  C   . PRO C  1 36  ? -14.134 10.082  105.748 1.00 17.18  ? 36   PRO C C   1 
ATOM   8647  O  O   . PRO C  1 36  ? -14.108 9.271   106.678 1.00 17.72  ? 36   PRO C O   1 
ATOM   8648  C  CB  . PRO C  1 36  ? -12.808 11.922  106.804 1.00 19.07  ? 36   PRO C CB  1 
ATOM   8649  C  CG  . PRO C  1 36  ? -13.221 11.855  108.247 1.00 18.69  ? 36   PRO C CG  1 
ATOM   8650  C  CD  . PRO C  1 36  ? -14.633 12.318  108.291 1.00 18.55  ? 36   PRO C CD  1 
ATOM   8651  N  N   . PHE C  1 37  ? -14.210 9.735   104.466 1.00 16.54  ? 37   PHE C N   1 
ATOM   8652  C  CA  . PHE C  1 37  ? -14.213 8.341   104.054 1.00 16.43  ? 37   PHE C CA  1 
ATOM   8653  C  C   . PHE C  1 37  ? -12.915 7.818   103.432 1.00 16.37  ? 37   PHE C C   1 
ATOM   8654  O  O   . PHE C  1 37  ? -12.818 6.649   103.071 1.00 18.09  ? 37   PHE C O   1 
ATOM   8655  C  CB  . PHE C  1 37  ? -15.462 7.989   103.236 1.00 15.98  ? 37   PHE C CB  1 
ATOM   8656  C  CG  . PHE C  1 37  ? -15.459 8.519   101.847 1.00 17.16  ? 37   PHE C CG  1 
ATOM   8657  C  CD1 . PHE C  1 37  ? -15.976 9.761   101.571 1.00 15.84  ? 37   PHE C CD1 1 
ATOM   8658  C  CD2 . PHE C  1 37  ? -14.966 7.758   100.807 1.00 21.22  ? 37   PHE C CD2 1 
ATOM   8659  C  CE1 . PHE C  1 37  ? -15.989 10.244  100.283 1.00 18.98  ? 37   PHE C CE1 1 
ATOM   8660  C  CE2 . PHE C  1 37  ? -14.973 8.235   99.514  1.00 23.41  ? 37   PHE C CE2 1 
ATOM   8661  C  CZ  . PHE C  1 37  ? -15.487 9.479   99.249  1.00 22.49  ? 37   PHE C CZ  1 
ATOM   8662  N  N   . ALA C  1 38  ? -11.922 8.682   103.298 1.00 21.68  ? 38   ALA C N   1 
ATOM   8663  C  CA  . ALA C  1 38  ? -10.645 8.246   102.751 1.00 21.85  ? 38   ALA C CA  1 
ATOM   8664  C  C   . ALA C  1 38  ? -9.510  9.130   103.231 1.00 24.86  ? 38   ALA C C   1 
ATOM   8665  O  O   . ALA C  1 38  ? -9.717  10.306  103.542 1.00 28.65  ? 38   ALA C O   1 
ATOM   8666  C  CB  . ALA C  1 38  ? -10.703 8.260   101.248 1.00 22.14  ? 38   ALA C CB  1 
ATOM   8667  N  N   . GLU C  1 39  ? -8.308  8.572   103.286 1.00 21.78  ? 39   GLU C N   1 
ATOM   8668  C  CA  . GLU C  1 39  ? -7.143  9.405   103.508 1.00 24.62  ? 39   GLU C CA  1 
ATOM   8669  C  C   . GLU C  1 39  ? -7.127  10.341  102.319 1.00 22.51  ? 39   GLU C C   1 
ATOM   8670  O  O   . GLU C  1 39  ? -7.418  9.909   101.193 1.00 19.90  ? 39   GLU C O   1 
ATOM   8671  C  CB  . GLU C  1 39  ? -5.860  8.576   103.572 1.00 38.35  ? 39   GLU C CB  1 
ATOM   8672  C  CG  . GLU C  1 39  ? -5.713  7.768   104.845 1.00 45.98  ? 39   GLU C CG  1 
ATOM   8673  C  CD  . GLU C  1 39  ? -5.511  8.634   106.075 1.00 53.30  ? 39   GLU C CD  1 
ATOM   8674  O  OE1 . GLU C  1 39  ? -4.516  9.384   106.099 1.00 59.05  ? 39   GLU C OE1 1 
ATOM   8675  O  OE2 . GLU C  1 39  ? -6.338  8.566   107.016 1.00 51.85  ? 39   GLU C OE2 1 
ATOM   8676  N  N   . PRO C  1 40  ? -6.831  11.631  102.567 1.00 30.99  ? 40   PRO C N   1 
ATOM   8677  C  CA  . PRO C  1 40  ? -6.836  12.649  101.517 1.00 30.07  ? 40   PRO C CA  1 
ATOM   8678  C  C   . PRO C  1 40  ? -5.891  12.259  100.408 1.00 26.60  ? 40   PRO C C   1 
ATOM   8679  O  O   . PRO C  1 40  ? -4.723  11.997  100.688 1.00 24.43  ? 40   PRO C O   1 
ATOM   8680  C  CB  . PRO C  1 40  ? -6.304  13.899  102.233 1.00 28.74  ? 40   PRO C CB  1 
ATOM   8681  C  CG  . PRO C  1 40  ? -5.622  13.398  103.435 1.00 28.91  ? 40   PRO C CG  1 
ATOM   8682  C  CD  . PRO C  1 40  ? -6.409  12.196  103.855 1.00 29.25  ? 40   PRO C CD  1 
ATOM   8683  N  N   . PRO C  1 41  ? -6.392  12.243  99.161  1.00 19.75  ? 41   PRO C N   1 
ATOM   8684  C  CA  . PRO C  1 41  ? -5.608  11.811  98.003  1.00 16.18  ? 41   PRO C CA  1 
ATOM   8685  C  C   . PRO C  1 41  ? -4.674  12.896  97.552  1.00 16.51  ? 41   PRO C C   1 
ATOM   8686  O  O   . PRO C  1 41  ? -4.622  13.178  96.364  1.00 16.74  ? 41   PRO C O   1 
ATOM   8687  C  CB  . PRO C  1 41  ? -6.671  11.614  96.917  1.00 18.11  ? 41   PRO C CB  1 
ATOM   8688  C  CG  . PRO C  1 41  ? -7.812  12.492  97.322  1.00 15.19  ? 41   PRO C CG  1 
ATOM   8689  C  CD  . PRO C  1 41  ? -7.809  12.491  98.823  1.00 15.67  ? 41   PRO C CD  1 
ATOM   8690  N  N   . VAL C  1 42  ? -3.925  13.481  98.471  1.00 17.20  ? 42   VAL C N   1 
ATOM   8691  C  CA  . VAL C  1 42  ? -3.048  14.571  98.103  1.00 17.64  ? 42   VAL C CA  1 
ATOM   8692  C  C   . VAL C  1 42  ? -1.605  14.093  97.985  1.00 19.28  ? 42   VAL C C   1 
ATOM   8693  O  O   . VAL C  1 42  ? -1.298  12.940  98.285  1.00 18.44  ? 42   VAL C O   1 
ATOM   8694  C  CB  . VAL C  1 42  ? -3.160  15.685  99.120  1.00 24.45  ? 42   VAL C CB  1 
ATOM   8695  C  CG1 . VAL C  1 42  ? -4.622  15.911  99.426  1.00 23.36  ? 42   VAL C CG1 1 
ATOM   8696  C  CG2 . VAL C  1 42  ? -2.431  15.301  100.384 1.00 27.13  ? 42   VAL C CG2 1 
ATOM   8697  N  N   . GLY C  1 43  ? -0.723  14.987  97.547  1.00 34.50  ? 43   GLY C N   1 
ATOM   8698  C  CA  . GLY C  1 43  ? 0.681   14.659  97.376  1.00 35.80  ? 43   GLY C CA  1 
ATOM   8699  C  C   . GLY C  1 43  ? 0.961   13.483  96.463  1.00 33.57  ? 43   GLY C C   1 
ATOM   8700  O  O   . GLY C  1 43  ? 0.591   13.467  95.285  1.00 33.04  ? 43   GLY C O   1 
ATOM   8701  N  N   . SER C  1 44  ? 1.648   12.502  97.037  1.00 25.47  ? 44   SER C N   1 
ATOM   8702  C  CA  . SER C  1 44  ? 2.038   11.278  96.352  1.00 26.35  ? 44   SER C CA  1 
ATOM   8703  C  C   . SER C  1 44  ? 0.846   10.408  95.984  1.00 26.57  ? 44   SER C C   1 
ATOM   8704  O  O   . SER C  1 44  ? 0.974   9.486   95.177  1.00 28.27  ? 44   SER C O   1 
ATOM   8705  C  CB  . SER C  1 44  ? 2.982   10.478  97.245  1.00 36.82  ? 44   SER C CB  1 
ATOM   8706  O  OG  . SER C  1 44  ? 3.216   11.175  98.457  1.00 41.28  ? 44   SER C OG  1 
ATOM   8707  N  N   . ARG C  1 45  ? -0.311  10.695  96.573  1.00 23.10  ? 45   ARG C N   1 
ATOM   8708  C  CA  . ARG C  1 45  ? -1.500  9.902   96.318  1.00 23.15  ? 45   ARG C CA  1 
ATOM   8709  C  C   . ARG C  1 45  ? -2.291  10.411  95.123  1.00 16.88  ? 45   ARG C C   1 
ATOM   8710  O  O   . ARG C  1 45  ? -3.255  9.782   94.702  1.00 17.28  ? 45   ARG C O   1 
ATOM   8711  C  CB  . ARG C  1 45  ? -2.376  9.821   97.559  1.00 40.13  ? 45   ARG C CB  1 
ATOM   8712  C  CG  . ARG C  1 45  ? -1.900  8.791   98.541  1.00 51.99  ? 45   ARG C CG  1 
ATOM   8713  C  CD  . ARG C  1 45  ? -2.955  8.538   99.602  1.00 68.03  ? 45   ARG C CD  1 
ATOM   8714  N  NE  . ARG C  1 45  ? -2.440  7.798   100.759 1.00 82.32  ? 45   ARG C NE  1 
ATOM   8715  C  CZ  . ARG C  1 45  ? -1.843  8.364   101.808 1.00 91.23  ? 45   ARG C CZ  1 
ATOM   8716  N  NH1 . ARG C  1 45  ? -1.672  9.685   101.846 1.00 93.61  ? 45   ARG C NH1 1 
ATOM   8717  N  NH2 . ARG C  1 45  ? -1.412  7.613   102.818 1.00 93.40  ? 45   ARG C NH2 1 
ATOM   8718  N  N   . ARG C  1 46  ? -1.875  11.532  94.556  1.00 16.98  ? 46   ARG C N   1 
ATOM   8719  C  CA  . ARG C  1 46  ? -2.563  12.062  93.388  1.00 16.40  ? 46   ARG C CA  1 
ATOM   8720  C  C   . ARG C  1 46  ? -2.723  11.049  92.221  1.00 16.06  ? 46   ARG C C   1 
ATOM   8721  O  O   . ARG C  1 46  ? -1.771  10.368  91.817  1.00 16.48  ? 46   ARG C O   1 
ATOM   8722  C  CB  . ARG C  1 46  ? -1.887  13.346  92.917  1.00 16.77  ? 46   ARG C CB  1 
ATOM   8723  C  CG  . ARG C  1 46  ? -2.637  14.027  91.799  1.00 20.18  ? 46   ARG C CG  1 
ATOM   8724  C  CD  . ARG C  1 46  ? -1.885  15.216  91.268  1.00 18.81  ? 46   ARG C CD  1 
ATOM   8725  N  NE  . ARG C  1 46  ? -1.870  16.330  92.190  1.00 17.14  ? 46   ARG C NE  1 
ATOM   8726  C  CZ  . ARG C  1 46  ? -1.454  17.534  91.850  1.00 17.60  ? 46   ARG C CZ  1 
ATOM   8727  N  NH1 . ARG C  1 46  ? -1.023  17.748  90.619  1.00 17.73  ? 46   ARG C NH1 1 
ATOM   8728  N  NH2 . ARG C  1 46  ? -1.478  18.517  92.731  1.00 18.00  ? 46   ARG C NH2 1 
ATOM   8729  N  N   . PHE C  1 47  ? -3.942  10.975  91.690  1.00 16.59  ? 47   PHE C N   1 
ATOM   8730  C  CA  . PHE C  1 47  ? -4.356  9.998   90.671  1.00 17.84  ? 47   PHE C CA  1 
ATOM   8731  C  C   . PHE C  1 47  ? -4.334  8.545   91.142  1.00 17.30  ? 47   PHE C C   1 
ATOM   8732  O  O   . PHE C  1 47  ? -4.290  7.634   90.319  1.00 16.93  ? 47   PHE C O   1 
ATOM   8733  C  CB  . PHE C  1 47  ? -3.499  10.062  89.395  1.00 16.59  ? 47   PHE C CB  1 
ATOM   8734  C  CG  . PHE C  1 47  ? -3.048  11.436  89.007  1.00 16.80  ? 47   PHE C CG  1 
ATOM   8735  C  CD1 . PHE C  1 47  ? -3.929  12.338  88.444  1.00 17.52  ? 47   PHE C CD1 1 
ATOM   8736  C  CD2 . PHE C  1 47  ? -1.726  11.802  89.150  1.00 16.23  ? 47   PHE C CD2 1 
ATOM   8737  C  CE1 . PHE C  1 47  ? -3.508  13.592  88.062  1.00 17.03  ? 47   PHE C CE1 1 
ATOM   8738  C  CE2 . PHE C  1 47  ? -1.299  13.044  88.763  1.00 20.29  ? 47   PHE C CE2 1 
ATOM   8739  C  CZ  . PHE C  1 47  ? -2.191  13.943  88.224  1.00 19.01  ? 47   PHE C CZ  1 
ATOM   8740  N  N   . MET C  1 48  ? -4.396  8.308   92.442  1.00 21.85  ? 48   MET C N   1 
ATOM   8741  C  CA  . MET C  1 48  ? -4.336  6.935   92.909  1.00 22.52  ? 48   MET C CA  1 
ATOM   8742  C  C   . MET C  1 48  ? -5.628  6.518   93.575  1.00 22.03  ? 48   MET C C   1 
ATOM   8743  O  O   . MET C  1 48  ? -6.326  7.368   94.144  1.00 20.61  ? 48   MET C O   1 
ATOM   8744  C  CB  . MET C  1 48  ? -3.185  6.764   93.876  1.00 16.36  ? 48   MET C CB  1 
ATOM   8745  C  CG  . MET C  1 48  ? -1.913  7.293   93.325  1.00 20.98  ? 48   MET C CG  1 
ATOM   8746  S  SD  . MET C  1 48  ? -0.680  6.002   93.256  1.00 48.89  ? 48   MET C SD  1 
ATOM   8747  C  CE  . MET C  1 48  ? -1.652  4.693   92.515  1.00 17.20  ? 48   MET C CE  1 
ATOM   8748  N  N   . PRO C  1 49  ? -5.941  5.204   93.511  1.00 17.10  ? 49   PRO C N   1 
ATOM   8749  C  CA  . PRO C  1 49  ? -7.095  4.619   94.176  1.00 15.16  ? 49   PRO C CA  1 
ATOM   8750  C  C   . PRO C  1 49  ? -7.109  5.086   95.618  1.00 18.92  ? 49   PRO C C   1 
ATOM   8751  O  O   . PRO C  1 49  ? -6.030  5.259   96.188  1.00 19.20  ? 49   PRO C O   1 
ATOM   8752  C  CB  . PRO C  1 49  ? -6.786  3.134   94.102  1.00 29.24  ? 49   PRO C CB  1 
ATOM   8753  C  CG  . PRO C  1 49  ? -6.081  2.994   92.828  1.00 15.62  ? 49   PRO C CG  1 
ATOM   8754  C  CD  . PRO C  1 49  ? -5.200  4.181   92.757  1.00 15.67  ? 49   PRO C CD  1 
ATOM   8755  N  N   . PRO C  1 50  ? -8.303  5.342   96.183  1.00 15.12  ? 50   PRO C N   1 
ATOM   8756  C  CA  . PRO C  1 50  ? -8.343  5.935   97.512  1.00 15.39  ? 50   PRO C CA  1 
ATOM   8757  C  C   . PRO C  1 50  ? -7.945  4.911   98.559  1.00 18.65  ? 50   PRO C C   1 
ATOM   8758  O  O   . PRO C  1 50  ? -8.269  3.733   98.408  1.00 16.16  ? 50   PRO C O   1 
ATOM   8759  C  CB  . PRO C  1 50  ? -9.809  6.326   97.657  1.00 14.96  ? 50   PRO C CB  1 
ATOM   8760  C  CG  . PRO C  1 50  ? -10.526 5.365   96.830  1.00 14.70  ? 50   PRO C CG  1 
ATOM   8761  C  CD  . PRO C  1 50  ? -9.656  5.135   95.646  1.00 18.83  ? 50   PRO C CD  1 
ATOM   8762  N  N   . GLU C  1 51  ? -7.201  5.345   99.571  1.00 40.36  ? 51   GLU C N   1 
ATOM   8763  C  CA  . GLU C  1 51  ? -6.952  4.513   100.736 1.00 46.79  ? 51   GLU C CA  1 
ATOM   8764  C  C   . GLU C  1 51  ? -7.950  4.929   101.792 1.00 47.42  ? 51   GLU C C   1 
ATOM   8765  O  O   . GLU C  1 51  ? -8.117  6.119   102.054 1.00 54.96  ? 51   GLU C O   1 
ATOM   8766  C  CB  . GLU C  1 51  ? -5.522  4.675   101.234 1.00 61.67  ? 51   GLU C CB  1 
ATOM   8767  C  CG  . GLU C  1 51  ? -4.590  3.637   100.644 1.00 75.06  ? 51   GLU C CG  1 
ATOM   8768  C  CD  . GLU C  1 51  ? -3.123  3.923   100.915 1.00 87.97  ? 51   GLU C CD  1 
ATOM   8769  O  OE1 . GLU C  1 51  ? -2.807  5.067   101.322 1.00 91.77  ? 51   GLU C OE1 1 
ATOM   8770  O  OE2 . GLU C  1 51  ? -2.290  3.000   100.717 1.00 91.50  ? 51   GLU C OE2 1 
ATOM   8771  N  N   . PRO C  1 52  ? -8.637  3.951   102.389 1.00 27.84  ? 52   PRO C N   1 
ATOM   8772  C  CA  . PRO C  1 52  ? -9.709  4.200   103.359 1.00 24.35  ? 52   PRO C CA  1 
ATOM   8773  C  C   . PRO C  1 52  ? -9.212  5.013   104.555 1.00 22.12  ? 52   PRO C C   1 
ATOM   8774  O  O   . PRO C  1 52  ? -8.035  4.892   104.925 1.00 18.75  ? 52   PRO C O   1 
ATOM   8775  C  CB  . PRO C  1 52  ? -10.104 2.789   103.798 1.00 30.77  ? 52   PRO C CB  1 
ATOM   8776  C  CG  . PRO C  1 52  ? -8.863  1.990   103.591 1.00 31.47  ? 52   PRO C CG  1 
ATOM   8777  C  CD  . PRO C  1 52  ? -8.282  2.527   102.324 1.00 32.53  ? 52   PRO C CD  1 
ATOM   8778  N  N   . LYS C  1 53  ? -10.095 5.815   105.150 1.00 24.32  ? 53   LYS C N   1 
ATOM   8779  C  CA  . LYS C  1 53  ? -9.687  6.741   106.201 1.00 25.26  ? 53   LYS C CA  1 
ATOM   8780  C  C   . LYS C  1 53  ? -9.288  5.957   107.428 1.00 28.30  ? 53   LYS C C   1 
ATOM   8781  O  O   . LYS C  1 53  ? -10.094 5.200   107.966 1.00 30.22  ? 53   LYS C O   1 
ATOM   8782  C  CB  . LYS C  1 53  ? -10.832 7.695   106.576 1.00 23.77  ? 53   LYS C CB  1 
ATOM   8783  C  CG  . LYS C  1 53  ? -10.479 8.728   107.651 1.00 18.98  ? 53   LYS C CG  1 
ATOM   8784  C  CD  . LYS C  1 53  ? -9.567  9.807   107.079 1.00 25.36  ? 53   LYS C CD  1 
ATOM   8785  C  CE  . LYS C  1 53  ? -9.348  10.974  108.029 1.00 19.42  ? 53   LYS C CE  1 
ATOM   8786  N  NZ  . LYS C  1 53  ? -8.420  10.588  109.108 1.00 38.30  ? 53   LYS C NZ  1 
ATOM   8787  N  N   . ARG C  1 54  ? -8.058  6.148   107.886 1.00 20.15  ? 54   ARG C N   1 
ATOM   8788  C  CA  . ARG C  1 54  ? -7.643  5.526   109.122 1.00 59.63  ? 54   ARG C CA  1 
ATOM   8789  C  C   . ARG C  1 54  ? -8.282  6.259   110.302 1.00 21.57  ? 54   ARG C C   1 
ATOM   8790  O  O   . ARG C  1 54  ? -8.411  7.481   110.284 1.00 40.20  ? 54   ARG C O   1 
ATOM   8791  C  CB  . ARG C  1 54  ? -6.128  5.520   109.231 1.00 72.22  ? 54   ARG C CB  1 
ATOM   8792  C  CG  . ARG C  1 54  ? -5.516  4.128   109.215 1.00 79.99  ? 54   ARG C CG  1 
ATOM   8793  C  CD  . ARG C  1 54  ? -4.005  4.220   109.305 1.00 89.78  ? 54   ARG C CD  1 
ATOM   8794  N  NE  . ARG C  1 54  ? -3.453  5.024   108.213 1.00 96.25  ? 54   ARG C NE  1 
ATOM   8795  C  CZ  . ARG C  1 54  ? -3.030  6.281   108.329 1.00 98.79  ? 54   ARG C CZ  1 
ATOM   8796  N  NH1 . ARG C  1 54  ? -3.085  6.903   109.504 1.00 99.67  ? 54   ARG C NH1 1 
ATOM   8797  N  NH2 . ARG C  1 54  ? -2.551  6.914   107.262 1.00 98.71  ? 54   ARG C NH2 1 
ATOM   8798  N  N   . PRO C  1 55  ? -8.688  5.509   111.332 1.00 22.27  ? 55   PRO C N   1 
ATOM   8799  C  CA  . PRO C  1 55  ? -9.363  6.011   112.524 1.00 22.81  ? 55   PRO C CA  1 
ATOM   8800  C  C   . PRO C  1 55  ? -8.719  7.235   113.139 1.00 23.26  ? 55   PRO C C   1 
ATOM   8801  O  O   . PRO C  1 55  ? -7.521  7.442   113.059 1.00 23.58  ? 55   PRO C O   1 
ATOM   8802  C  CB  . PRO C  1 55  ? -9.255  4.839   113.488 1.00 23.79  ? 55   PRO C CB  1 
ATOM   8803  C  CG  . PRO C  1 55  ? -9.134  3.611   112.608 1.00 30.91  ? 55   PRO C CG  1 
ATOM   8804  C  CD  . PRO C  1 55  ? -8.900  4.062   111.192 1.00 27.81  ? 55   PRO C CD  1 
ATOM   8805  N  N   . TRP C  1 56  ? -9.558  8.064   113.733 1.00 35.65  ? 56   TRP C N   1 
ATOM   8806  C  CA  . TRP C  1 56  ? -9.149  9.342   114.276 1.00 39.89  ? 56   TRP C CA  1 
ATOM   8807  C  C   . TRP C  1 56  ? -9.427  9.330   115.761 1.00 46.94  ? 56   TRP C C   1 
ATOM   8808  O  O   . TRP C  1 56  ? -10.196 8.508   116.256 1.00 51.48  ? 56   TRP C O   1 
ATOM   8809  C  CB  . TRP C  1 56  ? -9.961  10.464  113.623 1.00 26.97  ? 56   TRP C CB  1 
ATOM   8810  C  CG  . TRP C  1 56  ? -11.492 10.310  113.748 1.00 24.15  ? 56   TRP C CG  1 
ATOM   8811  C  CD1 . TRP C  1 56  ? -12.271 10.703  114.792 1.00 23.31  ? 56   TRP C CD1 1 
ATOM   8812  C  CD2 . TRP C  1 56  ? -12.388 9.736   112.784 1.00 21.83  ? 56   TRP C CD2 1 
ATOM   8813  N  NE1 . TRP C  1 56  ? -13.589 10.411  114.541 1.00 24.40  ? 56   TRP C NE1 1 
ATOM   8814  C  CE2 . TRP C  1 56  ? -13.683 9.814   113.318 1.00 22.00  ? 56   TRP C CE2 1 
ATOM   8815  C  CE3 . TRP C  1 56  ? -12.215 9.163   111.527 1.00 21.02  ? 56   TRP C CE3 1 
ATOM   8816  C  CZ2 . TRP C  1 56  ? -14.788 9.351   112.646 1.00 21.40  ? 56   TRP C CZ2 1 
ATOM   8817  C  CZ3 . TRP C  1 56  ? -13.312 8.703   110.862 1.00 20.41  ? 56   TRP C CZ3 1 
ATOM   8818  C  CH2 . TRP C  1 56  ? -14.586 8.797   111.421 1.00 20.80  ? 56   TRP C CH2 1 
ATOM   8819  N  N   . SER C  1 57  ? -8.790  10.238  116.479 1.00 41.32  ? 57   SER C N   1 
ATOM   8820  C  CA  . SER C  1 57  ? -9.021  10.345  117.909 1.00 42.18  ? 57   SER C CA  1 
ATOM   8821  C  C   . SER C  1 57  ? -9.932  11.525  118.190 1.00 36.37  ? 57   SER C C   1 
ATOM   8822  O  O   . SER C  1 57  ? -9.931  12.522  117.469 1.00 37.64  ? 57   SER C O   1 
ATOM   8823  C  CB  . SER C  1 57  ? -7.698  10.476  118.666 1.00 64.48  ? 57   SER C CB  1 
ATOM   8824  O  OG  . SER C  1 57  ? -6.862  11.453  118.066 1.00 68.97  ? 57   SER C OG  1 
ATOM   8825  N  N   . GLY C  1 58  ? -10.746 11.390  119.221 1.00 30.37  ? 58   GLY C N   1 
ATOM   8826  C  CA  . GLY C  1 58  ? -11.639 12.462  119.610 1.00 30.15  ? 58   GLY C CA  1 
ATOM   8827  C  C   . GLY C  1 58  ? -12.980 12.347  118.931 1.00 27.70  ? 58   GLY C C   1 
ATOM   8828  O  O   . GLY C  1 58  ? -13.193 11.426  118.148 1.00 27.34  ? 58   GLY C O   1 
ATOM   8829  N  N   . VAL C  1 59  ? -13.897 13.254  119.250 1.00 26.78  ? 59   VAL C N   1 
ATOM   8830  C  CA  . VAL C  1 59  ? -15.125 13.335  118.485 1.00 36.71  ? 59   VAL C CA  1 
ATOM   8831  C  C   . VAL C  1 59  ? -14.900 14.264  117.313 1.00 35.27  ? 59   VAL C C   1 
ATOM   8832  O  O   . VAL C  1 59  ? -14.401 15.379  117.485 1.00 34.35  ? 59   VAL C O   1 
ATOM   8833  C  CB  . VAL C  1 59  ? -16.294 13.828  119.304 1.00 26.61  ? 59   VAL C CB  1 
ATOM   8834  C  CG1 . VAL C  1 59  ? -17.402 14.244  118.393 1.00 25.81  ? 59   VAL C CG1 1 
ATOM   8835  C  CG2 . VAL C  1 59  ? -16.773 12.728  120.182 1.00 27.31  ? 59   VAL C CG2 1 
ATOM   8836  N  N   . LEU C  1 60  ? -15.249 13.776  116.125 1.00 42.85  ? 60   LEU C N   1 
ATOM   8837  C  CA  . LEU C  1 60  ? -15.060 14.493  114.874 1.00 42.01  ? 60   LEU C CA  1 
ATOM   8838  C  C   . LEU C  1 60  ? -16.272 15.361  114.589 1.00 43.55  ? 60   LEU C C   1 
ATOM   8839  O  O   . LEU C  1 60  ? -17.398 14.978  114.918 1.00 46.07  ? 60   LEU C O   1 
ATOM   8840  C  CB  . LEU C  1 60  ? -14.857 13.493  113.749 1.00 24.89  ? 60   LEU C CB  1 
ATOM   8841  C  CG  . LEU C  1 60  ? -14.703 14.091  112.362 1.00 22.73  ? 60   LEU C CG  1 
ATOM   8842  C  CD1 . LEU C  1 60  ? -13.428 13.560  111.714 1.00 23.25  ? 60   LEU C CD1 1 
ATOM   8843  C  CD2 . LEU C  1 60  ? -15.927 13.745  111.543 1.00 20.58  ? 60   LEU C CD2 1 
ATOM   8844  N  N   . ASP C  1 61  ? -16.060 16.530  113.990 1.00 33.84  ? 61   ASP C N   1 
ATOM   8845  C  CA  . ASP C  1 61  ? -17.173 17.454  113.845 1.00 36.22  ? 61   ASP C CA  1 
ATOM   8846  C  C   . ASP C  1 61  ? -17.878 17.277  112.505 1.00 34.93  ? 61   ASP C C   1 
ATOM   8847  O  O   . ASP C  1 61  ? -17.388 17.682  111.451 1.00 38.50  ? 61   ASP C O   1 
ATOM   8848  C  CB  . ASP C  1 61  ? -16.701 18.898  114.045 1.00 47.89  ? 61   ASP C CB  1 
ATOM   8849  C  CG  . ASP C  1 61  ? -17.749 19.923  113.647 1.00 54.52  ? 61   ASP C CG  1 
ATOM   8850  O  OD1 . ASP C  1 61  ? -18.943 19.580  113.641 1.00 57.29  ? 61   ASP C OD1 1 
ATOM   8851  O  OD2 . ASP C  1 61  ? -17.381 21.080  113.337 1.00 57.44  ? 61   ASP C OD2 1 
ATOM   8852  N  N   . ALA C  1 62  ? -19.066 16.698  112.581 1.00 26.21  ? 62   ALA C N   1 
ATOM   8853  C  CA  . ALA C  1 62  ? -19.904 16.466  111.420 1.00 25.78  ? 62   ALA C CA  1 
ATOM   8854  C  C   . ALA C  1 62  ? -20.976 17.532  111.214 1.00 29.24  ? 62   ALA C C   1 
ATOM   8855  O  O   . ALA C  1 62  ? -21.913 17.302  110.451 1.00 30.68  ? 62   ALA C O   1 
ATOM   8856  C  CB  . ALA C  1 62  ? -20.510 15.089  111.458 1.00 31.27  ? 62   ALA C CB  1 
ATOM   8857  N  N   . THR C  1 63  ? -20.908 18.637  111.959 1.00 21.79  ? 63   THR C N   1 
ATOM   8858  C  CA  . THR C  1 63  ? -21.895 19.718  111.818 1.00 31.04  ? 63   THR C CA  1 
ATOM   8859  C  C   . THR C  1 63  ? -21.849 20.525  110.517 1.00 30.89  ? 63   THR C C   1 
ATOM   8860  O  O   . THR C  1 63  ? -22.741 21.345  110.277 1.00 30.27  ? 63   THR C O   1 
ATOM   8861  C  CB  . THR C  1 63  ? -21.729 20.777  112.879 1.00 23.14  ? 63   THR C CB  1 
ATOM   8862  O  OG1 . THR C  1 63  ? -20.410 21.322  112.768 1.00 23.10  ? 63   THR C OG1 1 
ATOM   8863  C  CG2 . THR C  1 63  ? -21.950 20.197  114.254 1.00 37.55  ? 63   THR C CG2 1 
ATOM   8864  N  N   . THR C  1 64  ? -20.816 20.346  109.696 1.00 43.43  ? 64   THR C N   1 
ATOM   8865  C  CA  . THR C  1 64  ? -20.757 21.131  108.472 1.00 40.53  ? 64   THR C CA  1 
ATOM   8866  C  C   . THR C  1 64  ? -20.000 20.505  107.293 1.00 38.43  ? 64   THR C C   1 
ATOM   8867  O  O   . THR C  1 64  ? -19.077 19.697  107.490 1.00 38.20  ? 64   THR C O   1 
ATOM   8868  C  CB  . THR C  1 64  ? -20.192 22.496  108.767 1.00 34.94  ? 64   THR C CB  1 
ATOM   8869  O  OG1 . THR C  1 64  ? -19.613 23.024  107.570 1.00 38.13  ? 64   THR C OG1 1 
ATOM   8870  C  CG2 . THR C  1 64  ? -19.134 22.378  109.839 1.00 33.97  ? 64   THR C CG2 1 
ATOM   8871  N  N   . PHE C  1 65  ? -20.410 20.919  106.082 1.00 26.67  ? 65   PHE C N   1 
ATOM   8872  C  CA  . PHE C  1 65  ? -19.907 20.437  104.780 1.00 24.22  ? 65   PHE C CA  1 
ATOM   8873  C  C   . PHE C  1 65  ? -18.415 20.641  104.560 1.00 17.99  ? 65   PHE C C   1 
ATOM   8874  O  O   . PHE C  1 65  ? -17.877 21.713  104.853 1.00 19.35  ? 65   PHE C O   1 
ATOM   8875  C  CB  . PHE C  1 65  ? -20.604 21.187  103.643 1.00 17.90  ? 65   PHE C CB  1 
ATOM   8876  C  CG  . PHE C  1 65  ? -21.924 20.616  103.238 1.00 18.73  ? 65   PHE C CG  1 
ATOM   8877  C  CD1 . PHE C  1 65  ? -22.068 19.267  102.994 1.00 18.54  ? 65   PHE C CD1 1 
ATOM   8878  C  CD2 . PHE C  1 65  ? -23.030 21.440  103.092 1.00 21.02  ? 65   PHE C CD2 1 
ATOM   8879  C  CE1 . PHE C  1 65  ? -23.306 18.743  102.616 1.00 19.64  ? 65   PHE C CE1 1 
ATOM   8880  C  CE2 . PHE C  1 65  ? -24.264 20.924  102.711 1.00 21.43  ? 65   PHE C CE2 1 
ATOM   8881  C  CZ  . PHE C  1 65  ? -24.400 19.578  102.472 1.00 17.53  ? 65   PHE C CZ  1 
ATOM   8882  N  N   . GLN C  1 66  ? -17.765 19.641  103.975 1.00 28.25  ? 66   GLN C N   1 
ATOM   8883  C  CA  . GLN C  1 66  ? -16.343 19.732  103.653 1.00 17.30  ? 66   GLN C CA  1 
ATOM   8884  C  C   . GLN C  1 66  ? -16.027 20.283  102.261 1.00 16.90  ? 66   GLN C C   1 
ATOM   8885  O  O   . GLN C  1 66  ? -16.921 20.650  101.498 1.00 16.68  ? 66   GLN C O   1 
ATOM   8886  C  CB  . GLN C  1 66  ? -15.693 18.372  103.794 1.00 21.98  ? 66   GLN C CB  1 
ATOM   8887  C  CG  . GLN C  1 66  ? -15.237 18.077  105.182 1.00 25.01  ? 66   GLN C CG  1 
ATOM   8888  C  CD  . GLN C  1 66  ? -13.963 18.796  105.525 1.00 26.87  ? 66   GLN C CD  1 
ATOM   8889  O  OE1 . GLN C  1 66  ? -13.394 19.499  104.693 1.00 28.05  ? 66   GLN C OE1 1 
ATOM   8890  N  NE2 . GLN C  1 66  ? -13.498 18.619  106.758 1.00 27.87  ? 66   GLN C NE2 1 
ATOM   8891  N  N   . ASN C  1 67  ? -14.742 20.315  101.929 1.00 16.87  ? 67   ASN C N   1 
ATOM   8892  C  CA  . ASN C  1 67  ? -14.297 20.946  100.704 1.00 16.66  ? 67   ASN C CA  1 
ATOM   8893  C  C   . ASN C  1 67  ? -14.805 20.275  99.462  1.00 15.94  ? 67   ASN C C   1 
ATOM   8894  O  O   . ASN C  1 67  ? -14.870 19.048  99.380  1.00 18.28  ? 67   ASN C O   1 
ATOM   8895  C  CB  . ASN C  1 67  ? -12.788 20.963  100.648 1.00 23.32  ? 67   ASN C CB  1 
ATOM   8896  C  CG  . ASN C  1 67  ? -12.194 21.547  101.870 1.00 26.61  ? 67   ASN C CG  1 
ATOM   8897  O  OD1 . ASN C  1 67  ? -12.679 22.555  102.379 1.00 27.32  ? 67   ASN C OD1 1 
ATOM   8898  N  ND2 . ASN C  1 67  ? -11.153 20.909  102.385 1.00 30.29  ? 67   ASN C ND2 1 
ATOM   8899  N  N   . VAL C  1 68  ? -15.150 21.098  98.481  1.00 18.43  ? 68   VAL C N   1 
ATOM   8900  C  CA  . VAL C  1 68  ? -15.476 20.610  97.153  1.00 17.79  ? 68   VAL C CA  1 
ATOM   8901  C  C   . VAL C  1 68  ? -14.204 20.114  96.478  1.00 15.13  ? 68   VAL C C   1 
ATOM   8902  O  O   . VAL C  1 68  ? -13.155 20.738  96.603  1.00 15.45  ? 68   VAL C O   1 
ATOM   8903  C  CB  . VAL C  1 68  ? -16.086 21.727  96.312  1.00 23.55  ? 68   VAL C CB  1 
ATOM   8904  C  CG1 . VAL C  1 68  ? -16.279 21.264  94.882  1.00 26.71  ? 68   VAL C CG1 1 
ATOM   8905  C  CG2 . VAL C  1 68  ? -17.402 22.180  96.918  1.00 22.32  ? 68   VAL C CG2 1 
ATOM   8906  N  N   . CYS C  1 69  ? -14.292 18.985  95.784  1.00 19.97  ? 69   CYS C N   1 
ATOM   8907  C  CA  . CYS C  1 69  ? -13.164 18.478  95.010  1.00 22.44  ? 69   CYS C CA  1 
ATOM   8908  C  C   . CYS C  1 69  ? -12.687 19.470  93.962  1.00 27.96  ? 69   CYS C C   1 
ATOM   8909  O  O   . CYS C  1 69  ? -13.484 20.213  93.391  1.00 30.80  ? 69   CYS C O   1 
ATOM   8910  C  CB  . CYS C  1 69  ? -13.521 17.138  94.379  1.00 16.56  ? 69   CYS C CB  1 
ATOM   8911  S  SG  . CYS C  1 69  ? -13.401 15.803  95.561  1.00 50.15  ? 69   CYS C SG  1 
ATOM   8912  N  N   . TYR C  1 70  ? -11.387 19.487  93.709  1.00 14.70  ? 70   TYR C N   1 
ATOM   8913  C  CA  . TYR C  1 70  ? -10.815 20.558  92.911  1.00 15.04  ? 70   TYR C CA  1 
ATOM   8914  C  C   . TYR C  1 70  ? -11.215 20.511  91.437  1.00 29.95  ? 70   TYR C C   1 
ATOM   8915  O  O   . TYR C  1 70  ? -11.107 19.468  90.775  1.00 14.33  ? 70   TYR C O   1 
ATOM   8916  C  CB  . TYR C  1 70  ? -9.314  20.542  93.040  1.00 15.44  ? 70   TYR C CB  1 
ATOM   8917  C  CG  . TYR C  1 70  ? -8.710  21.894  92.920  1.00 16.11  ? 70   TYR C CG  1 
ATOM   8918  C  CD1 . TYR C  1 70  ? -8.556  22.698  94.030  1.00 16.69  ? 70   TYR C CD1 1 
ATOM   8919  C  CD2 . TYR C  1 70  ? -8.281  22.374  91.697  1.00 16.26  ? 70   TYR C CD2 1 
ATOM   8920  C  CE1 . TYR C  1 70  ? -7.968  23.955  93.938  1.00 17.43  ? 70   TYR C CE1 1 
ATOM   8921  C  CE2 . TYR C  1 70  ? -7.698  23.634  91.584  1.00 17.11  ? 70   TYR C CE2 1 
ATOM   8922  C  CZ  . TYR C  1 70  ? -7.544  24.424  92.710  1.00 17.59  ? 70   TYR C CZ  1 
ATOM   8923  O  OH  . TYR C  1 70  ? -6.970  25.674  92.610  1.00 18.42  ? 70   TYR C OH  1 
ATOM   8924  N  N   . GLN C  1 71  ? -11.662 21.643  90.905  1.00 15.00  ? 71   GLN C N   1 
ATOM   8925  C  CA  . GLN C  1 71  ? -12.283 21.591  89.598  1.00 28.25  ? 71   GLN C CA  1 
ATOM   8926  C  C   . GLN C  1 71  ? -12.377 22.884  88.814  1.00 30.85  ? 71   GLN C C   1 
ATOM   8927  O  O   . GLN C  1 71  ? -12.042 23.970  89.303  1.00 33.29  ? 71   GLN C O   1 
ATOM   8928  C  CB  . GLN C  1 71  ? -13.695 21.071  89.774  1.00 25.83  ? 71   GLN C CB  1 
ATOM   8929  C  CG  . GLN C  1 71  ? -14.507 21.874  90.749  1.00 14.67  ? 71   GLN C CG  1 
ATOM   8930  C  CD  . GLN C  1 71  ? -15.773 21.157  91.134  1.00 14.34  ? 71   GLN C CD  1 
ATOM   8931  O  OE1 . GLN C  1 71  ? -16.854 21.467  90.639  1.00 14.37  ? 71   GLN C OE1 1 
ATOM   8932  N  NE2 . GLN C  1 71  ? -15.645 20.174  92.007  1.00 14.10  ? 71   GLN C NE2 1 
ATOM   8933  N  N   . TYR C  1 72  ? -12.876 22.742  87.588  1.00 28.21  ? 72   TYR C N   1 
ATOM   8934  C  CA  . TYR C  1 72  ? -13.185 23.876  86.747  1.00 30.14  ? 72   TYR C CA  1 
ATOM   8935  C  C   . TYR C  1 72  ? -14.291 24.653  87.442  1.00 30.03  ? 72   TYR C C   1 
ATOM   8936  O  O   . TYR C  1 72  ? -15.178 24.061  88.058  1.00 28.88  ? 72   TYR C O   1 
ATOM   8937  C  CB  . TYR C  1 72  ? -13.643 23.410  85.362  1.00 45.45  ? 72   TYR C CB  1 
ATOM   8938  C  CG  . TYR C  1 72  ? -13.864 24.558  84.410  1.00 52.47  ? 72   TYR C CG  1 
ATOM   8939  C  CD1 . TYR C  1 72  ? -12.785 25.228  83.847  1.00 57.08  ? 72   TYR C CD1 1 
ATOM   8940  C  CD2 . TYR C  1 72  ? -15.148 24.993  84.095  1.00 55.62  ? 72   TYR C CD2 1 
ATOM   8941  C  CE1 . TYR C  1 72  ? -12.971 26.298  82.996  1.00 60.49  ? 72   TYR C CE1 1 
ATOM   8942  C  CE2 . TYR C  1 72  ? -15.348 26.066  83.240  1.00 59.08  ? 72   TYR C CE2 1 
ATOM   8943  C  CZ  . TYR C  1 72  ? -14.252 26.717  82.695  1.00 60.54  ? 72   TYR C CZ  1 
ATOM   8944  O  OH  . TYR C  1 72  ? -14.426 27.790  81.848  1.00 60.08  ? 72   TYR C OH  1 
ATOM   8945  N  N   . VAL C  1 73  ? -14.222 25.976  87.383  1.00 45.79  ? 73   VAL C N   1 
ATOM   8946  C  CA  . VAL C  1 73  ? -15.326 26.798  87.849  1.00 43.09  ? 73   VAL C CA  1 
ATOM   8947  C  C   . VAL C  1 73  ? -15.953 27.478  86.654  1.00 48.60  ? 73   VAL C C   1 
ATOM   8948  O  O   . VAL C  1 73  ? -15.241 28.057  85.832  1.00 54.69  ? 73   VAL C O   1 
ATOM   8949  C  CB  . VAL C  1 73  ? -14.851 27.854  88.807  1.00 17.85  ? 73   VAL C CB  1 
ATOM   8950  C  CG1 . VAL C  1 73  ? -16.018 28.669  89.270  1.00 18.00  ? 73   VAL C CG1 1 
ATOM   8951  C  CG2 . VAL C  1 73  ? -14.183 27.193  89.975  1.00 17.27  ? 73   VAL C CG2 1 
ATOM   8952  N  N   . ASP C  1 74  ? -17.279 27.434  86.557  1.00 25.46  ? 74   ASP C N   1 
ATOM   8953  C  CA  . ASP C  1 74  ? -17.930 27.816  85.306  1.00 29.51  ? 74   ASP C CA  1 
ATOM   8954  C  C   . ASP C  1 74  ? -17.996 29.334  85.111  1.00 36.24  ? 74   ASP C C   1 
ATOM   8955  O  O   . ASP C  1 74  ? -18.622 30.062  85.886  1.00 36.59  ? 74   ASP C O   1 
ATOM   8956  C  CB  . ASP C  1 74  ? -19.328 27.206  85.219  1.00 45.32  ? 74   ASP C CB  1 
ATOM   8957  C  CG  . ASP C  1 74  ? -19.972 27.440  83.875  1.00 50.43  ? 74   ASP C CG  1 
ATOM   8958  O  OD1 . ASP C  1 74  ? -19.256 27.316  82.860  1.00 52.71  ? 74   ASP C OD1 1 
ATOM   8959  O  OD2 . ASP C  1 74  ? -21.182 27.757  83.834  1.00 50.94  ? 74   ASP C OD2 1 
ATOM   8960  N  N   . THR C  1 75  ? -17.343 29.801  84.055  1.00 62.82  ? 75   THR C N   1 
ATOM   8961  C  CA  . THR C  1 75  ? -17.195 31.226  83.823  1.00 69.49  ? 75   THR C CA  1 
ATOM   8962  C  C   . THR C  1 75  ? -18.184 31.799  82.804  1.00 68.90  ? 75   THR C C   1 
ATOM   8963  O  O   . THR C  1 75  ? -18.163 32.998  82.540  1.00 73.81  ? 75   THR C O   1 
ATOM   8964  C  CB  . THR C  1 75  ? -15.751 31.550  83.395  1.00 81.14  ? 75   THR C CB  1 
ATOM   8965  O  OG1 . THR C  1 75  ? -15.517 31.074  82.061  1.00 85.58  ? 75   THR C OG1 1 
ATOM   8966  C  CG2 . THR C  1 75  ? -14.768 30.877  84.337  1.00 81.16  ? 75   THR C CG2 1 
ATOM   8967  N  N   . LEU C  1 76  ? -19.048 30.955  82.240  1.00 52.01  ? 76   LEU C N   1 
ATOM   8968  C  CA  . LEU C  1 76  ? -19.902 31.344  81.099  1.00 49.86  ? 76   LEU C CA  1 
ATOM   8969  C  C   . LEU C  1 76  ? -20.845 32.541  81.313  1.00 48.31  ? 76   LEU C C   1 
ATOM   8970  O  O   . LEU C  1 76  ? -20.850 33.491  80.525  1.00 47.83  ? 76   LEU C O   1 
ATOM   8971  C  CB  . LEU C  1 76  ? -20.723 30.143  80.590  1.00 48.47  ? 76   LEU C CB  1 
ATOM   8972  C  CG  . LEU C  1 76  ? -21.692 30.418  79.427  1.00 43.32  ? 76   LEU C CG  1 
ATOM   8973  C  CD1 . LEU C  1 76  ? -20.947 30.853  78.183  1.00 42.95  ? 76   LEU C CD1 1 
ATOM   8974  C  CD2 . LEU C  1 76  ? -22.550 29.221  79.120  1.00 38.73  ? 76   LEU C CD2 1 
ATOM   8975  N  N   . TYR C  1 77  ? -21.665 32.468  82.352  1.00 54.32  ? 77   TYR C N   1 
ATOM   8976  C  CA  . TYR C  1 77  ? -22.631 33.515  82.637  1.00 55.29  ? 77   TYR C CA  1 
ATOM   8977  C  C   . TYR C  1 77  ? -22.509 33.937  84.090  1.00 56.65  ? 77   TYR C C   1 
ATOM   8978  O  O   . TYR C  1 77  ? -23.303 33.506  84.920  1.00 59.49  ? 77   TYR C O   1 
ATOM   8979  C  CB  . TYR C  1 77  ? -24.047 32.995  82.412  1.00 48.50  ? 77   TYR C CB  1 
ATOM   8980  C  CG  . TYR C  1 77  ? -24.424 32.786  80.977  1.00 48.32  ? 77   TYR C CG  1 
ATOM   8981  C  CD1 . TYR C  1 77  ? -24.076 33.712  80.015  1.00 50.33  ? 77   TYR C CD1 1 
ATOM   8982  C  CD2 . TYR C  1 77  ? -25.130 31.658  80.583  1.00 49.54  ? 77   TYR C CD2 1 
ATOM   8983  C  CE1 . TYR C  1 77  ? -24.424 33.532  78.691  1.00 53.00  ? 77   TYR C CE1 1 
ATOM   8984  C  CE2 . TYR C  1 77  ? -25.489 31.462  79.257  1.00 51.45  ? 77   TYR C CE2 1 
ATOM   8985  C  CZ  . TYR C  1 77  ? -25.132 32.409  78.314  1.00 53.00  ? 77   TYR C CZ  1 
ATOM   8986  O  OH  . TYR C  1 77  ? -25.470 32.243  76.987  1.00 53.61  ? 77   TYR C OH  1 
ATOM   8987  N  N   . PRO C  1 78  ? -21.513 34.775  84.408  1.00 49.20  ? 78   PRO C N   1 
ATOM   8988  C  CA  . PRO C  1 78  ? -21.269 35.207  85.788  1.00 47.71  ? 78   PRO C CA  1 
ATOM   8989  C  C   . PRO C  1 78  ? -22.513 35.733  86.503  1.00 47.75  ? 78   PRO C C   1 
ATOM   8990  O  O   . PRO C  1 78  ? -23.275 36.499  85.923  1.00 48.62  ? 78   PRO C O   1 
ATOM   8991  C  CB  . PRO C  1 78  ? -20.248 36.324  85.609  1.00 37.93  ? 78   PRO C CB  1 
ATOM   8992  C  CG  . PRO C  1 78  ? -19.465 35.884  84.430  1.00 37.18  ? 78   PRO C CG  1 
ATOM   8993  C  CD  . PRO C  1 78  ? -20.471 35.269  83.495  1.00 38.72  ? 78   PRO C CD  1 
ATOM   8994  N  N   . GLY C  1 79  ? -22.715 35.291  87.742  1.00 47.74  ? 79   GLY C N   1 
ATOM   8995  C  CA  . GLY C  1 79  ? -23.829 35.733  88.556  1.00 49.16  ? 79   GLY C CA  1 
ATOM   8996  C  C   . GLY C  1 79  ? -25.192 35.372  87.999  1.00 51.21  ? 79   GLY C C   1 
ATOM   8997  O  O   . GLY C  1 79  ? -26.179 36.056  88.262  1.00 56.27  ? 79   GLY C O   1 
ATOM   8998  N  N   . PHE C  1 80  ? -25.259 34.300  87.225  1.00 47.03  ? 80   PHE C N   1 
ATOM   8999  C  CA  . PHE C  1 80  ? -26.533 33.867  86.670  1.00 45.86  ? 80   PHE C CA  1 
ATOM   9000  C  C   . PHE C  1 80  ? -26.964 32.572  87.344  1.00 45.78  ? 80   PHE C C   1 
ATOM   9001  O  O   . PHE C  1 80  ? -26.354 31.529  87.131  1.00 47.73  ? 80   PHE C O   1 
ATOM   9002  C  CB  . PHE C  1 80  ? -26.423 33.709  85.146  1.00 41.43  ? 80   PHE C CB  1 
ATOM   9003  C  CG  . PHE C  1 80  ? -27.555 32.939  84.522  1.00 42.34  ? 80   PHE C CG  1 
ATOM   9004  C  CD1 . PHE C  1 80  ? -28.866 33.345  84.681  1.00 46.09  ? 80   PHE C CD1 1 
ATOM   9005  C  CD2 . PHE C  1 80  ? -27.304 31.822  83.757  1.00 42.71  ? 80   PHE C CD2 1 
ATOM   9006  C  CE1 . PHE C  1 80  ? -29.907 32.638  84.101  1.00 46.98  ? 80   PHE C CE1 1 
ATOM   9007  C  CE2 . PHE C  1 80  ? -28.342 31.112  83.177  1.00 44.58  ? 80   PHE C CE2 1 
ATOM   9008  C  CZ  . PHE C  1 80  ? -29.646 31.520  83.353  1.00 45.92  ? 80   PHE C CZ  1 
ATOM   9009  N  N   . GLU C  1 81  ? -28.028 32.642  88.139  1.00 39.66  ? 81   GLU C N   1 
ATOM   9010  C  CA  . GLU C  1 81  ? -28.463 31.516  88.968  1.00 43.77  ? 81   GLU C CA  1 
ATOM   9011  C  C   . GLU C  1 81  ? -28.593 30.193  88.196  1.00 41.09  ? 81   GLU C C   1 
ATOM   9012  O  O   . GLU C  1 81  ? -28.414 29.110  88.761  1.00 41.16  ? 81   GLU C O   1 
ATOM   9013  C  CB  . GLU C  1 81  ? -29.781 31.858  89.662  1.00 69.55  ? 81   GLU C CB  1 
ATOM   9014  C  CG  . GLU C  1 81  ? -30.272 30.808  90.643  1.00 78.25  ? 81   GLU C CG  1 
ATOM   9015  C  CD  . GLU C  1 81  ? -31.596 31.194  91.285  1.00 87.36  ? 81   GLU C CD  1 
ATOM   9016  O  OE1 . GLU C  1 81  ? -31.607 32.147  92.102  1.00 90.18  ? 81   GLU C OE1 1 
ATOM   9017  O  OE2 . GLU C  1 81  ? -32.623 30.551  90.963  1.00 89.61  ? 81   GLU C OE2 1 
ATOM   9018  N  N   . GLY C  1 82  ? -28.870 30.284  86.900  1.00 45.80  ? 82   GLY C N   1 
ATOM   9019  C  CA  . GLY C  1 82  ? -28.983 29.099  86.076  1.00 43.33  ? 82   GLY C CA  1 
ATOM   9020  C  C   . GLY C  1 82  ? -27.702 28.286  86.024  1.00 39.79  ? 82   GLY C C   1 
ATOM   9021  O  O   . GLY C  1 82  ? -27.711 27.102  86.368  1.00 41.02  ? 82   GLY C O   1 
ATOM   9022  N  N   . THR C  1 83  ? -26.605 28.908  85.593  1.00 29.74  ? 83   THR C N   1 
ATOM   9023  C  CA  . THR C  1 83  ? -25.312 28.223  85.546  1.00 26.25  ? 83   THR C CA  1 
ATOM   9024  C  C   . THR C  1 83  ? -24.641 28.221  86.907  1.00 24.49  ? 83   THR C C   1 
ATOM   9025  O  O   . THR C  1 83  ? -23.838 27.336  87.210  1.00 24.72  ? 83   THR C O   1 
ATOM   9026  C  CB  . THR C  1 83  ? -24.317 28.873  84.570  1.00 24.01  ? 83   THR C CB  1 
ATOM   9027  O  OG1 . THR C  1 83  ? -23.889 30.135  85.092  1.00 19.81  ? 83   THR C OG1 1 
ATOM   9028  C  CG2 . THR C  1 83  ? -24.937 29.072  83.211  1.00 24.71  ? 83   THR C CG2 1 
ATOM   9029  N  N   . GLU C  1 84  ? -24.964 29.228  87.714  1.00 19.35  ? 84   GLU C N   1 
ATOM   9030  C  CA  . GLU C  1 84  ? -24.268 29.462  88.972  1.00 21.47  ? 84   GLU C CA  1 
ATOM   9031  C  C   . GLU C  1 84  ? -24.739 28.467  90.035  1.00 18.96  ? 84   GLU C C   1 
ATOM   9032  O  O   . GLU C  1 84  ? -24.051 28.223  91.040  1.00 18.60  ? 84   GLU C O   1 
ATOM   9033  C  CB  . GLU C  1 84  ? -24.472 30.916  89.423  1.00 46.59  ? 84   GLU C CB  1 
ATOM   9034  C  CG  . GLU C  1 84  ? -23.430 31.440  90.391  1.00 57.50  ? 84   GLU C CG  1 
ATOM   9035  C  CD  . GLU C  1 84  ? -22.043 31.534  89.779  1.00 64.91  ? 84   GLU C CD  1 
ATOM   9036  O  OE1 . GLU C  1 84  ? -21.875 32.292  88.796  1.00 66.95  ? 84   GLU C OE1 1 
ATOM   9037  O  OE2 . GLU C  1 84  ? -21.124 30.850  90.292  1.00 65.90  ? 84   GLU C OE2 1 
ATOM   9038  N  N   . MET C  1 85  ? -25.910 27.880  89.796  1.00 24.80  ? 85   MET C N   1 
ATOM   9039  C  CA  . MET C  1 85  ? -26.466 26.923  90.742  1.00 23.37  ? 85   MET C CA  1 
ATOM   9040  C  C   . MET C  1 85  ? -25.573 25.689  90.862  1.00 22.22  ? 85   MET C C   1 
ATOM   9041  O  O   . MET C  1 85  ? -25.513 25.058  91.911  1.00 21.97  ? 85   MET C O   1 
ATOM   9042  C  CB  . MET C  1 85  ? -27.926 26.559  90.388  1.00 19.70  ? 85   MET C CB  1 
ATOM   9043  C  CG  . MET C  1 85  ? -28.136 25.341  89.488  1.00 18.15  ? 85   MET C CG  1 
ATOM   9044  S  SD  . MET C  1 85  ? -29.834 25.146  88.871  1.00 44.32  ? 85   MET C SD  1 
ATOM   9045  C  CE  . MET C  1 85  ? -30.819 24.894  90.356  1.00 30.76  ? 85   MET C CE  1 
ATOM   9046  N  N   . TRP C  1 86  ? -24.860 25.368  89.792  1.00 22.73  ? 86   TRP C N   1 
ATOM   9047  C  CA  . TRP C  1 86  ? -24.051 24.159  89.753  1.00 25.76  ? 86   TRP C CA  1 
ATOM   9048  C  C   . TRP C  1 86  ? -22.590 24.366  90.200  1.00 30.84  ? 86   TRP C C   1 
ATOM   9049  O  O   . TRP C  1 86  ? -21.848 23.401  90.402  1.00 31.14  ? 86   TRP C O   1 
ATOM   9050  C  CB  . TRP C  1 86  ? -24.098 23.568  88.345  1.00 24.20  ? 86   TRP C CB  1 
ATOM   9051  C  CG  . TRP C  1 86  ? -25.482 23.422  87.807  1.00 25.25  ? 86   TRP C CG  1 
ATOM   9052  C  CD1 . TRP C  1 86  ? -26.082 24.187  86.834  1.00 26.35  ? 86   TRP C CD1 1 
ATOM   9053  C  CD2 . TRP C  1 86  ? -26.452 22.452  88.208  1.00 26.69  ? 86   TRP C CD2 1 
ATOM   9054  N  NE1 . TRP C  1 86  ? -27.367 23.744  86.607  1.00 27.69  ? 86   TRP C NE1 1 
ATOM   9055  C  CE2 . TRP C  1 86  ? -27.618 22.675  87.440  1.00 28.87  ? 86   TRP C CE2 1 
ATOM   9056  C  CE3 . TRP C  1 86  ? -26.449 21.401  89.132  1.00 24.67  ? 86   TRP C CE3 1 
ATOM   9057  C  CZ2 . TRP C  1 86  ? -28.771 21.886  87.576  1.00 27.47  ? 86   TRP C CZ2 1 
ATOM   9058  C  CZ3 . TRP C  1 86  ? -27.599 20.625  89.266  1.00 23.83  ? 86   TRP C CZ3 1 
ATOM   9059  C  CH2 . TRP C  1 86  ? -28.739 20.871  88.493  1.00 23.03  ? 86   TRP C CH2 1 
ATOM   9060  N  N   . ASN C  1 87  ? -22.179 25.618  90.360  1.00 37.87  ? 87   ASN C N   1 
ATOM   9061  C  CA  . ASN C  1 87  ? -20.800 25.912  90.730  1.00 40.28  ? 87   ASN C CA  1 
ATOM   9062  C  C   . ASN C  1 87  ? -20.516 25.527  92.177  1.00 38.01  ? 87   ASN C C   1 
ATOM   9063  O  O   . ASN C  1 87  ? -21.447 25.472  92.987  1.00 40.31  ? 87   ASN C O   1 
ATOM   9064  C  CB  . ASN C  1 87  ? -20.486 27.395  90.501  1.00 50.96  ? 87   ASN C CB  1 
ATOM   9065  C  CG  . ASN C  1 87  ? -20.007 27.681  89.093  1.00 57.47  ? 87   ASN C CG  1 
ATOM   9066  O  OD1 . ASN C  1 87  ? -18.910 27.273  88.696  1.00 59.78  ? 87   ASN C OD1 1 
ATOM   9067  N  ND2 . ASN C  1 87  ? -20.819 28.401  88.334  1.00 60.12  ? 87   ASN C ND2 1 
ATOM   9068  N  N   . PRO C  1 88  ? -19.233 25.250  92.503  1.00 26.58  ? 88   PRO C N   1 
ATOM   9069  C  CA  . PRO C  1 88  ? -18.799 24.881  93.858  1.00 23.34  ? 88   PRO C CA  1 
ATOM   9070  C  C   . PRO C  1 88  ? -19.160 25.923  94.889  1.00 26.51  ? 88   PRO C C   1 
ATOM   9071  O  O   . PRO C  1 88  ? -18.872 27.091  94.669  1.00 27.38  ? 88   PRO C O   1 
ATOM   9072  C  CB  . PRO C  1 88  ? -17.284 24.812  93.721  1.00 16.66  ? 88   PRO C CB  1 
ATOM   9073  C  CG  . PRO C  1 88  ? -17.086 24.351  92.325  1.00 16.90  ? 88   PRO C CG  1 
ATOM   9074  C  CD  . PRO C  1 88  ? -18.140 25.079  91.529  1.00 19.39  ? 88   PRO C CD  1 
ATOM   9075  N  N   . ASN C  1 89  ? -19.820 25.493  95.965  1.00 37.79  ? 89   ASN C N   1 
ATOM   9076  C  CA  . ASN C  1 89  ? -20.227 26.354  97.080  1.00 41.68  ? 89   ASN C CA  1 
ATOM   9077  C  C   . ASN C  1 89  ? -19.359 26.286  98.331  1.00 40.51  ? 89   ASN C C   1 
ATOM   9078  O  O   . ASN C  1 89  ? -19.705 26.850  99.353  1.00 40.43  ? 89   ASN C O   1 
ATOM   9079  C  CB  . ASN C  1 89  ? -21.681 26.098  97.454  1.00 44.88  ? 89   ASN C CB  1 
ATOM   9080  C  CG  . ASN C  1 89  ? -21.895 24.725  98.038  1.00 43.62  ? 89   ASN C CG  1 
ATOM   9081  O  OD1 . ASN C  1 89  ? -21.007 23.870  98.002  1.00 40.99  ? 89   ASN C OD1 1 
ATOM   9082  N  ND2 . ASN C  1 89  ? -23.088 24.499  98.577  1.00 45.12  ? 89   ASN C ND2 1 
ATOM   9083  N  N   . ARG C  1 90  ? -18.281 25.528  98.282  1.00 44.68  ? 90   ARG C N   1 
ATOM   9084  C  CA  . ARG C  1 90  ? -17.319 25.557  99.367  1.00 45.91  ? 90   ARG C CA  1 
ATOM   9085  C  C   . ARG C  1 90  ? -15.929 25.770  98.788  1.00 51.40  ? 90   ARG C C   1 
ATOM   9086  O  O   . ARG C  1 90  ? -15.784 25.988  97.579  1.00 56.37  ? 90   ARG C O   1 
ATOM   9087  C  CB  . ARG C  1 90  ? -17.385 24.274  100.169 1.00 30.31  ? 90   ARG C CB  1 
ATOM   9088  C  CG  . ARG C  1 90  ? -18.658 24.132  100.944 1.00 30.47  ? 90   ARG C CG  1 
ATOM   9089  C  CD  . ARG C  1 90  ? -18.463 24.592  102.380 1.00 36.12  ? 90   ARG C CD  1 
ATOM   9090  N  NE  . ARG C  1 90  ? -19.676 24.421  103.171 1.00 39.09  ? 90   ARG C NE  1 
ATOM   9091  C  CZ  . ARG C  1 90  ? -20.784 25.134  102.993 1.00 40.94  ? 90   ARG C CZ  1 
ATOM   9092  N  NH1 . ARG C  1 90  ? -20.836 26.068  102.053 1.00 39.09  ? 90   ARG C NH1 1 
ATOM   9093  N  NH2 . ARG C  1 90  ? -21.848 24.913  103.753 1.00 44.95  ? 90   ARG C NH2 1 
ATOM   9094  N  N   . GLU C  1 91  ? -14.908 25.726  99.638  1.00 29.27  ? 91   GLU C N   1 
ATOM   9095  C  CA  . GLU C  1 91  ? -13.558 25.977  99.165  1.00 27.64  ? 91   GLU C CA  1 
ATOM   9096  C  C   . GLU C  1 91  ? -13.001 24.741  98.442  1.00 18.47  ? 91   GLU C C   1 
ATOM   9097  O  O   . GLU C  1 91  ? -13.329 23.615  98.799  1.00 17.22  ? 91   GLU C O   1 
ATOM   9098  C  CB  . GLU C  1 91  ? -12.669 26.438  100.316 1.00 60.86  ? 91   GLU C CB  1 
ATOM   9099  C  CG  . GLU C  1 91  ? -11.869 25.351  100.971 1.00 71.96  ? 91   GLU C CG  1 
ATOM   9100  C  CD  . GLU C  1 91  ? -10.554 25.874  101.503 1.00 80.23  ? 91   GLU C CD  1 
ATOM   9101  O  OE1 . GLU C  1 91  ? -10.541 27.023  101.993 1.00 83.04  ? 91   GLU C OE1 1 
ATOM   9102  O  OE2 . GLU C  1 91  ? -9.538  25.147  101.422 1.00 81.68  ? 91   GLU C OE2 1 
ATOM   9103  N  N   . LEU C  1 92  ? -12.190 24.939  97.405  1.00 21.75  ? 92   LEU C N   1 
ATOM   9104  C  CA  . LEU C  1 92  ? -11.683 23.804  96.635  1.00 19.85  ? 92   LEU C CA  1 
ATOM   9105  C  C   . LEU C  1 92  ? -10.424 23.239  97.226  1.00 19.68  ? 92   LEU C C   1 
ATOM   9106  O  O   . LEU C  1 92  ? -9.492  23.985  97.524  1.00 21.53  ? 92   LEU C O   1 
ATOM   9107  C  CB  . LEU C  1 92  ? -11.336 24.228  95.228  1.00 16.91  ? 92   LEU C CB  1 
ATOM   9108  C  CG  . LEU C  1 92  ? -12.430 24.828  94.376  1.00 16.81  ? 92   LEU C CG  1 
ATOM   9109  C  CD1 . LEU C  1 92  ? -11.931 24.809  92.944  1.00 16.64  ? 92   LEU C CD1 1 
ATOM   9110  C  CD2 . LEU C  1 92  ? -13.713 24.048  94.533  1.00 16.27  ? 92   LEU C CD2 1 
ATOM   9111  N  N   . SER C  1 93  ? -10.371 21.922  97.372  1.00 27.50  ? 93   SER C N   1 
ATOM   9112  C  CA  . SER C  1 93  ? -9.121  21.289  97.760  1.00 29.76  ? 93   SER C CA  1 
ATOM   9113  C  C   . SER C  1 93  ? -8.967  19.925  97.143  1.00 29.37  ? 93   SER C C   1 
ATOM   9114  O  O   . SER C  1 93  ? -9.958  19.294  96.779  1.00 30.30  ? 93   SER C O   1 
ATOM   9115  C  CB  . SER C  1 93  ? -9.009  21.149  99.267  1.00 28.54  ? 93   SER C CB  1 
ATOM   9116  O  OG  . SER C  1 93  ? -7.643  21.152  99.620  1.00 28.08  ? 93   SER C OG  1 
ATOM   9117  N  N   . GLU C  1 94  ? -7.724  19.463  97.026  1.00 23.49  ? 94   GLU C N   1 
ATOM   9118  C  CA  . GLU C  1 94  ? -7.506  18.100  96.600  1.00 16.03  ? 94   GLU C CA  1 
ATOM   9119  C  C   . GLU C  1 94  ? -7.913  17.219  97.751  1.00 16.00  ? 94   GLU C C   1 
ATOM   9120  O  O   . GLU C  1 94  ? -8.175  16.044  97.546  1.00 15.60  ? 94   GLU C O   1 
ATOM   9121  C  CB  . GLU C  1 94  ? -6.065  17.837  96.194  1.00 16.38  ? 94   GLU C CB  1 
ATOM   9122  C  CG  . GLU C  1 94  ? -5.844  17.924  94.706  1.00 16.14  ? 94   GLU C CG  1 
ATOM   9123  C  CD  . GLU C  1 94  ? -4.370  17.928  94.305  1.00 20.17  ? 94   GLU C CD  1 
ATOM   9124  O  OE1 . GLU C  1 94  ? -3.557  18.623  94.956  1.00 19.02  ? 94   GLU C OE1 1 
ATOM   9125  O  OE2 . GLU C  1 94  ? -4.029  17.257  93.307  1.00 21.85  ? 94   GLU C OE2 1 
ATOM   9126  N  N   . ASP C  1 95  ? -8.061  17.797  98.946  1.00 16.47  ? 95   ASP C N   1 
ATOM   9127  C  CA  . ASP C  1 95  ? -8.460  16.980  100.078 1.00 20.99  ? 95   ASP C CA  1 
ATOM   9128  C  C   . ASP C  1 95  ? -9.961  17.147  100.136 1.00 22.80  ? 95   ASP C C   1 
ATOM   9129  O  O   . ASP C  1 95  ? -10.472 18.001  100.867 1.00 16.52  ? 95   ASP C O   1 
ATOM   9130  C  CB  . ASP C  1 95  ? -7.839  17.623  101.328 1.00 19.33  ? 95   ASP C CB  1 
ATOM   9131  C  CG  . ASP C  1 95  ? -8.187  16.902  102.628 1.00 19.71  ? 95   ASP C CG  1 
ATOM   9132  O  OD1 . ASP C  1 95  ? -9.211  16.195  102.688 1.00 20.40  ? 95   ASP C OD1 1 
ATOM   9133  O  OD2 . ASP C  1 95  ? -7.426  17.063  103.608 1.00 19.28  ? 95   ASP C OD2 1 
ATOM   9134  N  N   . CYS C  1 96  ? -10.651 16.288  99.374  1.00 15.54  ? 96   CYS C N   1 
ATOM   9135  C  CA  . CYS C  1 96  ? -12.116 16.325  99.237  1.00 15.19  ? 96   CYS C CA  1 
ATOM   9136  C  C   . CYS C  1 96  ? -13.001 15.168  99.675  1.00 14.99  ? 96   CYS C C   1 
ATOM   9137  O  O   . CYS C  1 96  ? -14.222 15.282  99.619  1.00 14.83  ? 96   CYS C O   1 
ATOM   9138  C  CB  . CYS C  1 96  ? -12.515 16.740  97.825  1.00 16.85  ? 96   CYS C CB  1 
ATOM   9139  S  SG  . CYS C  1 96  ? -11.592 15.938  96.505  1.00 35.62  ? 96   CYS C SG  1 
ATOM   9140  N  N   . LEU C  1 97  ? -12.434 14.045  100.074 1.00 20.45  ? 97   LEU C N   1 
ATOM   9141  C  CA  . LEU C  1 97  ? -13.285 12.871  100.096 1.00 19.99  ? 97   LEU C CA  1 
ATOM   9142  C  C   . LEU C  1 97  ? -13.932 12.786  101.463 1.00 20.57  ? 97   LEU C C   1 
ATOM   9143  O  O   . LEU C  1 97  ? -13.310 12.329  102.423 1.00 21.39  ? 97   LEU C O   1 
ATOM   9144  C  CB  . LEU C  1 97  ? -12.459 11.604  99.790  1.00 14.79  ? 97   LEU C CB  1 
ATOM   9145  C  CG  . LEU C  1 97  ? -11.746 11.561  98.421  1.00 14.45  ? 97   LEU C CG  1 
ATOM   9146  C  CD1 . LEU C  1 97  ? -10.797 10.378  98.221  1.00 14.58  ? 97   LEU C CD1 1 
ATOM   9147  C  CD2 . LEU C  1 97  ? -12.785 11.549  97.343  1.00 25.05  ? 97   LEU C CD2 1 
ATOM   9148  N  N   . TYR C  1 98  ? -15.210 13.176  101.506 1.00 15.19  ? 98   TYR C N   1 
ATOM   9149  C  CA  . TYR C  1 98  ? -16.033 13.229  102.719 1.00 15.65  ? 98   TYR C CA  1 
ATOM   9150  C  C   . TYR C  1 98  ? -17.426 12.966  102.254 1.00 20.36  ? 98   TYR C C   1 
ATOM   9151  O  O   . TYR C  1 98  ? -17.754 13.309  101.120 1.00 22.58  ? 98   TYR C O   1 
ATOM   9152  C  CB  . TYR C  1 98  ? -16.015 14.611  103.369 1.00 16.08  ? 98   TYR C CB  1 
ATOM   9153  C  CG  . TYR C  1 98  ? -14.628 15.068  103.753 1.00 20.81  ? 98   TYR C CG  1 
ATOM   9154  C  CD1 . TYR C  1 98  ? -13.823 15.724  102.844 1.00 16.21  ? 98   TYR C CD1 1 
ATOM   9155  C  CD2 . TYR C  1 98  ? -14.117 14.820  105.009 1.00 17.05  ? 98   TYR C CD2 1 
ATOM   9156  C  CE1 . TYR C  1 98  ? -12.574 16.126  103.174 1.00 16.62  ? 98   TYR C CE1 1 
ATOM   9157  C  CE2 . TYR C  1 98  ? -12.868 15.213  105.344 1.00 17.45  ? 98   TYR C CE2 1 
ATOM   9158  C  CZ  . TYR C  1 98  ? -12.095 15.868  104.426 1.00 17.24  ? 98   TYR C CZ  1 
ATOM   9159  O  OH  . TYR C  1 98  ? -10.813 16.276  104.756 1.00 17.75  ? 98   TYR C OH  1 
ATOM   9160  N  N   . LEU C  1 99  ? -18.254 12.353  103.095 1.00 16.76  ? 99   LEU C N   1 
ATOM   9161  C  CA  . LEU C  1 99  ? -19.645 12.143  102.704 1.00 15.63  ? 99   LEU C CA  1 
ATOM   9162  C  C   . LEU C  1 99  ? -20.622 12.789  103.680 1.00 16.18  ? 99   LEU C C   1 
ATOM   9163  O  O   . LEU C  1 99  ? -20.218 13.399  104.670 1.00 16.65  ? 99   LEU C O   1 
ATOM   9164  C  CB  . LEU C  1 99  ? -19.940 10.666  102.462 1.00 15.53  ? 99   LEU C CB  1 
ATOM   9165  C  CG  . LEU C  1 99  ? -19.374 9.695   103.483 1.00 15.96  ? 99   LEU C CG  1 
ATOM   9166  C  CD1 . LEU C  1 99  ? -20.339 9.594   104.614 1.00 16.58  ? 99   LEU C CD1 1 
ATOM   9167  C  CD2 . LEU C  1 99  ? -19.120 8.328   102.883 1.00 15.78  ? 99   LEU C CD2 1 
ATOM   9168  N  N   . ASN C  1 100 ? -21.909 12.669  103.388 1.00 24.04  ? 100  ASN C N   1 
ATOM   9169  C  CA  . ASN C  1 100 ? -22.943 13.360  104.144 1.00 23.36  ? 100  ASN C CA  1 
ATOM   9170  C  C   . ASN C  1 100 ? -24.127 12.441  104.415 1.00 24.10  ? 100  ASN C C   1 
ATOM   9171  O  O   . ASN C  1 100 ? -24.523 11.687  103.543 1.00 23.95  ? 100  ASN C O   1 
ATOM   9172  C  CB  . ASN C  1 100 ? -23.388 14.584  103.355 1.00 18.81  ? 100  ASN C CB  1 
ATOM   9173  C  CG  . ASN C  1 100 ? -22.239 15.486  103.017 1.00 18.37  ? 100  ASN C CG  1 
ATOM   9174  O  OD1 . ASN C  1 100 ? -21.527 15.954  103.898 1.00 16.76  ? 100  ASN C OD1 1 
ATOM   9175  N  ND2 . ASN C  1 100 ? -22.026 15.709  101.737 1.00 15.87  ? 100  ASN C ND2 1 
ATOM   9176  N  N   . VAL C  1 101 ? -24.673 12.478  105.623 1.00 17.83  ? 101  VAL C N   1 
ATOM   9177  C  CA  . VAL C  1 101 ? -25.811 11.641  105.957 1.00 20.51  ? 101  VAL C CA  1 
ATOM   9178  C  C   . VAL C  1 101 ? -26.966 12.437  106.586 1.00 19.72  ? 101  VAL C C   1 
ATOM   9179  O  O   . VAL C  1 101 ? -26.815 13.038  107.652 1.00 19.54  ? 101  VAL C O   1 
ATOM   9180  C  CB  . VAL C  1 101 ? -25.425 10.506  106.920 1.00 18.69  ? 101  VAL C CB  1 
ATOM   9181  C  CG1 . VAL C  1 101 ? -26.488 9.438   106.885 1.00 19.04  ? 101  VAL C CG1 1 
ATOM   9182  C  CG2 . VAL C  1 101 ? -24.094 9.914   106.554 1.00 18.18  ? 101  VAL C CG2 1 
ATOM   9183  N  N   . TRP C  1 102 ? -28.124 12.446  105.932 1.00 19.06  ? 102  TRP C N   1 
ATOM   9184  C  CA  . TRP C  1 102 ? -29.319 12.982  106.566 1.00 19.88  ? 102  TRP C CA  1 
ATOM   9185  C  C   . TRP C  1 102 ? -30.132 11.794  107.053 1.00 20.45  ? 102  TRP C C   1 
ATOM   9186  O  O   . TRP C  1 102 ? -30.196 10.770  106.382 1.00 20.13  ? 102  TRP C O   1 
ATOM   9187  C  CB  . TRP C  1 102 ? -30.140 13.824  105.590 1.00 22.21  ? 102  TRP C CB  1 
ATOM   9188  C  CG  . TRP C  1 102 ? -29.499 15.121  105.181 1.00 24.32  ? 102  TRP C CG  1 
ATOM   9189  C  CD1 . TRP C  1 102 ? -29.724 16.361  105.717 1.00 24.29  ? 102  TRP C CD1 1 
ATOM   9190  C  CD2 . TRP C  1 102 ? -28.540 15.308  104.135 1.00 26.12  ? 102  TRP C CD2 1 
ATOM   9191  N  NE1 . TRP C  1 102 ? -28.963 17.307  105.070 1.00 23.47  ? 102  TRP C NE1 1 
ATOM   9192  C  CE2 . TRP C  1 102 ? -28.224 16.684  104.098 1.00 26.09  ? 102  TRP C CE2 1 
ATOM   9193  C  CE3 . TRP C  1 102 ? -27.911 14.448  103.233 1.00 25.27  ? 102  TRP C CE3 1 
ATOM   9194  C  CZ2 . TRP C  1 102 ? -27.300 17.210  103.190 1.00 25.68  ? 102  TRP C CZ2 1 
ATOM   9195  C  CZ3 . TRP C  1 102 ? -26.997 14.978  102.335 1.00 23.61  ? 102  TRP C CZ3 1 
ATOM   9196  C  CH2 . TRP C  1 102 ? -26.702 16.343  102.321 1.00 22.72  ? 102  TRP C CH2 1 
ATOM   9197  N  N   . THR C  1 103 ? -30.699 11.910  108.249 1.00 21.36  ? 103  THR C N   1 
ATOM   9198  C  CA  . THR C  1 103 ? -31.593 10.895  108.807 1.00 22.11  ? 103  THR C CA  1 
ATOM   9199  C  C   . THR C  1 103 ? -32.682 11.667  109.527 1.00 25.17  ? 103  THR C C   1 
ATOM   9200  O  O   . THR C  1 103 ? -32.495 12.843  109.837 1.00 23.20  ? 103  THR C O   1 
ATOM   9201  C  CB  . THR C  1 103 ? -30.901 9.981   109.852 1.00 24.84  ? 103  THR C CB  1 
ATOM   9202  O  OG1 . THR C  1 103 ? -30.629 10.735  111.034 1.00 26.35  ? 103  THR C OG1 1 
ATOM   9203  C  CG2 . THR C  1 103 ? -29.607 9.394   109.336 1.00 25.82  ? 103  THR C CG2 1 
ATOM   9204  N  N   . PRO C  1 104 ? -33.828 11.021  109.792 1.00 32.24  ? 104  PRO C N   1 
ATOM   9205  C  CA  . PRO C  1 104 ? -34.879 11.762  110.496 1.00 30.75  ? 104  PRO C CA  1 
ATOM   9206  C  C   . PRO C  1 104 ? -34.464 12.135  111.928 1.00 32.53  ? 104  PRO C C   1 
ATOM   9207  O  O   . PRO C  1 104 ? -33.498 11.583  112.451 1.00 30.40  ? 104  PRO C O   1 
ATOM   9208  C  CB  . PRO C  1 104 ? -36.048 10.776  110.498 1.00 31.25  ? 104  PRO C CB  1 
ATOM   9209  C  CG  . PRO C  1 104 ? -35.767 9.837   109.359 1.00 24.84  ? 104  PRO C CG  1 
ATOM   9210  C  CD  . PRO C  1 104 ? -34.292 9.701   109.328 1.00 23.93  ? 104  PRO C CD  1 
ATOM   9211  N  N   . TYR C  1 105 ? -35.154 13.102  112.529 1.00 50.71  ? 105  TYR C N   1 
ATOM   9212  C  CA  . TYR C  1 105 ? -34.944 13.448  113.934 1.00 51.80  ? 105  TYR C CA  1 
ATOM   9213  C  C   . TYR C  1 105 ? -36.211 13.133  114.690 1.00 60.88  ? 105  TYR C C   1 
ATOM   9214  O  O   . TYR C  1 105 ? -37.274 13.647  114.364 1.00 67.08  ? 105  TYR C O   1 
ATOM   9215  C  CB  . TYR C  1 105 ? -34.615 14.918  114.099 1.00 29.65  ? 105  TYR C CB  1 
ATOM   9216  C  CG  . TYR C  1 105 ? -34.097 15.303  115.460 1.00 30.01  ? 105  TYR C CG  1 
ATOM   9217  C  CD1 . TYR C  1 105 ? -34.963 15.627  116.488 1.00 34.22  ? 105  TYR C CD1 1 
ATOM   9218  C  CD2 . TYR C  1 105 ? -32.734 15.386  115.710 1.00 30.85  ? 105  TYR C CD2 1 
ATOM   9219  C  CE1 . TYR C  1 105 ? -34.486 16.008  117.747 1.00 36.43  ? 105  TYR C CE1 1 
ATOM   9220  C  CE2 . TYR C  1 105 ? -32.247 15.762  116.959 1.00 32.11  ? 105  TYR C CE2 1 
ATOM   9221  C  CZ  . TYR C  1 105 ? -33.128 16.069  117.971 1.00 34.59  ? 105  TYR C CZ  1 
ATOM   9222  O  OH  . TYR C  1 105 ? -32.653 16.437  119.208 1.00 35.36  ? 105  TYR C OH  1 
ATOM   9223  N  N   . PRO C  1 106 ? -36.115 12.259  115.686 1.00 56.17  ? 106  PRO C N   1 
ATOM   9224  C  CA  . PRO C  1 106 ? -34.894 11.564  116.075 1.00 56.05  ? 106  PRO C CA  1 
ATOM   9225  C  C   . PRO C  1 106 ? -34.614 10.430  115.104 1.00 56.76  ? 106  PRO C C   1 
ATOM   9226  O  O   . PRO C  1 106 ? -35.526 10.023  114.372 1.00 54.90  ? 106  PRO C O   1 
ATOM   9227  C  CB  . PRO C  1 106 ? -35.270 10.981  117.427 1.00 52.90  ? 106  PRO C CB  1 
ATOM   9228  C  CG  . PRO C  1 106 ? -36.706 10.634  117.250 1.00 53.72  ? 106  PRO C CG  1 
ATOM   9229  C  CD  . PRO C  1 106 ? -37.286 11.750  116.417 1.00 53.45  ? 106  PRO C CD  1 
ATOM   9230  N  N   . ARG C  1 107 ? -33.379 9.936   115.107 1.00 67.33  ? 107  ARG C N   1 
ATOM   9231  C  CA  . ARG C  1 107 ? -33.004 8.778   114.312 1.00 67.55  ? 107  ARG C CA  1 
ATOM   9232  C  C   . ARG C  1 107 ? -33.999 7.647   114.572 1.00 74.96  ? 107  ARG C C   1 
ATOM   9233  O  O   . ARG C  1 107 ? -34.474 7.489   115.696 1.00 80.87  ? 107  ARG C O   1 
ATOM   9234  C  CB  . ARG C  1 107 ? -31.587 8.342   114.685 1.00 40.47  ? 107  ARG C CB  1 
ATOM   9235  C  CG  . ARG C  1 107 ? -30.520 8.863   113.751 1.00 35.68  ? 107  ARG C CG  1 
ATOM   9236  C  CD  . ARG C  1 107 ? -29.507 9.824   114.396 1.00 34.49  ? 107  ARG C CD  1 
ATOM   9237  N  NE  . ARG C  1 107 ? -28.842 9.380   115.635 1.00 38.45  ? 107  ARG C NE  1 
ATOM   9238  C  CZ  . ARG C  1 107 ? -28.411 8.147   115.949 1.00 39.77  ? 107  ARG C CZ  1 
ATOM   9239  N  NH1 . ARG C  1 107 ? -28.551 7.116   115.118 1.00 39.63  ? 107  ARG C NH1 1 
ATOM   9240  N  NH2 . ARG C  1 107 ? -27.825 7.945   117.137 1.00 39.36  ? 107  ARG C NH2 1 
ATOM   9241  N  N   . PRO C  1 108 ? -34.340 6.869   113.531 1.00 62.14  ? 108  PRO C N   1 
ATOM   9242  C  CA  . PRO C  1 108 ? -35.368 5.832   113.703 1.00 59.89  ? 108  PRO C CA  1 
ATOM   9243  C  C   . PRO C  1 108 ? -34.856 4.625   114.495 1.00 56.48  ? 108  PRO C C   1 
ATOM   9244  O  O   . PRO C  1 108 ? -33.647 4.453   114.654 1.00 59.62  ? 108  PRO C O   1 
ATOM   9245  C  CB  . PRO C  1 108 ? -35.670 5.413   112.261 1.00 64.30  ? 108  PRO C CB  1 
ATOM   9246  C  CG  . PRO C  1 108 ? -34.363 5.634   111.529 1.00 63.33  ? 108  PRO C CG  1 
ATOM   9247  C  CD  . PRO C  1 108 ? -33.749 6.860   112.174 1.00 63.34  ? 108  PRO C CD  1 
ATOM   9248  N  N   . ALA C  1 109 ? -35.766 3.809   115.014 1.00 41.67  ? 109  ALA C N   1 
ATOM   9249  C  CA  . ALA C  1 109 ? -35.398 2.463   115.444 1.00 40.22  ? 109  ALA C CA  1 
ATOM   9250  C  C   . ALA C  1 109 ? -36.117 1.544   114.485 1.00 44.85  ? 109  ALA C C   1 
ATOM   9251  O  O   . ALA C  1 109 ? -37.196 1.886   113.992 1.00 47.32  ? 109  ALA C O   1 
ATOM   9252  C  CB  . ALA C  1 109 ? -35.818 2.196   116.852 1.00 46.19  ? 109  ALA C CB  1 
ATOM   9253  N  N   . SER C  1 110 ? -35.507 0.390   114.233 1.00 61.04  ? 110  SER C N   1 
ATOM   9254  C  CA  . SER C  1 110 ? -35.728 -0.449  113.040 1.00 62.52  ? 110  SER C CA  1 
ATOM   9255  C  C   . SER C  1 110 ? -35.165 0.237   111.784 1.00 57.22  ? 110  SER C C   1 
ATOM   9256  O  O   . SER C  1 110 ? -35.353 1.441   111.573 1.00 57.16  ? 110  SER C O   1 
ATOM   9257  C  CB  . SER C  1 110 ? -37.211 -0.776  112.832 1.00 60.14  ? 110  SER C CB  1 
ATOM   9258  O  OG  . SER C  1 110 ? -37.907 0.370   112.363 1.00 59.50  ? 110  SER C OG  1 
ATOM   9259  N  N   . PRO C  1 111 ? -34.547 -0.558  110.902 1.00 40.22  ? 111  PRO C N   1 
ATOM   9260  C  CA  . PRO C  1 111 ? -33.673 0.080   109.927 1.00 39.07  ? 111  PRO C CA  1 
ATOM   9261  C  C   . PRO C  1 111 ? -34.424 0.705   108.781 1.00 41.93  ? 111  PRO C C   1 
ATOM   9262  O  O   . PRO C  1 111 ? -35.353 0.097   108.244 1.00 43.92  ? 111  PRO C O   1 
ATOM   9263  C  CB  . PRO C  1 111 ? -32.795 -1.073  109.445 1.00 38.11  ? 111  PRO C CB  1 
ATOM   9264  C  CG  . PRO C  1 111 ? -32.913 -2.106  110.504 1.00 38.14  ? 111  PRO C CG  1 
ATOM   9265  C  CD  . PRO C  1 111 ? -34.343 -2.006  110.918 1.00 39.17  ? 111  PRO C CD  1 
ATOM   9266  N  N   . THR C  1 112 ? -33.987 1.903   108.407 1.00 38.84  ? 112  THR C N   1 
ATOM   9267  C  CA  . THR C  1 112 ? -34.565 2.656   107.309 1.00 37.32  ? 112  THR C CA  1 
ATOM   9268  C  C   . THR C  1 112 ? -33.730 2.372   106.066 1.00 31.58  ? 112  THR C C   1 
ATOM   9269  O  O   . THR C  1 112 ? -32.507 2.267   106.173 1.00 26.05  ? 112  THR C O   1 
ATOM   9270  C  CB  . THR C  1 112 ? -34.611 4.163   107.663 1.00 50.84  ? 112  THR C CB  1 
ATOM   9271  O  OG1 . THR C  1 112 ? -35.661 4.405   108.613 1.00 53.23  ? 112  THR C OG1 1 
ATOM   9272  C  CG2 . THR C  1 112 ? -34.854 5.008   106.442 1.00 52.26  ? 112  THR C CG2 1 
ATOM   9273  N  N   . PRO C  1 113 ? -34.386 2.207   104.895 1.00 47.23  ? 113  PRO C N   1 
ATOM   9274  C  CA  . PRO C  1 113 ? -33.655 1.963   103.653 1.00 44.41  ? 113  PRO C CA  1 
ATOM   9275  C  C   . PRO C  1 113 ? -32.929 3.225   103.212 1.00 42.24  ? 113  PRO C C   1 
ATOM   9276  O  O   . PRO C  1 113 ? -33.432 4.346   103.356 1.00 41.75  ? 113  PRO C O   1 
ATOM   9277  C  CB  . PRO C  1 113 ? -34.764 1.603   102.662 1.00 22.51  ? 113  PRO C CB  1 
ATOM   9278  C  CG  . PRO C  1 113 ? -35.897 2.394   103.124 1.00 23.17  ? 113  PRO C CG  1 
ATOM   9279  C  CD  . PRO C  1 113 ? -35.832 2.303   104.633 1.00 24.25  ? 113  PRO C CD  1 
ATOM   9280  N  N   . VAL C  1 114 ? -31.742 3.014   102.663 1.00 31.25  ? 114  VAL C N   1 
ATOM   9281  C  CA  . VAL C  1 114 ? -30.811 4.078   102.378 1.00 27.39  ? 114  VAL C CA  1 
ATOM   9282  C  C   . VAL C  1 114 ? -30.821 4.466   100.903 1.00 27.94  ? 114  VAL C C   1 
ATOM   9283  O  O   . VAL C  1 114 ? -30.896 3.611   100.023 1.00 28.64  ? 114  VAL C O   1 
ATOM   9284  C  CB  . VAL C  1 114 ? -29.409 3.649   102.781 1.00 19.12  ? 114  VAL C CB  1 
ATOM   9285  C  CG1 . VAL C  1 114 ? -28.445 4.781   102.588 1.00 18.36  ? 114  VAL C CG1 1 
ATOM   9286  C  CG2 . VAL C  1 114 ? -29.409 3.215   104.219 1.00 19.89  ? 114  VAL C CG2 1 
ATOM   9287  N  N   . LEU C  1 115 ? -30.760 5.771   100.663 1.00 24.03  ? 115  LEU C N   1 
ATOM   9288  C  CA  . LEU C  1 115 ? -30.626 6.346   99.343  1.00 22.50  ? 115  LEU C CA  1 
ATOM   9289  C  C   . LEU C  1 115 ? -29.257 7.026   99.200  1.00 23.49  ? 115  LEU C C   1 
ATOM   9290  O  O   . LEU C  1 115 ? -28.997 8.027   99.860  1.00 24.57  ? 115  LEU C O   1 
ATOM   9291  C  CB  . LEU C  1 115 ? -31.722 7.385   99.147  1.00 18.09  ? 115  LEU C CB  1 
ATOM   9292  C  CG  . LEU C  1 115 ? -32.975 6.852   98.493  1.00 32.85  ? 115  LEU C CG  1 
ATOM   9293  C  CD1 . LEU C  1 115 ? -33.982 7.959   98.223  1.00 18.99  ? 115  LEU C CD1 1 
ATOM   9294  C  CD2 . LEU C  1 115 ? -32.515 6.234   97.218  1.00 18.12  ? 115  LEU C CD2 1 
ATOM   9295  N  N   . ILE C  1 116 ? -28.389 6.500   98.340  1.00 16.45  ? 116  ILE C N   1 
ATOM   9296  C  CA  . ILE C  1 116 ? -27.131 7.171   98.039  1.00 15.79  ? 116  ILE C CA  1 
ATOM   9297  C  C   . ILE C  1 116 ? -27.180 8.006   96.748  1.00 34.40  ? 116  ILE C C   1 
ATOM   9298  O  O   . ILE C  1 116 ? -27.503 7.501   95.673  1.00 15.26  ? 116  ILE C O   1 
ATOM   9299  C  CB  . ILE C  1 116 ? -26.008 6.169   97.941  1.00 15.54  ? 116  ILE C CB  1 
ATOM   9300  C  CG1 . ILE C  1 116 ? -25.931 5.378   99.226  1.00 16.07  ? 116  ILE C CG1 1 
ATOM   9301  C  CG2 . ILE C  1 116 ? -24.701 6.861   97.718  1.00 14.99  ? 116  ILE C CG2 1 
ATOM   9302  C  CD1 . ILE C  1 116 ? -24.797 4.411   99.246  1.00 15.96  ? 116  ILE C CD1 1 
ATOM   9303  N  N   . TRP C  1 117 ? -26.845 9.289   96.867  1.00 15.15  ? 117  TRP C N   1 
ATOM   9304  C  CA  . TRP C  1 117 ? -26.797 10.210  95.731  1.00 15.78  ? 117  TRP C CA  1 
ATOM   9305  C  C   . TRP C  1 117 ? -25.389 10.430  95.155  1.00 17.28  ? 117  TRP C C   1 
ATOM   9306  O  O   . TRP C  1 117 ? -24.468 10.827  95.871  1.00 17.97  ? 117  TRP C O   1 
ATOM   9307  C  CB  . TRP C  1 117 ? -27.353 11.566  96.140  1.00 15.10  ? 117  TRP C CB  1 
ATOM   9308  C  CG  . TRP C  1 117 ? -27.208 12.611  95.072  1.00 14.85  ? 117  TRP C CG  1 
ATOM   9309  C  CD1 . TRP C  1 117 ? -26.256 13.595  94.991  1.00 14.59  ? 117  TRP C CD1 1 
ATOM   9310  C  CD2 . TRP C  1 117 ? -28.048 12.773  93.928  1.00 14.95  ? 117  TRP C CD2 1 
ATOM   9311  N  NE1 . TRP C  1 117 ? -26.460 14.361  93.864  1.00 14.52  ? 117  TRP C NE1 1 
ATOM   9312  C  CE2 . TRP C  1 117 ? -27.554 13.874  93.197  1.00 14.74  ? 117  TRP C CE2 1 
ATOM   9313  C  CE3 . TRP C  1 117 ? -29.164 12.089  93.446  1.00 15.29  ? 117  TRP C CE3 1 
ATOM   9314  C  CZ2 . TRP C  1 117 ? -28.145 14.299  92.015  1.00 14.85  ? 117  TRP C CZ2 1 
ATOM   9315  C  CZ3 . TRP C  1 117 ? -29.738 12.507  92.271  1.00 15.70  ? 117  TRP C CZ3 1 
ATOM   9316  C  CH2 . TRP C  1 117 ? -29.233 13.601  91.569  1.00 15.17  ? 117  TRP C CH2 1 
ATOM   9317  N  N   . ILE C  1 118 ? -25.234 10.192  93.854  1.00 18.12  ? 118  ILE C N   1 
ATOM   9318  C  CA  . ILE C  1 118 ? -23.981 10.481  93.174  1.00 18.92  ? 118  ILE C CA  1 
ATOM   9319  C  C   . ILE C  1 118 ? -24.202 11.626  92.204  1.00 18.14  ? 118  ILE C C   1 
ATOM   9320  O  O   . ILE C  1 118 ? -24.901 11.455  91.212  1.00 13.46  ? 118  ILE C O   1 
ATOM   9321  C  CB  . ILE C  1 118 ? -23.468 9.269   92.370  1.00 18.06  ? 118  ILE C CB  1 
ATOM   9322  C  CG1 . ILE C  1 118 ? -23.591 7.987   93.181  1.00 19.31  ? 118  ILE C CG1 1 
ATOM   9323  C  CG2 . ILE C  1 118 ? -22.004 9.459   91.959  1.00 19.98  ? 118  ILE C CG2 1 
ATOM   9324  C  CD1 . ILE C  1 118 ? -22.928 6.797   92.507  1.00 20.58  ? 118  ILE C CD1 1 
ATOM   9325  N  N   . TYR C  1 119 ? -23.593 12.781  92.473  1.00 13.35  ? 119  TYR C N   1 
ATOM   9326  C  CA  . TYR C  1 119 ? -23.778 13.961  91.622  1.00 13.39  ? 119  TYR C CA  1 
ATOM   9327  C  C   . TYR C  1 119 ? -23.186 13.853  90.232  1.00 13.10  ? 119  TYR C C   1 
ATOM   9328  O  O   . TYR C  1 119 ? -22.326 13.015  89.968  1.00 12.82  ? 119  TYR C O   1 
ATOM   9329  C  CB  . TYR C  1 119 ? -23.238 15.232  92.279  1.00 20.08  ? 119  TYR C CB  1 
ATOM   9330  C  CG  . TYR C  1 119 ? -21.761 15.224  92.593  1.00 21.18  ? 119  TYR C CG  1 
ATOM   9331  C  CD1 . TYR C  1 119 ? -20.811 15.581  91.641  1.00 21.28  ? 119  TYR C CD1 1 
ATOM   9332  C  CD2 . TYR C  1 119 ? -21.320 14.903  93.861  1.00 23.74  ? 119  TYR C CD2 1 
ATOM   9333  C  CE1 . TYR C  1 119 ? -19.451 15.584  91.944  1.00 21.78  ? 119  TYR C CE1 1 
ATOM   9334  C  CE2 . TYR C  1 119 ? -19.974 14.915  94.178  1.00 25.95  ? 119  TYR C CE2 1 
ATOM   9335  C  CZ  . TYR C  1 119 ? -19.043 15.252  93.224  1.00 24.15  ? 119  TYR C CZ  1 
ATOM   9336  O  OH  . TYR C  1 119 ? -17.715 15.235  93.589  1.00 22.99  ? 119  TYR C OH  1 
ATOM   9337  N  N   . GLY C  1 120 ? -23.675 14.724  89.354  1.00 13.27  ? 120  GLY C N   1 
ATOM   9338  C  CA  . GLY C  1 120 ? -23.159 14.878  88.003  1.00 13.12  ? 120  GLY C CA  1 
ATOM   9339  C  C   . GLY C  1 120 ? -22.182 16.033  87.899  1.00 13.12  ? 120  GLY C C   1 
ATOM   9340  O  O   . GLY C  1 120 ? -21.510 16.374  88.866  1.00 13.10  ? 120  GLY C O   1 
ATOM   9341  N  N   . GLY C  1 121 ? -22.152 16.698  86.753  1.00 22.71  ? 121  GLY C N   1 
ATOM   9342  C  CA  . GLY C  1 121 ? -21.091 17.654  86.488  1.00 23.50  ? 121  GLY C CA  1 
ATOM   9343  C  C   . GLY C  1 121 ? -20.075 17.228  85.450  1.00 22.24  ? 121  GLY C C   1 
ATOM   9344  O  O   . GLY C  1 121 ? -18.976 17.760  85.419  1.00 23.96  ? 121  GLY C O   1 
ATOM   9345  N  N   . GLY C  1 122 ? -20.427 16.235  84.637  1.00 17.55  ? 122  GLY C N   1 
ATOM   9346  C  CA  . GLY C  1 122 ? -19.641 15.865  83.472  1.00 12.91  ? 122  GLY C CA  1 
ATOM   9347  C  C   . GLY C  1 122 ? -18.319 15.180  83.756  1.00 20.71  ? 122  GLY C C   1 
ATOM   9348  O  O   . GLY C  1 122 ? -17.460 15.101  82.893  1.00 12.70  ? 122  GLY C O   1 
ATOM   9349  N  N   . PHE C  1 123 ? -18.162 14.685  84.975  1.00 14.97  ? 123  PHE C N   1 
ATOM   9350  C  CA  . PHE C  1 123 ? -16.894 14.130  85.447  1.00 23.34  ? 123  PHE C CA  1 
ATOM   9351  C  C   . PHE C  1 123 ? -15.792 15.189  85.593  1.00 24.16  ? 123  PHE C C   1 
ATOM   9352  O  O   . PHE C  1 123 ? -14.686 14.883  86.051  1.00 23.37  ? 123  PHE C O   1 
ATOM   9353  C  CB  . PHE C  1 123 ? -16.429 12.947  84.589  1.00 20.09  ? 123  PHE C CB  1 
ATOM   9354  C  CG  . PHE C  1 123 ? -17.324 11.737  84.686  1.00 12.17  ? 123  PHE C CG  1 
ATOM   9355  C  CD1 . PHE C  1 123 ? -17.471 11.055  85.874  1.00 24.68  ? 123  PHE C CD1 1 
ATOM   9356  C  CD2 . PHE C  1 123 ? -18.002 11.272  83.586  1.00 27.39  ? 123  PHE C CD2 1 
ATOM   9357  C  CE1 . PHE C  1 123 ? -18.284 9.948   85.949  1.00 12.12  ? 123  PHE C CE1 1 
ATOM   9358  C  CE2 . PHE C  1 123 ? -18.817 10.165  83.668  1.00 27.21  ? 123  PHE C CE2 1 
ATOM   9359  C  CZ  . PHE C  1 123 ? -18.955 9.510   84.840  1.00 12.22  ? 123  PHE C CZ  1 
ATOM   9360  N  N   . TYR C  1 124 ? -16.088 16.417  85.168  1.00 23.92  ? 124  TYR C N   1 
ATOM   9361  C  CA  . TYR C  1 124 ? -15.178 17.542  85.356  1.00 25.11  ? 124  TYR C CA  1 
ATOM   9362  C  C   . TYR C  1 124 ? -15.535 18.465  86.501  1.00 27.80  ? 124  TYR C C   1 
ATOM   9363  O  O   . TYR C  1 124 ? -14.866 19.470  86.667  1.00 31.16  ? 124  TYR C O   1 
ATOM   9364  C  CB  . TYR C  1 124 ? -15.021 18.376  84.070  1.00 20.81  ? 124  TYR C CB  1 
ATOM   9365  C  CG  . TYR C  1 124 ? -16.241 19.190  83.707  1.00 19.86  ? 124  TYR C CG  1 
ATOM   9366  C  CD1 . TYR C  1 124 ? -17.273 18.620  82.986  1.00 23.21  ? 124  TYR C CD1 1 
ATOM   9367  C  CD2 . TYR C  1 124 ? -16.358 20.521  84.084  1.00 19.08  ? 124  TYR C CD2 1 
ATOM   9368  C  CE1 . TYR C  1 124 ? -18.405 19.337  82.656  1.00 28.20  ? 124  TYR C CE1 1 
ATOM   9369  C  CE2 . TYR C  1 124 ? -17.478 21.259  83.753  1.00 24.33  ? 124  TYR C CE2 1 
ATOM   9370  C  CZ  . TYR C  1 124 ? -18.511 20.657  83.036  1.00 31.05  ? 124  TYR C CZ  1 
ATOM   9371  O  OH  . TYR C  1 124 ? -19.659 21.357  82.693  1.00 35.92  ? 124  TYR C OH  1 
ATOM   9372  N  N   . SER C  1 125 ? -16.594 18.178  87.252  1.00 13.13  ? 125  SER C N   1 
ATOM   9373  C  CA  . SER C  1 125 ? -17.042 19.120  88.289  1.00 16.62  ? 125  SER C CA  1 
ATOM   9374  C  C   . SER C  1 125 ? -18.118 18.579  89.233  1.00 17.52  ? 125  SER C C   1 
ATOM   9375  O  O   . SER C  1 125 ? -18.524 17.424  89.139  1.00 19.26  ? 125  SER C O   1 
ATOM   9376  C  CB  . SER C  1 125 ? -17.620 20.353  87.633  1.00 13.82  ? 125  SER C CB  1 
ATOM   9377  O  OG  . SER C  1 125 ? -18.904 20.030  87.144  1.00 13.76  ? 125  SER C OG  1 
ATOM   9378  N  N   . GLY C  1 126 ? -18.606 19.428  90.130  1.00 13.66  ? 126  GLY C N   1 
ATOM   9379  C  CA  . GLY C  1 126 ? -19.721 19.054  90.975  1.00 13.70  ? 126  GLY C CA  1 
ATOM   9380  C  C   . GLY C  1 126 ? -19.348 18.816  92.416  1.00 13.77  ? 126  GLY C C   1 
ATOM   9381  O  O   . GLY C  1 126 ? -18.187 18.676  92.734  1.00 25.49  ? 126  GLY C O   1 
ATOM   9382  N  N   . ALA C  1 127 ? -20.332 18.791  93.303  1.00 13.99  ? 127  ALA C N   1 
ATOM   9383  C  CA  . ALA C  1 127 ? -20.075 18.519  94.713  1.00 16.34  ? 127  ALA C CA  1 
ATOM   9384  C  C   . ALA C  1 127 ? -21.334 18.013  95.398  1.00 14.30  ? 127  ALA C C   1 
ATOM   9385  O  O   . ALA C  1 127 ? -22.434 18.302  94.955  1.00 16.04  ? 127  ALA C O   1 
ATOM   9386  C  CB  . ALA C  1 127 ? -19.584 19.763  95.398  1.00 14.61  ? 127  ALA C CB  1 
ATOM   9387  N  N   . ALA C  1 128 ? -21.186 17.283  96.498  1.00 17.64  ? 128  ALA C N   1 
ATOM   9388  C  CA  . ALA C  1 128 ? -22.356 16.776  97.192  1.00 17.87  ? 128  ALA C CA  1 
ATOM   9389  C  C   . ALA C  1 128 ? -22.969 17.908  97.988  1.00 19.54  ? 128  ALA C C   1 
ATOM   9390  O  O   . ALA C  1 128 ? -24.126 17.832  98.392  1.00 20.56  ? 128  ALA C O   1 
ATOM   9391  C  CB  . ALA C  1 128 ? -22.002 15.616  98.090  1.00 14.60  ? 128  ALA C CB  1 
ATOM   9392  N  N   . SER C  1 129 ? -22.208 18.983  98.170  1.00 15.41  ? 129  SER C N   1 
ATOM   9393  C  CA  . SER C  1 129 ? -22.631 20.080  99.038  1.00 17.23  ? 129  SER C CA  1 
ATOM   9394  C  C   . SER C  1 129 ? -23.472 21.164  98.354  1.00 16.40  ? 129  SER C C   1 
ATOM   9395  O  O   . SER C  1 129 ? -23.774 22.174  98.969  1.00 17.03  ? 129  SER C O   1 
ATOM   9396  C  CB  . SER C  1 129 ? -21.429 20.705  99.748  1.00 16.32  ? 129  SER C CB  1 
ATOM   9397  O  OG  . SER C  1 129 ? -20.446 21.095  98.815  1.00 16.04  ? 129  SER C OG  1 
ATOM   9398  N  N   . LEU C  1 130 ? -23.847 20.971  97.092  1.00 22.88  ? 130  LEU C N   1 
ATOM   9399  C  CA  . LEU C  1 130 ? -24.715 21.937  96.413  1.00 26.49  ? 130  LEU C CA  1 
ATOM   9400  C  C   . LEU C  1 130 ? -26.111 21.965  97.047  1.00 33.73  ? 130  LEU C C   1 
ATOM   9401  O  O   . LEU C  1 130 ? -26.511 21.030  97.745  1.00 36.55  ? 130  LEU C O   1 
ATOM   9402  C  CB  . LEU C  1 130 ? -24.824 21.641  94.917  1.00 19.78  ? 130  LEU C CB  1 
ATOM   9403  C  CG  . LEU C  1 130 ? -23.521 21.519  94.130  1.00 19.77  ? 130  LEU C CG  1 
ATOM   9404  C  CD1 . LEU C  1 130 ? -23.795 21.375  92.636  1.00 19.79  ? 130  LEU C CD1 1 
ATOM   9405  C  CD2 . LEU C  1 130 ? -22.624 22.703  94.398  1.00 22.18  ? 130  LEU C CD2 1 
ATOM   9406  N  N   . ASP C  1 131 ? -26.850 23.044  96.807  1.00 29.03  ? 131  ASP C N   1 
ATOM   9407  C  CA  . ASP C  1 131 ? -28.095 23.275  97.532  1.00 30.77  ? 131  ASP C CA  1 
ATOM   9408  C  C   . ASP C  1 131 ? -29.272 22.481  96.962  1.00 24.54  ? 131  ASP C C   1 
ATOM   9409  O  O   . ASP C  1 131 ? -30.316 22.348  97.595  1.00 23.46  ? 131  ASP C O   1 
ATOM   9410  C  CB  . ASP C  1 131 ? -28.431 24.779  97.590  1.00 51.07  ? 131  ASP C CB  1 
ATOM   9411  C  CG  . ASP C  1 131 ? -27.400 25.592  98.376  1.00 57.53  ? 131  ASP C CG  1 
ATOM   9412  O  OD1 . ASP C  1 131 ? -26.520 24.991  99.035  1.00 61.01  ? 131  ASP C OD1 1 
ATOM   9413  O  OD2 . ASP C  1 131 ? -27.482 26.838  98.347  1.00 57.51  ? 131  ASP C OD2 1 
ATOM   9414  N  N   . VAL C  1 132 ? -29.112 21.962  95.759  1.00 29.57  ? 132  VAL C N   1 
ATOM   9415  C  CA  . VAL C  1 132 ? -30.203 21.255  95.123  1.00 30.78  ? 132  VAL C CA  1 
ATOM   9416  C  C   . VAL C  1 132 ? -30.113 19.765  95.489  1.00 31.77  ? 132  VAL C C   1 
ATOM   9417  O  O   . VAL C  1 132 ? -31.008 18.984  95.201  1.00 37.33  ? 132  VAL C O   1 
ATOM   9418  C  CB  . VAL C  1 132 ? -30.144 21.484  93.603  1.00 28.14  ? 132  VAL C CB  1 
ATOM   9419  C  CG1 . VAL C  1 132 ? -29.037 20.646  92.998  1.00 26.51  ? 132  VAL C CG1 1 
ATOM   9420  C  CG2 . VAL C  1 132 ? -31.475 21.190  92.942  1.00 26.55  ? 132  VAL C CG2 1 
ATOM   9421  N  N   . TYR C  1 133 ? -29.010 19.378  96.114  1.00 21.44  ? 133  TYR C N   1 
ATOM   9422  C  CA  . TYR C  1 133 ? -28.809 18.020  96.615  1.00 19.25  ? 133  TYR C CA  1 
ATOM   9423  C  C   . TYR C  1 133 ? -29.099 17.847  98.114  1.00 21.44  ? 133  TYR C C   1 
ATOM   9424  O  O   . TYR C  1 133 ? -28.701 16.835  98.700  1.00 16.89  ? 133  TYR C O   1 
ATOM   9425  C  CB  . TYR C  1 133 ? -27.390 17.545  96.342  1.00 22.76  ? 133  TYR C CB  1 
ATOM   9426  C  CG  . TYR C  1 133 ? -26.922 17.644  94.909  1.00 23.27  ? 133  TYR C CG  1 
ATOM   9427  C  CD1 . TYR C  1 133 ? -27.791 17.438  93.852  1.00 24.50  ? 133  TYR C CD1 1 
ATOM   9428  C  CD2 . TYR C  1 133 ? -25.596 17.927  94.623  1.00 19.38  ? 133  TYR C CD2 1 
ATOM   9429  C  CE1 . TYR C  1 133 ? -27.345 17.525  92.551  1.00 23.22  ? 133  TYR C CE1 1 
ATOM   9430  C  CE2 . TYR C  1 133 ? -25.155 18.017  93.338  1.00 17.92  ? 133  TYR C CE2 1 
ATOM   9431  C  CZ  . TYR C  1 133 ? -26.025 17.817  92.306  1.00 19.40  ? 133  TYR C CZ  1 
ATOM   9432  O  OH  . TYR C  1 133 ? -25.568 17.913  91.018  1.00 14.53  ? 133  TYR C OH  1 
ATOM   9433  N  N   . ASP C  1 134 ? -29.671 18.872  98.750  1.00 21.39  ? 134  ASP C N   1 
ATOM   9434  C  CA  . ASP C  1 134 ? -29.986 18.843  100.192 1.00 22.78  ? 134  ASP C CA  1 
ATOM   9435  C  C   . ASP C  1 134 ? -30.892 17.683  100.606 1.00 20.87  ? 134  ASP C C   1 
ATOM   9436  O  O   . ASP C  1 134 ? -32.028 17.577  100.135 1.00 20.05  ? 134  ASP C O   1 
ATOM   9437  C  CB  . ASP C  1 134 ? -30.675 20.143  100.597 1.00 32.64  ? 134  ASP C CB  1 
ATOM   9438  C  CG  . ASP C  1 134 ? -30.605 20.412  102.091 1.00 40.32  ? 134  ASP C CG  1 
ATOM   9439  O  OD1 . ASP C  1 134 ? -30.564 19.459  102.906 1.00 40.52  ? 134  ASP C OD1 1 
ATOM   9440  O  OD2 . ASP C  1 134 ? -30.592 21.608  102.447 1.00 44.83  ? 134  ASP C OD2 1 
ATOM   9441  N  N   . GLY C  1 135 ? -30.413 16.860  101.540 1.00 22.50  ? 135  GLY C N   1 
ATOM   9442  C  CA  . GLY C  1 135 ? -31.127 15.661  101.942 1.00 23.59  ? 135  GLY C CA  1 
ATOM   9443  C  C   . GLY C  1 135 ? -32.312 15.907  102.866 1.00 28.76  ? 135  GLY C C   1 
ATOM   9444  O  O   . GLY C  1 135 ? -33.190 15.054  102.991 1.00 30.83  ? 135  GLY C O   1 
ATOM   9445  N  N   . ARG C  1 136 ? -32.358 17.080  103.493 1.00 26.36  ? 136  ARG C N   1 
ATOM   9446  C  CA  . ARG C  1 136 ? -33.275 17.317  104.603 1.00 21.40  ? 136  ARG C CA  1 
ATOM   9447  C  C   . ARG C  1 136 ? -34.739 17.041  104.296 1.00 22.05  ? 136  ARG C C   1 
ATOM   9448  O  O   . ARG C  1 136 ? -35.448 16.549  105.158 1.00 25.65  ? 136  ARG C O   1 
ATOM   9449  C  CB  . ARG C  1 136 ? -33.075 18.713  105.213 1.00 21.90  ? 136  ARG C CB  1 
ATOM   9450  C  CG  . ARG C  1 136 ? -33.952 19.811  104.661 1.00 25.48  ? 136  ARG C CG  1 
ATOM   9451  C  CD  . ARG C  1 136 ? -33.139 21.064  104.386 1.00 29.09  ? 136  ARG C CD  1 
ATOM   9452  N  NE  . ARG C  1 136 ? -32.898 21.912  105.559 1.00 34.98  ? 136  ARG C NE  1 
ATOM   9453  C  CZ  . ARG C  1 136 ? -31.691 22.339  105.955 1.00 38.40  ? 136  ARG C CZ  1 
ATOM   9454  N  NH1 . ARG C  1 136 ? -30.586 21.984  105.293 1.00 36.97  ? 136  ARG C NH1 1 
ATOM   9455  N  NH2 . ARG C  1 136 ? -31.582 23.121  107.032 1.00 40.52  ? 136  ARG C NH2 1 
ATOM   9456  N  N   . PHE C  1 137 ? -35.203 17.318  103.082 1.00 26.67  ? 137  PHE C N   1 
ATOM   9457  C  CA  . PHE C  1 137 ? -36.621 17.084  102.793 1.00 30.69  ? 137  PHE C CA  1 
ATOM   9458  C  C   . PHE C  1 137 ? -36.950 15.600  102.657 1.00 37.26  ? 137  PHE C C   1 
ATOM   9459  O  O   . PHE C  1 137 ? -37.987 15.134  103.134 1.00 38.59  ? 137  PHE C O   1 
ATOM   9460  C  CB  . PHE C  1 137 ? -37.085 17.857  101.562 1.00 26.22  ? 137  PHE C CB  1 
ATOM   9461  C  CG  . PHE C  1 137 ? -36.638 19.269  101.561 1.00 26.58  ? 137  PHE C CG  1 
ATOM   9462  C  CD1 . PHE C  1 137 ? -37.408 20.247  102.161 1.00 27.25  ? 137  PHE C CD1 1 
ATOM   9463  C  CD2 . PHE C  1 137 ? -35.421 19.622  100.987 1.00 25.74  ? 137  PHE C CD2 1 
ATOM   9464  C  CE1 . PHE C  1 137 ? -36.984 21.562  102.177 1.00 27.98  ? 137  PHE C CE1 1 
ATOM   9465  C  CE2 . PHE C  1 137 ? -34.988 20.935  100.996 1.00 25.61  ? 137  PHE C CE2 1 
ATOM   9466  C  CZ  . PHE C  1 137 ? -35.768 21.908  101.596 1.00 27.17  ? 137  PHE C CZ  1 
ATOM   9467  N  N   . LEU C  1 138 ? -36.070 14.856  102.000 1.00 36.73  ? 138  LEU C N   1 
ATOM   9468  C  CA  . LEU C  1 138 ? -36.291 13.432  101.845 1.00 34.34  ? 138  LEU C CA  1 
ATOM   9469  C  C   . LEU C  1 138 ? -36.159 12.780  103.209 1.00 34.10  ? 138  LEU C C   1 
ATOM   9470  O  O   . LEU C  1 138 ? -36.875 11.843  103.544 1.00 34.28  ? 138  LEU C O   1 
ATOM   9471  C  CB  . LEU C  1 138 ? -35.302 12.838  100.841 1.00 20.49  ? 138  LEU C CB  1 
ATOM   9472  C  CG  . LEU C  1 138 ? -35.638 13.047  99.362  1.00 20.22  ? 138  LEU C CG  1 
ATOM   9473  C  CD1 . LEU C  1 138 ? -34.558 12.402  98.545  1.00 19.26  ? 138  LEU C CD1 1 
ATOM   9474  C  CD2 . LEU C  1 138 ? -36.993 12.450  99.006  1.00 20.99  ? 138  LEU C CD2 1 
ATOM   9475  N  N   . ALA C  1 139 ? -35.251 13.309  104.011 1.00 30.89  ? 139  ALA C N   1 
ATOM   9476  C  CA  . ALA C  1 139 ? -35.050 12.768  105.334 1.00 28.29  ? 139  ALA C CA  1 
ATOM   9477  C  C   . ALA C  1 139 ? -36.284 13.012  106.166 1.00 27.57  ? 139  ALA C C   1 
ATOM   9478  O  O   . ALA C  1 139 ? -36.784 12.091  106.783 1.00 30.80  ? 139  ALA C O   1 
ATOM   9479  C  CB  . ALA C  1 139 ? -33.833 13.376  105.995 1.00 26.64  ? 139  ALA C CB  1 
ATOM   9480  N  N   . GLN C  1 140 ? -36.794 14.238  106.176 1.00 23.85  ? 140  GLN C N   1 
ATOM   9481  C  CA  . GLN C  1 140 ? -37.879 14.560  107.093 1.00 25.10  ? 140  GLN C CA  1 
ATOM   9482  C  C   . GLN C  1 140 ? -39.195 13.990  106.636 1.00 25.78  ? 140  GLN C C   1 
ATOM   9483  O  O   . GLN C  1 140 ? -39.912 13.385  107.414 1.00 26.70  ? 140  GLN C O   1 
ATOM   9484  C  CB  . GLN C  1 140 ? -38.021 16.064  107.308 1.00 33.20  ? 140  GLN C CB  1 
ATOM   9485  C  CG  . GLN C  1 140 ? -38.983 16.423  108.445 1.00 37.31  ? 140  GLN C CG  1 
ATOM   9486  C  CD  . GLN C  1 140 ? -40.359 16.860  107.961 1.00 42.81  ? 140  GLN C CD  1 
ATOM   9487  O  OE1 . GLN C  1 140 ? -40.499 17.626  106.981 1.00 45.28  ? 140  GLN C OE1 1 
ATOM   9488  N  NE2 . GLN C  1 140 ? -41.389 16.390  108.656 1.00 43.02  ? 140  GLN C NE2 1 
ATOM   9489  N  N   . VAL C  1 141 ? -39.510 14.198  105.369 1.00 29.67  ? 141  VAL C N   1 
ATOM   9490  C  CA  . VAL C  1 141 ? -40.829 13.873  104.879 1.00 39.84  ? 141  VAL C CA  1 
ATOM   9491  C  C   . VAL C  1 141 ? -41.005 12.398  104.605 1.00 42.42  ? 141  VAL C C   1 
ATOM   9492  O  O   . VAL C  1 141 ? -41.990 11.798  105.041 1.00 48.88  ? 141  VAL C O   1 
ATOM   9493  C  CB  . VAL C  1 141 ? -41.166 14.639  103.601 1.00 31.38  ? 141  VAL C CB  1 
ATOM   9494  C  CG1 . VAL C  1 141 ? -42.603 14.326  103.176 1.00 33.34  ? 141  VAL C CG1 1 
ATOM   9495  C  CG2 . VAL C  1 141 ? -40.979 16.120  103.822 1.00 29.43  ? 141  VAL C CG2 1 
ATOM   9496  N  N   . GLU C  1 142 ? -40.067 11.809  103.875 1.00 26.42  ? 142  GLU C N   1 
ATOM   9497  C  CA  . GLU C  1 142 ? -40.217 10.407  103.505 1.00 29.69  ? 142  GLU C CA  1 
ATOM   9498  C  C   . GLU C  1 142 ? -39.472 9.522   104.466 1.00 30.55  ? 142  GLU C C   1 
ATOM   9499  O  O   . GLU C  1 142 ? -39.410 8.298   104.289 1.00 24.92  ? 142  GLU C O   1 
ATOM   9500  C  CB  . GLU C  1 142 ? -39.813 10.143  102.059 1.00 44.07  ? 142  GLU C CB  1 
ATOM   9501  C  CG  . GLU C  1 142 ? -40.878 10.577  101.085 1.00 50.25  ? 142  GLU C CG  1 
ATOM   9502  C  CD  . GLU C  1 142 ? -42.226 9.924   101.373 1.00 55.65  ? 142  GLU C CD  1 
ATOM   9503  O  OE1 . GLU C  1 142 ? -42.228 8.779   101.896 1.00 57.27  ? 142  GLU C OE1 1 
ATOM   9504  O  OE2 . GLU C  1 142 ? -43.274 10.555  101.069 1.00 55.84  ? 142  GLU C OE2 1 
ATOM   9505  N  N   . GLY C  1 143 ? -38.901 10.174  105.475 1.00 24.93  ? 143  GLY C N   1 
ATOM   9506  C  CA  . GLY C  1 143 ? -38.317 9.498   106.613 1.00 27.37  ? 143  GLY C CA  1 
ATOM   9507  C  C   . GLY C  1 143 ? -37.182 8.579   106.256 1.00 24.97  ? 143  GLY C C   1 
ATOM   9508  O  O   . GLY C  1 143 ? -37.041 7.518   106.866 1.00 24.54  ? 143  GLY C O   1 
ATOM   9509  N  N   . ALA C  1 144 ? -36.358 9.005   105.299 1.00 29.84  ? 144  ALA C N   1 
ATOM   9510  C  CA  . ALA C  1 144 ? -35.339 8.144   104.709 1.00 30.73  ? 144  ALA C CA  1 
ATOM   9511  C  C   . ALA C  1 144 ? -33.954 8.566   105.160 1.00 27.80  ? 144  ALA C C   1 
ATOM   9512  O  O   . ALA C  1 144 ? -33.751 9.709   105.554 1.00 26.63  ? 144  ALA C O   1 
ATOM   9513  C  CB  . ALA C  1 144 ? -35.438 8.164   103.211 1.00 21.66  ? 144  ALA C CB  1 
ATOM   9514  N  N   . VAL C  1 145 ? -33.028 7.613   105.179 1.00 32.25  ? 145  VAL C N   1 
ATOM   9515  C  CA  . VAL C  1 145 ? -31.618 7.905   105.416 1.00 31.16  ? 145  VAL C CA  1 
ATOM   9516  C  C   . VAL C  1 145 ? -30.974 8.115   104.068 1.00 28.98  ? 145  VAL C C   1 
ATOM   9517  O  O   . VAL C  1 145 ? -31.078 7.268   103.192 1.00 27.80  ? 145  VAL C O   1 
ATOM   9518  C  CB  . VAL C  1 145 ? -30.885 6.760   106.116 1.00 20.69  ? 145  VAL C CB  1 
ATOM   9519  C  CG1 . VAL C  1 145 ? -29.408 6.913   105.936 1.00 19.91  ? 145  VAL C CG1 1 
ATOM   9520  C  CG2 . VAL C  1 145 ? -31.224 6.749   107.575 1.00 21.63  ? 145  VAL C CG2 1 
ATOM   9521  N  N   . LEU C  1 146 ? -30.303 9.246   103.907 1.00 26.42  ? 146  LEU C N   1 
ATOM   9522  C  CA  . LEU C  1 146 ? -29.803 9.642   102.612 1.00 27.99  ? 146  LEU C CA  1 
ATOM   9523  C  C   . LEU C  1 146 ? -28.337 10.057  102.696 1.00 28.82  ? 146  LEU C C   1 
ATOM   9524  O  O   . LEU C  1 146 ? -27.992 10.943  103.474 1.00 29.10  ? 146  LEU C O   1 
ATOM   9525  C  CB  . LEU C  1 146 ? -30.654 10.783  102.094 1.00 18.37  ? 146  LEU C CB  1 
ATOM   9526  C  CG  . LEU C  1 146 ? -30.271 11.192  100.691 1.00 18.20  ? 146  LEU C CG  1 
ATOM   9527  C  CD1 . LEU C  1 146 ? -31.534 11.392  99.903  1.00 17.99  ? 146  LEU C CD1 1 
ATOM   9528  C  CD2 . LEU C  1 146 ? -29.461 12.467  100.741 1.00 17.87  ? 146  LEU C CD2 1 
ATOM   9529  N  N   . VAL C  1 147 ? -27.488 9.416   101.886 1.00 23.89  ? 147  VAL C N   1 
ATOM   9530  C  CA  . VAL C  1 147 ? -26.042 9.641   101.894 1.00 16.54  ? 147  VAL C CA  1 
ATOM   9531  C  C   . VAL C  1 147 ? -25.585 10.264  100.599 1.00 15.88  ? 147  VAL C C   1 
ATOM   9532  O  O   . VAL C  1 147 ? -26.134 9.961   99.557  1.00 15.69  ? 147  VAL C O   1 
ATOM   9533  C  CB  . VAL C  1 147 ? -25.288 8.331   102.050 1.00 16.49  ? 147  VAL C CB  1 
ATOM   9534  C  CG1 . VAL C  1 147 ? -23.818 8.586   102.251 1.00 16.17  ? 147  VAL C CG1 1 
ATOM   9535  C  CG2 . VAL C  1 147 ? -25.843 7.579   103.224 1.00 18.35  ? 147  VAL C CG2 1 
ATOM   9536  N  N   . SER C  1 148 ? -24.589 11.142  100.659 1.00 23.11  ? 148  SER C N   1 
ATOM   9537  C  CA  . SER C  1 148 ? -23.947 11.649  99.442  1.00 26.73  ? 148  SER C CA  1 
ATOM   9538  C  C   . SER C  1 148 ? -22.430 11.830  99.602  1.00 29.10  ? 148  SER C C   1 
ATOM   9539  O  O   . SER C  1 148 ? -21.978 12.423  100.567 1.00 30.13  ? 148  SER C O   1 
ATOM   9540  C  CB  . SER C  1 148 ? -24.602 12.960  99.001  1.00 15.12  ? 148  SER C CB  1 
ATOM   9541  O  OG  . SER C  1 148 ? -24.481 13.960  99.990  1.00 15.50  ? 148  SER C OG  1 
ATOM   9542  N  N   . MET C  1 149 ? -21.638 11.335  98.658  1.00 14.33  ? 149  MET C N   1 
ATOM   9543  C  CA  . MET C  1 149 ? -20.184 11.481  98.779  1.00 18.75  ? 149  MET C CA  1 
ATOM   9544  C  C   . MET C  1 149 ? -19.585 12.424  97.750  1.00 18.81  ? 149  MET C C   1 
ATOM   9545  O  O   . MET C  1 149 ? -20.103 12.578  96.652  1.00 13.60  ? 149  MET C O   1 
ATOM   9546  C  CB  . MET C  1 149 ? -19.476 10.134  98.654  1.00 14.08  ? 149  MET C CB  1 
ATOM   9547  C  CG  . MET C  1 149 ? -19.193 9.713   97.222  1.00 13.64  ? 149  MET C CG  1 
ATOM   9548  S  SD  . MET C  1 149 ? -20.734 9.352   96.372  1.00 13.58  ? 149  MET C SD  1 
ATOM   9549  C  CE  . MET C  1 149 ? -21.128 7.722   96.971  1.00 13.93  ? 149  MET C CE  1 
ATOM   9550  N  N   . ASN C  1 150 ? -18.492 13.065  98.124  1.00 13.93  ? 150  ASN C N   1 
ATOM   9551  C  CA  . ASN C  1 150 ? -17.680 13.766  97.159  1.00 15.97  ? 150  ASN C CA  1 
ATOM   9552  C  C   . ASN C  1 150 ? -16.810 12.748  96.430  1.00 17.20  ? 150  ASN C C   1 
ATOM   9553  O  O   . ASN C  1 150 ? -16.298 11.822  97.048  1.00 18.95  ? 150  ASN C O   1 
ATOM   9554  C  CB  . ASN C  1 150 ? -16.811 14.789  97.877  1.00 14.02  ? 150  ASN C CB  1 
ATOM   9555  C  CG  . ASN C  1 150 ? -17.554 16.074  98.163  1.00 22.30  ? 150  ASN C CG  1 
ATOM   9556  O  OD1 . ASN C  1 150 ? -18.639 16.296  97.631  1.00 14.23  ? 150  ASN C OD1 1 
ATOM   9557  N  ND2 . ASN C  1 150 ? -16.967 16.941  98.981  1.00 14.75  ? 150  ASN C ND2 1 
ATOM   9558  N  N   . TYR C  1 151 ? -16.652 12.870  95.122  1.00 13.10  ? 151  TYR C N   1 
ATOM   9559  C  CA  . TYR C  1 151 ? -15.725 11.976  94.459  1.00 12.93  ? 151  TYR C CA  1 
ATOM   9560  C  C   . TYR C  1 151 ? -14.838 12.829  93.613  1.00 14.24  ? 151  TYR C C   1 
ATOM   9561  O  O   . TYR C  1 151 ? -15.269 13.891  93.191  1.00 13.76  ? 151  TYR C O   1 
ATOM   9562  C  CB  . TYR C  1 151 ? -16.443 10.907  93.638  1.00 35.52  ? 151  TYR C CB  1 
ATOM   9563  C  CG  . TYR C  1 151 ? -17.303 11.406  92.507  1.00 12.52  ? 151  TYR C CG  1 
ATOM   9564  C  CD1 . TYR C  1 151 ? -16.766 11.639  91.255  1.00 12.36  ? 151  TYR C CD1 1 
ATOM   9565  C  CD2 . TYR C  1 151 ? -18.664 11.599  92.678  1.00 12.71  ? 151  TYR C CD2 1 
ATOM   9566  C  CE1 . TYR C  1 151 ? -17.552 12.081  90.209  1.00 12.28  ? 151  TYR C CE1 1 
ATOM   9567  C  CE2 . TYR C  1 151 ? -19.463 12.048  91.637  1.00 12.53  ? 151  TYR C CE2 1 
ATOM   9568  C  CZ  . TYR C  1 151 ? -18.895 12.290  90.407  1.00 12.37  ? 151  TYR C CZ  1 
ATOM   9569  O  OH  . TYR C  1 151 ? -19.670 12.732  89.365  1.00 12.38  ? 151  TYR C OH  1 
ATOM   9570  N  N   . ARG C  1 152 ? -13.600 12.392  93.395  1.00 12.93  ? 152  ARG C N   1 
ATOM   9571  C  CA  . ARG C  1 152 ? -12.627 13.183  92.662  1.00 13.00  ? 152  ARG C CA  1 
ATOM   9572  C  C   . ARG C  1 152 ? -13.069 13.341  91.220  1.00 22.27  ? 152  ARG C C   1 
ATOM   9573  O  O   . ARG C  1 152 ? -13.460 12.378  90.587  1.00 12.54  ? 152  ARG C O   1 
ATOM   9574  C  CB  . ARG C  1 152 ? -11.268 12.498  92.712  1.00 15.53  ? 152  ARG C CB  1 
ATOM   9575  C  CG  . ARG C  1 152 ? -10.346 12.976  93.816  1.00 16.24  ? 152  ARG C CG  1 
ATOM   9576  C  CD  . ARG C  1 152 ? -9.090  12.144  93.872  1.00 13.91  ? 152  ARG C CD  1 
ATOM   9577  N  NE  . ARG C  1 152 ? -9.431  10.778  94.206  1.00 13.84  ? 152  ARG C NE  1 
ATOM   9578  C  CZ  . ARG C  1 152 ? -8.564  9.779   94.242  1.00 14.10  ? 152  ARG C CZ  1 
ATOM   9579  N  NH1 . ARG C  1 152 ? -7.284  9.999   93.972  1.00 14.45  ? 152  ARG C NH1 1 
ATOM   9580  N  NH2 . ARG C  1 152 ? -8.980  8.558   94.557  1.00 14.11  ? 152  ARG C NH2 1 
ATOM   9581  N  N   . VAL C  1 153 ? -13.018 14.559  90.701  1.00 12.84  ? 153  VAL C N   1 
ATOM   9582  C  CA  . VAL C  1 153 ? -13.382 14.789  89.309  1.00 12.70  ? 153  VAL C CA  1 
ATOM   9583  C  C   . VAL C  1 153 ? -12.226 15.430  88.545  1.00 15.34  ? 153  VAL C C   1 
ATOM   9584  O  O   . VAL C  1 153 ? -11.216 15.798  89.138  1.00 15.38  ? 153  VAL C O   1 
ATOM   9585  C  CB  . VAL C  1 153 ? -14.607 15.713  89.196  1.00 12.73  ? 153  VAL C CB  1 
ATOM   9586  C  CG1 . VAL C  1 153 ? -15.768 15.139  89.959  1.00 12.61  ? 153  VAL C CG1 1 
ATOM   9587  C  CG2 . VAL C  1 153 ? -14.278 17.089  89.718  1.00 13.08  ? 153  VAL C CG2 1 
ATOM   9588  N  N   . GLY C  1 154 ? -12.399 15.603  87.236  1.00 16.41  ? 154  GLY C N   1 
ATOM   9589  C  CA  . GLY C  1 154 ? -11.358 16.160  86.388  1.00 14.90  ? 154  GLY C CA  1 
ATOM   9590  C  C   . GLY C  1 154 ? -10.165 15.229  86.318  1.00 14.73  ? 154  GLY C C   1 
ATOM   9591  O  O   . GLY C  1 154 ? -10.324 14.031  86.566  1.00 14.96  ? 154  GLY C O   1 
ATOM   9592  N  N   . THR C  1 155 ? -8.986  15.773  85.994  1.00 13.68  ? 155  THR C N   1 
ATOM   9593  C  CA  . THR C  1 155 ? -7.746  14.996  85.970  1.00 13.91  ? 155  THR C CA  1 
ATOM   9594  C  C   . THR C  1 155 ? -7.584  14.189  87.252  1.00 15.14  ? 155  THR C C   1 
ATOM   9595  O  O   . THR C  1 155 ? -7.207  13.015  87.218  1.00 15.31  ? 155  THR C O   1 
ATOM   9596  C  CB  . THR C  1 155 ? -6.486  15.879  85.765  1.00 14.51  ? 155  THR C CB  1 
ATOM   9597  O  OG1 . THR C  1 155 ? -6.481  16.973  86.688  1.00 14.75  ? 155  THR C OG1 1 
ATOM   9598  C  CG2 . THR C  1 155 ? -6.453  16.436  84.368  1.00 16.51  ? 155  THR C CG2 1 
ATOM   9599  N  N   . PHE C  1 156 ? -7.920  14.817  88.375  1.00 17.87  ? 156  PHE C N   1 
ATOM   9600  C  CA  . PHE C  1 156 ? -7.716  14.233  89.693  1.00 14.31  ? 156  PHE C CA  1 
ATOM   9601  C  C   . PHE C  1 156 ? -8.373  12.885  89.885  1.00 20.77  ? 156  PHE C C   1 
ATOM   9602  O  O   . PHE C  1 156 ? -7.774  12.008  90.504  1.00 21.10  ? 156  PHE C O   1 
ATOM   9603  C  CB  . PHE C  1 156 ? -8.149  15.212  90.777  1.00 14.06  ? 156  PHE C CB  1 
ATOM   9604  C  CG  . PHE C  1 156 ? -7.506  16.543  90.636  1.00 14.51  ? 156  PHE C CG  1 
ATOM   9605  C  CD1 . PHE C  1 156 ? -6.139  16.684  90.849  1.00 15.06  ? 156  PHE C CD1 1 
ATOM   9606  C  CD2 . PHE C  1 156 ? -8.239  17.643  90.238  1.00 14.50  ? 156  PHE C CD2 1 
ATOM   9607  C  CE1 . PHE C  1 156 ? -5.518  17.904  90.688  1.00 15.59  ? 156  PHE C CE1 1 
ATOM   9608  C  CE2 . PHE C  1 156 ? -7.629  18.864  90.079  1.00 15.02  ? 156  PHE C CE2 1 
ATOM   9609  C  CZ  . PHE C  1 156 ? -6.263  18.995  90.301  1.00 15.57  ? 156  PHE C CZ  1 
ATOM   9610  N  N   . GLY C  1 157 ? -9.606  12.719  89.410  1.00 18.90  ? 157  GLY C N   1 
ATOM   9611  C  CA  . GLY C  1 157 ? -10.213 11.398  89.429  1.00 12.96  ? 157  GLY C CA  1 
ATOM   9612  C  C   . GLY C  1 157 ? -10.056 10.535  88.190  1.00 33.11  ? 157  GLY C C   1 
ATOM   9613  O  O   . GLY C  1 157 ? -10.028 9.309   88.263  1.00 12.93  ? 157  GLY C O   1 
ATOM   9614  N  N   . PHE C  1 158 ? -10.024 11.177  87.034  1.00 12.89  ? 158  PHE C N   1 
ATOM   9615  C  CA  . PHE C  1 158 ? -10.057 10.420  85.790  1.00 12.86  ? 158  PHE C CA  1 
ATOM   9616  C  C   . PHE C  1 158 ? -8.847  10.348  84.867  1.00 13.71  ? 158  PHE C C   1 
ATOM   9617  O  O   . PHE C  1 158 ? -8.914  9.678   83.837  1.00 13.24  ? 158  PHE C O   1 
ATOM   9618  C  CB  . PHE C  1 158 ? -11.391 10.645  85.072  1.00 12.61  ? 158  PHE C CB  1 
ATOM   9619  C  CG  . PHE C  1 158 ? -12.576 10.280  85.943  1.00 12.38  ? 158  PHE C CG  1 
ATOM   9620  C  CD1 . PHE C  1 158 ? -13.120 11.203  86.821  1.00 12.31  ? 158  PHE C CD1 1 
ATOM   9621  C  CD2 . PHE C  1 158 ? -13.093 8.998   85.936  1.00 12.52  ? 158  PHE C CD2 1 
ATOM   9622  C  CE1 . PHE C  1 158 ? -14.160 10.864  87.631  1.00 12.20  ? 158  PHE C CE1 1 
ATOM   9623  C  CE2 . PHE C  1 158 ? -14.139 8.659   86.758  1.00 12.24  ? 158  PHE C CE2 1 
ATOM   9624  C  CZ  . PHE C  1 158 ? -14.669 9.592   87.601  1.00 31.33  ? 158  PHE C CZ  1 
ATOM   9625  N  N   . LEU C  1 159 ? -7.758  11.040  85.194  1.00 16.46  ? 159  LEU C N   1 
ATOM   9626  C  CA  . LEU C  1 159 ? -6.613  11.019  84.289  1.00 13.95  ? 159  LEU C CA  1 
ATOM   9627  C  C   . LEU C  1 159 ? -6.059  9.637   84.348  1.00 14.13  ? 159  LEU C C   1 
ATOM   9628  O  O   . LEU C  1 159 ? -5.942  9.069   85.423  1.00 14.15  ? 159  LEU C O   1 
ATOM   9629  C  CB  . LEU C  1 159 ? -5.527  12.002  84.700  1.00 14.38  ? 159  LEU C CB  1 
ATOM   9630  C  CG  . LEU C  1 159 ? -4.199  11.876  83.954  1.00 14.97  ? 159  LEU C CG  1 
ATOM   9631  C  CD1 . LEU C  1 159 ? -3.688  13.261  83.659  1.00 15.35  ? 159  LEU C CD1 1 
ATOM   9632  C  CD2 . LEU C  1 159 ? -3.196  11.106  84.773  1.00 15.35  ? 159  LEU C CD2 1 
ATOM   9633  N  N   . ALA C  1 160 ? -5.714  9.084   83.204  1.00 22.75  ? 160  ALA C N   1 
ATOM   9634  C  CA  . ALA C  1 160 ? -5.357  7.689   83.187  1.00 23.09  ? 160  ALA C CA  1 
ATOM   9635  C  C   . ALA C  1 160 ? -4.228  7.455   82.244  1.00 23.72  ? 160  ALA C C   1 
ATOM   9636  O  O   . ALA C  1 160 ? -4.247  7.943   81.118  1.00 24.10  ? 160  ALA C O   1 
ATOM   9637  C  CB  . ALA C  1 160 ? -6.539  6.863   82.762  1.00 38.69  ? 160  ALA C CB  1 
ATOM   9638  N  N   . LEU C  1 161 ? -3.245  6.701   82.714  1.00 33.54  ? 161  LEU C N   1 
ATOM   9639  C  CA  . LEU C  1 161 ? -2.259  6.096   81.845  1.00 29.77  ? 161  LEU C CA  1 
ATOM   9640  C  C   . LEU C  1 161 ? -2.422  4.604   82.022  1.00 28.14  ? 161  LEU C C   1 
ATOM   9641  O  O   . LEU C  1 161 ? -1.672  4.010   82.785  1.00 28.58  ? 161  LEU C O   1 
ATOM   9642  C  CB  . LEU C  1 161 ? -0.858  6.496   82.266  1.00 22.18  ? 161  LEU C CB  1 
ATOM   9643  C  CG  . LEU C  1 161 ? -0.386  7.890   81.926  1.00 17.07  ? 161  LEU C CG  1 
ATOM   9644  C  CD1 . LEU C  1 161 ? 1.074   7.783   81.795  1.00 24.92  ? 161  LEU C CD1 1 
ATOM   9645  C  CD2 . LEU C  1 161 ? -0.957  8.326   80.627  1.00 25.55  ? 161  LEU C CD2 1 
ATOM   9646  N  N   . PRO C  1 162 ? -3.384  3.993   81.297  1.00 18.28  ? 162  PRO C N   1 
ATOM   9647  C  CA  . PRO C  1 162 ? -3.873  2.639   81.546  1.00 19.42  ? 162  PRO C CA  1 
ATOM   9648  C  C   . PRO C  1 162 ? -2.751  1.636   81.782  1.00 24.02  ? 162  PRO C C   1 
ATOM   9649  O  O   . PRO C  1 162 ? -1.748  1.624   81.053  1.00 25.71  ? 162  PRO C O   1 
ATOM   9650  C  CB  . PRO C  1 162 ? -4.571  2.302   80.235  1.00 16.17  ? 162  PRO C CB  1 
ATOM   9651  C  CG  . PRO C  1 162 ? -5.087  3.549   79.787  1.00 37.39  ? 162  PRO C CG  1 
ATOM   9652  C  CD  . PRO C  1 162 ? -4.097  4.603   80.169  1.00 15.86  ? 162  PRO C CD  1 
ATOM   9653  N  N   . GLY C  1 163 ? -2.911  0.818   82.821  1.00 29.25  ? 163  GLY C N   1 
ATOM   9654  C  CA  . GLY C  1 163 ? -1.966  -0.246  83.090  1.00 33.02  ? 163  GLY C CA  1 
ATOM   9655  C  C   . GLY C  1 163 ? -0.747  0.217   83.848  1.00 37.19  ? 163  GLY C C   1 
ATOM   9656  O  O   . GLY C  1 163 ? 0.079   -0.588  84.265  1.00 43.16  ? 163  GLY C O   1 
ATOM   9657  N  N   . SER C  1 164 ? -0.618  1.523   84.013  1.00 32.50  ? 164  SER C N   1 
ATOM   9658  C  CA  . SER C  1 164 ? 0.399   2.058   84.897  1.00 33.04  ? 164  SER C CA  1 
ATOM   9659  C  C   . SER C  1 164 ? -0.043  1.831   86.325  1.00 32.30  ? 164  SER C C   1 
ATOM   9660  O  O   . SER C  1 164 ? -1.240  1.702   86.602  1.00 27.67  ? 164  SER C O   1 
ATOM   9661  C  CB  . SER C  1 164 ? 0.549   3.550   84.691  1.00 41.54  ? 164  SER C CB  1 
ATOM   9662  O  OG  . SER C  1 164 ? -0.681  4.193   84.979  1.00 39.54  ? 164  SER C OG  1 
ATOM   9663  N  N   . ARG C  1 165 ? 0.928   1.799   87.229  1.00 38.07  ? 165  ARG C N   1 
ATOM   9664  C  CA  . ARG C  1 165 ? 0.652   1.594   88.641  1.00 41.74  ? 165  ARG C CA  1 
ATOM   9665  C  C   . ARG C  1 165 ? 0.176   2.888   89.296  1.00 33.09  ? 165  ARG C C   1 
ATOM   9666  O  O   . ARG C  1 165 ? -0.749  2.873   90.114  1.00 29.13  ? 165  ARG C O   1 
ATOM   9667  C  CB  . ARG C  1 165 ? 1.902   1.061   89.351  1.00 69.66  ? 165  ARG C CB  1 
ATOM   9668  C  CG  . ARG C  1 165 ? 1.673   0.627   90.787  1.00 77.94  ? 165  ARG C CG  1 
ATOM   9669  C  CD  . ARG C  1 165 ? 2.922   0.813   91.648  1.00 87.42  ? 165  ARG C CD  1 
ATOM   9670  N  NE  . ARG C  1 165 ? 2.601   1.529   92.881  1.00 94.26  ? 165  ARG C NE  1 
ATOM   9671  C  CZ  . ARG C  1 165 ? 2.166   0.946   93.996  1.00 99.45  ? 165  ARG C CZ  1 
ATOM   9672  N  NH1 . ARG C  1 165 ? 2.012   -0.375  94.041  1.00 101.01 ? 165  ARG C NH1 1 
ATOM   9673  N  NH2 . ARG C  1 165 ? 1.885   1.683   95.069  1.00 99.87  ? 165  ARG C NH2 1 
ATOM   9674  N  N   . GLU C  1 166 ? 0.808   4.001   88.927  1.00 23.19  ? 166  GLU C N   1 
ATOM   9675  C  CA  . GLU C  1 166 ? 0.606   5.252   89.647  1.00 25.17  ? 166  GLU C CA  1 
ATOM   9676  C  C   . GLU C  1 166 ? -0.412  6.242   89.050  1.00 22.68  ? 166  GLU C C   1 
ATOM   9677  O  O   . GLU C  1 166 ? -0.613  7.342   89.602  1.00 23.01  ? 166  GLU C O   1 
ATOM   9678  C  CB  . GLU C  1 166 ? 1.945   5.936   89.916  1.00 54.61  ? 166  GLU C CB  1 
ATOM   9679  C  CG  . GLU C  1 166 ? 2.990   5.661   88.869  1.00 65.24  ? 166  GLU C CG  1 
ATOM   9680  C  CD  . GLU C  1 166 ? 4.015   4.681   89.358  1.00 75.53  ? 166  GLU C CD  1 
ATOM   9681  O  OE1 . GLU C  1 166 ? 3.873   4.231   90.514  1.00 80.07  ? 166  GLU C OE1 1 
ATOM   9682  O  OE2 . GLU C  1 166 ? 4.956   4.365   88.599  1.00 77.71  ? 166  GLU C OE2 1 
ATOM   9683  N  N   . ALA C  1 167 ? -1.002  5.892   87.909  1.00 28.35  ? 167  ALA C N   1 
ATOM   9684  C  CA  . ALA C  1 167 ? -2.218  6.561   87.438  1.00 26.20  ? 167  ALA C CA  1 
ATOM   9685  C  C   . ALA C  1 167 ? -3.110  5.578   86.694  1.00 28.53  ? 167  ALA C C   1 
ATOM   9686  O  O   . ALA C  1 167 ? -3.302  5.694   85.488  1.00 30.26  ? 167  ALA C O   1 
ATOM   9687  C  CB  . ALA C  1 167 ? -1.883  7.728   86.569  1.00 18.93  ? 167  ALA C CB  1 
ATOM   9688  N  N   . PRO C  1 168 ? -3.671  4.617   87.417  1.00 15.64  ? 168  PRO C N   1 
ATOM   9689  C  CA  . PRO C  1 168 ? -4.376  3.449   86.905  1.00 15.55  ? 168  PRO C CA  1 
ATOM   9690  C  C   . PRO C  1 168 ? -5.585  3.832   86.084  1.00 28.75  ? 168  PRO C C   1 
ATOM   9691  O  O   . PRO C  1 168 ? -5.950  3.109   85.149  1.00 24.13  ? 168  PRO C O   1 
ATOM   9692  C  CB  . PRO C  1 168 ? -4.888  2.791   88.172  1.00 23.31  ? 168  PRO C CB  1 
ATOM   9693  C  CG  . PRO C  1 168 ? -4.053  3.322   89.238  1.00 23.22  ? 168  PRO C CG  1 
ATOM   9694  C  CD  . PRO C  1 168 ? -3.802  4.721   88.866  1.00 22.94  ? 168  PRO C CD  1 
ATOM   9695  N  N   . GLY C  1 169 ? -6.215  4.946   86.454  1.00 37.79  ? 169  GLY C N   1 
ATOM   9696  C  CA  . GLY C  1 169 ? -7.451  5.372   85.830  1.00 37.27  ? 169  GLY C CA  1 
ATOM   9697  C  C   . GLY C  1 169 ? -8.631  4.887   86.637  1.00 36.14  ? 169  GLY C C   1 
ATOM   9698  O  O   . GLY C  1 169 ? -8.533  3.881   87.342  1.00 40.45  ? 169  GLY C O   1 
ATOM   9699  N  N   . ASN C  1 170 ? -9.745  5.602   86.503  1.00 25.38  ? 170  ASN C N   1 
ATOM   9700  C  CA  . ASN C  1 170 ? -11.014 5.341   87.215  1.00 24.46  ? 170  ASN C CA  1 
ATOM   9701  C  C   . ASN C  1 170 ? -11.015 5.542   88.730  1.00 13.12  ? 170  ASN C C   1 
ATOM   9702  O  O   . ASN C  1 170 ? -11.889 5.029   89.413  1.00 13.32  ? 170  ASN C O   1 
ATOM   9703  C  CB  . ASN C  1 170 ? -11.577 3.947   86.886  1.00 13.25  ? 170  ASN C CB  1 
ATOM   9704  C  CG  . ASN C  1 170 ? -12.039 3.819   85.446  1.00 13.46  ? 170  ASN C CG  1 
ATOM   9705  O  OD1 . ASN C  1 170 ? -12.625 4.734   84.894  1.00 14.57  ? 170  ASN C OD1 1 
ATOM   9706  N  ND2 . ASN C  1 170 ? -11.772 2.675   84.835  1.00 13.54  ? 170  ASN C ND2 1 
ATOM   9707  N  N   . VAL C  1 171 ? -10.092 6.338   89.254  1.00 16.03  ? 171  VAL C N   1 
ATOM   9708  C  CA  . VAL C  1 171 ? -10.042 6.492   90.698  1.00 16.13  ? 171  VAL C CA  1 
ATOM   9709  C  C   . VAL C  1 171 ? -11.239 7.284   91.208  1.00 16.76  ? 171  VAL C C   1 
ATOM   9710  O  O   . VAL C  1 171 ? -11.604 7.156   92.370  1.00 18.13  ? 171  VAL C O   1 
ATOM   9711  C  CB  . VAL C  1 171 ? -8.707  7.093   91.223  1.00 13.72  ? 171  VAL C CB  1 
ATOM   9712  C  CG1 . VAL C  1 171 ? -7.509  6.408   90.591  1.00 14.09  ? 171  VAL C CG1 1 
ATOM   9713  C  CG2 . VAL C  1 171 ? -8.673  8.575   90.993  1.00 13.56  ? 171  VAL C CG2 1 
ATOM   9714  N  N   . GLY C  1 172 ? -11.862 8.087   90.354  1.00 12.78  ? 172  GLY C N   1 
ATOM   9715  C  CA  . GLY C  1 172 ? -13.082 8.761   90.761  1.00 12.59  ? 172  GLY C CA  1 
ATOM   9716  C  C   . GLY C  1 172 ? -14.148 7.755   91.185  1.00 17.48  ? 172  GLY C C   1 
ATOM   9717  O  O   . GLY C  1 172 ? -14.774 7.863   92.261  1.00 15.84  ? 172  GLY C O   1 
ATOM   9718  N  N   . LEU C  1 173 ? -14.339 6.755   90.328  1.00 21.97  ? 173  LEU C N   1 
ATOM   9719  C  CA  . LEU C  1 173 ? -15.280 5.673   90.575  1.00 21.92  ? 173  LEU C CA  1 
ATOM   9720  C  C   . LEU C  1 173 ? -14.906 4.855   91.801  1.00 24.64  ? 173  LEU C C   1 
ATOM   9721  O  O   . LEU C  1 173 ? -15.776 4.425   92.555  1.00 26.22  ? 173  LEU C O   1 
ATOM   9722  C  CB  . LEU C  1 173 ? -15.365 4.774   89.345  1.00 14.13  ? 173  LEU C CB  1 
ATOM   9723  C  CG  . LEU C  1 173 ? -16.085 5.495   88.209  1.00 13.40  ? 173  LEU C CG  1 
ATOM   9724  C  CD1 . LEU C  1 173 ? -16.110 4.638   86.960  1.00 12.66  ? 173  LEU C CD1 1 
ATOM   9725  C  CD2 . LEU C  1 173 ? -17.505 5.925   88.643  1.00 12.49  ? 173  LEU C CD2 1 
ATOM   9726  N  N   . LEU C  1 174 ? -13.610 4.640   91.999  1.00 20.83  ? 174  LEU C N   1 
ATOM   9727  C  CA  . LEU C  1 174 ? -13.145 3.938   93.184  1.00 20.93  ? 174  LEU C CA  1 
ATOM   9728  C  C   . LEU C  1 174 ? -13.494 4.715   94.437  1.00 21.34  ? 174  LEU C C   1 
ATOM   9729  O  O   . LEU C  1 174 ? -13.871 4.106   95.423  1.00 21.65  ? 174  LEU C O   1 
ATOM   9730  C  CB  . LEU C  1 174 ? -11.643 3.689   93.126  1.00 13.94  ? 174  LEU C CB  1 
ATOM   9731  C  CG  . LEU C  1 174 ? -11.197 2.755   92.011  1.00 14.07  ? 174  LEU C CG  1 
ATOM   9732  C  CD1 . LEU C  1 174 ? -9.862  2.188   92.346  1.00 19.20  ? 174  LEU C CD1 1 
ATOM   9733  C  CD2 . LEU C  1 174 ? -12.202 1.644   91.825  1.00 20.82  ? 174  LEU C CD2 1 
ATOM   9734  N  N   . ASP C  1 175 ? -13.361 6.047   94.392  1.00 13.46  ? 175  ASP C N   1 
ATOM   9735  C  CA  . ASP C  1 175 ? -13.789 6.941   95.477  1.00 13.53  ? 175  ASP C CA  1 
ATOM   9736  C  C   . ASP C  1 175 ? -15.247 6.679   95.802  1.00 13.52  ? 175  ASP C C   1 
ATOM   9737  O  O   . ASP C  1 175 ? -15.607 6.421   96.958  1.00 13.85  ? 175  ASP C O   1 
ATOM   9738  C  CB  . ASP C  1 175 ? -13.647 8.413   95.076  1.00 13.30  ? 175  ASP C CB  1 
ATOM   9739  C  CG  . ASP C  1 175 ? -12.199 8.897   95.040  1.00 16.53  ? 175  ASP C CG  1 
ATOM   9740  O  OD1 . ASP C  1 175 ? -11.253 8.149   95.399  1.00 13.78  ? 175  ASP C OD1 1 
ATOM   9741  O  OD2 . ASP C  1 175 ? -12.010 10.071  94.661  1.00 17.75  ? 175  ASP C OD2 1 
ATOM   9742  N  N   . GLN C  1 176 ? -16.082 6.749   94.766  1.00 13.22  ? 176  GLN C N   1 
ATOM   9743  C  CA  . GLN C  1 176 ? -17.506 6.483   94.921  1.00 13.29  ? 176  GLN C CA  1 
ATOM   9744  C  C   . GLN C  1 176 ? -17.693 5.173   95.634  1.00 22.93  ? 176  GLN C C   1 
ATOM   9745  O  O   . GLN C  1 176 ? -18.396 5.082   96.644  1.00 13.99  ? 176  GLN C O   1 
ATOM   9746  C  CB  . GLN C  1 176 ? -18.181 6.372   93.564  1.00 27.26  ? 176  GLN C CB  1 
ATOM   9747  C  CG  . GLN C  1 176 ? -17.946 7.539   92.655  1.00 26.93  ? 176  GLN C CG  1 
ATOM   9748  C  CD  . GLN C  1 176 ? -18.878 7.525   91.477  1.00 26.44  ? 176  GLN C CD  1 
ATOM   9749  O  OE1 . GLN C  1 176 ? -19.666 6.598   91.305  1.00 23.96  ? 176  GLN C OE1 1 
ATOM   9750  N  NE2 . GLN C  1 176 ? -18.798 8.556   90.654  1.00 28.27  ? 176  GLN C NE2 1 
ATOM   9751  N  N   . ARG C  1 177 ? -17.041 4.153   95.100  1.00 22.60  ? 177  ARG C N   1 
ATOM   9752  C  CA  . ARG C  1 177 ? -17.180 2.814   95.626  1.00 22.12  ? 177  ARG C CA  1 
ATOM   9753  C  C   . ARG C  1 177 ? -16.825 2.751   97.090  1.00 23.96  ? 177  ARG C C   1 
ATOM   9754  O  O   . ARG C  1 177 ? -17.545 2.138   97.863  1.00 26.42  ? 177  ARG C O   1 
ATOM   9755  C  CB  . ARG C  1 177 ? -16.311 1.824   94.865  1.00 17.68  ? 177  ARG C CB  1 
ATOM   9756  C  CG  . ARG C  1 177 ? -16.564 0.405   95.315  1.00 14.93  ? 177  ARG C CG  1 
ATOM   9757  C  CD  . ARG C  1 177 ? -15.614 -0.533  94.662  1.00 15.16  ? 177  ARG C CD  1 
ATOM   9758  N  NE  . ARG C  1 177 ? -16.120 -0.995  93.382  1.00 17.75  ? 177  ARG C NE  1 
ATOM   9759  C  CZ  . ARG C  1 177 ? -15.346 -1.528  92.445  1.00 20.32  ? 177  ARG C CZ  1 
ATOM   9760  N  NH1 . ARG C  1 177 ? -14.035 -1.644  92.679  1.00 20.11  ? 177  ARG C NH1 1 
ATOM   9761  N  NH2 . ARG C  1 177 ? -15.874 -1.930  91.284  1.00 20.83  ? 177  ARG C NH2 1 
ATOM   9762  N  N   . LEU C  1 178 ? -15.721 3.386   97.462  1.00 14.62  ? 178  LEU C N   1 
ATOM   9763  C  CA  . LEU C  1 178 ? -15.224 3.326   98.823  1.00 15.10  ? 178  LEU C CA  1 
ATOM   9764  C  C   . LEU C  1 178 ? -16.256 3.951   99.724  1.00 15.21  ? 178  LEU C C   1 
ATOM   9765  O  O   . LEU C  1 178 ? -16.500 3.461   100.819 1.00 15.74  ? 178  LEU C O   1 
ATOM   9766  C  CB  . LEU C  1 178 ? -13.879 4.039   98.955  1.00 15.08  ? 178  LEU C CB  1 
ATOM   9767  C  CG  . LEU C  1 178 ? -13.256 4.167   100.346 1.00 15.64  ? 178  LEU C CG  1 
ATOM   9768  C  CD1 . LEU C  1 178 ? -12.878 2.830   100.952 1.00 16.28  ? 178  LEU C CD1 1 
ATOM   9769  C  CD2 . LEU C  1 178 ? -12.056 5.051   100.264 1.00 15.60  ? 178  LEU C CD2 1 
ATOM   9770  N  N   . ALA C  1 179 ? -16.890 5.019   99.260  1.00 14.79  ? 179  ALA C N   1 
ATOM   9771  C  CA  . ALA C  1 179 ? -17.988 5.586   100.033 1.00 14.97  ? 179  ALA C CA  1 
ATOM   9772  C  C   . ALA C  1 179 ? -19.132 4.574   100.215 1.00 15.30  ? 179  ALA C C   1 
ATOM   9773  O  O   . ALA C  1 179 ? -19.693 4.464   101.301 1.00 15.79  ? 179  ALA C O   1 
ATOM   9774  C  CB  . ALA C  1 179 ? -18.484 6.843   99.391  1.00 14.55  ? 179  ALA C CB  1 
ATOM   9775  N  N   . LEU C  1 180 ? -19.459 3.831   99.156  1.00 19.72  ? 180  LEU C N   1 
ATOM   9776  C  CA  . LEU C  1 180 ? -20.457 2.747   99.236  1.00 21.06  ? 180  LEU C CA  1 
ATOM   9777  C  C   . LEU C  1 180 ? -20.109 1.635   100.251 1.00 24.30  ? 180  LEU C C   1 
ATOM   9778  O  O   . LEU C  1 180 ? -20.975 1.177   101.006 1.00 25.48  ? 180  LEU C O   1 
ATOM   9779  C  CB  . LEU C  1 180 ? -20.717 2.140   97.854  1.00 15.30  ? 180  LEU C CB  1 
ATOM   9780  C  CG  . LEU C  1 180 ? -21.866 2.726   97.037  1.00 21.76  ? 180  LEU C CG  1 
ATOM   9781  C  CD1 . LEU C  1 180 ? -21.814 4.221   97.049  1.00 14.67  ? 180  LEU C CD1 1 
ATOM   9782  C  CD2 . LEU C  1 180 ? -21.786 2.238   95.624  1.00 14.82  ? 180  LEU C CD2 1 
ATOM   9783  N  N   . GLN C  1 181 ? -18.852 1.201   100.265 1.00 16.26  ? 181  GLN C N   1 
ATOM   9784  C  CA  . GLN C  1 181 ? -18.379 0.267   101.271 1.00 16.96  ? 181  GLN C CA  1 
ATOM   9785  C  C   . GLN C  1 181 ? -18.533 0.876   102.658 1.00 17.34  ? 181  GLN C C   1 
ATOM   9786  O  O   . GLN C  1 181 ? -18.974 0.196   103.601 1.00 18.50  ? 181  GLN C O   1 
ATOM   9787  C  CB  . GLN C  1 181 ? -16.918 -0.085  101.039 1.00 38.38  ? 181  GLN C CB  1 
ATOM   9788  C  CG  . GLN C  1 181 ? -16.558 -0.319  99.589  1.00 39.93  ? 181  GLN C CG  1 
ATOM   9789  C  CD  . GLN C  1 181 ? -15.278 -1.125  99.419  1.00 44.53  ? 181  GLN C CD  1 
ATOM   9790  O  OE1 . GLN C  1 181 ? -14.235 -0.609  98.978  1.00 42.57  ? 181  GLN C OE1 1 
ATOM   9791  N  NE2 . GLN C  1 181 ? -15.358 -2.410  99.759  1.00 50.29  ? 181  GLN C NE2 1 
ATOM   9792  N  N   . TRP C  1 182 ? -18.174 2.153   102.796 1.00 23.17  ? 182  TRP C N   1 
ATOM   9793  C  CA  . TRP C  1 182 ? -18.337 2.841   104.081 1.00 23.06  ? 182  TRP C CA  1 
ATOM   9794  C  C   . TRP C  1 182 ? -19.771 2.722   104.542 1.00 23.23  ? 182  TRP C C   1 
ATOM   9795  O  O   . TRP C  1 182 ? -20.033 2.394   105.694 1.00 24.58  ? 182  TRP C O   1 
ATOM   9796  C  CB  . TRP C  1 182 ? -17.983 4.326   104.000 1.00 22.48  ? 182  TRP C CB  1 
ATOM   9797  C  CG  . TRP C  1 182 ? -18.081 5.048   105.338 1.00 17.41  ? 182  TRP C CG  1 
ATOM   9798  C  CD1 . TRP C  1 182 ? -17.084 5.209   106.252 1.00 30.47  ? 182  TRP C CD1 1 
ATOM   9799  C  CD2 . TRP C  1 182 ? -19.229 5.699   105.888 1.00 17.61  ? 182  TRP C CD2 1 
ATOM   9800  N  NE1 . TRP C  1 182 ? -17.536 5.920   107.335 1.00 18.30  ? 182  TRP C NE1 1 
ATOM   9801  C  CE2 . TRP C  1 182 ? -18.849 6.228   107.138 1.00 18.17  ? 182  TRP C CE2 1 
ATOM   9802  C  CE3 . TRP C  1 182 ? -20.536 5.884   105.449 1.00 17.47  ? 182  TRP C CE3 1 
ATOM   9803  C  CZ2 . TRP C  1 182 ? -19.733 6.926   107.954 1.00 18.58  ? 182  TRP C CZ2 1 
ATOM   9804  C  CZ3 . TRP C  1 182 ? -21.422 6.586   106.266 1.00 27.23  ? 182  TRP C CZ3 1 
ATOM   9805  C  CH2 . TRP C  1 182 ? -21.012 7.101   107.502 1.00 25.98  ? 182  TRP C CH2 1 
ATOM   9806  N  N   . VAL C  1 183 ? -20.696 2.991   103.628 1.00 21.93  ? 183  VAL C N   1 
ATOM   9807  C  CA  . VAL C  1 183 ? -22.105 2.900   103.937 1.00 17.66  ? 183  VAL C CA  1 
ATOM   9808  C  C   . VAL C  1 183 ? -22.416 1.499   104.405 1.00 26.55  ? 183  VAL C C   1 
ATOM   9809  O  O   . VAL C  1 183 ? -23.157 1.324   105.367 1.00 19.06  ? 183  VAL C O   1 
ATOM   9810  C  CB  . VAL C  1 183 ? -22.973 3.277   102.735 1.00 17.86  ? 183  VAL C CB  1 
ATOM   9811  C  CG1 . VAL C  1 183 ? -24.436 2.971   103.003 1.00 17.71  ? 183  VAL C CG1 1 
ATOM   9812  C  CG2 . VAL C  1 183 ? -22.785 4.749   102.405 1.00 16.62  ? 183  VAL C CG2 1 
ATOM   9813  N  N   . GLN C  1 184 ? -21.827 0.497   103.760 1.00 28.09  ? 184  GLN C N   1 
ATOM   9814  C  CA  . GLN C  1 184 ? -22.110 -0.886  104.170 1.00 28.50  ? 184  GLN C CA  1 
ATOM   9815  C  C   . GLN C  1 184 ? -21.770 -1.167  105.612 1.00 30.08  ? 184  GLN C C   1 
ATOM   9816  O  O   . GLN C  1 184 ? -22.629 -1.614  106.376 1.00 34.45  ? 184  GLN C O   1 
ATOM   9817  C  CB  . GLN C  1 184 ? -21.439 -1.908  103.273 1.00 19.04  ? 184  GLN C CB  1 
ATOM   9818  C  CG  . GLN C  1 184 ? -22.203 -2.111  102.002 1.00 18.70  ? 184  GLN C CG  1 
ATOM   9819  C  CD  . GLN C  1 184 ? -23.433 -2.924  102.223 1.00 19.44  ? 184  GLN C CD  1 
ATOM   9820  O  OE1 . GLN C  1 184 ? -23.336 -4.133  102.434 1.00 20.13  ? 184  GLN C OE1 1 
ATOM   9821  N  NE2 . GLN C  1 184 ? -24.606 -2.282  102.179 1.00 19.39  ? 184  GLN C NE2 1 
ATOM   9822  N  N   . GLU C  1 185 ? -20.534 -0.890  105.997 1.00 21.23  ? 185  GLU C N   1 
ATOM   9823  C  CA  . GLU C  1 185 ? -20.176 -1.111  107.395 1.00 24.25  ? 185  GLU C CA  1 
ATOM   9824  C  C   . GLU C  1 185 ? -20.938 -0.213  108.376 1.00 29.17  ? 185  GLU C C   1 
ATOM   9825  O  O   . GLU C  1 185 ? -21.441 -0.670  109.407 1.00 31.44  ? 185  GLU C O   1 
ATOM   9826  C  CB  . GLU C  1 185 ? -18.684 -0.936  107.618 1.00 21.35  ? 185  GLU C CB  1 
ATOM   9827  C  CG  . GLU C  1 185 ? -18.274 -1.252  109.026 1.00 26.48  ? 185  GLU C CG  1 
ATOM   9828  C  CD  . GLU C  1 185 ? -16.786 -1.498  109.144 1.00 31.15  ? 185  GLU C CD  1 
ATOM   9829  O  OE1 . GLU C  1 185 ? -16.070 -1.311  108.117 1.00 32.70  ? 185  GLU C OE1 1 
ATOM   9830  O  OE2 . GLU C  1 185 ? -16.334 -1.871  110.263 1.00 31.30  ? 185  GLU C OE2 1 
ATOM   9831  N  N   . ASN C  1 186 ? -20.981 1.078   108.081 1.00 29.12  ? 186  ASN C N   1 
ATOM   9832  C  CA  . ASN C  1 186 ? -21.435 2.037   109.077 1.00 28.66  ? 186  ASN C CA  1 
ATOM   9833  C  C   . ASN C  1 186 ? -22.847 2.610   109.030 1.00 20.63  ? 186  ASN C C   1 
ATOM   9834  O  O   . ASN C  1 186 ? -23.235 3.294   109.957 1.00 21.08  ? 186  ASN C O   1 
ATOM   9835  C  CB  . ASN C  1 186 ? -20.416 3.168   109.154 1.00 27.29  ? 186  ASN C CB  1 
ATOM   9836  C  CG  . ASN C  1 186 ? -19.005 2.648   109.274 1.00 25.53  ? 186  ASN C CG  1 
ATOM   9837  O  OD1 . ASN C  1 186 ? -18.557 2.326   110.369 1.00 30.71  ? 186  ASN C OD1 1 
ATOM   9838  N  ND2 . ASN C  1 186 ? -18.307 2.534   108.149 1.00 20.61  ? 186  ASN C ND2 1 
ATOM   9839  N  N   . ILE C  1 187 ? -23.638 2.338   108.004 1.00 26.13  ? 187  ILE C N   1 
ATOM   9840  C  CA  . ILE C  1 187 ? -24.887 3.099   107.903 1.00 28.67  ? 187  ILE C CA  1 
ATOM   9841  C  C   . ILE C  1 187 ? -25.872 2.564   108.923 1.00 31.04  ? 187  ILE C C   1 
ATOM   9842  O  O   . ILE C  1 187 ? -26.828 3.243   109.321 1.00 31.96  ? 187  ILE C O   1 
ATOM   9843  C  CB  . ILE C  1 187 ? -25.506 3.118   106.476 1.00 23.24  ? 187  ILE C CB  1 
ATOM   9844  C  CG1 . ILE C  1 187 ? -26.424 4.332   106.302 1.00 19.51  ? 187  ILE C CG1 1 
ATOM   9845  C  CG2 . ILE C  1 187 ? -26.245 1.837   106.181 1.00 23.11  ? 187  ILE C CG2 1 
ATOM   9846  C  CD1 . ILE C  1 187 ? -25.687 5.645   106.278 1.00 18.98  ? 187  ILE C CD1 1 
ATOM   9847  N  N   . ALA C  1 188 ? -25.602 1.342   109.368 1.00 27.00  ? 188  ALA C N   1 
ATOM   9848  C  CA  . ALA C  1 188 ? -26.428 0.702   110.369 1.00 28.80  ? 188  ALA C CA  1 
ATOM   9849  C  C   . ALA C  1 188 ? -26.486 1.533   111.651 1.00 27.66  ? 188  ALA C C   1 
ATOM   9850  O  O   . ALA C  1 188 ? -27.489 1.514   112.357 1.00 26.77  ? 188  ALA C O   1 
ATOM   9851  C  CB  . ALA C  1 188 ? -25.914 -0.705  110.650 1.00 42.26  ? 188  ALA C CB  1 
ATOM   9852  N  N   . ALA C  1 189 ? -25.415 2.268   111.935 1.00 23.23  ? 189  ALA C N   1 
ATOM   9853  C  CA  . ALA C  1 189 ? -25.344 3.068   113.149 1.00 27.27  ? 189  ALA C CA  1 
ATOM   9854  C  C   . ALA C  1 189 ? -26.185 4.342   113.057 1.00 26.44  ? 189  ALA C C   1 
ATOM   9855  O  O   . ALA C  1 189 ? -26.484 4.965   114.081 1.00 24.31  ? 189  ALA C O   1 
ATOM   9856  C  CB  . ALA C  1 189 ? -23.906 3.400   113.499 1.00 23.61  ? 189  ALA C CB  1 
ATOM   9857  N  N   . PHE C  1 190 ? -26.563 4.744   111.846 1.00 37.61  ? 190  PHE C N   1 
ATOM   9858  C  CA  . PHE C  1 190 ? -27.398 5.934   111.699 1.00 36.22  ? 190  PHE C CA  1 
ATOM   9859  C  C   . PHE C  1 190 ? -28.855 5.558   111.572 1.00 39.07  ? 190  PHE C C   1 
ATOM   9860  O  O   . PHE C  1 190 ? -29.716 6.416   111.416 1.00 44.40  ? 190  PHE C O   1 
ATOM   9861  C  CB  . PHE C  1 190 ? -26.965 6.789   110.512 1.00 21.64  ? 190  PHE C CB  1 
ATOM   9862  C  CG  . PHE C  1 190 ? -25.571 7.317   110.629 1.00 21.21  ? 190  PHE C CG  1 
ATOM   9863  C  CD1 . PHE C  1 190 ? -24.486 6.546   110.242 1.00 20.80  ? 190  PHE C CD1 1 
ATOM   9864  C  CD2 . PHE C  1 190 ? -25.338 8.584   111.126 1.00 21.31  ? 190  PHE C CD2 1 
ATOM   9865  C  CE1 . PHE C  1 190 ? -23.191 7.031   110.346 1.00 20.50  ? 190  PHE C CE1 1 
ATOM   9866  C  CE2 . PHE C  1 190 ? -24.039 9.073   111.234 1.00 21.01  ? 190  PHE C CE2 1 
ATOM   9867  C  CZ  . PHE C  1 190 ? -22.967 8.292   110.841 1.00 20.61  ? 190  PHE C CZ  1 
ATOM   9868  N  N   . GLY C  1 191 ? -29.138 4.268   111.638 1.00 29.69  ? 191  GLY C N   1 
ATOM   9869  C  CA  . GLY C  1 191 ? -30.505 3.814   111.490 1.00 31.03  ? 191  GLY C CA  1 
ATOM   9870  C  C   . GLY C  1 191 ? -30.747 3.373   110.064 1.00 32.18  ? 191  GLY C C   1 
ATOM   9871  O  O   . GLY C  1 191 ? -31.894 3.178   109.643 1.00 32.87  ? 191  GLY C O   1 
ATOM   9872  N  N   . GLY C  1 192 ? -29.649 3.219   109.326 1.00 39.40  ? 192  GLY C N   1 
ATOM   9873  C  CA  . GLY C  1 192 ? -29.689 2.746   107.957 1.00 38.44  ? 192  GLY C CA  1 
ATOM   9874  C  C   . GLY C  1 192 ? -29.755 1.233   107.874 1.00 38.20  ? 192  GLY C C   1 
ATOM   9875  O  O   . GLY C  1 192 ? -29.518 0.531   108.857 1.00 41.55  ? 192  GLY C O   1 
ATOM   9876  N  N   . ASP C  1 193 ? -30.063 0.733   106.684 1.00 27.07  ? 193  ASP C N   1 
ATOM   9877  C  CA  . ASP C  1 193 ? -30.297 -0.681  106.455 1.00 26.74  ? 193  ASP C CA  1 
ATOM   9878  C  C   . ASP C  1 193 ? -29.379 -1.141  105.355 1.00 22.01  ? 193  ASP C C   1 
ATOM   9879  O  O   . ASP C  1 193 ? -29.721 -1.019  104.197 1.00 32.21  ? 193  ASP C O   1 
ATOM   9880  C  CB  . ASP C  1 193 ? -31.741 -0.867  106.007 1.00 35.85  ? 193  ASP C CB  1 
ATOM   9881  C  CG  . ASP C  1 193 ? -32.119 -2.323  105.810 1.00 40.23  ? 193  ASP C CG  1 
ATOM   9882  O  OD1 . ASP C  1 193 ? -31.215 -3.205  105.754 1.00 38.68  ? 193  ASP C OD1 1 
ATOM   9883  O  OD2 . ASP C  1 193 ? -33.349 -2.566  105.705 1.00 42.56  ? 193  ASP C OD2 1 
ATOM   9884  N  N   . PRO C  1 194 ? -28.213 -1.686  105.701 1.00 21.96  ? 194  PRO C N   1 
ATOM   9885  C  CA  . PRO C  1 194 ? -27.234 -2.003  104.658 1.00 21.93  ? 194  PRO C CA  1 
ATOM   9886  C  C   . PRO C  1 194 ? -27.791 -2.966  103.617 1.00 23.51  ? 194  PRO C C   1 
ATOM   9887  O  O   . PRO C  1 194 ? -27.179 -3.139  102.554 1.00 20.78  ? 194  PRO C O   1 
ATOM   9888  C  CB  . PRO C  1 194 ? -26.077 -2.648  105.437 1.00 25.25  ? 194  PRO C CB  1 
ATOM   9889  C  CG  . PRO C  1 194 ? -26.189 -2.083  106.801 1.00 29.56  ? 194  PRO C CG  1 
ATOM   9890  C  CD  . PRO C  1 194 ? -27.689 -1.985  107.040 1.00 33.62  ? 194  PRO C CD  1 
ATOM   9891  N  N   . MET C  1 195 ? -28.931 -3.584  103.929 1.00 26.57  ? 195  MET C N   1 
ATOM   9892  C  CA  . MET C  1 195 ? -29.523 -4.578  103.047 1.00 28.05  ? 195  MET C CA  1 
ATOM   9893  C  C   . MET C  1 195 ? -30.587 -4.023  102.101 1.00 27.22  ? 195  MET C C   1 
ATOM   9894  O  O   . MET C  1 195 ? -31.108 -4.737  101.247 1.00 26.34  ? 195  MET C O   1 
ATOM   9895  C  CB  . MET C  1 195 ? -30.037 -5.772  103.854 1.00 31.56  ? 195  MET C CB  1 
ATOM   9896  C  CG  . MET C  1 195 ? -29.077 -6.969  103.847 1.00 24.31  ? 195  MET C CG  1 
ATOM   9897  S  SD  . MET C  1 195 ? -29.322 -8.081  105.247 1.00 98.31  ? 195  MET C SD  1 
ATOM   9898  C  CE  . MET C  1 195 ? -31.082 -8.461  105.141 1.00 44.96  ? 195  MET C CE  1 
ATOM   9899  N  N   . SER C  1 196 ? -30.920 -2.755  102.243 1.00 22.04  ? 196  SER C N   1 
ATOM   9900  C  CA  . SER C  1 196 ? -31.613 -2.095  101.159 1.00 21.63  ? 196  SER C CA  1 
ATOM   9901  C  C   . SER C  1 196 ? -30.955 -0.741  100.881 1.00 20.58  ? 196  SER C C   1 
ATOM   9902  O  O   . SER C  1 196 ? -31.164 0.217   101.612 1.00 20.58  ? 196  SER C O   1 
ATOM   9903  C  CB  . SER C  1 196 ? -33.099 -1.965  101.515 1.00 30.29  ? 196  SER C CB  1 
ATOM   9904  O  OG  . SER C  1 196 ? -33.792 -1.028  100.709 1.00 31.68  ? 196  SER C OG  1 
ATOM   9905  N  N   . VAL C  1 197 ? -30.221 -0.637  99.778  1.00 27.95  ? 197  VAL C N   1 
ATOM   9906  C  CA  . VAL C  1 197 ? -29.473 0.569   99.463  1.00 27.04  ? 197  VAL C CA  1 
ATOM   9907  C  C   . VAL C  1 197 ? -29.712 0.862   98.009  1.00 29.14  ? 197  VAL C C   1 
ATOM   9908  O  O   . VAL C  1 197 ? -29.370 0.044   97.163  1.00 33.58  ? 197  VAL C O   1 
ATOM   9909  C  CB  . VAL C  1 197 ? -27.966 0.344   99.600  1.00 18.37  ? 197  VAL C CB  1 
ATOM   9910  C  CG1 . VAL C  1 197 ? -27.240 1.635   99.389  1.00 17.57  ? 197  VAL C CG1 1 
ATOM   9911  C  CG2 . VAL C  1 197 ? -27.620 -0.243  100.951 1.00 21.89  ? 197  VAL C CG2 1 
ATOM   9912  N  N   . THR C  1 198 ? -30.287 2.018   97.706  1.00 29.18  ? 198  THR C N   1 
ATOM   9913  C  CA  . THR C  1 198 ? -30.527 2.418   96.320  1.00 29.61  ? 198  THR C CA  1 
ATOM   9914  C  C   . THR C  1 198 ? -29.561 3.520   95.875  1.00 30.32  ? 198  THR C C   1 
ATOM   9915  O  O   . THR C  1 198 ? -29.473 4.559   96.528  1.00 32.65  ? 198  THR C O   1 
ATOM   9916  C  CB  . THR C  1 198 ? -31.936 2.963   96.166  1.00 18.29  ? 198  THR C CB  1 
ATOM   9917  O  OG1 . THR C  1 198 ? -32.872 1.968   96.572  1.00 21.87  ? 198  THR C OG1 1 
ATOM   9918  C  CG2 . THR C  1 198 ? -32.204 3.335   94.744  1.00 25.64  ? 198  THR C CG2 1 
ATOM   9919  N  N   . LEU C  1 199 ? -28.827 3.304   94.781  1.00 24.63  ? 199  LEU C N   1 
ATOM   9920  C  CA  . LEU C  1 199 ? -28.009 4.378   94.219  1.00 20.33  ? 199  LEU C CA  1 
ATOM   9921  C  C   . LEU C  1 199 ? -28.910 5.192   93.324  1.00 21.05  ? 199  LEU C C   1 
ATOM   9922  O  O   . LEU C  1 199 ? -29.717 4.648   92.583  1.00 22.34  ? 199  LEU C O   1 
ATOM   9923  C  CB  . LEU C  1 199 ? -26.857 3.831   93.390  1.00 15.24  ? 199  LEU C CB  1 
ATOM   9924  C  CG  . LEU C  1 199 ? -25.924 2.880   94.108  1.00 15.31  ? 199  LEU C CG  1 
ATOM   9925  C  CD1 . LEU C  1 199 ? -24.915 2.358   93.149  1.00 14.98  ? 199  LEU C CD1 1 
ATOM   9926  C  CD2 . LEU C  1 199 ? -25.242 3.602   95.230  1.00 15.15  ? 199  LEU C CD2 1 
ATOM   9927  N  N   . PHE C  1 200 ? -28.810 6.504   93.394  1.00 18.96  ? 200  PHE C N   1 
ATOM   9928  C  CA  . PHE C  1 200 ? -29.475 7.301   92.376  1.00 20.16  ? 200  PHE C CA  1 
ATOM   9929  C  C   . PHE C  1 200 ? -28.583 8.480   92.002  1.00 21.90  ? 200  PHE C C   1 
ATOM   9930  O  O   . PHE C  1 200 ? -27.844 9.016   92.841  1.00 14.70  ? 200  PHE C O   1 
ATOM   9931  C  CB  . PHE C  1 200 ? -30.935 7.673   92.746  1.00 16.16  ? 200  PHE C CB  1 
ATOM   9932  C  CG  . PHE C  1 200 ? -31.077 8.780   93.785  1.00 22.40  ? 200  PHE C CG  1 
ATOM   9933  C  CD1 . PHE C  1 200 ? -30.237 8.857   94.895  1.00 21.46  ? 200  PHE C CD1 1 
ATOM   9934  C  CD2 . PHE C  1 200 ? -32.076 9.739   93.648  1.00 20.80  ? 200  PHE C CD2 1 
ATOM   9935  C  CE1 . PHE C  1 200 ? -30.382 9.872   95.838  1.00 19.66  ? 200  PHE C CE1 1 
ATOM   9936  C  CE2 . PHE C  1 200 ? -32.225 10.751  94.589  1.00 20.38  ? 200  PHE C CE2 1 
ATOM   9937  C  CZ  . PHE C  1 200 ? -31.373 10.816  95.683  1.00 20.62  ? 200  PHE C CZ  1 
ATOM   9938  N  N   . GLY C  1 201 ? -28.594 8.830   90.722  1.00 24.60  ? 201  GLY C N   1 
ATOM   9939  C  CA  . GLY C  1 201 ? -27.780 9.943   90.281  1.00 14.33  ? 201  GLY C CA  1 
ATOM   9940  C  C   . GLY C  1 201 ? -28.283 10.543  88.994  1.00 14.44  ? 201  GLY C C   1 
ATOM   9941  O  O   . GLY C  1 201 ? -29.104 9.953   88.287  1.00 14.77  ? 201  GLY C O   1 
ATOM   9942  N  N   . GLU C  1 202 ? -27.785 11.722  88.675  1.00 14.24  ? 202  GLU C N   1 
ATOM   9943  C  CA  . GLU C  1 202 ? -28.189 12.371  87.449  1.00 17.65  ? 202  GLU C CA  1 
ATOM   9944  C  C   . GLU C  1 202 ? -26.952 12.691  86.605  1.00 16.52  ? 202  GLU C C   1 
ATOM   9945  O  O   . GLU C  1 202 ? -25.862 12.839  87.148  1.00 18.81  ? 202  GLU C O   1 
ATOM   9946  C  CB  . GLU C  1 202 ? -29.009 13.605  87.802  1.00 22.97  ? 202  GLU C CB  1 
ATOM   9947  C  CG  . GLU C  1 202 ? -29.532 14.370  86.642  1.00 27.21  ? 202  GLU C CG  1 
ATOM   9948  C  CD  . GLU C  1 202 ? -28.556 15.420  86.209  1.00 31.36  ? 202  GLU C CD  1 
ATOM   9949  O  OE1 . GLU C  1 202 ? -27.569 15.645  86.938  1.00 32.28  ? 202  GLU C OE1 1 
ATOM   9950  O  OE2 . GLU C  1 202 ? -28.768 16.019  85.141  1.00 34.50  ? 202  GLU C OE2 1 
ATOM   9951  N  N   . SER C  1 203 ? -27.120 12.758  85.282  1.00 14.09  ? 203  SER C N   1 
ATOM   9952  C  CA  . SER C  1 203 ? -26.034 13.030  84.304  1.00 13.81  ? 203  SER C CA  1 
ATOM   9953  C  C   . SER C  1 203 ? -24.825 12.110  84.442  1.00 13.36  ? 203  SER C C   1 
ATOM   9954  O  O   . SER C  1 203 ? -24.948 10.902  84.330  1.00 13.36  ? 203  SER C O   1 
ATOM   9955  C  CB  . SER C  1 203 ? -25.591 14.493  84.347  1.00 13.92  ? 203  SER C CB  1 
ATOM   9956  O  OG  . SER C  1 203 ? -25.032 14.899  83.112  1.00 13.85  ? 203  SER C OG  1 
ATOM   9957  N  N   . ALA C  1 204 ? -23.656 12.677  84.702  1.00 20.94  ? 204  ALA C N   1 
ATOM   9958  C  CA  . ALA C  1 204 ? -22.479 11.843  84.933  1.00 19.25  ? 204  ALA C CA  1 
ATOM   9959  C  C   . ALA C  1 204 ? -22.635 11.017  86.209  1.00 19.71  ? 204  ALA C C   1 
ATOM   9960  O  O   . ALA C  1 204 ? -21.903 10.044  86.424  1.00 17.26  ? 204  ALA C O   1 
ATOM   9961  C  CB  . ALA C  1 204 ? -21.228 12.676  84.995  1.00 12.56  ? 204  ALA C CB  1 
ATOM   9962  N  N   . GLY C  1 205 ? -23.593 11.405  87.045  1.00 23.79  ? 205  GLY C N   1 
ATOM   9963  C  CA  . GLY C  1 205 ? -23.953 10.625  88.213  1.00 23.53  ? 205  GLY C CA  1 
ATOM   9964  C  C   . GLY C  1 205 ? -24.771 9.404   87.828  1.00 23.23  ? 205  GLY C C   1 
ATOM   9965  O  O   . GLY C  1 205 ? -24.624 8.339   88.434  1.00 24.17  ? 205  GLY C O   1 
ATOM   9966  N  N   . ALA C  1 206 ? -25.632 9.542   86.823  1.00 15.12  ? 206  ALA C N   1 
ATOM   9967  C  CA  . ALA C  1 206 ? -26.397 8.392   86.354  1.00 13.80  ? 206  ALA C CA  1 
ATOM   9968  C  C   . ALA C  1 206 ? -25.464 7.447   85.624  1.00 13.60  ? 206  ALA C C   1 
ATOM   9969  O  O   . ALA C  1 206 ? -25.609 6.225   85.710  1.00 13.81  ? 206  ALA C O   1 
ATOM   9970  C  CB  . ALA C  1 206 ? -27.536 8.816   85.459  1.00 14.21  ? 206  ALA C CB  1 
ATOM   9971  N  N   . ALA C  1 207 ? -24.499 8.029   84.913  1.00 13.30  ? 207  ALA C N   1 
ATOM   9972  C  CA  . ALA C  1 207 ? -23.431 7.265   84.279  1.00 13.86  ? 207  ALA C CA  1 
ATOM   9973  C  C   . ALA C  1 207 ? -22.724 6.482   85.350  1.00 14.46  ? 207  ALA C C   1 
ATOM   9974  O  O   . ALA C  1 207 ? -22.475 5.292   85.201  1.00 13.16  ? 207  ALA C O   1 
ATOM   9975  C  CB  . ALA C  1 207 ? -22.450 8.174   83.595  1.00 12.89  ? 207  ALA C CB  1 
ATOM   9976  N  N   . SER C  1 208 ? -22.409 7.155   86.444  1.00 12.83  ? 208  SER C N   1 
ATOM   9977  C  CA  . SER C  1 208 ? -21.734 6.488   87.538  1.00 15.61  ? 208  SER C CA  1 
ATOM   9978  C  C   . SER C  1 208 ? -22.542 5.313   88.098  1.00 14.24  ? 208  SER C C   1 
ATOM   9979  O  O   . SER C  1 208 ? -22.022 4.198   88.267  1.00 13.29  ? 208  SER C O   1 
ATOM   9980  C  CB  . SER C  1 208 ? -21.387 7.493   88.627  1.00 12.64  ? 208  SER C CB  1 
ATOM   9981  O  OG  . SER C  1 208 ? -20.311 8.305   88.205  1.00 12.40  ? 208  SER C OG  1 
ATOM   9982  N  N   . VAL C  1 209 ? -23.813 5.555   88.378  1.00 13.41  ? 209  VAL C N   1 
ATOM   9983  C  CA  . VAL C  1 209 ? -24.656 4.485   88.886  1.00 17.01  ? 209  VAL C CA  1 
ATOM   9984  C  C   . VAL C  1 209 ? -24.634 3.280   87.944  1.00 16.10  ? 209  VAL C C   1 
ATOM   9985  O  O   . VAL C  1 209 ? -24.418 2.144   88.383  1.00 15.97  ? 209  VAL C O   1 
ATOM   9986  C  CB  . VAL C  1 209 ? -26.072 4.983   89.152  1.00 14.22  ? 209  VAL C CB  1 
ATOM   9987  C  CG1 . VAL C  1 209 ? -27.052 3.817   89.254  1.00 14.82  ? 209  VAL C CG1 1 
ATOM   9988  C  CG2 . VAL C  1 209 ? -26.068 5.833   90.411  1.00 14.15  ? 209  VAL C CG2 1 
ATOM   9989  N  N   . GLY C  1 210 ? -24.797 3.534   86.649  1.00 16.26  ? 210  GLY C N   1 
ATOM   9990  C  CA  . GLY C  1 210 ? -24.678 2.476   85.660  1.00 18.41  ? 210  GLY C CA  1 
ATOM   9991  C  C   . GLY C  1 210 ? -23.314 1.793   85.669  1.00 19.57  ? 210  GLY C C   1 
ATOM   9992  O  O   . GLY C  1 210 ? -23.193 0.586   85.442  1.00 18.63  ? 210  GLY C O   1 
ATOM   9993  N  N   . MET C  1 211 ? -22.276 2.564   85.942  1.00 13.73  ? 211  MET C N   1 
ATOM   9994  C  CA  . MET C  1 211 ? -20.946 1.998   86.016  1.00 14.23  ? 211  MET C CA  1 
ATOM   9995  C  C   . MET C  1 211 ? -20.832 1.018   87.182  1.00 13.94  ? 211  MET C C   1 
ATOM   9996  O  O   . MET C  1 211 ? -20.140 0.014   87.090  1.00 14.20  ? 211  MET C O   1 
ATOM   9997  C  CB  . MET C  1 211 ? -19.904 3.101   86.161  1.00 20.43  ? 211  MET C CB  1 
ATOM   9998  C  CG  . MET C  1 211 ? -18.792 3.019   85.160  1.00 16.12  ? 211  MET C CG  1 
ATOM   9999  S  SD  . MET C  1 211 ? -19.066 4.174   83.824  1.00 26.78  ? 211  MET C SD  1 
ATOM   10000 C  CE  . MET C  1 211 ? -19.215 3.023   82.477  1.00 64.89  ? 211  MET C CE  1 
ATOM   10001 N  N   . HIS C  1 212 ? -21.496 1.306   88.291  1.00 13.99  ? 212  HIS C N   1 
ATOM   10002 C  CA  . HIS C  1 212 ? -21.464 0.350   89.388  1.00 16.66  ? 212  HIS C CA  1 
ATOM   10003 C  C   . HIS C  1 212 ? -22.319 -0.865  89.092  1.00 18.71  ? 212  HIS C C   1 
ATOM   10004 O  O   . HIS C  1 212 ? -21.992 -1.960  89.537  1.00 17.69  ? 212  HIS C O   1 
ATOM   10005 C  CB  . HIS C  1 212 ? -21.877 0.988   90.699  1.00 14.36  ? 212  HIS C CB  1 
ATOM   10006 C  CG  . HIS C  1 212 ? -20.933 2.043   91.154  1.00 13.92  ? 212  HIS C CG  1 
ATOM   10007 N  ND1 . HIS C  1 212 ? -19.716 1.749   91.730  1.00 13.93  ? 212  HIS C ND1 1 
ATOM   10008 C  CD2 . HIS C  1 212 ? -21.008 3.394   91.094  1.00 13.54  ? 212  HIS C CD2 1 
ATOM   10009 C  CE1 . HIS C  1 212 ? -19.091 2.873   92.027  1.00 13.58  ? 212  HIS C CE1 1 
ATOM   10010 N  NE2 . HIS C  1 212 ? -19.853 3.887   91.649  1.00 22.62  ? 212  HIS C NE2 1 
ATOM   10011 N  N   . ILE C  1 213 ? -23.415 -0.676  88.353  1.00 22.50  ? 213  ILE C N   1 
ATOM   10012 C  CA  . ILE C  1 213 ? -24.229 -1.809  87.909  1.00 22.88  ? 213  ILE C CA  1 
ATOM   10013 C  C   . ILE C  1 213 ? -23.379 -2.720  87.037  1.00 24.40  ? 213  ILE C C   1 
ATOM   10014 O  O   . ILE C  1 213 ? -23.476 -3.939  87.109  1.00 16.57  ? 213  ILE C O   1 
ATOM   10015 C  CB  . ILE C  1 213 ? -25.421 -1.361  87.079  1.00 15.91  ? 213  ILE C CB  1 
ATOM   10016 C  CG1 . ILE C  1 213 ? -26.416 -0.609  87.929  1.00 15.95  ? 213  ILE C CG1 1 
ATOM   10017 C  CG2 . ILE C  1 213 ? -26.126 -2.535  86.519  1.00 16.66  ? 213  ILE C CG2 1 
ATOM   10018 C  CD1 . ILE C  1 213 ? -27.519 -0.030  87.120  1.00 16.12  ? 213  ILE C CD1 1 
ATOM   10019 N  N   . LEU C  1 214 ? -22.533 -2.124  86.212  1.00 15.48  ? 214  LEU C N   1 
ATOM   10020 C  CA  . LEU C  1 214 ? -21.692 -2.913  85.328  1.00 15.69  ? 214  LEU C CA  1 
ATOM   10021 C  C   . LEU C  1 214 ? -20.401 -3.461  85.945  1.00 19.14  ? 214  LEU C C   1 
ATOM   10022 O  O   . LEU C  1 214 ? -19.836 -4.409  85.417  1.00 21.22  ? 214  LEU C O   1 
ATOM   10023 C  CB  . LEU C  1 214 ? -21.386 -2.142  84.052  1.00 16.80  ? 214  LEU C CB  1 
ATOM   10024 C  CG  . LEU C  1 214 ? -22.624 -1.913  83.212  1.00 15.55  ? 214  LEU C CG  1 
ATOM   10025 C  CD1 . LEU C  1 214 ? -22.245 -1.230  81.942  1.00 15.32  ? 214  LEU C CD1 1 
ATOM   10026 C  CD2 . LEU C  1 214 ? -23.217 -3.242  82.929  1.00 19.72  ? 214  LEU C CD2 1 
ATOM   10027 N  N   . SER C  1 215 ? -19.925 -2.878  87.042  1.00 21.35  ? 215  SER C N   1 
ATOM   10028 C  CA  . SER C  1 215 ? -18.684 -3.352  87.680  1.00 24.26  ? 215  SER C CA  1 
ATOM   10029 C  C   . SER C  1 215 ? -18.992 -4.286  88.845  1.00 23.26  ? 215  SER C C   1 
ATOM   10030 O  O   . SER C  1 215 ? -19.666 -3.905  89.795  1.00 23.38  ? 215  SER C O   1 
ATOM   10031 C  CB  . SER C  1 215 ? -17.816 -2.175  88.157  1.00 36.04  ? 215  SER C CB  1 
ATOM   10032 O  OG  . SER C  1 215 ? -16.660 -2.616  88.857  1.00 37.51  ? 215  SER C OG  1 
ATOM   10033 N  N   . LEU C  1 216 ? -18.487 -5.507  88.776  1.00 31.02  ? 216  LEU C N   1 
ATOM   10034 C  CA  . LEU C  1 216 ? -18.877 -6.543  89.730  1.00 33.52  ? 216  LEU C CA  1 
ATOM   10035 C  C   . LEU C  1 216 ? -18.619 -6.306  91.224  1.00 36.25  ? 216  LEU C C   1 
ATOM   10036 O  O   . LEU C  1 216 ? -19.464 -6.660  92.053  1.00 42.43  ? 216  LEU C O   1 
ATOM   10037 C  CB  . LEU C  1 216 ? -18.275 -7.871  89.329  1.00 27.86  ? 216  LEU C CB  1 
ATOM   10038 C  CG  . LEU C  1 216 ? -19.355 -8.914  89.152  1.00 28.79  ? 216  LEU C CG  1 
ATOM   10039 C  CD1 . LEU C  1 216 ? -19.467 -9.324  87.668  1.00 24.85  ? 216  LEU C CD1 1 
ATOM   10040 C  CD2 . LEU C  1 216 ? -19.054 -10.091 90.099  1.00 32.38  ? 216  LEU C CD2 1 
ATOM   10041 N  N   . PRO C  1 217 ? -17.453 -5.746  91.586  1.00 24.09  ? 217  PRO C N   1 
ATOM   10042 C  CA  . PRO C  1 217 ? -17.250 -5.495  93.017  1.00 22.85  ? 217  PRO C CA  1 
ATOM   10043 C  C   . PRO C  1 217 ? -18.253 -4.510  93.592  1.00 21.70  ? 217  PRO C C   1 
ATOM   10044 O  O   . PRO C  1 217 ? -18.554 -4.583  94.778  1.00 23.08  ? 217  PRO C O   1 
ATOM   10045 C  CB  . PRO C  1 217 ? -15.850 -4.894  93.068  1.00 16.86  ? 217  PRO C CB  1 
ATOM   10046 C  CG  . PRO C  1 217 ? -15.180 -5.453  91.885  1.00 16.99  ? 217  PRO C CG  1 
ATOM   10047 C  CD  . PRO C  1 217 ? -16.219 -5.507  90.822  1.00 16.83  ? 217  PRO C CD  1 
ATOM   10048 N  N   . SER C  1 218 ? -18.755 -3.603  92.766  1.00 22.90  ? 218  SER C N   1 
ATOM   10049 C  CA  . SER C  1 218 ? -19.731 -2.630  93.232  1.00 25.51  ? 218  SER C CA  1 
ATOM   10050 C  C   . SER C  1 218 ? -21.124 -3.259  93.401  1.00 27.89  ? 218  SER C C   1 
ATOM   10051 O  O   . SER C  1 218 ? -21.971 -2.721  94.116  1.00 30.10  ? 218  SER C O   1 
ATOM   10052 C  CB  . SER C  1 218 ? -19.791 -1.419  92.285  1.00 21.82  ? 218  SER C CB  1 
ATOM   10053 O  OG  . SER C  1 218 ? -18.564 -0.704  92.251  1.00 14.79  ? 218  SER C OG  1 
ATOM   10054 N  N   . ARG C  1 219 ? -21.354 -4.399  92.753  1.00 26.60  ? 219  ARG C N   1 
ATOM   10055 C  CA  . ARG C  1 219 ? -22.680 -5.011  92.738  1.00 27.76  ? 219  ARG C CA  1 
ATOM   10056 C  C   . ARG C  1 219 ? -23.139 -5.485  94.122  1.00 31.65  ? 219  ARG C C   1 
ATOM   10057 O  O   . ARG C  1 219 ? -24.334 -5.457  94.449  1.00 33.98  ? 219  ARG C O   1 
ATOM   10058 C  CB  . ARG C  1 219 ? -22.734 -6.157  91.732  1.00 27.10  ? 219  ARG C CB  1 
ATOM   10059 C  CG  . ARG C  1 219 ? -22.839 -5.717  90.278  1.00 29.84  ? 219  ARG C CG  1 
ATOM   10060 C  CD  . ARG C  1 219 ? -24.106 -4.890  89.994  1.00 36.30  ? 219  ARG C CD  1 
ATOM   10061 N  NE  . ARG C  1 219 ? -25.372 -5.594  90.245  1.00 41.71  ? 219  ARG C NE  1 
ATOM   10062 C  CZ  . ARG C  1 219 ? -26.068 -6.292  89.342  1.00 43.60  ? 219  ARG C CZ  1 
ATOM   10063 N  NH1 . ARG C  1 219 ? -25.643 -6.423  88.087  1.00 43.36  ? 219  ARG C NH1 1 
ATOM   10064 N  NH2 . ARG C  1 219 ? -27.201 -6.874  89.706  1.00 44.32  ? 219  ARG C NH2 1 
ATOM   10065 N  N   . SER C  1 220 ? -22.191 -5.895  94.949  1.00 26.81  ? 220  SER C N   1 
ATOM   10066 C  CA  . SER C  1 220 ? -22.538 -6.331  96.292  1.00 28.95  ? 220  SER C CA  1 
ATOM   10067 C  C   . SER C  1 220 ? -22.677 -5.183  97.294  1.00 27.95  ? 220  SER C C   1 
ATOM   10068 O  O   . SER C  1 220 ? -22.799 -5.433  98.490  1.00 31.35  ? 220  SER C O   1 
ATOM   10069 C  CB  . SER C  1 220 ? -21.520 -7.341  96.805  1.00 45.79  ? 220  SER C CB  1 
ATOM   10070 O  OG  . SER C  1 220 ? -20.207 -6.874  96.584  1.00 51.13  ? 220  SER C OG  1 
ATOM   10071 N  N   . LEU C  1 221 ? -22.562 -3.938  96.833  1.00 28.57  ? 221  LEU C N   1 
ATOM   10072 C  CA  . LEU C  1 221 ? -22.759 -2.789  97.712  1.00 25.03  ? 221  LEU C CA  1 
ATOM   10073 C  C   . LEU C  1 221 ? -24.110 -2.088  97.616  1.00 26.86  ? 221  LEU C C   1 
ATOM   10074 O  O   . LEU C  1 221 ? -24.376 -1.180  98.393  1.00 32.98  ? 221  LEU C O   1 
ATOM   10075 C  CB  . LEU C  1 221 ? -21.675 -1.763  97.466  1.00 21.47  ? 221  LEU C CB  1 
ATOM   10076 C  CG  . LEU C  1 221 ? -20.281 -2.354  97.422  1.00 23.93  ? 221  LEU C CG  1 
ATOM   10077 C  CD1 . LEU C  1 221 ? -19.275 -1.252  97.111  1.00 25.55  ? 221  LEU C CD1 1 
ATOM   10078 C  CD2 . LEU C  1 221 ? -19.968 -3.045  98.740  1.00 26.61  ? 221  LEU C CD2 1 
ATOM   10079 N  N   . PHE C  1 222 ? -24.960 -2.483  96.677  1.00 18.07  ? 222  PHE C N   1 
ATOM   10080 C  CA  . PHE C  1 222 ? -26.258 -1.823  96.514  1.00 17.71  ? 222  PHE C CA  1 
ATOM   10081 C  C   . PHE C  1 222 ? -27.252 -2.797  95.909  1.00 21.75  ? 222  PHE C C   1 
ATOM   10082 O  O   . PHE C  1 222 ? -26.862 -3.766  95.250  1.00 23.58  ? 222  PHE C O   1 
ATOM   10083 C  CB  . PHE C  1 222 ? -26.140 -0.571  95.639  1.00 16.91  ? 222  PHE C CB  1 
ATOM   10084 C  CG  . PHE C  1 222 ? -25.891 -0.866  94.180  1.00 16.62  ? 222  PHE C CG  1 
ATOM   10085 C  CD1 . PHE C  1 222 ? -24.618 -1.197  93.729  1.00 16.29  ? 222  PHE C CD1 1 
ATOM   10086 C  CD2 . PHE C  1 222 ? -26.922 -0.814  93.260  1.00 16.77  ? 222  PHE C CD2 1 
ATOM   10087 C  CE1 . PHE C  1 222 ? -24.385 -1.470  92.399  1.00 16.11  ? 222  PHE C CE1 1 
ATOM   10088 C  CE2 . PHE C  1 222 ? -26.688 -1.092  91.929  1.00 16.59  ? 222  PHE C CE2 1 
ATOM   10089 C  CZ  . PHE C  1 222 ? -25.420 -1.419  91.500  1.00 16.25  ? 222  PHE C CZ  1 
ATOM   10090 N  N   . HIS C  1 223 ? -28.527 -2.603  96.207  1.00 18.83  ? 223  HIS C N   1 
ATOM   10091 C  CA  . HIS C  1 223 ? -29.557 -3.444  95.620  1.00 20.99  ? 223  HIS C CA  1 
ATOM   10092 C  C   . HIS C  1 223 ? -30.460 -2.839  94.531  1.00 19.42  ? 223  HIS C C   1 
ATOM   10093 O  O   . HIS C  1 223 ? -31.243 -3.544  93.896  1.00 20.04  ? 223  HIS C O   1 
ATOM   10094 C  CB  . HIS C  1 223 ? -30.379 -4.024  96.742  1.00 32.61  ? 223  HIS C CB  1 
ATOM   10095 C  CG  . HIS C  1 223 ? -29.580 -4.295  97.974  1.00 35.88  ? 223  HIS C CG  1 
ATOM   10096 N  ND1 . HIS C  1 223 ? -29.131 -3.291  98.803  1.00 34.41  ? 223  HIS C ND1 1 
ATOM   10097 C  CD2 . HIS C  1 223 ? -29.141 -5.457  98.516  1.00 40.20  ? 223  HIS C CD2 1 
ATOM   10098 C  CE1 . HIS C  1 223 ? -28.453 -3.821  99.805  1.00 37.40  ? 223  HIS C CE1 1 
ATOM   10099 N  NE2 . HIS C  1 223 ? -28.447 -5.133  99.656  1.00 40.73  ? 223  HIS C NE2 1 
ATOM   10100 N  N   . ARG C  1 224 ? -30.346 -1.545  94.287  1.00 30.50  ? 224  ARG C N   1 
ATOM   10101 C  CA  . ARG C  1 224 ? -31.328 -0.908  93.429  1.00 31.97  ? 224  ARG C CA  1 
ATOM   10102 C  C   . ARG C  1 224 ? -30.792 0.332   92.762  1.00 30.78  ? 224  ARG C C   1 
ATOM   10103 O  O   . ARG C  1 224 ? -29.926 1.011   93.318  1.00 31.77  ? 224  ARG C O   1 
ATOM   10104 C  CB  . ARG C  1 224 ? -32.524 -0.511  94.262  1.00 33.85  ? 224  ARG C CB  1 
ATOM   10105 C  CG  . ARG C  1 224 ? -33.806 -0.854  93.605  1.00 38.00  ? 224  ARG C CG  1 
ATOM   10106 C  CD  . ARG C  1 224 ? -34.484 -1.909  94.406  1.00 39.81  ? 224  ARG C CD  1 
ATOM   10107 N  NE  . ARG C  1 224 ? -34.700 -1.430  95.756  1.00 39.59  ? 224  ARG C NE  1 
ATOM   10108 C  CZ  . ARG C  1 224 ? -35.413 -2.084  96.652  1.00 41.25  ? 224  ARG C CZ  1 
ATOM   10109 N  NH1 . ARG C  1 224 ? -35.958 -3.245  96.320  1.00 40.85  ? 224  ARG C NH1 1 
ATOM   10110 N  NH2 . ARG C  1 224 ? -35.568 -1.583  97.870  1.00 44.24  ? 224  ARG C NH2 1 
ATOM   10111 N  N   . ALA C  1 225 ? -31.327 0.675   91.596  1.00 17.87  ? 225  ALA C N   1 
ATOM   10112 C  CA  . ALA C  1 225 ? -30.705 1.783   90.893  1.00 17.10  ? 225  ALA C CA  1 
ATOM   10113 C  C   . ALA C  1 225 ? -31.647 2.755   90.208  1.00 17.22  ? 225  ALA C C   1 
ATOM   10114 O  O   . ALA C  1 225 ? -32.574 2.339   89.514  1.00 17.80  ? 225  ALA C O   1 
ATOM   10115 C  CB  . ALA C  1 225 ? -29.679 1.252   89.900  1.00 24.38  ? 225  ALA C CB  1 
ATOM   10116 N  N   . VAL C  1 226 ? -31.382 4.049   90.392  1.00 16.76  ? 226  VAL C N   1 
ATOM   10117 C  CA  . VAL C  1 226 ? -32.014 5.092   89.595  1.00 18.74  ? 226  VAL C CA  1 
ATOM   10118 C  C   . VAL C  1 226 ? -31.021 5.916   88.764  1.00 17.79  ? 226  VAL C C   1 
ATOM   10119 O  O   . VAL C  1 226 ? -30.088 6.556   89.302  1.00 16.79  ? 226  VAL C O   1 
ATOM   10120 C  CB  . VAL C  1 226 ? -32.903 6.023   90.435  1.00 25.13  ? 226  VAL C CB  1 
ATOM   10121 C  CG1 . VAL C  1 226 ? -33.290 7.258   89.643  1.00 25.32  ? 226  VAL C CG1 1 
ATOM   10122 C  CG2 . VAL C  1 226 ? -34.141 5.311   90.835  1.00 25.23  ? 226  VAL C CG2 1 
ATOM   10123 N  N   . LEU C  1 227 ? -31.259 5.900   87.449  1.00 16.18  ? 227  LEU C N   1 
ATOM   10124 C  CA  . LEU C  1 227 ? -30.476 6.670   86.487  1.00 15.94  ? 227  LEU C CA  1 
ATOM   10125 C  C   . LEU C  1 227 ? -31.319 7.785   85.847  1.00 15.98  ? 227  LEU C C   1 
ATOM   10126 O  O   . LEU C  1 227 ? -32.221 7.536   85.017  1.00 16.54  ? 227  LEU C O   1 
ATOM   10127 C  CB  . LEU C  1 227 ? -29.894 5.751   85.405  1.00 15.58  ? 227  LEU C CB  1 
ATOM   10128 C  CG  . LEU C  1 227 ? -28.878 4.672   85.807  1.00 15.31  ? 227  LEU C CG  1 
ATOM   10129 C  CD1 . LEU C  1 227 ? -29.550 3.454   86.358  1.00 15.88  ? 227  LEU C CD1 1 
ATOM   10130 C  CD2 . LEU C  1 227 ? -28.012 4.253   84.647  1.00 15.10  ? 227  LEU C CD2 1 
ATOM   10131 N  N   . GLN C  1 228 ? -31.013 9.019   86.238  1.00 15.84  ? 228  GLN C N   1 
ATOM   10132 C  CA  . GLN C  1 228 ? -31.711 10.181  85.703  1.00 19.17  ? 228  GLN C CA  1 
ATOM   10133 C  C   . GLN C  1 228 ? -30.853 10.917  84.669  1.00 18.74  ? 228  GLN C C   1 
ATOM   10134 O  O   . GLN C  1 228 ? -29.760 11.404  84.993  1.00 17.68  ? 228  GLN C O   1 
ATOM   10135 C  CB  . GLN C  1 228 ? -32.103 11.135  86.835  1.00 28.36  ? 228  GLN C CB  1 
ATOM   10136 C  CG  . GLN C  1 228 ? -32.797 10.456  88.027  1.00 31.91  ? 228  GLN C CG  1 
ATOM   10137 C  CD  . GLN C  1 228 ? -32.934 11.378  89.241  1.00 31.86  ? 228  GLN C CD  1 
ATOM   10138 O  OE1 . GLN C  1 228 ? -33.290 10.938  90.344  1.00 30.60  ? 228  GLN C OE1 1 
ATOM   10139 N  NE2 . GLN C  1 228 ? -32.638 12.662  89.040  1.00 29.89  ? 228  GLN C NE2 1 
ATOM   10140 N  N   . SER C  1 229 ? -31.355 10.987  83.433  1.00 16.24  ? 229  SER C N   1 
ATOM   10141 C  CA  . SER C  1 229 ? -30.713 11.715  82.328  1.00 15.88  ? 229  SER C CA  1 
ATOM   10142 C  C   . SER C  1 229 ? -29.237 11.400  82.177  1.00 15.19  ? 229  SER C C   1 
ATOM   10143 O  O   . SER C  1 229 ? -28.432 12.311  82.020  1.00 14.91  ? 229  SER C O   1 
ATOM   10144 C  CB  . SER C  1 229 ? -30.877 13.231  82.498  1.00 21.65  ? 229  SER C CB  1 
ATOM   10145 O  OG  . SER C  1 229 ? -32.169 13.567  82.979  1.00 24.46  ? 229  SER C OG  1 
ATOM   10146 N  N   . GLY C  1 230 ? -28.884 10.121  82.251  1.00 19.49  ? 230  GLY C N   1 
ATOM   10147 C  CA  . GLY C  1 230 ? -27.508 9.690   82.069  1.00 14.49  ? 230  GLY C CA  1 
ATOM   10148 C  C   . GLY C  1 230 ? -27.431 8.177   82.037  1.00 14.54  ? 230  GLY C C   1 
ATOM   10149 O  O   . GLY C  1 230 ? -28.407 7.528   82.384  1.00 14.95  ? 230  GLY C O   1 
ATOM   10150 N  N   . THR C  1 231 ? -26.267 7.627   81.682  1.00 14.22  ? 231  THR C N   1 
ATOM   10151 C  CA  . THR C  1 231 ? -26.129 6.220   81.291  1.00 14.46  ? 231  THR C CA  1 
ATOM   10152 C  C   . THR C  1 231 ? -24.653 5.920   81.072  1.00 14.02  ? 231  THR C C   1 
ATOM   10153 O  O   . THR C  1 231 ? -23.948 6.760   80.533  1.00 18.76  ? 231  THR C O   1 
ATOM   10154 C  CB  . THR C  1 231 ? -26.786 5.957   79.903  1.00 26.89  ? 231  THR C CB  1 
ATOM   10155 O  OG1 . THR C  1 231 ? -26.685 7.141   79.097  1.00 25.35  ? 231  THR C OG1 1 
ATOM   10156 C  CG2 . THR C  1 231 ? -28.240 5.524   80.010  1.00 15.55  ? 231  THR C CG2 1 
ATOM   10157 N  N   . PRO C  1 232 ? -24.191 4.710   81.458  1.00 21.96  ? 232  PRO C N   1 
ATOM   10158 C  CA  . PRO C  1 232 ? -22.804 4.290   81.265  1.00 13.82  ? 232  PRO C CA  1 
ATOM   10159 C  C   . PRO C  1 232 ? -22.519 4.004   79.802  1.00 14.07  ? 232  PRO C C   1 
ATOM   10160 O  O   . PRO C  1 232 ? -21.365 4.047   79.393  1.00 13.91  ? 232  PRO C O   1 
ATOM   10161 C  CB  . PRO C  1 232 ? -22.718 3.005   82.077  1.00 13.99  ? 232  PRO C CB  1 
ATOM   10162 C  CG  . PRO C  1 232 ? -24.034 2.411   81.914  1.00 23.55  ? 232  PRO C CG  1 
ATOM   10163 C  CD  . PRO C  1 232 ? -25.005 3.588   81.955  1.00 24.31  ? 232  PRO C CD  1 
ATOM   10164 N  N   . ASN C  1 233 ? -23.542 3.704   79.013  1.00 14.53  ? 233  ASN C N   1 
ATOM   10165 C  CA  . ASN C  1 233 ? -23.310 3.532   77.589  1.00 21.20  ? 233  ASN C CA  1 
ATOM   10166 C  C   . ASN C  1 233 ? -23.454 4.878   76.915  1.00 26.92  ? 233  ASN C C   1 
ATOM   10167 O  O   . ASN C  1 233 ? -23.810 5.861   77.574  1.00 29.29  ? 233  ASN C O   1 
ATOM   10168 C  CB  . ASN C  1 233 ? -24.280 2.517   76.982  1.00 24.33  ? 233  ASN C CB  1 
ATOM   10169 C  CG  . ASN C  1 233 ? -25.715 2.778   77.373  1.00 26.41  ? 233  ASN C CG  1 
ATOM   10170 O  OD1 . ASN C  1 233 ? -25.985 3.273   78.461  1.00 25.51  ? 233  ASN C OD1 1 
ATOM   10171 N  ND2 . ASN C  1 233 ? -26.647 2.443   76.484  1.00 29.28  ? 233  ASN C ND2 1 
ATOM   10172 N  N   . GLY C  1 234 ? -23.196 4.924   75.609  1.00 37.56  ? 234  GLY C N   1 
ATOM   10173 C  CA  . GLY C  1 234 ? -23.346 6.157   74.856  1.00 37.04  ? 234  GLY C CA  1 
ATOM   10174 C  C   . GLY C  1 234 ? -22.063 6.948   74.661  1.00 34.69  ? 234  GLY C C   1 
ATOM   10175 O  O   . GLY C  1 234 ? -21.020 6.591   75.201  1.00 39.52  ? 234  GLY C O   1 
ATOM   10176 N  N   . PRO C  1 235 ? -22.152 8.060   73.919  1.00 15.92  ? 235  PRO C N   1 
ATOM   10177 C  CA  . PRO C  1 235 ? -21.033 8.822   73.368  1.00 14.95  ? 235  PRO C CA  1 
ATOM   10178 C  C   . PRO C  1 235 ? -20.049 9.428   74.371  1.00 14.42  ? 235  PRO C C   1 
ATOM   10179 O  O   . PRO C  1 235 ? -18.854 9.319   74.147  1.00 14.37  ? 235  PRO C O   1 
ATOM   10180 C  CB  . PRO C  1 235 ? -21.732 9.942   72.597  1.00 15.35  ? 235  PRO C CB  1 
ATOM   10181 C  CG  . PRO C  1 235 ? -23.023 10.115  73.272  1.00 15.37  ? 235  PRO C CG  1 
ATOM   10182 C  CD  . PRO C  1 235 ? -23.432 8.750   73.703  1.00 15.34  ? 235  PRO C CD  1 
ATOM   10183 N  N   . TRP C  1 236 ? -20.533 10.080  75.423  1.00 14.14  ? 236  TRP C N   1 
ATOM   10184 C  CA  . TRP C  1 236 ? -19.677 10.887  76.297  1.00 13.77  ? 236  TRP C CA  1 
ATOM   10185 C  C   . TRP C  1 236 ? -19.142 10.266  77.586  1.00 18.88  ? 236  TRP C C   1 
ATOM   10186 O  O   . TRP C  1 236 ? -18.253 10.840  78.201  1.00 13.14  ? 236  TRP C O   1 
ATOM   10187 C  CB  . TRP C  1 236 ? -20.437 12.145  76.689  1.00 15.29  ? 236  TRP C CB  1 
ATOM   10188 C  CG  . TRP C  1 236 ? -21.743 11.815  77.327  1.00 13.84  ? 236  TRP C CG  1 
ATOM   10189 C  CD1 . TRP C  1 236 ? -22.940 11.632  76.696  1.00 15.97  ? 236  TRP C CD1 1 
ATOM   10190 C  CD2 . TRP C  1 236 ? -21.986 11.597  78.722  1.00 16.78  ? 236  TRP C CD2 1 
ATOM   10191 N  NE1 . TRP C  1 236 ? -23.913 11.313  77.611  1.00 16.46  ? 236  TRP C NE1 1 
ATOM   10192 C  CE2 . TRP C  1 236 ? -23.355 11.289  78.863  1.00 17.23  ? 236  TRP C CE2 1 
ATOM   10193 C  CE3 . TRP C  1 236 ? -21.180 11.629  79.864  1.00 13.14  ? 236  TRP C CE3 1 
ATOM   10194 C  CZ2 . TRP C  1 236 ? -23.937 11.026  80.099  1.00 19.12  ? 236  TRP C CZ2 1 
ATOM   10195 C  CZ3 . TRP C  1 236 ? -21.750 11.374  81.082  1.00 19.79  ? 236  TRP C CZ3 1 
ATOM   10196 C  CH2 . TRP C  1 236 ? -23.120 11.083  81.197  1.00 20.59  ? 236  TRP C CH2 1 
ATOM   10197 N  N   . ALA C  1 237 ? -19.659 9.123   78.010  1.00 13.32  ? 237  ALA C N   1 
ATOM   10198 C  CA  . ALA C  1 237 ? -19.354 8.673   79.361  1.00 13.00  ? 237  ALA C CA  1 
ATOM   10199 C  C   . ALA C  1 237 ? -18.025 7.910   79.590  1.00 16.99  ? 237  ALA C C   1 
ATOM   10200 O  O   . ALA C  1 237 ? -17.553 7.832   80.731  1.00 15.95  ? 237  ALA C O   1 
ATOM   10201 C  CB  . ALA C  1 237 ? -20.503 7.912   79.924  1.00 13.09  ? 237  ALA C CB  1 
ATOM   10202 N  N   . THR C  1 238 ? -17.427 7.337   78.541  1.00 20.01  ? 238  THR C N   1 
ATOM   10203 C  CA  . THR C  1 238 ? -16.163 6.586   78.693  1.00 17.49  ? 238  THR C CA  1 
ATOM   10204 C  C   . THR C  1 238 ? -15.135 6.878   77.603  1.00 16.81  ? 238  THR C C   1 
ATOM   10205 O  O   . THR C  1 238 ? -15.436 7.546   76.622  1.00 16.52  ? 238  THR C O   1 
ATOM   10206 C  CB  . THR C  1 238 ? -16.363 5.050   78.784  1.00 26.05  ? 238  THR C CB  1 
ATOM   10207 O  OG1 . THR C  1 238 ? -16.833 4.538   77.532  1.00 23.77  ? 238  THR C OG1 1 
ATOM   10208 C  CG2 . THR C  1 238 ? -17.358 4.698   79.880  1.00 29.26  ? 238  THR C CG2 1 
ATOM   10209 N  N   . VAL C  1 239 ? -13.910 6.410   77.786  1.00 13.51  ? 239  VAL C N   1 
ATOM   10210 C  CA  . VAL C  1 239 ? -12.924 6.542   76.723  1.00 19.14  ? 239  VAL C CA  1 
ATOM   10211 C  C   . VAL C  1 239 ? -12.084 5.291   76.529  1.00 19.92  ? 239  VAL C C   1 
ATOM   10212 O  O   . VAL C  1 239 ? -11.775 4.573   77.504  1.00 15.83  ? 239  VAL C O   1 
ATOM   10213 C  CB  . VAL C  1 239 ? -11.969 7.749   76.905  1.00 13.82  ? 239  VAL C CB  1 
ATOM   10214 C  CG1 . VAL C  1 239 ? -12.634 9.019   76.445  1.00 14.38  ? 239  VAL C CG1 1 
ATOM   10215 C  CG2 . VAL C  1 239 ? -11.478 7.853   78.328  1.00 13.55  ? 239  VAL C CG2 1 
ATOM   10216 N  N   . SER C  1 240 ? -11.722 5.059   75.258  1.00 25.36  ? 240  SER C N   1 
ATOM   10217 C  CA  . SER C  1 240 ? -10.786 4.021   74.859  1.00 30.34  ? 240  SER C CA  1 
ATOM   10218 C  C   . SER C  1 240 ? -9.560  4.175   75.718  1.00 26.10  ? 240  SER C C   1 
ATOM   10219 O  O   . SER C  1 240 ? -9.126  5.297   75.963  1.00 31.51  ? 240  SER C O   1 
ATOM   10220 C  CB  . SER C  1 240 ? -10.390 4.240   73.403  1.00 66.03  ? 240  SER C CB  1 
ATOM   10221 O  OG  . SER C  1 240 ? -9.016  3.942   73.185  1.00 74.07  ? 240  SER C OG  1 
ATOM   10222 N  N   . ALA C  1 241 ? -9.005  3.072   76.205  1.00 24.75  ? 241  ALA C N   1 
ATOM   10223 C  CA  . ALA C  1 241 ? -7.843  3.184   77.088  1.00 27.51  ? 241  ALA C CA  1 
ATOM   10224 C  C   . ALA C  1 241 ? -6.703  3.851   76.361  1.00 15.80  ? 241  ALA C C   1 
ATOM   10225 O  O   . ALA C  1 241 ? -5.975  4.658   76.929  1.00 23.51  ? 241  ALA C O   1 
ATOM   10226 C  CB  . ALA C  1 241 ? -7.418  1.843   77.606  1.00 16.79  ? 241  ALA C CB  1 
ATOM   10227 N  N   . GLY C  1 242 ? -6.566  3.535   75.086  1.00 23.91  ? 242  GLY C N   1 
ATOM   10228 C  CA  . GLY C  1 242 ? -5.563  4.193   74.282  1.00 27.52  ? 242  GLY C CA  1 
ATOM   10229 C  C   . GLY C  1 242 ? -5.707  5.704   74.290  1.00 28.48  ? 242  GLY C C   1 
ATOM   10230 O  O   . GLY C  1 242 ? -4.710  6.423   74.395  1.00 33.84  ? 242  GLY C O   1 
ATOM   10231 N  N   . GLU C  1 243 ? -6.949  6.175   74.181  1.00 20.25  ? 243  GLU C N   1 
ATOM   10232 C  CA  . GLU C  1 243 ? -7.256  7.600   74.173  1.00 18.79  ? 243  GLU C CA  1 
ATOM   10233 C  C   . GLU C  1 243 ? -7.063  8.238   75.539  1.00 20.61  ? 243  GLU C C   1 
ATOM   10234 O  O   . GLU C  1 243 ? -6.561  9.351   75.644  1.00 19.33  ? 243  GLU C O   1 
ATOM   10235 C  CB  . GLU C  1 243 ? -8.690  7.829   73.732  1.00 17.86  ? 243  GLU C CB  1 
ATOM   10236 C  CG  . GLU C  1 243 ? -9.115  9.272   73.820  1.00 19.86  ? 243  GLU C CG  1 
ATOM   10237 C  CD  . GLU C  1 243 ? -8.713  10.081  72.602  1.00 24.78  ? 243  GLU C CD  1 
ATOM   10238 O  OE1 . GLU C  1 243 ? -7.737  9.704   71.883  1.00 26.67  ? 243  GLU C OE1 1 
ATOM   10239 O  OE2 . GLU C  1 243 ? -9.400  11.102  72.370  1.00 25.00  ? 243  GLU C OE2 1 
ATOM   10240 N  N   . ALA C  1 244 ? -7.491  7.543   76.584  1.00 27.62  ? 244  ALA C N   1 
ATOM   10241 C  CA  . ALA C  1 244 ? -7.218  7.997   77.933  1.00 28.32  ? 244  ALA C CA  1 
ATOM   10242 C  C   . ALA C  1 244 ? -5.718  8.285   78.023  1.00 29.20  ? 244  ALA C C   1 
ATOM   10243 O  O   . ALA C  1 244 ? -5.290  9.334   78.542  1.00 31.21  ? 244  ALA C O   1 
ATOM   10244 C  CB  . ALA C  1 244 ? -7.633  6.935   78.935  1.00 23.82  ? 244  ALA C CB  1 
ATOM   10245 N  N   . ARG C  1 245 ? -4.929  7.369   77.462  1.00 21.67  ? 245  ARG C N   1 
ATOM   10246 C  CA  . ARG C  1 245 ? -3.485  7.528   77.442  1.00 21.41  ? 245  ARG C CA  1 
ATOM   10247 C  C   . ARG C  1 245 ? -3.083  8.745   76.626  1.00 24.64  ? 245  ARG C C   1 
ATOM   10248 O  O   . ARG C  1 245 ? -2.180  9.497   77.015  1.00 26.14  ? 245  ARG C O   1 
ATOM   10249 C  CB  . ARG C  1 245 ? -2.801  6.279   76.888  1.00 20.56  ? 245  ARG C CB  1 
ATOM   10250 C  CG  . ARG C  1 245 ? -1.300  6.451   76.658  1.00 22.42  ? 245  ARG C CG  1 
ATOM   10251 C  CD  . ARG C  1 245 ? -0.614  5.107   76.469  1.00 24.97  ? 245  ARG C CD  1 
ATOM   10252 N  NE  . ARG C  1 245 ? -0.583  4.334   77.704  1.00 25.81  ? 245  ARG C NE  1 
ATOM   10253 C  CZ  . ARG C  1 245 ? 0.367   4.472   78.625  1.00 30.21  ? 245  ARG C CZ  1 
ATOM   10254 N  NH1 . ARG C  1 245 ? 1.356   5.343   78.429  1.00 32.56  ? 245  ARG C NH1 1 
ATOM   10255 N  NH2 . ARG C  1 245 ? 0.332   3.748   79.739  1.00 31.15  ? 245  ARG C NH2 1 
ATOM   10256 N  N   . ARG C  1 246 ? -3.764  8.933   75.499  1.00 30.60  ? 246  ARG C N   1 
ATOM   10257 C  CA  . ARG C  1 246 ? -3.436  9.992   74.555  1.00 32.41  ? 246  ARG C CA  1 
ATOM   10258 C  C   . ARG C  1 246 ? -3.541  11.321  75.254  1.00 33.83  ? 246  ARG C C   1 
ATOM   10259 O  O   . ARG C  1 246 ? -2.583  12.098  75.306  1.00 35.08  ? 246  ARG C O   1 
ATOM   10260 C  CB  . ARG C  1 246 ? -4.426  9.974   73.388  1.00 29.23  ? 246  ARG C CB  1 
ATOM   10261 C  CG  . ARG C  1 246 ? -3.881  10.511  72.079  1.00 32.20  ? 246  ARG C CG  1 
ATOM   10262 C  CD  . ARG C  1 246 ? -4.209  11.960  71.831  1.00 32.27  ? 246  ARG C CD  1 
ATOM   10263 N  NE  . ARG C  1 246 ? -5.647  12.183  71.825  1.00 33.99  ? 246  ARG C NE  1 
ATOM   10264 C  CZ  . ARG C  1 246 ? -6.202  13.381  71.675  1.00 41.20  ? 246  ARG C CZ  1 
ATOM   10265 N  NH1 . ARG C  1 246 ? -5.425  14.450  71.490  1.00 46.21  ? 246  ARG C NH1 1 
ATOM   10266 N  NH2 . ARG C  1 246 ? -7.526  13.514  71.703  1.00 40.90  ? 246  ARG C NH2 1 
ATOM   10267 N  N   . ARG C  1 247 ? -4.723  11.550  75.807  1.00 16.14  ? 247  ARG C N   1 
ATOM   10268 C  CA  . ARG C  1 247 ? -5.089  12.821  76.357  1.00 15.95  ? 247  ARG C CA  1 
ATOM   10269 C  C   . ARG C  1 247 ? -4.249  13.073  77.567  1.00 16.02  ? 247  ARG C C   1 
ATOM   10270 O  O   . ARG C  1 247 ? -3.761  14.172  77.758  1.00 16.34  ? 247  ARG C O   1 
ATOM   10271 C  CB  . ARG C  1 247 ? -6.560  12.811  76.734  1.00 37.03  ? 247  ARG C CB  1 
ATOM   10272 C  CG  . ARG C  1 247 ? -7.484  12.463  75.595  1.00 15.28  ? 247  ARG C CG  1 
ATOM   10273 C  CD  . ARG C  1 247 ? -8.885  12.703  76.006  1.00 14.77  ? 247  ARG C CD  1 
ATOM   10274 N  NE  . ARG C  1 247 ? -9.832  12.338  74.968  1.00 14.82  ? 247  ARG C NE  1 
ATOM   10275 C  CZ  . ARG C  1 247 ? -11.153 12.457  75.097  1.00 14.52  ? 247  ARG C CZ  1 
ATOM   10276 N  NH1 . ARG C  1 247 ? -11.662 12.935  76.229  1.00 14.13  ? 247  ARG C NH1 1 
ATOM   10277 N  NH2 . ARG C  1 247 ? -11.965 12.095  74.101  1.00 14.67  ? 247  ARG C NH2 1 
ATOM   10278 N  N   . ALA C  1 248 ? -4.067  12.052  78.394  1.00 22.93  ? 248  ALA C N   1 
ATOM   10279 C  CA  . ALA C  1 248 ? -3.222  12.215  79.580  1.00 20.69  ? 248  ALA C CA  1 
ATOM   10280 C  C   . ALA C  1 248 ? -1.774  12.622  79.216  1.00 17.53  ? 248  ALA C C   1 
ATOM   10281 O  O   . ALA C  1 248 ? -1.162  13.485  79.862  1.00 17.10  ? 248  ALA C O   1 
ATOM   10282 C  CB  . ALA C  1 248 ? -3.262  10.952  80.437  1.00 15.73  ? 248  ALA C CB  1 
ATOM   10283 N  N   . THR C  1 249 ? -1.247  12.032  78.152  1.00 17.23  ? 249  THR C N   1 
ATOM   10284 C  CA  . THR C  1 249 ? 0.099   12.368  77.732  1.00 20.95  ? 249  THR C CA  1 
ATOM   10285 C  C   . THR C  1 249 ? 0.179   13.763  77.148  1.00 23.30  ? 249  THR C C   1 
ATOM   10286 O  O   . THR C  1 249 ? 1.119   14.505  77.431  1.00 22.95  ? 249  THR C O   1 
ATOM   10287 C  CB  . THR C  1 249 ? 0.640   11.411  76.690  1.00 18.61  ? 249  THR C CB  1 
ATOM   10288 O  OG1 . THR C  1 249 ? 0.432   10.061  77.117  1.00 18.88  ? 249  THR C OG1 1 
ATOM   10289 C  CG2 . THR C  1 249 ? 2.117   11.660  76.540  1.00 19.59  ? 249  THR C CG2 1 
ATOM   10290 N  N   . LEU C  1 250 ? -0.788  14.113  76.311  1.00 31.94  ? 250  LEU C N   1 
ATOM   10291 C  CA  . LEU C  1 250 ? -0.816  15.446  75.724  1.00 32.76  ? 250  LEU C CA  1 
ATOM   10292 C  C   . LEU C  1 250 ? -0.900  16.480  76.829  1.00 33.75  ? 250  LEU C C   1 
ATOM   10293 O  O   . LEU C  1 250 ? -0.286  17.536  76.736  1.00 37.92  ? 250  LEU C O   1 
ATOM   10294 C  CB  . LEU C  1 250 ? -1.977  15.602  74.739  1.00 26.02  ? 250  LEU C CB  1 
ATOM   10295 C  CG  . LEU C  1 250 ? -2.427  17.019  74.402  1.00 18.50  ? 250  LEU C CG  1 
ATOM   10296 C  CD1 . LEU C  1 250 ? -1.318  17.776  73.749  1.00 19.50  ? 250  LEU C CD1 1 
ATOM   10297 C  CD2 . LEU C  1 250 ? -3.633  16.980  73.499  1.00 18.23  ? 250  LEU C CD2 1 
ATOM   10298 N  N   . LEU C  1 251 ? -1.640  16.173  77.887  1.00 19.40  ? 251  LEU C N   1 
ATOM   10299 C  CA  . LEU C  1 251 ? -1.759  17.121  78.985  1.00 18.32  ? 251  LEU C CA  1 
ATOM   10300 C  C   . LEU C  1 251 ? -0.421  17.265  79.686  1.00 18.29  ? 251  LEU C C   1 
ATOM   10301 O  O   . LEU C  1 251 ? 0.030   18.382  79.928  1.00 18.83  ? 251  LEU C O   1 
ATOM   10302 C  CB  . LEU C  1 251 ? -2.834  16.717  79.991  1.00 18.17  ? 251  LEU C CB  1 
ATOM   10303 C  CG  . LEU C  1 251 ? -2.889  17.748  81.110  1.00 16.89  ? 251  LEU C CG  1 
ATOM   10304 C  CD1 . LEU C  1 251 ? -4.208  18.434  81.077  1.00 16.56  ? 251  LEU C CD1 1 
ATOM   10305 C  CD2 . LEU C  1 251 ? -2.648  17.104  82.438  1.00 16.66  ? 251  LEU C CD2 1 
ATOM   10306 N  N   . ALA C  1 252 ? 0.219   16.141  80.006  1.00 25.81  ? 252  ALA C N   1 
ATOM   10307 C  CA  . ALA C  1 252 ? 1.545   16.217  80.614  1.00 27.42  ? 252  ALA C CA  1 
ATOM   10308 C  C   . ALA C  1 252 ? 2.486   17.058  79.750  1.00 29.94  ? 252  ALA C C   1 
ATOM   10309 O  O   . ALA C  1 252 ? 3.268   17.834  80.284  1.00 31.36  ? 252  ALA C O   1 
ATOM   10310 C  CB  . ALA C  1 252 ? 2.117   14.842  80.875  1.00 23.98  ? 252  ALA C CB  1 
ATOM   10311 N  N   . ARG C  1 253 ? 2.386   16.924  78.424  1.00 22.60  ? 253  ARG C N   1 
ATOM   10312 C  CA  . ARG C  1 253 ? 3.131   17.777  77.495  1.00 25.67  ? 253  ARG C CA  1 
ATOM   10313 C  C   . ARG C  1 253 ? 2.818   19.247  77.753  1.00 21.33  ? 253  ARG C C   1 
ATOM   10314 O  O   . ARG C  1 253 ? 3.688   20.006  78.152  1.00 22.12  ? 253  ARG C O   1 
ATOM   10315 C  CB  . ARG C  1 253 ? 2.832   17.419  76.037  1.00 60.64  ? 253  ARG C CB  1 
ATOM   10316 C  CG  . ARG C  1 253 ? 4.035   17.577  75.101  1.00 76.50  ? 253  ARG C CG  1 
ATOM   10317 C  CD  . ARG C  1 253 ? 3.653   17.553  73.611  1.00 89.48  ? 253  ARG C CD  1 
ATOM   10318 N  NE  . ARG C  1 253 ? 3.365   18.888  73.076  1.00 98.80  ? 253  ARG C NE  1 
ATOM   10319 C  CZ  . ARG C  1 253 ? 4.294   19.729  72.625  1.00 104.00 ? 253  ARG C CZ  1 
ATOM   10320 N  NH1 . ARG C  1 253 ? 5.576   19.373  72.641  1.00 105.00 ? 253  ARG C NH1 1 
ATOM   10321 N  NH2 . ARG C  1 253 ? 3.944   20.923  72.160  1.00 104.47 ? 253  ARG C NH2 1 
ATOM   10322 N  N   . LEU C  1 254 ? 1.567   19.639  77.551  1.00 20.68  ? 254  LEU C N   1 
ATOM   10323 C  CA  . LEU C  1 254 ? 1.153   21.032  77.717  1.00 20.91  ? 254  LEU C CA  1 
ATOM   10324 C  C   . LEU C  1 254 ? 1.537   21.683  79.056  1.00 29.31  ? 254  LEU C C   1 
ATOM   10325 O  O   . LEU C  1 254 ? 1.728   22.900  79.127  1.00 29.67  ? 254  LEU C O   1 
ATOM   10326 C  CB  . LEU C  1 254 ? -0.349  21.159  77.493  1.00 20.11  ? 254  LEU C CB  1 
ATOM   10327 C  CG  . LEU C  1 254 ? -0.788  20.652  76.133  1.00 20.02  ? 254  LEU C CG  1 
ATOM   10328 C  CD1 . LEU C  1 254 ? -2.288  20.636  76.005  1.00 30.57  ? 254  LEU C CD1 1 
ATOM   10329 C  CD2 . LEU C  1 254 ? -0.195  21.550  75.115  1.00 21.02  ? 254  LEU C CD2 1 
ATOM   10330 N  N   . VAL C  1 255 ? 1.649   20.895  80.116  1.00 20.68  ? 255  VAL C N   1 
ATOM   10331 C  CA  . VAL C  1 255 ? 2.047   21.460  81.407  1.00 22.56  ? 255  VAL C CA  1 
ATOM   10332 C  C   . VAL C  1 255 ? 3.553   21.403  81.649  1.00 25.60  ? 255  VAL C C   1 
ATOM   10333 O  O   . VAL C  1 255 ? 4.019   21.587  82.782  1.00 24.51  ? 255  VAL C O   1 
ATOM   10334 C  CB  . VAL C  1 255 ? 1.289   20.889  82.619  1.00 24.95  ? 255  VAL C CB  1 
ATOM   10335 C  CG1 . VAL C  1 255 ? -0.185  21.234  82.531  1.00 25.05  ? 255  VAL C CG1 1 
ATOM   10336 C  CG2 . VAL C  1 255 ? 1.533   19.396  82.756  1.00 24.60  ? 255  VAL C CG2 1 
ATOM   10337 N  N   . GLY C  1 256 ? 4.306   21.075  80.605  1.00 33.93  ? 256  GLY C N   1 
ATOM   10338 C  CA  . GLY C  1 256 ? 5.755   21.058  80.708  1.00 36.92  ? 256  GLY C CA  1 
ATOM   10339 C  C   . GLY C  1 256 ? 6.306   19.833  81.407  1.00 37.32  ? 256  GLY C C   1 
ATOM   10340 O  O   . GLY C  1 256 ? 7.100   19.945  82.339  1.00 38.34  ? 256  GLY C O   1 
ATOM   10341 N  N   . CYS C  1 257 ? 5.869   18.660  80.960  1.00 31.23  ? 257  CYS C N   1 
ATOM   10342 C  CA  . CYS C  1 257 ? 6.335   17.406  81.533  1.00 34.99  ? 257  CYS C CA  1 
ATOM   10343 C  C   . CYS C  1 257 ? 6.869   16.404  80.502  1.00 45.13  ? 257  CYS C C   1 
ATOM   10344 O  O   . CYS C  1 257 ? 6.406   15.259  80.421  1.00 39.77  ? 257  CYS C O   1 
ATOM   10345 C  CB  . CYS C  1 257 ? 5.200   16.757  82.329  1.00 36.80  ? 257  CYS C CB  1 
ATOM   10346 S  SG  . CYS C  1 257 ? 5.268   17.094  84.071  1.00 56.95  ? 257  CYS C SG  1 
ATOM   10347 N  N   . PRO C  1 258 ? 7.851   16.814  79.695  1.00 83.25  ? 258  PRO C N   1 
ATOM   10348 C  CA  . PRO C  1 258 ? 8.512   15.579  79.276  1.00 89.62  ? 258  PRO C CA  1 
ATOM   10349 C  C   . PRO C  1 258 ? 9.259   14.991  80.502  1.00 142.42 ? 258  PRO C C   1 
ATOM   10350 O  O   . PRO C  1 258 ? 9.117   13.787  80.721  1.00 142.78 ? 258  PRO C O   1 
ATOM   10351 C  CB  . PRO C  1 258 ? 9.386   16.012  78.092  1.00 103.47 ? 258  PRO C CB  1 
ATOM   10352 C  CG  . PRO C  1 258 ? 8.729   17.303  77.595  1.00 104.17 ? 258  PRO C CG  1 
ATOM   10353 C  CD  . PRO C  1 258 ? 8.139   17.961  78.813  1.00 99.35  ? 258  PRO C CD  1 
ATOM   10354 N  N   . PRO C  1 259 ? 9.999   15.815  81.300  1.00 135.68 ? 259  PRO C N   1 
ATOM   10355 C  CA  . PRO C  1 259 ? 10.790  17.006  80.935  1.00 136.99 ? 259  PRO C CA  1 
ATOM   10356 C  C   . PRO C  1 259 ? 12.039  16.581  80.134  1.00 141.22 ? 259  PRO C C   1 
ATOM   10357 O  O   . PRO C  1 259 ? 12.828  15.742  80.582  1.00 141.83 ? 259  PRO C O   1 
ATOM   10358 C  CB  . PRO C  1 259 ? 11.168  17.610  82.292  1.00 113.25 ? 259  PRO C CB  1 
ATOM   10359 C  CG  . PRO C  1 259 ? 10.100  17.137  83.219  1.00 110.87 ? 259  PRO C CG  1 
ATOM   10360 C  CD  . PRO C  1 259 ? 9.805   15.737  82.761  1.00 111.43 ? 259  PRO C CD  1 
ATOM   10361 N  N   . GLY C  1 260 ? 12.215  17.182  78.960  1.00 145.00 ? 260  GLY C N   1 
ATOM   10362 C  CA  . GLY C  1 260 ? 13.117  16.645  77.956  1.00 145.46 ? 260  GLY C CA  1 
ATOM   10363 C  C   . GLY C  1 260 ? 12.503  16.931  76.595  1.00 144.91 ? 260  GLY C C   1 
ATOM   10364 O  O   . GLY C  1 260 ? 11.757  17.901  76.431  1.00 145.48 ? 260  GLY C O   1 
ATOM   10365 N  N   . GLY C  1 261 ? 12.855  16.124  75.600  1.00 131.95 ? 261  GLY C N   1 
ATOM   10366 C  CA  . GLY C  1 261 ? 12.039  16.015  74.402  1.00 129.98 ? 261  GLY C CA  1 
ATOM   10367 C  C   . GLY C  1 261 ? 10.810  15.121  74.566  1.00 126.65 ? 261  GLY C C   1 
ATOM   10368 O  O   . GLY C  1 261 ? 9.691   15.509  74.216  1.00 123.64 ? 261  GLY C O   1 
ATOM   10369 N  N   . ALA C  1 262 ? 11.023  13.929  75.129  1.00 134.33 ? 262  ALA C N   1 
ATOM   10370 C  CA  . ALA C  1 262 ? 10.016  12.863  75.138  1.00 129.99 ? 262  ALA C CA  1 
ATOM   10371 C  C   . ALA C  1 262 ? 9.407   12.556  76.512  1.00 129.16 ? 262  ALA C C   1 
ATOM   10372 O  O   . ALA C  1 262 ? 8.241   12.876  76.756  1.00 129.19 ? 262  ALA C O   1 
ATOM   10373 C  CB  . ALA C  1 262 ? 10.585  11.584  74.510  1.00 112.21 ? 262  ALA C CB  1 
ATOM   10374 N  N   . GLY C  1 263 ? 10.199  11.986  77.422  1.00 124.18 ? 263  GLY C N   1 
ATOM   10375 C  CA  . GLY C  1 263 ? 9.653   11.423  78.652  1.00 121.89 ? 263  GLY C CA  1 
ATOM   10376 C  C   . GLY C  1 263 ? 8.966   10.068  78.506  1.00 118.76 ? 263  GLY C C   1 
ATOM   10377 O  O   . GLY C  1 263 ? 7.793   9.894   78.873  1.00 115.95 ? 263  GLY C O   1 
ATOM   10378 N  N   . GLY C  1 264 ? 9.722   9.106   77.974  1.00 128.97 ? 264  GLY C N   1 
ATOM   10379 C  CA  . GLY C  1 264 ? 9.239   7.777   77.618  1.00 125.23 ? 264  GLY C CA  1 
ATOM   10380 C  C   . GLY C  1 264 ? 9.097   6.751   78.740  1.00 119.80 ? 264  GLY C C   1 
ATOM   10381 O  O   . GLY C  1 264 ? 9.165   5.544   78.493  1.00 120.91 ? 264  GLY C O   1 
ATOM   10382 N  N   . ASN C  1 265 ? 8.961   7.230   79.975  1.00 93.06  ? 265  ASN C N   1 
ATOM   10383 C  CA  . ASN C  1 265 ? 8.729   6.379   81.141  1.00 82.78  ? 265  ASN C CA  1 
ATOM   10384 C  C   . ASN C  1 265 ? 7.423   6.790   81.832  1.00 70.06  ? 265  ASN C C   1 
ATOM   10385 O  O   . ASN C  1 265 ? 7.265   7.951   82.190  1.00 70.53  ? 265  ASN C O   1 
ATOM   10386 C  CB  . ASN C  1 265 ? 9.908   6.532   82.102  1.00 88.52  ? 265  ASN C CB  1 
ATOM   10387 C  CG  . ASN C  1 265 ? 10.007  5.403   83.105  1.00 92.74  ? 265  ASN C CG  1 
ATOM   10388 O  OD1 . ASN C  1 265 ? 9.023   5.033   83.751  1.00 92.17  ? 265  ASN C OD1 1 
ATOM   10389 N  ND2 . ASN C  1 265 ? 11.210  4.845   83.241  1.00 97.56  ? 265  ASN C ND2 1 
ATOM   10390 N  N   . ASP C  1 266 ? 6.494   5.850   82.014  1.00 55.02  ? 266  ASP C N   1 
ATOM   10391 C  CA  . ASP C  1 266 ? 5.169   6.143   82.602  1.00 46.10  ? 266  ASP C CA  1 
ATOM   10392 C  C   . ASP C  1 266 ? 5.255   6.687   84.022  1.00 41.97  ? 266  ASP C C   1 
ATOM   10393 O  O   . ASP C  1 266 ? 4.494   7.591   84.424  1.00 40.83  ? 266  ASP C O   1 
ATOM   10394 C  CB  . ASP C  1 266 ? 4.280   4.890   82.619  1.00 45.22  ? 266  ASP C CB  1 
ATOM   10395 C  CG  . ASP C  1 266 ? 3.151   4.948   81.593  1.00 41.76  ? 266  ASP C CG  1 
ATOM   10396 O  OD1 . ASP C  1 266 ? 3.215   5.775   80.659  1.00 43.04  ? 266  ASP C OD1 1 
ATOM   10397 O  OD2 . ASP C  1 266 ? 2.203   4.145   81.711  1.00 38.31  ? 266  ASP C OD2 1 
ATOM   10398 N  N   . THR C  1 267 ? 6.177   6.114   84.786  1.00 44.24  ? 267  THR C N   1 
ATOM   10399 C  CA  . THR C  1 267 ? 6.377   6.543   86.152  1.00 39.03  ? 267  THR C CA  1 
ATOM   10400 C  C   . THR C  1 267 ? 6.816   7.986   86.150  1.00 39.26  ? 267  THR C C   1 
ATOM   10401 O  O   . THR C  1 267 ? 6.299   8.780   86.912  1.00 40.93  ? 267  THR C O   1 
ATOM   10402 C  CB  . THR C  1 267 ? 7.426   5.706   86.878  1.00 36.96  ? 267  THR C CB  1 
ATOM   10403 O  OG1 . THR C  1 267 ? 6.939   4.371   87.029  1.00 35.62  ? 267  THR C OG1 1 
ATOM   10404 C  CG2 . THR C  1 267 ? 7.674   6.282   88.255  1.00 39.10  ? 267  THR C CG2 1 
ATOM   10405 N  N   . GLU C  1 268 ? 7.754   8.335   85.277  1.00 37.37  ? 268  GLU C N   1 
ATOM   10406 C  CA  . GLU C  1 268 ? 8.287   9.692   85.292  1.00 38.82  ? 268  GLU C CA  1 
ATOM   10407 C  C   . GLU C  1 268 ? 7.250   10.719  84.894  1.00 30.28  ? 268  GLU C C   1 
ATOM   10408 O  O   . GLU C  1 268 ? 7.128   11.768  85.535  1.00 27.19  ? 268  GLU C O   1 
ATOM   10409 C  CB  . GLU C  1 268 ? 9.562   9.810   84.459  1.00 67.88  ? 268  GLU C CB  1 
ATOM   10410 C  CG  . GLU C  1 268 ? 10.775  9.279   85.210  1.00 80.46  ? 268  GLU C CG  1 
ATOM   10411 C  CD  . GLU C  1 268 ? 10.679  9.498   86.731  1.00 89.14  ? 268  GLU C CD  1 
ATOM   10412 O  OE1 . GLU C  1 268 ? 10.598  10.670  87.174  1.00 91.88  ? 268  GLU C OE1 1 
ATOM   10413 O  OE2 . GLU C  1 268 ? 10.682  8.492   87.482  1.00 90.71  ? 268  GLU C OE2 1 
ATOM   10414 N  N   . LEU C  1 269 ? 6.497   10.393  83.849  1.00 36.27  ? 269  LEU C N   1 
ATOM   10415 C  CA  . LEU C  1 269 ? 5.380   11.213  83.423  1.00 34.88  ? 269  LEU C CA  1 
ATOM   10416 C  C   . LEU C  1 269 ? 4.485   11.503  84.605  1.00 32.23  ? 269  LEU C C   1 
ATOM   10417 O  O   . LEU C  1 269 ? 4.177   12.662  84.899  1.00 29.54  ? 269  LEU C O   1 
ATOM   10418 C  CB  . LEU C  1 269 ? 4.544   10.497  82.380  1.00 20.21  ? 269  LEU C CB  1 
ATOM   10419 C  CG  . LEU C  1 269 ? 3.786   11.558  81.616  1.00 19.78  ? 269  LEU C CG  1 
ATOM   10420 C  CD1 . LEU C  1 269 ? 4.727   12.009  80.559  1.00 53.79  ? 269  LEU C CD1 1 
ATOM   10421 C  CD2 . LEU C  1 269 ? 2.524   11.059  81.005  1.00 39.40  ? 269  LEU C CD2 1 
ATOM   10422 N  N   . ILE C  1 270 ? 4.072   10.446  85.295  1.00 27.28  ? 270  ILE C N   1 
ATOM   10423 C  CA  . ILE C  1 270 ? 3.144   10.643  86.397  1.00 28.00  ? 270  ILE C CA  1 
ATOM   10424 C  C   . ILE C  1 270 ? 3.777   11.467  87.513  1.00 29.35  ? 270  ILE C C   1 
ATOM   10425 O  O   . ILE C  1 270 ? 3.171   12.400  88.034  1.00 29.54  ? 270  ILE C O   1 
ATOM   10426 C  CB  . ILE C  1 270 ? 2.628   9.322   86.958  1.00 18.70  ? 270  ILE C CB  1 
ATOM   10427 C  CG1 . ILE C  1 270 ? 1.320   8.933   86.293  1.00 17.84  ? 270  ILE C CG1 1 
ATOM   10428 C  CG2 . ILE C  1 270 ? 2.294   9.477   88.409  1.00 18.55  ? 270  ILE C CG2 1 
ATOM   10429 C  CD1 . ILE C  1 270 ? 1.243   9.208   84.849  1.00 17.79  ? 270  ILE C CD1 1 
ATOM   10430 N  N   . ALA C  1 271 ? 5.009   11.133  87.860  1.00 32.23  ? 271  ALA C N   1 
ATOM   10431 C  CA  . ALA C  1 271 ? 5.605   11.655  89.070  1.00 33.89  ? 271  ALA C CA  1 
ATOM   10432 C  C   . ALA C  1 271 ? 5.844   13.126  88.871  1.00 25.79  ? 271  ALA C C   1 
ATOM   10433 O  O   . ALA C  1 271 ? 5.771   13.911  89.816  1.00 22.54  ? 271  ALA C O   1 
ATOM   10434 C  CB  . ALA C  1 271 ? 6.897   10.930  89.377  1.00 59.99  ? 271  ALA C CB  1 
ATOM   10435 N  N   . CYS C  1 272 ? 6.119   13.494  87.627  1.00 23.93  ? 272  CYS C N   1 
ATOM   10436 C  CA  . CYS C  1 272 ? 6.255   14.899  87.278  1.00 24.50  ? 272  CYS C CA  1 
ATOM   10437 C  C   . CYS C  1 272 ? 4.867   15.574  87.333  1.00 24.47  ? 272  CYS C C   1 
ATOM   10438 O  O   . CYS C  1 272 ? 4.723   16.621  87.967  1.00 21.90  ? 272  CYS C O   1 
ATOM   10439 C  CB  . CYS C  1 272 ? 6.986   15.060  85.926  1.00 23.07  ? 272  CYS C CB  1 
ATOM   10440 S  SG  . CYS C  1 272 ? 6.981   16.710  85.150  1.00 76.73  ? 272  CYS C SG  1 
ATOM   10441 N  N   . LEU C  1 273 ? 3.845   14.955  86.723  1.00 27.24  ? 273  LEU C N   1 
ATOM   10442 C  CA  . LEU C  1 273 ? 2.479   15.495  86.768  1.00 19.14  ? 273  LEU C CA  1 
ATOM   10443 C  C   . LEU C  1 273 ? 2.027   15.756  88.191  1.00 19.21  ? 273  LEU C C   1 
ATOM   10444 O  O   . LEU C  1 273 ? 1.202   16.623  88.424  1.00 20.98  ? 273  LEU C O   1 
ATOM   10445 C  CB  . LEU C  1 273 ? 1.472   14.538  86.139  1.00 18.29  ? 273  LEU C CB  1 
ATOM   10446 C  CG  . LEU C  1 273 ? 1.120   14.670  84.664  1.00 18.11  ? 273  LEU C CG  1 
ATOM   10447 C  CD1 . LEU C  1 273 ? 0.024   13.701  84.288  1.00 17.31  ? 273  LEU C CD1 1 
ATOM   10448 C  CD2 . LEU C  1 273 ? 0.672   16.062  84.410  1.00 18.11  ? 273  LEU C CD2 1 
ATOM   10449 N  N   . ARG C  1 274 ? 2.558   14.996  89.141  1.00 21.75  ? 274  ARG C N   1 
ATOM   10450 C  CA  . ARG C  1 274 ? 2.162   15.119  90.537  1.00 19.12  ? 274  ARG C CA  1 
ATOM   10451 C  C   . ARG C  1 274 ? 2.732   16.360  91.201  1.00 19.84  ? 274  ARG C C   1 
ATOM   10452 O  O   . ARG C  1 274 ? 2.291   16.763  92.277  1.00 19.80  ? 274  ARG C O   1 
ATOM   10453 C  CB  . ARG C  1 274 ? 2.605   13.887  91.312  1.00 25.05  ? 274  ARG C CB  1 
ATOM   10454 C  CG  . ARG C  1 274 ? 1.504   12.903  91.598  1.00 23.91  ? 274  ARG C CG  1 
ATOM   10455 C  CD  . ARG C  1 274 ? 1.954   11.892  92.625  1.00 27.12  ? 274  ARG C CD  1 
ATOM   10456 N  NE  . ARG C  1 274 ? 3.004   11.042  92.087  1.00 32.12  ? 274  ARG C NE  1 
ATOM   10457 C  CZ  . ARG C  1 274 ? 2.846   9.757   91.795  1.00 34.31  ? 274  ARG C CZ  1 
ATOM   10458 N  NH1 . ARG C  1 274 ? 1.666   9.146   92.008  1.00 27.13  ? 274  ARG C NH1 1 
ATOM   10459 N  NH2 . ARG C  1 274 ? 3.887   9.088   91.293  1.00 39.34  ? 274  ARG C NH2 1 
ATOM   10460 N  N   . THR C  1 275 ? 3.734   16.945  90.561  1.00 26.12  ? 275  THR C N   1 
ATOM   10461 C  CA  . THR C  1 275 ? 4.391   18.129  91.089  1.00 27.14  ? 275  THR C CA  1 
ATOM   10462 C  C   . THR C  1 275 ? 3.735   19.407  90.593  1.00 26.41  ? 275  THR C C   1 
ATOM   10463 O  O   . THR C  1 275 ? 4.007   20.488  91.095  1.00 30.48  ? 275  THR C O   1 
ATOM   10464 C  CB  . THR C  1 275 ? 5.853   18.189  90.652  1.00 28.69  ? 275  THR C CB  1 
ATOM   10465 O  OG1 . THR C  1 275 ? 5.907   18.577  89.276  1.00 31.11  ? 275  THR C OG1 1 
ATOM   10466 C  CG2 . THR C  1 275 ? 6.524   16.844  90.833  1.00 28.26  ? 275  THR C CG2 1 
ATOM   10467 N  N   . ARG C  1 276 ? 2.879   19.298  89.596  1.00 20.56  ? 276  ARG C N   1 
ATOM   10468 C  CA  . ARG C  1 276 ? 2.164   20.468  89.151  1.00 20.44  ? 276  ARG C CA  1 
ATOM   10469 C  C   . ARG C  1 276 ? 1.188   20.988  90.216  1.00 23.14  ? 276  ARG C C   1 
ATOM   10470 O  O   . ARG C  1 276 ? 0.704   20.226  91.057  1.00 23.07  ? 276  ARG C O   1 
ATOM   10471 C  CB  . ARG C  1 276 ? 1.410   20.141  87.883  1.00 23.16  ? 276  ARG C CB  1 
ATOM   10472 C  CG  . ARG C  1 276 ? 2.089   20.651  86.669  1.00 27.02  ? 276  ARG C CG  1 
ATOM   10473 C  CD  . ARG C  1 276 ? 3.214   19.758  86.293  1.00 30.64  ? 276  ARG C CD  1 
ATOM   10474 N  NE  . ARG C  1 276 ? 4.167   20.466  85.452  1.00 33.07  ? 276  ARG C NE  1 
ATOM   10475 C  CZ  . ARG C  1 276 ? 5.358   20.858  85.876  1.00 35.25  ? 276  ARG C CZ  1 
ATOM   10476 N  NH1 . ARG C  1 276 ? 5.728   20.601  87.124  1.00 34.70  ? 276  ARG C NH1 1 
ATOM   10477 N  NH2 . ARG C  1 276 ? 6.177   21.494  85.055  1.00 39.51  ? 276  ARG C NH2 1 
ATOM   10478 N  N   . PRO C  1 277 ? 0.903   22.298  90.188  1.00 30.45  ? 277  PRO C N   1 
ATOM   10479 C  CA  . PRO C  1 277 ? -0.141  22.899  91.025  1.00 28.64  ? 277  PRO C CA  1 
ATOM   10480 C  C   . PRO C  1 277 ? -1.535  22.487  90.542  1.00 28.27  ? 277  PRO C C   1 
ATOM   10481 O  O   . PRO C  1 277 ? -1.742  22.444  89.338  1.00 19.27  ? 277  PRO C O   1 
ATOM   10482 C  CB  . PRO C  1 277 ? 0.054   24.402  90.791  1.00 20.95  ? 277  PRO C CB  1 
ATOM   10483 C  CG  . PRO C  1 277 ? 1.397   24.539  90.182  1.00 21.80  ? 277  PRO C CG  1 
ATOM   10484 C  CD  . PRO C  1 277 ? 1.616   23.308  89.393  1.00 21.28  ? 277  PRO C CD  1 
ATOM   10485 N  N   . ALA C  1 278 ? -2.468  22.215  91.453  1.00 28.89  ? 278  ALA C N   1 
ATOM   10486 C  CA  . ALA C  1 278 ? -3.817  21.758  91.098  1.00 27.96  ? 278  ALA C CA  1 
ATOM   10487 C  C   . ALA C  1 278 ? -4.486  22.624  90.025  1.00 28.55  ? 278  ALA C C   1 
ATOM   10488 O  O   . ALA C  1 278 ? -5.090  22.128  89.039  1.00 28.07  ? 278  ALA C O   1 
ATOM   10489 C  CB  . ALA C  1 278 ? -4.681  21.691  92.344  1.00 17.44  ? 278  ALA C CB  1 
ATOM   10490 N  N   . GLN C  1 279 ? -4.357  23.928  90.196  1.00 18.31  ? 279  GLN C N   1 
ATOM   10491 C  CA  . GLN C  1 279 ? -4.989  24.822  89.265  1.00 23.67  ? 279  GLN C CA  1 
ATOM   10492 C  C   . GLN C  1 279 ? -4.382  24.706  87.870  1.00 24.39  ? 279  GLN C C   1 
ATOM   10493 O  O   . GLN C  1 279 ? -5.080  24.894  86.883  1.00 18.32  ? 279  GLN C O   1 
ATOM   10494 C  CB  . GLN C  1 279 ? -4.928  26.251  89.771  1.00 19.23  ? 279  GLN C CB  1 
ATOM   10495 C  CG  . GLN C  1 279 ? -5.875  27.184  89.039  1.00 19.33  ? 279  GLN C CG  1 
ATOM   10496 C  CD  . GLN C  1 279 ? -7.334  26.717  89.066  1.00 18.51  ? 279  GLN C CD  1 
ATOM   10497 O  OE1 . GLN C  1 279 ? -7.891  26.375  90.121  1.00 18.20  ? 279  GLN C OE1 1 
ATOM   10498 N  NE2 . GLN C  1 279 ? -7.960  26.712  87.896  1.00 18.25  ? 279  GLN C NE2 1 
ATOM   10499 N  N   . ASP C  1 280 ? -3.094  24.379  87.790  1.00 18.98  ? 280  ASP C N   1 
ATOM   10500 C  CA  . ASP C  1 280 ? -2.382  24.301  86.511  1.00 19.29  ? 280  ASP C CA  1 
ATOM   10501 C  C   . ASP C  1 280 ? -3.001  23.232  85.632  1.00 18.47  ? 280  ASP C C   1 
ATOM   10502 O  O   . ASP C  1 280 ? -3.247  23.418  84.417  1.00 18.50  ? 280  ASP C O   1 
ATOM   10503 C  CB  . ASP C  1 280 ? -0.926  23.949  86.772  1.00 19.91  ? 280  ASP C CB  1 
ATOM   10504 C  CG  . ASP C  1 280 ? -0.047  24.175  85.568  1.00 20.55  ? 280  ASP C CG  1 
ATOM   10505 O  OD1 . ASP C  1 280 ? -0.227  25.202  84.873  1.00 21.00  ? 280  ASP C OD1 1 
ATOM   10506 O  OD2 . ASP C  1 280 ? 0.845   23.335  85.320  1.00 20.69  ? 280  ASP C OD2 1 
ATOM   10507 N  N   . LEU C  1 281 ? -3.250  22.103  86.291  1.00 19.67  ? 281  LEU C N   1 
ATOM   10508 C  CA  . LEU C  1 281 ? -3.976  20.975  85.732  1.00 19.22  ? 281  LEU C CA  1 
ATOM   10509 C  C   . LEU C  1 281 ? -5.344  21.408  85.252  1.00 16.64  ? 281  LEU C C   1 
ATOM   10510 O  O   . LEU C  1 281 ? -5.684  21.192  84.083  1.00 17.48  ? 281  LEU C O   1 
ATOM   10511 C  CB  . LEU C  1 281 ? -4.097  19.854  86.762  1.00 16.57  ? 281  LEU C CB  1 
ATOM   10512 C  CG  . LEU C  1 281 ? -3.057  18.753  86.555  1.00 31.24  ? 281  LEU C CG  1 
ATOM   10513 C  CD1 . LEU C  1 281 ? -1.648  19.281  86.359  1.00 17.60  ? 281  LEU C CD1 1 
ATOM   10514 C  CD2 . LEU C  1 281 ? -3.110  17.793  87.709  1.00 16.42  ? 281  LEU C CD2 1 
ATOM   10515 N  N   . VAL C  1 282 ? -6.130  22.041  86.121  1.00 16.56  ? 282  VAL C N   1 
ATOM   10516 C  CA  . VAL C  1 282 ? -7.452  22.471  85.644  1.00 16.28  ? 282  VAL C CA  1 
ATOM   10517 C  C   . VAL C  1 282 ? -7.389  23.364  84.398  1.00 16.77  ? 282  VAL C C   1 
ATOM   10518 O  O   . VAL C  1 282 ? -8.044  23.082  83.386  1.00 16.82  ? 282  VAL C O   1 
ATOM   10519 C  CB  . VAL C  1 282 ? -8.275  23.163  86.719  1.00 16.30  ? 282  VAL C CB  1 
ATOM   10520 C  CG1 . VAL C  1 282 ? -9.576  23.663  86.117  1.00 19.05  ? 282  VAL C CG1 1 
ATOM   10521 C  CG2 . VAL C  1 282 ? -8.552  22.204  87.872  1.00 24.20  ? 282  VAL C CG2 1 
ATOM   10522 N  N   . ASP C  1 283 ? -6.575  24.416  84.480  1.00 17.56  ? 283  ASP C N   1 
ATOM   10523 C  CA  . ASP C  1 283 ? -6.342  25.347  83.379  1.00 18.23  ? 283  ASP C CA  1 
ATOM   10524 C  C   . ASP C  1 283 ? -5.955  24.650  82.074  1.00 18.16  ? 283  ASP C C   1 
ATOM   10525 O  O   . ASP C  1 283 ? -6.220  25.156  80.987  1.00 18.48  ? 283  ASP C O   1 
ATOM   10526 C  CB  . ASP C  1 283 ? -5.231  26.321  83.756  1.00 44.73  ? 283  ASP C CB  1 
ATOM   10527 C  CG  . ASP C  1 283 ? -5.592  27.181  84.936  1.00 55.90  ? 283  ASP C CG  1 
ATOM   10528 O  OD1 . ASP C  1 283 ? -6.626  26.888  85.573  1.00 57.53  ? 283  ASP C OD1 1 
ATOM   10529 O  OD2 . ASP C  1 283 ? -4.837  28.143  85.227  1.00 62.24  ? 283  ASP C OD2 1 
ATOM   10530 N  N   . HIS C  1 284 ? -5.288  23.509  82.153  1.00 23.32  ? 284  HIS C N   1 
ATOM   10531 C  CA  . HIS C  1 284 ? -5.014  22.811  80.897  1.00 23.01  ? 284  HIS C CA  1 
ATOM   10532 C  C   . HIS C  1 284 ? -5.934  21.650  80.500  1.00 21.24  ? 284  HIS C C   1 
ATOM   10533 O  O   . HIS C  1 284 ? -5.766  21.083  79.424  1.00 19.94  ? 284  HIS C O   1 
ATOM   10534 C  CB  . HIS C  1 284 ? -3.544  22.412  80.821  1.00 25.06  ? 284  HIS C CB  1 
ATOM   10535 C  CG  . HIS C  1 284 ? -2.630  23.587  80.831  1.00 28.86  ? 284  HIS C CG  1 
ATOM   10536 N  ND1 . HIS C  1 284 ? -2.226  24.199  81.997  1.00 30.99  ? 284  HIS C ND1 1 
ATOM   10537 C  CD2 . HIS C  1 284 ? -2.096  24.309  79.819  1.00 34.23  ? 284  HIS C CD2 1 
ATOM   10538 C  CE1 . HIS C  1 284 ? -1.455  25.231  81.702  1.00 36.29  ? 284  HIS C CE1 1 
ATOM   10539 N  NE2 . HIS C  1 284 ? -1.361  25.322  80.387  1.00 38.02  ? 284  HIS C NE2 1 
ATOM   10540 N  N   . GLU C  1 285 ? -6.903  21.287  81.334  1.00 16.37  ? 285  GLU C N   1 
ATOM   10541 C  CA  . GLU C  1 285 ? -7.611  20.041  81.033  1.00 15.71  ? 285  GLU C CA  1 
ATOM   10542 C  C   . GLU C  1 285 ? -8.504  20.059  79.806  1.00 20.07  ? 285  GLU C C   1 
ATOM   10543 O  O   . GLU C  1 285 ? -8.720  19.021  79.211  1.00 19.68  ? 285  GLU C O   1 
ATOM   10544 C  CB  . GLU C  1 285 ? -8.338  19.455  82.238  1.00 23.46  ? 285  GLU C CB  1 
ATOM   10545 C  CG  . GLU C  1 285 ? -9.571  20.172  82.669  1.00 27.80  ? 285  GLU C CG  1 
ATOM   10546 C  CD  . GLU C  1 285 ? -10.160 19.518  83.901  1.00 33.04  ? 285  GLU C CD  1 
ATOM   10547 O  OE1 . GLU C  1 285 ? -9.361  18.970  84.694  1.00 34.53  ? 285  GLU C OE1 1 
ATOM   10548 O  OE2 . GLU C  1 285 ? -11.404 19.525  84.074  1.00 35.77  ? 285  GLU C OE2 1 
ATOM   10549 N  N   . TRP C  1 286 ? -9.008  21.216  79.401  1.00 26.56  ? 286  TRP C N   1 
ATOM   10550 C  CA  . TRP C  1 286 ? -9.863  21.262  78.213  1.00 29.24  ? 286  TRP C CA  1 
ATOM   10551 C  C   . TRP C  1 286 ? -9.087  21.228  76.906  1.00 25.70  ? 286  TRP C C   1 
ATOM   10552 O  O   . TRP C  1 286 ? -9.672  21.004  75.860  1.00 24.12  ? 286  TRP C O   1 
ATOM   10553 C  CB  . TRP C  1 286 ? -10.755 22.500  78.224  1.00 54.49  ? 286  TRP C CB  1 
ATOM   10554 C  CG  . TRP C  1 286 ? -11.852 22.440  79.232  1.00 64.69  ? 286  TRP C CG  1 
ATOM   10555 C  CD1 . TRP C  1 286 ? -11.972 23.199  80.366  1.00 68.42  ? 286  TRP C CD1 1 
ATOM   10556 C  CD2 . TRP C  1 286 ? -12.994 21.579  79.202  1.00 64.75  ? 286  TRP C CD2 1 
ATOM   10557 N  NE1 . TRP C  1 286 ? -13.125 22.860  81.042  1.00 66.61  ? 286  TRP C NE1 1 
ATOM   10558 C  CE2 . TRP C  1 286 ? -13.771 21.872  80.342  1.00 65.04  ? 286  TRP C CE2 1 
ATOM   10559 C  CE3 . TRP C  1 286 ? -13.440 20.597  78.317  1.00 63.39  ? 286  TRP C CE3 1 
ATOM   10560 C  CZ2 . TRP C  1 286 ? -14.957 21.214  80.622  1.00 64.03  ? 286  TRP C CZ2 1 
ATOM   10561 C  CZ3 . TRP C  1 286 ? -14.617 19.947  78.596  1.00 64.11  ? 286  TRP C CZ3 1 
ATOM   10562 C  CH2 . TRP C  1 286 ? -15.364 20.256  79.739  1.00 64.56  ? 286  TRP C CH2 1 
ATOM   10563 N  N   . HIS C  1 287 ? -7.779  21.459  76.963  1.00 34.82  ? 287  HIS C N   1 
ATOM   10564 C  CA  . HIS C  1 287 ? -6.977  21.616  75.750  1.00 38.01  ? 287  HIS C CA  1 
ATOM   10565 C  C   . HIS C  1 287 ? -6.781  20.282  75.050  1.00 38.54  ? 287  HIS C C   1 
ATOM   10566 O  O   . HIS C  1 287 ? -6.476  20.232  73.860  1.00 44.83  ? 287  HIS C O   1 
ATOM   10567 C  CB  . HIS C  1 287 ? -5.599  22.225  76.060  1.00 39.29  ? 287  HIS C CB  1 
ATOM   10568 C  CG  . HIS C  1 287 ? -5.652  23.576  76.716  1.00 42.30  ? 287  HIS C CG  1 
ATOM   10569 N  ND1 . HIS C  1 287 ? -4.513  24.287  77.049  1.00 42.39  ? 287  HIS C ND1 1 
ATOM   10570 C  CD2 . HIS C  1 287 ? -6.697  24.347  77.103  1.00 42.18  ? 287  HIS C CD2 1 
ATOM   10571 C  CE1 . HIS C  1 287 ? -4.858  25.427  77.613  1.00 42.39  ? 287  HIS C CE1 1 
ATOM   10572 N  NE2 . HIS C  1 287 ? -6.178  25.491  77.660  1.00 41.68  ? 287  HIS C NE2 1 
ATOM   10573 N  N   . VAL C  1 288 ? -6.961  19.194  75.785  1.00 25.01  ? 288  VAL C N   1 
ATOM   10574 C  CA  . VAL C  1 288 ? -6.630  17.882  75.249  1.00 22.24  ? 288  VAL C CA  1 
ATOM   10575 C  C   . VAL C  1 288 ? -7.750  17.230  74.424  1.00 22.39  ? 288  VAL C C   1 
ATOM   10576 O  O   . VAL C  1 288 ? -7.587  16.115  73.919  1.00 22.33  ? 288  VAL C O   1 
ATOM   10577 C  CB  . VAL C  1 288 ? -6.143  16.948  76.356  1.00 16.29  ? 288  VAL C CB  1 
ATOM   10578 C  CG1 . VAL C  1 288 ? -5.054  17.633  77.146  1.00 24.81  ? 288  VAL C CG1 1 
ATOM   10579 C  CG2 . VAL C  1 288 ? -7.279  16.571  77.265  1.00 28.86  ? 288  VAL C CG2 1 
ATOM   10580 N  N   . LEU C  1 289 ? -8.879  17.918  74.272  1.00 40.70  ? 289  LEU C N   1 
ATOM   10581 C  CA  . LEU C  1 289 ? -9.966  17.376  73.459  1.00 41.88  ? 289  LEU C CA  1 
ATOM   10582 C  C   . LEU C  1 289 ? -9.533  17.281  72.000  1.00 43.94  ? 289  LEU C C   1 
ATOM   10583 O  O   . LEU C  1 289 ? -8.789  18.146  71.513  1.00 47.05  ? 289  LEU C O   1 
ATOM   10584 C  CB  . LEU C  1 289 ? -11.250 18.204  73.592  1.00 29.33  ? 289  LEU C CB  1 
ATOM   10585 C  CG  . LEU C  1 289 ? -12.065 18.075  74.884  1.00 26.52  ? 289  LEU C CG  1 
ATOM   10586 C  CD1 . LEU C  1 289 ? -13.360 18.838  74.769  1.00 25.33  ? 289  LEU C CD1 1 
ATOM   10587 C  CD2 . LEU C  1 289 ? -12.350 16.626  75.231  1.00 25.48  ? 289  LEU C CD2 1 
ATOM   10588 N  N   . PRO C  1 290 ? -9.938  16.189  71.325  1.00 29.83  ? 290  PRO C N   1 
ATOM   10589 C  CA  . PRO C  1 290 ? -9.687  15.920  69.903  1.00 28.34  ? 290  PRO C CA  1 
ATOM   10590 C  C   . PRO C  1 290 ? -10.452 16.801  68.908  1.00 30.95  ? 290  PRO C C   1 
ATOM   10591 O  O   . PRO C  1 290 ? -9.830  17.281  67.956  1.00 33.76  ? 290  PRO C O   1 
ATOM   10592 C  CB  . PRO C  1 290 ? -10.097 14.461  69.753  1.00 20.15  ? 290  PRO C CB  1 
ATOM   10593 C  CG  . PRO C  1 290 ? -11.131 14.284  70.778  1.00 21.62  ? 290  PRO C CG  1 
ATOM   10594 C  CD  . PRO C  1 290 ? -10.707 15.104  71.949  1.00 22.04  ? 290  PRO C CD  1 
ATOM   10595 N  N   . GLN C  1 291 ? -11.746 17.037  69.117  1.00 31.31  ? 291  GLN C N   1 
ATOM   10596 C  CA  . GLN C  1 291 ? -12.502 17.852  68.162  1.00 33.66  ? 291  GLN C CA  1 
ATOM   10597 C  C   . GLN C  1 291 ? -13.247 18.997  68.805  1.00 35.52  ? 291  GLN C C   1 
ATOM   10598 O  O   . GLN C  1 291 ? -13.492 18.988  70.014  1.00 42.13  ? 291  GLN C O   1 
ATOM   10599 C  CB  . GLN C  1 291 ? -13.510 17.013  67.394  1.00 32.33  ? 291  GLN C CB  1 
ATOM   10600 C  CG  . GLN C  1 291 ? -12.908 15.904  66.582  1.00 34.15  ? 291  GLN C CG  1 
ATOM   10601 C  CD  . GLN C  1 291 ? -12.955 14.608  67.322  1.00 36.12  ? 291  GLN C CD  1 
ATOM   10602 O  OE1 . GLN C  1 291 ? -13.705 14.462  68.289  1.00 35.83  ? 291  GLN C OE1 1 
ATOM   10603 N  NE2 . GLN C  1 291 ? -12.154 13.646  66.881  1.00 39.91  ? 291  GLN C NE2 1 
ATOM   10604 N  N   . GLU C  1 292 ? -13.625 19.975  67.987  1.00 23.11  ? 292  GLU C N   1 
ATOM   10605 C  CA  . GLU C  1 292 ? -14.489 21.039  68.465  1.00 25.68  ? 292  GLU C CA  1 
ATOM   10606 C  C   . GLU C  1 292 ? -15.864 20.397  68.717  1.00 25.16  ? 292  GLU C C   1 
ATOM   10607 O  O   . GLU C  1 292 ? -16.511 19.851  67.800  1.00 23.25  ? 292  GLU C O   1 
ATOM   10608 C  CB  . GLU C  1 292 ? -14.568 22.175  67.434  1.00 48.67  ? 292  GLU C CB  1 
ATOM   10609 C  CG  . GLU C  1 292 ? -15.570 23.281  67.771  1.00 57.11  ? 292  GLU C CG  1 
ATOM   10610 C  CD  . GLU C  1 292 ? -15.650 24.363  66.701  1.00 64.47  ? 292  GLU C CD  1 
ATOM   10611 O  OE1 . GLU C  1 292 ? -14.962 24.227  65.662  1.00 65.93  ? 292  GLU C OE1 1 
ATOM   10612 O  OE2 . GLU C  1 292 ? -16.402 25.348  66.901  1.00 67.29  ? 292  GLU C OE2 1 
ATOM   10613 N  N   . SER C  1 293 ? -16.312 20.479  69.968  1.00 35.38  ? 293  SER C N   1 
ATOM   10614 C  CA  . SER C  1 293 ? -17.436 19.674  70.417  1.00 33.45  ? 293  SER C CA  1 
ATOM   10615 C  C   . SER C  1 293 ? -18.132 20.270  71.619  1.00 31.54  ? 293  SER C C   1 
ATOM   10616 O  O   . SER C  1 293 ? -17.553 21.056  72.357  1.00 35.45  ? 293  SER C O   1 
ATOM   10617 C  CB  . SER C  1 293 ? -16.937 18.282  70.806  1.00 32.12  ? 293  SER C CB  1 
ATOM   10618 O  OG  . SER C  1 293 ? -16.053 18.338  71.919  1.00 31.59  ? 293  SER C OG  1 
ATOM   10619 N  N   . ILE C  1 294 ? -19.381 19.872  71.812  1.00 22.08  ? 294  ILE C N   1 
ATOM   10620 C  CA  . ILE C  1 294 ? -20.070 20.078  73.072  1.00 22.94  ? 294  ILE C CA  1 
ATOM   10621 C  C   . ILE C  1 294 ? -20.515 18.706  73.583  1.00 24.43  ? 294  ILE C C   1 
ATOM   10622 O  O   . ILE C  1 294 ? -20.534 17.724  72.832  1.00 22.80  ? 294  ILE C O   1 
ATOM   10623 C  CB  . ILE C  1 294 ? -21.301 21.026  72.959  1.00 17.27  ? 294  ILE C CB  1 
ATOM   10624 C  CG1 . ILE C  1 294 ? -22.238 20.586  71.827  1.00 28.91  ? 294  ILE C CG1 1 
ATOM   10625 C  CG2 . ILE C  1 294 ? -20.873 22.467  72.778  1.00 17.87  ? 294  ILE C CG2 1 
ATOM   10626 C  CD1 . ILE C  1 294 ? -23.695 20.928  72.071  1.00 18.11  ? 294  ILE C CD1 1 
ATOM   10627 N  N   . PHE C  1 295 ? -20.866 18.653  74.864  1.00 26.68  ? 295  PHE C N   1 
ATOM   10628 C  CA  . PHE C  1 295 ? -21.242 17.415  75.540  1.00 23.22  ? 295  PHE C CA  1 
ATOM   10629 C  C   . PHE C  1 295 ? -20.143 16.368  75.401  1.00 22.79  ? 295  PHE C C   1 
ATOM   10630 O  O   . PHE C  1 295 ? -20.414 15.193  75.220  1.00 20.66  ? 295  PHE C O   1 
ATOM   10631 C  CB  . PHE C  1 295 ? -22.608 16.900  75.064  1.00 23.67  ? 295  PHE C CB  1 
ATOM   10632 C  CG  . PHE C  1 295 ? -23.407 16.205  76.140  1.00 24.35  ? 295  PHE C CG  1 
ATOM   10633 C  CD1 . PHE C  1 295 ? -22.788 15.395  77.084  1.00 26.02  ? 295  PHE C CD1 1 
ATOM   10634 C  CD2 . PHE C  1 295 ? -24.771 16.373  76.222  1.00 22.50  ? 295  PHE C CD2 1 
ATOM   10635 C  CE1 . PHE C  1 295 ? -23.518 14.767  78.081  1.00 24.35  ? 295  PHE C CE1 1 
ATOM   10636 C  CE2 . PHE C  1 295 ? -25.506 15.734  77.216  1.00 21.56  ? 295  PHE C CE2 1 
ATOM   10637 C  CZ  . PHE C  1 295 ? -24.880 14.939  78.142  1.00 22.28  ? 295  PHE C CZ  1 
ATOM   10638 N  N   . ARG C  1 296 ? -18.897 16.818  75.462  1.00 43.89  ? 296  ARG C N   1 
ATOM   10639 C  CA  . ARG C  1 296 ? -17.763 15.916  75.553  1.00 47.78  ? 296  ARG C CA  1 
ATOM   10640 C  C   . ARG C  1 296 ? -16.810 16.494  76.577  1.00 51.94  ? 296  ARG C C   1 
ATOM   10641 O  O   . ARG C  1 296 ? -16.488 17.683  76.544  1.00 57.30  ? 296  ARG C O   1 
ATOM   10642 C  CB  . ARG C  1 296 ? -17.042 15.770  74.214  1.00 30.96  ? 296  ARG C CB  1 
ATOM   10643 C  CG  . ARG C  1 296 ? -17.859 15.182  73.083  1.00 30.74  ? 296  ARG C CG  1 
ATOM   10644 C  CD  . ARG C  1 296 ? -18.266 13.757  73.342  1.00 31.75  ? 296  ARG C CD  1 
ATOM   10645 N  NE  . ARG C  1 296 ? -18.875 13.162  72.157  1.00 34.13  ? 296  ARG C NE  1 
ATOM   10646 C  CZ  . ARG C  1 296 ? -20.177 13.173  71.897  1.00 34.35  ? 296  ARG C CZ  1 
ATOM   10647 N  NH1 . ARG C  1 296 ? -21.016 13.748  72.743  1.00 33.56  ? 296  ARG C NH1 1 
ATOM   10648 N  NH2 . ARG C  1 296 ? -20.636 12.614  70.786  1.00 35.37  ? 296  ARG C NH2 1 
ATOM   10649 N  N   . PHE C  1 297 ? -16.357 15.644  77.484  1.00 30.04  ? 297  PHE C N   1 
ATOM   10650 C  CA  . PHE C  1 297 ? -15.523 16.085  78.576  1.00 21.97  ? 297  PHE C CA  1 
ATOM   10651 C  C   . PHE C  1 297 ? -14.210 15.310  78.512  1.00 16.38  ? 297  PHE C C   1 
ATOM   10652 O  O   . PHE C  1 297 ? -14.182 14.183  78.022  1.00 15.38  ? 297  PHE C O   1 
ATOM   10653 C  CB  . PHE C  1 297 ? -16.251 15.818  79.879  1.00 28.10  ? 297  PHE C CB  1 
ATOM   10654 C  CG  . PHE C  1 297 ? -17.762 15.885  79.768  1.00 33.07  ? 297  PHE C CG  1 
ATOM   10655 C  CD1 . PHE C  1 297 ? -18.442 17.084  79.979  1.00 37.22  ? 297  PHE C CD1 1 
ATOM   10656 C  CD2 . PHE C  1 297 ? -18.508 14.749  79.488  1.00 33.29  ? 297  PHE C CD2 1 
ATOM   10657 C  CE1 . PHE C  1 297 ? -19.845 17.150  79.912  1.00 36.97  ? 297  PHE C CE1 1 
ATOM   10658 C  CE2 . PHE C  1 297 ? -19.907 14.813  79.412  1.00 35.10  ? 297  PHE C CE2 1 
ATOM   10659 C  CZ  . PHE C  1 297 ? -20.571 16.012  79.628  1.00 35.99  ? 297  PHE C CZ  1 
ATOM   10660 N  N   . SER C  1 298 ? -13.129 15.902  79.010  1.00 14.24  ? 298  SER C N   1 
ATOM   10661 C  CA  . SER C  1 298 ? -11.782 15.380  78.754  1.00 13.84  ? 298  SER C CA  1 
ATOM   10662 C  C   . SER C  1 298 ? -11.372 14.130  79.494  1.00 14.11  ? 298  SER C C   1 
ATOM   10663 O  O   . SER C  1 298 ? -10.710 13.265  78.924  1.00 14.78  ? 298  SER C O   1 
ATOM   10664 C  CB  . SER C  1 298 ? -10.744 16.439  79.044  1.00 17.95  ? 298  SER C CB  1 
ATOM   10665 O  OG  . SER C  1 298 ? -10.637 17.300  77.945  1.00 23.20  ? 298  SER C OG  1 
ATOM   10666 N  N   . PHE C  1 299 ? -11.723 14.054  80.769  1.00 16.45  ? 299  PHE C N   1 
ATOM   10667 C  CA  . PHE C  1 299 ? -11.320 12.923  81.580  1.00 15.37  ? 299  PHE C CA  1 
ATOM   10668 C  C   . PHE C  1 299 ? -12.514 12.254  82.209  1.00 15.37  ? 299  PHE C C   1 
ATOM   10669 O  O   . PHE C  1 299 ? -13.195 12.820  83.060  1.00 16.19  ? 299  PHE C O   1 
ATOM   10670 C  CB  . PHE C  1 299 ? -10.322 13.392  82.608  1.00 17.95  ? 299  PHE C CB  1 
ATOM   10671 C  CG  . PHE C  1 299 ? -9.108  13.994  81.989  1.00 24.24  ? 299  PHE C CG  1 
ATOM   10672 C  CD1 . PHE C  1 299 ? -8.022  13.198  81.648  1.00 26.80  ? 299  PHE C CD1 1 
ATOM   10673 C  CD2 . PHE C  1 299 ? -9.062  15.335  81.697  1.00 27.01  ? 299  PHE C CD2 1 
ATOM   10674 C  CE1 . PHE C  1 299 ? -6.899  13.732  81.062  1.00 28.63  ? 299  PHE C CE1 1 
ATOM   10675 C  CE2 . PHE C  1 299 ? -7.947  15.873  81.102  1.00 30.30  ? 299  PHE C CE2 1 
ATOM   10676 C  CZ  . PHE C  1 299 ? -6.858  15.067  80.787  1.00 30.33  ? 299  PHE C CZ  1 
ATOM   10677 N  N   . VAL C  1 300 ? -12.775 11.039  81.751  1.00 12.68  ? 300  VAL C N   1 
ATOM   10678 C  CA  . VAL C  1 300 ? -13.973 10.320  82.126  1.00 15.81  ? 300  VAL C CA  1 
ATOM   10679 C  C   . VAL C  1 300 ? -13.555 8.891   82.465  1.00 13.22  ? 300  VAL C C   1 
ATOM   10680 O  O   . VAL C  1 300 ? -12.370 8.572   82.379  1.00 14.26  ? 300  VAL C O   1 
ATOM   10681 C  CB  . VAL C  1 300 ? -14.987 10.320  80.970  1.00 18.70  ? 300  VAL C CB  1 
ATOM   10682 C  CG1 . VAL C  1 300 ? -15.244 11.715  80.502  1.00 12.68  ? 300  VAL C CG1 1 
ATOM   10683 C  CG2 . VAL C  1 300 ? -14.479 9.479   79.846  1.00 12.80  ? 300  VAL C CG2 1 
ATOM   10684 N  N   . PRO C  1 301 ? -14.512 8.032   82.873  1.00 12.43  ? 301  PRO C N   1 
ATOM   10685 C  CA  . PRO C  1 301 ? -14.112 6.637   83.031  1.00 13.03  ? 301  PRO C CA  1 
ATOM   10686 C  C   . PRO C  1 301 ? -13.422 6.047   81.793  1.00 14.22  ? 301  PRO C C   1 
ATOM   10687 O  O   . PRO C  1 301 ? -13.910 6.209   80.681  1.00 12.96  ? 301  PRO C O   1 
ATOM   10688 C  CB  . PRO C  1 301 ? -15.446 5.940   83.286  1.00 16.08  ? 301  PRO C CB  1 
ATOM   10689 C  CG  . PRO C  1 301 ? -16.237 6.939   84.012  1.00 12.37  ? 301  PRO C CG  1 
ATOM   10690 C  CD  . PRO C  1 301 ? -15.858 8.268   83.438  1.00 12.30  ? 301  PRO C CD  1 
ATOM   10691 N  N   . VAL C  1 302 ? -12.287 5.383   82.008  1.00 18.59  ? 302  VAL C N   1 
ATOM   10692 C  CA  . VAL C  1 302 ? -11.522 4.718   80.952  1.00 19.51  ? 302  VAL C CA  1 
ATOM   10693 C  C   . VAL C  1 302 ? -11.951 3.266   80.899  1.00 18.48  ? 302  VAL C C   1 
ATOM   10694 O  O   . VAL C  1 302 ? -12.254 2.690   81.950  1.00 17.64  ? 302  VAL C O   1 
ATOM   10695 C  CB  . VAL C  1 302 ? -10.014 4.772   81.273  1.00 21.06  ? 302  VAL C CB  1 
ATOM   10696 C  CG1 . VAL C  1 302 ? -9.747  4.346   82.716  1.00 13.70  ? 302  VAL C CG1 1 
ATOM   10697 C  CG2 . VAL C  1 302 ? -9.222  3.936   80.306  1.00 14.22  ? 302  VAL C CG2 1 
ATOM   10698 N  N   . VAL C  1 303 ? -12.015 2.652   79.712  1.00 14.74  ? 303  VAL C N   1 
ATOM   10699 C  CA  . VAL C  1 303 ? -12.310 1.215   79.721  1.00 15.96  ? 303  VAL C CA  1 
ATOM   10700 C  C   . VAL C  1 303 ? -10.988 0.485   79.719  1.00 16.56  ? 303  VAL C C   1 
ATOM   10701 O  O   . VAL C  1 303 ? -10.362 0.284   78.672  1.00 15.26  ? 303  VAL C O   1 
ATOM   10702 C  CB  . VAL C  1 303 ? -13.174 0.766   78.532  1.00 14.69  ? 303  VAL C CB  1 
ATOM   10703 C  CG1 . VAL C  1 303 ? -13.610 -0.660  78.725  1.00 15.10  ? 303  VAL C CG1 1 
ATOM   10704 C  CG2 . VAL C  1 303 ? -14.401 1.648   78.418  1.00 14.33  ? 303  VAL C CG2 1 
ATOM   10705 N  N   . ASP C  1 304 ? -10.644 0.052   80.934  1.00 20.52  ? 304  ASP C N   1 
ATOM   10706 C  CA  . ASP C  1 304 ? -9.313  -0.394  81.347  1.00 24.68  ? 304  ASP C CA  1 
ATOM   10707 C  C   . ASP C  1 304 ? -9.156  -1.895  81.436  1.00 27.30  ? 304  ASP C C   1 
ATOM   10708 O  O   . ASP C  1 304 ? -8.067  -2.397  81.721  1.00 28.57  ? 304  ASP C O   1 
ATOM   10709 C  CB  . ASP C  1 304 ? -8.998  0.188   82.735  1.00 34.11  ? 304  ASP C CB  1 
ATOM   10710 C  CG  . ASP C  1 304 ? -10.100 -0.119  83.786  1.00 54.65  ? 304  ASP C CG  1 
ATOM   10711 O  OD1 . ASP C  1 304 ? -11.258 -0.395  83.388  1.00 55.91  ? 304  ASP C OD1 1 
ATOM   10712 O  OD2 . ASP C  1 304 ? -9.809  -0.062  85.009  1.00 50.09  ? 304  ASP C OD2 1 
ATOM   10713 N  N   . GLY C  1 305 ? -10.252 -2.614  81.235  1.00 33.89  ? 305  GLY C N   1 
ATOM   10714 C  CA  . GLY C  1 305 ? -10.245 -4.043  81.459  1.00 36.72  ? 305  GLY C CA  1 
ATOM   10715 C  C   . GLY C  1 305 ? -10.232 -4.400  82.930  1.00 39.12  ? 305  GLY C C   1 
ATOM   10716 O  O   . GLY C  1 305 ? -10.195 -5.579  83.269  1.00 42.44  ? 305  GLY C O   1 
ATOM   10717 N  N   . ASP C  1 306 ? -10.261 -3.396  83.808  1.00 36.71  ? 306  ASP C N   1 
ATOM   10718 C  CA  . ASP C  1 306 ? -10.398 -3.669  85.240  1.00 35.88  ? 306  ASP C CA  1 
ATOM   10719 C  C   . ASP C  1 306 ? -11.764 -3.292  85.829  1.00 31.51  ? 306  ASP C C   1 
ATOM   10720 O  O   . ASP C  1 306 ? -12.586 -4.176  86.075  1.00 32.06  ? 306  ASP C O   1 
ATOM   10721 C  CB  . ASP C  1 306 ? -9.273  -3.037  86.065  1.00 41.92  ? 306  ASP C CB  1 
ATOM   10722 C  CG  . ASP C  1 306 ? -9.017  -3.802  87.354  1.00 46.86  ? 306  ASP C CG  1 
ATOM   10723 O  OD1 . ASP C  1 306 ? -8.953  -5.055  87.286  1.00 52.30  ? 306  ASP C OD1 1 
ATOM   10724 O  OD2 . ASP C  1 306 ? -8.909  -3.174  88.431  1.00 44.76  ? 306  ASP C OD2 1 
ATOM   10725 N  N   . PHE C  1 307 ? -12.007 -1.998  86.049  1.00 26.84  ? 307  PHE C N   1 
ATOM   10726 C  CA  . PHE C  1 307 ? -13.290 -1.549  86.602  1.00 25.43  ? 307  PHE C CA  1 
ATOM   10727 C  C   . PHE C  1 307 ? -14.379 -1.871  85.589  1.00 23.84  ? 307  PHE C C   1 
ATOM   10728 O  O   . PHE C  1 307 ? -15.442 -2.383  85.933  1.00 25.25  ? 307  PHE C O   1 
ATOM   10729 C  CB  . PHE C  1 307 ? -13.266 -0.050  86.909  1.00 21.86  ? 307  PHE C CB  1 
ATOM   10730 C  CG  . PHE C  1 307 ? -14.398 0.417   87.792  1.00 22.74  ? 307  PHE C CG  1 
ATOM   10731 C  CD1 . PHE C  1 307 ? -15.654 0.683   87.264  1.00 24.75  ? 307  PHE C CD1 1 
ATOM   10732 C  CD2 . PHE C  1 307 ? -14.203 0.609   89.145  1.00 23.31  ? 307  PHE C CD2 1 
ATOM   10733 C  CE1 . PHE C  1 307 ? -16.701 1.120   88.077  1.00 23.99  ? 307  PHE C CE1 1 
ATOM   10734 C  CE2 . PHE C  1 307 ? -15.236 1.046   89.951  1.00 23.58  ? 307  PHE C CE2 1 
ATOM   10735 C  CZ  . PHE C  1 307 ? -16.488 1.296   89.415  1.00 23.19  ? 307  PHE C CZ  1 
ATOM   10736 N  N   . LEU C  1 308 ? -14.096 -1.576  84.330  1.00 23.04  ? 308  LEU C N   1 
ATOM   10737 C  CA  . LEU C  1 308 ? -14.923 -2.047  83.242  1.00 23.40  ? 308  LEU C CA  1 
ATOM   10738 C  C   . LEU C  1 308 ? -14.143 -3.115  82.478  1.00 28.22  ? 308  LEU C C   1 
ATOM   10739 O  O   . LEU C  1 308 ? -13.140 -2.816  81.814  1.00 31.06  ? 308  LEU C O   1 
ATOM   10740 C  CB  . LEU C  1 308 ? -15.265 -0.887  82.324  1.00 17.19  ? 308  LEU C CB  1 
ATOM   10741 C  CG  . LEU C  1 308 ? -15.998 0.266   82.993  1.00 16.19  ? 308  LEU C CG  1 
ATOM   10742 C  CD1 . LEU C  1 308 ? -15.966 1.491   82.088  1.00 15.23  ? 308  LEU C CD1 1 
ATOM   10743 C  CD2 . LEU C  1 308 ? -17.421 -0.145  83.317  1.00 14.16  ? 308  LEU C CD2 1 
ATOM   10744 N  N   . SER C  1 309 ? -14.604 -4.359  82.579  1.00 23.28  ? 309  SER C N   1 
ATOM   10745 C  CA  . SER C  1 309 ? -13.946 -5.496  81.941  1.00 20.28  ? 309  SER C CA  1 
ATOM   10746 C  C   . SER C  1 309 ? -14.065 -5.431  80.432  1.00 22.88  ? 309  SER C C   1 
ATOM   10747 O  O   . SER C  1 309 ? -13.263 -6.005  79.715  1.00 27.41  ? 309  SER C O   1 
ATOM   10748 C  CB  . SER C  1 309 ? -14.644 -6.755  82.380  1.00 20.45  ? 309  SER C CB  1 
ATOM   10749 O  OG  . SER C  1 309 ? -16.024 -6.592  82.130  1.00 20.16  ? 309  SER C OG  1 
ATOM   10750 N  N   . ASP C  1 310 ? -15.108 -4.770  79.955  1.00 20.89  ? 310  ASP C N   1 
ATOM   10751 C  CA  . ASP C  1 310 ? -15.295 -4.531  78.537  1.00 23.52  ? 310  ASP C CA  1 
ATOM   10752 C  C   . ASP C  1 310 ? -15.960 -3.153  78.439  1.00 22.39  ? 310  ASP C C   1 
ATOM   10753 O  O   . ASP C  1 310 ? -16.163 -2.487  79.447  1.00 22.26  ? 310  ASP C O   1 
ATOM   10754 C  CB  . ASP C  1 310 ? -16.185 -5.631  77.946  1.00 39.55  ? 310  ASP C CB  1 
ATOM   10755 C  CG  . ASP C  1 310 ? -16.040 -5.776  76.442  1.00 46.52  ? 310  ASP C CG  1 
ATOM   10756 O  OD1 . ASP C  1 310 ? -16.437 -4.852  75.710  1.00 48.85  ? 310  ASP C OD1 1 
ATOM   10757 O  OD2 . ASP C  1 310 ? -15.550 -6.826  75.984  1.00 50.49  ? 310  ASP C OD2 1 
ATOM   10758 N  N   . THR C  1 311 ? -16.295 -2.708  77.239  1.00 23.17  ? 311  THR C N   1 
ATOM   10759 C  CA  . THR C  1 311 ? -17.043 -1.471  77.094  1.00 24.68  ? 311  THR C CA  1 
ATOM   10760 C  C   . THR C  1 311 ? -18.459 -1.650  77.660  1.00 25.94  ? 311  THR C C   1 
ATOM   10761 O  O   . THR C  1 311 ? -19.018 -2.745  77.597  1.00 24.58  ? 311  THR C O   1 
ATOM   10762 C  CB  . THR C  1 311 ? -17.145 -1.102  75.634  1.00 32.23  ? 311  THR C CB  1 
ATOM   10763 O  OG1 . THR C  1 311 ? -18.232 -1.821  75.050  1.00 35.01  ? 311  THR C OG1 1 
ATOM   10764 C  CG2 . THR C  1 311 ? -15.874 -1.500  74.925  1.00 34.91  ? 311  THR C CG2 1 
ATOM   10765 N  N   . PRO C  1 312 ? -19.036 -0.575  78.229  1.00 31.08  ? 312  PRO C N   1 
ATOM   10766 C  CA  . PRO C  1 312 ? -20.392 -0.575  78.772  1.00 30.74  ? 312  PRO C CA  1 
ATOM   10767 C  C   . PRO C  1 312 ? -21.359 -1.128  77.770  1.00 38.12  ? 312  PRO C C   1 
ATOM   10768 O  O   . PRO C  1 312 ? -22.289 -1.839  78.152  1.00 43.25  ? 312  PRO C O   1 
ATOM   10769 C  CB  . PRO C  1 312 ? -20.674 0.904   78.962  1.00 18.56  ? 312  PRO C CB  1 
ATOM   10770 C  CG  . PRO C  1 312 ? -19.365 1.456   79.314  1.00 19.13  ? 312  PRO C CG  1 
ATOM   10771 C  CD  . PRO C  1 312 ? -18.364 0.707   78.487  1.00 22.94  ? 312  PRO C CD  1 
ATOM   10772 N  N   . GLU C  1 313 ? -21.125 -0.802  76.503  1.00 42.24  ? 313  GLU C N   1 
ATOM   10773 C  CA  . GLU C  1 313 ? -21.895 -1.355  75.396  1.00 48.31  ? 313  GLU C CA  1 
ATOM   10774 C  C   . GLU C  1 313 ? -22.025 -2.875  75.558  1.00 42.07  ? 313  GLU C C   1 
ATOM   10775 O  O   . GLU C  1 313 ? -23.134 -3.403  75.741  1.00 44.35  ? 313  GLU C O   1 
ATOM   10776 C  CB  . GLU C  1 313 ? -21.216 -1.001  74.069  1.00 73.02  ? 313  GLU C CB  1 
ATOM   10777 C  CG  . GLU C  1 313 ? -22.135 -1.012  72.869  1.00 82.44  ? 313  GLU C CG  1 
ATOM   10778 C  CD  . GLU C  1 313 ? -23.440 -0.296  73.142  1.00 89.17  ? 313  GLU C CD  1 
ATOM   10779 O  OE1 . GLU C  1 313 ? -23.416 0.888   73.559  1.00 87.52  ? 313  GLU C OE1 1 
ATOM   10780 O  OE2 . GLU C  1 313 ? -24.492 -0.934  72.942  1.00 94.73  ? 313  GLU C OE2 1 
ATOM   10781 N  N   . ALA C  1 314 ? -20.883 -3.562  75.517  1.00 26.05  ? 314  ALA C N   1 
ATOM   10782 C  CA  . ALA C  1 314 ? -20.823 -5.008  75.696  1.00 22.87  ? 314  ALA C CA  1 
ATOM   10783 C  C   . ALA C  1 314 ? -21.469 -5.466  76.992  1.00 22.61  ? 314  ALA C C   1 
ATOM   10784 O  O   . ALA C  1 314 ? -22.280 -6.399  77.001  1.00 25.55  ? 314  ALA C O   1 
ATOM   10785 C  CB  . ALA C  1 314 ? -19.394 -5.475  75.668  1.00 18.16  ? 314  ALA C CB  1 
ATOM   10786 N  N   . LEU C  1 315 ? -21.101 -4.814  78.088  1.00 23.55  ? 315  LEU C N   1 
ATOM   10787 C  CA  . LEU C  1 315 ? -21.483 -5.304  79.394  1.00 20.91  ? 315  LEU C CA  1 
ATOM   10788 C  C   . LEU C  1 315 ? -22.992 -5.302  79.538  1.00 26.29  ? 315  LEU C C   1 
ATOM   10789 O  O   . LEU C  1 315 ? -23.555 -6.278  80.043  1.00 32.33  ? 315  LEU C O   1 
ATOM   10790 C  CB  . LEU C  1 315 ? -20.781 -4.524  80.507  1.00 16.78  ? 315  LEU C CB  1 
ATOM   10791 C  CG  . LEU C  1 315 ? -19.254 -4.560  80.371  1.00 17.09  ? 315  LEU C CG  1 
ATOM   10792 C  CD1 . LEU C  1 315 ? -18.524 -4.014  81.590  1.00 19.88  ? 315  LEU C CD1 1 
ATOM   10793 C  CD2 . LEU C  1 315 ? -18.833 -5.960  80.135  1.00 17.37  ? 315  LEU C CD2 1 
ATOM   10794 N  N   . ILE C  1 316 ? -23.659 -4.247  79.064  1.00 25.51  ? 316  ILE C N   1 
ATOM   10795 C  CA  . ILE C  1 316 ? -25.128 -4.227  79.145  1.00 31.39  ? 316  ILE C CA  1 
ATOM   10796 C  C   . ILE C  1 316 ? -25.745 -5.078  78.039  1.00 36.52  ? 316  ILE C C   1 
ATOM   10797 O  O   . ILE C  1 316 ? -26.926 -5.426  78.088  1.00 35.41  ? 316  ILE C O   1 
ATOM   10798 C  CB  . ILE C  1 316 ? -25.758 -2.806  79.077  1.00 29.47  ? 316  ILE C CB  1 
ATOM   10799 C  CG1 . ILE C  1 316 ? -25.843 -2.321  77.632  1.00 36.38  ? 316  ILE C CG1 1 
ATOM   10800 C  CG2 . ILE C  1 316 ? -25.026 -1.813  79.961  1.00 24.16  ? 316  ILE C CG2 1 
ATOM   10801 C  CD1 . ILE C  1 316 ? -26.540 -0.994  77.491  1.00 40.61  ? 316  ILE C CD1 1 
ATOM   10802 N  N   . ASN C  1 317 ? -24.944 -5.398  77.029  1.00 43.77  ? 317  ASN C N   1 
ATOM   10803 C  CA  . ASN C  1 317 ? -25.446 -6.201  75.925  1.00 46.55  ? 317  ASN C CA  1 
ATOM   10804 C  C   . ASN C  1 317 ? -25.542 -7.673  76.281  1.00 44.71  ? 317  ASN C C   1 
ATOM   10805 O  O   . ASN C  1 317 ? -26.376 -8.386  75.736  1.00 43.66  ? 317  ASN C O   1 
ATOM   10806 C  CB  . ASN C  1 317 ? -24.581 -6.001  74.678  1.00 58.25  ? 317  ASN C CB  1 
ATOM   10807 C  CG  . ASN C  1 317 ? -25.365 -5.430  73.521  1.00 62.83  ? 317  ASN C CG  1 
ATOM   10808 O  OD1 . ASN C  1 317 ? -26.485 -5.872  73.254  1.00 67.58  ? 317  ASN C OD1 1 
ATOM   10809 N  ND2 . ASN C  1 317 ? -24.793 -4.437  72.833  1.00 60.20  ? 317  ASN C ND2 1 
ATOM   10810 N  N   . THR C  1 318 ? -24.699 -8.121  77.207  1.00 55.27  ? 318  THR C N   1 
ATOM   10811 C  CA  . THR C  1 318 ? -24.610 -9.547  77.522  1.00 58.54  ? 318  THR C CA  1 
ATOM   10812 C  C   . THR C  1 318 ? -25.079 -9.943  78.924  1.00 68.56  ? 318  THR C C   1 
ATOM   10813 O  O   . THR C  1 318 ? -26.002 -10.749 79.068  1.00 74.68  ? 318  THR C O   1 
ATOM   10814 C  CB  . THR C  1 318 ? -23.189 -10.081 77.371  1.00 37.73  ? 318  THR C CB  1 
ATOM   10815 O  OG1 . THR C  1 318 ? -22.462 -9.818  78.580  1.00 35.81  ? 318  THR C OG1 1 
ATOM   10816 C  CG2 . THR C  1 318 ? -22.487 -9.454  76.162  1.00 35.08  ? 318  THR C CG2 1 
ATOM   10817 N  N   . GLY C  1 319 ? -24.428 -9.390  79.948  1.00 57.38  ? 319  GLY C N   1 
ATOM   10818 C  CA  . GLY C  1 319 ? -24.479 -9.931  81.301  1.00 58.91  ? 319  GLY C CA  1 
ATOM   10819 C  C   . GLY C  1 319 ? -25.849 -10.061 81.956  1.00 59.39  ? 319  GLY C C   1 
ATOM   10820 O  O   . GLY C  1 319 ? -26.856 -9.626  81.399  1.00 54.73  ? 319  GLY C O   1 
ATOM   10821 N  N   . ASP C  1 320 ? -25.893 -10.700 83.127  1.00 79.31  ? 320  ASP C N   1 
ATOM   10822 C  CA  . ASP C  1 320 ? -27.177 -11.020 83.757  1.00 84.09  ? 320  ASP C CA  1 
ATOM   10823 C  C   . ASP C  1 320 ? -27.706 -9.976  84.730  1.00 83.09  ? 320  ASP C C   1 
ATOM   10824 O  O   . ASP C  1 320 ? -27.055 -9.593  85.707  1.00 83.73  ? 320  ASP C O   1 
ATOM   10825 C  CB  . ASP C  1 320 ? -27.184 -12.403 84.409  1.00 79.63  ? 320  ASP C CB  1 
ATOM   10826 C  CG  . ASP C  1 320 ? -28.592 -12.958 84.552  1.00 80.76  ? 320  ASP C CG  1 
ATOM   10827 O  OD1 . ASP C  1 320 ? -29.500 -12.412 83.888  1.00 79.79  ? 320  ASP C OD1 1 
ATOM   10828 O  OD2 . ASP C  1 320 ? -28.792 -13.934 85.309  1.00 82.26  ? 320  ASP C OD2 1 
ATOM   10829 N  N   . PHE C  1 321 ? -28.885 -9.486  84.381  1.00 70.15  ? 321  PHE C N   1 
ATOM   10830 C  CA  . PHE C  1 321 ? -29.624 -8.487  85.134  1.00 64.42  ? 321  PHE C CA  1 
ATOM   10831 C  C   . PHE C  1 321 ? -30.814 -8.973  85.970  1.00 67.97  ? 321  PHE C C   1 
ATOM   10832 O  O   . PHE C  1 321 ? -31.663 -8.170  86.350  1.00 69.93  ? 321  PHE C O   1 
ATOM   10833 C  CB  . PHE C  1 321 ? -29.912 -7.277  84.258  1.00 50.22  ? 321  PHE C CB  1 
ATOM   10834 C  CG  . PHE C  1 321 ? -28.655 -6.638  83.718  1.00 42.97  ? 321  PHE C CG  1 
ATOM   10835 C  CD1 . PHE C  1 321 ? -27.742 -6.047  84.582  1.00 38.30  ? 321  PHE C CD1 1 
ATOM   10836 C  CD2 . PHE C  1 321 ? -28.360 -6.671  82.356  1.00 41.04  ? 321  PHE C CD2 1 
ATOM   10837 C  CE1 . PHE C  1 321 ? -26.580 -5.476  84.093  1.00 36.43  ? 321  PHE C CE1 1 
ATOM   10838 C  CE2 . PHE C  1 321 ? -27.185 -6.100  81.862  1.00 37.85  ? 321  PHE C CE2 1 
ATOM   10839 C  CZ  . PHE C  1 321 ? -26.301 -5.503  82.728  1.00 35.12  ? 321  PHE C CZ  1 
ATOM   10840 N  N   . GLN C  1 322 ? -30.907 -10.288 86.175  1.00 67.09  ? 322  GLN C N   1 
ATOM   10841 C  CA  . GLN C  1 322 ? -32.076 -10.949 86.782  1.00 71.40  ? 322  GLN C CA  1 
ATOM   10842 C  C   . GLN C  1 322 ? -32.692 -10.285 88.026  1.00 72.88  ? 322  GLN C C   1 
ATOM   10843 O  O   . GLN C  1 322 ? -33.911 -10.102 88.109  1.00 73.05  ? 322  GLN C O   1 
ATOM   10844 C  CB  . GLN C  1 322 ? -31.708 -12.396 87.159  1.00 77.34  ? 322  GLN C CB  1 
ATOM   10845 C  CG  . GLN C  1 322 ? -31.718 -13.393 86.015  1.00 80.11  ? 322  GLN C CG  1 
ATOM   10846 C  CD  . GLN C  1 322 ? -33.116 -13.716 85.530  1.00 82.30  ? 322  GLN C CD  1 
ATOM   10847 O  OE1 . GLN C  1 322 ? -33.451 -13.500 84.359  1.00 82.50  ? 322  GLN C OE1 1 
ATOM   10848 N  NE2 . GLN C  1 322 ? -33.942 -14.248 86.427  1.00 82.64  ? 322  GLN C NE2 1 
ATOM   10849 N  N   . ASP C  1 323 ? -31.853 -9.941  88.993  1.00 78.95  ? 323  ASP C N   1 
ATOM   10850 C  CA  . ASP C  1 323 ? -32.329 -9.535  90.312  1.00 80.79  ? 323  ASP C CA  1 
ATOM   10851 C  C   . ASP C  1 323 ? -32.472 -8.019  90.484  1.00 72.20  ? 323  ASP C C   1 
ATOM   10852 O  O   . ASP C  1 323 ? -32.788 -7.530  91.568  1.00 74.42  ? 323  ASP C O   1 
ATOM   10853 C  CB  . ASP C  1 323 ? -31.405 -10.119 91.388  1.00 107.63 ? 323  ASP C CB  1 
ATOM   10854 C  CG  . ASP C  1 323 ? -29.958 -10.258 90.908  1.00 113.41 ? 323  ASP C CG  1 
ATOM   10855 O  OD1 . ASP C  1 323 ? -29.468 -9.348  90.200  1.00 113.03 ? 323  ASP C OD1 1 
ATOM   10856 O  OD2 . ASP C  1 323 ? -29.316 -11.284 91.234  1.00 115.81 ? 323  ASP C OD2 1 
ATOM   10857 N  N   . LEU C  1 324 ? -32.250 -7.281  89.407  1.00 55.00  ? 324  LEU C N   1 
ATOM   10858 C  CA  . LEU C  1 324 ? -32.077 -5.835  89.488  1.00 45.86  ? 324  LEU C CA  1 
ATOM   10859 C  C   . LEU C  1 324 ? -33.337 -5.040  89.210  1.00 39.94  ? 324  LEU C C   1 
ATOM   10860 O  O   . LEU C  1 324 ? -33.980 -5.255  88.188  1.00 40.06  ? 324  LEU C O   1 
ATOM   10861 C  CB  . LEU C  1 324 ? -31.036 -5.408  88.459  1.00 38.01  ? 324  LEU C CB  1 
ATOM   10862 C  CG  . LEU C  1 324 ? -30.428 -4.026  88.628  1.00 19.24  ? 324  LEU C CG  1 
ATOM   10863 C  CD1 . LEU C  1 324 ? -29.655 -3.972  89.946  1.00 22.61  ? 324  LEU C CD1 1 
ATOM   10864 C  CD2 . LEU C  1 324 ? -29.553 -3.721  87.426  1.00 18.62  ? 324  LEU C CD2 1 
ATOM   10865 N  N   . GLN C  1 325 ? -33.678 -4.104  90.094  1.00 30.39  ? 325  GLN C N   1 
ATOM   10866 C  CA  . GLN C  1 325 ? -34.690 -3.113  89.732  1.00 28.60  ? 325  GLN C CA  1 
ATOM   10867 C  C   . GLN C  1 325 ? -34.052 -1.768  89.433  1.00 24.85  ? 325  GLN C C   1 
ATOM   10868 O  O   . GLN C  1 325 ? -33.170 -1.272  90.163  1.00 23.93  ? 325  GLN C O   1 
ATOM   10869 C  CB  . GLN C  1 325 ? -35.800 -2.970  90.773  1.00 42.40  ? 325  GLN C CB  1 
ATOM   10870 C  CG  . GLN C  1 325 ? -36.378 -4.278  91.245  1.00 48.96  ? 325  GLN C CG  1 
ATOM   10871 C  CD  . GLN C  1 325 ? -35.919 -4.592  92.644  1.00 53.60  ? 325  GLN C CD  1 
ATOM   10872 O  OE1 . GLN C  1 325 ? -36.589 -4.237  93.618  1.00 55.20  ? 325  GLN C OE1 1 
ATOM   10873 N  NE2 . GLN C  1 325 ? -34.749 -5.226  92.763  1.00 53.28  ? 325  GLN C NE2 1 
ATOM   10874 N  N   . VAL C  1 326 ? -34.492 -1.189  88.330  1.00 20.16  ? 326  VAL C N   1 
ATOM   10875 C  CA  . VAL C  1 326 ? -33.899 0.028   87.855  1.00 19.29  ? 326  VAL C CA  1 
ATOM   10876 C  C   . VAL C  1 326 ? -35.001 0.932   87.383  1.00 19.65  ? 326  VAL C C   1 
ATOM   10877 O  O   . VAL C  1 326 ? -35.843 0.531   86.582  1.00 20.36  ? 326  VAL C O   1 
ATOM   10878 C  CB  . VAL C  1 326 ? -32.931 -0.241  86.692  1.00 21.11  ? 326  VAL C CB  1 
ATOM   10879 C  CG1 . VAL C  1 326 ? -32.598 1.030   85.980  1.00 18.18  ? 326  VAL C CG1 1 
ATOM   10880 C  CG2 . VAL C  1 326 ? -31.661 -0.862  87.201  1.00 18.35  ? 326  VAL C CG2 1 
ATOM   10881 N  N   . LEU C  1 327 ? -34.988 2.154   87.904  1.00 21.05  ? 327  LEU C N   1 
ATOM   10882 C  CA  . LEU C  1 327 ? -35.842 3.236   87.442  1.00 21.49  ? 327  LEU C CA  1 
ATOM   10883 C  C   . LEU C  1 327 ? -34.961 4.254   86.686  1.00 21.01  ? 327  LEU C C   1 
ATOM   10884 O  O   . LEU C  1 327 ? -33.995 4.801   87.256  1.00 18.61  ? 327  LEU C O   1 
ATOM   10885 C  CB  . LEU C  1 327 ? -36.547 3.858   88.646  1.00 19.84  ? 327  LEU C CB  1 
ATOM   10886 C  CG  . LEU C  1 327 ? -37.084 5.269   88.529  1.00 19.90  ? 327  LEU C CG  1 
ATOM   10887 C  CD1 . LEU C  1 327 ? -38.091 5.317   87.426  1.00 38.96  ? 327  LEU C CD1 1 
ATOM   10888 C  CD2 . LEU C  1 327 ? -37.711 5.670   89.825  1.00 20.34  ? 327  LEU C CD2 1 
ATOM   10889 N  N   . VAL C  1 328 ? -35.265 4.460   85.396  1.00 24.97  ? 328  VAL C N   1 
ATOM   10890 C  CA  . VAL C  1 328 ? -34.534 5.402   84.532  1.00 26.06  ? 328  VAL C CA  1 
ATOM   10891 C  C   . VAL C  1 328 ? -35.444 6.442   83.918  1.00 27.30  ? 328  VAL C C   1 
ATOM   10892 O  O   . VAL C  1 328 ? -36.655 6.245   83.791  1.00 27.89  ? 328  VAL C O   1 
ATOM   10893 C  CB  . VAL C  1 328 ? -33.885 4.722   83.327  1.00 18.10  ? 328  VAL C CB  1 
ATOM   10894 C  CG1 . VAL C  1 328 ? -32.872 3.701   83.765  1.00 17.69  ? 328  VAL C CG1 1 
ATOM   10895 C  CG2 . VAL C  1 328 ? -34.949 4.107   82.446  1.00 19.02  ? 328  VAL C CG2 1 
ATOM   10896 N  N   . GLY C  1 329 ? -34.870 7.552   83.493  1.00 18.25  ? 329  GLY C N   1 
ATOM   10897 C  CA  . GLY C  1 329 ? -35.718 8.485   82.788  1.00 18.81  ? 329  GLY C CA  1 
ATOM   10898 C  C   . GLY C  1 329 ? -35.024 9.698   82.241  1.00 18.36  ? 329  GLY C C   1 
ATOM   10899 O  O   . GLY C  1 329 ? -33.855 9.918   82.521  1.00 17.58  ? 329  GLY C O   1 
ATOM   10900 N  N   . VAL C  1 330 ? -35.739 10.497  81.456  1.00 30.07  ? 330  VAL C N   1 
ATOM   10901 C  CA  . VAL C  1 330 ? -35.125 11.685  80.850  1.00 29.80  ? 330  VAL C CA  1 
ATOM   10902 C  C   . VAL C  1 330 ? -36.003 12.920  81.051  1.00 31.01  ? 330  VAL C C   1 
ATOM   10903 O  O   . VAL C  1 330 ? -37.115 12.804  81.524  1.00 34.54  ? 330  VAL C O   1 
ATOM   10904 C  CB  . VAL C  1 330 ? -34.835 11.477  79.357  1.00 18.78  ? 330  VAL C CB  1 
ATOM   10905 C  CG1 . VAL C  1 330 ? -34.344 10.076  79.114  1.00 18.51  ? 330  VAL C CG1 1 
ATOM   10906 C  CG2 . VAL C  1 330 ? -36.077 11.724  78.537  1.00 19.82  ? 330  VAL C CG2 1 
ATOM   10907 N  N   . VAL C  1 331 ? -35.513 14.104  80.711  1.00 27.11  ? 331  VAL C N   1 
ATOM   10908 C  CA  . VAL C  1 331 ? -36.337 15.304  80.844  1.00 27.28  ? 331  VAL C CA  1 
ATOM   10909 C  C   . VAL C  1 331 ? -36.681 15.840  79.464  1.00 32.28  ? 331  VAL C C   1 
ATOM   10910 O  O   . VAL C  1 331 ? -35.991 15.532  78.478  1.00 35.53  ? 331  VAL C O   1 
ATOM   10911 C  CB  . VAL C  1 331 ? -35.665 16.403  81.695  1.00 21.72  ? 331  VAL C CB  1 
ATOM   10912 C  CG1 . VAL C  1 331 ? -35.150 15.814  82.985  1.00 22.24  ? 331  VAL C CG1 1 
ATOM   10913 C  CG2 . VAL C  1 331 ? -34.533 17.071  80.942  1.00 18.98  ? 331  VAL C CG2 1 
ATOM   10914 N  N   . LYS C  1 332 ? -37.759 16.620  79.402  1.00 30.15  ? 332  LYS C N   1 
ATOM   10915 C  CA  . LYS C  1 332 ? -38.387 16.984  78.137  1.00 31.39  ? 332  LYS C CA  1 
ATOM   10916 C  C   . LYS C  1 332 ? -37.374 17.479  77.114  1.00 30.09  ? 332  LYS C C   1 
ATOM   10917 O  O   . LYS C  1 332 ? -37.261 16.884  76.047  1.00 34.10  ? 332  LYS C O   1 
ATOM   10918 C  CB  . LYS C  1 332 ? -39.480 18.036  78.355  1.00 41.20  ? 332  LYS C CB  1 
ATOM   10919 C  CG  . LYS C  1 332 ? -40.537 18.098  77.251  1.00 44.30  ? 332  LYS C CG  1 
ATOM   10920 C  CD  . LYS C  1 332 ? -41.317 19.414  77.294  1.00 46.76  ? 332  LYS C CD  1 
ATOM   10921 C  CE  . LYS C  1 332 ? -42.590 19.345  76.462  1.00 50.25  ? 332  LYS C CE  1 
ATOM   10922 N  NZ  . LYS C  1 332 ? -42.401 18.680  75.135  1.00 51.97  ? 332  LYS C NZ  1 
ATOM   10923 N  N   . ASP C  1 333 ? -36.611 18.522  77.432  1.00 23.18  ? 333  ASP C N   1 
ATOM   10924 C  CA  . ASP C  1 333 ? -35.547 18.933  76.516  1.00 23.62  ? 333  ASP C CA  1 
ATOM   10925 C  C   . ASP C  1 333 ? -34.152 18.798  77.111  1.00 22.24  ? 333  ASP C C   1 
ATOM   10926 O  O   . ASP C  1 333 ? -33.710 19.666  77.855  1.00 25.84  ? 333  ASP C O   1 
ATOM   10927 C  CB  . ASP C  1 333 ? -35.780 20.371  76.085  1.00 32.72  ? 333  ASP C CB  1 
ATOM   10928 C  CG  . ASP C  1 333 ? -37.242 20.727  76.087  1.00 39.89  ? 333  ASP C CG  1 
ATOM   10929 O  OD1 . ASP C  1 333 ? -37.774 20.969  77.193  1.00 42.02  ? 333  ASP C OD1 1 
ATOM   10930 O  OD2 . ASP C  1 333 ? -37.864 20.748  74.998  1.00 42.92  ? 333  ASP C OD2 1 
ATOM   10931 N  N   . GLU C  1 334 ? -33.436 17.753  76.700  1.00 19.54  ? 334  GLU C N   1 
ATOM   10932 C  CA  . GLU C  1 334 ? -32.114 17.430  77.232  1.00 18.54  ? 334  GLU C CA  1 
ATOM   10933 C  C   . GLU C  1 334 ? -30.975 18.208  76.588  1.00 18.34  ? 334  GLU C C   1 
ATOM   10934 O  O   . GLU C  1 334 ? -29.911 18.366  77.165  1.00 17.69  ? 334  GLU C O   1 
ATOM   10935 C  CB  . GLU C  1 334 ? -31.848 15.939  77.056  1.00 32.56  ? 334  GLU C CB  1 
ATOM   10936 C  CG  . GLU C  1 334 ? -32.709 15.053  77.909  1.00 36.90  ? 334  GLU C CG  1 
ATOM   10937 C  CD  . GLU C  1 334 ? -32.080 14.786  79.249  1.00 41.64  ? 334  GLU C CD  1 
ATOM   10938 O  OE1 . GLU C  1 334 ? -30.946 15.248  79.489  1.00 40.96  ? 334  GLU C OE1 1 
ATOM   10939 O  OE2 . GLU C  1 334 ? -32.718 14.104  80.065  1.00 46.47  ? 334  GLU C OE2 1 
ATOM   10940 N  N   . GLY C  1 335 ? -31.186 18.654  75.365  1.00 18.97  ? 335  GLY C N   1 
ATOM   10941 C  CA  . GLY C  1 335 ? -30.107 19.255  74.626  1.00 18.88  ? 335  GLY C CA  1 
ATOM   10942 C  C   . GLY C  1 335 ? -29.891 20.721  74.930  1.00 22.80  ? 335  GLY C C   1 
ATOM   10943 O  O   . GLY C  1 335 ? -28.762 21.200  74.849  1.00 25.16  ? 335  GLY C O   1 
ATOM   10944 N  N   . SER C  1 336 ? -30.958 21.437  75.281  1.00 22.03  ? 336  SER C N   1 
ATOM   10945 C  CA  . SER C  1 336 ? -30.925 22.900  75.297  1.00 22.77  ? 336  SER C CA  1 
ATOM   10946 C  C   . SER C  1 336 ? -29.814 23.481  76.145  1.00 25.47  ? 336  SER C C   1 
ATOM   10947 O  O   . SER C  1 336 ? -29.098 24.365  75.691  1.00 26.45  ? 336  SER C O   1 
ATOM   10948 C  CB  . SER C  1 336 ? -32.269 23.486  75.706  1.00 21.26  ? 336  SER C CB  1 
ATOM   10949 O  OG  . SER C  1 336 ? -32.914 22.650  76.637  1.00 31.81  ? 336  SER C OG  1 
ATOM   10950 N  N   . TYR C  1 337 ? -29.647 22.972  77.358  1.00 36.41  ? 337  TYR C N   1 
ATOM   10951 C  CA  . TYR C  1 337 ? -28.572 23.445  78.232  1.00 39.25  ? 337  TYR C CA  1 
ATOM   10952 C  C   . TYR C  1 337 ? -27.213 23.511  77.502  1.00 34.39  ? 337  TYR C C   1 
ATOM   10953 O  O   . TYR C  1 337 ? -26.503 24.510  77.589  1.00 34.66  ? 337  TYR C O   1 
ATOM   10954 C  CB  . TYR C  1 337 ? -28.485 22.557  79.491  1.00 44.47  ? 337  TYR C CB  1 
ATOM   10955 C  CG  . TYR C  1 337 ? -27.578 23.080  80.577  1.00 44.84  ? 337  TYR C CG  1 
ATOM   10956 C  CD1 . TYR C  1 337 ? -26.204 22.937  80.484  1.00 45.62  ? 337  TYR C CD1 1 
ATOM   10957 C  CD2 . TYR C  1 337 ? -28.099 23.708  81.697  1.00 48.86  ? 337  TYR C CD2 1 
ATOM   10958 C  CE1 . TYR C  1 337 ? -25.361 23.418  81.464  1.00 50.63  ? 337  TYR C CE1 1 
ATOM   10959 C  CE2 . TYR C  1 337 ? -27.267 24.194  82.697  1.00 54.12  ? 337  TYR C CE2 1 
ATOM   10960 C  CZ  . TYR C  1 337 ? -25.891 24.047  82.576  1.00 56.34  ? 337  TYR C CZ  1 
ATOM   10961 O  OH  . TYR C  1 337 ? -25.039 24.523  83.566  1.00 59.52  ? 337  TYR C OH  1 
ATOM   10962 N  N   . PHE C  1 338 ? -26.881 22.467  76.750  1.00 23.01  ? 338  PHE C N   1 
ATOM   10963 C  CA  . PHE C  1 338 ? -25.546 22.318  76.185  1.00 21.58  ? 338  PHE C CA  1 
ATOM   10964 C  C   . PHE C  1 338 ? -25.320 23.161  74.947  1.00 24.97  ? 338  PHE C C   1 
ATOM   10965 O  O   . PHE C  1 338 ? -24.173 23.350  74.529  1.00 24.82  ? 338  PHE C O   1 
ATOM   10966 C  CB  . PHE C  1 338 ? -25.257 20.855  75.856  1.00 26.21  ? 338  PHE C CB  1 
ATOM   10967 C  CG  . PHE C  1 338 ? -25.382 19.947  77.032  1.00 30.68  ? 338  PHE C CG  1 
ATOM   10968 C  CD1 . PHE C  1 338 ? -26.618 19.436  77.403  1.00 32.03  ? 338  PHE C CD1 1 
ATOM   10969 C  CD2 . PHE C  1 338 ? -24.271 19.610  77.781  1.00 32.34  ? 338  PHE C CD2 1 
ATOM   10970 C  CE1 . PHE C  1 338 ? -26.746 18.603  78.496  1.00 32.01  ? 338  PHE C CE1 1 
ATOM   10971 C  CE2 . PHE C  1 338 ? -24.386 18.773  78.879  1.00 32.69  ? 338  PHE C CE2 1 
ATOM   10972 C  CZ  . PHE C  1 338 ? -25.628 18.273  79.238  1.00 33.39  ? 338  PHE C CZ  1 
ATOM   10973 N  N   . LEU C  1 339 ? -26.399 23.660  74.352  1.00 37.62  ? 339  LEU C N   1 
ATOM   10974 C  CA  . LEU C  1 339 ? -26.279 24.441  73.122  1.00 39.08  ? 339  LEU C CA  1 
ATOM   10975 C  C   . LEU C  1 339 ? -25.545 25.763  73.325  1.00 41.59  ? 339  LEU C C   1 
ATOM   10976 O  O   . LEU C  1 339 ? -24.665 26.119  72.543  1.00 44.67  ? 339  LEU C O   1 
ATOM   10977 C  CB  . LEU C  1 339 ? -27.649 24.696  72.509  1.00 30.93  ? 339  LEU C CB  1 
ATOM   10978 C  CG  . LEU C  1 339 ? -28.322 23.447  71.963  1.00 28.51  ? 339  LEU C CG  1 
ATOM   10979 C  CD1 . LEU C  1 339 ? -29.673 23.813  71.395  1.00 30.39  ? 339  LEU C CD1 1 
ATOM   10980 C  CD2 . LEU C  1 339 ? -27.447 22.800  70.905  1.00 26.68  ? 339  LEU C CD2 1 
ATOM   10981 N  N   . VAL C  1 340 ? -25.884 26.473  74.397  1.00 36.50  ? 340  VAL C N   1 
ATOM   10982 C  CA  . VAL C  1 340 ? -25.324 27.794  74.657  1.00 34.48  ? 340  VAL C CA  1 
ATOM   10983 C  C   . VAL C  1 340 ? -23.860 27.674  75.042  1.00 39.31  ? 340  VAL C C   1 
ATOM   10984 O  O   . VAL C  1 340 ? -23.162 28.665  75.231  1.00 45.49  ? 340  VAL C O   1 
ATOM   10985 C  CB  . VAL C  1 340 ? -26.080 28.518  75.764  1.00 22.65  ? 340  VAL C CB  1 
ATOM   10986 C  CG1 . VAL C  1 340 ? -27.567 28.564  75.444  1.00 21.97  ? 340  VAL C CG1 1 
ATOM   10987 C  CG2 . VAL C  1 340 ? -25.831 27.831  77.082  1.00 20.63  ? 340  VAL C CG2 1 
ATOM   10988 N  N   . TYR C  1 341 ? -23.397 26.441  75.133  1.00 34.38  ? 341  TYR C N   1 
ATOM   10989 C  CA  . TYR C  1 341 ? -22.005 26.154  75.438  1.00 35.06  ? 341  TYR C CA  1 
ATOM   10990 C  C   . TYR C  1 341 ? -21.050 26.121  74.236  1.00 36.28  ? 341  TYR C C   1 
ATOM   10991 O  O   . TYR C  1 341 ? -19.952 25.575  74.320  1.00 34.17  ? 341  TYR C O   1 
ATOM   10992 C  CB  . TYR C  1 341 ? -21.856 24.967  76.374  1.00 35.66  ? 341  TYR C CB  1 
ATOM   10993 C  CG  . TYR C  1 341 ? -22.013 25.394  77.811  1.00 38.01  ? 341  TYR C CG  1 
ATOM   10994 C  CD1 . TYR C  1 341 ? -23.278 25.546  78.382  1.00 41.38  ? 341  TYR C CD1 1 
ATOM   10995 C  CD2 . TYR C  1 341 ? -20.900 25.671  78.594  1.00 37.26  ? 341  TYR C CD2 1 
ATOM   10996 C  CE1 . TYR C  1 341 ? -23.425 25.940  79.706  1.00 41.72  ? 341  TYR C CE1 1 
ATOM   10997 C  CE2 . TYR C  1 341 ? -21.031 26.073  79.909  1.00 38.03  ? 341  TYR C CE2 1 
ATOM   10998 C  CZ  . TYR C  1 341 ? -22.291 26.203  80.463  1.00 40.63  ? 341  TYR C CZ  1 
ATOM   10999 O  OH  . TYR C  1 341 ? -22.407 26.606  81.773  1.00 41.57  ? 341  TYR C OH  1 
ATOM   11000 N  N   . GLY C  1 342 ? -21.472 26.707  73.121  1.00 51.23  ? 342  GLY C N   1 
ATOM   11001 C  CA  . GLY C  1 342 ? -20.578 26.825  71.986  1.00 54.83  ? 342  GLY C CA  1 
ATOM   11002 C  C   . GLY C  1 342 ? -20.896 26.166  70.665  1.00 55.45  ? 342  GLY C C   1 
ATOM   11003 O  O   . GLY C  1 342 ? -20.021 26.009  69.810  1.00 60.18  ? 342  GLY C O   1 
ATOM   11004 N  N   . VAL C  1 343 ? -22.140 25.747  70.504  1.00 36.12  ? 343  VAL C N   1 
ATOM   11005 C  CA  . VAL C  1 343 ? -22.726 25.785  69.178  1.00 30.71  ? 343  VAL C CA  1 
ATOM   11006 C  C   . VAL C  1 343 ? -23.046 27.257  68.944  1.00 29.94  ? 343  VAL C C   1 
ATOM   11007 O  O   . VAL C  1 343 ? -23.577 27.923  69.835  1.00 27.69  ? 343  VAL C O   1 
ATOM   11008 C  CB  . VAL C  1 343 ? -24.007 24.962  69.098  1.00 29.54  ? 343  VAL C CB  1 
ATOM   11009 C  CG1 . VAL C  1 343 ? -24.810 25.323  67.846  1.00 28.84  ? 343  VAL C CG1 1 
ATOM   11010 C  CG2 . VAL C  1 343 ? -23.661 23.492  69.128  1.00 29.80  ? 343  VAL C CG2 1 
ATOM   11011 N  N   . PRO C  1 344 ? -22.674 27.786  67.768  1.00 33.67  ? 344  PRO C N   1 
ATOM   11012 C  CA  . PRO C  1 344 ? -22.957 29.179  67.416  1.00 34.16  ? 344  PRO C CA  1 
ATOM   11013 C  C   . PRO C  1 344 ? -24.435 29.398  67.218  1.00 36.49  ? 344  PRO C C   1 
ATOM   11014 O  O   . PRO C  1 344 ? -25.138 28.473  66.810  1.00 37.61  ? 344  PRO C O   1 
ATOM   11015 C  CB  . PRO C  1 344 ? -22.239 29.354  66.081  1.00 27.34  ? 344  PRO C CB  1 
ATOM   11016 C  CG  . PRO C  1 344 ? -21.144 28.373  66.134  1.00 26.99  ? 344  PRO C CG  1 
ATOM   11017 C  CD  . PRO C  1 344 ? -21.744 27.174  66.810  1.00 27.17  ? 344  PRO C CD  1 
ATOM   11018 N  N   . GLY C  1 345 ? -24.889 30.610  67.522  1.00 34.79  ? 345  GLY C N   1 
ATOM   11019 C  CA  . GLY C  1 345 ? -26.270 30.997  67.317  1.00 36.43  ? 345  GLY C CA  1 
ATOM   11020 C  C   . GLY C  1 345 ? -27.117 30.938  68.569  1.00 38.29  ? 345  GLY C C   1 
ATOM   11021 O  O   . GLY C  1 345 ? -28.196 31.531  68.602  1.00 38.99  ? 345  GLY C O   1 
ATOM   11022 N  N   . PHE C  1 346 ? -26.630 30.232  69.591  1.00 50.01  ? 346  PHE C N   1 
ATOM   11023 C  CA  . PHE C  1 346 ? -27.420 29.965  70.793  1.00 53.54  ? 346  PHE C CA  1 
ATOM   11024 C  C   . PHE C  1 346 ? -26.946 30.747  72.005  1.00 60.94  ? 346  PHE C C   1 
ATOM   11025 O  O   . PHE C  1 346 ? -25.754 30.760  72.326  1.00 64.88  ? 346  PHE C O   1 
ATOM   11026 C  CB  . PHE C  1 346 ? -27.428 28.472  71.124  1.00 37.90  ? 346  PHE C CB  1 
ATOM   11027 C  CG  . PHE C  1 346 ? -28.150 27.642  70.115  1.00 34.38  ? 346  PHE C CG  1 
ATOM   11028 C  CD1 . PHE C  1 346 ? -27.477 27.128  69.012  1.00 32.43  ? 346  PHE C CD1 1 
ATOM   11029 C  CD2 . PHE C  1 346 ? -29.503 27.389  70.253  1.00 32.14  ? 346  PHE C CD2 1 
ATOM   11030 C  CE1 . PHE C  1 346 ? -28.142 26.374  68.069  1.00 30.48  ? 346  PHE C CE1 1 
ATOM   11031 C  CE2 . PHE C  1 346 ? -30.175 26.637  69.315  1.00 30.59  ? 346  PHE C CE2 1 
ATOM   11032 C  CZ  . PHE C  1 346 ? -29.495 26.129  68.218  1.00 29.67  ? 346  PHE C CZ  1 
ATOM   11033 N  N   . SER C  1 347 ? -27.900 31.388  72.680  1.00 54.06  ? 347  SER C N   1 
ATOM   11034 C  CA  . SER C  1 347 ? -27.623 32.206  73.854  1.00 51.08  ? 347  SER C CA  1 
ATOM   11035 C  C   . SER C  1 347 ? -28.801 32.197  74.806  1.00 48.17  ? 347  SER C C   1 
ATOM   11036 O  O   . SER C  1 347 ? -29.945 32.050  74.387  1.00 48.49  ? 347  SER C O   1 
ATOM   11037 C  CB  . SER C  1 347 ? -27.326 33.643  73.452  1.00 56.91  ? 347  SER C CB  1 
ATOM   11038 O  OG  . SER C  1 347 ? -27.136 34.438  74.603  1.00 59.10  ? 347  SER C OG  1 
ATOM   11039 N  N   . LYS C  1 348 ? -28.515 32.371  76.091  1.00 49.41  ? 348  LYS C N   1 
ATOM   11040 C  CA  . LYS C  1 348 ? -29.544 32.342  77.120  1.00 46.80  ? 348  LYS C CA  1 
ATOM   11041 C  C   . LYS C  1 348 ? -30.444 33.562  76.999  1.00 48.74  ? 348  LYS C C   1 
ATOM   11042 O  O   . LYS C  1 348 ? -31.533 33.604  77.564  1.00 48.58  ? 348  LYS C O   1 
ATOM   11043 C  CB  . LYS C  1 348 ? -28.903 32.304  78.513  1.00 37.23  ? 348  LYS C CB  1 
ATOM   11044 C  CG  . LYS C  1 348 ? -28.261 33.626  78.961  1.00 33.64  ? 348  LYS C CG  1 
ATOM   11045 C  CD  . LYS C  1 348 ? -27.840 33.576  80.433  1.00 29.00  ? 348  LYS C CD  1 
ATOM   11046 C  CE  . LYS C  1 348 ? -28.492 34.668  81.246  1.00 28.71  ? 348  LYS C CE  1 
ATOM   11047 N  NZ  . LYS C  1 348 ? -28.088 35.999  80.740  1.00 31.54  ? 348  LYS C NZ  1 
ATOM   11048 N  N   . ASP C  1 349 ? -29.988 34.551  76.243  1.00 48.18  ? 349  ASP C N   1 
ATOM   11049 C  CA  . ASP C  1 349 ? -30.648 35.843  76.223  1.00 51.65  ? 349  ASP C CA  1 
ATOM   11050 C  C   . ASP C  1 349 ? -31.751 35.993  75.187  1.00 54.09  ? 349  ASP C C   1 
ATOM   11051 O  O   . ASP C  1 349 ? -32.917 36.214  75.542  1.00 56.39  ? 349  ASP C O   1 
ATOM   11052 C  CB  . ASP C  1 349 ? -29.612 36.947  76.133  1.00 52.61  ? 349  ASP C CB  1 
ATOM   11053 C  CG  . ASP C  1 349 ? -28.851 37.103  77.431  1.00 55.66  ? 349  ASP C CG  1 
ATOM   11054 O  OD1 . ASP C  1 349 ? -29.361 37.817  78.325  1.00 57.53  ? 349  ASP C OD1 1 
ATOM   11055 O  OD2 . ASP C  1 349 ? -27.771 36.486  77.575  1.00 55.03  ? 349  ASP C OD2 1 
ATOM   11056 N  N   . ASN C  1 350 ? -31.393 35.883  73.915  1.00 48.90  ? 350  ASN C N   1 
ATOM   11057 C  CA  . ASN C  1 350 ? -32.398 35.959  72.857  1.00 49.33  ? 350  ASN C CA  1 
ATOM   11058 C  C   . ASN C  1 350 ? -33.147 34.643  72.566  1.00 48.96  ? 350  ASN C C   1 
ATOM   11059 O  O   . ASN C  1 350 ? -32.885 33.597  73.159  1.00 43.17  ? 350  ASN C O   1 
ATOM   11060 C  CB  . ASN C  1 350 ? -31.771 36.499  71.579  1.00 47.03  ? 350  ASN C CB  1 
ATOM   11061 C  CG  . ASN C  1 350 ? -30.616 35.656  71.108  1.00 45.39  ? 350  ASN C CG  1 
ATOM   11062 O  OD1 . ASN C  1 350 ? -30.126 34.786  71.834  1.00 43.02  ? 350  ASN C OD1 1 
ATOM   11063 N  ND2 . ASN C  1 350 ? -30.163 35.913  69.886  1.00 47.61  ? 350  ASN C ND2 1 
ATOM   11064 N  N   . GLU C  1 351 ? -34.077 34.707  71.625  1.00 57.86  ? 351  GLU C N   1 
ATOM   11065 C  CA  . GLU C  1 351 ? -34.910 33.563  71.299  1.00 60.79  ? 351  GLU C CA  1 
ATOM   11066 C  C   . GLU C  1 351 ? -34.109 32.486  70.581  1.00 58.12  ? 351  GLU C C   1 
ATOM   11067 O  O   . GLU C  1 351 ? -34.620 31.400  70.318  1.00 57.40  ? 351  GLU C O   1 
ATOM   11068 C  CB  . GLU C  1 351 ? -36.074 34.016  70.429  1.00 77.60  ? 351  GLU C CB  1 
ATOM   11069 C  CG  . GLU C  1 351 ? -37.344 33.251  70.677  1.00 85.60  ? 351  GLU C CG  1 
ATOM   11070 C  CD  . GLU C  1 351 ? -38.539 33.924  70.045  1.00 94.82  ? 351  GLU C CD  1 
ATOM   11071 O  OE1 . GLU C  1 351 ? -38.336 34.837  69.209  1.00 96.39  ? 351  GLU C OE1 1 
ATOM   11072 O  OE2 . GLU C  1 351 ? -39.680 33.544  70.392  1.00 98.74  ? 351  GLU C OE2 1 
ATOM   11073 N  N   . SER C  1 352 ? -32.860 32.812  70.256  1.00 65.77  ? 352  SER C N   1 
ATOM   11074 C  CA  . SER C  1 352 ? -31.928 31.904  69.589  1.00 60.54  ? 352  SER C CA  1 
ATOM   11075 C  C   . SER C  1 352 ? -32.493 31.184  68.378  1.00 60.22  ? 352  SER C C   1 
ATOM   11076 O  O   . SER C  1 352 ? -32.372 29.970  68.281  1.00 61.73  ? 352  SER C O   1 
ATOM   11077 C  CB  . SER C  1 352 ? -31.377 30.870  70.568  1.00 40.43  ? 352  SER C CB  1 
ATOM   11078 O  OG  . SER C  1 352 ? -30.438 31.462  71.437  1.00 37.98  ? 352  SER C OG  1 
ATOM   11079 N  N   . LEU C  1 353 ? -33.116 31.925  67.468  1.00 47.46  ? 353  LEU C N   1 
ATOM   11080 C  CA  . LEU C  1 353 ? -33.538 31.354  66.194  1.00 43.61  ? 353  LEU C CA  1 
ATOM   11081 C  C   . LEU C  1 353 ? -32.323 31.290  65.274  1.00 42.21  ? 353  LEU C C   1 
ATOM   11082 O  O   . LEU C  1 353 ? -31.590 32.264  65.162  1.00 45.77  ? 353  LEU C O   1 
ATOM   11083 C  CB  . LEU C  1 353 ? -34.621 32.212  65.555  1.00 33.04  ? 353  LEU C CB  1 
ATOM   11084 C  CG  . LEU C  1 353 ? -35.849 32.563  66.383  1.00 33.61  ? 353  LEU C CG  1 
ATOM   11085 C  CD1 . LEU C  1 353 ? -36.822 33.247  65.475  1.00 35.41  ? 353  LEU C CD1 1 
ATOM   11086 C  CD2 . LEU C  1 353 ? -36.481 31.343  66.990  1.00 32.74  ? 353  LEU C CD2 1 
ATOM   11087 N  N   . ILE C  1 354 ? -32.106 30.161  64.607  1.00 31.52  ? 354  ILE C N   1 
ATOM   11088 C  CA  . ILE C  1 354 ? -30.860 29.966  63.868  1.00 30.30  ? 354  ILE C CA  1 
ATOM   11089 C  C   . ILE C  1 354 ? -31.087 29.855  62.364  1.00 36.97  ? 354  ILE C C   1 
ATOM   11090 O  O   . ILE C  1 354 ? -32.188 29.524  61.910  1.00 36.58  ? 354  ILE C O   1 
ATOM   11091 C  CB  . ILE C  1 354 ? -30.102 28.719  64.361  1.00 28.74  ? 354  ILE C CB  1 
ATOM   11092 C  CG1 . ILE C  1 354 ? -30.920 27.460  64.065  1.00 28.54  ? 354  ILE C CG1 1 
ATOM   11093 C  CG2 . ILE C  1 354 ? -29.803 28.841  65.840  1.00 27.74  ? 354  ILE C CG2 1 
ATOM   11094 C  CD1 . ILE C  1 354 ? -30.355 26.178  64.623  1.00 27.12  ? 354  ILE C CD1 1 
ATOM   11095 N  N   . SER C  1 355 ? -30.048 30.148  61.586  1.00 42.06  ? 355  SER C N   1 
ATOM   11096 C  CA  . SER C  1 355 ? -30.131 29.987  60.140  1.00 45.21  ? 355  SER C CA  1 
ATOM   11097 C  C   . SER C  1 355 ? -30.022 28.513  59.824  1.00 39.93  ? 355  SER C C   1 
ATOM   11098 O  O   . SER C  1 355 ? -29.811 27.693  60.716  1.00 36.60  ? 355  SER C O   1 
ATOM   11099 C  CB  . SER C  1 355 ? -29.003 30.742  59.438  1.00 73.71  ? 355  SER C CB  1 
ATOM   11100 O  OG  . SER C  1 355 ? -27.768 30.066  59.593  1.00 77.24  ? 355  SER C OG  1 
ATOM   11101 N  N   . ARG C  1 356 ? -30.146 28.161  58.555  1.00 47.20  ? 356  ARG C N   1 
ATOM   11102 C  CA  . ARG C  1 356 ? -30.054 26.757  58.225  1.00 47.79  ? 356  ARG C CA  1 
ATOM   11103 C  C   . ARG C  1 356 ? -28.601 26.346  58.265  1.00 48.19  ? 356  ARG C C   1 
ATOM   11104 O  O   . ARG C  1 356 ? -28.279 25.266  58.745  1.00 49.55  ? 356  ARG C O   1 
ATOM   11105 C  CB  . ARG C  1 356 ? -30.683 26.432  56.874  1.00 48.06  ? 356  ARG C CB  1 
ATOM   11106 C  CG  . ARG C  1 356 ? -30.419 25.008  56.465  1.00 48.32  ? 356  ARG C CG  1 
ATOM   11107 C  CD  . ARG C  1 356 ? -31.529 24.377  55.662  1.00 50.99  ? 356  ARG C CD  1 
ATOM   11108 N  NE  . ARG C  1 356 ? -31.215 22.965  55.471  1.00 52.84  ? 356  ARG C NE  1 
ATOM   11109 C  CZ  . ARG C  1 356 ? -31.740 21.977  56.189  1.00 51.88  ? 356  ARG C CZ  1 
ATOM   11110 N  NH1 . ARG C  1 356 ? -32.642 22.250  57.126  1.00 50.35  ? 356  ARG C NH1 1 
ATOM   11111 N  NH2 . ARG C  1 356 ? -31.379 20.717  55.954  1.00 51.09  ? 356  ARG C NH2 1 
ATOM   11112 N  N   . ALA C  1 357 ? -27.724 27.221  57.782  1.00 43.63  ? 357  ALA C N   1 
ATOM   11113 C  CA  . ALA C  1 357 ? -26.292 26.933  57.773  1.00 41.49  ? 357  ALA C CA  1 
ATOM   11114 C  C   . ALA C  1 357 ? -25.779 26.774  59.188  1.00 39.08  ? 357  ALA C C   1 
ATOM   11115 O  O   . ALA C  1 357 ? -24.905 25.941  59.444  1.00 38.40  ? 357  ALA C O   1 
ATOM   11116 C  CB  . ALA C  1 357 ? -25.535 28.018  57.063  1.00 48.51  ? 357  ALA C CB  1 
ATOM   11117 N  N   . GLN C  1 358 ? -26.335 27.569  60.102  1.00 43.96  ? 358  GLN C N   1 
ATOM   11118 C  CA  . GLN C  1 358 ? -26.024 27.450  61.525  1.00 43.32  ? 358  GLN C CA  1 
ATOM   11119 C  C   . GLN C  1 358 ? -26.414 26.084  62.050  1.00 41.22  ? 358  GLN C C   1 
ATOM   11120 O  O   . GLN C  1 358 ? -25.637 25.435  62.751  1.00 40.45  ? 358  GLN C O   1 
ATOM   11121 C  CB  . GLN C  1 358 ? -26.720 28.535  62.342  1.00 44.42  ? 358  GLN C CB  1 
ATOM   11122 C  CG  . GLN C  1 358 ? -25.959 29.834  62.343  1.00 50.12  ? 358  GLN C CG  1 
ATOM   11123 C  CD  . GLN C  1 358 ? -26.613 30.908  63.184  1.00 53.90  ? 358  GLN C CD  1 
ATOM   11124 O  OE1 . GLN C  1 358 ? -27.842 30.955  63.323  1.00 53.39  ? 358  GLN C OE1 1 
ATOM   11125 N  NE2 . GLN C  1 358 ? -25.788 31.788  63.753  1.00 55.48  ? 358  GLN C NE2 1 
ATOM   11126 N  N   . PHE C  1 359 ? -27.624 25.655  61.708  1.00 28.06  ? 359  PHE C N   1 
ATOM   11127 C  CA  . PHE C  1 359 ? -28.094 24.340  62.103  1.00 27.00  ? 359  PHE C CA  1 
ATOM   11128 C  C   . PHE C  1 359 ? -27.140 23.271  61.581  1.00 26.24  ? 359  PHE C C   1 
ATOM   11129 O  O   . PHE C  1 359 ? -26.797 22.325  62.284  1.00 28.82  ? 359  PHE C O   1 
ATOM   11130 C  CB  . PHE C  1 359 ? -29.511 24.100  61.591  1.00 27.67  ? 359  PHE C CB  1 
ATOM   11131 C  CG  . PHE C  1 359 ? -29.949 22.675  61.697  1.00 27.12  ? 359  PHE C CG  1 
ATOM   11132 C  CD1 . PHE C  1 359 ? -30.217 22.110  62.930  1.00 26.13  ? 359  PHE C CD1 1 
ATOM   11133 C  CD2 . PHE C  1 359 ? -30.075 21.894  60.571  1.00 27.66  ? 359  PHE C CD2 1 
ATOM   11134 C  CE1 . PHE C  1 359 ? -30.616 20.796  63.031  1.00 25.73  ? 359  PHE C CE1 1 
ATOM   11135 C  CE2 . PHE C  1 359 ? -30.470 20.575  60.673  1.00 43.30  ? 359  PHE C CE2 1 
ATOM   11136 C  CZ  . PHE C  1 359 ? -30.744 20.030  61.901  1.00 26.29  ? 359  PHE C CZ  1 
ATOM   11137 N  N   . LEU C  1 360 ? -26.696 23.459  60.349  1.00 31.39  ? 360  LEU C N   1 
ATOM   11138 C  CA  . LEU C  1 360 ? -25.795 22.533  59.688  1.00 29.05  ? 360  LEU C CA  1 
ATOM   11139 C  C   . LEU C  1 360 ? -24.445 22.405  60.396  1.00 29.55  ? 360  LEU C C   1 
ATOM   11140 O  O   . LEU C  1 360 ? -23.916 21.293  60.523  1.00 27.14  ? 360  LEU C O   1 
ATOM   11141 C  CB  . LEU C  1 360 ? -25.590 22.967  58.238  1.00 43.26  ? 360  LEU C CB  1 
ATOM   11142 C  CG  . LEU C  1 360 ? -26.450 22.246  57.203  1.00 45.97  ? 360  LEU C CG  1 
ATOM   11143 C  CD1 . LEU C  1 360 ? -26.094 20.775  57.244  1.00 48.19  ? 360  LEU C CD1 1 
ATOM   11144 C  CD2 . LEU C  1 360 ? -27.949 22.445  57.423  1.00 43.90  ? 360  LEU C CD2 1 
ATOM   11145 N  N   . ALA C  1 361 ? -23.890 23.535  60.844  1.00 31.23  ? 361  ALA C N   1 
ATOM   11146 C  CA  . ALA C  1 361 ? -22.605 23.541  61.549  1.00 27.63  ? 361  ALA C CA  1 
ATOM   11147 C  C   . ALA C  1 361 ? -22.761 22.977  62.953  1.00 25.95  ? 361  ALA C C   1 
ATOM   11148 O  O   . ALA C  1 361 ? -21.928 22.183  63.422  1.00 24.65  ? 361  ALA C O   1 
ATOM   11149 C  CB  . ALA C  1 361 ? -22.050 24.929  61.612  1.00 25.54  ? 361  ALA C CB  1 
ATOM   11150 N  N   . GLY C  1 362 ? -23.835 23.400  63.619  1.00 26.22  ? 362  GLY C N   1 
ATOM   11151 C  CA  . GLY C  1 362 ? -24.211 22.878  64.921  1.00 26.51  ? 362  GLY C CA  1 
ATOM   11152 C  C   . GLY C  1 362 ? -24.354 21.358  64.966  1.00 28.17  ? 362  GLY C C   1 
ATOM   11153 O  O   . GLY C  1 362 ? -23.951 20.730  65.940  1.00 23.22  ? 362  GLY C O   1 
ATOM   11154 N  N   . VAL C  1 363 ? -24.934 20.760  63.923  1.00 36.42  ? 363  VAL C N   1 
ATOM   11155 C  CA  . VAL C  1 363 ? -25.052 19.299  63.845  1.00 35.05  ? 363  VAL C CA  1 
ATOM   11156 C  C   . VAL C  1 363 ? -23.681 18.649  63.899  1.00 33.32  ? 363  VAL C C   1 
ATOM   11157 O  O   . VAL C  1 363 ? -23.491 17.599  64.515  1.00 28.48  ? 363  VAL C O   1 
ATOM   11158 C  CB  . VAL C  1 363 ? -25.778 18.853  62.560  1.00 23.59  ? 363  VAL C CB  1 
ATOM   11159 C  CG1 . VAL C  1 363 ? -25.465 17.405  62.221  1.00 22.99  ? 363  VAL C CG1 1 
ATOM   11160 C  CG2 . VAL C  1 363 ? -27.271 19.065  62.714  1.00 23.80  ? 363  VAL C CG2 1 
ATOM   11161 N  N   . ARG C  1 364 ? -22.718 19.301  63.268  1.00 37.57  ? 364  ARG C N   1 
ATOM   11162 C  CA  . ARG C  1 364 ? -21.371 18.777  63.220  1.00 38.54  ? 364  ARG C CA  1 
ATOM   11163 C  C   . ARG C  1 364 ? -20.622 19.018  64.530  1.00 39.91  ? 364  ARG C C   1 
ATOM   11164 O  O   . ARG C  1 364 ? -19.690 18.288  64.851  1.00 43.72  ? 364  ARG C O   1 
ATOM   11165 C  CB  . ARG C  1 364 ? -20.641 19.377  62.030  1.00 39.12  ? 364  ARG C CB  1 
ATOM   11166 C  CG  . ARG C  1 364 ? -21.499 19.363  60.773  1.00 45.40  ? 364  ARG C CG  1 
ATOM   11167 C  CD  . ARG C  1 364 ? -20.924 18.431  59.729  1.00 51.83  ? 364  ARG C CD  1 
ATOM   11168 N  NE  . ARG C  1 364 ? -20.147 17.365  60.351  1.00 55.95  ? 364  ARG C NE  1 
ATOM   11169 C  CZ  . ARG C  1 364 ? -19.459 16.451  59.677  1.00 59.00  ? 364  ARG C CZ  1 
ATOM   11170 N  NH1 . ARG C  1 364 ? -19.451 16.464  58.346  1.00 57.90  ? 364  ARG C NH1 1 
ATOM   11171 N  NH2 . ARG C  1 364 ? -18.783 15.521  60.340  1.00 61.25  ? 364  ARG C NH2 1 
ATOM   11172 N  N   . ILE C  1 365 ? -21.018 20.033  65.295  1.00 37.74  ? 365  ILE C N   1 
ATOM   11173 C  CA  . ILE C  1 365 ? -20.431 20.203  66.629  1.00 33.66  ? 365  ILE C CA  1 
ATOM   11174 C  C   . ILE C  1 365 ? -21.015 19.238  67.660  1.00 35.42  ? 365  ILE C C   1 
ATOM   11175 O  O   . ILE C  1 365 ? -20.290 18.641  68.449  1.00 39.01  ? 365  ILE C O   1 
ATOM   11176 C  CB  . ILE C  1 365 ? -20.661 21.590  67.176  1.00 20.16  ? 365  ILE C CB  1 
ATOM   11177 C  CG1 . ILE C  1 365 ? -19.953 22.622  66.319  1.00 20.99  ? 365  ILE C CG1 1 
ATOM   11178 C  CG2 . ILE C  1 365 ? -20.171 21.658  68.599  1.00 19.35  ? 365  ILE C CG2 1 
ATOM   11179 C  CD1 . ILE C  1 365 ? -20.132 24.022  66.833  1.00 21.39  ? 365  ILE C CD1 1 
ATOM   11180 N  N   . GLY C  1 366 ? -22.336 19.112  67.662  1.00 31.13  ? 366  GLY C N   1 
ATOM   11181 C  CA  . GLY C  1 366 ? -23.027 18.217  68.565  1.00 25.88  ? 366  GLY C CA  1 
ATOM   11182 C  C   . GLY C  1 366 ? -22.683 16.767  68.296  1.00 23.38  ? 366  GLY C C   1 
ATOM   11183 O  O   . GLY C  1 366 ? -22.678 15.952  69.209  1.00 25.93  ? 366  GLY C O   1 
ATOM   11184 N  N   . VAL C  1 367 ? -22.393 16.431  67.045  1.00 18.88  ? 367  VAL C N   1 
ATOM   11185 C  CA  . VAL C  1 367 ? -21.985 15.067  66.727  1.00 18.78  ? 367  VAL C CA  1 
ATOM   11186 C  C   . VAL C  1 367 ? -20.548 14.990  66.136  1.00 22.44  ? 367  VAL C C   1 
ATOM   11187 O  O   . VAL C  1 367 ? -20.355 14.730  64.942  1.00 20.75  ? 367  VAL C O   1 
ATOM   11188 C  CB  . VAL C  1 367 ? -23.018 14.360  65.830  1.00 22.85  ? 367  VAL C CB  1 
ATOM   11189 C  CG1 . VAL C  1 367 ? -22.998 12.883  66.118  1.00 25.31  ? 367  VAL C CG1 1 
ATOM   11190 C  CG2 . VAL C  1 367 ? -24.403 14.905  66.073  1.00 19.63  ? 367  VAL C CG2 1 
ATOM   11191 N  N   . PRO C  1 368 ? -19.534 15.184  67.001  1.00 25.22  ? 368  PRO C N   1 
ATOM   11192 C  CA  . PRO C  1 368 ? -18.123 15.418  66.658  1.00 28.26  ? 368  PRO C CA  1 
ATOM   11193 C  C   . PRO C  1 368 ? -17.475 14.223  66.013  1.00 38.36  ? 368  PRO C C   1 
ATOM   11194 O  O   . PRO C  1 368 ? -16.575 14.390  65.191  1.00 43.19  ? 368  PRO C O   1 
ATOM   11195 C  CB  . PRO C  1 368 ? -17.454 15.638  68.012  1.00 24.40  ? 368  PRO C CB  1 
ATOM   11196 C  CG  . PRO C  1 368 ? -18.570 15.754  68.995  1.00 24.43  ? 368  PRO C CG  1 
ATOM   11197 C  CD  . PRO C  1 368 ? -19.712 15.006  68.447  1.00 24.57  ? 368  PRO C CD  1 
ATOM   11198 N  N   . GLN C  1 369 ? -17.910 13.030  66.392  1.00 52.29  ? 369  GLN C N   1 
ATOM   11199 C  CA  . GLN C  1 369 ? -17.348 11.829  65.809  1.00 57.39  ? 369  GLN C CA  1 
ATOM   11200 C  C   . GLN C  1 369 ? -18.088 11.467  64.513  1.00 58.16  ? 369  GLN C C   1 
ATOM   11201 O  O   . GLN C  1 369 ? -17.739 10.498  63.844  1.00 61.81  ? 369  GLN C O   1 
ATOM   11202 C  CB  . GLN C  1 369 ? -17.362 10.677  66.820  1.00 61.28  ? 369  GLN C CB  1 
ATOM   11203 C  CG  . GLN C  1 369 ? -18.639 9.822   66.822  1.00 67.99  ? 369  GLN C CG  1 
ATOM   11204 C  CD  . GLN C  1 369 ? -19.777 10.387  67.672  1.00 69.52  ? 369  GLN C CD  1 
ATOM   11205 O  OE1 . GLN C  1 369 ? -19.970 11.603  67.768  1.00 66.33  ? 369  GLN C OE1 1 
ATOM   11206 N  NE2 . GLN C  1 369 ? -20.543 9.488   68.289  1.00 71.26  ? 369  GLN C NE2 1 
ATOM   11207 N  N   . ALA C  1 370 ? -19.095 12.257  64.143  1.00 42.63  ? 370  ALA C N   1 
ATOM   11208 C  CA  . ALA C  1 370 ? -19.865 11.954  62.937  1.00 38.75  ? 370  ALA C CA  1 
ATOM   11209 C  C   . ALA C  1 370 ? -19.116 12.319  61.677  1.00 40.39  ? 370  ALA C C   1 
ATOM   11210 O  O   . ALA C  1 370 ? -18.699 13.461  61.514  1.00 42.29  ? 370  ALA C O   1 
ATOM   11211 C  CB  . ALA C  1 370 ? -21.187 12.660  62.955  1.00 29.49  ? 370  ALA C CB  1 
ATOM   11212 N  N   . SER C  1 371 ? -18.977 11.350  60.775  1.00 38.18  ? 371  SER C N   1 
ATOM   11213 C  CA  . SER C  1 371 ? -18.347 11.587  59.481  1.00 39.19  ? 371  SER C CA  1 
ATOM   11214 C  C   . SER C  1 371 ? -19.291 12.406  58.631  1.00 39.65  ? 371  SER C C   1 
ATOM   11215 O  O   . SER C  1 371 ? -20.417 12.687  59.044  1.00 39.67  ? 371  SER C O   1 
ATOM   11216 C  CB  . SER C  1 371 ? -18.064 10.260  58.776  1.00 49.67  ? 371  SER C CB  1 
ATOM   11217 O  OG  . SER C  1 371 ? -19.266 9.546   58.534  1.00 50.87  ? 371  SER C OG  1 
ATOM   11218 N  N   . ASP C  1 372 ? -18.848 12.765  57.431  1.00 44.14  ? 372  ASP C N   1 
ATOM   11219 C  CA  . ASP C  1 372 ? -19.636 13.639  56.567  1.00 45.62  ? 372  ASP C CA  1 
ATOM   11220 C  C   . ASP C  1 372 ? -20.993 13.044  56.232  1.00 38.99  ? 372  ASP C C   1 
ATOM   11221 O  O   . ASP C  1 372 ? -22.019 13.718  56.360  1.00 36.63  ? 372  ASP C O   1 
ATOM   11222 C  CB  . ASP C  1 372 ? -18.875 13.979  55.291  1.00 69.77  ? 372  ASP C CB  1 
ATOM   11223 C  CG  . ASP C  1 372 ? -17.979 15.185  55.456  1.00 74.94  ? 372  ASP C CG  1 
ATOM   11224 O  OD1 . ASP C  1 372 ? -17.438 15.370  56.569  1.00 75.95  ? 372  ASP C OD1 1 
ATOM   11225 O  OD2 . ASP C  1 372 ? -17.821 15.948  54.475  1.00 76.38  ? 372  ASP C OD2 1 
ATOM   11226 N  N   . LEU C  1 373 ? -21.000 11.780  55.817  1.00 37.05  ? 373  LEU C N   1 
ATOM   11227 C  CA  . LEU C  1 373 ? -22.257 11.119  55.486  1.00 36.46  ? 373  LEU C CA  1 
ATOM   11228 C  C   . LEU C  1 373 ? -23.141 10.933  56.726  1.00 34.04  ? 373  LEU C C   1 
ATOM   11229 O  O   . LEU C  1 373 ? -24.370 10.958  56.625  1.00 33.72  ? 373  LEU C O   1 
ATOM   11230 C  CB  . LEU C  1 373 ? -22.020 9.778   54.763  1.00 41.48  ? 373  LEU C CB  1 
ATOM   11231 C  CG  . LEU C  1 373 ? -23.263 8.932   54.400  1.00 40.99  ? 373  LEU C CG  1 
ATOM   11232 C  CD1 . LEU C  1 373 ? -24.176 9.636   53.396  1.00 41.02  ? 373  LEU C CD1 1 
ATOM   11233 C  CD2 . LEU C  1 373 ? -22.895 7.541   53.897  1.00 39.30  ? 373  LEU C CD2 1 
ATOM   11234 N  N   . ALA C  1 374 ? -22.521 10.753  57.891  1.00 31.20  ? 374  ALA C N   1 
ATOM   11235 C  CA  . ALA C  1 374 ? -23.283 10.502  59.117  1.00 29.47  ? 374  ALA C CA  1 
ATOM   11236 C  C   . ALA C  1 374 ? -24.070 11.744  59.489  1.00 28.43  ? 374  ALA C C   1 
ATOM   11237 O  O   . ALA C  1 374 ? -25.260 11.675  59.817  1.00 27.06  ? 374  ALA C O   1 
ATOM   11238 C  CB  . ALA C  1 374 ? -22.358 10.096  60.250  1.00 30.49  ? 374  ALA C CB  1 
ATOM   11239 N  N   . ALA C  1 375 ? -23.384 12.880  59.428  1.00 23.51  ? 375  ALA C N   1 
ATOM   11240 C  CA  . ALA C  1 375 ? -24.019 14.172  59.601  1.00 23.73  ? 375  ALA C CA  1 
ATOM   11241 C  C   . ALA C  1 375 ? -25.105 14.332  58.568  1.00 24.89  ? 375  ALA C C   1 
ATOM   11242 O  O   . ALA C  1 375 ? -26.198 14.764  58.889  1.00 30.23  ? 375  ALA C O   1 
ATOM   11243 C  CB  . ALA C  1 375 ? -23.011 15.272  59.443  1.00 34.31  ? 375  ALA C CB  1 
ATOM   11244 N  N   . GLU C  1 376 ? -24.792 13.990  57.323  1.00 31.21  ? 376  GLU C N   1 
ATOM   11245 C  CA  . GLU C  1 376 ? -25.767 14.062  56.240  1.00 34.64  ? 376  GLU C CA  1 
ATOM   11246 C  C   . GLU C  1 376 ? -27.061 13.364  56.646  1.00 29.79  ? 376  GLU C C   1 
ATOM   11247 O  O   . GLU C  1 376 ? -28.165 13.879  56.436  1.00 30.39  ? 376  GLU C O   1 
ATOM   11248 C  CB  . GLU C  1 376 ? -25.193 13.421  54.974  1.00 65.60  ? 376  GLU C CB  1 
ATOM   11249 C  CG  . GLU C  1 376 ? -25.088 14.352  53.784  1.00 76.52  ? 376  GLU C CG  1 
ATOM   11250 C  CD  . GLU C  1 376 ? -26.355 14.376  52.948  1.00 85.82  ? 376  GLU C CD  1 
ATOM   11251 O  OE1 . GLU C  1 376 ? -27.474 14.418  53.520  1.00 89.08  ? 376  GLU C OE1 1 
ATOM   11252 O  OE2 . GLU C  1 376 ? -26.225 14.343  51.707  1.00 87.74  ? 376  GLU C OE2 1 
ATOM   11253 N  N   . ALA C  1 377 ? -26.907 12.199  57.260  1.00 28.12  ? 377  ALA C N   1 
ATOM   11254 C  CA  . ALA C  1 377 ? -28.039 11.415  57.710  1.00 29.40  ? 377  ALA C CA  1 
ATOM   11255 C  C   . ALA C  1 377 ? -28.766 12.113  58.844  1.00 30.51  ? 377  ALA C C   1 
ATOM   11256 O  O   . ALA C  1 377 ? -29.996 12.146  58.858  1.00 31.10  ? 377  ALA C O   1 
ATOM   11257 C  CB  . ALA C  1 377 ? -27.580 10.057  58.150  1.00 35.08  ? 377  ALA C CB  1 
ATOM   11258 N  N   . VAL C  1 378 ? -28.005 12.662  59.794  1.00 24.82  ? 378  VAL C N   1 
ATOM   11259 C  CA  . VAL C  1 378 ? -28.587 13.319  60.969  1.00 24.28  ? 378  VAL C CA  1 
ATOM   11260 C  C   . VAL C  1 378 ? -29.448 14.483  60.524  1.00 25.18  ? 378  VAL C C   1 
ATOM   11261 O  O   . VAL C  1 378 ? -30.561 14.679  61.006  1.00 25.70  ? 378  VAL C O   1 
ATOM   11262 C  CB  . VAL C  1 378 ? -27.500 13.828  61.942  1.00 23.19  ? 378  VAL C CB  1 
ATOM   11263 C  CG1 . VAL C  1 378 ? -28.114 14.694  63.017  1.00 22.85  ? 378  VAL C CG1 1 
ATOM   11264 C  CG2 . VAL C  1 378 ? -26.752 12.665  62.566  1.00 22.32  ? 378  VAL C CG2 1 
ATOM   11265 N  N   . VAL C  1 379 ? -28.918 15.233  59.571  1.00 25.79  ? 379  VAL C N   1 
ATOM   11266 C  CA  . VAL C  1 379 ? -29.574 16.409  59.051  1.00 26.76  ? 379  VAL C CA  1 
ATOM   11267 C  C   . VAL C  1 379 ? -30.840 16.008  58.330  1.00 27.88  ? 379  VAL C C   1 
ATOM   11268 O  O   . VAL C  1 379 ? -31.891 16.590  58.571  1.00 29.97  ? 379  VAL C O   1 
ATOM   11269 C  CB  . VAL C  1 379 ? -28.658 17.186  58.101  1.00 27.28  ? 379  VAL C CB  1 
ATOM   11270 C  CG1 . VAL C  1 379 ? -29.446 18.253  57.374  1.00 28.55  ? 379  VAL C CG1 1 
ATOM   11271 C  CG2 . VAL C  1 379 ? -27.512 17.803  58.868  1.00 26.34  ? 379  VAL C CG2 1 
ATOM   11272 N  N   . LEU C  1 380 ? -30.743 15.013  57.452  1.00 30.08  ? 380  LEU C N   1 
ATOM   11273 C  CA  . LEU C  1 380 ? -31.931 14.532  56.751  1.00 31.31  ? 380  LEU C CA  1 
ATOM   11274 C  C   . LEU C  1 380 ? -32.994 14.155  57.761  1.00 33.77  ? 380  LEU C C   1 
ATOM   11275 O  O   . LEU C  1 380 ? -34.164 14.505  57.624  1.00 37.17  ? 380  LEU C O   1 
ATOM   11276 C  CB  . LEU C  1 380 ? -31.628 13.315  55.876  1.00 29.89  ? 380  LEU C CB  1 
ATOM   11277 C  CG  . LEU C  1 380 ? -32.891 12.490  55.586  1.00 30.79  ? 380  LEU C CG  1 
ATOM   11278 C  CD1 . LEU C  1 380 ? -33.721 13.108  54.485  1.00 34.25  ? 380  LEU C CD1 1 
ATOM   11279 C  CD2 . LEU C  1 380 ? -32.579 11.059  55.255  1.00 43.14  ? 380  LEU C CD2 1 
ATOM   11280 N  N   . HIS C  1 381 ? -32.576 13.458  58.800  1.00 28.03  ? 381  HIS C N   1 
ATOM   11281 C  CA  . HIS C  1 381 ? -33.540 12.938  59.739  1.00 29.51  ? 381  HIS C CA  1 
ATOM   11282 C  C   . HIS C  1 381 ? -34.223 14.031  60.557  1.00 27.78  ? 381  HIS C C   1 
ATOM   11283 O  O   . HIS C  1 381 ? -35.408 13.923  60.831  1.00 28.36  ? 381  HIS C O   1 
ATOM   11284 C  CB  . HIS C  1 381 ? -32.901 11.902  60.650  1.00 40.02  ? 381  HIS C CB  1 
ATOM   11285 C  CG  . HIS C  1 381 ? -33.889 11.125  61.451  1.00 43.07  ? 381  HIS C CG  1 
ATOM   11286 N  ND1 . HIS C  1 381 ? -34.494 9.982   60.975  1.00 45.21  ? 381  HIS C ND1 1 
ATOM   11287 C  CD2 . HIS C  1 381 ? -34.392 11.333  62.691  1.00 45.68  ? 381  HIS C CD2 1 
ATOM   11288 C  CE1 . HIS C  1 381 ? -35.319 9.511   61.893  1.00 48.07  ? 381  HIS C CE1 1 
ATOM   11289 N  NE2 . HIS C  1 381 ? -35.277 10.314  62.943  1.00 48.30  ? 381  HIS C NE2 1 
ATOM   11290 N  N   . TYR C  1 382 ? -33.497 15.079  60.946  1.00 34.32  ? 382  TYR C N   1 
ATOM   11291 C  CA  . TYR C  1 382 ? -34.098 16.109  61.804  1.00 35.30  ? 382  TYR C CA  1 
ATOM   11292 C  C   . TYR C  1 382 ? -34.740 17.322  61.113  1.00 37.13  ? 382  TYR C C   1 
ATOM   11293 O  O   . TYR C  1 382 ? -35.461 18.081  61.761  1.00 39.53  ? 382  TYR C O   1 
ATOM   11294 C  CB  . TYR C  1 382 ? -33.101 16.586  62.856  1.00 34.91  ? 382  TYR C CB  1 
ATOM   11295 C  CG  . TYR C  1 382 ? -32.938 15.622  64.001  1.00 37.41  ? 382  TYR C CG  1 
ATOM   11296 C  CD1 . TYR C  1 382 ? -33.880 15.559  65.010  1.00 38.37  ? 382  TYR C CD1 1 
ATOM   11297 C  CD2 . TYR C  1 382 ? -31.847 14.772  64.076  1.00 39.28  ? 382  TYR C CD2 1 
ATOM   11298 C  CE1 . TYR C  1 382 ? -33.741 14.685  66.074  1.00 37.53  ? 382  TYR C CE1 1 
ATOM   11299 C  CE2 . TYR C  1 382 ? -31.697 13.893  65.141  1.00 39.24  ? 382  TYR C CE2 1 
ATOM   11300 C  CZ  . TYR C  1 382 ? -32.651 13.857  66.137  1.00 37.84  ? 382  TYR C CZ  1 
ATOM   11301 O  OH  . TYR C  1 382 ? -32.524 12.989  67.198  1.00 37.22  ? 382  TYR C OH  1 
ATOM   11302 N  N   . THR C  1 383 ? -34.511 17.494  59.813  1.00 29.43  ? 383  THR C N   1 
ATOM   11303 C  CA  . THR C  1 383 ? -35.112 18.607  59.076  1.00 30.56  ? 383  THR C CA  1 
ATOM   11304 C  C   . THR C  1 383 ? -36.589 18.359  58.832  1.00 31.72  ? 383  THR C C   1 
ATOM   11305 O  O   . THR C  1 383 ? -37.000 17.224  58.615  1.00 31.88  ? 383  THR C O   1 
ATOM   11306 C  CB  . THR C  1 383 ? -34.474 18.776  57.693  1.00 31.31  ? 383  THR C CB  1 
ATOM   11307 O  OG1 . THR C  1 383 ? -33.054 18.819  57.820  1.00 32.15  ? 383  THR C OG1 1 
ATOM   11308 C  CG2 . THR C  1 383 ? -34.943 20.050  57.041  1.00 32.60  ? 383  THR C CG2 1 
ATOM   11309 N  N   . ASP C  1 384 ? -37.391 19.416  58.871  1.00 45.96  ? 384  ASP C N   1 
ATOM   11310 C  CA  . ASP C  1 384 ? -38.726 19.343  58.299  1.00 51.60  ? 384  ASP C CA  1 
ATOM   11311 C  C   . ASP C  1 384 ? -38.650 19.861  56.874  1.00 53.85  ? 384  ASP C C   1 
ATOM   11312 O  O   . ASP C  1 384 ? -38.413 21.047  56.657  1.00 56.34  ? 384  ASP C O   1 
ATOM   11313 C  CB  . ASP C  1 384 ? -39.718 20.184  59.083  1.00 54.54  ? 384  ASP C CB  1 
ATOM   11314 C  CG  . ASP C  1 384 ? -40.984 20.443  58.305  1.00 58.93  ? 384  ASP C CG  1 
ATOM   11315 O  OD1 . ASP C  1 384 ? -41.430 19.527  57.580  1.00 60.76  ? 384  ASP C OD1 1 
ATOM   11316 O  OD2 . ASP C  1 384 ? -41.524 21.565  58.397  1.00 60.93  ? 384  ASP C OD2 1 
ATOM   11317 N  N   . TRP C  1 385 ? -38.875 18.981  55.904  1.00 44.89  ? 385  TRP C N   1 
ATOM   11318 C  CA  . TRP C  1 385 ? -38.617 19.317  54.509  1.00 43.13  ? 385  TRP C CA  1 
ATOM   11319 C  C   . TRP C  1 385 ? -39.750 20.098  53.867  1.00 43.89  ? 385  TRP C C   1 
ATOM   11320 O  O   . TRP C  1 385 ? -39.643 20.569  52.735  1.00 42.77  ? 385  TRP C O   1 
ATOM   11321 C  CB  . TRP C  1 385 ? -38.257 18.066  53.713  1.00 37.37  ? 385  TRP C CB  1 
ATOM   11322 C  CG  . TRP C  1 385 ? -36.986 17.475  54.194  1.00 35.77  ? 385  TRP C CG  1 
ATOM   11323 C  CD1 . TRP C  1 385 ? -36.848 16.507  55.125  1.00 38.74  ? 385  TRP C CD1 1 
ATOM   11324 C  CD2 . TRP C  1 385 ? -35.663 17.841  53.799  1.00 35.28  ? 385  TRP C CD2 1 
ATOM   11325 N  NE1 . TRP C  1 385 ? -35.522 16.230  55.330  1.00 36.89  ? 385  TRP C NE1 1 
ATOM   11326 C  CE2 . TRP C  1 385 ? -34.774 17.038  54.522  1.00 33.78  ? 385  TRP C CE2 1 
ATOM   11327 C  CE3 . TRP C  1 385 ? -35.147 18.756  52.891  1.00 36.06  ? 385  TRP C CE3 1 
ATOM   11328 C  CZ2 . TRP C  1 385 ? -33.404 17.122  54.372  1.00 33.04  ? 385  TRP C CZ2 1 
ATOM   11329 C  CZ3 . TRP C  1 385 ? -33.779 18.836  52.741  1.00 35.33  ? 385  TRP C CZ3 1 
ATOM   11330 C  CH2 . TRP C  1 385 ? -32.925 18.029  53.478  1.00 33.84  ? 385  TRP C CH2 1 
ATOM   11331 N  N   . LEU C  1 386 ? -40.838 20.253  54.598  1.00 51.96  ? 386  LEU C N   1 
ATOM   11332 C  CA  . LEU C  1 386 ? -41.858 21.168  54.142  1.00 57.31  ? 386  LEU C CA  1 
ATOM   11333 C  C   . LEU C  1 386 ? -41.305 22.588  54.242  1.00 59.60  ? 386  LEU C C   1 
ATOM   11334 O  O   . LEU C  1 386 ? -41.473 23.397  53.323  1.00 62.07  ? 386  LEU C O   1 
ATOM   11335 C  CB  . LEU C  1 386 ? -43.131 21.008  54.964  1.00 45.28  ? 386  LEU C CB  1 
ATOM   11336 C  CG  . LEU C  1 386 ? -44.365 20.703  54.117  1.00 48.59  ? 386  LEU C CG  1 
ATOM   11337 C  CD1 . LEU C  1 386 ? -45.544 20.368  55.034  1.00 49.18  ? 386  LEU C CD1 1 
ATOM   11338 C  CD2 . LEU C  1 386 ? -44.683 21.863  53.148  1.00 45.13  ? 386  LEU C CD2 1 
ATOM   11339 N  N   . HIS C  1 387 ? -40.629 22.868  55.359  1.00 50.28  ? 387  HIS C N   1 
ATOM   11340 C  CA  . HIS C  1 387 ? -39.999 24.167  55.601  1.00 50.29  ? 387  HIS C CA  1 
ATOM   11341 C  C   . HIS C  1 387 ? -38.596 23.993  56.171  1.00 42.16  ? 387  HIS C C   1 
ATOM   11342 O  O   . HIS C  1 387 ? -38.383 24.177  57.365  1.00 39.48  ? 387  HIS C O   1 
ATOM   11343 C  CB  . HIS C  1 387 ? -40.820 25.009  56.583  1.00 69.27  ? 387  HIS C CB  1 
ATOM   11344 C  CG  . HIS C  1 387 ? -42.297 24.779  56.504  1.00 75.53  ? 387  HIS C CG  1 
ATOM   11345 N  ND1 . HIS C  1 387 ? -42.958 23.901  57.338  1.00 76.29  ? 387  HIS C ND1 1 
ATOM   11346 C  CD2 . HIS C  1 387 ? -43.243 25.321  55.701  1.00 79.43  ? 387  HIS C CD2 1 
ATOM   11347 C  CE1 . HIS C  1 387 ? -44.246 23.908  57.048  1.00 79.33  ? 387  HIS C CE1 1 
ATOM   11348 N  NE2 . HIS C  1 387 ? -44.445 24.759  56.058  1.00 81.52  ? 387  HIS C NE2 1 
ATOM   11349 N  N   . PRO C  1 388 ? -37.627 23.656  55.313  1.00 37.60  ? 388  PRO C N   1 
ATOM   11350 C  CA  . PRO C  1 388 ? -36.266 23.320  55.744  1.00 36.04  ? 388  PRO C CA  1 
ATOM   11351 C  C   . PRO C  1 388 ? -35.537 24.492  56.391  1.00 35.54  ? 388  PRO C C   1 
ATOM   11352 O  O   . PRO C  1 388 ? -34.531 24.307  57.083  1.00 34.16  ? 388  PRO C O   1 
ATOM   11353 C  CB  . PRO C  1 388 ? -35.577 22.961  54.428  1.00 57.62  ? 388  PRO C CB  1 
ATOM   11354 C  CG  . PRO C  1 388 ? -36.312 23.736  53.397  1.00 60.80  ? 388  PRO C CG  1 
ATOM   11355 C  CD  . PRO C  1 388 ? -37.741 23.702  53.847  1.00 60.30  ? 388  PRO C CD  1 
ATOM   11356 N  N   . GLU C  1 389 ? -36.050 25.690  56.135  1.00 43.27  ? 389  GLU C N   1 
ATOM   11357 C  CA  . GLU C  1 389 ? -35.386 26.924  56.516  1.00 45.37  ? 389  GLU C CA  1 
ATOM   11358 C  C   . GLU C  1 389 ? -35.883 27.531  57.822  1.00 43.25  ? 389  GLU C C   1 
ATOM   11359 O  O   . GLU C  1 389 ? -35.330 28.528  58.280  1.00 40.73  ? 389  GLU C O   1 
ATOM   11360 C  CB  . GLU C  1 389 ? -35.578 27.947  55.400  1.00 63.88  ? 389  GLU C CB  1 
ATOM   11361 C  CG  . GLU C  1 389 ? -34.922 27.567  54.103  1.00 71.69  ? 389  GLU C CG  1 
ATOM   11362 C  CD  . GLU C  1 389 ? -33.462 27.947  54.093  1.00 79.21  ? 389  GLU C CD  1 
ATOM   11363 O  OE1 . GLU C  1 389 ? -33.051 28.697  55.010  1.00 81.79  ? 389  GLU C OE1 1 
ATOM   11364 O  OE2 . GLU C  1 389 ? -32.731 27.501  53.179  1.00 81.52  ? 389  GLU C OE2 1 
ATOM   11365 N  N   . ASP C  1 390 ? -36.912 26.937  58.425  1.00 53.45  ? 390  ASP C N   1 
ATOM   11366 C  CA  . ASP C  1 390 ? -37.642 27.605  59.507  1.00 52.81  ? 390  ASP C CA  1 
ATOM   11367 C  C   . ASP C  1 390 ? -36.889 27.639  60.846  1.00 51.53  ? 390  ASP C C   1 
ATOM   11368 O  O   . ASP C  1 390 ? -36.729 26.606  61.511  1.00 49.35  ? 390  ASP C O   1 
ATOM   11369 C  CB  . ASP C  1 390 ? -39.032 26.989  59.675  1.00 46.59  ? 390  ASP C CB  1 
ATOM   11370 C  CG  . ASP C  1 390 ? -39.753 27.519  60.889  1.00 48.72  ? 390  ASP C CG  1 
ATOM   11371 O  OD1 . ASP C  1 390 ? -39.665 28.735  61.141  1.00 51.86  ? 390  ASP C OD1 1 
ATOM   11372 O  OD2 . ASP C  1 390 ? -40.395 26.724  61.606  1.00 48.63  ? 390  ASP C OD2 1 
ATOM   11373 N  N   . PRO C  1 391 ? -36.472 28.852  61.258  1.00 49.72  ? 391  PRO C N   1 
ATOM   11374 C  CA  . PRO C  1 391 ? -35.550 29.133  62.358  1.00 49.57  ? 391  PRO C CA  1 
ATOM   11375 C  C   . PRO C  1 391 ? -35.998 28.560  63.679  1.00 51.38  ? 391  PRO C C   1 
ATOM   11376 O  O   . PRO C  1 391 ? -35.174 27.985  64.392  1.00 51.60  ? 391  PRO C O   1 
ATOM   11377 C  CB  . PRO C  1 391 ? -35.567 30.656  62.434  1.00 41.68  ? 391  PRO C CB  1 
ATOM   11378 C  CG  . PRO C  1 391 ? -35.834 31.073  61.076  1.00 42.72  ? 391  PRO C CG  1 
ATOM   11379 C  CD  . PRO C  1 391 ? -36.856 30.097  60.578  1.00 43.56  ? 391  PRO C CD  1 
ATOM   11380 N  N   . THR C  1 392 ? -37.270 28.722  64.015  1.00 54.79  ? 392  THR C N   1 
ATOM   11381 C  CA  . THR C  1 392 ? -37.759 28.170  65.269  1.00 53.41  ? 392  THR C CA  1 
ATOM   11382 C  C   . THR C  1 392 ? -37.641 26.646  65.232  1.00 51.56  ? 392  THR C C   1 
ATOM   11383 O  O   . THR C  1 392 ? -37.251 25.993  66.219  1.00 52.25  ? 392  THR C O   1 
ATOM   11384 C  CB  . THR C  1 392 ? -39.202 28.610  65.565  1.00 45.84  ? 392  THR C CB  1 
ATOM   11385 O  OG1 . THR C  1 392 ? -39.855 27.594  66.331  1.00 43.00  ? 392  THR C OG1 1 
ATOM   11386 C  CG2 . THR C  1 392 ? -39.975 28.835  64.273  1.00 49.28  ? 392  THR C CG2 1 
ATOM   11387 N  N   . HIS C  1 393 ? -37.927 26.083  64.067  1.00 36.66  ? 393  HIS C N   1 
ATOM   11388 C  CA  . HIS C  1 393 ? -37.882 24.645  63.939  1.00 35.30  ? 393  HIS C CA  1 
ATOM   11389 C  C   . HIS C  1 393 ? -36.457 24.138  63.985  1.00 30.97  ? 393  HIS C C   1 
ATOM   11390 O  O   . HIS C  1 393 ? -36.158 23.138  64.638  1.00 29.02  ? 393  HIS C O   1 
ATOM   11391 C  CB  . HIS C  1 393 ? -38.540 24.169  62.660  1.00 46.46  ? 393  HIS C CB  1 
ATOM   11392 C  CG  . HIS C  1 393 ? -38.536 22.685  62.534  1.00 49.39  ? 393  HIS C CG  1 
ATOM   11393 N  ND1 . HIS C  1 393 ? -37.497 21.995  61.949  1.00 50.46  ? 393  HIS C ND1 1 
ATOM   11394 C  CD2 . HIS C  1 393 ? -39.410 21.752  62.975  1.00 51.43  ? 393  HIS C CD2 1 
ATOM   11395 C  CE1 . HIS C  1 393 ? -37.745 20.700  62.009  1.00 51.66  ? 393  HIS C CE1 1 
ATOM   11396 N  NE2 . HIS C  1 393 ? -38.898 20.525  62.630  1.00 52.58  ? 393  HIS C NE2 1 
ATOM   11397 N  N   . LEU C  1 394 ? -35.575 24.825  63.282  1.00 39.52  ? 394  LEU C N   1 
ATOM   11398 C  CA  . LEU C  1 394 ? -34.170 24.461  63.320  1.00 41.83  ? 394  LEU C CA  1 
ATOM   11399 C  C   . LEU C  1 394 ? -33.584 24.556  64.734  1.00 41.45  ? 394  LEU C C   1 
ATOM   11400 O  O   . LEU C  1 394 ? -32.794 23.711  65.135  1.00 43.84  ? 394  LEU C O   1 
ATOM   11401 C  CB  . LEU C  1 394 ? -33.382 25.327  62.344  1.00 36.47  ? 394  LEU C CB  1 
ATOM   11402 C  CG  . LEU C  1 394 ? -33.745 25.092  60.887  1.00 31.02  ? 394  LEU C CG  1 
ATOM   11403 C  CD1 . LEU C  1 394 ? -33.123 26.169  60.018  1.00 31.90  ? 394  LEU C CD1 1 
ATOM   11404 C  CD2 . LEU C  1 394 ? -33.272 23.704  60.482  1.00 30.32  ? 394  LEU C CD2 1 
ATOM   11405 N  N   . ARG C  1 395 ? -33.970 25.580  65.484  1.00 31.10  ? 395  ARG C N   1 
ATOM   11406 C  CA  . ARG C  1 395 ? -33.519 25.713  66.859  1.00 28.49  ? 395  ARG C CA  1 
ATOM   11407 C  C   . ARG C  1 395 ? -33.973 24.509  67.698  1.00 29.80  ? 395  ARG C C   1 
ATOM   11408 O  O   . ARG C  1 395 ? -33.136 23.798  68.309  1.00 30.26  ? 395  ARG C O   1 
ATOM   11409 C  CB  . ARG C  1 395 ? -34.038 27.021  67.447  1.00 27.95  ? 395  ARG C CB  1 
ATOM   11410 C  CG  . ARG C  1 395 ? -33.727 27.218  68.906  1.00 27.07  ? 395  ARG C CG  1 
ATOM   11411 C  CD  . ARG C  1 395 ? -34.989 27.110  69.719  1.00 27.38  ? 395  ARG C CD  1 
ATOM   11412 N  NE  . ARG C  1 395 ? -35.689 28.385  69.845  1.00 28.56  ? 395  ARG C NE  1 
ATOM   11413 C  CZ  . ARG C  1 395 ? -37.009 28.507  69.965  1.00 29.50  ? 395  ARG C CZ  1 
ATOM   11414 N  NH1 . ARG C  1 395 ? -37.782 27.430  69.954  1.00 29.40  ? 395  ARG C NH1 1 
ATOM   11415 N  NH2 . ARG C  1 395 ? -37.556 29.708  70.093  1.00 30.63  ? 395  ARG C NH2 1 
ATOM   11416 N  N   . ASP C  1 396 ? -35.286 24.262  67.707  1.00 30.68  ? 396  ASP C N   1 
ATOM   11417 C  CA  . ASP C  1 396 ? -35.838 23.094  68.409  1.00 34.33  ? 396  ASP C CA  1 
ATOM   11418 C  C   . ASP C  1 396 ? -35.190 21.754  67.971  1.00 25.75  ? 396  ASP C C   1 
ATOM   11419 O  O   . ASP C  1 396 ? -35.065 20.794  68.759  1.00 24.86  ? 396  ASP C O   1 
ATOM   11420 C  CB  . ASP C  1 396 ? -37.362 23.049  68.234  1.00 58.54  ? 396  ASP C CB  1 
ATOM   11421 C  CG  . ASP C  1 396 ? -38.080 24.109  69.063  1.00 66.46  ? 396  ASP C CG  1 
ATOM   11422 O  OD1 . ASP C  1 396 ? -37.390 25.017  69.575  1.00 68.51  ? 396  ASP C OD1 1 
ATOM   11423 O  OD2 . ASP C  1 396 ? -39.326 24.035  69.205  1.00 68.77  ? 396  ASP C OD2 1 
ATOM   11424 N  N   . ALA C  1 397 ? -34.762 21.715  66.711  1.00 26.17  ? 397  ALA C N   1 
ATOM   11425 C  CA  . ALA C  1 397 ? -34.146 20.534  66.126  1.00 25.66  ? 397  ALA C CA  1 
ATOM   11426 C  C   . ALA C  1 397 ? -32.706 20.356  66.567  1.00 24.46  ? 397  ALA C C   1 
ATOM   11427 O  O   . ALA C  1 397 ? -32.233 19.247  66.706  1.00 23.72  ? 397  ALA C O   1 
ATOM   11428 C  CB  . ALA C  1 397 ? -34.211 20.609  64.625  1.00 26.67  ? 397  ALA C CB  1 
ATOM   11429 N  N   . MET C  1 398 ? -31.997 21.454  66.758  1.00 25.59  ? 398  MET C N   1 
ATOM   11430 C  CA  . MET C  1 398 ? -30.616 21.376  67.184  1.00 24.13  ? 398  MET C CA  1 
ATOM   11431 C  C   . MET C  1 398 ? -30.633 20.872  68.606  1.00 22.95  ? 398  MET C C   1 
ATOM   11432 O  O   . MET C  1 398 ? -29.855 19.961  68.989  1.00 21.47  ? 398  MET C O   1 
ATOM   11433 C  CB  . MET C  1 398 ? -29.973 22.757  67.128  1.00 26.97  ? 398  MET C CB  1 
ATOM   11434 C  CG  . MET C  1 398 ? -28.483 22.762  67.374  1.00 24.84  ? 398  MET C CG  1 
ATOM   11435 S  SD  . MET C  1 398 ? -27.660 21.838  66.088  1.00 23.82  ? 398  MET C SD  1 
ATOM   11436 C  CE  . MET C  1 398 ? -27.126 20.428  67.046  1.00 25.86  ? 398  MET C CE  1 
ATOM   11437 N  N   . SER C  1 399 ? -31.539 21.467  69.382  1.00 31.66  ? 399  SER C N   1 
ATOM   11438 C  CA  . SER C  1 399 ? -31.780 20.981  70.732  1.00 34.96  ? 399  SER C CA  1 
ATOM   11439 C  C   . SER C  1 399 ? -31.990 19.464  70.662  1.00 35.46  ? 399  SER C C   1 
ATOM   11440 O  O   . SER C  1 399 ? -31.311 18.693  71.361  1.00 34.29  ? 399  SER C O   1 
ATOM   11441 C  CB  . SER C  1 399 ? -32.991 21.689  71.360  1.00 30.97  ? 399  SER C CB  1 
ATOM   11442 O  OG  . SER C  1 399 ? -33.383 21.098  72.596  1.00 29.34  ? 399  SER C OG  1 
ATOM   11443 N  N   . ALA C  1 400 ? -32.885 19.047  69.765  1.00 22.38  ? 400  ALA C N   1 
ATOM   11444 C  CA  . ALA C  1 400 ? -33.261 17.639  69.645  1.00 22.26  ? 400  ALA C CA  1 
ATOM   11445 C  C   . ALA C  1 400 ? -32.093 16.705  69.328  1.00 21.51  ? 400  ALA C C   1 
ATOM   11446 O  O   . ALA C  1 400 ? -31.952 15.658  69.949  1.00 20.90  ? 400  ALA C O   1 
ATOM   11447 C  CB  . ALA C  1 400 ? -34.358 17.487  68.625  1.00 25.45  ? 400  ALA C CB  1 
ATOM   11448 N  N   . VAL C  1 401 ? -31.265 17.092  68.363  1.00 28.99  ? 401  VAL C N   1 
ATOM   11449 C  CA  . VAL C  1 401 ? -30.092 16.310  67.979  1.00 26.99  ? 401  VAL C CA  1 
ATOM   11450 C  C   . VAL C  1 401 ? -29.185 16.085  69.177  1.00 23.67  ? 401  VAL C C   1 
ATOM   11451 O  O   . VAL C  1 401 ? -28.861 14.941  69.521  1.00 20.43  ? 401  VAL C O   1 
ATOM   11452 C  CB  . VAL C  1 401 ? -29.281 16.995  66.869  1.00 21.47  ? 401  VAL C CB  1 
ATOM   11453 C  CG1 . VAL C  1 401 ? -28.091 16.168  66.502  1.00 20.96  ? 401  VAL C CG1 1 
ATOM   11454 C  CG2 . VAL C  1 401 ? -30.134 17.178  65.674  1.00 27.97  ? 401  VAL C CG2 1 
ATOM   11455 N  N   . VAL C  1 402 ? -28.786 17.166  69.836  1.00 21.91  ? 402  VAL C N   1 
ATOM   11456 C  CA  . VAL C  1 402 ? -27.892 16.981  70.969  1.00 18.75  ? 402  VAL C CA  1 
ATOM   11457 C  C   . VAL C  1 402 ? -28.521 16.115  72.073  1.00 25.79  ? 402  VAL C C   1 
ATOM   11458 O  O   . VAL C  1 402 ? -27.908 15.149  72.571  1.00 17.68  ? 402  VAL C O   1 
ATOM   11459 C  CB  . VAL C  1 402 ? -27.435 18.318  71.508  1.00 25.68  ? 402  VAL C CB  1 
ATOM   11460 C  CG1 . VAL C  1 402 ? -27.108 18.202  72.972  1.00 25.08  ? 402  VAL C CG1 1 
ATOM   11461 C  CG2 . VAL C  1 402 ? -26.232 18.793  70.711  1.00 25.56  ? 402  VAL C CG2 1 
ATOM   11462 N  N   . GLY C  1 403 ? -29.766 16.437  72.404  1.00 29.80  ? 403  GLY C N   1 
ATOM   11463 C  CA  . GLY C  1 403 ? -30.508 15.720  73.428  1.00 31.03  ? 403  GLY C CA  1 
ATOM   11464 C  C   . GLY C  1 403 ? -30.619 14.225  73.213  1.00 32.54  ? 403  GLY C C   1 
ATOM   11465 O  O   . GLY C  1 403 ? -30.239 13.452  74.088  1.00 32.56  ? 403  GLY C O   1 
ATOM   11466 N  N   . ASP C  1 404 ? -31.126 13.811  72.052  1.00 32.08  ? 404  ASP C N   1 
ATOM   11467 C  CA  . ASP C  1 404 ? -31.276 12.382  71.770  1.00 31.58  ? 404  ASP C CA  1 
ATOM   11468 C  C   . ASP C  1 404 ? -29.940 11.683  71.631  1.00 29.39  ? 404  ASP C C   1 
ATOM   11469 O  O   . ASP C  1 404 ? -29.750 10.586  72.143  1.00 29.93  ? 404  ASP C O   1 
ATOM   11470 C  CB  . ASP C  1 404 ? -32.074 12.134  70.497  1.00 28.46  ? 404  ASP C CB  1 
ATOM   11471 C  CG  . ASP C  1 404 ? -33.281 13.002  70.400  1.00 32.05  ? 404  ASP C CG  1 
ATOM   11472 O  OD1 . ASP C  1 404 ? -33.882 13.321  71.455  1.00 34.87  ? 404  ASP C OD1 1 
ATOM   11473 O  OD2 . ASP C  1 404 ? -33.615 13.376  69.256  1.00 32.80  ? 404  ASP C OD2 1 
ATOM   11474 N  N   . HIS C  1 405 ? -29.019 12.304  70.914  1.00 28.94  ? 405  HIS C N   1 
ATOM   11475 C  CA  . HIS C  1 405 ? -27.743 11.653  70.692  1.00 29.17  ? 405  HIS C CA  1 
ATOM   11476 C  C   . HIS C  1 405 ? -27.011 11.305  71.988  1.00 29.54  ? 405  HIS C C   1 
ATOM   11477 O  O   . HIS C  1 405 ? -26.588 10.161  72.162  1.00 29.98  ? 405  HIS C O   1 
ATOM   11478 C  CB  . HIS C  1 405 ? -26.842 12.510  69.824  1.00 25.13  ? 405  HIS C CB  1 
ATOM   11479 C  CG  . HIS C  1 405 ? -25.444 12.001  69.749  1.00 23.58  ? 405  HIS C CG  1 
ATOM   11480 N  ND1 . HIS C  1 405 ? -25.153 10.660  69.611  1.00 23.09  ? 405  HIS C ND1 1 
ATOM   11481 C  CD2 . HIS C  1 405 ? -24.256 12.644  69.807  1.00 23.05  ? 405  HIS C CD2 1 
ATOM   11482 C  CE1 . HIS C  1 405 ? -23.843 10.500  69.581  1.00 23.87  ? 405  HIS C CE1 1 
ATOM   11483 N  NE2 . HIS C  1 405 ? -23.275 11.691  69.695  1.00 24.31  ? 405  HIS C NE2 1 
ATOM   11484 N  N   . ASN C  1 406 ? -26.845 12.288  72.881  1.00 24.40  ? 406  ASN C N   1 
ATOM   11485 C  CA  . ASN C  1 406 ? -26.134 12.034  74.142  1.00 19.66  ? 406  ASN C CA  1 
ATOM   11486 C  C   . ASN C  1 406 ? -26.955 11.395  75.255  1.00 18.45  ? 406  ASN C C   1 
ATOM   11487 O  O   . ASN C  1 406 ? -26.414 10.681  76.090  1.00 18.14  ? 406  ASN C O   1 
ATOM   11488 C  CB  . ASN C  1 406 ? -25.507 13.311  74.686  1.00 15.74  ? 406  ASN C CB  1 
ATOM   11489 C  CG  . ASN C  1 406 ? -24.618 13.984  73.686  1.00 19.13  ? 406  ASN C CG  1 
ATOM   11490 O  OD1 . ASN C  1 406 ? -23.461 13.617  73.543  1.00 20.05  ? 406  ASN C OD1 1 
ATOM   11491 N  ND2 . ASN C  1 406 ? -25.148 14.976  72.980  1.00 16.49  ? 406  ASN C ND2 1 
ATOM   11492 N  N   . VAL C  1 407 ? -28.252 11.669  75.302  1.00 27.24  ? 407  VAL C N   1 
ATOM   11493 C  CA  . VAL C  1 407 ? -29.033 11.216  76.450  1.00 31.13  ? 407  VAL C CA  1 
ATOM   11494 C  C   . VAL C  1 407 ? -30.199 10.299  76.143  1.00 30.90  ? 407  VAL C C   1 
ATOM   11495 O  O   . VAL C  1 407 ? -30.193 9.152   76.570  1.00 32.27  ? 407  VAL C O   1 
ATOM   11496 C  CB  . VAL C  1 407 ? -29.541 12.379  77.315  1.00 16.41  ? 407  VAL C CB  1 
ATOM   11497 C  CG1 . VAL C  1 407 ? -30.539 11.857  78.362  1.00 16.58  ? 407  VAL C CG1 1 
ATOM   11498 C  CG2 . VAL C  1 407 ? -28.353 13.121  77.958  1.00 15.78  ? 407  VAL C CG2 1 
ATOM   11499 N  N   . VAL C  1 408 ? -31.206 10.799  75.433  1.00 24.56  ? 408  VAL C N   1 
ATOM   11500 C  CA  . VAL C  1 408 ? -32.439 10.028  75.300  1.00 23.91  ? 408  VAL C CA  1 
ATOM   11501 C  C   . VAL C  1 408 ? -32.189 8.668   74.703  1.00 21.15  ? 408  VAL C C   1 
ATOM   11502 O  O   . VAL C  1 408 ? -32.567 7.667   75.273  1.00 22.63  ? 408  VAL C O   1 
ATOM   11503 C  CB  . VAL C  1 408 ? -33.537 10.717  74.487  1.00 19.38  ? 408  VAL C CB  1 
ATOM   11504 C  CG1 . VAL C  1 408 ? -34.838 9.976   74.695  1.00 20.13  ? 408  VAL C CG1 1 
ATOM   11505 C  CG2 . VAL C  1 408 ? -33.689 12.141  74.931  1.00 19.37  ? 408  VAL C CG2 1 
ATOM   11506 N  N   . CYS C  1 409 ? -31.534 8.619   73.564  1.00 18.62  ? 409  CYS C N   1 
ATOM   11507 C  CA  . CYS C  1 409 ? -31.312 7.327   72.939  1.00 21.60  ? 409  CYS C CA  1 
ATOM   11508 C  C   . CYS C  1 409 ? -30.406 6.357   73.722  1.00 19.18  ? 409  CYS C C   1 
ATOM   11509 O  O   . CYS C  1 409 ? -30.706 5.166   73.779  1.00 18.51  ? 409  CYS C O   1 
ATOM   11510 C  CB  . CYS C  1 409 ? -30.929 7.496   71.469  1.00 28.09  ? 409  CYS C CB  1 
ATOM   11511 S  SG  . CYS C  1 409 ? -32.263 8.356   70.573  1.00 25.78  ? 409  CYS C SG  1 
ATOM   11512 N  N   . PRO C  1 410 ? -29.317 6.855   74.340  1.00 17.38  ? 410  PRO C N   1 
ATOM   11513 C  CA  . PRO C  1 410 ? -28.573 5.958   75.225  1.00 16.87  ? 410  PRO C CA  1 
ATOM   11514 C  C   . PRO C  1 410 ? -29.416 5.446   76.388  1.00 17.17  ? 410  PRO C C   1 
ATOM   11515 O  O   . PRO C  1 410 ? -29.242 4.297   76.806  1.00 18.47  ? 410  PRO C O   1 
ATOM   11516 C  CB  . PRO C  1 410 ? -27.442 6.845   75.737  1.00 22.67  ? 410  PRO C CB  1 
ATOM   11517 C  CG  . PRO C  1 410 ? -27.185 7.755   74.635  1.00 23.05  ? 410  PRO C CG  1 
ATOM   11518 C  CD  . PRO C  1 410 ? -28.538 8.070   74.051  1.00 24.34  ? 410  PRO C CD  1 
ATOM   11519 N  N   . VAL C  1 411 ? -30.325 6.279   76.890  1.00 20.37  ? 411  VAL C N   1 
ATOM   11520 C  CA  . VAL C  1 411 ? -31.224 5.877   77.976  1.00 20.53  ? 411  VAL C CA  1 
ATOM   11521 C  C   . VAL C  1 411 ? -32.207 4.812   77.501  1.00 20.55  ? 411  VAL C C   1 
ATOM   11522 O  O   . VAL C  1 411 ? -32.445 3.830   78.191  1.00 18.37  ? 411  VAL C O   1 
ATOM   11523 C  CB  . VAL C  1 411 ? -31.983 7.072   78.568  1.00 17.45  ? 411  VAL C CB  1 
ATOM   11524 C  CG1 . VAL C  1 411 ? -33.196 6.601   79.317  1.00 18.03  ? 411  VAL C CG1 1 
ATOM   11525 C  CG2 . VAL C  1 411 ? -31.067 7.876   79.463  1.00 16.67  ? 411  VAL C CG2 1 
ATOM   11526 N  N   . ALA C  1 412 ? -32.743 5.009   76.304  1.00 23.20  ? 412  ALA C N   1 
ATOM   11527 C  CA  . ALA C  1 412 ? -33.666 4.073   75.690  1.00 21.46  ? 412  ALA C CA  1 
ATOM   11528 C  C   . ALA C  1 412 ? -32.983 2.752   75.526  1.00 27.05  ? 412  ALA C C   1 
ATOM   11529 O  O   . ALA C  1 412 ? -33.571 1.698   75.798  1.00 29.48  ? 412  ALA C O   1 
ATOM   11530 C  CB  . ALA C  1 412 ? -34.107 4.574   74.336  1.00 20.37  ? 412  ALA C CB  1 
ATOM   11531 N  N   . GLN C  1 413 ? -31.738 2.802   75.069  1.00 21.28  ? 413  GLN C N   1 
ATOM   11532 C  CA  . GLN C  1 413 ? -31.031 1.568   74.790  1.00 24.56  ? 413  GLN C CA  1 
ATOM   11533 C  C   . GLN C  1 413 ? -30.762 0.822   76.070  1.00 24.94  ? 413  GLN C C   1 
ATOM   11534 O  O   . GLN C  1 413 ? -30.952 -0.399  76.131  1.00 27.64  ? 413  GLN C O   1 
ATOM   11535 C  CB  . GLN C  1 413 ? -29.730 1.800   74.060  1.00 36.56  ? 413  GLN C CB  1 
ATOM   11536 C  CG  . GLN C  1 413 ? -29.188 0.508   73.547  1.00 42.79  ? 413  GLN C CG  1 
ATOM   11537 C  CD  . GLN C  1 413 ? -27.782 0.626   73.044  1.00 50.02  ? 413  GLN C CD  1 
ATOM   11538 O  OE1 . GLN C  1 413 ? -27.245 -0.333  72.491  1.00 56.51  ? 413  GLN C OE1 1 
ATOM   11539 N  NE2 . GLN C  1 413 ? -27.163 1.798   73.233  1.00 48.31  ? 413  GLN C NE2 1 
ATOM   11540 N  N   . LEU C  1 414 ? -30.335 1.555   77.095  1.00 27.64  ? 414  LEU C N   1 
ATOM   11541 C  CA  . LEU C  1 414 ? -30.166 0.949   78.407  1.00 25.37  ? 414  LEU C CA  1 
ATOM   11542 C  C   . LEU C  1 414 ? -31.471 0.315   78.917  1.00 25.98  ? 414  LEU C C   1 
ATOM   11543 O  O   . LEU C  1 414 ? -31.480 -0.867  79.265  1.00 26.95  ? 414  LEU C O   1 
ATOM   11544 C  CB  . LEU C  1 414 ? -29.616 1.942   79.428  1.00 20.33  ? 414  LEU C CB  1 
ATOM   11545 C  CG  . LEU C  1 414 ? -29.313 1.257   80.756  1.00 16.94  ? 414  LEU C CG  1 
ATOM   11546 C  CD1 . LEU C  1 414 ? -28.088 0.404   80.625  1.00 16.72  ? 414  LEU C CD1 1 
ATOM   11547 C  CD2 . LEU C  1 414 ? -29.149 2.269   81.843  1.00 16.39  ? 414  LEU C CD2 1 
ATOM   11548 N  N   . ALA C  1 415 ? -32.562 1.086   78.948  1.00 23.10  ? 415  ALA C N   1 
ATOM   11549 C  CA  . ALA C  1 415 ? -33.845 0.579   79.448  1.00 24.50  ? 415  ALA C CA  1 
ATOM   11550 C  C   . ALA C  1 415 ? -34.149 -0.725  78.770  1.00 26.80  ? 415  ALA C C   1 
ATOM   11551 O  O   . ALA C  1 415 ? -34.345 -1.730  79.439  1.00 30.53  ? 415  ALA C O   1 
ATOM   11552 C  CB  . ALA C  1 415 ? -34.978 1.559   79.199  1.00 20.32  ? 415  ALA C CB  1 
ATOM   11553 N  N   . GLY C  1 416 ? -34.135 -0.711  77.441  1.00 25.11  ? 416  GLY C N   1 
ATOM   11554 C  CA  . GLY C  1 416 ? -34.434 -1.899  76.662  1.00 26.18  ? 416  GLY C CA  1 
ATOM   11555 C  C   . GLY C  1 416 ? -33.558 -3.118  76.921  1.00 26.43  ? 416  GLY C C   1 
ATOM   11556 O  O   . GLY C  1 416 ? -34.087 -4.188  77.258  1.00 26.58  ? 416  GLY C O   1 
ATOM   11557 N  N   . ARG C  1 417 ? -32.238 -2.974  76.769  1.00 21.02  ? 417  ARG C N   1 
ATOM   11558 C  CA  . ARG C  1 417 ? -31.338 -4.104  76.986  1.00 22.02  ? 417  ARG C CA  1 
ATOM   11559 C  C   . ARG C  1 417 ? -31.368 -4.585  78.441  1.00 20.92  ? 417  ARG C C   1 
ATOM   11560 O  O   . ARG C  1 417 ? -31.009 -5.719  78.739  1.00 21.29  ? 417  ARG C O   1 
ATOM   11561 C  CB  . ARG C  1 417 ? -29.910 -3.777  76.555  1.00 58.91  ? 417  ARG C CB  1 
ATOM   11562 C  CG  . ARG C  1 417 ? -29.775 -3.516  75.080  1.00 73.66  ? 417  ARG C CG  1 
ATOM   11563 C  CD  . ARG C  1 417 ? -29.375 -4.762  74.284  1.00 85.70  ? 417  ARG C CD  1 
ATOM   11564 N  NE  . ARG C  1 417 ? -29.642 -4.603  72.845  1.00 94.69  ? 417  ARG C NE  1 
ATOM   11565 C  CZ  . ARG C  1 417 ? -28.979 -3.787  72.017  1.00 96.36  ? 417  ARG C CZ  1 
ATOM   11566 N  NH1 . ARG C  1 417 ? -27.985 -3.024  72.466  1.00 96.34  ? 417  ARG C NH1 1 
ATOM   11567 N  NH2 . ARG C  1 417 ? -29.317 -3.725  70.731  1.00 94.97  ? 417  ARG C NH2 1 
ATOM   11568 N  N   . LEU C  1 418 ? -31.790 -3.735  79.363  1.00 24.08  ? 418  LEU C N   1 
ATOM   11569 C  CA  . LEU C  1 418 ? -31.959 -4.202  80.736  1.00 27.00  ? 418  LEU C CA  1 
ATOM   11570 C  C   . LEU C  1 418 ? -33.258 -5.004  80.883  1.00 27.34  ? 418  LEU C C   1 
ATOM   11571 O  O   . LEU C  1 418 ? -33.265 -6.078  81.468  1.00 24.64  ? 418  LEU C O   1 
ATOM   11572 C  CB  . LEU C  1 418 ? -31.874 -3.044  81.742  1.00 29.19  ? 418  LEU C CB  1 
ATOM   11573 C  CG  . LEU C  1 418 ? -30.470 -2.449  81.939  1.00 26.82  ? 418  LEU C CG  1 
ATOM   11574 C  CD1 . LEU C  1 418 ? -30.469 -1.381  83.011  1.00 23.66  ? 418  LEU C CD1 1 
ATOM   11575 C  CD2 . LEU C  1 418 ? -29.488 -3.535  82.284  1.00 18.76  ? 418  LEU C CD2 1 
ATOM   11576 N  N   . ALA C  1 419 ? -34.351 -4.498  80.328  1.00 43.00  ? 419  ALA C N   1 
ATOM   11577 C  CA  . ALA C  1 419 ? -35.616 -5.227  80.374  1.00 48.34  ? 419  ALA C CA  1 
ATOM   11578 C  C   . ALA C  1 419 ? -35.488 -6.581  79.708  1.00 50.59  ? 419  ALA C C   1 
ATOM   11579 O  O   . ALA C  1 419 ? -36.161 -7.532  80.100  1.00 54.43  ? 419  ALA C O   1 
ATOM   11580 C  CB  . ALA C  1 419 ? -36.726 -4.430  79.715  1.00 46.94  ? 419  ALA C CB  1 
ATOM   11581 N  N   . ALA C  1 420 ? -34.620 -6.663  78.703  1.00 39.78  ? 420  ALA C N   1 
ATOM   11582 C  CA  . ALA C  1 420 ? -34.457 -7.898  77.941  1.00 39.88  ? 420  ALA C CA  1 
ATOM   11583 C  C   . ALA C  1 420 ? -33.593 -8.932  78.653  1.00 37.75  ? 420  ALA C C   1 
ATOM   11584 O  O   . ALA C  1 420 ? -33.782 -10.131 78.477  1.00 41.77  ? 420  ALA C O   1 
ATOM   11585 C  CB  . ALA C  1 420 ? -33.908 -7.610  76.574  1.00 49.50  ? 420  ALA C CB  1 
ATOM   11586 N  N   . GLN C  1 421 ? -32.651 -8.470  79.461  1.00 32.23  ? 421  GLN C N   1 
ATOM   11587 C  CA  . GLN C  1 421 ? -31.858 -9.368  80.296  1.00 35.97  ? 421  GLN C CA  1 
ATOM   11588 C  C   . GLN C  1 421 ? -32.572 -9.569  81.623  1.00 37.86  ? 421  GLN C C   1 
ATOM   11589 O  O   . GLN C  1 421 ? -31.990 -10.078 82.585  1.00 36.87  ? 421  GLN C O   1 
ATOM   11590 C  CB  . GLN C  1 421 ? -30.429 -8.870  80.503  1.00 51.16  ? 421  GLN C CB  1 
ATOM   11591 C  CG  . GLN C  1 421 ? -29.403 -9.563  79.629  1.00 55.41  ? 421  GLN C CG  1 
ATOM   11592 C  CD  . GLN C  1 421 ? -29.361 -8.998  78.228  1.00 59.92  ? 421  GLN C CD  1 
ATOM   11593 O  OE1 . GLN C  1 421 ? -30.369 -8.971  77.527  1.00 62.89  ? 421  GLN C OE1 1 
ATOM   11594 N  NE2 . GLN C  1 421 ? -28.190 -8.533  77.814  1.00 60.95  ? 421  GLN C NE2 1 
ATOM   11595 N  N   . GLY C  1 422 ? -33.812 -9.086  81.676  1.00 57.22  ? 422  GLY C N   1 
ATOM   11596 C  CA  . GLY C  1 422 ? -34.737 -9.408  82.746  1.00 60.19  ? 422  GLY C CA  1 
ATOM   11597 C  C   . GLY C  1 422 ? -34.580 -8.681  84.062  1.00 57.15  ? 422  GLY C C   1 
ATOM   11598 O  O   . GLY C  1 422 ? -34.591 -9.296  85.126  1.00 59.78  ? 422  GLY C O   1 
ATOM   11599 N  N   . ALA C  1 423 ? -34.436 -7.367  83.988  1.00 38.43  ? 423  ALA C N   1 
ATOM   11600 C  CA  . ALA C  1 423 ? -34.527 -6.533  85.174  1.00 32.19  ? 423  ALA C CA  1 
ATOM   11601 C  C   . ALA C  1 423 ? -35.867 -5.773  85.172  1.00 36.22  ? 423  ALA C C   1 
ATOM   11602 O  O   . ALA C  1 423 ? -36.427 -5.465  84.112  1.00 37.78  ? 423  ALA C O   1 
ATOM   11603 C  CB  . ALA C  1 423 ? -33.370 -5.593  85.236  1.00 23.35  ? 423  ALA C CB  1 
ATOM   11604 N  N   . ARG C  1 424 ? -36.415 -5.508  86.352  1.00 33.79  ? 424  ARG C N   1 
ATOM   11605 C  CA  . ARG C  1 424 ? -37.652 -4.764  86.403  1.00 36.29  ? 424  ARG C CA  1 
ATOM   11606 C  C   . ARG C  1 424 ? -37.236 -3.336  86.110  1.00 33.42  ? 424  ARG C C   1 
ATOM   11607 O  O   . ARG C  1 424 ? -36.424 -2.763  86.833  1.00 36.75  ? 424  ARG C O   1 
ATOM   11608 C  CB  . ARG C  1 424 ? -38.300 -4.892  87.788  1.00 58.55  ? 424  ARG C CB  1 
ATOM   11609 C  CG  . ARG C  1 424 ? -39.832 -4.736  87.804  1.00 67.02  ? 424  ARG C CG  1 
ATOM   11610 C  CD  . ARG C  1 424 ? -40.478 -5.455  88.998  1.00 75.51  ? 424  ARG C CD  1 
ATOM   11611 N  NE  . ARG C  1 424 ? -40.593 -6.912  88.812  1.00 83.01  ? 424  ARG C NE  1 
ATOM   11612 C  CZ  . ARG C  1 424 ? -39.974 -7.838  89.553  1.00 83.53  ? 424  ARG C CZ  1 
ATOM   11613 N  NH1 . ARG C  1 424 ? -39.173 -7.480  90.556  1.00 82.40  ? 424  ARG C NH1 1 
ATOM   11614 N  NH2 . ARG C  1 424 ? -40.157 -9.130  89.291  1.00 81.79  ? 424  ARG C NH2 1 
ATOM   11615 N  N   . VAL C  1 425 ? -37.759 -2.757  85.041  1.00 31.37  ? 425  VAL C N   1 
ATOM   11616 C  CA  . VAL C  1 425 ? -37.399 -1.384  84.743  1.00 28.88  ? 425  VAL C CA  1 
ATOM   11617 C  C   . VAL C  1 425 ? -38.613 -0.494  84.752  1.00 29.38  ? 425  VAL C C   1 
ATOM   11618 O  O   . VAL C  1 425 ? -39.601 -0.824  84.115  1.00 34.82  ? 425  VAL C O   1 
ATOM   11619 C  CB  . VAL C  1 425 ? -36.763 -1.258  83.371  1.00 22.02  ? 425  VAL C CB  1 
ATOM   11620 C  CG1 . VAL C  1 425 ? -36.634 0.215   82.981  1.00 21.28  ? 425  VAL C CG1 1 
ATOM   11621 C  CG2 . VAL C  1 425 ? -35.420 -1.950  83.361  1.00 23.28  ? 425  VAL C CG2 1 
ATOM   11622 N  N   . TYR C  1 426 ? -38.552 0.626   85.464  1.00 22.35  ? 426  TYR C N   1 
ATOM   11623 C  CA  . TYR C  1 426 ? -39.573 1.657   85.309  1.00 22.81  ? 426  TYR C CA  1 
ATOM   11624 C  C   . TYR C  1 426 ? -38.938 2.845   84.597  1.00 25.68  ? 426  TYR C C   1 
ATOM   11625 O  O   . TYR C  1 426 ? -37.776 3.163   84.851  1.00 27.15  ? 426  TYR C O   1 
ATOM   11626 C  CB  . TYR C  1 426 ? -40.187 2.044   86.659  1.00 27.02  ? 426  TYR C CB  1 
ATOM   11627 C  CG  . TYR C  1 426 ? -40.745 0.846   87.388  1.00 29.19  ? 426  TYR C CG  1 
ATOM   11628 C  CD1 . TYR C  1 426 ? -39.920 0.047   88.161  1.00 31.29  ? 426  TYR C CD1 1 
ATOM   11629 C  CD2 . TYR C  1 426 ? -42.087 0.488   87.278  1.00 30.90  ? 426  TYR C CD2 1 
ATOM   11630 C  CE1 . TYR C  1 426 ? -40.411 -1.071  88.823  1.00 37.03  ? 426  TYR C CE1 1 
ATOM   11631 C  CE2 . TYR C  1 426 ? -42.594 -0.643  87.937  1.00 34.06  ? 426  TYR C CE2 1 
ATOM   11632 C  CZ  . TYR C  1 426 ? -41.745 -1.418  88.712  1.00 37.67  ? 426  TYR C CZ  1 
ATOM   11633 O  OH  . TYR C  1 426 ? -42.187 -2.545  89.383  1.00 38.32  ? 426  TYR C OH  1 
ATOM   11634 N  N   . ALA C  1 427 ? -39.686 3.475   83.687  1.00 31.02  ? 427  ALA C N   1 
ATOM   11635 C  CA  . ALA C  1 427 ? -39.157 4.580   82.877  1.00 28.32  ? 427  ALA C CA  1 
ATOM   11636 C  C   . ALA C  1 427 ? -40.043 5.820   82.894  1.00 28.22  ? 427  ALA C C   1 
ATOM   11637 O  O   . ALA C  1 427 ? -41.269 5.728   82.857  1.00 29.06  ? 427  ALA C O   1 
ATOM   11638 C  CB  . ALA C  1 427 ? -38.923 4.128   81.464  1.00 22.64  ? 427  ALA C CB  1 
ATOM   11639 N  N   . TYR C  1 428 ? -39.410 6.986   82.941  1.00 22.63  ? 428  TYR C N   1 
ATOM   11640 C  CA  . TYR C  1 428 ? -40.158 8.233   83.101  1.00 24.78  ? 428  TYR C CA  1 
ATOM   11641 C  C   . TYR C  1 428 ? -39.676 9.307   82.136  1.00 25.94  ? 428  TYR C C   1 
ATOM   11642 O  O   . TYR C  1 428 ? -38.533 9.283   81.652  1.00 24.12  ? 428  TYR C O   1 
ATOM   11643 C  CB  . TYR C  1 428 ? -40.066 8.759   84.560  1.00 25.92  ? 428  TYR C CB  1 
ATOM   11644 C  CG  . TYR C  1 428 ? -38.722 9.372   84.909  1.00 23.87  ? 428  TYR C CG  1 
ATOM   11645 C  CD1 . TYR C  1 428 ? -38.417 10.656  84.508  1.00 24.27  ? 428  TYR C CD1 1 
ATOM   11646 C  CD2 . TYR C  1 428 ? -37.761 8.665   85.618  1.00 19.97  ? 428  TYR C CD2 1 
ATOM   11647 C  CE1 . TYR C  1 428 ? -37.202 11.220  84.770  1.00 24.58  ? 428  TYR C CE1 1 
ATOM   11648 C  CE2 . TYR C  1 428 ? -36.535 9.227   85.901  1.00 19.04  ? 428  TYR C CE2 1 
ATOM   11649 C  CZ  . TYR C  1 428 ? -36.257 10.519  85.467  1.00 23.09  ? 428  TYR C CZ  1 
ATOM   11650 O  OH  . TYR C  1 428 ? -35.048 11.165  85.705  1.00 20.53  ? 428  TYR C OH  1 
ATOM   11651 N  N   . ILE C  1 429 ? -40.539 10.285  81.904  1.00 39.63  ? 429  ILE C N   1 
ATOM   11652 C  CA  . ILE C  1 429 ? -40.150 11.473  81.163  1.00 43.10  ? 429  ILE C CA  1 
ATOM   11653 C  C   . ILE C  1 429 ? -40.646 12.696  81.935  1.00 43.54  ? 429  ILE C C   1 
ATOM   11654 O  O   . ILE C  1 429 ? -41.830 12.840  82.212  1.00 44.94  ? 429  ILE C O   1 
ATOM   11655 C  CB  . ILE C  1 429 ? -40.656 11.432  79.698  1.00 32.35  ? 429  ILE C CB  1 
ATOM   11656 C  CG1 . ILE C  1 429 ? -40.187 12.648  78.919  1.00 30.81  ? 429  ILE C CG1 1 
ATOM   11657 C  CG2 . ILE C  1 429 ? -42.162 11.353  79.643  1.00 35.22  ? 429  ILE C CG2 1 
ATOM   11658 C  CD1 . ILE C  1 429 ? -41.031 12.893  77.692  1.00 32.53  ? 429  ILE C CD1 1 
ATOM   11659 N  N   . PHE C  1 430 ? -39.716 13.563  82.308  1.00 37.65  ? 430  PHE C N   1 
ATOM   11660 C  CA  . PHE C  1 430 ? -40.006 14.663  83.205  1.00 34.74  ? 430  PHE C CA  1 
ATOM   11661 C  C   . PHE C  1 430 ? -40.329 15.877  82.365  1.00 35.40  ? 430  PHE C C   1 
ATOM   11662 O  O   . PHE C  1 430 ? -39.463 16.409  81.679  1.00 38.12  ? 430  PHE C O   1 
ATOM   11663 C  CB  . PHE C  1 430 ? -38.786 14.926  84.084  1.00 24.40  ? 430  PHE C CB  1 
ATOM   11664 C  CG  . PHE C  1 430 ? -39.011 15.950  85.155  1.00 25.33  ? 430  PHE C CG  1 
ATOM   11665 C  CD1 . PHE C  1 430 ? -38.766 17.296  84.911  1.00 21.44  ? 430  PHE C CD1 1 
ATOM   11666 C  CD2 . PHE C  1 430 ? -39.445 15.566  86.412  1.00 21.53  ? 430  PHE C CD2 1 
ATOM   11667 C  CE1 . PHE C  1 430 ? -38.963 18.239  85.903  1.00 21.74  ? 430  PHE C CE1 1 
ATOM   11668 C  CE2 . PHE C  1 430 ? -39.650 16.502  87.404  1.00 21.82  ? 430  PHE C CE2 1 
ATOM   11669 C  CZ  . PHE C  1 430 ? -39.409 17.841  87.153  1.00 21.93  ? 430  PHE C CZ  1 
ATOM   11670 N  N   . GLU C  1 431 ? -41.598 16.266  82.385  1.00 25.56  ? 431  GLU C N   1 
ATOM   11671 C  CA  . GLU C  1 431 ? -42.084 17.369  81.570  1.00 28.69  ? 431  GLU C CA  1 
ATOM   11672 C  C   . GLU C  1 431 ? -42.310 18.709  82.260  1.00 30.52  ? 431  GLU C C   1 
ATOM   11673 O  O   . GLU C  1 431 ? -42.753 19.650  81.609  1.00 36.18  ? 431  GLU C O   1 
ATOM   11674 C  CB  . GLU C  1 431 ? -43.337 16.951  80.797  1.00 44.61  ? 431  GLU C CB  1 
ATOM   11675 C  CG  . GLU C  1 431 ? -43.027 16.473  79.388  1.00 50.44  ? 431  GLU C CG  1 
ATOM   11676 C  CD  . GLU C  1 431 ? -44.069 15.518  78.833  1.00 53.83  ? 431  GLU C CD  1 
ATOM   11677 O  OE1 . GLU C  1 431 ? -44.816 14.923  79.645  1.00 54.78  ? 431  GLU C OE1 1 
ATOM   11678 O  OE2 . GLU C  1 431 ? -44.131 15.366  77.587  1.00 54.10  ? 431  GLU C OE2 1 
ATOM   11679 N  N   . HIS C  1 432 ? -42.064 18.815  83.563  1.00 30.14  ? 432  HIS C N   1 
ATOM   11680 C  CA  . HIS C  1 432 ? -42.416 20.066  84.246  1.00 28.24  ? 432  HIS C CA  1 
ATOM   11681 C  C   . HIS C  1 432 ? -41.319 21.118  84.258  1.00 25.44  ? 432  HIS C C   1 
ATOM   11682 O  O   . HIS C  1 432 ? -40.242 20.891  84.807  1.00 23.67  ? 432  HIS C O   1 
ATOM   11683 C  CB  . HIS C  1 432 ? -42.893 19.838  85.682  1.00 33.56  ? 432  HIS C CB  1 
ATOM   11684 C  CG  . HIS C  1 432 ? -43.321 21.103  86.365  1.00 39.07  ? 432  HIS C CG  1 
ATOM   11685 N  ND1 . HIS C  1 432 ? -44.574 21.652  86.194  1.00 42.72  ? 432  HIS C ND1 1 
ATOM   11686 C  CD2 . HIS C  1 432 ? -42.647 21.946  87.183  1.00 38.88  ? 432  HIS C CD2 1 
ATOM   11687 C  CE1 . HIS C  1 432 ? -44.660 22.771  86.894  1.00 42.17  ? 432  HIS C CE1 1 
ATOM   11688 N  NE2 . HIS C  1 432 ? -43.504 22.974  87.501  1.00 39.67  ? 432  HIS C NE2 1 
ATOM   11689 N  N   . ARG C  1 433 ? -41.597 22.281  83.676  1.00 30.83  ? 433  ARG C N   1 
ATOM   11690 C  CA  . ARG C  1 433 ? -40.662 23.395  83.780  1.00 31.74  ? 433  ARG C CA  1 
ATOM   11691 C  C   . ARG C  1 433 ? -40.902 24.158  85.076  1.00 31.31  ? 433  ARG C C   1 
ATOM   11692 O  O   . ARG C  1 433 ? -42.026 24.572  85.362  1.00 34.18  ? 433  ARG C O   1 
ATOM   11693 C  CB  . ARG C  1 433 ? -40.783 24.334  82.587  1.00 34.33  ? 433  ARG C CB  1 
ATOM   11694 C  CG  . ARG C  1 433 ? -39.819 25.510  82.646  1.00 36.53  ? 433  ARG C CG  1 
ATOM   11695 C  CD  . ARG C  1 433 ? -40.059 26.481  81.500  1.00 39.68  ? 433  ARG C CD  1 
ATOM   11696 N  NE  . ARG C  1 433 ? -39.376 27.759  81.691  1.00 41.88  ? 433  ARG C NE  1 
ATOM   11697 C  CZ  . ARG C  1 433 ? -38.318 28.159  80.988  1.00 42.14  ? 433  ARG C CZ  1 
ATOM   11698 N  NH1 . ARG C  1 433 ? -37.804 27.386  80.034  1.00 38.71  ? 433  ARG C NH1 1 
ATOM   11699 N  NH2 . ARG C  1 433 ? -37.776 29.342  81.241  1.00 44.37  ? 433  ARG C NH2 1 
ATOM   11700 N  N   . ALA C  1 434 ? -39.846 24.331  85.863  1.00 28.32  ? 434  ALA C N   1 
ATOM   11701 C  CA  . ALA C  1 434 ? -39.967 24.994  87.154  1.00 29.67  ? 434  ALA C CA  1 
ATOM   11702 C  C   . ALA C  1 434 ? -40.398 26.437  86.961  1.00 32.62  ? 434  ALA C C   1 
ATOM   11703 O  O   . ALA C  1 434 ? -39.990 27.086  85.995  1.00 36.21  ? 434  ALA C O   1 
ATOM   11704 C  CB  . ALA C  1 434 ? -38.649 24.934  87.906  1.00 28.49  ? 434  ALA C CB  1 
ATOM   11705 N  N   . SER C  1 435 ? -41.227 26.937  87.871  1.00 27.92  ? 435  SER C N   1 
ATOM   11706 C  CA  . SER C  1 435 ? -41.662 28.327  87.805  1.00 32.45  ? 435  SER C CA  1 
ATOM   11707 C  C   . SER C  1 435 ? -40.513 29.289  88.159  1.00 37.53  ? 435  SER C C   1 
ATOM   11708 O  O   . SER C  1 435 ? -40.484 30.444  87.727  1.00 41.05  ? 435  SER C O   1 
ATOM   11709 C  CB  . SER C  1 435 ? -42.882 28.555  88.707  1.00 39.88  ? 435  SER C CB  1 
ATOM   11710 O  OG  . SER C  1 435 ? -42.563 28.419  90.084  1.00 39.41  ? 435  SER C OG  1 
ATOM   11711 N  N   . THR C  1 436 ? -39.557 28.792  88.929  1.00 45.55  ? 436  THR C N   1 
ATOM   11712 C  CA  . THR C  1 436 ? -38.428 29.588  89.381  1.00 50.93  ? 436  THR C CA  1 
ATOM   11713 C  C   . THR C  1 436 ? -37.257 29.518  88.404  1.00 53.34  ? 436  THR C C   1 
ATOM   11714 O  O   . THR C  1 436 ? -36.142 29.936  88.729  1.00 56.22  ? 436  THR C O   1 
ATOM   11715 C  CB  . THR C  1 436 ? -37.955 29.156  90.775  1.00 60.07  ? 436  THR C CB  1 
ATOM   11716 O  OG1 . THR C  1 436 ? -37.959 27.724  90.857  1.00 61.30  ? 436  THR C OG1 1 
ATOM   11717 C  CG2 . THR C  1 436 ? -38.868 29.727  91.842  1.00 61.84  ? 436  THR C CG2 1 
ATOM   11718 N  N   . LEU C  1 437 ? -37.486 28.931  87.234  1.00 52.07  ? 437  LEU C N   1 
ATOM   11719 C  CA  . LEU C  1 437 ? -36.409 28.766  86.263  1.00 48.07  ? 437  LEU C CA  1 
ATOM   11720 C  C   . LEU C  1 437 ? -35.850 30.089  85.758  1.00 49.54  ? 437  LEU C C   1 
ATOM   11721 O  O   . LEU C  1 437 ? -36.588 30.991  85.353  1.00 52.11  ? 437  LEU C O   1 
ATOM   11722 C  CB  . LEU C  1 437 ? -36.842 27.897  85.089  1.00 37.73  ? 437  LEU C CB  1 
ATOM   11723 C  CG  . LEU C  1 437 ? -35.747 26.926  84.655  1.00 34.79  ? 437  LEU C CG  1 
ATOM   11724 C  CD1 . LEU C  1 437 ? -36.157 25.497  84.971  1.00 35.61  ? 437  LEU C CD1 1 
ATOM   11725 C  CD2 . LEU C  1 437 ? -35.449 27.080  83.190  1.00 33.87  ? 437  LEU C CD2 1 
ATOM   11726 N  N   . THR C  1 438 ? -34.530 30.184  85.814  1.00 48.71  ? 438  THR C N   1 
ATOM   11727 C  CA  . THR C  1 438 ? -33.788 31.352  85.371  1.00 48.79  ? 438  THR C CA  1 
ATOM   11728 C  C   . THR C  1 438 ? -33.560 31.375  83.854  1.00 49.29  ? 438  THR C C   1 
ATOM   11729 O  O   . THR C  1 438 ? -33.440 32.449  83.259  1.00 51.26  ? 438  THR C O   1 
ATOM   11730 C  CB  . THR C  1 438 ? -32.423 31.409  86.076  1.00 49.34  ? 438  THR C CB  1 
ATOM   11731 O  OG1 . THR C  1 438 ? -32.340 30.367  87.061  1.00 47.89  ? 438  THR C OG1 1 
ATOM   11732 C  CG2 . THR C  1 438 ? -32.229 32.755  86.743  1.00 52.31  ? 438  THR C CG2 1 
ATOM   11733 N  N   . TRP C  1 439 ? -33.493 30.189  83.242  1.00 44.22  ? 439  TRP C N   1 
ATOM   11734 C  CA  . TRP C  1 439 ? -33.204 30.044  81.811  1.00 40.93  ? 439  TRP C CA  1 
ATOM   11735 C  C   . TRP C  1 439 ? -34.361 30.504  80.916  1.00 43.91  ? 439  TRP C C   1 
ATOM   11736 O  O   . TRP C  1 439 ? -35.501 30.563  81.364  1.00 46.57  ? 439  TRP C O   1 
ATOM   11737 C  CB  . TRP C  1 439 ? -32.862 28.591  81.499  1.00 33.26  ? 439  TRP C CB  1 
ATOM   11738 C  CG  . TRP C  1 439 ? -31.579 28.108  82.097  1.00 31.44  ? 439  TRP C CG  1 
ATOM   11739 C  CD1 . TRP C  1 439 ? -31.437 27.366  83.226  1.00 29.50  ? 439  TRP C CD1 1 
ATOM   11740 C  CD2 . TRP C  1 439 ? -30.254 28.316  81.583  1.00 32.18  ? 439  TRP C CD2 1 
ATOM   11741 N  NE1 . TRP C  1 439 ? -30.107 27.097  83.452  1.00 28.15  ? 439  TRP C NE1 1 
ATOM   11742 C  CE2 . TRP C  1 439 ? -29.360 27.669  82.458  1.00 29.81  ? 439  TRP C CE2 1 
ATOM   11743 C  CE3 . TRP C  1 439 ? -29.736 28.993  80.469  1.00 34.83  ? 439  TRP C CE3 1 
ATOM   11744 C  CZ2 . TRP C  1 439 ? -27.979 27.676  82.260  1.00 31.41  ? 439  TRP C CZ2 1 
ATOM   11745 C  CZ3 . TRP C  1 439 ? -28.360 28.997  80.269  1.00 33.90  ? 439  TRP C CZ3 1 
ATOM   11746 C  CH2 . TRP C  1 439 ? -27.500 28.342  81.161  1.00 32.39  ? 439  TRP C CH2 1 
ATOM   11747 N  N   . PRO C  1 440 ? -34.079 30.820  79.638  1.00 41.79  ? 440  PRO C N   1 
ATOM   11748 C  CA  . PRO C  1 440 ? -35.158 31.340  78.782  1.00 40.93  ? 440  PRO C CA  1 
ATOM   11749 C  C   . PRO C  1 440 ? -36.248 30.314  78.494  1.00 39.31  ? 440  PRO C C   1 
ATOM   11750 O  O   . PRO C  1 440 ? -36.154 29.153  78.893  1.00 37.39  ? 440  PRO C O   1 
ATOM   11751 C  CB  . PRO C  1 440 ? -34.436 31.691  77.481  1.00 47.20  ? 440  PRO C CB  1 
ATOM   11752 C  CG  . PRO C  1 440 ? -33.197 30.825  77.488  1.00 47.26  ? 440  PRO C CG  1 
ATOM   11753 C  CD  . PRO C  1 440 ? -32.789 30.741  78.923  1.00 45.95  ? 440  PRO C CD  1 
ATOM   11754 N  N   . LEU C  1 441 ? -37.279 30.736  77.779  1.00 40.70  ? 441  LEU C N   1 
ATOM   11755 C  CA  . LEU C  1 441 ? -38.430 29.867  77.603  1.00 39.98  ? 441  LEU C CA  1 
ATOM   11756 C  C   . LEU C  1 441 ? -38.171 28.798  76.548  1.00 38.46  ? 441  LEU C C   1 
ATOM   11757 O  O   . LEU C  1 441 ? -38.764 27.716  76.594  1.00 35.89  ? 441  LEU C O   1 
ATOM   11758 C  CB  . LEU C  1 441 ? -39.681 30.682  77.270  1.00 44.24  ? 441  LEU C CB  1 
ATOM   11759 C  CG  . LEU C  1 441 ? -40.971 29.861  77.184  1.00 47.79  ? 441  LEU C CG  1 
ATOM   11760 C  CD1 . LEU C  1 441 ? -41.226 29.137  78.497  1.00 49.60  ? 441  LEU C CD1 1 
ATOM   11761 C  CD2 . LEU C  1 441 ? -42.173 30.722  76.790  1.00 50.25  ? 441  LEU C CD2 1 
ATOM   11762 N  N   . TRP C  1 442 ? -37.280 29.096  75.604  1.00 49.73  ? 442  TRP C N   1 
ATOM   11763 C  CA  . TRP C  1 442 ? -37.063 28.187  74.479  1.00 50.31  ? 442  TRP C CA  1 
ATOM   11764 C  C   . TRP C  1 442 ? -36.360 26.905  74.892  1.00 48.49  ? 442  TRP C C   1 
ATOM   11765 O  O   . TRP C  1 442 ? -36.420 25.900  74.181  1.00 51.30  ? 442  TRP C O   1 
ATOM   11766 C  CB  . TRP C  1 442 ? -36.318 28.867  73.325  1.00 40.41  ? 442  TRP C CB  1 
ATOM   11767 C  CG  . TRP C  1 442 ? -34.894 29.208  73.599  1.00 43.21  ? 442  TRP C CG  1 
ATOM   11768 C  CD1 . TRP C  1 442 ? -34.404 30.419  73.999  1.00 48.51  ? 442  TRP C CD1 1 
ATOM   11769 C  CD2 . TRP C  1 442 ? -33.761 28.343  73.474  1.00 40.75  ? 442  TRP C CD2 1 
ATOM   11770 N  NE1 . TRP C  1 442 ? -33.035 30.359  74.140  1.00 46.77  ? 442  TRP C NE1 1 
ATOM   11771 C  CE2 . TRP C  1 442 ? -32.618 29.094  73.827  1.00 43.00  ? 442  TRP C CE2 1 
ATOM   11772 C  CE3 . TRP C  1 442 ? -33.603 27.010  73.109  1.00 39.03  ? 442  TRP C CE3 1 
ATOM   11773 C  CZ2 . TRP C  1 442 ? -31.340 28.555  73.825  1.00 42.15  ? 442  TRP C CZ2 1 
ATOM   11774 C  CZ3 . TRP C  1 442 ? -32.335 26.475  73.110  1.00 39.97  ? 442  TRP C CZ3 1 
ATOM   11775 C  CH2 . TRP C  1 442 ? -31.216 27.246  73.463  1.00 41.25  ? 442  TRP C CH2 1 
ATOM   11776 N  N   . MET C  1 443 ? -35.707 26.943  76.049  1.00 29.09  ? 443  MET C N   1 
ATOM   11777 C  CA  . MET C  1 443 ? -34.980 25.787  76.554  1.00 23.75  ? 443  MET C CA  1 
ATOM   11778 C  C   . MET C  1 443 ? -35.887 24.789  77.272  1.00 23.60  ? 443  MET C C   1 
ATOM   11779 O  O   . MET C  1 443 ? -35.439 23.707  77.643  1.00 22.67  ? 443  MET C O   1 
ATOM   11780 C  CB  . MET C  1 443 ? -33.821 26.225  77.453  1.00 30.02  ? 443  MET C CB  1 
ATOM   11781 C  CG  . MET C  1 443 ? -32.659 26.867  76.692  1.00 32.39  ? 443  MET C CG  1 
ATOM   11782 S  SD  . MET C  1 443 ? -31.370 27.588  77.735  1.00 30.71  ? 443  MET C SD  1 
ATOM   11783 C  CE  . MET C  1 443 ? -30.920 26.164  78.730  1.00 22.74  ? 443  MET C CE  1 
ATOM   11784 N  N   . GLY C  1 444 ? -37.159 25.145  77.462  1.00 36.67  ? 444  GLY C N   1 
ATOM   11785 C  CA  . GLY C  1 444 ? -38.161 24.186  77.916  1.00 35.62  ? 444  GLY C CA  1 
ATOM   11786 C  C   . GLY C  1 444 ? -37.932 23.656  79.317  1.00 32.86  ? 444  GLY C C   1 
ATOM   11787 O  O   . GLY C  1 444 ? -37.886 24.416  80.289  1.00 32.19  ? 444  GLY C O   1 
ATOM   11788 N  N   . VAL C  1 445 ? -37.783 22.339  79.413  1.00 23.41  ? 445  VAL C N   1 
ATOM   11789 C  CA  . VAL C  1 445 ? -37.484 21.681  80.678  1.00 24.03  ? 445  VAL C CA  1 
ATOM   11790 C  C   . VAL C  1 445 ? -36.086 21.130  80.510  1.00 24.85  ? 445  VAL C C   1 
ATOM   11791 O  O   . VAL C  1 445 ? -35.907 19.964  80.177  1.00 25.50  ? 445  VAL C O   1 
ATOM   11792 C  CB  . VAL C  1 445 ? -38.432 20.504  80.970  1.00 22.68  ? 445  VAL C CB  1 
ATOM   11793 C  CG1 . VAL C  1 445 ? -38.288 20.030  82.404  1.00 22.15  ? 445  VAL C CG1 1 
ATOM   11794 C  CG2 . VAL C  1 445 ? -39.844 20.910  80.728  1.00 27.78  ? 445  VAL C CG2 1 
ATOM   11795 N  N   . PRO C  1 446 ? -35.086 21.987  80.731  1.00 20.92  ? 446  PRO C N   1 
ATOM   11796 C  CA  . PRO C  1 446 ? -33.695 21.682  80.438  1.00 20.00  ? 446  PRO C CA  1 
ATOM   11797 C  C   . PRO C  1 446 ? -33.185 20.563  81.320  1.00 19.11  ? 446  PRO C C   1 
ATOM   11798 O  O   . PRO C  1 446 ? -33.808 20.225  82.334  1.00 19.18  ? 446  PRO C O   1 
ATOM   11799 C  CB  . PRO C  1 446 ? -32.967 22.976  80.805  1.00 20.04  ? 446  PRO C CB  1 
ATOM   11800 C  CG  . PRO C  1 446 ? -34.033 23.996  80.996  1.00 21.09  ? 446  PRO C CG  1 
ATOM   11801 C  CD  . PRO C  1 446 ? -35.218 23.258  81.451  1.00 27.33  ? 446  PRO C CD  1 
ATOM   11802 N  N   . HIS C  1 447 ? -32.049 20.006  80.903  1.00 18.66  ? 447  HIS C N   1 
ATOM   11803 C  CA  . HIS C  1 447 ? -31.296 18.990  81.622  1.00 18.17  ? 447  HIS C CA  1 
ATOM   11804 C  C   . HIS C  1 447 ? -31.030 19.431  83.065  1.00 17.29  ? 447  HIS C C   1 
ATOM   11805 O  O   . HIS C  1 447 ? -30.697 20.584  83.320  1.00 17.48  ? 447  HIS C O   1 
ATOM   11806 C  CB  . HIS C  1 447 ? -29.982 18.819  80.864  1.00 23.54  ? 447  HIS C CB  1 
ATOM   11807 C  CG  . HIS C  1 447 ? -29.089 17.744  81.393  1.00 27.01  ? 447  HIS C CG  1 
ATOM   11808 N  ND1 . HIS C  1 447 ? -29.442 16.412  81.389  1.00 30.69  ? 447  HIS C ND1 1 
ATOM   11809 C  CD2 . HIS C  1 447 ? -27.833 17.801  81.894  1.00 27.11  ? 447  HIS C CD2 1 
ATOM   11810 C  CE1 . HIS C  1 447 ? -28.449 15.696  81.887  1.00 31.12  ? 447  HIS C CE1 1 
ATOM   11811 N  NE2 . HIS C  1 447 ? -27.461 16.516  82.202  1.00 29.22  ? 447  HIS C NE2 1 
ATOM   11812 N  N   . GLY C  1 448 ? -31.195 18.526  84.018  1.00 24.06  ? 448  GLY C N   1 
ATOM   11813 C  CA  . GLY C  1 448 ? -30.847 18.843  85.392  1.00 24.06  ? 448  GLY C CA  1 
ATOM   11814 C  C   . GLY C  1 448 ? -31.945 19.454  86.243  1.00 25.45  ? 448  GLY C C   1 
ATOM   11815 O  O   . GLY C  1 448 ? -31.756 19.632  87.450  1.00 25.46  ? 448  GLY C O   1 
ATOM   11816 N  N   . TYR C  1 449 ? -33.085 19.778  85.629  1.00 24.10  ? 449  TYR C N   1 
ATOM   11817 C  CA  . TYR C  1 449 ? -34.159 20.486  86.334  1.00 20.40  ? 449  TYR C CA  1 
ATOM   11818 C  C   . TYR C  1 449 ? -35.258 19.612  86.882  1.00 21.23  ? 449  TYR C C   1 
ATOM   11819 O  O   . TYR C  1 449 ? -36.258 20.115  87.379  1.00 23.90  ? 449  TYR C O   1 
ATOM   11820 C  CB  . TYR C  1 449 ? -34.656 21.707  85.548  1.00 22.98  ? 449  TYR C CB  1 
ATOM   11821 C  CG  . TYR C  1 449 ? -33.532 22.700  85.516  1.00 28.19  ? 449  TYR C CG  1 
ATOM   11822 C  CD1 . TYR C  1 449 ? -32.530 22.591  84.565  1.00 30.05  ? 449  TYR C CD1 1 
ATOM   11823 C  CD2 . TYR C  1 449 ? -33.394 23.668  86.509  1.00 29.99  ? 449  TYR C CD2 1 
ATOM   11824 C  CE1 . TYR C  1 449 ? -31.454 23.441  84.559  1.00 30.96  ? 449  TYR C CE1 1 
ATOM   11825 C  CE2 . TYR C  1 449 ? -32.316 24.541  86.504  1.00 30.41  ? 449  TYR C CE2 1 
ATOM   11826 C  CZ  . TYR C  1 449 ? -31.347 24.416  85.520  1.00 31.78  ? 449  TYR C CZ  1 
ATOM   11827 O  OH  . TYR C  1 449 ? -30.250 25.250  85.477  1.00 33.86  ? 449  TYR C OH  1 
ATOM   11828 N  N   . GLU C  1 450 ? -35.086 18.301  86.780  1.00 18.97  ? 450  GLU C N   1 
ATOM   11829 C  CA  . GLU C  1 450 ? -35.925 17.424  87.574  1.00 23.30  ? 450  GLU C CA  1 
ATOM   11830 C  C   . GLU C  1 450 ? -35.396 17.360  89.021  1.00 22.45  ? 450  GLU C C   1 
ATOM   11831 O  O   . GLU C  1 450 ? -36.167 17.182  89.974  1.00 22.18  ? 450  GLU C O   1 
ATOM   11832 C  CB  . GLU C  1 450 ? -36.050 16.034  86.947  1.00 31.07  ? 450  GLU C CB  1 
ATOM   11833 C  CG  . GLU C  1 450 ? -35.007 15.040  87.379  1.00 38.13  ? 450  GLU C CG  1 
ATOM   11834 C  CD  . GLU C  1 450 ? -33.723 15.126  86.555  1.00 45.67  ? 450  GLU C CD  1 
ATOM   11835 O  OE1 . GLU C  1 450 ? -32.964 16.114  86.712  1.00 43.94  ? 450  GLU C OE1 1 
ATOM   11836 O  OE2 . GLU C  1 450 ? -33.473 14.191  85.748  1.00 50.39  ? 450  GLU C OE2 1 
ATOM   11837 N  N   . ILE C  1 451 ? -34.083 17.556  89.175  1.00 25.43  ? 451  ILE C N   1 
ATOM   11838 C  CA  . ILE C  1 451 ? -33.380 17.302  90.440  1.00 22.06  ? 451  ILE C CA  1 
ATOM   11839 C  C   . ILE C  1 451 ? -33.996 17.992  91.655  1.00 23.22  ? 451  ILE C C   1 
ATOM   11840 O  O   . ILE C  1 451 ? -34.189 17.359  92.700  1.00 22.89  ? 451  ILE C O   1 
ATOM   11841 C  CB  . ILE C  1 451 ? -31.877 17.657  90.346  1.00 20.47  ? 451  ILE C CB  1 
ATOM   11842 C  CG1 . ILE C  1 451 ? -31.138 16.682  89.426  1.00 16.35  ? 451  ILE C CG1 1 
ATOM   11843 C  CG2 . ILE C  1 451 ? -31.237 17.635  91.712  1.00 16.78  ? 451  ILE C CG2 1 
ATOM   11844 C  CD1 . ILE C  1 451 ? -29.652 16.954  89.346  1.00 15.71  ? 451  ILE C CD1 1 
ATOM   11845 N  N   . GLU C  1 452 ? -34.317 19.278  91.514  1.00 26.59  ? 452  GLU C N   1 
ATOM   11846 C  CA  . GLU C  1 452 ? -34.845 20.043  92.638  1.00 27.24  ? 452  GLU C CA  1 
ATOM   11847 C  C   . GLU C  1 452 ? -36.175 19.489  93.098  1.00 27.94  ? 452  GLU C C   1 
ATOM   11848 O  O   . GLU C  1 452 ? -36.500 19.579  94.276  1.00 28.19  ? 452  GLU C O   1 
ATOM   11849 C  CB  . GLU C  1 452 ? -34.930 21.547  92.335  1.00 20.11  ? 452  GLU C CB  1 
ATOM   11850 C  CG  . GLU C  1 452 ? -35.663 21.922  91.060  1.00 32.13  ? 452  GLU C CG  1 
ATOM   11851 C  CD  . GLU C  1 452 ? -35.215 23.275  90.480  1.00 31.73  ? 452  GLU C CD  1 
ATOM   11852 O  OE1 . GLU C  1 452 ? -34.047 23.389  90.023  1.00 30.44  ? 452  GLU C OE1 1 
ATOM   11853 O  OE2 . GLU C  1 452 ? -36.041 24.219  90.464  1.00 32.11  ? 452  GLU C OE2 1 
ATOM   11854 N  N   . PHE C  1 453 ? -36.934 18.889  92.185  1.00 30.19  ? 453  PHE C N   1 
ATOM   11855 C  CA  . PHE C  1 453 ? -38.239 18.333  92.555  1.00 33.60  ? 453  PHE C CA  1 
ATOM   11856 C  C   . PHE C  1 453 ? -38.136 16.969  93.247  1.00 33.96  ? 453  PHE C C   1 
ATOM   11857 O  O   . PHE C  1 453 ? -38.877 16.678  94.181  1.00 34.00  ? 453  PHE C O   1 
ATOM   11858 C  CB  . PHE C  1 453 ? -39.181 18.273  91.349  1.00 32.72  ? 453  PHE C CB  1 
ATOM   11859 C  CG  . PHE C  1 453 ? -39.595 19.621  90.852  1.00 35.25  ? 453  PHE C CG  1 
ATOM   11860 C  CD1 . PHE C  1 453 ? -38.711 20.410  90.132  1.00 35.05  ? 453  PHE C CD1 1 
ATOM   11861 C  CD2 . PHE C  1 453 ? -40.861 20.113  91.118  1.00 36.25  ? 453  PHE C CD2 1 
ATOM   11862 C  CE1 . PHE C  1 453 ? -39.087 21.658  89.687  1.00 35.17  ? 453  PHE C CE1 1 
ATOM   11863 C  CE2 . PHE C  1 453 ? -41.244 21.366  90.670  1.00 35.48  ? 453  PHE C CE2 1 
ATOM   11864 C  CZ  . PHE C  1 453 ? -40.359 22.136  89.957  1.00 35.20  ? 453  PHE C CZ  1 
ATOM   11865 N  N   . ILE C  1 454 ? -37.216 16.135  92.784  1.00 20.20  ? 454  ILE C N   1 
ATOM   11866 C  CA  . ILE C  1 454 ? -36.993 14.845  93.404  1.00 19.93  ? 454  ILE C CA  1 
ATOM   11867 C  C   . ILE C  1 454 ? -36.511 15.064  94.832  1.00 19.87  ? 454  ILE C C   1 
ATOM   11868 O  O   . ILE C  1 454 ? -36.900 14.350  95.745  1.00 20.23  ? 454  ILE C O   1 
ATOM   11869 C  CB  . ILE C  1 454 ? -35.938 14.065  92.620  1.00 32.62  ? 454  ILE C CB  1 
ATOM   11870 C  CG1 . ILE C  1 454 ? -36.340 13.968  91.147  1.00 19.11  ? 454  ILE C CG1 1 
ATOM   11871 C  CG2 . ILE C  1 454 ? -35.735 12.683  93.201  1.00 18.85  ? 454  ILE C CG2 1 
ATOM   11872 C  CD1 . ILE C  1 454 ? -37.514 13.084  90.918  1.00 19.84  ? 454  ILE C CD1 1 
ATOM   11873 N  N   . PHE C  1 455 ? -35.675 16.075  95.030  1.00 32.47  ? 455  PHE C N   1 
ATOM   11874 C  CA  . PHE C  1 455 ? -35.113 16.332  96.352  1.00 32.78  ? 455  PHE C CA  1 
ATOM   11875 C  C   . PHE C  1 455 ? -36.055 17.105  97.268  1.00 34.44  ? 455  PHE C C   1 
ATOM   11876 O  O   . PHE C  1 455 ? -35.751 17.326  98.438  1.00 38.35  ? 455  PHE C O   1 
ATOM   11877 C  CB  . PHE C  1 455 ? -33.774 17.054  96.238  1.00 27.64  ? 455  PHE C CB  1 
ATOM   11878 C  CG  . PHE C  1 455 ? -32.587 16.132  96.192  1.00 25.26  ? 455  PHE C CG  1 
ATOM   11879 C  CD1 . PHE C  1 455 ? -31.953 15.739  97.357  1.00 24.09  ? 455  PHE C CD1 1 
ATOM   11880 C  CD2 . PHE C  1 455 ? -32.101 15.662  94.988  1.00 24.78  ? 455  PHE C CD2 1 
ATOM   11881 C  CE1 . PHE C  1 455 ? -30.850 14.898  97.317  1.00 23.16  ? 455  PHE C CE1 1 
ATOM   11882 C  CE2 . PHE C  1 455 ? -30.991 14.815  94.950  1.00 24.51  ? 455  PHE C CE2 1 
ATOM   11883 C  CZ  . PHE C  1 455 ? -30.373 14.436  96.111  1.00 22.37  ? 455  PHE C CZ  1 
ATOM   11884 N  N   . GLY C  1 456 ? -37.188 17.533  96.726  1.00 25.72  ? 456  GLY C N   1 
ATOM   11885 C  CA  . GLY C  1 456 ? -38.248 18.127  97.524  1.00 25.35  ? 456  GLY C CA  1 
ATOM   11886 C  C   . GLY C  1 456 ? -38.059 19.570  97.940  1.00 26.56  ? 456  GLY C C   1 
ATOM   11887 O  O   . GLY C  1 456 ? -38.531 19.971  98.998  1.00 29.66  ? 456  GLY C O   1 
ATOM   11888 N  N   . LEU C  1 457 ? -37.366 20.349  97.117  1.00 22.36  ? 457  LEU C N   1 
ATOM   11889 C  CA  . LEU C  1 457 ? -37.152 21.768  97.407  1.00 22.57  ? 457  LEU C CA  1 
ATOM   11890 C  C   . LEU C  1 457 ? -38.392 22.634  97.423  1.00 26.86  ? 457  LEU C C   1 
ATOM   11891 O  O   . LEU C  1 457 ? -38.444 23.555  98.220  1.00 24.42  ? 457  LEU C O   1 
ATOM   11892 C  CB  . LEU C  1 457 ? -36.092 22.399  96.511  1.00 21.88  ? 457  LEU C CB  1 
ATOM   11893 C  CG  . LEU C  1 457 ? -34.694 22.441  97.110  1.00 21.15  ? 457  LEU C CG  1 
ATOM   11894 C  CD1 . LEU C  1 457 ? -34.116 21.046  97.255  1.00 20.33  ? 457  LEU C CD1 1 
ATOM   11895 C  CD2 . LEU C  1 457 ? -33.846 23.255  96.213  1.00 20.78  ? 457  LEU C CD2 1 
ATOM   11896 N  N   . PRO C  1 458 ? -39.374 22.375  96.529  1.00 40.22  ? 458  PRO C N   1 
ATOM   11897 C  CA  . PRO C  1 458 ? -40.648 23.108  96.597  1.00 39.76  ? 458  PRO C CA  1 
ATOM   11898 C  C   . PRO C  1 458 ? -41.325 23.103  97.969  1.00 38.58  ? 458  PRO C C   1 
ATOM   11899 O  O   . PRO C  1 458 ? -42.124 24.003  98.243  1.00 41.14  ? 458  PRO C O   1 
ATOM   11900 C  CB  . PRO C  1 458 ? -41.518 22.368  95.583  1.00 34.70  ? 458  PRO C CB  1 
ATOM   11901 C  CG  . PRO C  1 458 ? -40.561 21.966  94.542  1.00 35.31  ? 458  PRO C CG  1 
ATOM   11902 C  CD  . PRO C  1 458 ? -39.276 21.619  95.265  1.00 35.19  ? 458  PRO C CD  1 
ATOM   11903 N  N   . LEU C  1 459 ? -41.011 22.117  98.807  1.00 26.01  ? 459  LEU C N   1 
ATOM   11904 C  CA  . LEU C  1 459 ? -41.552 22.044  100.161 1.00 27.19  ? 459  LEU C CA  1 
ATOM   11905 C  C   . LEU C  1 459 ? -41.079 23.202  101.045 1.00 31.93  ? 459  LEU C C   1 
ATOM   11906 O  O   . LEU C  1 459 ? -41.735 23.566  102.014 1.00 33.91  ? 459  LEU C O   1 
ATOM   11907 C  CB  . LEU C  1 459 ? -41.191 20.714  100.809 1.00 26.29  ? 459  LEU C CB  1 
ATOM   11908 C  CG  . LEU C  1 459 ? -42.154 19.540  100.639 1.00 26.69  ? 459  LEU C CG  1 
ATOM   11909 C  CD1 . LEU C  1 459 ? -42.638 19.443  99.226  1.00 26.65  ? 459  LEU C CD1 1 
ATOM   11910 C  CD2 . LEU C  1 459 ? -41.447 18.246  101.012 1.00 41.09  ? 459  LEU C CD2 1 
ATOM   11911 N  N   . ASP C  1 460 ? -39.930 23.774  100.722 1.00 47.23  ? 460  ASP C N   1 
ATOM   11912 C  CA  . ASP C  1 460 ? -39.498 24.994  101.375 1.00 48.09  ? 460  ASP C CA  1 
ATOM   11913 C  C   . ASP C  1 460 ? -40.370 26.152  100.895 1.00 54.01  ? 460  ASP C C   1 
ATOM   11914 O  O   . ASP C  1 460 ? -40.411 26.445  99.701  1.00 59.82  ? 460  ASP C O   1 
ATOM   11915 C  CB  . ASP C  1 460 ? -38.053 25.262  100.999 1.00 34.63  ? 460  ASP C CB  1 
ATOM   11916 C  CG  . ASP C  1 460 ? -37.455 26.411  101.763 1.00 35.81  ? 460  ASP C CG  1 
ATOM   11917 O  OD1 . ASP C  1 460 ? -38.176 27.388  102.073 1.00 37.51  ? 460  ASP C OD1 1 
ATOM   11918 O  OD2 . ASP C  1 460 ? -36.241 26.331  102.057 1.00 35.49  ? 460  ASP C OD2 1 
ATOM   11919 N  N   . PRO C  1 461 ? -41.058 26.830  101.825 1.00 37.96  ? 461  PRO C N   1 
ATOM   11920 C  CA  . PRO C  1 461 ? -41.912 27.975  101.482 1.00 38.15  ? 461  PRO C CA  1 
ATOM   11921 C  C   . PRO C  1 461 ? -41.101 29.166  100.984 1.00 39.71  ? 461  PRO C C   1 
ATOM   11922 O  O   . PRO C  1 461 ? -41.515 29.858  100.053 1.00 42.42  ? 461  PRO C O   1 
ATOM   11923 C  CB  . PRO C  1 461 ? -42.578 28.331  102.812 1.00 56.34  ? 461  PRO C CB  1 
ATOM   11924 C  CG  . PRO C  1 461 ? -42.412 27.127  103.670 1.00 58.83  ? 461  PRO C CG  1 
ATOM   11925 C  CD  . PRO C  1 461 ? -41.099 26.533  103.261 1.00 55.71  ? 461  PRO C CD  1 
ATOM   11926 N  N   . SER C  1 462 ? -39.930 29.381  101.572 1.00 48.43  ? 462  SER C N   1 
ATOM   11927 C  CA  . SER C  1 462 ? -39.113 30.543  101.239 1.00 49.45  ? 462  SER C CA  1 
ATOM   11928 C  C   . SER C  1 462 ? -38.520 30.423  99.850  1.00 46.18  ? 462  SER C C   1 
ATOM   11929 O  O   . SER C  1 462 ? -37.794 31.299  99.400  1.00 47.70  ? 462  SER C O   1 
ATOM   11930 C  CB  . SER C  1 462 ? -37.995 30.735  102.254 1.00 57.44  ? 462  SER C CB  1 
ATOM   11931 O  OG  . SER C  1 462 ? -37.117 29.629  102.230 1.00 59.67  ? 462  SER C OG  1 
ATOM   11932 N  N   . LEU C  1 463 ? -38.781 29.313  99.184  1.00 39.29  ? 463  LEU C N   1 
ATOM   11933 C  CA  . LEU C  1 463 ? -38.242 29.146  97.856  1.00 37.98  ? 463  LEU C CA  1 
ATOM   11934 C  C   . LEU C  1 463 ? -39.150 29.634  96.711  1.00 43.66  ? 463  LEU C C   1 
ATOM   11935 O  O   . LEU C  1 463 ? -38.784 29.505  95.539  1.00 47.03  ? 463  LEU C O   1 
ATOM   11936 C  CB  . LEU C  1 463 ? -37.795 27.708  97.660  1.00 37.65  ? 463  LEU C CB  1 
ATOM   11937 C  CG  . LEU C  1 463 ? -36.398 27.487  98.236  1.00 38.08  ? 463  LEU C CG  1 
ATOM   11938 C  CD1 . LEU C  1 463 ? -35.840 26.118  97.832  1.00 39.30  ? 463  LEU C CD1 1 
ATOM   11939 C  CD2 . LEU C  1 463 ? -35.466 28.613  97.791  1.00 36.33  ? 463  LEU C CD2 1 
ATOM   11940 N  N   . ASN C  1 464 ? -40.312 30.199  97.047  1.00 36.78  ? 464  ASN C N   1 
ATOM   11941 C  CA  . ASN C  1 464 ? -41.197 30.856  96.063  1.00 38.76  ? 464  ASN C CA  1 
ATOM   11942 C  C   . ASN C  1 464 ? -41.700 29.975  94.907  1.00 33.41  ? 464  ASN C C   1 
ATOM   11943 O  O   . ASN C  1 464 ? -41.966 30.480  93.819  1.00 30.20  ? 464  ASN C O   1 
ATOM   11944 C  CB  . ASN C  1 464 ? -40.552 32.141  95.503  1.00 68.52  ? 464  ASN C CB  1 
ATOM   11945 C  CG  . ASN C  1 464 ? -40.160 33.139  96.597  1.00 79.38  ? 464  ASN C CG  1 
ATOM   11946 O  OD1 . ASN C  1 464 ? -40.768 33.169  97.669  1.00 84.57  ? 464  ASN C OD1 1 
ATOM   11947 N  ND2 . ASN C  1 464 ? -39.138 33.962  96.326  1.00 80.61  ? 464  ASN C ND2 1 
ATOM   11948 N  N   . TYR C  1 465 ? -41.813 28.667  95.147  1.00 34.11  ? 465  TYR C N   1 
ATOM   11949 C  CA  . TYR C  1 465 ? -42.417 27.721  94.203  1.00 34.00  ? 465  TYR C CA  1 
ATOM   11950 C  C   . TYR C  1 465 ? -43.947 27.764  94.315  1.00 39.08  ? 465  TYR C C   1 
ATOM   11951 O  O   . TYR C  1 465 ? -44.488 28.022  95.394  1.00 38.65  ? 465  TYR C O   1 
ATOM   11952 C  CB  . TYR C  1 465 ? -41.962 26.286  94.498  1.00 37.04  ? 465  TYR C CB  1 
ATOM   11953 C  CG  . TYR C  1 465 ? -40.562 25.915  94.054  1.00 36.02  ? 465  TYR C CG  1 
ATOM   11954 C  CD1 . TYR C  1 465 ? -40.304 25.521  92.753  1.00 35.95  ? 465  TYR C CD1 1 
ATOM   11955 C  CD2 . TYR C  1 465 ? -39.505 25.913  94.950  1.00 36.34  ? 465  TYR C CD2 1 
ATOM   11956 C  CE1 . TYR C  1 465 ? -39.027 25.162  92.349  1.00 34.51  ? 465  TYR C CE1 1 
ATOM   11957 C  CE2 . TYR C  1 465 ? -38.231 25.560  94.557  1.00 35.78  ? 465  TYR C CE2 1 
ATOM   11958 C  CZ  . TYR C  1 465 ? -37.998 25.190  93.257  1.00 36.08  ? 465  TYR C CZ  1 
ATOM   11959 O  OH  . TYR C  1 465 ? -36.726 24.845  92.865  1.00 37.26  ? 465  TYR C OH  1 
ATOM   11960 N  N   . THR C  1 466 ? -44.642 27.494  93.210  1.00 45.82  ? 466  THR C N   1 
ATOM   11961 C  CA  . THR C  1 466 ? -46.102 27.393  93.215  1.00 49.88  ? 466  THR C CA  1 
ATOM   11962 C  C   . THR C  1 466 ? -46.537 26.203  94.057  1.00 49.97  ? 466  THR C C   1 
ATOM   11963 O  O   . THR C  1 466 ? -45.828 25.210  94.163  1.00 46.43  ? 466  THR C O   1 
ATOM   11964 C  CB  . THR C  1 466 ? -46.675 27.207  91.794  1.00 65.77  ? 466  THR C CB  1 
ATOM   11965 O  OG1 . THR C  1 466 ? -46.659 25.821  91.439  1.00 66.06  ? 466  THR C OG1 1 
ATOM   11966 C  CG2 . THR C  1 466 ? -45.864 27.979  90.780  1.00 68.51  ? 466  THR C CG2 1 
ATOM   11967 N  N   . THR C  1 467 ? -47.718 26.294  94.642  1.00 64.87  ? 467  THR C N   1 
ATOM   11968 C  CA  . THR C  1 467 ? -48.181 25.273  95.568  1.00 68.70  ? 467  THR C CA  1 
ATOM   11969 C  C   . THR C  1 467 ? -48.455 23.909  94.910  1.00 72.91  ? 467  THR C C   1 
ATOM   11970 O  O   . THR C  1 467 ? -48.312 22.862  95.552  1.00 75.46  ? 467  THR C O   1 
ATOM   11971 C  CB  . THR C  1 467 ? -49.412 25.770  96.304  1.00 59.67  ? 467  THR C CB  1 
ATOM   11972 O  OG1 . THR C  1 467 ? -50.362 26.238  95.341  1.00 63.49  ? 467  THR C OG1 1 
ATOM   11973 C  CG2 . THR C  1 467 ? -49.034 26.933  97.194  1.00 56.57  ? 467  THR C CG2 1 
ATOM   11974 N  N   . GLU C  1 468 ? -48.838 23.907  93.636  1.00 71.02  ? 468  GLU C N   1 
ATOM   11975 C  CA  . GLU C  1 468 ? -49.001 22.640  92.918  1.00 70.88  ? 468  GLU C CA  1 
ATOM   11976 C  C   . GLU C  1 468 ? -47.629 22.057  92.580  1.00 63.81  ? 468  GLU C C   1 
ATOM   11977 O  O   . GLU C  1 468 ? -47.482 20.846  92.426  1.00 63.33  ? 468  GLU C O   1 
ATOM   11978 C  CB  . GLU C  1 468 ? -49.857 22.789  91.653  1.00 84.39  ? 468  GLU C CB  1 
ATOM   11979 C  CG  . GLU C  1 468 ? -50.617 24.099  91.539  1.00 91.25  ? 468  GLU C CG  1 
ATOM   11980 C  CD  . GLU C  1 468 ? -49.792 25.202  90.891  1.00 95.62  ? 468  GLU C CD  1 
ATOM   11981 O  OE1 . GLU C  1 468 ? -49.243 24.970  89.788  1.00 96.39  ? 468  GLU C OE1 1 
ATOM   11982 O  OE2 . GLU C  1 468 ? -49.691 26.297  91.490  1.00 96.78  ? 468  GLU C OE2 1 
ATOM   11983 N  N   . GLU C  1 469 ? -46.630 22.929  92.464  1.00 55.71  ? 469  GLU C N   1 
ATOM   11984 C  CA  . GLU C  1 469 ? -45.256 22.480  92.336  1.00 51.16  ? 469  GLU C CA  1 
ATOM   11985 C  C   . GLU C  1 469 ? -44.838 21.821  93.645  1.00 53.19  ? 469  GLU C C   1 
ATOM   11986 O  O   . GLU C  1 469 ? -44.022 20.892  93.661  1.00 54.24  ? 469  GLU C O   1 
ATOM   11987 C  CB  . GLU C  1 469 ? -44.324 23.647  92.009  1.00 44.53  ? 469  GLU C CB  1 
ATOM   11988 C  CG  . GLU C  1 469 ? -44.325 24.054  90.550  1.00 44.81  ? 469  GLU C CG  1 
ATOM   11989 C  CD  . GLU C  1 469 ? -43.345 25.179  90.253  1.00 44.10  ? 469  GLU C CD  1 
ATOM   11990 O  OE1 . GLU C  1 469 ? -43.190 26.068  91.120  1.00 42.62  ? 469  GLU C OE1 1 
ATOM   11991 O  OE2 . GLU C  1 469 ? -42.730 25.172  89.157  1.00 44.60  ? 469  GLU C OE2 1 
ATOM   11992 N  N   . ARG C  1 470 ? -45.399 22.313  94.746  1.00 44.66  ? 470  ARG C N   1 
ATOM   11993 C  CA  . ARG C  1 470 ? -45.118 21.744  96.057  1.00 40.06  ? 470  ARG C CA  1 
ATOM   11994 C  C   . ARG C  1 470 ? -45.719 20.346  96.148  1.00 37.77  ? 470  ARG C C   1 
ATOM   11995 O  O   . ARG C  1 470 ? -45.008 19.372  96.409  1.00 37.30  ? 470  ARG C O   1 
ATOM   11996 C  CB  . ARG C  1 470 ? -45.624 22.662  97.171  1.00 49.18  ? 470  ARG C CB  1 
ATOM   11997 C  CG  . ARG C  1 470 ? -45.038 22.387  98.538  1.00 54.63  ? 470  ARG C CG  1 
ATOM   11998 C  CD  . ARG C  1 470 ? -46.062 21.736  99.462  1.00 62.52  ? 470  ARG C CD  1 
ATOM   11999 N  NE  . ARG C  1 470 ? -47.171 22.637  99.773  1.00 68.35  ? 470  ARG C NE  1 
ATOM   12000 C  CZ  . ARG C  1 470 ? -48.393 22.237  100.118 1.00 69.60  ? 470  ARG C CZ  1 
ATOM   12001 N  NH1 . ARG C  1 470 ? -48.676 20.937  100.198 1.00 68.07  ? 470  ARG C NH1 1 
ATOM   12002 N  NH2 . ARG C  1 470 ? -49.332 23.143  100.375 1.00 70.96  ? 470  ARG C NH2 1 
ATOM   12003 N  N   . ILE C  1 471 ? -47.011 20.213  95.885  1.00 59.94  ? 471  ILE C N   1 
ATOM   12004 C  CA  . ILE C  1 471 ? -47.593 18.874  95.963  1.00 62.98  ? 471  ILE C CA  1 
ATOM   12005 C  C   . ILE C  1 471 ? -46.966 17.933  94.911  1.00 61.49  ? 471  ILE C C   1 
ATOM   12006 O  O   . ILE C  1 471 ? -46.882 16.713  95.118  1.00 64.70  ? 471  ILE C O   1 
ATOM   12007 C  CB  . ILE C  1 471 ? -49.156 18.888  95.940  1.00 41.31  ? 471  ILE C CB  1 
ATOM   12008 C  CG1 . ILE C  1 471 ? -49.703 18.626  94.535  1.00 41.77  ? 471  ILE C CG1 1 
ATOM   12009 C  CG2 . ILE C  1 471 ? -49.689 20.182  96.537  1.00 33.34  ? 471  ILE C CG2 1 
ATOM   12010 C  CD1 . ILE C  1 471 ? -50.044 17.152  94.262  1.00 43.19  ? 471  ILE C CD1 1 
ATOM   12011 N  N   . PHE C  1 472 ? -46.498 18.510  93.805  1.00 42.05  ? 472  PHE C N   1 
ATOM   12012 C  CA  . PHE C  1 472 ? -45.793 17.739  92.779  1.00 36.87  ? 472  PHE C CA  1 
ATOM   12013 C  C   . PHE C  1 472 ? -44.502 17.142  93.354  1.00 34.87  ? 472  PHE C C   1 
ATOM   12014 O  O   . PHE C  1 472 ? -44.242 15.933  93.224  1.00 32.41  ? 472  PHE C O   1 
ATOM   12015 C  CB  . PHE C  1 472 ? -45.490 18.617  91.552  1.00 28.43  ? 472  PHE C CB  1 
ATOM   12016 C  CG  . PHE C  1 472 ? -44.806 17.885  90.411  1.00 27.52  ? 472  PHE C CG  1 
ATOM   12017 C  CD1 . PHE C  1 472 ? -45.167 16.588  90.075  1.00 30.31  ? 472  PHE C CD1 1 
ATOM   12018 C  CD2 . PHE C  1 472 ? -43.826 18.512  89.660  1.00 25.94  ? 472  PHE C CD2 1 
ATOM   12019 C  CE1 . PHE C  1 472 ? -44.554 15.926  89.038  1.00 26.06  ? 472  PHE C CE1 1 
ATOM   12020 C  CE2 . PHE C  1 472 ? -43.213 17.855  88.620  1.00 26.57  ? 472  PHE C CE2 1 
ATOM   12021 C  CZ  . PHE C  1 472 ? -43.580 16.558  88.307  1.00 29.27  ? 472  PHE C CZ  1 
ATOM   12022 N  N   . ALA C  1 473 ? -43.709 18.006  93.988  1.00 33.08  ? 473  ALA C N   1 
ATOM   12023 C  CA  . ALA C  1 473 ? -42.495 17.599  94.680  1.00 28.95  ? 473  ALA C CA  1 
ATOM   12024 C  C   . ALA C  1 473 ? -42.803 16.430  95.609  1.00 30.83  ? 473  ALA C C   1 
ATOM   12025 O  O   . ALA C  1 473 ? -42.136 15.385  95.574  1.00 27.84  ? 473  ALA C O   1 
ATOM   12026 C  CB  . ALA C  1 473 ? -41.919 18.774  95.464  1.00 24.92  ? 473  ALA C CB  1 
ATOM   12027 N  N   . GLN C  1 474 ? -43.840 16.599  96.417  1.00 44.72  ? 474  GLN C N   1 
ATOM   12028 C  CA  . GLN C  1 474 ? -44.266 15.525  97.302  1.00 49.93  ? 474  GLN C CA  1 
ATOM   12029 C  C   . GLN C  1 474 ? -44.503 14.202  96.564  1.00 50.22  ? 474  GLN C C   1 
ATOM   12030 O  O   . GLN C  1 474 ? -43.964 13.156  96.966  1.00 52.51  ? 474  GLN C O   1 
ATOM   12031 C  CB  . GLN C  1 474 ? -45.532 15.931  98.042  1.00 52.24  ? 474  GLN C CB  1 
ATOM   12032 C  CG  . GLN C  1 474 ? -45.432 17.266  98.724  1.00 53.78  ? 474  GLN C CG  1 
ATOM   12033 C  CD  . GLN C  1 474 ? -46.432 17.398  99.830  1.00 56.80  ? 474  GLN C CD  1 
ATOM   12034 O  OE1 . GLN C  1 474 ? -47.361 18.211  99.758  1.00 59.51  ? 474  GLN C OE1 1 
ATOM   12035 N  NE2 . GLN C  1 474 ? -46.258 16.590  100.872 1.00 56.39  ? 474  GLN C NE2 1 
ATOM   12036 N  N   . ARG C  1 475 ? -45.299 14.249  95.491  1.00 36.64  ? 475  ARG C N   1 
ATOM   12037 C  CA  . ARG C  1 475 ? -45.637 13.026  94.764  1.00 33.90  ? 475  ARG C CA  1 
ATOM   12038 C  C   . ARG C  1 475 ? -44.393 12.352  94.183  1.00 35.00  ? 475  ARG C C   1 
ATOM   12039 O  O   . ARG C  1 475 ? -44.276 11.113  94.195  1.00 32.34  ? 475  ARG C O   1 
ATOM   12040 C  CB  . ARG C  1 475 ? -46.667 13.284  93.663  1.00 34.96  ? 475  ARG C CB  1 
ATOM   12041 C  CG  . ARG C  1 475 ? -47.216 11.980  93.067  1.00 38.68  ? 475  ARG C CG  1 
ATOM   12042 C  CD  . ARG C  1 475 ? -48.437 12.179  92.173  1.00 42.69  ? 475  ARG C CD  1 
ATOM   12043 N  NE  . ARG C  1 475 ? -48.088 12.354  90.761  1.00 45.70  ? 475  ARG C NE  1 
ATOM   12044 C  CZ  . ARG C  1 475 ? -48.079 13.529  90.128  1.00 46.44  ? 475  ARG C CZ  1 
ATOM   12045 N  NH1 . ARG C  1 475 ? -48.406 14.647  90.786  1.00 49.91  ? 475  ARG C NH1 1 
ATOM   12046 N  NH2 . ARG C  1 475 ? -47.750 13.586  88.838  1.00 40.71  ? 475  ARG C NH2 1 
ATOM   12047 N  N   . LEU C  1 476 ? -43.467 13.173  93.689  1.00 41.52  ? 476  LEU C N   1 
ATOM   12048 C  CA  . LEU C  1 476 ? -42.208 12.671  93.145  1.00 39.17  ? 476  LEU C CA  1 
ATOM   12049 C  C   . LEU C  1 476 ? -41.362 11.964  94.198  1.00 39.70  ? 476  LEU C C   1 
ATOM   12050 O  O   . LEU C  1 476 ? -40.901 10.842  93.963  1.00 42.14  ? 476  LEU C O   1 
ATOM   12051 C  CB  . LEU C  1 476 ? -41.391 13.787  92.486  1.00 29.63  ? 476  LEU C CB  1 
ATOM   12052 C  CG  . LEU C  1 476 ? -41.843 14.321  91.127  1.00 26.51  ? 476  LEU C CG  1 
ATOM   12053 C  CD1 . LEU C  1 476 ? -40.735 15.154  90.495  1.00 22.55  ? 476  LEU C CD1 1 
ATOM   12054 C  CD2 . LEU C  1 476 ? -42.261 13.186  90.213  1.00 24.16  ? 476  LEU C CD2 1 
ATOM   12055 N  N   . MET C  1 477 ? -41.146 12.607  95.349  1.00 32.13  ? 477  MET C N   1 
ATOM   12056 C  CA  . MET C  1 477 ? -40.369 11.955  96.413  1.00 31.61  ? 477  MET C CA  1 
ATOM   12057 C  C   . MET C  1 477 ? -41.038 10.658  96.815  1.00 32.17  ? 477  MET C C   1 
ATOM   12058 O  O   . MET C  1 477 ? -40.350 9.691   97.159  1.00 29.63  ? 477  MET C O   1 
ATOM   12059 C  CB  . MET C  1 477 ? -40.221 12.829  97.651  1.00 23.06  ? 477  MET C CB  1 
ATOM   12060 C  CG  . MET C  1 477 ? -39.609 14.154  97.388  1.00 22.60  ? 477  MET C CG  1 
ATOM   12061 S  SD  . MET C  1 477 ? -40.119 15.354  98.619  1.00 26.77  ? 477  MET C SD  1 
ATOM   12062 C  CE  . MET C  1 477 ? -39.448 14.661  100.128 1.00 23.33  ? 477  MET C CE  1 
ATOM   12063 N  N   . LYS C  1 478 ? -42.377 10.649  96.776  1.00 33.15  ? 478  LYS C N   1 
ATOM   12064 C  CA  . LYS C  1 478 ? -43.145 9.436   97.049  1.00 34.73  ? 478  LYS C CA  1 
ATOM   12065 C  C   . LYS C  1 478 ? -42.779 8.316   96.075  1.00 30.50  ? 478  LYS C C   1 
ATOM   12066 O  O   . LYS C  1 478 ? -42.420 7.216   96.507  1.00 27.76  ? 478  LYS C O   1 
ATOM   12067 C  CB  . LYS C  1 478 ? -44.648 9.712   97.029  1.00 59.73  ? 478  LYS C CB  1 
ATOM   12068 C  CG  . LYS C  1 478 ? -45.266 9.839   98.413  1.00 67.48  ? 478  LYS C CG  1 
ATOM   12069 C  CD  . LYS C  1 478 ? -45.568 8.475   99.028  1.00 71.80  ? 478  LYS C CD  1 
ATOM   12070 C  CE  . LYS C  1 478 ? -46.127 8.604   100.450 1.00 74.72  ? 478  LYS C CE  1 
ATOM   12071 N  NZ  . LYS C  1 478 ? -47.489 9.233   100.517 1.00 76.23  ? 478  LYS C NZ  1 
ATOM   12072 N  N   . TYR C  1 479 ? -42.849 8.601   94.771  1.00 34.11  ? 479  TYR C N   1 
ATOM   12073 C  CA  . TYR C  1 479 ? -42.413 7.639   93.747  1.00 30.39  ? 479  TYR C CA  1 
ATOM   12074 C  C   . TYR C  1 479 ? -40.998 7.124   94.027  1.00 27.17  ? 479  TYR C C   1 
ATOM   12075 O  O   . TYR C  1 479 ? -40.766 5.919   94.098  1.00 26.42  ? 479  TYR C O   1 
ATOM   12076 C  CB  . TYR C  1 479 ? -42.439 8.267   92.351  1.00 26.56  ? 479  TYR C CB  1 
ATOM   12077 C  CG  . TYR C  1 479 ? -43.809 8.575   91.778  1.00 28.20  ? 479  TYR C CG  1 
ATOM   12078 C  CD1 . TYR C  1 479 ? -44.841 7.647   91.838  1.00 29.40  ? 479  TYR C CD1 1 
ATOM   12079 C  CD2 . TYR C  1 479 ? -44.061 9.803   91.154  1.00 29.76  ? 479  TYR C CD2 1 
ATOM   12080 C  CE1 . TYR C  1 479 ? -46.105 7.939   91.302  1.00 34.01  ? 479  TYR C CE1 1 
ATOM   12081 C  CE2 . TYR C  1 479 ? -45.308 10.105  90.614  1.00 32.92  ? 479  TYR C CE2 1 
ATOM   12082 C  CZ  . TYR C  1 479 ? -46.335 9.171   90.689  1.00 35.80  ? 479  TYR C CZ  1 
ATOM   12083 O  OH  . TYR C  1 479 ? -47.584 9.466   90.154  1.00 36.09  ? 479  TYR C OH  1 
ATOM   12084 N  N   . TRP C  1 480 ? -40.058 8.046   94.198  1.00 22.32  ? 480  TRP C N   1 
ATOM   12085 C  CA  . TRP C  1 480 ? -38.654 7.676   94.353  1.00 26.40  ? 480  TRP C CA  1 
ATOM   12086 C  C   . TRP C  1 480 ? -38.362 6.824   95.579  1.00 27.95  ? 480  TRP C C   1 
ATOM   12087 O  O   . TRP C  1 480 ? -37.637 5.826   95.484  1.00 27.60  ? 480  TRP C O   1 
ATOM   12088 C  CB  . TRP C  1 480 ? -37.769 8.918   94.382  1.00 20.50  ? 480  TRP C CB  1 
ATOM   12089 C  CG  . TRP C  1 480 ? -37.068 9.197   93.101  1.00 19.76  ? 480  TRP C CG  1 
ATOM   12090 C  CD1 . TRP C  1 480 ? -35.727 9.284   92.913  1.00 18.81  ? 480  TRP C CD1 1 
ATOM   12091 C  CD2 . TRP C  1 480 ? -37.673 9.435   91.817  1.00 20.02  ? 480  TRP C CD2 1 
ATOM   12092 N  NE1 . TRP C  1 480 ? -35.455 9.566   91.599  1.00 18.45  ? 480  TRP C NE1 1 
ATOM   12093 C  CE2 . TRP C  1 480 ? -36.636 9.659   90.905  1.00 19.18  ? 480  TRP C CE2 1 
ATOM   12094 C  CE3 . TRP C  1 480 ? -38.996 9.480   91.352  1.00 20.97  ? 480  TRP C CE3 1 
ATOM   12095 C  CZ2 . TRP C  1 480 ? -36.879 9.921   89.552  1.00 19.24  ? 480  TRP C CZ2 1 
ATOM   12096 C  CZ3 . TRP C  1 480 ? -39.230 9.739   90.007  1.00 21.03  ? 480  TRP C CZ3 1 
ATOM   12097 C  CH2 . TRP C  1 480 ? -38.183 9.949   89.129  1.00 20.18  ? 480  TRP C CH2 1 
ATOM   12098 N  N   . THR C  1 481 ? -38.903 7.218   96.733  1.00 31.76  ? 481  THR C N   1 
ATOM   12099 C  CA  . THR C  1 481 ? -38.596 6.508   97.969  1.00 31.33  ? 481  THR C CA  1 
ATOM   12100 C  C   . THR C  1 481 ? -39.381 5.214   97.996  1.00 33.04  ? 481  THR C C   1 
ATOM   12101 O  O   . THR C  1 481 ? -38.968 4.252   98.639  1.00 31.86  ? 481  THR C O   1 
ATOM   12102 C  CB  . THR C  1 481 ? -38.949 7.305   99.225  1.00 29.53  ? 481  THR C CB  1 
ATOM   12103 O  OG1 . THR C  1 481 ? -40.351 7.557   99.229  1.00 33.43  ? 481  THR C OG1 1 
ATOM   12104 C  CG2 . THR C  1 481 ? -38.191 8.619   99.295  1.00 27.55  ? 481  THR C CG2 1 
ATOM   12105 N  N   . ASN C  1 482 ? -40.520 5.194   97.307  1.00 32.27  ? 482  ASN C N   1 
ATOM   12106 C  CA  . ASN C  1 482 ? -41.245 3.943   97.112  1.00 36.79  ? 482  ASN C CA  1 
ATOM   12107 C  C   . ASN C  1 482 ? -40.427 2.958   96.294  1.00 37.25  ? 482  ASN C C   1 
ATOM   12108 O  O   . ASN C  1 482 ? -40.435 1.756   96.564  1.00 35.18  ? 482  ASN C O   1 
ATOM   12109 C  CB  . ASN C  1 482 ? -42.607 4.172   96.469  1.00 50.81  ? 482  ASN C CB  1 
ATOM   12110 C  CG  . ASN C  1 482 ? -43.663 4.512   97.485  1.00 58.02  ? 482  ASN C CG  1 
ATOM   12111 O  OD1 . ASN C  1 482 ? -44.363 5.514   97.358  1.00 61.10  ? 482  ASN C OD1 1 
ATOM   12112 N  ND2 . ASN C  1 482 ? -43.776 3.682   98.520  1.00 59.76  ? 482  ASN C ND2 1 
ATOM   12113 N  N   . PHE C  1 483 ? -39.712 3.471   95.297  1.00 51.04  ? 483  PHE C N   1 
ATOM   12114 C  CA  . PHE C  1 483 ? -38.795 2.634   94.540  1.00 48.30  ? 483  PHE C CA  1 
ATOM   12115 C  C   . PHE C  1 483 ? -37.666 2.136   95.424  1.00 47.39  ? 483  PHE C C   1 
ATOM   12116 O  O   . PHE C  1 483 ? -37.328 0.958   95.414  1.00 48.33  ? 483  PHE C O   1 
ATOM   12117 C  CB  . PHE C  1 483 ? -38.204 3.383   93.356  1.00 30.67  ? 483  PHE C CB  1 
ATOM   12118 C  CG  . PHE C  1 483 ? -37.316 2.530   92.511  1.00 26.93  ? 483  PHE C CG  1 
ATOM   12119 C  CD1 . PHE C  1 483 ? -37.825 1.405   91.874  1.00 30.54  ? 483  PHE C CD1 1 
ATOM   12120 C  CD2 . PHE C  1 483 ? -35.979 2.820   92.374  1.00 23.95  ? 483  PHE C CD2 1 
ATOM   12121 C  CE1 . PHE C  1 483 ? -37.016 0.592   91.094  1.00 31.49  ? 483  PHE C CE1 1 
ATOM   12122 C  CE2 . PHE C  1 483 ? -35.165 2.022   91.599  1.00 27.63  ? 483  PHE C CE2 1 
ATOM   12123 C  CZ  . PHE C  1 483 ? -35.685 0.905   90.952  1.00 30.99  ? 483  PHE C CZ  1 
ATOM   12124 N  N   . ALA C  1 484 ? -37.082 3.048   96.186  1.00 36.32  ? 484  ALA C N   1 
ATOM   12125 C  CA  . ALA C  1 484 ? -36.009 2.696   97.102  1.00 35.87  ? 484  ALA C CA  1 
ATOM   12126 C  C   . ALA C  1 484 ? -36.435 1.613   98.104  1.00 38.49  ? 484  ALA C C   1 
ATOM   12127 O  O   . ALA C  1 484 ? -35.631 0.760   98.493  1.00 38.36  ? 484  ALA C O   1 
ATOM   12128 C  CB  . ALA C  1 484 ? -35.527 3.940   97.830  1.00 30.11  ? 484  ALA C CB  1 
ATOM   12129 N  N   . ARG C  1 485 ? -37.706 1.655   98.500  1.00 37.43  ? 485  ARG C N   1 
ATOM   12130 C  CA  . ARG C  1 485 ? -38.264 0.768   99.519  1.00 35.26  ? 485  ARG C CA  1 
ATOM   12131 C  C   . ARG C  1 485 ? -38.663 -0.588  98.950  1.00 28.37  ? 485  ARG C C   1 
ATOM   12132 O  O   . ARG C  1 485 ? -38.131 -1.611  99.362  1.00 28.09  ? 485  ARG C O   1 
ATOM   12133 C  CB  . ARG C  1 485 ? -39.509 1.411   100.122 1.00 48.09  ? 485  ARG C CB  1 
ATOM   12134 C  CG  . ARG C  1 485 ? -39.455 1.697   101.600 1.00 52.87  ? 485  ARG C CG  1 
ATOM   12135 C  CD  . ARG C  1 485 ? -40.759 2.348   102.056 1.00 58.43  ? 485  ARG C CD  1 
ATOM   12136 N  NE  . ARG C  1 485 ? -41.107 3.561   101.302 1.00 61.74  ? 485  ARG C NE  1 
ATOM   12137 C  CZ  . ARG C  1 485 ? -40.970 4.808   101.760 1.00 63.87  ? 485  ARG C CZ  1 
ATOM   12138 N  NH1 . ARG C  1 485 ? -40.484 5.035   102.978 1.00 65.54  ? 485  ARG C NH1 1 
ATOM   12139 N  NH2 . ARG C  1 485 ? -41.322 5.839   101.001 1.00 62.40  ? 485  ARG C NH2 1 
ATOM   12140 N  N   . THR C  1 486 ? -39.651 -0.595  98.058  1.00 25.19  ? 486  THR C N   1 
ATOM   12141 C  CA  . THR C  1 486 ? -40.180 -1.836  97.514  1.00 26.01  ? 486  THR C CA  1 
ATOM   12142 C  C   . THR C  1 486 ? -39.602 -2.260  96.171  1.00 25.40  ? 486  THR C C   1 
ATOM   12143 O  O   . THR C  1 486 ? -39.763 -3.407  95.769  1.00 26.80  ? 486  THR C O   1 
ATOM   12144 C  CB  . THR C  1 486 ? -41.709 -1.745  97.366  1.00 56.91  ? 486  THR C CB  1 
ATOM   12145 O  OG1 . THR C  1 486 ? -42.047 -1.260  96.064  1.00 59.66  ? 486  THR C OG1 1 
ATOM   12146 C  CG2 . THR C  1 486 ? -42.290 -0.796  98.403  1.00 62.43  ? 486  THR C CG2 1 
ATOM   12147 N  N   . GLY C  1 487 ? -38.899 -1.363  95.487  1.00 24.27  ? 487  GLY C N   1 
ATOM   12148 C  CA  . GLY C  1 487 ? -38.443 -1.640  94.132  1.00 23.76  ? 487  GLY C CA  1 
ATOM   12149 C  C   . GLY C  1 487 ? -39.491 -1.320  93.075  1.00 27.11  ? 487  GLY C C   1 
ATOM   12150 O  O   . GLY C  1 487 ? -39.285 -1.570  91.894  1.00 26.39  ? 487  GLY C O   1 
ATOM   12151 N  N   . ASP C  1 488 ? -40.621 -0.775  93.518  1.00 33.91  ? 488  ASP C N   1 
ATOM   12152 C  CA  . ASP C  1 488 ? -41.813 -0.516  92.699  1.00 38.11  ? 488  ASP C CA  1 
ATOM   12153 C  C   . ASP C  1 488 ? -42.415 0.874   92.989  1.00 38.11  ? 488  ASP C C   1 
ATOM   12154 O  O   . ASP C  1 488 ? -43.117 1.042   93.983  1.00 42.60  ? 488  ASP C O   1 
ATOM   12155 C  CB  . ASP C  1 488 ? -42.840 -1.644  92.890  1.00 55.53  ? 488  ASP C CB  1 
ATOM   12156 C  CG  . ASP C  1 488 ? -44.117 -1.436  92.089  1.00 63.75  ? 488  ASP C CG  1 
ATOM   12157 O  OD1 . ASP C  1 488 ? -44.174 -0.511  91.254  1.00 67.21  ? 488  ASP C OD1 1 
ATOM   12158 O  OD2 . ASP C  1 488 ? -45.077 -2.209  92.299  1.00 66.08  ? 488  ASP C OD2 1 
ATOM   12159 N  N   . PRO C  1 489 ? -42.136 1.873   92.138  1.00 36.10  ? 489  PRO C N   1 
ATOM   12160 C  CA  . PRO C  1 489 ? -42.441 3.294   92.387  1.00 36.74  ? 489  PRO C CA  1 
ATOM   12161 C  C   . PRO C  1 489 ? -43.889 3.578   92.809  1.00 42.37  ? 489  PRO C C   1 
ATOM   12162 O  O   . PRO C  1 489 ? -44.172 4.676   93.303  1.00 43.62  ? 489  PRO C O   1 
ATOM   12163 C  CB  . PRO C  1 489 ? -42.179 3.955   91.025  1.00 28.63  ? 489  PRO C CB  1 
ATOM   12164 C  CG  . PRO C  1 489 ? -42.391 2.869   90.034  1.00 29.50  ? 489  PRO C CG  1 
ATOM   12165 C  CD  . PRO C  1 489 ? -41.870 1.618   90.712  1.00 30.49  ? 489  PRO C CD  1 
ATOM   12166 N  N   . ASN C  1 490 ? -44.789 2.622   92.578  1.00 31.84  ? 490  ASN C N   1 
ATOM   12167 C  CA  . ASN C  1 490 ? -46.211 2.776   92.892  1.00 36.13  ? 490  ASN C CA  1 
ATOM   12168 C  C   . ASN C  1 490 ? -46.592 2.871   94.372  1.00 48.19  ? 490  ASN C C   1 
ATOM   12169 O  O   . ASN C  1 490 ? -46.040 2.157   95.216  1.00 45.17  ? 490  ASN C O   1 
ATOM   12170 C  CB  . ASN C  1 490 ? -46.986 1.613   92.296  1.00 40.22  ? 490  ASN C CB  1 
ATOM   12171 C  CG  . ASN C  1 490 ? -46.936 1.590   90.796  1.00 37.48  ? 490  ASN C CG  1 
ATOM   12172 O  OD1 . ASN C  1 490 ? -47.585 2.402   90.136  1.00 36.80  ? 490  ASN C OD1 1 
ATOM   12173 N  ND2 . ASN C  1 490 ? -46.199 0.636   90.241  1.00 29.33  ? 490  ASN C ND2 1 
ATOM   12174 N  N   . ASP C  1 491 ? -47.548 3.751   94.677  1.00 96.93  ? 491  ASP C N   1 
ATOM   12175 C  CA  . ASP C  1 491 ? -48.241 3.706   95.963  1.00 110.82 ? 491  ASP C CA  1 
ATOM   12176 C  C   . ASP C  1 491 ? -48.999 2.399   95.894  1.00 117.73 ? 491  ASP C C   1 
ATOM   12177 O  O   . ASP C  1 491 ? -49.678 2.141   94.896  1.00 120.76 ? 491  ASP C O   1 
ATOM   12178 C  CB  . ASP C  1 491 ? -49.196 4.893   96.135  1.00 104.23 ? 491  ASP C CB  1 
ATOM   12179 C  CG  . ASP C  1 491 ? -48.460 6.224   96.286  1.00 105.32 ? 491  ASP C CG  1 
ATOM   12180 O  OD1 . ASP C  1 491 ? -48.082 6.575   97.430  1.00 105.02 ? 491  ASP C OD1 1 
ATOM   12181 O  OD2 . ASP C  1 491 ? -48.257 6.916   95.261  1.00 104.67 ? 491  ASP C OD2 1 
ATOM   12182 N  N   . PRO C  1 492 ? -48.880 1.565   96.941  1.00 124.76 ? 492  PRO C N   1 
ATOM   12183 C  CA  . PRO C  1 492 ? -49.026 0.136   96.636  1.00 130.37 ? 492  PRO C CA  1 
ATOM   12184 C  C   . PRO C  1 492 ? -50.339 -0.353  95.995  1.00 143.03 ? 492  PRO C C   1 
ATOM   12185 O  O   . PRO C  1 492 ? -50.233 -0.881  94.883  1.00 146.26 ? 492  PRO C O   1 
ATOM   12186 C  CB  . PRO C  1 492 ? -48.833 -0.519  98.010  1.00 69.48  ? 492  PRO C CB  1 
ATOM   12187 C  CG  . PRO C  1 492 ? -47.880 0.403   98.700  1.00 65.01  ? 492  PRO C CG  1 
ATOM   12188 C  CD  . PRO C  1 492 ? -48.272 1.794   98.263  1.00 66.03  ? 492  PRO C CD  1 
ATOM   12189 N  N   . ARG C  1 493 ? -51.519 -0.184  96.588  0.96 135.87 ? 493  ARG C N   1 
ATOM   12190 C  CA  . ARG C  1 493 ? -52.724 -0.507  95.805  0.96 138.41 ? 493  ARG C CA  1 
ATOM   12191 C  C   . ARG C  1 493 ? -53.710 0.573   95.325  0.96 142.85 ? 493  ARG C C   1 
ATOM   12192 O  O   . ARG C  1 493 ? -54.665 0.244   94.613  0.96 145.49 ? 493  ARG C O   1 
ATOM   12193 C  CB  . ARG C  1 493 ? -53.453 -1.770  96.290  0.96 117.11 ? 493  ARG C CB  1 
ATOM   12194 C  CG  . ARG C  1 493 ? -53.829 -2.696  95.113  0.96 113.82 ? 493  ARG C CG  1 
ATOM   12195 C  CD  . ARG C  1 493 ? -55.232 -3.266  95.247  0.96 113.26 ? 493  ARG C CD  1 
ATOM   12196 N  NE  . ARG C  1 493 ? -55.326 -4.115  96.427  0.96 112.74 ? 493  ARG C NE  1 
ATOM   12197 C  CZ  . ARG C  1 493 ? -55.037 -5.411  96.438  0.96 111.43 ? 493  ARG C CZ  1 
ATOM   12198 N  NH1 . ARG C  1 493 ? -54.651 -6.017  95.320  0.96 110.54 ? 493  ARG C NH1 1 
ATOM   12199 N  NH2 . ARG C  1 493 ? -55.138 -6.103  97.567  0.96 111.04 ? 493  ARG C NH2 1 
ATOM   12200 N  N   . ASP C  1 494 ? -53.512 1.835   95.699  1.00 141.77 ? 494  ASP C N   1 
ATOM   12201 C  CA  . ASP C  1 494 ? -54.518 2.839   95.356  1.00 143.61 ? 494  ASP C CA  1 
ATOM   12202 C  C   . ASP C  1 494 ? -54.669 2.921   93.839  1.00 145.67 ? 494  ASP C C   1 
ATOM   12203 O  O   . ASP C  1 494 ? -53.693 3.131   93.114  1.00 145.68 ? 494  ASP C O   1 
ATOM   12204 C  CB  . ASP C  1 494 ? -54.175 4.203   95.951  1.00 123.68 ? 494  ASP C CB  1 
ATOM   12205 C  CG  . ASP C  1 494 ? -55.152 5.286   95.525  1.00 122.04 ? 494  ASP C CG  1 
ATOM   12206 O  OD1 . ASP C  1 494 ? -56.267 4.954   95.058  1.00 121.59 ? 494  ASP C OD1 1 
ATOM   12207 O  OD2 . ASP C  1 494 ? -54.790 6.477   95.638  1.00 120.91 ? 494  ASP C OD2 1 
ATOM   12208 N  N   . SER C  1 495 ? -55.898 2.711   93.371  0.91 145.59 ? 495  SER C N   1 
ATOM   12209 C  CA  . SER C  1 495 ? -56.148 2.548   91.939  0.91 143.85 ? 495  SER C CA  1 
ATOM   12210 C  C   . SER C  1 495 ? -56.705 3.743   91.141  0.91 143.38 ? 495  SER C C   1 
ATOM   12211 O  O   . SER C  1 495 ? -56.809 3.652   89.913  0.91 144.26 ? 495  SER C O   1 
ATOM   12212 C  CB  . SER C  1 495 ? -56.990 1.291   91.692  0.91 125.09 ? 495  SER C CB  1 
ATOM   12213 O  OG  . SER C  1 495 ? -56.357 0.148   92.246  0.91 122.44 ? 495  SER C OG  1 
ATOM   12214 N  N   . LYS C  1 496 ? -57.036 4.857   91.798  0.84 135.64 ? 496  LYS C N   1 
ATOM   12215 C  CA  . LYS C  1 496 ? -57.517 6.014   91.040  0.84 130.95 ? 496  LYS C CA  1 
ATOM   12216 C  C   . LYS C  1 496 ? -56.264 6.573   90.386  0.84 126.90 ? 496  LYS C C   1 
ATOM   12217 O  O   . LYS C  1 496 ? -56.084 6.426   89.173  0.84 126.31 ? 496  LYS C O   1 
ATOM   12218 C  CB  . LYS C  1 496 ? -58.174 7.033   91.973  0.84 114.33 ? 496  LYS C CB  1 
ATOM   12219 C  CG  . LYS C  1 496 ? -58.517 8.382   91.339  0.84 110.36 ? 496  LYS C CG  1 
ATOM   12220 C  CD  . LYS C  1 496 ? -59.449 8.259   90.142  0.84 107.09 ? 496  LYS C CD  1 
ATOM   12221 C  CE  . LYS C  1 496 ? -60.048 9.617   89.787  0.84 104.10 ? 496  LYS C CE  1 
ATOM   12222 N  NZ  . LYS C  1 496 ? -59.063 10.731  89.948  0.84 100.00 ? 496  LYS C NZ  1 
ATOM   12223 N  N   . SER C  1 497 ? -55.438 7.266   91.168  0.92 121.41 ? 497  SER C N   1 
ATOM   12224 C  CA  . SER C  1 497 ? -54.037 6.889   91.358  0.92 116.17 ? 497  SER C CA  1 
ATOM   12225 C  C   . SER C  1 497 ? -53.455 6.018   90.236  0.92 112.15 ? 497  SER C C   1 
ATOM   12226 O  O   . SER C  1 497 ? -53.155 4.842   90.476  0.92 110.89 ? 497  SER C O   1 
ATOM   12227 C  CB  . SER C  1 497 ? -53.883 6.197   92.708  0.92 108.85 ? 497  SER C CB  1 
ATOM   12228 O  OG  . SER C  1 497 ? -52.538 6.146   93.138  0.92 107.11 ? 497  SER C OG  1 
ATOM   12229 N  N   . PRO C  1 498 ? -53.336 6.562   89.012  1.00 103.00 ? 498  PRO C N   1 
ATOM   12230 C  CA  . PRO C  1 498 ? -53.005 5.708   87.863  1.00 96.03  ? 498  PRO C CA  1 
ATOM   12231 C  C   . PRO C  1 498 ? -51.727 4.911   88.094  1.00 85.80  ? 498  PRO C C   1 
ATOM   12232 O  O   . PRO C  1 498 ? -50.789 5.388   88.746  1.00 80.99  ? 498  PRO C O   1 
ATOM   12233 C  CB  . PRO C  1 498 ? -52.837 6.706   86.711  1.00 102.95 ? 498  PRO C CB  1 
ATOM   12234 C  CG  . PRO C  1 498 ? -52.534 8.010   87.374  1.00 104.80 ? 498  PRO C CG  1 
ATOM   12235 C  CD  . PRO C  1 498 ? -53.285 7.995   88.673  1.00 107.68 ? 498  PRO C CD  1 
ATOM   12236 N  N   . GLN C  1 499 ? -51.711 3.683   87.595  1.00 83.45  ? 499  GLN C N   1 
ATOM   12237 C  CA  . GLN C  1 499 ? -50.582 2.808   87.848  1.00 76.82  ? 499  GLN C CA  1 
ATOM   12238 C  C   . GLN C  1 499 ? -49.513 3.025   86.798  1.00 69.39  ? 499  GLN C C   1 
ATOM   12239 O  O   . GLN C  1 499 ? -49.802 3.077   85.599  1.00 69.66  ? 499  GLN C O   1 
ATOM   12240 C  CB  . GLN C  1 499 ? -51.010 1.330   87.926  1.00 69.31  ? 499  GLN C CB  1 
ATOM   12241 C  CG  . GLN C  1 499 ? -50.339 0.511   89.054  1.00 68.24  ? 499  GLN C CG  1 
ATOM   12242 C  CD  . GLN C  1 499 ? -50.734 0.963   90.478  1.00 71.76  ? 499  GLN C CD  1 
ATOM   12243 O  OE1 . GLN C  1 499 ? -51.254 2.062   90.688  1.00 73.57  ? 499  GLN C OE1 1 
ATOM   12244 N  NE2 . GLN C  1 499 ? -50.484 0.100   91.459  1.00 72.47  ? 499  GLN C NE2 1 
ATOM   12245 N  N   . TRP C  1 500 ? -48.286 3.184   87.291  1.00 38.85  ? 500  TRP C N   1 
ATOM   12246 C  CA  . TRP C  1 500 ? -47.065 3.265   86.495  1.00 29.79  ? 500  TRP C CA  1 
ATOM   12247 C  C   . TRP C  1 500 ? -46.532 1.847   86.284  1.00 29.21  ? 500  TRP C C   1 
ATOM   12248 O  O   . TRP C  1 500 ? -46.050 1.217   87.217  1.00 28.89  ? 500  TRP C O   1 
ATOM   12249 C  CB  . TRP C  1 500 ? -46.060 4.129   87.261  1.00 40.78  ? 500  TRP C CB  1 
ATOM   12250 C  CG  . TRP C  1 500 ? -44.698 4.304   86.682  1.00 38.45  ? 500  TRP C CG  1 
ATOM   12251 C  CD1 . TRP C  1 500 ? -44.165 3.681   85.592  1.00 39.57  ? 500  TRP C CD1 1 
ATOM   12252 C  CD2 . TRP C  1 500 ? -43.681 5.171   87.186  1.00 35.34  ? 500  TRP C CD2 1 
ATOM   12253 N  NE1 . TRP C  1 500 ? -42.874 4.109   85.387  1.00 37.25  ? 500  TRP C NE1 1 
ATOM   12254 C  CE2 . TRP C  1 500 ? -42.555 5.022   86.352  1.00 34.47  ? 500  TRP C CE2 1 
ATOM   12255 C  CE3 . TRP C  1 500 ? -43.616 6.057   88.260  1.00 33.21  ? 500  TRP C CE3 1 
ATOM   12256 C  CZ2 . TRP C  1 500 ? -41.381 5.728   86.560  1.00 31.46  ? 500  TRP C CZ2 1 
ATOM   12257 C  CZ3 . TRP C  1 500 ? -42.455 6.758   88.463  1.00 32.34  ? 500  TRP C CZ3 1 
ATOM   12258 C  CH2 . TRP C  1 500 ? -41.347 6.589   87.620  1.00 31.34  ? 500  TRP C CH2 1 
ATOM   12259 N  N   . PRO C  1 501 ? -46.644 1.344   85.049  1.00 29.57  ? 501  PRO C N   1 
ATOM   12260 C  CA  . PRO C  1 501 ? -46.250 0.007   84.605  1.00 29.68  ? 501  PRO C CA  1 
ATOM   12261 C  C   . PRO C  1 501 ? -44.756 -0.107  84.361  1.00 31.25  ? 501  PRO C C   1 
ATOM   12262 O  O   . PRO C  1 501 ? -44.102 0.887   84.020  1.00 28.90  ? 501  PRO C O   1 
ATOM   12263 C  CB  . PRO C  1 501 ? -46.960 -0.136  83.255  1.00 30.64  ? 501  PRO C CB  1 
ATOM   12264 C  CG  . PRO C  1 501 ? -47.833 1.089   83.104  1.00 31.25  ? 501  PRO C CG  1 
ATOM   12265 C  CD  . PRO C  1 501 ? -47.210 2.130   83.944  1.00 31.23  ? 501  PRO C CD  1 
ATOM   12266 N  N   . PRO C  1 502 ? -44.208 -1.317  84.497  1.00 43.94  ? 502  PRO C N   1 
ATOM   12267 C  CA  . PRO C  1 502 ? -42.798 -1.488  84.161  1.00 44.58  ? 502  PRO C CA  1 
ATOM   12268 C  C   . PRO C  1 502 ? -42.588 -1.384  82.648  1.00 46.31  ? 502  PRO C C   1 
ATOM   12269 O  O   . PRO C  1 502 ? -43.467 -1.752  81.866  1.00 48.96  ? 502  PRO C O   1 
ATOM   12270 C  CB  . PRO C  1 502 ? -42.503 -2.902  84.653  1.00 39.60  ? 502  PRO C CB  1 
ATOM   12271 C  CG  . PRO C  1 502 ? -43.795 -3.601  84.502  1.00 41.86  ? 502  PRO C CG  1 
ATOM   12272 C  CD  . PRO C  1 502 ? -44.846 -2.589  84.856  1.00 41.31  ? 502  PRO C CD  1 
ATOM   12273 N  N   . TYR C  1 503 ? -41.436 -0.849  82.255  1.00 36.72  ? 503  TYR C N   1 
ATOM   12274 C  CA  . TYR C  1 503 ? -41.037 -0.763  80.860  1.00 33.96  ? 503  TYR C CA  1 
ATOM   12275 C  C   . TYR C  1 503 ? -40.569 -2.134  80.416  1.00 33.86  ? 503  TYR C C   1 
ATOM   12276 O  O   . TYR C  1 503 ? -39.685 -2.719  81.036  1.00 33.22  ? 503  TYR C O   1 
ATOM   12277 C  CB  . TYR C  1 503 ? -39.908 0.254   80.706  1.00 24.14  ? 503  TYR C CB  1 
ATOM   12278 C  CG  . TYR C  1 503 ? -39.399 0.403   79.300  1.00 24.74  ? 503  TYR C CG  1 
ATOM   12279 C  CD1 . TYR C  1 503 ? -39.981 1.307   78.424  1.00 26.96  ? 503  TYR C CD1 1 
ATOM   12280 C  CD2 . TYR C  1 503 ? -38.323 -0.350  78.844  1.00 25.53  ? 503  TYR C CD2 1 
ATOM   12281 C  CE1 . TYR C  1 503 ? -39.509 1.452   77.113  1.00 29.09  ? 503  TYR C CE1 1 
ATOM   12282 C  CE2 . TYR C  1 503 ? -37.838 -0.214  77.535  1.00 27.44  ? 503  TYR C CE2 1 
ATOM   12283 C  CZ  . TYR C  1 503 ? -38.436 0.689   76.672  1.00 27.04  ? 503  TYR C CZ  1 
ATOM   12284 O  OH  . TYR C  1 503 ? -37.971 0.828   75.374  1.00 23.75  ? 503  TYR C OH  1 
ATOM   12285 N  N   . THR C  1 504 ? -41.179 -2.648  79.352  1.00 40.91  ? 504  THR C N   1 
ATOM   12286 C  CA  . THR C  1 504 ? -40.835 -3.953  78.802  1.00 44.74  ? 504  THR C CA  1 
ATOM   12287 C  C   . THR C  1 504 ? -40.413 -3.773  77.355  1.00 50.26  ? 504  THR C C   1 
ATOM   12288 O  O   . THR C  1 504 ? -40.756 -2.766  76.734  1.00 52.81  ? 504  THR C O   1 
ATOM   12289 C  CB  . THR C  1 504 ? -42.037 -4.886  78.838  1.00 47.34  ? 504  THR C CB  1 
ATOM   12290 O  OG1 . THR C  1 504 ? -43.069 -4.366  77.992  1.00 47.08  ? 504  THR C OG1 1 
ATOM   12291 C  CG2 . THR C  1 504 ? -42.572 -4.986  80.247  1.00 50.39  ? 504  THR C CG2 1 
ATOM   12292 N  N   . THR C  1 505 ? -39.675 -4.738  76.811  1.00 50.41  ? 505  THR C N   1 
ATOM   12293 C  CA  . THR C  1 505 ? -39.167 -4.608  75.444  1.00 48.33  ? 505  THR C CA  1 
ATOM   12294 C  C   . THR C  1 505 ? -40.298 -4.615  74.442  1.00 47.26  ? 505  THR C C   1 
ATOM   12295 O  O   . THR C  1 505 ? -40.319 -3.812  73.512  1.00 46.32  ? 505  THR C O   1 
ATOM   12296 C  CB  . THR C  1 505 ? -38.194 -5.729  75.082  1.00 46.46  ? 505  THR C CB  1 
ATOM   12297 O  OG1 . THR C  1 505 ? -38.604 -6.937  75.734  1.00 47.79  ? 505  THR C OG1 1 
ATOM   12298 C  CG2 . THR C  1 505 ? -36.788 -5.362  75.528  1.00 44.75  ? 505  THR C CG2 1 
ATOM   12299 N  N   . ALA C  1 506 ? -41.230 -5.538  74.639  1.00 44.53  ? 506  ALA C N   1 
ATOM   12300 C  CA  . ALA C  1 506 ? -42.413 -5.639  73.797  1.00 45.57  ? 506  ALA C CA  1 
ATOM   12301 C  C   . ALA C  1 506 ? -43.264 -4.369  73.785  1.00 41.09  ? 506  ALA C C   1 
ATOM   12302 O  O   . ALA C  1 506 ? -43.324 -3.667  72.780  1.00 40.33  ? 506  ALA C O   1 
ATOM   12303 C  CB  . ALA C  1 506 ? -43.256 -6.824  74.231  1.00 62.10  ? 506  ALA C CB  1 
ATOM   12304 N  N   . ALA C  1 507 ? -43.922 -4.091  74.907  1.00 40.75  ? 507  ALA C N   1 
ATOM   12305 C  CA  . ALA C  1 507 ? -44.927 -3.029  74.994  1.00 41.17  ? 507  ALA C CA  1 
ATOM   12306 C  C   . ALA C  1 507 ? -44.393 -1.597  75.195  1.00 40.06  ? 507  ALA C C   1 
ATOM   12307 O  O   . ALA C  1 507 ? -45.079 -0.635  74.835  1.00 39.60  ? 507  ALA C O   1 
ATOM   12308 C  CB  . ALA C  1 507 ? -45.946 -3.375  76.061  1.00 47.48  ? 507  ALA C CB  1 
ATOM   12309 N  N   . GLN C  1 508 ? -43.203 -1.479  75.803  1.00 35.46  ? 508  GLN C N   1 
ATOM   12310 C  CA  . GLN C  1 508 ? -42.442 -0.220  75.963  1.00 30.85  ? 508  GLN C CA  1 
ATOM   12311 C  C   . GLN C  1 508 ? -43.109 0.977   76.656  1.00 28.90  ? 508  GLN C C   1 
ATOM   12312 O  O   . GLN C  1 508 ? -43.130 2.069   76.098  1.00 28.24  ? 508  GLN C O   1 
ATOM   12313 C  CB  . GLN C  1 508 ? -41.951 0.270   74.613  1.00 39.56  ? 508  GLN C CB  1 
ATOM   12314 C  CG  . GLN C  1 508 ? -41.236 -0.748  73.781  1.00 45.26  ? 508  GLN C CG  1 
ATOM   12315 C  CD  . GLN C  1 508 ? -40.568 -0.096  72.591  1.00 49.11  ? 508  GLN C CD  1 
ATOM   12316 O  OE1 . GLN C  1 508 ? -40.049 1.029   72.699  1.00 47.67  ? 508  GLN C OE1 1 
ATOM   12317 N  NE2 . GLN C  1 508 ? -40.591 -0.780  71.440  1.00 50.95  ? 508  GLN C NE2 1 
ATOM   12318 N  N   . GLN C  1 509 ? -43.625 0.801   77.864  1.00 34.06  ? 509  GLN C N   1 
ATOM   12319 C  CA  . GLN C  1 509 ? -44.360 1.880   78.516  1.00 35.56  ? 509  GLN C CA  1 
ATOM   12320 C  C   . GLN C  1 509 ? -43.503 2.756   79.436  1.00 37.25  ? 509  GLN C C   1 
ATOM   12321 O  O   . GLN C  1 509 ? -42.777 2.248   80.282  1.00 42.21  ? 509  GLN C O   1 
ATOM   12322 C  CB  . GLN C  1 509 ? -45.534 1.293   79.302  1.00 42.24  ? 509  GLN C CB  1 
ATOM   12323 C  CG  . GLN C  1 509 ? -46.556 0.565   78.438  1.00 46.40  ? 509  GLN C CG  1 
ATOM   12324 C  CD  . GLN C  1 509 ? -47.625 -0.149  79.251  1.00 49.46  ? 509  GLN C CD  1 
ATOM   12325 O  OE1 . GLN C  1 509 ? -47.315 -0.905  80.170  1.00 51.06  ? 509  GLN C OE1 1 
ATOM   12326 N  NE2 . GLN C  1 509 ? -48.893 0.087   78.910  1.00 50.01  ? 509  GLN C NE2 1 
ATOM   12327 N  N   . TYR C  1 510 ? -43.582 4.072   79.272  1.00 29.10  ? 510  TYR C N   1 
ATOM   12328 C  CA  . TYR C  1 510 ? -43.043 5.003   80.266  1.00 25.65  ? 510  TYR C CA  1 
ATOM   12329 C  C   . TYR C  1 510 ? -44.170 5.922   80.723  1.00 27.34  ? 510  TYR C C   1 
ATOM   12330 O  O   . TYR C  1 510 ? -45.278 5.841   80.201  1.00 28.09  ? 510  TYR C O   1 
ATOM   12331 C  CB  . TYR C  1 510 ? -41.887 5.821   79.698  1.00 28.75  ? 510  TYR C CB  1 
ATOM   12332 C  CG  . TYR C  1 510 ? -42.239 6.668   78.489  1.00 30.27  ? 510  TYR C CG  1 
ATOM   12333 C  CD1 . TYR C  1 510 ? -42.511 6.083   77.257  1.00 32.37  ? 510  TYR C CD1 1 
ATOM   12334 C  CD2 . TYR C  1 510 ? -42.269 8.055   78.570  1.00 31.49  ? 510  TYR C CD2 1 
ATOM   12335 C  CE1 . TYR C  1 510 ? -42.830 6.851   76.149  1.00 36.05  ? 510  TYR C CE1 1 
ATOM   12336 C  CE2 . TYR C  1 510 ? -42.579 8.837   77.458  1.00 34.06  ? 510  TYR C CE2 1 
ATOM   12337 C  CZ  . TYR C  1 510 ? -42.858 8.227   76.256  1.00 38.13  ? 510  TYR C CZ  1 
ATOM   12338 O  OH  . TYR C  1 510 ? -43.181 8.989   75.156  1.00 42.21  ? 510  TYR C OH  1 
ATOM   12339 N  N   . VAL C  1 511 ? -43.906 6.797   81.689  1.00 31.87  ? 511  VAL C N   1 
ATOM   12340 C  CA  . VAL C  1 511 ? -44.953 7.701   82.177  1.00 32.07  ? 511  VAL C CA  1 
ATOM   12341 C  C   . VAL C  1 511 ? -44.476 9.134   82.077  1.00 32.17  ? 511  VAL C C   1 
ATOM   12342 O  O   . VAL C  1 511 ? -43.276 9.392   82.096  1.00 31.55  ? 511  VAL C O   1 
ATOM   12343 C  CB  . VAL C  1 511 ? -45.383 7.405   83.646  1.00 26.99  ? 511  VAL C CB  1 
ATOM   12344 C  CG1 . VAL C  1 511 ? -45.887 5.987   83.789  1.00 27.70  ? 511  VAL C CG1 1 
ATOM   12345 C  CG2 . VAL C  1 511 ? -44.242 7.645   84.607  1.00 25.72  ? 511  VAL C CG2 1 
ATOM   12346 N  N   . SER C  1 512 ? -45.410 10.064  81.947  1.00 27.06  ? 512  SER C N   1 
ATOM   12347 C  CA  . SER C  1 512 ? -45.060 11.470  82.026  1.00 26.94  ? 512  SER C CA  1 
ATOM   12348 C  C   . SER C  1 512 ? -45.101 11.934  83.494  1.00 26.52  ? 512  SER C C   1 
ATOM   12349 O  O   . SER C  1 512 ? -46.096 11.728  84.200  1.00 27.44  ? 512  SER C O   1 
ATOM   12350 C  CB  . SER C  1 512 ? -45.992 12.321  81.149  1.00 57.35  ? 512  SER C CB  1 
ATOM   12351 O  OG  . SER C  1 512 ? -47.362 12.220  81.538  1.00 64.41  ? 512  SER C OG  1 
ATOM   12352 N  N   . LEU C  1 513 ? -44.016 12.536  83.971  1.00 43.34  ? 513  LEU C N   1 
ATOM   12353 C  CA  . LEU C  1 513 ? -44.042 13.157  85.283  1.00 40.44  ? 513  LEU C CA  1 
ATOM   12354 C  C   . LEU C  1 513 ? -44.194 14.638  85.034  1.00 40.84  ? 513  LEU C C   1 
ATOM   12355 O  O   . LEU C  1 513 ? -43.249 15.318  84.626  1.00 42.35  ? 513  LEU C O   1 
ATOM   12356 C  CB  . LEU C  1 513 ? -42.754 12.867  86.049  1.00 27.15  ? 513  LEU C CB  1 
ATOM   12357 C  CG  . LEU C  1 513 ? -42.458 11.386  86.296  1.00 28.04  ? 513  LEU C CG  1 
ATOM   12358 C  CD1 . LEU C  1 513 ? -41.093 11.184  86.926  1.00 27.50  ? 513  LEU C CD1 1 
ATOM   12359 C  CD2 . LEU C  1 513 ? -43.526 10.777  87.179  1.00 29.90  ? 513  LEU C CD2 1 
ATOM   12360 N  N   . ASN C  1 514 ? -45.401 15.125  85.292  1.00 33.90  ? 514  ASN C N   1 
ATOM   12361 C  CA  . ASN C  1 514 ? -45.777 16.513  85.057  1.00 35.08  ? 514  ASN C CA  1 
ATOM   12362 C  C   . ASN C  1 514 ? -46.777 16.900  86.130  1.00 34.38  ? 514  ASN C C   1 
ATOM   12363 O  O   . ASN C  1 514 ? -46.919 16.179  87.125  1.00 32.12  ? 514  ASN C O   1 
ATOM   12364 C  CB  . ASN C  1 514 ? -46.332 16.726  83.639  1.00 46.21  ? 514  ASN C CB  1 
ATOM   12365 C  CG  . ASN C  1 514 ? -47.474 15.778  83.296  1.00 54.20  ? 514  ASN C CG  1 
ATOM   12366 O  OD1 . ASN C  1 514 ? -48.344 15.512  84.118  1.00 56.05  ? 514  ASN C OD1 1 
ATOM   12367 N  ND2 . ASN C  1 514 ? -47.475 15.269  82.066  1.00 58.48  ? 514  ASN C ND2 1 
ATOM   12368 N  N   . LEU C  1 515 ? -47.452 18.032  85.967  1.00 40.17  ? 515  LEU C N   1 
ATOM   12369 C  CA  . LEU C  1 515 ? -48.441 18.420  86.971  1.00 40.86  ? 515  LEU C CA  1 
ATOM   12370 C  C   . LEU C  1 515 ? -49.685 17.534  86.956  1.00 44.82  ? 515  LEU C C   1 
ATOM   12371 O  O   . LEU C  1 515 ? -50.108 17.067  88.005  1.00 43.72  ? 515  LEU C O   1 
ATOM   12372 C  CB  . LEU C  1 515 ? -48.797 19.902  86.890  1.00 34.02  ? 515  LEU C CB  1 
ATOM   12373 C  CG  . LEU C  1 515 ? -47.682 20.853  87.344  1.00 32.93  ? 515  LEU C CG  1 
ATOM   12374 C  CD1 . LEU C  1 515 ? -48.266 22.159  87.877  1.00 34.20  ? 515  LEU C CD1 1 
ATOM   12375 C  CD2 . LEU C  1 515 ? -46.776 20.211  88.384  1.00 32.32  ? 515  LEU C CD2 1 
ATOM   12376 N  N   . LYS C  1 516 ? -50.241 17.268  85.774  1.00 59.33  ? 516  LYS C N   1 
ATOM   12377 C  CA  . LYS C  1 516 ? -51.408 16.383  85.648  1.00 63.16  ? 516  LYS C CA  1 
ATOM   12378 C  C   . LYS C  1 516 ? -51.011 14.968  86.080  1.00 64.33  ? 516  LYS C C   1 
ATOM   12379 O  O   . LYS C  1 516 ? -49.823 14.680  86.236  1.00 65.58  ? 516  LYS C O   1 
ATOM   12380 C  CB  . LYS C  1 516 ? -51.939 16.381  84.206  1.00 53.72  ? 516  LYS C CB  1 
ATOM   12381 C  CG  . LYS C  1 516 ? -52.642 17.663  83.774  1.00 55.49  ? 516  LYS C CG  1 
ATOM   12382 C  CD  . LYS C  1 516 ? -53.077 17.613  82.296  1.00 58.12  ? 516  LYS C CD  1 
ATOM   12383 C  CE  . LYS C  1 516 ? -51.889 17.609  81.314  1.00 56.00  ? 516  LYS C CE  1 
ATOM   12384 N  NZ  . LYS C  1 516 ? -52.287 17.457  79.864  1.00 55.55  ? 516  LYS C NZ  1 
ATOM   12385 N  N   . PRO C  1 517 ? -51.993 14.079  86.306  1.00 56.85  ? 517  PRO C N   1 
ATOM   12386 C  CA  . PRO C  1 517 ? -51.585 12.778  86.846  1.00 55.81  ? 517  PRO C CA  1 
ATOM   12387 C  C   . PRO C  1 517 ? -50.893 11.920  85.808  1.00 57.90  ? 517  PRO C C   1 
ATOM   12388 O  O   . PRO C  1 517 ? -50.784 12.323  84.652  1.00 58.72  ? 517  PRO C O   1 
ATOM   12389 C  CB  . PRO C  1 517 ? -52.908 12.132  87.251  1.00 35.70  ? 517  PRO C CB  1 
ATOM   12390 C  CG  . PRO C  1 517 ? -53.884 13.257  87.303  1.00 36.40  ? 517  PRO C CG  1 
ATOM   12391 C  CD  . PRO C  1 517 ? -53.452 14.201  86.242  1.00 36.56  ? 517  PRO C CD  1 
ATOM   12392 N  N   . LEU C  1 518 ? -50.437 10.746  86.225  1.00 55.87  ? 518  LEU C N   1 
ATOM   12393 C  CA  . LEU C  1 518 ? -49.635 9.905   85.353  1.00 52.93  ? 518  LEU C CA  1 
ATOM   12394 C  C   . LEU C  1 518 ? -50.392 9.554   84.102  1.00 54.98  ? 518  LEU C C   1 
ATOM   12395 O  O   . LEU C  1 518 ? -51.574 9.191   84.149  1.00 57.55  ? 518  LEU C O   1 
ATOM   12396 C  CB  . LEU C  1 518 ? -49.197 8.621   86.047  1.00 38.03  ? 518  LEU C CB  1 
ATOM   12397 C  CG  . LEU C  1 518 ? -48.084 8.737   87.075  1.00 34.86  ? 518  LEU C CG  1 
ATOM   12398 C  CD1 . LEU C  1 518 ? -47.668 7.350   87.523  1.00 33.34  ? 518  LEU C CD1 1 
ATOM   12399 C  CD2 . LEU C  1 518 ? -46.921 9.500   86.475  1.00 34.62  ? 518  LEU C CD2 1 
ATOM   12400 N  N   . GLU C  1 519 ? -49.691 9.692   82.984  1.00 45.83  ? 519  GLU C N   1 
ATOM   12401 C  CA  . GLU C  1 519 ? -50.189 9.291   81.688  1.00 46.43  ? 519  GLU C CA  1 
ATOM   12402 C  C   . GLU C  1 519 ? -49.261 8.194   81.239  1.00 40.60  ? 519  GLU C C   1 
ATOM   12403 O  O   . GLU C  1 519 ? -48.058 8.332   81.406  1.00 41.13  ? 519  GLU C O   1 
ATOM   12404 C  CB  . GLU C  1 519 ? -50.092 10.469  80.735  1.00 58.25  ? 519  GLU C CB  1 
ATOM   12405 C  CG  . GLU C  1 519 ? -50.389 10.124  79.311  1.00 68.94  ? 519  GLU C CG  1 
ATOM   12406 C  CD  . GLU C  1 519 ? -50.199 11.314  78.418  1.00 79.17  ? 519  GLU C CD  1 
ATOM   12407 O  OE1 . GLU C  1 519 ? -50.480 12.441  78.889  1.00 81.50  ? 519  GLU C OE1 1 
ATOM   12408 O  OE2 . GLU C  1 519 ? -49.747 11.126  77.264  1.00 83.23  ? 519  GLU C OE2 1 
ATOM   12409 N  N   . VAL C  1 520 ? -49.783 7.091   80.714  1.00 32.33  ? 520  VAL C N   1 
ATOM   12410 C  CA  . VAL C  1 520 ? -48.876 6.067   80.201  1.00 33.34  ? 520  VAL C CA  1 
ATOM   12411 C  C   . VAL C  1 520 ? -48.648 6.205   78.702  1.00 37.03  ? 520  VAL C C   1 
ATOM   12412 O  O   . VAL C  1 520 ? -49.594 6.258   77.919  1.00 39.35  ? 520  VAL C O   1 
ATOM   12413 C  CB  . VAL C  1 520 ? -49.313 4.640   80.531  1.00 32.26  ? 520  VAL C CB  1 
ATOM   12414 C  CG1 . VAL C  1 520 ? -48.404 3.642   79.834  1.00 31.61  ? 520  VAL C CG1 1 
ATOM   12415 C  CG2 . VAL C  1 520 ? -49.259 4.418   82.007  1.00 31.97  ? 520  VAL C CG2 1 
ATOM   12416 N  N   . ARG C  1 521 ? -47.379 6.266   78.314  1.00 47.10  ? 521  ARG C N   1 
ATOM   12417 C  CA  . ARG C  1 521 ? -47.004 6.423   76.920  1.00 47.61  ? 521  ARG C CA  1 
ATOM   12418 C  C   . ARG C  1 521 ? -46.221 5.218   76.433  1.00 48.67  ? 521  ARG C C   1 
ATOM   12419 O  O   . ARG C  1 521 ? -45.525 4.569   77.209  1.00 48.65  ? 521  ARG C O   1 
ATOM   12420 C  CB  . ARG C  1 521 ? -46.190 7.694   76.749  1.00 38.20  ? 521  ARG C CB  1 
ATOM   12421 C  CG  . ARG C  1 521 ? -46.906 8.902   77.279  1.00 37.67  ? 521  ARG C CG  1 
ATOM   12422 C  CD  . ARG C  1 521 ? -46.155 10.170  76.974  1.00 39.88  ? 521  ARG C CD  1 
ATOM   12423 N  NE  . ARG C  1 521 ? -46.894 11.317  77.487  1.00 44.31  ? 521  ARG C NE  1 
ATOM   12424 C  CZ  . ARG C  1 521 ? -46.348 12.497  77.757  1.00 47.11  ? 521  ARG C CZ  1 
ATOM   12425 N  NH1 . ARG C  1 521 ? -45.046 12.682  77.554  1.00 49.98  ? 521  ARG C NH1 1 
ATOM   12426 N  NH2 . ARG C  1 521 ? -47.101 13.488  78.233  1.00 46.09  ? 521  ARG C NH2 1 
ATOM   12427 N  N   . ARG C  1 522 ? -46.356 4.913   75.147  1.00 41.74  ? 522  ARG C N   1 
ATOM   12428 C  CA  . ARG C  1 522 ? -45.653 3.792   74.548  1.00 44.81  ? 522  ARG C CA  1 
ATOM   12429 C  C   . ARG C  1 522 ? -44.610 4.394   73.642  1.00 43.73  ? 522  ARG C C   1 
ATOM   12430 O  O   . ARG C  1 522 ? -44.839 5.471   73.097  1.00 44.46  ? 522  ARG C O   1 
ATOM   12431 C  CB  . ARG C  1 522 ? -46.620 2.918   73.744  1.00 66.84  ? 522  ARG C CB  1 
ATOM   12432 C  CG  . ARG C  1 522 ? -47.535 2.031   74.599  1.00 74.92  ? 522  ARG C CG  1 
ATOM   12433 C  CD  . ARG C  1 522 ? -49.029 2.275   74.336  1.00 84.12  ? 522  ARG C CD  1 
ATOM   12434 N  NE  . ARG C  1 522 ? -49.525 3.540   74.893  1.00 91.59  ? 522  ARG C NE  1 
ATOM   12435 C  CZ  . ARG C  1 522 ? -50.047 4.537   74.174  1.00 96.62  ? 522  ARG C CZ  1 
ATOM   12436 N  NH1 . ARG C  1 522 ? -50.155 4.437   72.853  1.00 99.26  ? 522  ARG C NH1 1 
ATOM   12437 N  NH2 . ARG C  1 522 ? -50.466 5.643   74.777  1.00 96.39  ? 522  ARG C NH2 1 
ATOM   12438 N  N   . GLY C  1 523 ? -43.475 3.714   73.476  1.00 53.23  ? 523  GLY C N   1 
ATOM   12439 C  CA  . GLY C  1 523 ? -42.458 4.179   72.548  1.00 54.09  ? 523  GLY C CA  1 
ATOM   12440 C  C   . GLY C  1 523 ? -41.636 5.417   72.873  1.00 54.45  ? 523  GLY C C   1 
ATOM   12441 O  O   . GLY C  1 523 ? -41.758 6.444   72.197  1.00 57.54  ? 523  GLY C O   1 
ATOM   12442 N  N   . LEU C  1 524 ? -40.820 5.356   73.917  1.00 45.98  ? 524  LEU C N   1 
ATOM   12443 C  CA  . LEU C  1 524 ? -40.045 6.534   74.293  1.00 44.49  ? 524  LEU C CA  1 
ATOM   12444 C  C   . LEU C  1 524 ? -39.037 6.836   73.179  1.00 46.36  ? 524  LEU C C   1 
ATOM   12445 O  O   . LEU C  1 524 ? -38.046 6.113   73.023  1.00 44.80  ? 524  LEU C O   1 
ATOM   12446 C  CB  . LEU C  1 524 ? -39.297 6.168   75.585  1.00 29.68  ? 524  LEU C CB  1 
ATOM   12447 C  CG  . LEU C  1 524 ? -38.497 7.093   76.503  1.00 26.40  ? 524  LEU C CG  1 
ATOM   12448 C  CD1 . LEU C  1 524 ? -36.998 6.775   76.437  1.00 21.28  ? 524  LEU C CD1 1 
ATOM   12449 C  CD2 . LEU C  1 524 ? -38.787 8.550   76.174  1.00 26.47  ? 524  LEU C CD2 1 
ATOM   12450 N  N   . ARG C  1 525 ? -39.268 7.947   72.465  1.00 51.14  ? 525  ARG C N   1 
ATOM   12451 C  CA  . ARG C  1 525 ? -38.495 8.328   71.259  1.00 54.38  ? 525  ARG C CA  1 
ATOM   12452 C  C   . ARG C  1 525 ? -38.077 7.124   70.388  1.00 52.97  ? 525  ARG C C   1 
ATOM   12453 O  O   . ARG C  1 525 ? -36.882 6.846   70.244  1.00 52.15  ? 525  ARG C O   1 
ATOM   12454 C  CB  . ARG C  1 525 ? -37.291 9.225   71.587  1.00 66.55  ? 525  ARG C CB  1 
ATOM   12455 C  CG  . ARG C  1 525 ? -37.628 10.704  71.848  1.00 72.53  ? 525  ARG C CG  1 
ATOM   12456 C  CD  . ARG C  1 525 ? -38.141 11.406  70.602  1.00 80.30  ? 525  ARG C CD  1 
ATOM   12457 N  NE  . ARG C  1 525 ? -37.249 12.468  70.127  1.00 86.36  ? 525  ARG C NE  1 
ATOM   12458 C  CZ  . ARG C  1 525 ? -37.281 12.979  68.892  1.00 91.95  ? 525  ARG C CZ  1 
ATOM   12459 N  NH1 . ARG C  1 525 ? -38.151 12.525  67.996  1.00 94.59  ? 525  ARG C NH1 1 
ATOM   12460 N  NH2 . ARG C  1 525 ? -36.439 13.943  68.542  1.00 92.55  ? 525  ARG C NH2 1 
ATOM   12461 N  N   . ALA C  1 526 ? -39.061 6.432   69.807  1.00 44.53  ? 526  ALA C N   1 
ATOM   12462 C  CA  . ALA C  1 526 ? -38.857 5.078   69.265  1.00 37.40  ? 526  ALA C CA  1 
ATOM   12463 C  C   . ALA C  1 526 ? -38.122 4.976   67.930  1.00 34.60  ? 526  ALA C C   1 
ATOM   12464 O  O   . ALA C  1 526 ? -37.163 4.201   67.789  1.00 32.22  ? 526  ALA C O   1 
ATOM   12465 C  CB  . ALA C  1 526 ? -40.186 4.356   69.181  1.00 28.69  ? 526  ALA C CB  1 
ATOM   12466 N  N   . GLN C  1 527 ? -38.586 5.756   66.957  1.00 36.34  ? 527  GLN C N   1 
ATOM   12467 C  CA  . GLN C  1 527 ? -38.091 5.674   65.592  1.00 38.88  ? 527  GLN C CA  1 
ATOM   12468 C  C   . GLN C  1 527 ? -36.766 6.378   65.530  1.00 36.49  ? 527  GLN C C   1 
ATOM   12469 O  O   . GLN C  1 527 ? -35.808 5.902   64.898  1.00 38.52  ? 527  GLN C O   1 
ATOM   12470 C  CB  . GLN C  1 527 ? -39.059 6.370   64.644  1.00 61.33  ? 527  GLN C CB  1 
ATOM   12471 C  CG  . GLN C  1 527 ? -40.521 6.212   65.026  1.00 68.17  ? 527  GLN C CG  1 
ATOM   12472 C  CD  . GLN C  1 527 ? -41.089 4.864   64.631  1.00 72.99  ? 527  GLN C CD  1 
ATOM   12473 O  OE1 . GLN C  1 527 ? -40.557 4.191   63.746  1.00 73.68  ? 527  GLN C OE1 1 
ATOM   12474 N  NE2 . GLN C  1 527 ? -42.175 4.461   65.289  1.00 75.65  ? 527  GLN C NE2 1 
ATOM   12475 N  N   . THR C  1 528 ? -36.721 7.524   66.201  1.00 33.77  ? 528  THR C N   1 
ATOM   12476 C  CA  . THR C  1 528 ? -35.529 8.353   66.222  1.00 30.94  ? 528  THR C CA  1 
ATOM   12477 C  C   . THR C  1 528 ? -34.377 7.579   66.852  1.00 29.50  ? 528  THR C C   1 
ATOM   12478 O  O   . THR C  1 528 ? -33.230 7.611   66.369  1.00 30.04  ? 528  THR C O   1 
ATOM   12479 C  CB  . THR C  1 528 ? -35.791 9.680   66.945  1.00 29.89  ? 528  THR C CB  1 
ATOM   12480 O  OG1 . THR C  1 528 ? -36.518 10.557  66.073  1.00 29.53  ? 528  THR C OG1 1 
ATOM   12481 C  CG2 . THR C  1 528 ? -34.484 10.344  67.323  1.00 31.41  ? 528  THR C CG2 1 
ATOM   12482 N  N   . CYS C  1 529 ? -34.691 6.840   67.909  1.00 23.31  ? 529  CYS C N   1 
ATOM   12483 C  CA  . CYS C  1 529 ? -33.677 6.012   68.543  1.00 23.18  ? 529  CYS C CA  1 
ATOM   12484 C  C   . CYS C  1 529 ? -33.348 4.766   67.733  1.00 23.75  ? 529  CYS C C   1 
ATOM   12485 O  O   . CYS C  1 529 ? -32.257 4.226   67.854  1.00 22.20  ? 529  CYS C O   1 
ATOM   12486 C  CB  . CYS C  1 529 ? -34.056 5.671   69.983  1.00 21.96  ? 529  CYS C CB  1 
ATOM   12487 S  SG  . CYS C  1 529 ? -33.739 7.054   71.094  1.00 64.19  ? 529  CYS C SG  1 
ATOM   12488 N  N   . ALA C  1 530 ? -34.283 4.296   66.914  1.00 30.90  ? 530  ALA C N   1 
ATOM   12489 C  CA  . ALA C  1 530 ? -33.922 3.219   66.004  1.00 29.58  ? 530  ALA C CA  1 
ATOM   12490 C  C   . ALA C  1 530 ? -32.801 3.742   65.129  1.00 28.70  ? 530  ALA C C   1 
ATOM   12491 O  O   . ALA C  1 530 ? -31.810 3.053   64.923  1.00 29.07  ? 530  ALA C O   1 
ATOM   12492 C  CB  . ALA C  1 530 ? -35.100 2.772   65.173  1.00 25.85  ? 530  ALA C CB  1 
ATOM   12493 N  N   . PHE C  1 531 ? -32.947 4.977   64.653  1.00 30.61  ? 531  PHE C N   1 
ATOM   12494 C  CA  . PHE C  1 531 ? -31.879 5.643   63.896  1.00 31.64  ? 531  PHE C CA  1 
ATOM   12495 C  C   . PHE C  1 531 ? -30.561 5.660   64.674  1.00 30.17  ? 531  PHE C C   1 
ATOM   12496 O  O   . PHE C  1 531 ? -29.571 4.997   64.296  1.00 29.24  ? 531  PHE C O   1 
ATOM   12497 C  CB  . PHE C  1 531 ? -32.305 7.076   63.545  1.00 24.35  ? 531  PHE C CB  1 
ATOM   12498 C  CG  . PHE C  1 531 ? -31.212 7.927   62.943  1.00 26.44  ? 531  PHE C CG  1 
ATOM   12499 C  CD1 . PHE C  1 531 ? -30.851 7.785   61.610  1.00 28.02  ? 531  PHE C CD1 1 
ATOM   12500 C  CD2 . PHE C  1 531 ? -30.578 8.905   63.696  1.00 23.17  ? 531  PHE C CD2 1 
ATOM   12501 C  CE1 . PHE C  1 531 ? -29.869 8.578   61.049  1.00 24.63  ? 531  PHE C CE1 1 
ATOM   12502 C  CE2 . PHE C  1 531 ? -29.590 9.702   63.138  1.00 23.03  ? 531  PHE C CE2 1 
ATOM   12503 C  CZ  . PHE C  1 531 ? -29.239 9.534   61.815  1.00 23.76  ? 531  PHE C CZ  1 
ATOM   12504 N  N   . TRP C  1 532 ? -30.574 6.404   65.776  1.00 28.85  ? 532  TRP C N   1 
ATOM   12505 C  CA  . TRP C  1 532 ? -29.371 6.634   66.575  1.00 26.02  ? 532  TRP C CA  1 
ATOM   12506 C  C   . TRP C  1 532 ? -28.663 5.364   67.067  1.00 25.04  ? 532  TRP C C   1 
ATOM   12507 O  O   . TRP C  1 532 ? -27.446 5.240   66.935  1.00 25.66  ? 532  TRP C O   1 
ATOM   12508 C  CB  . TRP C  1 532 ? -29.686 7.562   67.757  1.00 20.40  ? 532  TRP C CB  1 
ATOM   12509 C  CG  . TRP C  1 532 ? -29.808 9.015   67.382  1.00 20.58  ? 532  TRP C CG  1 
ATOM   12510 C  CD1 . TRP C  1 532 ? -30.955 9.754   67.300  1.00 23.96  ? 532  TRP C CD1 1 
ATOM   12511 C  CD2 . TRP C  1 532 ? -28.738 9.898   67.043  1.00 20.25  ? 532  TRP C CD2 1 
ATOM   12512 N  NE1 . TRP C  1 532 ? -30.663 11.041  66.927  1.00 21.26  ? 532  TRP C NE1 1 
ATOM   12513 C  CE2 . TRP C  1 532 ? -29.308 11.156  66.763  1.00 20.69  ? 532  TRP C CE2 1 
ATOM   12514 C  CE3 . TRP C  1 532 ? -27.349 9.746   66.943  1.00 19.71  ? 532  TRP C CE3 1 
ATOM   12515 C  CZ2 . TRP C  1 532 ? -28.541 12.255  66.395  1.00 20.62  ? 532  TRP C CZ2 1 
ATOM   12516 C  CZ3 . TRP C  1 532 ? -26.589 10.835  66.573  1.00 19.64  ? 532  TRP C CZ3 1 
ATOM   12517 C  CH2 . TRP C  1 532 ? -27.185 12.076  66.301  1.00 20.09  ? 532  TRP C CH2 1 
ATOM   12518 N  N   . ASN C  1 533 ? -29.427 4.444   67.648  1.00 21.31  ? 533  ASN C N   1 
ATOM   12519 C  CA  . ASN C  1 533 ? -28.886 3.218   68.236  1.00 24.30  ? 533  ASN C CA  1 
ATOM   12520 C  C   . ASN C  1 533 ? -28.594 2.085   67.245  1.00 26.37  ? 533  ASN C C   1 
ATOM   12521 O  O   . ASN C  1 533 ? -27.620 1.351   67.398  1.00 27.61  ? 533  ASN C O   1 
ATOM   12522 C  CB  . ASN C  1 533 ? -29.821 2.683   69.324  1.00 33.41  ? 533  ASN C CB  1 
ATOM   12523 C  CG  . ASN C  1 533 ? -30.138 3.709   70.385  1.00 35.26  ? 533  ASN C CG  1 
ATOM   12524 O  OD1 . ASN C  1 533 ? -29.373 4.651   70.616  1.00 36.16  ? 533  ASN C OD1 1 
ATOM   12525 N  ND2 . ASN C  1 533 ? -31.276 3.525   71.052  1.00 35.23  ? 533  ASN C ND2 1 
ATOM   12526 N  N   . ARG C  1 534 ? -29.465 1.913   66.259  1.00 24.27  ? 534  ARG C N   1 
ATOM   12527 C  CA  . ARG C  1 534 ? -29.303 0.822   65.308  1.00 27.71  ? 534  ARG C CA  1 
ATOM   12528 C  C   . ARG C  1 534 ? -28.578 1.235   64.022  1.00 25.36  ? 534  ARG C C   1 
ATOM   12529 O  O   . ARG C  1 534 ? -27.560 0.645   63.682  1.00 24.74  ? 534  ARG C O   1 
ATOM   12530 C  CB  . ARG C  1 534 ? -30.637 0.146   65.006  1.00 55.66  ? 534  ARG C CB  1 
ATOM   12531 C  CG  . ARG C  1 534 ? -31.191 -0.632  66.170  1.00 64.59  ? 534  ARG C CG  1 
ATOM   12532 C  CD  . ARG C  1 534 ? -32.699 -0.487  66.212  1.00 74.30  ? 534  ARG C CD  1 
ATOM   12533 N  NE  . ARG C  1 534 ? -33.390 -1.772  66.144  1.00 81.24  ? 534  ARG C NE  1 
ATOM   12534 C  CZ  . ARG C  1 534 ? -33.914 -2.401  67.193  1.00 84.15  ? 534  ARG C CZ  1 
ATOM   12535 N  NH1 . ARG C  1 534 ? -33.828 -1.862  68.407  1.00 82.60  ? 534  ARG C NH1 1 
ATOM   12536 N  NH2 . ARG C  1 534 ? -34.532 -3.567  67.025  1.00 86.39  ? 534  ARG C NH2 1 
ATOM   12537 N  N   . PHE C  1 535 ? -29.115 2.205   63.286  1.00 26.11  ? 535  PHE C N   1 
ATOM   12538 C  CA  . PHE C  1 535 ? -28.563 2.532   61.966  1.00 24.46  ? 535  PHE C CA  1 
ATOM   12539 C  C   . PHE C  1 535 ? -27.275 3.343   62.004  1.00 23.48  ? 535  PHE C C   1 
ATOM   12540 O  O   . PHE C  1 535 ? -26.240 2.892   61.516  1.00 23.52  ? 535  PHE C O   1 
ATOM   12541 C  CB  . PHE C  1 535 ? -29.582 3.265   61.104  1.00 28.44  ? 535  PHE C CB  1 
ATOM   12542 C  CG  . PHE C  1 535 ? -29.037 3.698   59.772  1.00 30.90  ? 535  PHE C CG  1 
ATOM   12543 C  CD1 . PHE C  1 535 ? -28.923 2.793   58.727  1.00 32.61  ? 535  PHE C CD1 1 
ATOM   12544 C  CD2 . PHE C  1 535 ? -28.636 5.006   59.561  1.00 31.48  ? 535  PHE C CD2 1 
ATOM   12545 C  CE1 . PHE C  1 535 ? -28.424 3.182   57.493  1.00 31.76  ? 535  PHE C CE1 1 
ATOM   12546 C  CE2 . PHE C  1 535 ? -28.135 5.396   58.330  1.00 32.41  ? 535  PHE C CE2 1 
ATOM   12547 C  CZ  . PHE C  1 535 ? -28.032 4.481   57.298  1.00 31.65  ? 535  PHE C CZ  1 
ATOM   12548 N  N   . LEU C  1 536 ? -27.368 4.549   62.565  1.00 22.89  ? 536  LEU C N   1 
ATOM   12549 C  CA  . LEU C  1 536 ? -26.273 5.521   62.571  1.00 22.30  ? 536  LEU C CA  1 
ATOM   12550 C  C   . LEU C  1 536 ? -24.876 4.931   62.892  1.00 33.97  ? 536  LEU C C   1 
ATOM   12551 O  O   . LEU C  1 536 ? -23.882 5.326   62.277  1.00 21.73  ? 536  LEU C O   1 
ATOM   12552 C  CB  . LEU C  1 536 ? -26.624 6.716   63.477  1.00 29.55  ? 536  LEU C CB  1 
ATOM   12553 C  CG  . LEU C  1 536 ? -25.959 8.079   63.216  1.00 33.85  ? 536  LEU C CG  1 
ATOM   12554 C  CD1 . LEU C  1 536 ? -24.672 8.289   64.021  1.00 34.51  ? 536  LEU C CD1 1 
ATOM   12555 C  CD2 . LEU C  1 536 ? -25.681 8.261   61.726  1.00 37.00  ? 536  LEU C CD2 1 
ATOM   12556 N  N   . PRO C  1 537 ? -24.794 3.991   63.855  1.00 42.03  ? 537  PRO C N   1 
ATOM   12557 C  CA  . PRO C  1 537 ? -23.550 3.240   64.039  1.00 41.42  ? 537  PRO C CA  1 
ATOM   12558 C  C   . PRO C  1 537 ? -23.043 2.533   62.789  1.00 44.35  ? 537  PRO C C   1 
ATOM   12559 O  O   . PRO C  1 537 ? -21.859 2.672   62.491  1.00 48.77  ? 537  PRO C O   1 
ATOM   12560 C  CB  . PRO C  1 537 ? -23.931 2.184   65.081  1.00 31.23  ? 537  PRO C CB  1 
ATOM   12561 C  CG  . PRO C  1 537 ? -25.405 2.332   65.301  1.00 32.35  ? 537  PRO C CG  1 
ATOM   12562 C  CD  . PRO C  1 537 ? -25.711 3.739   64.973  1.00 32.01  ? 537  PRO C CD  1 
ATOM   12563 N  N   . LYS C  1 538 ? -23.899 1.810   62.070  1.00 37.58  ? 538  LYS C N   1 
ATOM   12564 C  CA  . LYS C  1 538 ? -23.461 1.111   60.855  1.00 38.55  ? 538  LYS C CA  1 
ATOM   12565 C  C   . LYS C  1 538 ? -22.986 2.090   59.766  1.00 41.93  ? 538  LYS C C   1 
ATOM   12566 O  O   . LYS C  1 538 ? -22.242 1.726   58.850  1.00 42.14  ? 538  LYS C O   1 
ATOM   12567 C  CB  . LYS C  1 538 ? -24.574 0.206   60.310  1.00 35.53  ? 538  LYS C CB  1 
ATOM   12568 C  CG  . LYS C  1 538 ? -25.119 -0.786  61.328  1.00 37.23  ? 538  LYS C CG  1 
ATOM   12569 C  CD  . LYS C  1 538 ? -25.890 -1.915  60.667  1.00 42.55  ? 538  LYS C CD  1 
ATOM   12570 C  CE  . LYS C  1 538 ? -24.953 -2.886  59.938  1.00 49.58  ? 538  LYS C CE  1 
ATOM   12571 N  NZ  . LYS C  1 538 ? -25.456 -3.353  58.589  1.00 53.98  ? 538  LYS C NZ  1 
ATOM   12572 N  N   . LEU C  1 539 ? -23.433 3.335   59.874  1.00 48.46  ? 539  LEU C N   1 
ATOM   12573 C  CA  . LEU C  1 539 ? -23.134 4.349   58.878  1.00 50.15  ? 539  LEU C CA  1 
ATOM   12574 C  C   . LEU C  1 539 ? -21.751 4.964   59.025  1.00 59.82  ? 539  LEU C C   1 
ATOM   12575 O  O   . LEU C  1 539 ? -21.040 5.127   58.039  1.00 64.86  ? 539  LEU C O   1 
ATOM   12576 C  CB  . LEU C  1 539 ? -24.183 5.445   58.925  1.00 27.95  ? 539  LEU C CB  1 
ATOM   12577 C  CG  . LEU C  1 539 ? -24.107 6.343   57.706  1.00 26.88  ? 539  LEU C CG  1 
ATOM   12578 C  CD1 . LEU C  1 539 ? -24.420 5.535   56.474  1.00 26.24  ? 539  LEU C CD1 1 
ATOM   12579 C  CD2 . LEU C  1 539 ? -25.066 7.491   57.870  1.00 27.77  ? 539  LEU C CD2 1 
ATOM   12580 N  N   . LEU C  1 540 ? -21.379 5.336   60.247  1.00 69.30  ? 540  LEU C N   1 
ATOM   12581 C  CA  . LEU C  1 540 ? -20.033 5.854   60.487  1.00 74.58  ? 540  LEU C CA  1 
ATOM   12582 C  C   . LEU C  1 540 ? -19.095 4.681   60.738  1.00 81.71  ? 540  LEU C C   1 
ATOM   12583 O  O   . LEU C  1 540 ? -17.913 4.868   61.025  1.00 84.61  ? 540  LEU C O   1 
ATOM   12584 C  CB  . LEU C  1 540 ? -19.992 6.912   61.606  1.00 62.28  ? 540  LEU C CB  1 
ATOM   12585 C  CG  . LEU C  1 540 ? -20.800 6.684   62.889  1.00 58.37  ? 540  LEU C CG  1 
ATOM   12586 C  CD1 . LEU C  1 540 ? -20.138 5.599   63.734  1.00 58.81  ? 540  LEU C CD1 1 
ATOM   12587 C  CD2 . LEU C  1 540 ? -21.018 7.982   63.698  1.00 53.09  ? 540  LEU C CD2 1 
ATOM   12588 N  N   . SER C  1 541 ? -19.655 3.474   60.635  1.00 79.69  ? 541  SER C N   1 
ATOM   12589 C  CA  . SER C  1 541 ? -18.879 2.237   60.536  1.00 81.57  ? 541  SER C CA  1 
ATOM   12590 C  C   . SER C  1 541 ? -18.443 1.951   59.091  1.00 87.62  ? 541  SER C C   1 
ATOM   12591 O  O   . SER C  1 541 ? -17.760 0.963   58.834  1.00 90.24  ? 541  SER C O   1 
ATOM   12592 C  CB  . SER C  1 541 ? -19.663 1.045   61.093  1.00 70.26  ? 541  SER C CB  1 
ATOM   12593 O  OG  . SER C  1 541 ? -19.471 -0.119  60.302  1.00 69.11  ? 541  SER C OG  1 
ATOM   12594 N  N   . ALA C  1 542 ? -18.873 2.789   58.148  1.00 85.09  ? 542  ALA C N   1 
ATOM   12595 C  CA  . ALA C  1 542 ? -18.232 2.848   56.836  1.00 85.85  ? 542  ALA C CA  1 
ATOM   12596 C  C   . ALA C  1 542 ? -17.574 4.226   56.658  1.00 91.91  ? 542  ALA C C   1 
ATOM   12597 O  O   . ALA C  1 542 ? -18.252 5.227   56.392  1.00 89.27  ? 542  ALA C O   1 
ATOM   12598 C  CB  . ALA C  1 542 ? -19.246 2.575   55.728  1.00 67.22  ? 542  ALA C CB  1 
ATOM   12599 N  N   . THR C  1 543 ? -16.245 4.258   56.772  1.00 117.28 ? 543  THR C N   1 
ATOM   12600 C  CA  . THR C  1 543 ? -15.467 5.504   56.727  1.00 122.55 ? 543  THR C CA  1 
ATOM   12601 C  C   . THR C  1 543 ? -13.995 5.241   56.359  1.00 124.48 ? 543  THR C C   1 
ATOM   12602 O  O   . THR C  1 543 ? -13.641 5.073   55.187  1.00 125.31 ? 543  THR C O   1 
ATOM   12603 C  CB  . THR C  1 543 ? -15.521 6.286   58.078  1.00 138.68 ? 543  THR C CB  1 
ATOM   12604 O  OG1 . THR C  1 543 ? -16.876 6.397   58.535  1.00 137.68 ? 543  THR C OG1 1 
ATOM   12605 C  CG2 . THR C  1 543 ? -14.925 7.690   57.923  1.00 138.35 ? 543  THR C CG2 1 
ATOM   12606 O  OXT . THR C  1 543 ? -13.115 5.188   57.225  1.00 106.59 ? 543  THR C OXT 1 
ATOM   12607 N  N   . GLU D  1 4   ? -72.196 8.264   1.068   1.00 112.52 ? 4    GLU D N   1 
ATOM   12608 C  CA  . GLU D  1 4   ? -72.467 7.582   2.329   1.00 112.71 ? 4    GLU D CA  1 
ATOM   12609 C  C   . GLU D  1 4   ? -72.771 8.599   3.426   1.00 109.50 ? 4    GLU D C   1 
ATOM   12610 O  O   . GLU D  1 4   ? -73.909 8.706   3.899   1.00 112.40 ? 4    GLU D O   1 
ATOM   12611 C  CB  . GLU D  1 4   ? -71.266 6.726   2.741   1.00 109.49 ? 4    GLU D CB  1 
ATOM   12612 C  CG  . GLU D  1 4   ? -70.460 6.166   1.579   1.00 109.22 ? 4    GLU D CG  1 
ATOM   12613 C  CD  . GLU D  1 4   ? -69.009 6.613   1.616   1.00 106.74 ? 4    GLU D CD  1 
ATOM   12614 O  OE1 . GLU D  1 4   ? -68.473 6.812   2.731   1.00 104.90 ? 4    GLU D OE1 1 
ATOM   12615 O  OE2 . GLU D  1 4   ? -68.406 6.761   0.530   1.00 105.97 ? 4    GLU D OE2 1 
ATOM   12616 N  N   . ASP D  1 5   ? -71.738 9.354   3.799   1.00 95.09  ? 5    ASP D N   1 
ATOM   12617 C  CA  . ASP D  1 5   ? -71.824 10.417  4.791   1.00 87.63  ? 5    ASP D CA  1 
ATOM   12618 C  C   . ASP D  1 5   ? -70.450 11.074  4.867   1.00 86.78  ? 5    ASP D C   1 
ATOM   12619 O  O   . ASP D  1 5   ? -69.443 10.403  5.080   1.00 87.15  ? 5    ASP D O   1 
ATOM   12620 C  CB  . ASP D  1 5   ? -72.176 9.797   6.149   1.00 70.50  ? 5    ASP D CB  1 
ATOM   12621 C  CG  . ASP D  1 5   ? -72.110 10.786  7.292   1.00 64.47  ? 5    ASP D CG  1 
ATOM   12622 O  OD1 . ASP D  1 5   ? -72.102 12.011  7.046   1.00 63.01  ? 5    ASP D OD1 1 
ATOM   12623 O  OD2 . ASP D  1 5   ? -72.086 10.327  8.452   1.00 62.11  ? 5    ASP D OD2 1 
ATOM   12624 N  N   . PRO D  1 6   ? -70.414 12.404  4.732   1.00 91.82  ? 6    PRO D N   1 
ATOM   12625 C  CA  . PRO D  1 6   ? -69.165 13.172  4.741   1.00 92.29  ? 6    PRO D CA  1 
ATOM   12626 C  C   . PRO D  1 6   ? -68.519 13.287  6.116   1.00 93.60  ? 6    PRO D C   1 
ATOM   12627 O  O   . PRO D  1 6   ? -67.330 13.605  6.207   1.00 95.44  ? 6    PRO D O   1 
ATOM   12628 C  CB  . PRO D  1 6   ? -69.597 14.546  4.223   1.00 81.96  ? 6    PRO D CB  1 
ATOM   12629 C  CG  . PRO D  1 6   ? -70.799 14.257  3.397   1.00 83.09  ? 6    PRO D CG  1 
ATOM   12630 C  CD  . PRO D  1 6   ? -71.520 13.180  4.152   1.00 82.88  ? 6    PRO D CD  1 
ATOM   12631 N  N   . GLN D  1 7   ? -69.286 13.051  7.173   1.00 86.30  ? 7    GLN D N   1 
ATOM   12632 C  CA  . GLN D  1 7   ? -68.726 13.124  8.510   1.00 81.44  ? 7    GLN D CA  1 
ATOM   12633 C  C   . GLN D  1 7   ? -67.720 12.004  8.661   1.00 73.80  ? 7    GLN D C   1 
ATOM   12634 O  O   . GLN D  1 7   ? -66.607 12.205  9.163   1.00 74.27  ? 7    GLN D O   1 
ATOM   12635 C  CB  . GLN D  1 7   ? -69.820 12.998  9.565   1.00 90.37  ? 7    GLN D CB  1 
ATOM   12636 C  CG  . GLN D  1 7   ? -70.841 14.121  9.527   1.00 95.54  ? 7    GLN D CG  1 
ATOM   12637 C  CD  . GLN D  1 7   ? -70.217 15.500  9.695   1.00 96.98  ? 7    GLN D CD  1 
ATOM   12638 O  OE1 . GLN D  1 7   ? -69.224 15.670  10.409  1.00 95.47  ? 7    GLN D OE1 1 
ATOM   12639 N  NE2 . GLN D  1 7   ? -70.804 16.496  9.031   1.00 99.26  ? 7    GLN D NE2 1 
ATOM   12640 N  N   . LEU D  1 8   ? -68.113 10.825  8.189   1.00 58.40  ? 8    LEU D N   1 
ATOM   12641 C  CA  . LEU D  1 8   ? -67.273 9.644   8.308   1.00 48.00  ? 8    LEU D CA  1 
ATOM   12642 C  C   . LEU D  1 8   ? -66.179 9.528   7.236   1.00 47.83  ? 8    LEU D C   1 
ATOM   12643 O  O   . LEU D  1 8   ? -65.289 8.701   7.362   1.00 50.50  ? 8    LEU D O   1 
ATOM   12644 C  CB  . LEU D  1 8   ? -68.123 8.369   8.337   1.00 40.30  ? 8    LEU D CB  1 
ATOM   12645 C  CG  . LEU D  1 8   ? -69.193 8.179   9.420   1.00 42.89  ? 8    LEU D CG  1 
ATOM   12646 C  CD1 . LEU D  1 8   ? -69.514 6.687   9.611   1.00 41.68  ? 8    LEU D CD1 1 
ATOM   12647 C  CD2 . LEU D  1 8   ? -68.806 8.828   10.744  1.00 40.83  ? 8    LEU D CD2 1 
ATOM   12648 N  N   . LEU D  1 9   ? -66.235 10.329  6.179   1.00 42.08  ? 9    LEU D N   1 
ATOM   12649 C  CA  . LEU D  1 9   ? -65.200 10.238  5.153   1.00 38.06  ? 9    LEU D CA  1 
ATOM   12650 C  C   . LEU D  1 9   ? -64.296 11.451  5.198   1.00 37.38  ? 9    LEU D C   1 
ATOM   12651 O  O   . LEU D  1 9   ? -64.726 12.575  4.970   1.00 38.31  ? 9    LEU D O   1 
ATOM   12652 C  CB  . LEU D  1 9   ? -65.784 10.024  3.746   1.00 41.36  ? 9    LEU D CB  1 
ATOM   12653 C  CG  . LEU D  1 9   ? -64.826 9.428   2.693   1.00 41.80  ? 9    LEU D CG  1 
ATOM   12654 C  CD1 . LEU D  1 9   ? -65.558 8.604   1.642   1.00 39.50  ? 9    LEU D CD1 1 
ATOM   12655 C  CD2 . LEU D  1 9   ? -63.985 10.492  2.001   1.00 38.08  ? 9    LEU D CD2 1 
ATOM   12656 N  N   . VAL D  1 10  ? -63.027 11.194  5.485   1.00 40.17  ? 10   VAL D N   1 
ATOM   12657 C  CA  . VAL D  1 10  ? -62.031 12.240  5.665   1.00 35.10  ? 10   VAL D CA  1 
ATOM   12658 C  C   . VAL D  1 10  ? -60.911 12.047  4.664   1.00 38.39  ? 10   VAL D C   1 
ATOM   12659 O  O   . VAL D  1 10  ? -60.651 10.924  4.271   1.00 40.36  ? 10   VAL D O   1 
ATOM   12660 C  CB  . VAL D  1 10  ? -61.441 12.136  7.071   1.00 37.89  ? 10   VAL D CB  1 
ATOM   12661 C  CG1 . VAL D  1 10  ? -60.283 13.076  7.240   1.00 38.07  ? 10   VAL D CG1 1 
ATOM   12662 C  CG2 . VAL D  1 10  ? -62.501 12.440  8.095   1.00 39.32  ? 10   VAL D CG2 1 
ATOM   12663 N  N   . ARG D  1 11  ? -60.261 13.120  4.219   1.00 34.31  ? 11   ARG D N   1 
ATOM   12664 C  CA  . ARG D  1 11  ? -59.018 12.962  3.452   1.00 35.47  ? 11   ARG D CA  1 
ATOM   12665 C  C   . ARG D  1 11  ? -57.798 13.449  4.220   1.00 32.34  ? 11   ARG D C   1 
ATOM   12666 O  O   . ARG D  1 11  ? -57.773 14.572  4.701   1.00 32.56  ? 11   ARG D O   1 
ATOM   12667 C  CB  . ARG D  1 11  ? -59.074 13.669  2.089   1.00 62.86  ? 11   ARG D CB  1 
ATOM   12668 C  CG  . ARG D  1 11  ? -57.676 13.905  1.496   1.00 67.51  ? 11   ARG D CG  1 
ATOM   12669 C  CD  . ARG D  1 11  ? -57.698 14.399  0.060   1.00 73.52  ? 11   ARG D CD  1 
ATOM   12670 N  NE  . ARG D  1 11  ? -57.167 13.396  -0.860  1.00 78.53  ? 11   ARG D NE  1 
ATOM   12671 C  CZ  . ARG D  1 11  ? -57.921 12.635  -1.650  1.00 81.08  ? 11   ARG D CZ  1 
ATOM   12672 N  NH1 . ARG D  1 11  ? -59.243 12.777  -1.636  1.00 84.12  ? 11   ARG D NH1 1 
ATOM   12673 N  NH2 . ARG D  1 11  ? -57.356 11.740  -2.457  1.00 77.57  ? 11   ARG D NH2 1 
ATOM   12674 N  N   . VAL D  1 12  ? -56.777 12.612  4.320   1.00 38.19  ? 12   VAL D N   1 
ATOM   12675 C  CA  . VAL D  1 12  ? -55.531 13.049  4.941   1.00 40.46  ? 12   VAL D CA  1 
ATOM   12676 C  C   . VAL D  1 12  ? -54.371 13.090  3.932   1.00 41.22  ? 12   VAL D C   1 
ATOM   12677 O  O   . VAL D  1 12  ? -54.564 12.833  2.737   1.00 41.85  ? 12   VAL D O   1 
ATOM   12678 C  CB  . VAL D  1 12  ? -55.177 12.188  6.171   1.00 31.17  ? 12   VAL D CB  1 
ATOM   12679 C  CG1 . VAL D  1 12  ? -56.349 12.172  7.159   1.00 29.56  ? 12   VAL D CG1 1 
ATOM   12680 C  CG2 . VAL D  1 12  ? -54.804 10.779  5.745   1.00 29.71  ? 12   VAL D CG2 1 
ATOM   12681 N  N   . ARG D  1 13  ? -53.176 13.416  4.415   1.00 37.92  ? 13   ARG D N   1 
ATOM   12682 C  CA  . ARG D  1 13  ? -52.019 13.599  3.542   1.00 42.80  ? 13   ARG D CA  1 
ATOM   12683 C  C   . ARG D  1 13  ? -51.692 12.328  2.741   1.00 42.02  ? 13   ARG D C   1 
ATOM   12684 O  O   . ARG D  1 13  ? -50.980 12.373  1.734   1.00 44.47  ? 13   ARG D O   1 
ATOM   12685 C  CB  . ARG D  1 13  ? -50.804 14.084  4.356   1.00 59.70  ? 13   ARG D CB  1 
ATOM   12686 C  CG  . ARG D  1 13  ? -49.558 14.506  3.552   1.00 64.45  ? 13   ARG D CG  1 
ATOM   12687 C  CD  . ARG D  1 13  ? -49.574 15.971  3.129   1.00 69.43  ? 13   ARG D CD  1 
ATOM   12688 N  NE  . ARG D  1 13  ? -49.668 16.893  4.264   1.00 75.87  ? 13   ARG D NE  1 
ATOM   12689 C  CZ  . ARG D  1 13  ? -48.630 17.352  4.963   1.00 78.34  ? 13   ARG D CZ  1 
ATOM   12690 N  NH1 . ARG D  1 13  ? -47.395 16.970  4.655   1.00 81.84  ? 13   ARG D NH1 1 
ATOM   12691 N  NH2 . ARG D  1 13  ? -48.825 18.196  5.975   1.00 74.14  ? 13   ARG D NH2 1 
ATOM   12692 N  N   . GLY D  1 14  ? -52.219 11.192  3.177   1.00 39.27  ? 14   GLY D N   1 
ATOM   12693 C  CA  . GLY D  1 14  ? -52.011 9.960   2.442   1.00 37.71  ? 14   GLY D CA  1 
ATOM   12694 C  C   . GLY D  1 14  ? -53.240 9.475   1.694   1.00 38.60  ? 14   GLY D C   1 
ATOM   12695 O  O   . GLY D  1 14  ? -53.255 8.352   1.188   1.00 39.61  ? 14   GLY D O   1 
ATOM   12696 N  N   . GLY D  1 15  ? -54.266 10.319  1.598   1.00 38.08  ? 15   GLY D N   1 
ATOM   12697 C  CA  . GLY D  1 15  ? -55.518 9.895   0.995   1.00 39.62  ? 15   GLY D CA  1 
ATOM   12698 C  C   . GLY D  1 15  ? -56.696 9.650   1.929   1.00 39.10  ? 15   GLY D C   1 
ATOM   12699 O  O   . GLY D  1 15  ? -56.677 10.046  3.095   1.00 37.48  ? 15   GLY D O   1 
ATOM   12700 N  N   . GLN D  1 16  ? -57.741 9.022   1.396   1.00 32.41  ? 16   GLN D N   1 
ATOM   12701 C  CA  . GLN D  1 16  ? -59.042 8.972   2.064   1.00 35.90  ? 16   GLN D CA  1 
ATOM   12702 C  C   . GLN D  1 16  ? -59.163 7.918   3.144   1.00 33.26  ? 16   GLN D C   1 
ATOM   12703 O  O   . GLN D  1 16  ? -58.485 6.903   3.114   1.00 31.84  ? 16   GLN D O   1 
ATOM   12704 C  CB  . GLN D  1 16  ? -60.164 8.761   1.054   1.00 57.56  ? 16   GLN D CB  1 
ATOM   12705 C  CG  . GLN D  1 16  ? -60.023 9.547   -0.224  1.00 63.61  ? 16   GLN D CG  1 
ATOM   12706 C  CD  . GLN D  1 16  ? -61.215 10.425  -0.470  1.00 70.51  ? 16   GLN D CD  1 
ATOM   12707 O  OE1 . GLN D  1 16  ? -61.288 11.539  0.049   1.00 73.26  ? 16   GLN D OE1 1 
ATOM   12708 N  NE2 . GLN D  1 16  ? -62.171 9.930   -1.255  1.00 72.93  ? 16   GLN D NE2 1 
ATOM   12709 N  N   . LEU D  1 17  ? -60.068 8.172   4.080   1.00 49.77  ? 17   LEU D N   1 
ATOM   12710 C  CA  . LEU D  1 17  ? -60.360 7.280   5.189   1.00 48.34  ? 17   LEU D CA  1 
ATOM   12711 C  C   . LEU D  1 17  ? -61.866 7.252   5.436   1.00 48.91  ? 17   LEU D C   1 
ATOM   12712 O  O   . LEU D  1 17  ? -62.515 8.298   5.523   1.00 51.29  ? 17   LEU D O   1 
ATOM   12713 C  CB  . LEU D  1 17  ? -59.661 7.765   6.462   1.00 31.56  ? 17   LEU D CB  1 
ATOM   12714 C  CG  . LEU D  1 17  ? -58.138 7.836   6.519   1.00 30.26  ? 17   LEU D CG  1 
ATOM   12715 C  CD1 . LEU D  1 17  ? -57.711 8.578   7.757   1.00 29.58  ? 17   LEU D CD1 1 
ATOM   12716 C  CD2 . LEU D  1 17  ? -57.575 6.456   6.540   1.00 29.67  ? 17   LEU D CD2 1 
ATOM   12717 N  N   . ARG D  1 18  ? -62.418 6.052   5.540   1.00 34.32  ? 18   ARG D N   1 
ATOM   12718 C  CA  . ARG D  1 18  ? -63.782 5.887   5.989   1.00 35.57  ? 18   ARG D CA  1 
ATOM   12719 C  C   . ARG D  1 18  ? -63.698 5.704   7.480   1.00 35.02  ? 18   ARG D C   1 
ATOM   12720 O  O   . ARG D  1 18  ? -62.833 4.973   7.966   1.00 33.96  ? 18   ARG D O   1 
ATOM   12721 C  CB  . ARG D  1 18  ? -64.404 4.639   5.375   1.00 57.92  ? 18   ARG D CB  1 
ATOM   12722 C  CG  . ARG D  1 18  ? -65.884 4.457   5.686   1.00 66.26  ? 18   ARG D CG  1 
ATOM   12723 C  CD  . ARG D  1 18  ? -66.496 3.291   4.911   1.00 72.06  ? 18   ARG D CD  1 
ATOM   12724 N  NE  . ARG D  1 18  ? -65.761 2.983   3.683   1.00 75.93  ? 18   ARG D NE  1 
ATOM   12725 C  CZ  . ARG D  1 18  ? -65.855 3.679   2.552   1.00 79.11  ? 18   ARG D CZ  1 
ATOM   12726 N  NH1 . ARG D  1 18  ? -66.650 4.739   2.490   1.00 79.31  ? 18   ARG D NH1 1 
ATOM   12727 N  NH2 . ARG D  1 18  ? -65.143 3.323   1.488   1.00 80.71  ? 18   ARG D NH2 1 
ATOM   12728 N  N   . GLY D  1 19  ? -64.588 6.376   8.203   1.00 38.30  ? 19   GLY D N   1 
ATOM   12729 C  CA  . GLY D  1 19  ? -64.635 6.300   9.653   1.00 37.28  ? 19   GLY D CA  1 
ATOM   12730 C  C   . GLY D  1 19  ? -65.827 5.489   10.098  1.00 38.54  ? 19   GLY D C   1 
ATOM   12731 O  O   . GLY D  1 19  ? -66.462 4.819   9.289   1.00 37.74  ? 19   GLY D O   1 
ATOM   12732 N  N   . ILE D  1 20  ? -66.132 5.537   11.384  1.00 43.65  ? 20   ILE D N   1 
ATOM   12733 C  CA  . ILE D  1 20  ? -67.325 4.874   11.876  1.00 49.86  ? 20   ILE D CA  1 
ATOM   12734 C  C   . ILE D  1 20  ? -68.043 5.770   12.886  1.00 54.60  ? 20   ILE D C   1 
ATOM   12735 O  O   . ILE D  1 20  ? -67.394 6.400   13.731  1.00 55.63  ? 20   ILE D O   1 
ATOM   12736 C  CB  . ILE D  1 20  ? -67.006 3.482   12.471  1.00 43.84  ? 20   ILE D CB  1 
ATOM   12737 C  CG1 . ILE D  1 20  ? -68.268 2.863   13.080  1.00 49.37  ? 20   ILE D CG1 1 
ATOM   12738 C  CG2 . ILE D  1 20  ? -65.931 3.587   13.507  1.00 39.81  ? 20   ILE D CG2 1 
ATOM   12739 C  CD1 . ILE D  1 20  ? -68.027 1.569   13.817  1.00 50.80  ? 20   ILE D CD1 1 
ATOM   12740 N  N   . ARG D  1 21  ? -69.372 5.855   12.763  1.00 48.38  ? 21   ARG D N   1 
ATOM   12741 C  CA  . ARG D  1 21  ? -70.201 6.589   13.722  1.00 50.65  ? 21   ARG D CA  1 
ATOM   12742 C  C   . ARG D  1 21  ? -70.556 5.697   14.911  1.00 49.20  ? 21   ARG D C   1 
ATOM   12743 O  O   . ARG D  1 21  ? -70.945 4.539   14.731  1.00 49.87  ? 21   ARG D O   1 
ATOM   12744 C  CB  . ARG D  1 21  ? -71.466 7.105   13.054  1.00 71.15  ? 21   ARG D CB  1 
ATOM   12745 C  CG  . ARG D  1 21  ? -72.611 7.355   14.007  1.00 77.80  ? 21   ARG D CG  1 
ATOM   12746 C  CD  . ARG D  1 21  ? -73.923 6.865   13.409  1.00 85.36  ? 21   ARG D CD  1 
ATOM   12747 N  NE  . ARG D  1 21  ? -75.069 7.500   14.048  1.00 93.91  ? 21   ARG D NE  1 
ATOM   12748 C  CZ  . ARG D  1 21  ? -75.534 8.704   13.718  1.00 100.27 ? 21   ARG D CZ  1 
ATOM   12749 N  NH1 . ARG D  1 21  ? -74.948 9.397   12.748  1.00 100.44 ? 21   ARG D NH1 1 
ATOM   12750 N  NH2 . ARG D  1 21  ? -76.585 9.216   14.355  1.00 104.00 ? 21   ARG D NH2 1 
ATOM   12751 N  N   . LEU D  1 22  ? -70.403 6.235   16.122  1.00 46.78  ? 22   LEU D N   1 
ATOM   12752 C  CA  . LEU D  1 22  ? -70.479 5.437   17.347  1.00 47.66  ? 22   LEU D CA  1 
ATOM   12753 C  C   . LEU D  1 22  ? -71.401 6.083   18.366  1.00 49.67  ? 22   LEU D C   1 
ATOM   12754 O  O   . LEU D  1 22  ? -71.659 7.286   18.292  1.00 47.47  ? 22   LEU D O   1 
ATOM   12755 C  CB  . LEU D  1 22  ? -69.084 5.263   17.966  1.00 53.69  ? 22   LEU D CB  1 
ATOM   12756 C  CG  . LEU D  1 22  ? -68.111 4.260   17.345  1.00 54.24  ? 22   LEU D CG  1 
ATOM   12757 C  CD1 . LEU D  1 22  ? -66.793 4.304   18.083  1.00 51.06  ? 22   LEU D CD1 1 
ATOM   12758 C  CD2 . LEU D  1 22  ? -68.696 2.841   17.350  1.00 57.62  ? 22   LEU D CD2 1 
ATOM   12759 N  N   . LYS D  1 23  ? -71.888 5.294   19.325  1.00 56.06  ? 23   LYS D N   1 
ATOM   12760 C  CA  . LYS D  1 23  ? -72.768 5.844   20.353  1.00 62.87  ? 23   LYS D CA  1 
ATOM   12761 C  C   . LYS D  1 23  ? -72.121 5.999   21.725  1.00 65.28  ? 23   LYS D C   1 
ATOM   12762 O  O   . LYS D  1 23  ? -71.854 5.019   22.421  1.00 65.11  ? 23   LYS D O   1 
ATOM   12763 C  CB  . LYS D  1 23  ? -74.057 5.031   20.483  1.00 81.32  ? 23   LYS D CB  1 
ATOM   12764 C  CG  . LYS D  1 23  ? -74.949 5.103   19.264  1.00 88.35  ? 23   LYS D CG  1 
ATOM   12765 C  CD  . LYS D  1 23  ? -75.039 6.520   18.710  1.00 92.82  ? 23   LYS D CD  1 
ATOM   12766 C  CE  . LYS D  1 23  ? -75.617 6.512   17.292  1.00 96.36  ? 23   LYS D CE  1 
ATOM   12767 N  NZ  . LYS D  1 23  ? -74.877 5.592   16.360  1.00 94.84  ? 23   LYS D NZ  1 
ATOM   12768 N  N   . ALA D  1 24  ? -71.876 7.251   22.097  1.00 79.95  ? 24   ALA D N   1 
ATOM   12769 C  CA  . ALA D  1 24  ? -71.651 7.611   23.482  1.00 82.42  ? 24   ALA D CA  1 
ATOM   12770 C  C   . ALA D  1 24  ? -73.053 7.653   24.058  1.00 87.46  ? 24   ALA D C   1 
ATOM   12771 O  O   . ALA D  1 24  ? -74.017 7.818   23.308  1.00 89.41  ? 24   ALA D O   1 
ATOM   12772 C  CB  . ALA D  1 24  ? -70.990 8.977   23.574  1.00 69.39  ? 24   ALA D CB  1 
ATOM   12773 N  N   . PRO D  1 25  ? -73.188 7.487   25.381  1.00 84.70  ? 25   PRO D N   1 
ATOM   12774 C  CA  . PRO D  1 25  ? -74.543 7.519   25.939  1.00 84.37  ? 25   PRO D CA  1 
ATOM   12775 C  C   . PRO D  1 25  ? -75.224 8.845   25.638  1.00 81.46  ? 25   PRO D C   1 
ATOM   12776 O  O   . PRO D  1 25  ? -76.441 8.882   25.493  1.00 84.97  ? 25   PRO D O   1 
ATOM   12777 C  CB  . PRO D  1 25  ? -74.305 7.364   27.441  1.00 92.99  ? 25   PRO D CB  1 
ATOM   12778 C  CG  . PRO D  1 25  ? -72.990 6.643   27.536  1.00 92.85  ? 25   PRO D CG  1 
ATOM   12779 C  CD  . PRO D  1 25  ? -72.171 7.180   26.402  1.00 90.62  ? 25   PRO D CD  1 
ATOM   12780 N  N   . GLY D  1 26  ? -74.440 9.911   25.507  1.00 71.08  ? 26   GLY D N   1 
ATOM   12781 C  CA  . GLY D  1 26  ? -74.987 11.235  25.264  1.00 70.44  ? 26   GLY D CA  1 
ATOM   12782 C  C   . GLY D  1 26  ? -74.860 11.785  23.851  1.00 68.81  ? 26   GLY D C   1 
ATOM   12783 O  O   . GLY D  1 26  ? -74.956 12.995  23.651  1.00 67.29  ? 26   GLY D O   1 
ATOM   12784 N  N   . GLY D  1 27  ? -74.636 10.919  22.867  1.00 73.89  ? 27   GLY D N   1 
ATOM   12785 C  CA  . GLY D  1 27  ? -74.538 11.383  21.494  1.00 74.79  ? 27   GLY D CA  1 
ATOM   12786 C  C   . GLY D  1 27  ? -73.793 10.466  20.545  1.00 74.18  ? 27   GLY D C   1 
ATOM   12787 O  O   . GLY D  1 27  ? -73.268 9.435   20.950  1.00 74.74  ? 27   GLY D O   1 
ATOM   12788 N  N   . PRO D  1 28  ? -73.793 10.814  19.255  1.00 71.01  ? 28   PRO D N   1 
ATOM   12789 C  CA  . PRO D  1 28  ? -72.966 10.165  18.235  1.00 69.75  ? 28   PRO D CA  1 
ATOM   12790 C  C   . PRO D  1 28  ? -71.528 10.725  18.222  1.00 68.53  ? 28   PRO D C   1 
ATOM   12791 O  O   . PRO D  1 28  ? -71.322 11.889  18.606  1.00 69.33  ? 28   PRO D O   1 
ATOM   12792 C  CB  . PRO D  1 28  ? -73.706 10.502  16.944  1.00 71.90  ? 28   PRO D CB  1 
ATOM   12793 C  CG  . PRO D  1 28  ? -74.304 11.856  17.217  1.00 73.66  ? 28   PRO D CG  1 
ATOM   12794 C  CD  . PRO D  1 28  ? -74.590 11.922  18.698  1.00 73.52  ? 28   PRO D CD  1 
ATOM   12795 N  N   . VAL D  1 29  ? -70.554 9.914   17.795  1.00 67.56  ? 29   VAL D N   1 
ATOM   12796 C  CA  . VAL D  1 29  ? -69.150 10.344  17.686  1.00 61.52  ? 29   VAL D CA  1 
ATOM   12797 C  C   . VAL D  1 29  ? -68.453 9.739   16.467  1.00 58.32  ? 29   VAL D C   1 
ATOM   12798 O  O   . VAL D  1 29  ? -68.700 8.591   16.107  1.00 60.60  ? 29   VAL D O   1 
ATOM   12799 C  CB  . VAL D  1 29  ? -68.315 9.957   18.931  1.00 48.52  ? 29   VAL D CB  1 
ATOM   12800 C  CG1 . VAL D  1 29  ? -68.947 10.491  20.206  1.00 41.27  ? 29   VAL D CG1 1 
ATOM   12801 C  CG2 . VAL D  1 29  ? -68.134 8.447   19.021  1.00 39.63  ? 29   VAL D CG2 1 
ATOM   12802 N  N   . SER D  1 30  ? -67.581 10.507  15.829  1.00 54.30  ? 30   SER D N   1 
ATOM   12803 C  CA  . SER D  1 30  ? -66.791 9.959   14.730  1.00 53.98  ? 30   SER D CA  1 
ATOM   12804 C  C   . SER D  1 30  ? -65.526 9.291   15.274  1.00 51.61  ? 30   SER D C   1 
ATOM   12805 O  O   . SER D  1 30  ? -64.806 9.877   16.086  1.00 53.14  ? 30   SER D O   1 
ATOM   12806 C  CB  . SER D  1 30  ? -66.403 11.048  13.717  1.00 54.73  ? 30   SER D CB  1 
ATOM   12807 O  OG  . SER D  1 30  ? -67.519 11.552  13.007  1.00 56.04  ? 30   SER D OG  1 
ATOM   12808 N  N   . ALA D  1 31  ? -65.255 8.064   14.840  1.00 42.41  ? 31   ALA D N   1 
ATOM   12809 C  CA  . ALA D  1 31  ? -63.987 7.427   15.167  1.00 38.72  ? 31   ALA D CA  1 
ATOM   12810 C  C   . ALA D  1 31  ? -63.286 6.970   13.897  1.00 39.11  ? 31   ALA D C   1 
ATOM   12811 O  O   . ALA D  1 31  ? -63.907 6.410   12.997  1.00 42.09  ? 31   ALA D O   1 
ATOM   12812 C  CB  . ALA D  1 31  ? -64.190 6.267   16.111  1.00 34.30  ? 31   ALA D CB  1 
ATOM   12813 N  N   . PHE D  1 32  ? -61.991 7.246   13.818  1.00 39.79  ? 32   PHE D N   1 
ATOM   12814 C  CA  . PHE D  1 32  ? -61.168 6.769   12.726  1.00 39.60  ? 32   PHE D CA  1 
ATOM   12815 C  C   . PHE D  1 32  ? -60.077 5.924   13.336  1.00 41.12  ? 32   PHE D C   1 
ATOM   12816 O  O   . PHE D  1 32  ? -59.156 6.441   13.961  1.00 40.40  ? 32   PHE D O   1 
ATOM   12817 C  CB  . PHE D  1 32  ? -60.619 7.965   11.974  1.00 39.19  ? 32   PHE D CB  1 
ATOM   12818 C  CG  . PHE D  1 32  ? -61.695 8.835   11.431  1.00 44.02  ? 32   PHE D CG  1 
ATOM   12819 C  CD1 . PHE D  1 32  ? -62.280 9.803   12.221  1.00 48.74  ? 32   PHE D CD1 1 
ATOM   12820 C  CD2 . PHE D  1 32  ? -62.174 8.642   10.152  1.00 45.93  ? 32   PHE D CD2 1 
ATOM   12821 C  CE1 . PHE D  1 32  ? -63.308 10.584  11.734  1.00 52.32  ? 32   PHE D CE1 1 
ATOM   12822 C  CE2 . PHE D  1 32  ? -63.193 9.420   9.660   1.00 49.78  ? 32   PHE D CE2 1 
ATOM   12823 C  CZ  . PHE D  1 32  ? -63.767 10.389  10.453  1.00 52.27  ? 32   PHE D CZ  1 
ATOM   12824 N  N   . LEU D  1 33  ? -60.182 4.614   13.137  1.00 39.12  ? 33   LEU D N   1 
ATOM   12825 C  CA  . LEU D  1 33  ? -59.428 3.674   13.950  1.00 35.60  ? 33   LEU D CA  1 
ATOM   12826 C  C   . LEU D  1 33  ? -58.451 2.875   13.097  1.00 36.11  ? 33   LEU D C   1 
ATOM   12827 O  O   . LEU D  1 33  ? -58.843 2.284   12.091  1.00 35.83  ? 33   LEU D O   1 
ATOM   12828 C  CB  . LEU D  1 33  ? -60.391 2.736   14.693  1.00 30.46  ? 33   LEU D CB  1 
ATOM   12829 C  CG  . LEU D  1 33  ? -61.549 3.360   15.490  1.00 31.50  ? 33   LEU D CG  1 
ATOM   12830 C  CD1 . LEU D  1 33  ? -62.286 2.322   16.293  1.00 32.39  ? 33   LEU D CD1 1 
ATOM   12831 C  CD2 . LEU D  1 33  ? -61.057 4.435   16.418  1.00 30.87  ? 33   LEU D CD2 1 
ATOM   12832 N  N   . GLY D  1 34  ? -57.177 2.863   13.496  1.00 39.06  ? 34   GLY D N   1 
ATOM   12833 C  CA  . GLY D  1 34  ? -56.170 2.084   12.789  1.00 34.43  ? 34   GLY D CA  1 
ATOM   12834 C  C   . GLY D  1 34  ? -55.708 2.751   11.510  1.00 30.56  ? 34   GLY D C   1 
ATOM   12835 O  O   . GLY D  1 34  ? -55.456 2.100   10.507  1.00 27.74  ? 34   GLY D O   1 
ATOM   12836 N  N   . ILE D  1 35  ? -55.627 4.071   11.553  1.00 26.73  ? 35   ILE D N   1 
ATOM   12837 C  CA  . ILE D  1 35  ? -54.995 4.840   10.505  1.00 26.49  ? 35   ILE D CA  1 
ATOM   12838 C  C   . ILE D  1 35  ? -53.520 4.537   10.596  1.00 25.95  ? 35   ILE D C   1 
ATOM   12839 O  O   . ILE D  1 35  ? -52.938 4.698   11.663  1.00 24.85  ? 35   ILE D O   1 
ATOM   12840 C  CB  . ILE D  1 35  ? -55.194 6.332   10.769  1.00 30.98  ? 35   ILE D CB  1 
ATOM   12841 C  CG1 . ILE D  1 35  ? -56.684 6.669   10.745  1.00 32.77  ? 35   ILE D CG1 1 
ATOM   12842 C  CG2 . ILE D  1 35  ? -54.417 7.172   9.762   1.00 29.84  ? 35   ILE D CG2 1 
ATOM   12843 C  CD1 . ILE D  1 35  ? -56.988 8.024   11.302  1.00 33.00  ? 35   ILE D CD1 1 
ATOM   12844 N  N   . PRO D  1 36  ? -52.918 4.050   9.504   1.00 25.48  ? 36   PRO D N   1 
ATOM   12845 C  CA  . PRO D  1 36  ? -51.487 3.724   9.503   1.00 24.70  ? 36   PRO D CA  1 
ATOM   12846 C  C   . PRO D  1 36  ? -50.638 4.975   9.557   1.00 24.17  ? 36   PRO D C   1 
ATOM   12847 O  O   . PRO D  1 36  ? -50.830 5.840   8.711   1.00 25.61  ? 36   PRO D O   1 
ATOM   12848 C  CB  . PRO D  1 36  ? -51.300 3.054   8.147   1.00 25.13  ? 36   PRO D CB  1 
ATOM   12849 C  CG  . PRO D  1 36  ? -52.359 3.655   7.288   1.00 25.95  ? 36   PRO D CG  1 
ATOM   12850 C  CD  . PRO D  1 36  ? -53.525 3.925   8.174   1.00 26.28  ? 36   PRO D CD  1 
ATOM   12851 N  N   . PHE D  1 37  ? -49.724 5.102   10.508  1.00 23.43  ? 37   PHE D N   1 
ATOM   12852 C  CA  . PHE D  1 37  ? -48.872 6.287   10.483  1.00 23.05  ? 37   PHE D CA  1 
ATOM   12853 C  C   . PHE D  1 37  ? -47.430 6.097   10.032  1.00 24.67  ? 37   PHE D C   1 
ATOM   12854 O  O   . PHE D  1 37  ? -46.675 7.070   9.922   1.00 24.58  ? 37   PHE D O   1 
ATOM   12855 C  CB  . PHE D  1 37  ? -48.949 7.065   11.782  1.00 22.71  ? 37   PHE D CB  1 
ATOM   12856 C  CG  . PHE D  1 37  ? -48.302 6.393   12.924  1.00 22.10  ? 37   PHE D CG  1 
ATOM   12857 C  CD1 . PHE D  1 37  ? -49.015 5.527   13.715  1.00 22.23  ? 37   PHE D CD1 1 
ATOM   12858 C  CD2 . PHE D  1 37  ? -46.980 6.654   13.230  1.00 21.51  ? 37   PHE D CD2 1 
ATOM   12859 C  CE1 . PHE D  1 37  ? -48.416 4.922   14.788  1.00 24.87  ? 37   PHE D CE1 1 
ATOM   12860 C  CE2 . PHE D  1 37  ? -46.375 6.054   14.298  1.00 21.03  ? 37   PHE D CE2 1 
ATOM   12861 C  CZ  . PHE D  1 37  ? -47.089 5.185   15.082  1.00 24.44  ? 37   PHE D CZ  1 
ATOM   12862 N  N   . ALA D  1 38  ? -47.060 4.844   9.785   1.00 32.47  ? 38   ALA D N   1 
ATOM   12863 C  CA  . ALA D  1 38  ? -45.704 4.485   9.396   1.00 30.04  ? 38   ALA D CA  1 
ATOM   12864 C  C   . ALA D  1 38  ? -45.730 3.196   8.596   1.00 33.83  ? 38   ALA D C   1 
ATOM   12865 O  O   . ALA D  1 38  ? -46.578 2.333   8.818   1.00 35.89  ? 38   ALA D O   1 
ATOM   12866 C  CB  . ALA D  1 38  ? -44.859 4.304   10.617  1.00 21.75  ? 38   ALA D CB  1 
ATOM   12867 N  N   . GLU D  1 39  ? -44.803 3.060   7.662   1.00 36.86  ? 39   GLU D N   1 
ATOM   12868 C  CA  . GLU D  1 39  ? -44.629 1.791   6.982   1.00 36.19  ? 39   GLU D CA  1 
ATOM   12869 C  C   . GLU D  1 39  ? -44.309 0.739   8.045   1.00 30.29  ? 39   GLU D C   1 
ATOM   12870 O  O   . GLU D  1 39  ? -43.547 1.021   8.970   1.00 27.68  ? 39   GLU D O   1 
ATOM   12871 C  CB  . GLU D  1 39  ? -43.515 1.904   5.938   1.00 39.37  ? 39   GLU D CB  1 
ATOM   12872 C  CG  . GLU D  1 39  ? -43.932 2.662   4.684   1.00 43.25  ? 39   GLU D CG  1 
ATOM   12873 C  CD  . GLU D  1 39  ? -44.933 1.889   3.828   1.00 50.54  ? 39   GLU D CD  1 
ATOM   12874 O  OE1 . GLU D  1 39  ? -44.687 0.694   3.519   1.00 55.27  ? 39   GLU D OE1 1 
ATOM   12875 O  OE2 . GLU D  1 39  ? -45.973 2.476   3.463   1.00 51.21  ? 39   GLU D OE2 1 
ATOM   12876 N  N   . PRO D  1 40  ? -44.917 -0.459  7.936   1.00 23.67  ? 40   PRO D N   1 
ATOM   12877 C  CA  . PRO D  1 40  ? -44.758 -1.515  8.941   1.00 23.57  ? 40   PRO D CA  1 
ATOM   12878 C  C   . PRO D  1 40  ? -43.306 -1.826  9.196   1.00 23.33  ? 40   PRO D C   1 
ATOM   12879 O  O   . PRO D  1 40  ? -42.606 -2.160  8.252   1.00 23.75  ? 40   PRO D O   1 
ATOM   12880 C  CB  . PRO D  1 40  ? -45.407 -2.723  8.270   1.00 24.40  ? 40   PRO D CB  1 
ATOM   12881 C  CG  . PRO D  1 40  ? -46.458 -2.141  7.454   1.00 31.05  ? 40   PRO D CG  1 
ATOM   12882 C  CD  . PRO D  1 40  ? -45.919 -0.831  6.930   1.00 24.42  ? 40   PRO D CD  1 
ATOM   12883 N  N   . PRO D  1 41  ? -42.880 -1.773  10.469  1.00 27.82  ? 41   PRO D N   1 
ATOM   12884 C  CA  . PRO D  1 41  ? -41.472 -1.902  10.857  1.00 28.14  ? 41   PRO D CA  1 
ATOM   12885 C  C   . PRO D  1 41  ? -41.059 -3.351  10.889  1.00 32.23  ? 41   PRO D C   1 
ATOM   12886 O  O   . PRO D  1 41  ? -40.479 -3.793  11.883  1.00 34.22  ? 41   PRO D O   1 
ATOM   12887 C  CB  . PRO D  1 41  ? -41.471 -1.377  12.287  1.00 21.90  ? 41   PRO D CB  1 
ATOM   12888 C  CG  . PRO D  1 41  ? -42.831 -1.734  12.800  1.00 22.03  ? 41   PRO D CG  1 
ATOM   12889 C  CD  . PRO D  1 41  ? -43.762 -1.580  11.634  1.00 22.47  ? 41   PRO D CD  1 
ATOM   12890 N  N   . VAL D  1 42  ? -41.346 -4.081  9.818   1.00 23.84  ? 42   VAL D N   1 
ATOM   12891 C  CA  . VAL D  1 42  ? -41.117 -5.516  9.810   1.00 29.02  ? 42   VAL D CA  1 
ATOM   12892 C  C   . VAL D  1 42  ? -39.841 -5.856  9.041   1.00 27.48  ? 42   VAL D C   1 
ATOM   12893 O  O   . VAL D  1 42  ? -39.200 -4.975  8.473   1.00 25.58  ? 42   VAL D O   1 
ATOM   12894 C  CB  . VAL D  1 42  ? -42.314 -6.234  9.187   1.00 25.24  ? 42   VAL D CB  1 
ATOM   12895 C  CG1 . VAL D  1 42  ? -43.583 -5.736  9.814   1.00 24.88  ? 42   VAL D CG1 1 
ATOM   12896 C  CG2 . VAL D  1 42  ? -42.362 -5.973  7.705   1.00 34.14  ? 42   VAL D CG2 1 
ATOM   12897 N  N   . GLY D  1 43  ? -39.473 -7.131  9.024   1.00 29.16  ? 43   GLY D N   1 
ATOM   12898 C  CA  . GLY D  1 43  ? -38.396 -7.587  8.166   1.00 32.93  ? 43   GLY D CA  1 
ATOM   12899 C  C   . GLY D  1 43  ? -37.051 -7.005  8.521   1.00 36.06  ? 43   GLY D C   1 
ATOM   12900 O  O   . GLY D  1 43  ? -36.585 -7.137  9.646   1.00 38.83  ? 43   GLY D O   1 
ATOM   12901 N  N   . SER D  1 44  ? -36.440 -6.340  7.550   1.00 38.69  ? 44   SER D N   1 
ATOM   12902 C  CA  . SER D  1 44  ? -35.147 -5.695  7.728   1.00 37.38  ? 44   SER D CA  1 
ATOM   12903 C  C   . SER D  1 44  ? -35.321 -4.331  8.398   1.00 31.94  ? 44   SER D C   1 
ATOM   12904 O  O   . SER D  1 44  ? -34.372 -3.556  8.501   1.00 31.50  ? 44   SER D O   1 
ATOM   12905 C  CB  . SER D  1 44  ? -34.468 -5.525  6.376   1.00 45.38  ? 44   SER D CB  1 
ATOM   12906 O  OG  . SER D  1 44  ? -35.249 -4.696  5.530   1.00 46.90  ? 44   SER D OG  1 
ATOM   12907 N  N   . ARG D  1 45  ? -36.558 -4.023  8.785   1.00 24.75  ? 45   ARG D N   1 
ATOM   12908 C  CA  . ARG D  1 45  ? -36.873 -2.819  9.542   1.00 25.83  ? 45   ARG D CA  1 
ATOM   12909 C  C   . ARG D  1 45  ? -36.979 -3.070  11.042  1.00 25.57  ? 45   ARG D C   1 
ATOM   12910 O  O   . ARG D  1 45  ? -37.223 -2.139  11.797  1.00 26.75  ? 45   ARG D O   1 
ATOM   12911 C  CB  . ARG D  1 45  ? -38.180 -2.174  9.052   1.00 44.15  ? 45   ARG D CB  1 
ATOM   12912 C  CG  . ARG D  1 45  ? -38.156 -1.680  7.618   1.00 54.43  ? 45   ARG D CG  1 
ATOM   12913 C  CD  . ARG D  1 45  ? -36.923 -0.822  7.338   1.00 66.38  ? 45   ARG D CD  1 
ATOM   12914 N  NE  . ARG D  1 45  ? -36.829 0.349   8.215   1.00 74.57  ? 45   ARG D NE  1 
ATOM   12915 C  CZ  . ARG D  1 45  ? -35.832 1.237   8.192   1.00 77.31  ? 45   ARG D CZ  1 
ATOM   12916 N  NH1 . ARG D  1 45  ? -34.823 1.101   7.333   1.00 77.64  ? 45   ARG D NH1 1 
ATOM   12917 N  NH2 . ARG D  1 45  ? -35.845 2.266   9.035   1.00 76.44  ? 45   ARG D NH2 1 
ATOM   12918 N  N   . ARG D  1 46  ? -36.823 -4.310  11.489  1.00 23.55  ? 46   ARG D N   1 
ATOM   12919 C  CA  . ARG D  1 46  ? -36.952 -4.586  12.921  1.00 23.64  ? 46   ARG D CA  1 
ATOM   12920 C  C   . ARG D  1 46  ? -35.813 -3.919  13.693  1.00 22.92  ? 46   ARG D C   1 
ATOM   12921 O  O   . ARG D  1 46  ? -34.652 -4.028  13.283  1.00 23.19  ? 46   ARG D O   1 
ATOM   12922 C  CB  . ARG D  1 46  ? -36.969 -6.091  13.196  1.00 23.91  ? 46   ARG D CB  1 
ATOM   12923 C  CG  . ARG D  1 46  ? -37.032 -6.461  14.669  1.00 23.70  ? 46   ARG D CG  1 
ATOM   12924 C  CD  . ARG D  1 46  ? -36.826 -7.947  14.863  1.00 24.61  ? 46   ARG D CD  1 
ATOM   12925 N  NE  . ARG D  1 46  ? -38.069 -8.706  14.789  1.00 25.03  ? 46   ARG D NE  1 
ATOM   12926 C  CZ  . ARG D  1 46  ? -38.122 -10.018 14.591  1.00 26.03  ? 46   ARG D CZ  1 
ATOM   12927 N  NH1 . ARG D  1 46  ? -37.003 -10.701 14.435  1.00 26.70  ? 46   ARG D NH1 1 
ATOM   12928 N  NH2 . ARG D  1 46  ? -39.288 -10.649 14.543  1.00 26.47  ? 46   ARG D NH2 1 
ATOM   12929 N  N   . PHE D  1 47  ? -36.160 -3.230  14.789  1.00 26.36  ? 47   PHE D N   1 
ATOM   12930 C  CA  . PHE D  1 47  ? -35.223 -2.475  15.647  1.00 27.28  ? 47   PHE D CA  1 
ATOM   12931 C  C   . PHE D  1 47  ? -34.799 -1.133  15.053  1.00 29.58  ? 47   PHE D C   1 
ATOM   12932 O  O   . PHE D  1 47  ? -33.997 -0.414  15.659  1.00 28.80  ? 47   PHE D O   1 
ATOM   12933 C  CB  . PHE D  1 47  ? -33.938 -3.242  15.994  1.00 22.17  ? 47   PHE D CB  1 
ATOM   12934 C  CG  . PHE D  1 47  ? -34.145 -4.668  16.405  1.00 23.24  ? 47   PHE D CG  1 
ATOM   12935 C  CD1 . PHE D  1 47  ? -34.822 -4.982  17.565  1.00 24.62  ? 47   PHE D CD1 1 
ATOM   12936 C  CD2 . PHE D  1 47  ? -33.600 -5.693  15.657  1.00 23.62  ? 47   PHE D CD2 1 
ATOM   12937 C  CE1 . PHE D  1 47  ? -34.979 -6.305  17.950  1.00 26.26  ? 47   PHE D CE1 1 
ATOM   12938 C  CE2 . PHE D  1 47  ? -33.753 -7.006  16.035  1.00 24.28  ? 47   PHE D CE2 1 
ATOM   12939 C  CZ  . PHE D  1 47  ? -34.439 -7.318  17.182  1.00 26.60  ? 47   PHE D CZ  1 
ATOM   12940 N  N   . MET D  1 48  ? -35.271 -0.837  13.844  1.00 25.73  ? 48   MET D N   1 
ATOM   12941 C  CA  . MET D  1 48  ? -34.937 0.409   13.158  1.00 21.45  ? 48   MET D CA  1 
ATOM   12942 C  C   . MET D  1 48  ? -35.967 1.489   13.467  1.00 27.61  ? 48   MET D C   1 
ATOM   12943 O  O   . MET D  1 48  ? -37.109 1.178   13.828  1.00 20.68  ? 48   MET D O   1 
ATOM   12944 C  CB  . MET D  1 48  ? -34.876 0.184   11.646  1.00 28.28  ? 48   MET D CB  1 
ATOM   12945 C  CG  . MET D  1 48  ? -33.768 -0.744  11.177  1.00 28.90  ? 48   MET D CG  1 
ATOM   12946 S  SD  . MET D  1 48  ? -32.162 0.053   11.160  1.00 58.24  ? 48   MET D SD  1 
ATOM   12947 C  CE  . MET D  1 48  ? -32.529 1.572   10.284  1.00 112.43 ? 48   MET D CE  1 
ATOM   12948 N  N   . PRO D  1 49  ? -35.567 2.765   13.325  1.00 30.48  ? 49   PRO D N   1 
ATOM   12949 C  CA  . PRO D  1 49  ? -36.497 3.893   13.445  1.00 28.10  ? 49   PRO D CA  1 
ATOM   12950 C  C   . PRO D  1 49  ? -37.587 3.802   12.383  1.00 27.82  ? 49   PRO D C   1 
ATOM   12951 O  O   . PRO D  1 49  ? -37.344 3.191   11.334  1.00 28.24  ? 49   PRO D O   1 
ATOM   12952 C  CB  . PRO D  1 49  ? -35.604 5.097   13.180  1.00 20.45  ? 49   PRO D CB  1 
ATOM   12953 C  CG  . PRO D  1 49  ? -34.240 4.627   13.527  1.00 20.64  ? 49   PRO D CG  1 
ATOM   12954 C  CD  . PRO D  1 49  ? -34.183 3.218   13.120  1.00 20.99  ? 49   PRO D CD  1 
ATOM   12955 N  N   . PRO D  1 50  ? -38.782 4.360   12.657  1.00 28.80  ? 50   PRO D N   1 
ATOM   12956 C  CA  . PRO D  1 50  ? -39.875 4.235   11.684  1.00 33.00  ? 50   PRO D CA  1 
ATOM   12957 C  C   . PRO D  1 50  ? -39.705 5.154   10.483  1.00 36.62  ? 50   PRO D C   1 
ATOM   12958 O  O   . PRO D  1 50  ? -39.310 6.304   10.650  1.00 39.10  ? 50   PRO D O   1 
ATOM   12959 C  CB  . PRO D  1 50  ? -41.111 4.633   12.494  1.00 20.50  ? 50   PRO D CB  1 
ATOM   12960 C  CG  . PRO D  1 50  ? -40.599 5.506   13.565  1.00 20.06  ? 50   PRO D CG  1 
ATOM   12961 C  CD  . PRO D  1 50  ? -39.204 5.060   13.880  1.00 28.43  ? 50   PRO D CD  1 
ATOM   12962 N  N   . GLU D  1 51  ? -39.970 4.644   9.286   1.00 34.99  ? 51   GLU D N   1 
ATOM   12963 C  CA  . GLU D  1 51  ? -40.134 5.496   8.121   1.00 38.58  ? 51   GLU D CA  1 
ATOM   12964 C  C   . GLU D  1 51  ? -41.631 5.728   8.061   1.00 34.48  ? 51   GLU D C   1 
ATOM   12965 O  O   . GLU D  1 51  ? -42.392 4.837   8.439   1.00 36.01  ? 51   GLU D O   1 
ATOM   12966 C  CB  . GLU D  1 51  ? -39.660 4.800   6.846   1.00 64.92  ? 51   GLU D CB  1 
ATOM   12967 C  CG  . GLU D  1 51  ? -38.301 4.108   6.923   1.00 72.01  ? 51   GLU D CG  1 
ATOM   12968 C  CD  . GLU D  1 51  ? -38.177 2.965   5.904   1.00 78.87  ? 51   GLU D CD  1 
ATOM   12969 O  OE1 . GLU D  1 51  ? -38.658 1.835   6.177   1.00 78.43  ? 51   GLU D OE1 1 
ATOM   12970 O  OE2 . GLU D  1 51  ? -37.610 3.203   4.817   1.00 82.75  ? 51   GLU D OE2 1 
ATOM   12971 N  N   . PRO D  1 52  ? -42.065 6.912   7.595   1.00 34.74  ? 52   PRO D N   1 
ATOM   12972 C  CA  . PRO D  1 52  ? -43.493 7.265   7.556   1.00 34.61  ? 52   PRO D CA  1 
ATOM   12973 C  C   . PRO D  1 52  ? -44.276 6.616   6.401   1.00 34.16  ? 52   PRO D C   1 
ATOM   12974 O  O   . PRO D  1 52  ? -43.695 6.278   5.362   1.00 34.07  ? 52   PRO D O   1 
ATOM   12975 C  CB  . PRO D  1 52  ? -43.460 8.786   7.387   1.00 27.57  ? 52   PRO D CB  1 
ATOM   12976 C  CG  . PRO D  1 52  ? -42.214 9.026   6.599   1.00 23.19  ? 52   PRO D CG  1 
ATOM   12977 C  CD  . PRO D  1 52  ? -41.217 8.018   7.117   1.00 27.56  ? 52   PRO D CD  1 
ATOM   12978 N  N   . LYS D  1 53  ? -45.591 6.482   6.591   1.00 28.40  ? 53   LYS D N   1 
ATOM   12979 C  CA  . LYS D  1 53  ? -46.469 5.796   5.641   1.00 28.30  ? 53   LYS D CA  1 
ATOM   12980 C  C   . LYS D  1 53  ? -46.520 6.426   4.237   1.00 29.48  ? 53   LYS D C   1 
ATOM   12981 O  O   . LYS D  1 53  ? -46.873 7.600   4.057   1.00 27.11  ? 53   LYS D O   1 
ATOM   12982 C  CB  . LYS D  1 53  ? -47.887 5.697   6.216   1.00 24.34  ? 53   LYS D CB  1 
ATOM   12983 C  CG  . LYS D  1 53  ? -48.868 4.956   5.333   1.00 25.11  ? 53   LYS D CG  1 
ATOM   12984 C  CD  . LYS D  1 53  ? -48.784 3.457   5.545   1.00 26.96  ? 53   LYS D CD  1 
ATOM   12985 C  CE  . LYS D  1 53  ? -49.466 2.658   4.418   1.00 27.82  ? 53   LYS D CE  1 
ATOM   12986 N  NZ  . LYS D  1 53  ? -48.627 2.456   3.187   1.00 26.30  ? 53   LYS D NZ  1 
ATOM   12987 N  N   . ARG D  1 54  ? -46.189 5.606   3.243   1.00 30.34  ? 54   ARG D N   1 
ATOM   12988 C  CA  . ARG D  1 54  ? -46.280 5.993   1.847   1.00 29.81  ? 54   ARG D CA  1 
ATOM   12989 C  C   . ARG D  1 54  ? -47.759 6.103   1.591   1.00 26.76  ? 54   ARG D C   1 
ATOM   12990 O  O   . ARG D  1 54  ? -48.529 5.337   2.153   1.00 26.65  ? 54   ARG D O   1 
ATOM   12991 C  CB  . ARG D  1 54  ? -45.650 4.911   0.954   1.00 38.64  ? 54   ARG D CB  1 
ATOM   12992 C  CG  . ARG D  1 54  ? -44.107 4.770   1.069   1.00 45.80  ? 54   ARG D CG  1 
ATOM   12993 C  CD  . ARG D  1 54  ? -43.555 3.573   0.281   1.00 47.01  ? 54   ARG D CD  1 
ATOM   12994 N  NE  . ARG D  1 54  ? -44.166 2.321   0.730   1.00 50.03  ? 54   ARG D NE  1 
ATOM   12995 C  CZ  . ARG D  1 54  ? -45.122 1.664   0.073   1.00 52.12  ? 54   ARG D CZ  1 
ATOM   12996 N  NH1 . ARG D  1 54  ? -45.577 2.122   -1.086  1.00 55.34  ? 54   ARG D NH1 1 
ATOM   12997 N  NH2 . ARG D  1 54  ? -45.623 0.540   0.571   1.00 49.73  ? 54   ARG D NH2 1 
ATOM   12998 N  N   . PRO D  1 55  ? -48.167 7.060   0.751   1.00 32.90  ? 55   PRO D N   1 
ATOM   12999 C  CA  . PRO D  1 55  ? -49.591 7.367   0.544   1.00 31.47  ? 55   PRO D CA  1 
ATOM   13000 C  C   . PRO D  1 55  ? -50.327 6.199   -0.101  1.00 31.33  ? 55   PRO D C   1 
ATOM   13001 O  O   . PRO D  1 55  ? -49.659 5.356   -0.717  1.00 30.73  ? 55   PRO D O   1 
ATOM   13002 C  CB  . PRO D  1 55  ? -49.555 8.570   -0.401  1.00 29.50  ? 55   PRO D CB  1 
ATOM   13003 C  CG  . PRO D  1 55  ? -48.265 8.410   -1.141  1.00 30.04  ? 55   PRO D CG  1 
ATOM   13004 C  CD  . PRO D  1 55  ? -47.296 7.811   -0.166  1.00 27.87  ? 55   PRO D CD  1 
ATOM   13005 N  N   . TRP D  1 56  ? -51.656 6.148   0.038   1.00 29.15  ? 56   TRP D N   1 
ATOM   13006 C  CA  . TRP D  1 56  ? -52.439 4.990   -0.426  1.00 34.26  ? 56   TRP D CA  1 
ATOM   13007 C  C   . TRP D  1 56  ? -53.587 5.305   -1.381  1.00 34.49  ? 56   TRP D C   1 
ATOM   13008 O  O   . TRP D  1 56  ? -54.161 6.398   -1.352  1.00 34.73  ? 56   TRP D O   1 
ATOM   13009 C  CB  . TRP D  1 56  ? -53.000 4.202   0.752   1.00 30.60  ? 56   TRP D CB  1 
ATOM   13010 C  CG  . TRP D  1 56  ? -53.919 5.009   1.600   1.00 29.39  ? 56   TRP D CG  1 
ATOM   13011 C  CD1 . TRP D  1 56  ? -55.253 5.179   1.422   1.00 30.28  ? 56   TRP D CD1 1 
ATOM   13012 C  CD2 . TRP D  1 56  ? -53.566 5.761   2.768   1.00 28.97  ? 56   TRP D CD2 1 
ATOM   13013 N  NE1 . TRP D  1 56  ? -55.756 5.995   2.403   1.00 30.48  ? 56   TRP D NE1 1 
ATOM   13014 C  CE2 . TRP D  1 56  ? -54.739 6.357   3.245   1.00 29.07  ? 56   TRP D CE2 1 
ATOM   13015 C  CE3 . TRP D  1 56  ? -52.372 5.985   3.451   1.00 27.59  ? 56   TRP D CE3 1 
ATOM   13016 C  CZ2 . TRP D  1 56  ? -54.754 7.159   4.374   1.00 35.36  ? 56   TRP D CZ2 1 
ATOM   13017 C  CZ3 . TRP D  1 56  ? -52.392 6.769   4.570   1.00 27.10  ? 56   TRP D CZ3 1 
ATOM   13018 C  CH2 . TRP D  1 56  ? -53.571 7.352   5.021   1.00 35.26  ? 56   TRP D CH2 1 
ATOM   13019 N  N   . SER D  1 57  ? -53.915 4.316   -2.212  1.00 41.65  ? 57   SER D N   1 
ATOM   13020 C  CA  . SER D  1 57  ? -54.932 4.450   -3.246  1.00 42.75  ? 57   SER D CA  1 
ATOM   13021 C  C   . SER D  1 57  ? -56.319 4.202   -2.685  1.00 43.54  ? 57   SER D C   1 
ATOM   13022 O  O   . SER D  1 57  ? -56.483 3.429   -1.741  1.00 44.60  ? 57   SER D O   1 
ATOM   13023 C  CB  . SER D  1 57  ? -54.663 3.487   -4.406  1.00 33.55  ? 57   SER D CB  1 
ATOM   13024 O  OG  . SER D  1 57  ? -54.938 2.142   -4.050  1.00 33.56  ? 57   SER D OG  1 
ATOM   13025 N  N   . GLY D  1 58  ? -57.310 4.875   -3.262  1.00 39.81  ? 58   GLY D N   1 
ATOM   13026 C  CA  . GLY D  1 58  ? -58.697 4.641   -2.914  1.00 40.51  ? 58   GLY D CA  1 
ATOM   13027 C  C   . GLY D  1 58  ? -59.039 5.136   -1.530  1.00 40.03  ? 58   GLY D C   1 
ATOM   13028 O  O   . GLY D  1 58  ? -58.375 6.015   -0.998  1.00 40.04  ? 58   GLY D O   1 
ATOM   13029 N  N   . VAL D  1 59  ? -60.086 4.575   -0.947  1.00 35.08  ? 59   VAL D N   1 
ATOM   13030 C  CA  . VAL D  1 59  ? -60.464 4.933   0.397   1.00 34.69  ? 59   VAL D CA  1 
ATOM   13031 C  C   . VAL D  1 59  ? -60.045 3.827   1.322   1.00 33.87  ? 59   VAL D C   1 
ATOM   13032 O  O   . VAL D  1 59  ? -60.425 2.681   1.141   1.00 34.94  ? 59   VAL D O   1 
ATOM   13033 C  CB  . VAL D  1 59  ? -61.959 5.099   0.518   1.00 51.27  ? 59   VAL D CB  1 
ATOM   13034 C  CG1 . VAL D  1 59  ? -62.378 5.055   1.977   1.00 51.22  ? 59   VAL D CG1 1 
ATOM   13035 C  CG2 . VAL D  1 59  ? -62.374 6.393   -0.127  1.00 52.60  ? 59   VAL D CG2 1 
ATOM   13036 N  N   . LEU D  1 60  ? -59.256 4.173   2.324   1.00 42.40  ? 60   LEU D N   1 
ATOM   13037 C  CA  . LEU D  1 60  ? -58.725 3.186   3.253   1.00 40.65  ? 60   LEU D CA  1 
ATOM   13038 C  C   . LEU D  1 60  ? -59.689 3.040   4.412   1.00 40.75  ? 60   LEU D C   1 
ATOM   13039 O  O   . LEU D  1 60  ? -60.243 4.025   4.909   1.00 32.48  ? 60   LEU D O   1 
ATOM   13040 C  CB  . LEU D  1 60  ? -57.361 3.651   3.751   1.00 30.63  ? 60   LEU D CB  1 
ATOM   13041 C  CG  . LEU D  1 60  ? -56.545 2.862   4.749   1.00 29.67  ? 60   LEU D CG  1 
ATOM   13042 C  CD1 . LEU D  1 60  ? -55.885 1.725   4.050   1.00 29.64  ? 60   LEU D CD1 1 
ATOM   13043 C  CD2 . LEU D  1 60  ? -55.529 3.803   5.285   1.00 28.67  ? 60   LEU D CD2 1 
ATOM   13044 N  N   . ASP D  1 61  ? -59.900 1.808   4.842   1.00 45.43  ? 61   ASP D N   1 
ATOM   13045 C  CA  . ASP D  1 61  ? -60.874 1.574   5.883   1.00 51.03  ? 61   ASP D CA  1 
ATOM   13046 C  C   . ASP D  1 61  ? -60.262 1.890   7.228   1.00 50.44  ? 61   ASP D C   1 
ATOM   13047 O  O   . ASP D  1 61  ? -59.284 1.246   7.612   1.00 52.53  ? 61   ASP D O   1 
ATOM   13048 C  CB  . ASP D  1 61  ? -61.286 0.102   5.861   1.00 69.24  ? 61   ASP D CB  1 
ATOM   13049 C  CG  . ASP D  1 61  ? -62.241 -0.258  6.985   1.00 75.35  ? 61   ASP D CG  1 
ATOM   13050 O  OD1 . ASP D  1 61  ? -62.942 0.652   7.481   1.00 76.85  ? 61   ASP D OD1 1 
ATOM   13051 O  OD2 . ASP D  1 61  ? -62.291 -1.453  7.366   1.00 77.50  ? 61   ASP D OD2 1 
ATOM   13052 N  N   . ALA D  1 62  ? -60.792 2.876   7.954   1.00 45.25  ? 62   ALA D N   1 
ATOM   13053 C  CA  . ALA D  1 62  ? -60.581 2.826   9.395   1.00 43.05  ? 62   ALA D CA  1 
ATOM   13054 C  C   . ALA D  1 62  ? -61.908 2.748   10.114  1.00 40.88  ? 62   ALA D C   1 
ATOM   13055 O  O   . ALA D  1 62  ? -62.420 3.764   10.558  1.00 39.02  ? 62   ALA D O   1 
ATOM   13056 C  CB  . ALA D  1 62  ? -59.835 4.078   9.845   1.00 47.34  ? 62   ALA D CB  1 
ATOM   13057 N  N   . THR D  1 63  ? -62.421 1.540   10.316  1.00 53.28  ? 63   THR D N   1 
ATOM   13058 C  CA  . THR D  1 63  ? -63.552 1.343   11.206  1.00 59.92  ? 63   THR D CA  1 
ATOM   13059 C  C   . THR D  1 63  ? -63.261 0.562   12.473  1.00 65.75  ? 63   THR D C   1 
ATOM   13060 O  O   . THR D  1 63  ? -64.147 0.398   13.307  1.00 72.26  ? 63   THR D O   1 
ATOM   13061 C  CB  . THR D  1 63  ? -64.715 0.691   10.493  1.00 58.74  ? 63   THR D CB  1 
ATOM   13062 O  OG1 . THR D  1 63  ? -64.270 -0.528  9.891   1.00 58.48  ? 63   THR D OG1 1 
ATOM   13063 C  CG2 . THR D  1 63  ? -65.230 1.620   9.426   1.00 61.32  ? 63   THR D CG2 1 
ATOM   13064 N  N   . THR D  1 64  ? -62.045 0.041   12.598  1.00 57.52  ? 64   THR D N   1 
ATOM   13065 C  CA  . THR D  1 64  ? -61.770 -0.976  13.604  1.00 52.98  ? 64   THR D CA  1 
ATOM   13066 C  C   . THR D  1 64  ? -60.330 -0.922  13.987  1.00 50.94  ? 64   THR D C   1 
ATOM   13067 O  O   . THR D  1 64  ? -59.481 -0.685  13.132  1.00 55.30  ? 64   THR D O   1 
ATOM   13068 C  CB  . THR D  1 64  ? -61.925 -2.355  13.006  1.00 47.63  ? 64   THR D CB  1 
ATOM   13069 O  OG1 . THR D  1 64  ? -61.402 -2.321  11.673  1.00 45.15  ? 64   THR D OG1 1 
ATOM   13070 C  CG2 . THR D  1 64  ? -63.388 -2.787  12.978  1.00 50.17  ? 64   THR D CG2 1 
ATOM   13071 N  N   . PHE D  1 65  ? -60.048 -1.220  15.250  1.00 34.80  ? 65   PHE D N   1 
ATOM   13072 C  CA  . PHE D  1 65  ? -58.676 -1.205  15.741  1.00 30.91  ? 65   PHE D CA  1 
ATOM   13073 C  C   . PHE D  1 65  ? -57.799 -2.182  14.966  1.00 30.06  ? 65   PHE D C   1 
ATOM   13074 O  O   . PHE D  1 65  ? -58.273 -3.217  14.491  1.00 30.11  ? 65   PHE D O   1 
ATOM   13075 C  CB  . PHE D  1 65  ? -58.626 -1.537  17.232  1.00 40.96  ? 65   PHE D CB  1 
ATOM   13076 C  CG  . PHE D  1 65  ? -59.275 -0.507  18.111  1.00 42.17  ? 65   PHE D CG  1 
ATOM   13077 C  CD1 . PHE D  1 65  ? -58.702 0.743   18.274  1.00 40.57  ? 65   PHE D CD1 1 
ATOM   13078 C  CD2 . PHE D  1 65  ? -60.448 -0.799  18.792  1.00 44.51  ? 65   PHE D CD2 1 
ATOM   13079 C  CE1 . PHE D  1 65  ? -59.295 1.688   19.085  1.00 41.09  ? 65   PHE D CE1 1 
ATOM   13080 C  CE2 . PHE D  1 65  ? -61.043 0.141   19.609  1.00 45.29  ? 65   PHE D CE2 1 
ATOM   13081 C  CZ  . PHE D  1 65  ? -60.467 1.388   19.756  1.00 43.52  ? 65   PHE D CZ  1 
ATOM   13082 N  N   . GLN D  1 66  ? -56.522 -1.829  14.834  1.00 37.97  ? 66   GLN D N   1 
ATOM   13083 C  CA  . GLN D  1 66  ? -55.535 -2.670  14.167  1.00 35.99  ? 66   GLN D CA  1 
ATOM   13084 C  C   . GLN D  1 66  ? -54.863 -3.586  15.166  1.00 33.75  ? 66   GLN D C   1 
ATOM   13085 O  O   . GLN D  1 66  ? -55.259 -3.644  16.322  1.00 37.41  ? 66   GLN D O   1 
ATOM   13086 C  CB  . GLN D  1 66  ? -54.483 -1.809  13.480  1.00 34.30  ? 66   GLN D CB  1 
ATOM   13087 C  CG  . GLN D  1 66  ? -54.683 -1.688  11.994  1.00 35.30  ? 66   GLN D CG  1 
ATOM   13088 C  CD  . GLN D  1 66  ? -54.626 -3.031  11.306  1.00 37.09  ? 66   GLN D CD  1 
ATOM   13089 O  OE1 . GLN D  1 66  ? -53.907 -3.940  11.733  1.00 33.05  ? 66   GLN D OE1 1 
ATOM   13090 N  NE2 . GLN D  1 66  ? -55.396 -3.171  10.236  1.00 42.60  ? 66   GLN D NE2 1 
ATOM   13091 N  N   . ASN D  1 67  ? -53.837 -4.294  14.728  1.00 27.16  ? 67   ASN D N   1 
ATOM   13092 C  CA  . ASN D  1 67  ? -53.125 -5.201  15.625  1.00 28.27  ? 67   ASN D CA  1 
ATOM   13093 C  C   . ASN D  1 67  ? -52.337 -4.541  16.768  1.00 26.13  ? 67   ASN D C   1 
ATOM   13094 O  O   . ASN D  1 67  ? -51.734 -3.480  16.603  1.00 25.29  ? 67   ASN D O   1 
ATOM   13095 C  CB  . ASN D  1 67  ? -52.208 -6.118  14.824  1.00 39.43  ? 67   ASN D CB  1 
ATOM   13096 C  CG  . ASN D  1 67  ? -52.974 -7.042  13.922  1.00 41.96  ? 67   ASN D CG  1 
ATOM   13097 O  OD1 . ASN D  1 67  ? -54.203 -7.127  14.013  1.00 43.09  ? 67   ASN D OD1 1 
ATOM   13098 N  ND2 . ASN D  1 67  ? -52.261 -7.747  13.044  1.00 41.39  ? 67   ASN D ND2 1 
ATOM   13099 N  N   . VAL D  1 68  ? -52.356 -5.187  17.929  1.00 26.87  ? 68   VAL D N   1 
ATOM   13100 C  CA  . VAL D  1 68  ? -51.527 -4.789  19.054  1.00 28.13  ? 68   VAL D CA  1 
ATOM   13101 C  C   . VAL D  1 68  ? -50.066 -5.107  18.708  1.00 28.25  ? 68   VAL D C   1 
ATOM   13102 O  O   . VAL D  1 68  ? -49.794 -6.050  17.974  1.00 27.18  ? 68   VAL D O   1 
ATOM   13103 C  CB  . VAL D  1 68  ? -51.944 -5.553  20.323  1.00 26.34  ? 68   VAL D CB  1 
ATOM   13104 C  CG1 . VAL D  1 68  ? -51.010 -5.255  21.446  1.00 26.88  ? 68   VAL D CG1 1 
ATOM   13105 C  CG2 . VAL D  1 68  ? -53.346 -5.183  20.724  1.00 27.09  ? 68   VAL D CG2 1 
ATOM   13106 N  N   . CYS D  1 69  ? -49.127 -4.313  19.208  1.00 24.13  ? 69   CYS D N   1 
ATOM   13107 C  CA  . CYS D  1 69  ? -47.720 -4.616  19.007  1.00 24.13  ? 69   CYS D CA  1 
ATOM   13108 C  C   . CYS D  1 69  ? -47.298 -5.895  19.740  1.00 25.56  ? 69   CYS D C   1 
ATOM   13109 O  O   . CYS D  1 69  ? -47.846 -6.233  20.795  1.00 26.39  ? 69   CYS D O   1 
ATOM   13110 C  CB  . CYS D  1 69  ? -46.855 -3.433  19.445  1.00 30.78  ? 69   CYS D CB  1 
ATOM   13111 S  SG  . CYS D  1 69  ? -46.995 -1.971  18.396  1.00 63.32  ? 69   CYS D SG  1 
ATOM   13112 N  N   . TYR D  1 70  ? -46.313 -6.594  19.181  1.00 24.19  ? 70   TYR D N   1 
ATOM   13113 C  CA  . TYR D  1 70  ? -45.844 -7.848  19.755  1.00 27.51  ? 70   TYR D CA  1 
ATOM   13114 C  C   . TYR D  1 70  ? -45.293 -7.731  21.189  1.00 26.23  ? 70   TYR D C   1 
ATOM   13115 O  O   . TYR D  1 70  ? -44.392 -6.940  21.486  1.00 24.51  ? 70   TYR D O   1 
ATOM   13116 C  CB  . TYR D  1 70  ? -44.838 -8.512  18.824  1.00 24.98  ? 70   TYR D CB  1 
ATOM   13117 C  CG  . TYR D  1 70  ? -45.205 -9.931  18.628  1.00 26.62  ? 70   TYR D CG  1 
ATOM   13118 C  CD1 . TYR D  1 70  ? -46.116 -10.285 17.667  1.00 27.76  ? 70   TYR D CD1 1 
ATOM   13119 C  CD2 . TYR D  1 70  ? -44.716 -10.913 19.461  1.00 30.97  ? 70   TYR D CD2 1 
ATOM   13120 C  CE1 . TYR D  1 70  ? -46.504 -11.589 17.494  1.00 32.94  ? 70   TYR D CE1 1 
ATOM   13121 C  CE2 . TYR D  1 70  ? -45.095 -12.226 19.304  1.00 36.25  ? 70   TYR D CE2 1 
ATOM   13122 C  CZ  . TYR D  1 70  ? -45.997 -12.562 18.313  1.00 37.90  ? 70   TYR D CZ  1 
ATOM   13123 O  OH  . TYR D  1 70  ? -46.402 -13.871 18.124  1.00 42.15  ? 70   TYR D OH  1 
ATOM   13124 N  N   . GLN D  1 71  ? -45.843 -8.530  22.087  1.00 31.27  ? 71   GLN D N   1 
ATOM   13125 C  CA  . GLN D  1 71  ? -45.531 -8.347  23.490  1.00 35.43  ? 71   GLN D CA  1 
ATOM   13126 C  C   . GLN D  1 71  ? -45.809 -9.578  24.349  1.00 41.90  ? 71   GLN D C   1 
ATOM   13127 O  O   . GLN D  1 71  ? -46.562 -10.477 23.946  1.00 46.99  ? 71   GLN D O   1 
ATOM   13128 C  CB  . GLN D  1 71  ? -46.326 -7.155  24.025  1.00 29.05  ? 71   GLN D CB  1 
ATOM   13129 C  CG  . GLN D  1 71  ? -47.828 -7.258  23.790  1.00 26.15  ? 71   GLN D CG  1 
ATOM   13130 C  CD  . GLN D  1 71  ? -48.591 -6.086  24.373  1.00 25.08  ? 71   GLN D CD  1 
ATOM   13131 O  OE1 . GLN D  1 71  ? -49.095 -6.154  25.494  1.00 25.55  ? 71   GLN D OE1 1 
ATOM   13132 N  NE2 . GLN D  1 71  ? -48.681 -5.004  23.613  1.00 24.43  ? 71   GLN D NE2 1 
ATOM   13133 N  N   . TYR D  1 72  ? -45.206 -9.613  25.538  1.00 34.13  ? 72   TYR D N   1 
ATOM   13134 C  CA  . TYR D  1 72  ? -45.563 -10.613 26.542  1.00 38.88  ? 72   TYR D CA  1 
ATOM   13135 C  C   . TYR D  1 72  ? -47.073 -10.518 26.821  1.00 39.70  ? 72   TYR D C   1 
ATOM   13136 O  O   . TYR D  1 72  ? -47.668 -9.433  26.729  1.00 38.32  ? 72   TYR D O   1 
ATOM   13137 C  CB  . TYR D  1 72  ? -44.745 -10.415 27.832  1.00 60.82  ? 72   TYR D CB  1 
ATOM   13138 C  CG  . TYR D  1 72  ? -45.228 -11.263 28.989  1.00 71.47  ? 72   TYR D CG  1 
ATOM   13139 C  CD1 . TYR D  1 72  ? -44.862 -12.603 29.101  1.00 76.37  ? 72   TYR D CD1 1 
ATOM   13140 C  CD2 . TYR D  1 72  ? -46.066 -10.729 29.964  1.00 76.32  ? 72   TYR D CD2 1 
ATOM   13141 C  CE1 . TYR D  1 72  ? -45.320 -13.395 30.161  1.00 80.20  ? 72   TYR D CE1 1 
ATOM   13142 C  CE2 . TYR D  1 72  ? -46.531 -11.509 31.024  1.00 80.04  ? 72   TYR D CE2 1 
ATOM   13143 C  CZ  . TYR D  1 72  ? -46.159 -12.842 31.119  1.00 80.99  ? 72   TYR D CZ  1 
ATOM   13144 O  OH  . TYR D  1 72  ? -46.623 -13.610 32.171  1.00 80.43  ? 72   TYR D OH  1 
ATOM   13145 N  N   . VAL D  1 73  ? -47.707 -11.651 27.112  1.00 54.98  ? 73   VAL D N   1 
ATOM   13146 C  CA  . VAL D  1 73  ? -49.120 -11.630 27.482  1.00 55.97  ? 73   VAL D CA  1 
ATOM   13147 C  C   . VAL D  1 73  ? -49.295 -12.254 28.844  1.00 59.71  ? 73   VAL D C   1 
ATOM   13148 O  O   . VAL D  1 73  ? -48.795 -13.351 29.074  1.00 62.70  ? 73   VAL D O   1 
ATOM   13149 C  CB  . VAL D  1 73  ? -49.968 -12.397 26.503  1.00 40.60  ? 73   VAL D CB  1 
ATOM   13150 C  CG1 . VAL D  1 73  ? -51.423 -12.134 26.798  1.00 39.97  ? 73   VAL D CG1 1 
ATOM   13151 C  CG2 . VAL D  1 73  ? -49.627 -11.970 25.088  1.00 41.54  ? 73   VAL D CG2 1 
ATOM   13152 N  N   . ASP D  1 74  ? -50.013 -11.571 29.738  1.00 49.10  ? 74   ASP D N   1 
ATOM   13153 C  CA  . ASP D  1 74  ? -49.920 -11.898 31.159  1.00 51.00  ? 74   ASP D CA  1 
ATOM   13154 C  C   . ASP D  1 74  ? -50.779 -13.056 31.650  1.00 54.71  ? 74   ASP D C   1 
ATOM   13155 O  O   . ASP D  1 74  ? -52.001 -13.059 31.518  1.00 56.05  ? 74   ASP D O   1 
ATOM   13156 C  CB  . ASP D  1 74  ? -50.136 -10.680 32.040  1.00 58.36  ? 74   ASP D CB  1 
ATOM   13157 C  CG  . ASP D  1 74  ? -49.849 -10.984 33.487  1.00 63.31  ? 74   ASP D CG  1 
ATOM   13158 O  OD1 . ASP D  1 74  ? -48.821 -11.655 33.753  1.00 62.18  ? 74   ASP D OD1 1 
ATOM   13159 O  OD2 . ASP D  1 74  ? -50.662 -10.582 34.348  1.00 66.89  ? 74   ASP D OD2 1 
ATOM   13160 N  N   . THR D  1 75  ? -50.101 -14.053 32.201  1.00 67.93  ? 75   THR D N   1 
ATOM   13161 C  CA  . THR D  1 75  ? -50.732 -15.291 32.633  1.00 66.25  ? 75   THR D CA  1 
ATOM   13162 C  C   . THR D  1 75  ? -50.996 -15.456 34.147  1.00 67.42  ? 75   THR D C   1 
ATOM   13163 O  O   . THR D  1 75  ? -51.541 -16.482 34.569  1.00 68.80  ? 75   THR D O   1 
ATOM   13164 C  CB  . THR D  1 75  ? -49.940 -16.492 32.082  1.00 48.11  ? 75   THR D CB  1 
ATOM   13165 O  OG1 . THR D  1 75  ? -48.581 -16.091 31.829  1.00 43.90  ? 75   THR D OG1 1 
ATOM   13166 C  CG2 . THR D  1 75  ? -50.574 -16.986 30.778  1.00 46.29  ? 75   THR D CG2 1 
ATOM   13167 N  N   . LEU D  1 76  ? -50.609 -14.461 34.948  1.00 53.30  ? 76   LEU D N   1 
ATOM   13168 C  CA  . LEU D  1 76  ? -50.547 -14.603 36.415  1.00 50.31  ? 76   LEU D CA  1 
ATOM   13169 C  C   . LEU D  1 76  ? -51.832 -15.058 37.080  1.00 55.03  ? 76   LEU D C   1 
ATOM   13170 O  O   . LEU D  1 76  ? -51.815 -15.986 37.886  1.00 57.85  ? 76   LEU D O   1 
ATOM   13171 C  CB  . LEU D  1 76  ? -50.090 -13.304 37.082  1.00 44.13  ? 76   LEU D CB  1 
ATOM   13172 C  CG  . LEU D  1 76  ? -50.273 -13.244 38.605  1.00 39.91  ? 76   LEU D CG  1 
ATOM   13173 C  CD1 . LEU D  1 76  ? -49.411 -14.295 39.299  1.00 39.67  ? 76   LEU D CD1 1 
ATOM   13174 C  CD2 . LEU D  1 76  ? -49.994 -11.841 39.162  1.00 35.56  ? 76   LEU D CD2 1 
ATOM   13175 N  N   . TYR D  1 77  ? -52.930 -14.374 36.774  1.00 69.54  ? 77   TYR D N   1 
ATOM   13176 C  CA  . TYR D  1 77  ? -54.250 -14.759 37.267  1.00 72.40  ? 77   TYR D CA  1 
ATOM   13177 C  C   . TYR D  1 77  ? -55.194 -14.825 36.077  1.00 71.17  ? 77   TYR D C   1 
ATOM   13178 O  O   . TYR D  1 77  ? -55.985 -13.910 35.868  1.00 71.76  ? 77   TYR D O   1 
ATOM   13179 C  CB  . TYR D  1 77  ? -54.779 -13.737 38.279  1.00 58.57  ? 77   TYR D CB  1 
ATOM   13180 C  CG  . TYR D  1 77  ? -53.984 -13.619 39.564  1.00 55.17  ? 77   TYR D CG  1 
ATOM   13181 C  CD1 . TYR D  1 77  ? -53.525 -14.747 40.229  1.00 56.28  ? 77   TYR D CD1 1 
ATOM   13182 C  CD2 . TYR D  1 77  ? -53.699 -12.376 40.111  1.00 51.94  ? 77   TYR D CD2 1 
ATOM   13183 C  CE1 . TYR D  1 77  ? -52.801 -14.642 41.410  1.00 57.00  ? 77   TYR D CE1 1 
ATOM   13184 C  CE2 . TYR D  1 77  ? -52.979 -12.258 41.290  1.00 52.70  ? 77   TYR D CE2 1 
ATOM   13185 C  CZ  . TYR D  1 77  ? -52.528 -13.394 41.939  1.00 54.93  ? 77   TYR D CZ  1 
ATOM   13186 O  OH  . TYR D  1 77  ? -51.803 -13.284 43.117  1.00 54.25  ? 77   TYR D OH  1 
ATOM   13187 N  N   . PRO D  1 78  ? -55.108 -15.910 35.289  1.00 57.17  ? 78   PRO D N   1 
ATOM   13188 C  CA  . PRO D  1 78  ? -55.787 -16.026 33.990  1.00 54.32  ? 78   PRO D CA  1 
ATOM   13189 C  C   . PRO D  1 78  ? -57.303 -15.943 34.096  1.00 56.08  ? 78   PRO D C   1 
ATOM   13190 O  O   . PRO D  1 78  ? -57.895 -16.617 34.939  1.00 57.13  ? 78   PRO D O   1 
ATOM   13191 C  CB  . PRO D  1 78  ? -55.368 -17.411 33.502  1.00 44.80  ? 78   PRO D CB  1 
ATOM   13192 C  CG  . PRO D  1 78  ? -55.003 -18.154 34.739  1.00 46.31  ? 78   PRO D CG  1 
ATOM   13193 C  CD  . PRO D  1 78  ? -54.398 -17.149 35.650  1.00 46.37  ? 78   PRO D CD  1 
ATOM   13194 N  N   . GLY D  1 79  ? -57.915 -15.116 33.252  1.00 57.18  ? 79   GLY D N   1 
ATOM   13195 C  CA  . GLY D  1 79  ? -59.355 -14.922 33.277  1.00 62.23  ? 79   GLY D CA  1 
ATOM   13196 C  C   . GLY D  1 79  ? -59.850 -13.946 34.336  1.00 65.52  ? 79   GLY D C   1 
ATOM   13197 O  O   . GLY D  1 79  ? -60.994 -13.499 34.286  1.00 66.77  ? 79   GLY D O   1 
ATOM   13198 N  N   . PHE D  1 80  ? -58.995 -13.621 35.301  1.00 75.67  ? 80   PHE D N   1 
ATOM   13199 C  CA  . PHE D  1 80  ? -59.310 -12.601 36.297  1.00 77.21  ? 80   PHE D CA  1 
ATOM   13200 C  C   . PHE D  1 80  ? -59.167 -11.238 35.626  1.00 73.83  ? 80   PHE D C   1 
ATOM   13201 O  O   . PHE D  1 80  ? -58.099 -10.905 35.113  1.00 73.57  ? 80   PHE D O   1 
ATOM   13202 C  CB  . PHE D  1 80  ? -58.374 -12.739 37.506  1.00 72.95  ? 80   PHE D CB  1 
ATOM   13203 C  CG  . PHE D  1 80  ? -58.363 -11.544 38.417  1.00 72.87  ? 80   PHE D CG  1 
ATOM   13204 C  CD1 . PHE D  1 80  ? -59.384 -11.332 39.318  1.00 76.52  ? 80   PHE D CD1 1 
ATOM   13205 C  CD2 . PHE D  1 80  ? -57.319 -10.644 38.384  1.00 71.48  ? 80   PHE D CD2 1 
ATOM   13206 C  CE1 . PHE D  1 80  ? -59.366 -10.235 40.159  1.00 77.33  ? 80   PHE D CE1 1 
ATOM   13207 C  CE2 . PHE D  1 80  ? -57.299 -9.548  39.224  1.00 72.27  ? 80   PHE D CE2 1 
ATOM   13208 C  CZ  . PHE D  1 80  ? -58.324 -9.340  40.107  1.00 74.46  ? 80   PHE D CZ  1 
ATOM   13209 N  N   . GLU D  1 81  ? -60.238 -10.451 35.624  1.00 55.00  ? 81   GLU D N   1 
ATOM   13210 C  CA  . GLU D  1 81  ? -60.286 -9.276  34.765  1.00 56.13  ? 81   GLU D CA  1 
ATOM   13211 C  C   . GLU D  1 81  ? -59.424 -8.098  35.242  1.00 56.36  ? 81   GLU D C   1 
ATOM   13212 O  O   . GLU D  1 81  ? -59.169 -7.163  34.480  1.00 57.48  ? 81   GLU D O   1 
ATOM   13213 C  CB  . GLU D  1 81  ? -61.725 -8.833  34.519  1.00 78.82  ? 81   GLU D CB  1 
ATOM   13214 C  CG  . GLU D  1 81  ? -62.234 -7.845  35.535  1.00 86.91  ? 81   GLU D CG  1 
ATOM   13215 C  CD  . GLU D  1 81  ? -62.861 -6.622  34.890  1.00 93.40  ? 81   GLU D CD  1 
ATOM   13216 O  OE1 . GLU D  1 81  ? -63.410 -6.751  33.772  1.00 95.14  ? 81   GLU D OE1 1 
ATOM   13217 O  OE2 . GLU D  1 81  ? -62.794 -5.530  35.500  1.00 95.86  ? 81   GLU D OE2 1 
ATOM   13218 N  N   . GLY D  1 82  ? -58.957 -8.141  36.484  1.00 68.94  ? 82   GLY D N   1 
ATOM   13219 C  CA  . GLY D  1 82  ? -58.053 -7.110  36.965  1.00 65.86  ? 82   GLY D CA  1 
ATOM   13220 C  C   . GLY D  1 82  ? -56.736 -7.087  36.200  1.00 62.27  ? 82   GLY D C   1 
ATOM   13221 O  O   . GLY D  1 82  ? -56.215 -6.017  35.873  1.00 62.43  ? 82   GLY D O   1 
ATOM   13222 N  N   . THR D  1 83  ? -56.183 -8.272  35.942  1.00 48.83  ? 83   THR D N   1 
ATOM   13223 C  CA  . THR D  1 83  ? -54.987 -8.414  35.113  1.00 45.03  ? 83   THR D CA  1 
ATOM   13224 C  C   . THR D  1 83  ? -55.357 -8.397  33.639  1.00 42.90  ? 83   THR D C   1 
ATOM   13225 O  O   . THR D  1 83  ? -54.668 -7.796  32.809  1.00 42.09  ? 83   THR D O   1 
ATOM   13226 C  CB  . THR D  1 83  ? -54.245 -9.737  35.391  1.00 48.91  ? 83   THR D CB  1 
ATOM   13227 O  OG1 . THR D  1 83  ? -55.118 -10.844 35.131  1.00 48.84  ? 83   THR D OG1 1 
ATOM   13228 C  CG2 . THR D  1 83  ? -53.771 -9.802  36.828  1.00 50.69  ? 83   THR D CG2 1 
ATOM   13229 N  N   . GLU D  1 84  ? -56.453 -9.080  33.328  1.00 37.33  ? 84   GLU D N   1 
ATOM   13230 C  CA  . GLU D  1 84  ? -56.892 -9.286  31.954  1.00 38.17  ? 84   GLU D CA  1 
ATOM   13231 C  C   . GLU D  1 84  ? -57.184 -7.973  31.218  1.00 34.61  ? 84   GLU D C   1 
ATOM   13232 O  O   . GLU D  1 84  ? -56.931 -7.867  30.023  1.00 33.63  ? 84   GLU D O   1 
ATOM   13233 C  CB  . GLU D  1 84  ? -58.123 -10.202 31.938  1.00 62.14  ? 84   GLU D CB  1 
ATOM   13234 C  CG  . GLU D  1 84  ? -58.117 -11.273 30.859  1.00 67.68  ? 84   GLU D CG  1 
ATOM   13235 C  CD  . GLU D  1 84  ? -56.944 -12.220 30.980  1.00 70.52  ? 84   GLU D CD  1 
ATOM   13236 O  OE1 . GLU D  1 84  ? -56.913 -13.021 31.938  1.00 70.71  ? 84   GLU D OE1 1 
ATOM   13237 O  OE2 . GLU D  1 84  ? -56.050 -12.158 30.111  1.00 71.76  ? 84   GLU D OE2 1 
ATOM   13238 N  N   . MET D  1 85  ? -57.704 -6.973  31.928  1.00 44.80  ? 85   MET D N   1 
ATOM   13239 C  CA  . MET D  1 85  ? -58.050 -5.686  31.307  1.00 47.46  ? 85   MET D CA  1 
ATOM   13240 C  C   . MET D  1 85  ? -56.867 -4.989  30.603  1.00 49.21  ? 85   MET D C   1 
ATOM   13241 O  O   . MET D  1 85  ? -57.061 -4.177  29.692  1.00 47.14  ? 85   MET D O   1 
ATOM   13242 C  CB  . MET D  1 85  ? -58.688 -4.739  32.341  1.00 48.80  ? 85   MET D CB  1 
ATOM   13243 C  CG  . MET D  1 85  ? -57.710 -3.798  33.041  1.00 46.39  ? 85   MET D CG  1 
ATOM   13244 S  SD  . MET D  1 85  ? -58.333 -3.024  34.548  1.00 43.45  ? 85   MET D SD  1 
ATOM   13245 C  CE  . MET D  1 85  ? -59.825 -2.202  33.984  1.00 60.78  ? 85   MET D CE  1 
ATOM   13246 N  N   . TRP D  1 86  ? -55.647 -5.293  31.041  1.00 59.56  ? 86   TRP D N   1 
ATOM   13247 C  CA  . TRP D  1 86  ? -54.460 -4.651  30.495  1.00 58.97  ? 86   TRP D CA  1 
ATOM   13248 C  C   . TRP D  1 86  ? -53.842 -5.459  29.368  1.00 61.60  ? 86   TRP D C   1 
ATOM   13249 O  O   . TRP D  1 86  ? -52.943 -4.977  28.674  1.00 65.05  ? 86   TRP D O   1 
ATOM   13250 C  CB  . TRP D  1 86  ? -53.428 -4.428  31.596  1.00 47.15  ? 86   TRP D CB  1 
ATOM   13251 C  CG  . TRP D  1 86  ? -53.958 -3.648  32.772  1.00 46.79  ? 86   TRP D CG  1 
ATOM   13252 C  CD1 . TRP D  1 86  ? -54.196 -4.116  34.039  1.00 46.91  ? 86   TRP D CD1 1 
ATOM   13253 C  CD2 . TRP D  1 86  ? -54.316 -2.267  32.782  1.00 45.88  ? 86   TRP D CD2 1 
ATOM   13254 N  NE1 . TRP D  1 86  ? -54.676 -3.106  34.831  1.00 46.67  ? 86   TRP D NE1 1 
ATOM   13255 C  CE2 . TRP D  1 86  ? -54.761 -1.959  34.080  1.00 47.89  ? 86   TRP D CE2 1 
ATOM   13256 C  CE3 . TRP D  1 86  ? -54.307 -1.256  31.815  1.00 45.04  ? 86   TRP D CE3 1 
ATOM   13257 C  CZ2 . TRP D  1 86  ? -55.195 -0.684  34.435  1.00 50.69  ? 86   TRP D CZ2 1 
ATOM   13258 C  CZ3 . TRP D  1 86  ? -54.741 0.007   32.166  1.00 45.45  ? 86   TRP D CZ3 1 
ATOM   13259 C  CH2 . TRP D  1 86  ? -55.178 0.283   33.463  1.00 48.61  ? 86   TRP D CH2 1 
ATOM   13260 N  N   . ASN D  1 87  ? -54.334 -6.684  29.195  1.00 45.98  ? 87   ASN D N   1 
ATOM   13261 C  CA  . ASN D  1 87  ? -53.836 -7.599  28.167  1.00 42.38  ? 87   ASN D CA  1 
ATOM   13262 C  C   . ASN D  1 87  ? -54.318 -7.227  26.759  1.00 37.51  ? 87   ASN D C   1 
ATOM   13263 O  O   . ASN D  1 87  ? -55.354 -6.566  26.612  1.00 35.11  ? 87   ASN D O   1 
ATOM   13264 C  CB  . ASN D  1 87  ? -54.223 -9.045  28.511  1.00 55.13  ? 87   ASN D CB  1 
ATOM   13265 C  CG  . ASN D  1 87  ? -53.083 -9.822  29.155  1.00 58.68  ? 87   ASN D CG  1 
ATOM   13266 O  OD1 . ASN D  1 87  ? -51.907 -9.487  28.990  1.00 59.91  ? 87   ASN D OD1 1 
ATOM   13267 N  ND2 . ASN D  1 87  ? -53.429 -10.874 29.882  1.00 59.72  ? 87   ASN D ND2 1 
ATOM   13268 N  N   . PRO D  1 88  ? -53.564 -7.641  25.719  1.00 47.42  ? 88   PRO D N   1 
ATOM   13269 C  CA  . PRO D  1 88  ? -53.915 -7.302  24.333  1.00 45.90  ? 88   PRO D CA  1 
ATOM   13270 C  C   . PRO D  1 88  ? -55.330 -7.709  23.982  1.00 43.64  ? 88   PRO D C   1 
ATOM   13271 O  O   . PRO D  1 88  ? -55.682 -8.864  24.186  1.00 45.62  ? 88   PRO D O   1 
ATOM   13272 C  CB  . PRO D  1 88  ? -52.943 -8.153  23.513  1.00 32.32  ? 88   PRO D CB  1 
ATOM   13273 C  CG  . PRO D  1 88  ? -51.765 -8.311  24.388  1.00 31.05  ? 88   PRO D CG  1 
ATOM   13274 C  CD  . PRO D  1 88  ? -52.262 -8.327  25.805  1.00 32.75  ? 88   PRO D CD  1 
ATOM   13275 N  N   . ASN D  1 89  ? -56.125 -6.770  23.480  1.00 30.42  ? 89   ASN D N   1 
ATOM   13276 C  CA  . ASN D  1 89  ? -57.469 -7.082  22.984  1.00 33.49  ? 89   ASN D CA  1 
ATOM   13277 C  C   . ASN D  1 89  ? -57.590 -7.259  21.460  1.00 36.44  ? 89   ASN D C   1 
ATOM   13278 O  O   . ASN D  1 89  ? -58.698 -7.273  20.914  1.00 36.09  ? 89   ASN D O   1 
ATOM   13279 C  CB  . ASN D  1 89  ? -58.566 -6.189  23.585  1.00 40.69  ? 89   ASN D CB  1 
ATOM   13280 C  CG  . ASN D  1 89  ? -58.598 -4.818  22.988  1.00 41.35  ? 89   ASN D CG  1 
ATOM   13281 O  OD1 . ASN D  1 89  ? -57.610 -4.344  22.433  1.00 43.59  ? 89   ASN D OD1 1 
ATOM   13282 N  ND2 . ASN D  1 89  ? -59.741 -4.158  23.104  1.00 40.65  ? 89   ASN D ND2 1 
ATOM   13283 N  N   . ARG D  1 90  ? -56.442 -7.297  20.783  1.00 53.43  ? 90   ARG D N   1 
ATOM   13284 C  CA  . ARG D  1 90  ? -56.375 -7.684  19.375  1.00 53.58  ? 90   ARG D CA  1 
ATOM   13285 C  C   . ARG D  1 90  ? -55.280 -8.717  19.126  1.00 59.13  ? 90   ARG D C   1 
ATOM   13286 O  O   . ARG D  1 90  ? -54.643 -9.212  20.064  1.00 62.62  ? 90   ARG D O   1 
ATOM   13287 C  CB  . ARG D  1 90  ? -56.124 -6.474  18.487  1.00 33.00  ? 90   ARG D CB  1 
ATOM   13288 C  CG  . ARG D  1 90  ? -57.269 -5.507  18.434  1.00 30.63  ? 90   ARG D CG  1 
ATOM   13289 C  CD  . ARG D  1 90  ? -58.468 -6.122  17.747  1.00 32.23  ? 90   ARG D CD  1 
ATOM   13290 N  NE  . ARG D  1 90  ? -59.600 -5.199  17.749  1.00 34.49  ? 90   ARG D NE  1 
ATOM   13291 C  CZ  . ARG D  1 90  ? -60.399 -4.999  18.796  1.00 36.65  ? 90   ARG D CZ  1 
ATOM   13292 N  NH1 . ARG D  1 90  ? -60.189 -5.660  19.934  1.00 33.06  ? 90   ARG D NH1 1 
ATOM   13293 N  NH2 . ARG D  1 90  ? -61.406 -4.132  18.707  1.00 37.83  ? 90   ARG D NH2 1 
ATOM   13294 N  N   . GLU D  1 91  ? -55.078 -9.038  17.849  1.00 43.60  ? 91   GLU D N   1 
ATOM   13295 C  CA  . GLU D  1 91  ? -54.054 -9.983  17.423  1.00 42.99  ? 91   GLU D CA  1 
ATOM   13296 C  C   . GLU D  1 91  ? -52.682 -9.342  17.512  1.00 33.12  ? 91   GLU D C   1 
ATOM   13297 O  O   . GLU D  1 91  ? -52.512 -8.198  17.100  1.00 29.84  ? 91   GLU D O   1 
ATOM   13298 C  CB  . GLU D  1 91  ? -54.319 -10.423 15.985  1.00 74.72  ? 91   GLU D CB  1 
ATOM   13299 C  CG  . GLU D  1 91  ? -55.442 -11.422 15.840  1.00 86.99  ? 91   GLU D CG  1 
ATOM   13300 C  CD  . GLU D  1 91  ? -55.067 -12.793 16.380  1.00 97.95  ? 91   GLU D CD  1 
ATOM   13301 O  OE1 . GLU D  1 91  ? -53.924 -12.961 16.868  1.00 100.65 ? 91   GLU D OE1 1 
ATOM   13302 O  OE2 . GLU D  1 91  ? -55.914 -13.709 16.313  1.00 102.31 ? 91   GLU D OE2 1 
ATOM   13303 N  N   . LEU D  1 92  ? -51.708 -10.065 18.058  1.00 29.78  ? 92   LEU D N   1 
ATOM   13304 C  CA  . LEU D  1 92  ? -50.360 -9.526  18.162  1.00 27.93  ? 92   LEU D CA  1 
ATOM   13305 C  C   . LEU D  1 92  ? -49.805 -9.431  16.775  1.00 27.66  ? 92   LEU D C   1 
ATOM   13306 O  O   . LEU D  1 92  ? -50.111 -10.271 15.953  1.00 28.48  ? 92   LEU D O   1 
ATOM   13307 C  CB  . LEU D  1 92  ? -49.460 -10.452 18.958  1.00 28.15  ? 92   LEU D CB  1 
ATOM   13308 C  CG  . LEU D  1 92  ? -49.714 -10.568 20.449  1.00 28.39  ? 92   LEU D CG  1 
ATOM   13309 C  CD1 . LEU D  1 92  ? -48.438 -11.045 21.151  1.00 28.17  ? 92   LEU D CD1 1 
ATOM   13310 C  CD2 . LEU D  1 92  ? -50.200 -9.236  21.005  1.00 29.73  ? 92   LEU D CD2 1 
ATOM   13311 N  N   . SER D  1 93  ? -49.013 -8.401  16.502  1.00 32.57  ? 93   SER D N   1 
ATOM   13312 C  CA  . SER D  1 93  ? -48.253 -8.332  15.258  1.00 29.22  ? 93   SER D CA  1 
ATOM   13313 C  C   . SER D  1 93  ? -47.077 -7.369  15.362  1.00 30.34  ? 93   SER D C   1 
ATOM   13314 O  O   . SER D  1 93  ? -47.085 -6.456  16.182  1.00 31.16  ? 93   SER D O   1 
ATOM   13315 C  CB  . SER D  1 93  ? -49.152 -7.904  14.111  1.00 29.24  ? 93   SER D CB  1 
ATOM   13316 O  OG  . SER D  1 93  ? -48.371 -7.472  13.021  1.00 29.81  ? 93   SER D OG  1 
ATOM   13317 N  N   . GLU D  1 94  ? -46.072 -7.562  14.516  1.00 25.24  ? 94   GLU D N   1 
ATOM   13318 C  CA  . GLU D  1 94  ? -44.998 -6.596  14.417  1.00 24.38  ? 94   GLU D CA  1 
ATOM   13319 C  C   . GLU D  1 94  ? -45.455 -5.485  13.492  1.00 24.07  ? 94   GLU D C   1 
ATOM   13320 O  O   . GLU D  1 94  ? -44.808 -4.452  13.406  1.00 23.41  ? 94   GLU D O   1 
ATOM   13321 C  CB  . GLU D  1 94  ? -43.729 -7.219  13.850  1.00 28.79  ? 94   GLU D CB  1 
ATOM   13322 C  CG  . GLU D  1 94  ? -42.790 -7.883  14.840  1.00 28.72  ? 94   GLU D CG  1 
ATOM   13323 C  CD  . GLU D  1 94  ? -41.441 -8.239  14.201  1.00 29.03  ? 94   GLU D CD  1 
ATOM   13324 O  OE1 . GLU D  1 94  ? -41.399 -9.163  13.353  1.00 31.19  ? 94   GLU D OE1 1 
ATOM   13325 O  OE2 . GLU D  1 94  ? -40.426 -7.585  14.538  1.00 26.30  ? 94   GLU D OE2 1 
ATOM   13326 N  N   . ASP D  1 95  ? -46.567 -5.689  12.791  1.00 24.66  ? 95   ASP D N   1 
ATOM   13327 C  CA  . ASP D  1 95  ? -47.066 -4.627  11.946  1.00 26.56  ? 95   ASP D CA  1 
ATOM   13328 C  C   . ASP D  1 95  ? -48.169 -4.024  12.799  1.00 24.66  ? 95   ASP D C   1 
ATOM   13329 O  O   . ASP D  1 95  ? -49.365 -4.278  12.604  1.00 25.05  ? 95   ASP D O   1 
ATOM   13330 C  CB  . ASP D  1 95  ? -47.643 -5.312  10.696  1.00 43.22  ? 95   ASP D CB  1 
ATOM   13331 C  CG  . ASP D  1 95  ? -48.363 -4.365  9.762   1.00 49.31  ? 95   ASP D CG  1 
ATOM   13332 O  OD1 . ASP D  1 95  ? -48.225 -3.138  9.933   1.00 54.55  ? 95   ASP D OD1 1 
ATOM   13333 O  OD2 . ASP D  1 95  ? -49.059 -4.858  8.840   1.00 47.80  ? 95   ASP D OD2 1 
ATOM   13334 N  N   . CYS D  1 96  ? -47.731 -3.160  13.714  1.00 27.56  ? 96   CYS D N   1 
ATOM   13335 C  CA  . CYS D  1 96  ? -48.597 -2.478  14.678  1.00 27.93  ? 96   CYS D CA  1 
ATOM   13336 C  C   . CYS D  1 96  ? -48.742 -0.961  14.627  1.00 23.06  ? 96   CYS D C   1 
ATOM   13337 O  O   . CYS D  1 96  ? -49.508 -0.412  15.406  1.00 23.11  ? 96   CYS D O   1 
ATOM   13338 C  CB  . CYS D  1 96  ? -48.283 -2.928  16.104  1.00 35.85  ? 96   CYS D CB  1 
ATOM   13339 S  SG  . CYS D  1 96  ? -46.548 -2.814  16.596  1.00 53.50  ? 96   CYS D SG  1 
ATOM   13340 N  N   . LEU D  1 97  ? -48.027 -0.270  13.745  1.00 25.40  ? 97   LEU D N   1 
ATOM   13341 C  CA  . LEU D  1 97  ? -47.916 1.168   13.934  1.00 22.73  ? 97   LEU D CA  1 
ATOM   13342 C  C   . LEU D  1 97  ? -49.070 1.871   13.249  1.00 25.62  ? 97   LEU D C   1 
ATOM   13343 O  O   . LEU D  1 97  ? -49.047 2.123   12.050  1.00 28.78  ? 97   LEU D O   1 
ATOM   13344 C  CB  . LEU D  1 97  ? -46.599 1.669   13.348  1.00 21.81  ? 97   LEU D CB  1 
ATOM   13345 C  CG  . LEU D  1 97  ? -45.386 1.162   14.113  1.00 21.37  ? 97   LEU D CG  1 
ATOM   13346 C  CD1 . LEU D  1 97  ? -44.112 1.737   13.568  1.00 21.05  ? 97   LEU D CD1 1 
ATOM   13347 C  CD2 . LEU D  1 97  ? -45.541 1.528   15.563  1.00 21.03  ? 97   LEU D CD2 1 
ATOM   13348 N  N   . TYR D  1 98  ? -50.032 2.281   14.068  1.00 29.53  ? 98   TYR D N   1 
ATOM   13349 C  CA  . TYR D  1 98  ? -51.318 2.782   13.615  1.00 32.86  ? 98   TYR D CA  1 
ATOM   13350 C  C   . TYR D  1 98  ? -51.785 3.696   14.726  1.00 38.13  ? 98   TYR D C   1 
ATOM   13351 O  O   . TYR D  1 98  ? -51.317 3.574   15.862  1.00 39.37  ? 98   TYR D O   1 
ATOM   13352 C  CB  . TYR D  1 98  ? -52.332 1.637   13.441  1.00 26.97  ? 98   TYR D CB  1 
ATOM   13353 C  CG  . TYR D  1 98  ? -51.987 0.621   12.356  1.00 27.34  ? 98   TYR D CG  1 
ATOM   13354 C  CD1 . TYR D  1 98  ? -52.362 0.825   11.036  1.00 27.65  ? 98   TYR D CD1 1 
ATOM   13355 C  CD2 . TYR D  1 98  ? -51.293 -0.550  12.658  1.00 27.56  ? 98   TYR D CD2 1 
ATOM   13356 C  CE1 . TYR D  1 98  ? -52.044 -0.097  10.046  1.00 25.50  ? 98   TYR D CE1 1 
ATOM   13357 C  CE2 . TYR D  1 98  ? -50.972 -1.482  11.669  1.00 26.44  ? 98   TYR D CE2 1 
ATOM   13358 C  CZ  . TYR D  1 98  ? -51.352 -1.246  10.368  1.00 25.80  ? 98   TYR D CZ  1 
ATOM   13359 O  OH  . TYR D  1 98  ? -51.046 -2.161  9.388   1.00 25.81  ? 98   TYR D OH  1 
ATOM   13360 N  N   . LEU D  1 99  ? -52.691 4.617   14.415  1.00 32.62  ? 99   LEU D N   1 
ATOM   13361 C  CA  . LEU D  1 99  ? -53.265 5.474   15.448  1.00 29.44  ? 99   LEU D CA  1 
ATOM   13362 C  C   . LEU D  1 99  ? -54.775 5.528   15.290  1.00 29.92  ? 99   LEU D C   1 
ATOM   13363 O  O   . LEU D  1 99  ? -55.310 5.057   14.284  1.00 31.24  ? 99   LEU D O   1 
ATOM   13364 C  CB  . LEU D  1 99  ? -52.606 6.870   15.483  1.00 23.87  ? 99   LEU D CB  1 
ATOM   13365 C  CG  . LEU D  1 99  ? -52.434 7.695   14.199  1.00 24.02  ? 99   LEU D CG  1 
ATOM   13366 C  CD1 . LEU D  1 99  ? -53.689 8.463   13.921  1.00 24.96  ? 99   LEU D CD1 1 
ATOM   13367 C  CD2 . LEU D  1 99  ? -51.240 8.643   14.244  1.00 23.39  ? 99   LEU D CD2 1 
ATOM   13368 N  N   . ASN D  1 100 ? -55.442 6.054   16.312  1.00 28.13  ? 100  ASN D N   1 
ATOM   13369 C  CA  . ASN D  1 100 ? -56.889 6.186   16.376  1.00 31.31  ? 100  ASN D CA  1 
ATOM   13370 C  C   . ASN D  1 100 ? -57.272 7.617   16.709  1.00 33.87  ? 100  ASN D C   1 
ATOM   13371 O  O   . ASN D  1 100 ? -56.561 8.304   17.447  1.00 38.21  ? 100  ASN D O   1 
ATOM   13372 C  CB  . ASN D  1 100 ? -57.444 5.319   17.492  1.00 27.93  ? 100  ASN D CB  1 
ATOM   13373 C  CG  . ASN D  1 100 ? -56.949 3.908   17.438  1.00 28.02  ? 100  ASN D CG  1 
ATOM   13374 O  OD1 . ASN D  1 100 ? -57.000 3.251   16.395  1.00 27.18  ? 100  ASN D OD1 1 
ATOM   13375 N  ND2 . ASN D  1 100 ? -56.481 3.415   18.579  1.00 26.64  ? 100  ASN D ND2 1 
ATOM   13376 N  N   . VAL D  1 101 ? -58.415 8.055   16.204  1.00 34.27  ? 101  VAL D N   1 
ATOM   13377 C  CA  . VAL D  1 101 ? -58.872 9.412   16.428  1.00 35.38  ? 101  VAL D CA  1 
ATOM   13378 C  C   . VAL D  1 101 ? -60.354 9.410   16.765  1.00 39.53  ? 101  VAL D C   1 
ATOM   13379 O  O   . VAL D  1 101 ? -61.142 8.828   16.039  1.00 44.47  ? 101  VAL D O   1 
ATOM   13380 C  CB  . VAL D  1 101 ? -58.697 10.258  15.161  1.00 29.07  ? 101  VAL D CB  1 
ATOM   13381 C  CG1 . VAL D  1 101 ? -59.240 11.639  15.388  1.00 29.88  ? 101  VAL D CG1 1 
ATOM   13382 C  CG2 . VAL D  1 101 ? -57.246 10.332  14.757  1.00 27.85  ? 101  VAL D CG2 1 
ATOM   13383 N  N   . TRP D  1 102 ? -60.742 10.054  17.859  1.00 31.24  ? 102  TRP D N   1 
ATOM   13384 C  CA  . TRP D  1 102 ? -62.154 10.294  18.134  1.00 34.51  ? 102  TRP D CA  1 
ATOM   13385 C  C   . TRP D  1 102 ? -62.456 11.792  18.021  1.00 39.41  ? 102  TRP D C   1 
ATOM   13386 O  O   . TRP D  1 102 ? -61.701 12.618  18.535  1.00 39.46  ? 102  TRP D O   1 
ATOM   13387 C  CB  . TRP D  1 102 ? -62.517 9.812   19.535  1.00 32.79  ? 102  TRP D CB  1 
ATOM   13388 C  CG  . TRP D  1 102 ? -62.610 8.333   19.697  1.00 34.65  ? 102  TRP D CG  1 
ATOM   13389 C  CD1 . TRP D  1 102 ? -63.718 7.559   19.518  1.00 36.82  ? 102  TRP D CD1 1 
ATOM   13390 C  CD2 . TRP D  1 102 ? -61.564 7.444   20.105  1.00 32.87  ? 102  TRP D CD2 1 
ATOM   13391 N  NE1 . TRP D  1 102 ? -63.428 6.237   19.780  1.00 35.45  ? 102  TRP D NE1 1 
ATOM   13392 C  CE2 . TRP D  1 102 ? -62.112 6.142   20.141  1.00 33.89  ? 102  TRP D CE2 1 
ATOM   13393 C  CE3 . TRP D  1 102 ? -60.219 7.619   20.435  1.00 32.82  ? 102  TRP D CE3 1 
ATOM   13394 C  CZ2 . TRP D  1 102 ? -61.358 5.025   20.497  1.00 35.19  ? 102  TRP D CZ2 1 
ATOM   13395 C  CZ3 . TRP D  1 102 ? -59.470 6.508   20.790  1.00 33.00  ? 102  TRP D CZ3 1 
ATOM   13396 C  CH2 . TRP D  1 102 ? -60.042 5.229   20.818  1.00 34.77  ? 102  TRP D CH2 1 
ATOM   13397 N  N   . THR D  1 103 ? -63.545 12.151  17.342  1.00 46.87  ? 103  THR D N   1 
ATOM   13398 C  CA  . THR D  1 103 ? -63.998 13.546  17.299  1.00 48.15  ? 103  THR D CA  1 
ATOM   13399 C  C   . THR D  1 103 ? -65.512 13.586  17.471  1.00 53.45  ? 103  THR D C   1 
ATOM   13400 O  O   . THR D  1 103 ? -66.171 12.551  17.371  1.00 54.17  ? 103  THR D O   1 
ATOM   13401 C  CB  . THR D  1 103 ? -63.619 14.262  15.981  1.00 40.33  ? 103  THR D CB  1 
ATOM   13402 O  OG1 . THR D  1 103 ? -64.394 13.724  14.916  1.00 41.54  ? 103  THR D OG1 1 
ATOM   13403 C  CG2 . THR D  1 103 ? -62.155 14.107  15.661  1.00 39.02  ? 103  THR D CG2 1 
ATOM   13404 N  N   . PRO D  1 104 ? -66.067 14.774  17.762  1.00 71.50  ? 104  PRO D N   1 
ATOM   13405 C  CA  . PRO D  1 104 ? -67.524 14.945  17.856  1.00 77.80  ? 104  PRO D CA  1 
ATOM   13406 C  C   . PRO D  1 104 ? -68.257 14.677  16.541  1.00 82.46  ? 104  PRO D C   1 
ATOM   13407 O  O   . PRO D  1 104 ? -67.679 14.871  15.473  1.00 86.13  ? 104  PRO D O   1 
ATOM   13408 C  CB  . PRO D  1 104 ? -67.670 16.425  18.206  1.00 62.80  ? 104  PRO D CB  1 
ATOM   13409 C  CG  . PRO D  1 104 ? -66.399 16.780  18.883  1.00 59.55  ? 104  PRO D CG  1 
ATOM   13410 C  CD  . PRO D  1 104 ? -65.344 15.973  18.218  1.00 55.91  ? 104  PRO D CD  1 
ATOM   13411 N  N   . TYR D  1 105 ? -69.508 14.234  16.620  1.00 65.77  ? 105  TYR D N   1 
ATOM   13412 C  CA  . TYR D  1 105 ? -70.338 14.083  15.426  1.00 68.92  ? 105  TYR D CA  1 
ATOM   13413 C  C   . TYR D  1 105 ? -71.532 15.025  15.535  1.00 74.43  ? 105  TYR D C   1 
ATOM   13414 O  O   . TYR D  1 105 ? -72.409 14.815  16.370  1.00 79.09  ? 105  TYR D O   1 
ATOM   13415 C  CB  . TYR D  1 105 ? -70.809 12.632  15.286  1.00 71.73  ? 105  TYR D CB  1 
ATOM   13416 C  CG  . TYR D  1 105 ? -71.599 12.310  14.030  1.00 71.43  ? 105  TYR D CG  1 
ATOM   13417 C  CD1 . TYR D  1 105 ? -72.912 12.730  13.884  1.00 73.85  ? 105  TYR D CD1 1 
ATOM   13418 C  CD2 . TYR D  1 105 ? -71.042 11.547  13.010  1.00 70.15  ? 105  TYR D CD2 1 
ATOM   13419 C  CE1 . TYR D  1 105 ? -73.641 12.430  12.748  1.00 76.21  ? 105  TYR D CE1 1 
ATOM   13420 C  CE2 . TYR D  1 105 ? -71.764 11.238  11.868  1.00 72.25  ? 105  TYR D CE2 1 
ATOM   13421 C  CZ  . TYR D  1 105 ? -73.067 11.684  11.741  1.00 74.96  ? 105  TYR D CZ  1 
ATOM   13422 O  OH  . TYR D  1 105 ? -73.809 11.391  10.613  1.00 74.72  ? 105  TYR D OH  1 
ATOM   13423 N  N   . PRO D  1 106 ? -71.598 16.052  14.674  1.00 77.98  ? 106  PRO D N   1 
ATOM   13424 C  CA  . PRO D  1 106 ? -70.741 16.361  13.530  1.00 78.25  ? 106  PRO D CA  1 
ATOM   13425 C  C   . PRO D  1 106 ? -69.378 16.910  13.925  1.00 78.98  ? 106  PRO D C   1 
ATOM   13426 O  O   . PRO D  1 106 ? -69.173 17.337  15.068  1.00 78.33  ? 106  PRO D O   1 
ATOM   13427 C  CB  . PRO D  1 106 ? -71.524 17.457  12.814  1.00 67.17  ? 106  PRO D CB  1 
ATOM   13428 C  CG  . PRO D  1 106 ? -72.191 18.187  13.918  1.00 66.95  ? 106  PRO D CG  1 
ATOM   13429 C  CD  . PRO D  1 106 ? -72.598 17.113  14.894  1.00 67.22  ? 106  PRO D CD  1 
ATOM   13430 N  N   . ARG D  1 107 ? -68.470 16.900  12.950  1.00 58.64  ? 107  ARG D N   1 
ATOM   13431 C  CA  . ARG D  1 107 ? -67.111 17.390  13.103  1.00 57.45  ? 107  ARG D CA  1 
ATOM   13432 C  C   . ARG D  1 107 ? -67.161 18.796  13.715  1.00 53.69  ? 107  ARG D C   1 
ATOM   13433 O  O   . ARG D  1 107 ? -68.089 19.559  13.442  1.00 47.67  ? 107  ARG D O   1 
ATOM   13434 C  CB  . ARG D  1 107 ? -66.435 17.400  11.722  1.00 93.18  ? 107  ARG D CB  1 
ATOM   13435 C  CG  . ARG D  1 107 ? -64.915 17.380  11.726  1.00 98.09  ? 107  ARG D CG  1 
ATOM   13436 C  CD  . ARG D  1 107 ? -64.332 18.530  10.891  1.00 105.30 ? 107  ARG D CD  1 
ATOM   13437 N  NE  . ARG D  1 107 ? -64.348 18.259  9.451   1.00 110.99 ? 107  ARG D NE  1 
ATOM   13438 C  CZ  . ARG D  1 107 ? -63.832 19.068  8.525   1.00 112.60 ? 107  ARG D CZ  1 
ATOM   13439 N  NH1 . ARG D  1 107 ? -63.255 20.214  8.877   1.00 112.11 ? 107  ARG D NH1 1 
ATOM   13440 N  NH2 . ARG D  1 107 ? -63.892 18.729  7.240   1.00 112.39 ? 107  ARG D NH2 1 
ATOM   13441 N  N   . PRO D  1 108 ? -66.189 19.122  14.587  1.00 82.73  ? 108  PRO D N   1 
ATOM   13442 C  CA  . PRO D  1 108 ? -66.126 20.426  15.256  1.00 86.11  ? 108  PRO D CA  1 
ATOM   13443 C  C   . PRO D  1 108 ? -66.127 21.604  14.293  1.00 87.97  ? 108  PRO D C   1 
ATOM   13444 O  O   . PRO D  1 108 ? -65.397 21.596  13.293  1.00 86.92  ? 108  PRO D O   1 
ATOM   13445 C  CB  . PRO D  1 108 ? -64.789 20.370  15.993  1.00 80.65  ? 108  PRO D CB  1 
ATOM   13446 C  CG  . PRO D  1 108 ? -64.602 18.942  16.286  1.00 80.01  ? 108  PRO D CG  1 
ATOM   13447 C  CD  . PRO D  1 108 ? -65.167 18.198  15.109  1.00 79.67  ? 108  PRO D CD  1 
ATOM   13448 N  N   . ALA D  1 109 ? -66.946 22.604  14.613  1.00 86.85  ? 109  ALA D N   1 
ATOM   13449 C  CA  . ALA D  1 109 ? -67.025 23.845  13.850  1.00 86.65  ? 109  ALA D CA  1 
ATOM   13450 C  C   . ALA D  1 109 ? -65.686 24.570  13.844  1.00 85.31  ? 109  ALA D C   1 
ATOM   13451 O  O   . ALA D  1 109 ? -65.201 25.011  12.804  1.00 84.61  ? 109  ALA D O   1 
ATOM   13452 C  CB  . ALA D  1 109 ? -68.100 24.749  14.436  1.00 81.03  ? 109  ALA D CB  1 
ATOM   13453 N  N   . SER D  1 110 ? -65.086 24.670  15.022  1.00 91.15  ? 110  SER D N   1 
ATOM   13454 C  CA  . SER D  1 110 ? -63.859 25.427  15.207  1.00 87.51  ? 110  SER D CA  1 
ATOM   13455 C  C   . SER D  1 110 ? -62.749 24.508  15.722  1.00 82.62  ? 110  SER D C   1 
ATOM   13456 O  O   . SER D  1 110 ? -63.026 23.459  16.299  1.00 82.85  ? 110  SER D O   1 
ATOM   13457 C  CB  . SER D  1 110 ? -64.140 26.569  16.181  1.00 74.82  ? 110  SER D CB  1 
ATOM   13458 O  OG  . SER D  1 110 ? -65.487 27.002  16.036  1.00 75.59  ? 110  SER D OG  1 
ATOM   13459 N  N   . PRO D  1 111 ? -61.487 24.909  15.541  1.00 74.11  ? 111  PRO D N   1 
ATOM   13460 C  CA  . PRO D  1 111 ? -60.341 24.034  15.832  1.00 71.39  ? 111  PRO D CA  1 
ATOM   13461 C  C   . PRO D  1 111 ? -60.193 23.607  17.302  1.00 69.99  ? 111  PRO D C   1 
ATOM   13462 O  O   . PRO D  1 111 ? -59.418 24.172  18.077  1.00 71.10  ? 111  PRO D O   1 
ATOM   13463 C  CB  . PRO D  1 111 ? -59.127 24.857  15.364  1.00 60.38  ? 111  PRO D CB  1 
ATOM   13464 C  CG  . PRO D  1 111 ? -59.657 26.225  15.072  1.00 62.48  ? 111  PRO D CG  1 
ATOM   13465 C  CD  . PRO D  1 111 ? -61.090 26.049  14.706  1.00 63.64  ? 111  PRO D CD  1 
ATOM   13466 N  N   . THR D  1 112 ? -60.989 22.604  17.658  1.00 61.74  ? 112  THR D N   1 
ATOM   13467 C  CA  . THR D  1 112 ? -60.959 21.941  18.957  1.00 57.70  ? 112  THR D CA  1 
ATOM   13468 C  C   . THR D  1 112 ? -59.559 21.498  19.410  1.00 53.98  ? 112  THR D C   1 
ATOM   13469 O  O   . THR D  1 112 ? -58.769 21.013  18.603  1.00 54.50  ? 112  THR D O   1 
ATOM   13470 C  CB  . THR D  1 112 ? -61.866 20.689  18.894  1.00 56.80  ? 112  THR D CB  1 
ATOM   13471 O  OG1 . THR D  1 112 ? -63.244 21.086  18.964  1.00 59.89  ? 112  THR D OG1 1 
ATOM   13472 C  CG2 . THR D  1 112 ? -61.555 19.718  20.014  1.00 54.15  ? 112  THR D CG2 1 
ATOM   13473 N  N   . PRO D  1 113 ? -59.247 21.692  20.707  1.00 49.11  ? 113  PRO D N   1 
ATOM   13474 C  CA  . PRO D  1 113 ? -58.064 21.166  21.391  1.00 44.57  ? 113  PRO D CA  1 
ATOM   13475 C  C   . PRO D  1 113 ? -57.919 19.646  21.304  1.00 43.50  ? 113  PRO D C   1 
ATOM   13476 O  O   . PRO D  1 113 ? -58.884 18.892  21.483  1.00 42.65  ? 113  PRO D O   1 
ATOM   13477 C  CB  . PRO D  1 113 ? -58.305 21.573  22.842  1.00 35.69  ? 113  PRO D CB  1 
ATOM   13478 C  CG  . PRO D  1 113 ? -59.013 22.833  22.731  1.00 38.57  ? 113  PRO D CG  1 
ATOM   13479 C  CD  . PRO D  1 113 ? -59.953 22.658  21.561  1.00 41.99  ? 113  PRO D CD  1 
ATOM   13480 N  N   . VAL D  1 114 ? -56.679 19.220  21.066  1.00 35.22  ? 114  VAL D N   1 
ATOM   13481 C  CA  . VAL D  1 114 ? -56.329 17.828  20.841  1.00 32.25  ? 114  VAL D CA  1 
ATOM   13482 C  C   . VAL D  1 114 ? -55.589 17.230  22.034  1.00 31.84  ? 114  VAL D C   1 
ATOM   13483 O  O   . VAL D  1 114 ? -54.654 17.841  22.576  1.00 27.97  ? 114  VAL D O   1 
ATOM   13484 C  CB  . VAL D  1 114 ? -55.453 17.716  19.596  1.00 28.56  ? 114  VAL D CB  1 
ATOM   13485 C  CG1 . VAL D  1 114 ? -54.656 16.427  19.604  1.00 32.25  ? 114  VAL D CG1 1 
ATOM   13486 C  CG2 . VAL D  1 114 ? -56.309 17.827  18.357  1.00 29.41  ? 114  VAL D CG2 1 
ATOM   13487 N  N   . LEU D  1 115 ? -56.038 16.039  22.437  1.00 36.07  ? 115  LEU D N   1 
ATOM   13488 C  CA  . LEU D  1 115 ? -55.449 15.275  23.536  1.00 33.74  ? 115  LEU D CA  1 
ATOM   13489 C  C   . LEU D  1 115 ? -54.907 13.975  22.992  1.00 33.24  ? 115  LEU D C   1 
ATOM   13490 O  O   . LEU D  1 115 ? -55.678 13.095  22.593  1.00 33.11  ? 115  LEU D O   1 
ATOM   13491 C  CB  . LEU D  1 115 ? -56.507 14.940  24.592  1.00 28.48  ? 115  LEU D CB  1 
ATOM   13492 C  CG  . LEU D  1 115 ? -56.892 16.084  25.528  1.00 31.05  ? 115  LEU D CG  1 
ATOM   13493 C  CD1 . LEU D  1 115 ? -58.135 15.801  26.376  1.00 30.68  ? 115  LEU D CD1 1 
ATOM   13494 C  CD2 . LEU D  1 115 ? -55.693 16.346  26.395  1.00 31.56  ? 115  LEU D CD2 1 
ATOM   13495 N  N   . ILE D  1 116 ? -53.582 13.850  22.994  1.00 26.22  ? 116  ILE D N   1 
ATOM   13496 C  CA  . ILE D  1 116 ? -52.921 12.644  22.516  1.00 24.60  ? 116  ILE D CA  1 
ATOM   13497 C  C   . ILE D  1 116 ? -52.536 11.783  23.703  1.00 24.18  ? 116  ILE D C   1 
ATOM   13498 O  O   . ILE D  1 116 ? -51.862 12.243  24.618  1.00 23.89  ? 116  ILE D O   1 
ATOM   13499 C  CB  . ILE D  1 116 ? -51.678 12.983  21.711  1.00 23.81  ? 116  ILE D CB  1 
ATOM   13500 C  CG1 . ILE D  1 116 ? -52.047 13.874  20.526  1.00 24.34  ? 116  ILE D CG1 1 
ATOM   13501 C  CG2 . ILE D  1 116 ? -51.018 11.724  21.231  1.00 23.06  ? 116  ILE D CG2 1 
ATOM   13502 C  CD1 . ILE D  1 116 ? -50.845 14.415  19.779  1.00 23.78  ? 116  ILE D CD1 1 
ATOM   13503 N  N   . TRP D  1 117 ? -52.984 10.537  23.689  1.00 24.26  ? 117  TRP D N   1 
ATOM   13504 C  CA  . TRP D  1 117 ? -52.767 9.625   24.801  1.00 24.09  ? 117  TRP D CA  1 
ATOM   13505 C  C   . TRP D  1 117 ? -51.707 8.571   24.482  1.00 23.96  ? 117  TRP D C   1 
ATOM   13506 O  O   . TRP D  1 117 ? -51.677 8.001   23.376  1.00 23.03  ? 117  TRP D O   1 
ATOM   13507 C  CB  . TRP D  1 117 ? -54.077 8.934   25.165  1.00 25.06  ? 117  TRP D CB  1 
ATOM   13508 C  CG  . TRP D  1 117 ? -53.922 7.698   26.013  1.00 24.99  ? 117  TRP D CG  1 
ATOM   13509 C  CD1 . TRP D  1 117 ? -53.908 6.393   25.587  1.00 26.04  ? 117  TRP D CD1 1 
ATOM   13510 C  CD2 . TRP D  1 117 ? -53.790 7.654   27.429  1.00 25.16  ? 117  TRP D CD2 1 
ATOM   13511 N  NE1 . TRP D  1 117 ? -53.764 5.546   26.659  1.00 25.02  ? 117  TRP D NE1 1 
ATOM   13512 C  CE2 . TRP D  1 117 ? -53.690 6.299   27.801  1.00 25.95  ? 117  TRP D CE2 1 
ATOM   13513 C  CE3 . TRP D  1 117 ? -53.737 8.632   28.422  1.00 25.40  ? 117  TRP D CE3 1 
ATOM   13514 C  CZ2 . TRP D  1 117 ? -53.537 5.903   29.120  1.00 25.74  ? 117  TRP D CZ2 1 
ATOM   13515 C  CZ3 . TRP D  1 117 ? -53.586 8.242   29.730  1.00 25.59  ? 117  TRP D CZ3 1 
ATOM   13516 C  CH2 . TRP D  1 117 ? -53.485 6.889   30.071  1.00 25.58  ? 117  TRP D CH2 1 
ATOM   13517 N  N   . ILE D  1 118 ? -50.837 8.310   25.456  1.00 28.22  ? 118  ILE D N   1 
ATOM   13518 C  CA  . ILE D  1 118 ? -49.781 7.325   25.294  1.00 26.00  ? 118  ILE D CA  1 
ATOM   13519 C  C   . ILE D  1 118 ? -49.913 6.296   26.401  1.00 25.40  ? 118  ILE D C   1 
ATOM   13520 O  O   . ILE D  1 118 ? -49.840 6.646   27.575  1.00 25.38  ? 118  ILE D O   1 
ATOM   13521 C  CB  . ILE D  1 118 ? -48.412 7.989   25.357  1.00 21.23  ? 118  ILE D CB  1 
ATOM   13522 C  CG1 . ILE D  1 118 ? -48.321 9.073   24.301  1.00 21.16  ? 118  ILE D CG1 1 
ATOM   13523 C  CG2 . ILE D  1 118 ? -47.339 6.982   25.114  1.00 20.64  ? 118  ILE D CG2 1 
ATOM   13524 C  CD1 . ILE D  1 118 ? -47.112 9.865   24.412  1.00 31.93  ? 118  ILE D CD1 1 
ATOM   13525 N  N   . TYR D  1 119 ? -50.129 5.033   26.036  1.00 22.39  ? 119  TYR D N   1 
ATOM   13526 C  CA  . TYR D  1 119 ? -50.325 3.986   27.043  1.00 24.21  ? 119  TYR D CA  1 
ATOM   13527 C  C   . TYR D  1 119 ? -49.060 3.590   27.811  1.00 22.25  ? 119  TYR D C   1 
ATOM   13528 O  O   . TYR D  1 119 ? -47.949 3.792   27.341  1.00 21.51  ? 119  TYR D O   1 
ATOM   13529 C  CB  . TYR D  1 119 ? -50.977 2.744   26.431  1.00 25.53  ? 119  TYR D CB  1 
ATOM   13530 C  CG  . TYR D  1 119 ? -50.261 2.187   25.231  1.00 26.77  ? 119  TYR D CG  1 
ATOM   13531 C  CD1 . TYR D  1 119 ? -49.206 1.290   25.375  1.00 29.10  ? 119  TYR D CD1 1 
ATOM   13532 C  CD2 . TYR D  1 119 ? -50.649 2.539   23.953  1.00 27.13  ? 119  TYR D CD2 1 
ATOM   13533 C  CE1 . TYR D  1 119 ? -48.547 0.765   24.269  1.00 29.03  ? 119  TYR D CE1 1 
ATOM   13534 C  CE2 . TYR D  1 119 ? -50.004 2.019   22.846  1.00 29.28  ? 119  TYR D CE2 1 
ATOM   13535 C  CZ  . TYR D  1 119 ? -48.953 1.136   23.006  1.00 29.90  ? 119  TYR D CZ  1 
ATOM   13536 O  OH  . TYR D  1 119 ? -48.318 0.635   21.891  1.00 30.55  ? 119  TYR D OH  1 
ATOM   13537 N  N   . GLY D  1 120 ? -49.255 3.024   28.997  1.00 33.22  ? 120  GLY D N   1 
ATOM   13538 C  CA  . GLY D  1 120 ? -48.180 2.513   29.828  1.00 22.41  ? 120  GLY D CA  1 
ATOM   13539 C  C   . GLY D  1 120 ? -48.003 1.030   29.571  1.00 40.43  ? 120  GLY D C   1 
ATOM   13540 O  O   . GLY D  1 120 ? -48.239 0.573   28.455  1.00 22.63  ? 120  GLY D O   1 
ATOM   13541 N  N   . GLY D  1 121 ? -47.626 0.263   30.592  1.00 22.94  ? 121  GLY D N   1 
ATOM   13542 C  CA  . GLY D  1 121 ? -47.245 -1.121  30.367  1.00 23.17  ? 121  GLY D CA  1 
ATOM   13543 C  C   . GLY D  1 121 ? -45.749 -1.401  30.381  1.00 22.58  ? 121  GLY D C   1 
ATOM   13544 O  O   . GLY D  1 121 ? -45.289 -2.383  29.819  1.00 23.32  ? 121  GLY D O   1 
ATOM   13545 N  N   . GLY D  1 122 ? -44.972 -0.506  30.971  1.00 22.06  ? 122  GLY D N   1 
ATOM   13546 C  CA  . GLY D  1 122 ? -43.584 -0.795  31.295  1.00 21.72  ? 122  GLY D CA  1 
ATOM   13547 C  C   . GLY D  1 122 ? -42.677 -0.873  30.099  1.00 21.17  ? 122  GLY D C   1 
ATOM   13548 O  O   . GLY D  1 122 ? -41.579 -1.400  30.168  1.00 21.09  ? 122  GLY D O   1 
ATOM   13549 N  N   . PHE D  1 123 ? -43.164 -0.337  28.995  1.00 24.96  ? 123  PHE D N   1 
ATOM   13550 C  CA  . PHE D  1 123 ? -42.511 -0.423  27.700  1.00 24.94  ? 123  PHE D CA  1 
ATOM   13551 C  C   . PHE D  1 123 ? -42.319 -1.872  27.279  1.00 23.54  ? 123  PHE D C   1 
ATOM   13552 O  O   . PHE D  1 123 ? -41.584 -2.137  26.334  1.00 21.72  ? 123  PHE D O   1 
ATOM   13553 C  CB  . PHE D  1 123 ? -41.114 0.224   27.725  1.00 19.94  ? 123  PHE D CB  1 
ATOM   13554 C  CG  . PHE D  1 123 ? -41.080 1.659   28.205  1.00 19.57  ? 123  PHE D CG  1 
ATOM   13555 C  CD1 . PHE D  1 123 ? -41.425 2.703   27.364  1.00 19.27  ? 123  PHE D CD1 1 
ATOM   13556 C  CD2 . PHE D  1 123 ? -40.635 1.968   29.477  1.00 19.60  ? 123  PHE D CD2 1 
ATOM   13557 C  CE1 . PHE D  1 123 ? -41.350 4.017   27.801  1.00 19.06  ? 123  PHE D CE1 1 
ATOM   13558 C  CE2 . PHE D  1 123 ? -40.569 3.283   29.906  1.00 19.35  ? 123  PHE D CE2 1 
ATOM   13559 C  CZ  . PHE D  1 123 ? -40.922 4.298   29.069  1.00 19.10  ? 123  PHE D CZ  1 
ATOM   13560 N  N   . TYR D  1 124 ? -42.961 -2.816  27.958  1.00 21.66  ? 124  TYR D N   1 
ATOM   13561 C  CA  . TYR D  1 124 ? -42.991 -4.174  27.438  1.00 22.26  ? 124  TYR D CA  1 
ATOM   13562 C  C   . TYR D  1 124 ? -44.340 -4.592  26.894  1.00 22.81  ? 124  TYR D C   1 
ATOM   13563 O  O   . TYR D  1 124 ? -44.479 -5.697  26.395  1.00 23.40  ? 124  TYR D O   1 
ATOM   13564 C  CB  . TYR D  1 124 ? -42.454 -5.198  28.437  1.00 29.41  ? 124  TYR D CB  1 
ATOM   13565 C  CG  . TYR D  1 124 ? -43.295 -5.341  29.665  1.00 29.95  ? 124  TYR D CG  1 
ATOM   13566 C  CD1 . TYR D  1 124 ? -43.057 -4.552  30.760  1.00 30.15  ? 124  TYR D CD1 1 
ATOM   13567 C  CD2 . TYR D  1 124 ? -44.332 -6.269  29.730  1.00 32.08  ? 124  TYR D CD2 1 
ATOM   13568 C  CE1 . TYR D  1 124 ? -43.817 -4.666  31.890  1.00 35.01  ? 124  TYR D CE1 1 
ATOM   13569 C  CE2 . TYR D  1 124 ? -45.108 -6.394  30.870  1.00 35.54  ? 124  TYR D CE2 1 
ATOM   13570 C  CZ  . TYR D  1 124 ? -44.836 -5.577  31.955  1.00 39.88  ? 124  TYR D CZ  1 
ATOM   13571 O  OH  . TYR D  1 124 ? -45.564 -5.630  33.129  1.00 46.31  ? 124  TYR D OH  1 
ATOM   13572 N  N   . SER D  1 125 ? -45.338 -3.729  27.002  1.00 25.41  ? 125  SER D N   1 
ATOM   13573 C  CA  . SER D  1 125 ? -46.699 -4.158  26.731  1.00 23.47  ? 125  SER D CA  1 
ATOM   13574 C  C   . SER D  1 125 ? -47.628 -2.991  26.492  1.00 23.30  ? 125  SER D C   1 
ATOM   13575 O  O   . SER D  1 125 ? -47.228 -1.834  26.535  1.00 22.61  ? 125  SER D O   1 
ATOM   13576 C  CB  . SER D  1 125 ? -47.226 -4.969  27.906  1.00 24.38  ? 125  SER D CB  1 
ATOM   13577 O  OG  . SER D  1 125 ? -47.371 -4.159  29.056  1.00 24.28  ? 125  SER D OG  1 
ATOM   13578 N  N   . GLY D  1 126 ? -48.887 -3.304  26.245  1.00 24.05  ? 126  GLY D N   1 
ATOM   13579 C  CA  . GLY D  1 126 ? -49.875 -2.272  26.039  1.00 24.11  ? 126  GLY D CA  1 
ATOM   13580 C  C   . GLY D  1 126 ? -50.298 -2.132  24.595  1.00 24.08  ? 126  GLY D C   1 
ATOM   13581 O  O   . GLY D  1 126 ? -49.732 -2.763  23.703  1.00 23.91  ? 126  GLY D O   1 
ATOM   13582 N  N   . ALA D  1 127 ? -51.312 -1.297  24.390  1.00 24.35  ? 127  ALA D N   1 
ATOM   13583 C  CA  . ALA D  1 127 ? -51.856 -0.996  23.082  1.00 24.44  ? 127  ALA D CA  1 
ATOM   13584 C  C   . ALA D  1 127 ? -52.956 0.003   23.294  1.00 27.26  ? 127  ALA D C   1 
ATOM   13585 O  O   . ALA D  1 127 ? -53.589 0.005   24.339  1.00 25.49  ? 127  ALA D O   1 
ATOM   13586 C  CB  . ALA D  1 127 ? -52.444 -2.230  22.480  1.00 35.14  ? 127  ALA D CB  1 
ATOM   13587 N  N   . ALA D  1 128 ? -53.257 0.776   22.259  1.00 38.47  ? 128  ALA D N   1 
ATOM   13588 C  CA  . ALA D  1 128 ? -54.182 1.888   22.394  1.00 40.03  ? 128  ALA D CA  1 
ATOM   13589 C  C   . ALA D  1 128 ? -55.626 1.421   22.260  1.00 40.20  ? 128  ALA D C   1 
ATOM   13590 O  O   . ALA D  1 128 ? -56.559 2.201   22.443  1.00 43.14  ? 128  ALA D O   1 
ATOM   13591 C  CB  . ALA D  1 128 ? -53.865 2.974   21.374  1.00 24.71  ? 128  ALA D CB  1 
ATOM   13592 N  N   . SER D  1 129 ? -55.809 0.139   21.963  1.00 26.91  ? 129  SER D N   1 
ATOM   13593 C  CA  . SER D  1 129 ? -57.138 -0.372  21.660  1.00 28.16  ? 129  SER D CA  1 
ATOM   13594 C  C   . SER D  1 129 ? -57.870 -0.932  22.875  1.00 29.16  ? 129  SER D C   1 
ATOM   13595 O  O   . SER D  1 129 ? -59.007 -1.377  22.760  1.00 30.38  ? 129  SER D O   1 
ATOM   13596 C  CB  . SER D  1 129 ? -57.081 -1.398  20.518  1.00 32.99  ? 129  SER D CB  1 
ATOM   13597 O  OG  . SER D  1 129 ? -56.148 -2.435  20.758  1.00 31.72  ? 129  SER D OG  1 
ATOM   13598 N  N   . LEU D  1 130 ? -57.222 -0.884  24.036  1.00 38.41  ? 130  LEU D N   1 
ATOM   13599 C  CA  . LEU D  1 130 ? -57.806 -1.370  25.289  1.00 40.29  ? 130  LEU D CA  1 
ATOM   13600 C  C   . LEU D  1 130 ? -59.104 -0.645  25.605  1.00 44.78  ? 130  LEU D C   1 
ATOM   13601 O  O   . LEU D  1 130 ? -59.275 0.517   25.229  1.00 47.94  ? 130  LEU D O   1 
ATOM   13602 C  CB  . LEU D  1 130 ? -56.829 -1.158  26.442  1.00 33.59  ? 130  LEU D CB  1 
ATOM   13603 C  CG  . LEU D  1 130 ? -55.513 -1.909  26.329  1.00 28.07  ? 130  LEU D CG  1 
ATOM   13604 C  CD1 . LEU D  1 130 ? -54.644 -1.491  27.451  1.00 33.78  ? 130  LEU D CD1 1 
ATOM   13605 C  CD2 . LEU D  1 130 ? -55.747 -3.393  26.399  1.00 29.68  ? 130  LEU D CD2 1 
ATOM   13606 N  N   . ASP D  1 131 ? -60.017 -1.326  26.292  1.00 42.13  ? 131  ASP D N   1 
ATOM   13607 C  CA  . ASP D  1 131 ? -61.319 -0.734  26.594  1.00 44.17  ? 131  ASP D CA  1 
ATOM   13608 C  C   . ASP D  1 131 ? -61.226 0.511   27.485  1.00 45.81  ? 131  ASP D C   1 
ATOM   13609 O  O   . ASP D  1 131 ? -62.026 1.438   27.361  1.00 48.10  ? 131  ASP D O   1 
ATOM   13610 C  CB  . ASP D  1 131 ? -62.270 -1.767  27.198  1.00 44.84  ? 131  ASP D CB  1 
ATOM   13611 C  CG  . ASP D  1 131 ? -62.805 -2.737  26.166  1.00 47.43  ? 131  ASP D CG  1 
ATOM   13612 O  OD1 . ASP D  1 131 ? -63.010 -2.321  24.999  1.00 46.53  ? 131  ASP D OD1 1 
ATOM   13613 O  OD2 . ASP D  1 131 ? -63.018 -3.918  26.523  1.00 49.63  ? 131  ASP D OD2 1 
ATOM   13614 N  N   . VAL D  1 132 ? -60.240 0.542   28.371  1.00 40.92  ? 132  VAL D N   1 
ATOM   13615 C  CA  . VAL D  1 132 ? -60.098 1.663   29.292  1.00 39.99  ? 132  VAL D CA  1 
ATOM   13616 C  C   . VAL D  1 132 ? -59.703 2.958   28.580  1.00 42.18  ? 132  VAL D C   1 
ATOM   13617 O  O   . VAL D  1 132 ? -59.900 4.047   29.111  1.00 43.58  ? 132  VAL D O   1 
ATOM   13618 C  CB  . VAL D  1 132 ? -59.055 1.359   30.366  1.00 31.62  ? 132  VAL D CB  1 
ATOM   13619 C  CG1 . VAL D  1 132 ? -59.402 2.091   31.625  1.00 32.31  ? 132  VAL D CG1 1 
ATOM   13620 C  CG2 . VAL D  1 132 ? -58.998 -0.132  30.638  1.00 32.09  ? 132  VAL D CG2 1 
ATOM   13621 N  N   . TYR D  1 133 ? -59.138 2.831   27.381  1.00 47.13  ? 133  TYR D N   1 
ATOM   13622 C  CA  . TYR D  1 133 ? -58.653 3.985   26.620  1.00 45.24  ? 133  TYR D CA  1 
ATOM   13623 C  C   . TYR D  1 133 ? -59.659 4.499   25.601  1.00 46.96  ? 133  TYR D C   1 
ATOM   13624 O  O   . TYR D  1 133 ? -59.316 5.349   24.785  1.00 46.90  ? 133  TYR D O   1 
ATOM   13625 C  CB  . TYR D  1 133 ? -57.317 3.697   25.927  1.00 30.93  ? 133  TYR D CB  1 
ATOM   13626 C  CG  . TYR D  1 133 ? -56.224 3.152   26.832  1.00 30.63  ? 133  TYR D CG  1 
ATOM   13627 C  CD1 . TYR D  1 133 ? -56.217 3.399   28.206  1.00 30.74  ? 133  TYR D CD1 1 
ATOM   13628 C  CD2 . TYR D  1 133 ? -55.208 2.377   26.306  1.00 26.54  ? 133  TYR D CD2 1 
ATOM   13629 C  CE1 . TYR D  1 133 ? -55.223 2.879   29.017  1.00 27.14  ? 133  TYR D CE1 1 
ATOM   13630 C  CE2 . TYR D  1 133 ? -54.219 1.867   27.097  1.00 30.92  ? 133  TYR D CE2 1 
ATOM   13631 C  CZ  . TYR D  1 133 ? -54.218 2.112   28.448  1.00 31.73  ? 133  TYR D CZ  1 
ATOM   13632 O  OH  . TYR D  1 133 ? -53.194 1.577   29.209  1.00 25.81  ? 133  TYR D OH  1 
ATOM   13633 N  N   . ASP D  1 134 ? -60.880 3.964   25.631  1.00 46.02  ? 134  ASP D N   1 
ATOM   13634 C  CA  . ASP D  1 134 ? -61.941 4.388   24.713  1.00 47.29  ? 134  ASP D CA  1 
ATOM   13635 C  C   . ASP D  1 134 ? -62.057 5.912   24.802  1.00 43.44  ? 134  ASP D C   1 
ATOM   13636 O  O   . ASP D  1 134 ? -62.301 6.467   25.863  1.00 45.21  ? 134  ASP D O   1 
ATOM   13637 C  CB  . ASP D  1 134 ? -63.272 3.733   25.149  1.00 54.94  ? 134  ASP D CB  1 
ATOM   13638 C  CG  . ASP D  1 134 ? -64.301 3.608   24.017  1.00 56.93  ? 134  ASP D CG  1 
ATOM   13639 O  OD1 . ASP D  1 134 ? -64.529 4.592   23.279  1.00 57.35  ? 134  ASP D OD1 1 
ATOM   13640 O  OD2 . ASP D  1 134 ? -64.897 2.512   23.886  1.00 56.74  ? 134  ASP D OD2 1 
ATOM   13641 N  N   . GLY D  1 135 ? -61.891 6.592   23.680  1.00 32.32  ? 135  GLY D N   1 
ATOM   13642 C  CA  . GLY D  1 135 ? -61.896 8.035   23.697  1.00 32.34  ? 135  GLY D CA  1 
ATOM   13643 C  C   . GLY D  1 135 ? -63.249 8.631   23.373  1.00 33.92  ? 135  GLY D C   1 
ATOM   13644 O  O   . GLY D  1 135 ? -63.363 9.846   23.234  1.00 34.20  ? 135  GLY D O   1 
ATOM   13645 N  N   . ARG D  1 136 ? -64.279 7.790   23.285  1.00 42.20  ? 136  ARG D N   1 
ATOM   13646 C  CA  . ARG D  1 136 ? -65.598 8.237   22.839  1.00 41.38  ? 136  ARG D CA  1 
ATOM   13647 C  C   . ARG D  1 136 ? -66.217 9.294   23.755  1.00 43.25  ? 136  ARG D C   1 
ATOM   13648 O  O   . ARG D  1 136 ? -66.760 10.290  23.269  1.00 44.43  ? 136  ARG D O   1 
ATOM   13649 C  CB  . ARG D  1 136 ? -66.539 7.049   22.641  1.00 43.63  ? 136  ARG D CB  1 
ATOM   13650 C  CG  . ARG D  1 136 ? -67.278 6.595   23.873  1.00 48.81  ? 136  ARG D CG  1 
ATOM   13651 C  CD  . ARG D  1 136 ? -67.632 5.119   23.794  1.00 55.88  ? 136  ARG D CD  1 
ATOM   13652 N  NE  . ARG D  1 136 ? -67.835 4.651   22.423  1.00 59.39  ? 136  ARG D NE  1 
ATOM   13653 C  CZ  . ARG D  1 136 ? -68.084 3.386   22.092  1.00 60.38  ? 136  ARG D CZ  1 
ATOM   13654 N  NH1 . ARG D  1 136 ? -68.168 2.450   23.029  1.00 59.22  ? 136  ARG D NH1 1 
ATOM   13655 N  NH2 . ARG D  1 136 ? -68.249 3.054   20.820  1.00 62.73  ? 136  ARG D NH2 1 
ATOM   13656 N  N   . PHE D  1 137 ? -66.108 9.104   25.069  1.00 43.42  ? 137  PHE D N   1 
ATOM   13657 C  CA  . PHE D  1 137 ? -66.686 10.050  26.018  1.00 45.10  ? 137  PHE D CA  1 
ATOM   13658 C  C   . PHE D  1 137 ? -65.996 11.404  25.989  1.00 45.62  ? 137  PHE D C   1 
ATOM   13659 O  O   . PHE D  1 137 ? -66.659 12.402  25.819  1.00 47.26  ? 137  PHE D O   1 
ATOM   13660 C  CB  . PHE D  1 137 ? -66.686 9.488   27.426  1.00 47.37  ? 137  PHE D CB  1 
ATOM   13661 C  CG  . PHE D  1 137 ? -67.009 8.041   27.479  1.00 55.59  ? 137  PHE D CG  1 
ATOM   13662 C  CD1 . PHE D  1 137 ? -68.321 7.615   27.495  1.00 61.33  ? 137  PHE D CD1 1 
ATOM   13663 C  CD2 . PHE D  1 137 ? -65.997 7.095   27.502  1.00 59.74  ? 137  PHE D CD2 1 
ATOM   13664 C  CE1 . PHE D  1 137 ? -68.626 6.269   27.543  1.00 65.24  ? 137  PHE D CE1 1 
ATOM   13665 C  CE2 . PHE D  1 137 ? -66.290 5.744   27.549  1.00 63.27  ? 137  PHE D CE2 1 
ATOM   13666 C  CZ  . PHE D  1 137 ? -67.607 5.330   27.570  1.00 65.54  ? 137  PHE D CZ  1 
ATOM   13667 N  N   . LEU D  1 138 ? -64.676 11.451  26.135  1.00 44.43  ? 138  LEU D N   1 
ATOM   13668 C  CA  . LEU D  1 138 ? -63.973 12.738  26.125  1.00 43.92  ? 138  LEU D CA  1 
ATOM   13669 C  C   . LEU D  1 138 ? -64.347 13.569  24.901  1.00 46.60  ? 138  LEU D C   1 
ATOM   13670 O  O   . LEU D  1 138 ? -64.600 14.780  25.006  1.00 47.56  ? 138  LEU D O   1 
ATOM   13671 C  CB  . LEU D  1 138 ? -62.459 12.542  26.228  1.00 34.32  ? 138  LEU D CB  1 
ATOM   13672 C  CG  . LEU D  1 138 ? -62.023 12.144  27.637  1.00 34.06  ? 138  LEU D CG  1 
ATOM   13673 C  CD1 . LEU D  1 138 ? -60.551 11.888  27.689  1.00 32.31  ? 138  LEU D CD1 1 
ATOM   13674 C  CD2 . LEU D  1 138 ? -62.409 13.246  28.591  1.00 35.11  ? 138  LEU D CD2 1 
ATOM   13675 N  N   . ALA D  1 139 ? -64.426 12.894  23.757  1.00 51.40  ? 139  ALA D N   1 
ATOM   13676 C  CA  . ALA D  1 139 ? -64.915 13.505  22.528  1.00 53.46  ? 139  ALA D CA  1 
ATOM   13677 C  C   . ALA D  1 139 ? -66.304 14.046  22.741  1.00 54.61  ? 139  ALA D C   1 
ATOM   13678 O  O   . ALA D  1 139 ? -66.501 15.254  22.752  1.00 56.10  ? 139  ALA D O   1 
ATOM   13679 C  CB  . ALA D  1 139 ? -64.923 12.503  21.385  1.00 50.27  ? 139  ALA D CB  1 
ATOM   13680 N  N   . GLN D  1 140 ? -67.260 13.143  22.936  1.00 51.70  ? 140  GLN D N   1 
ATOM   13681 C  CA  . GLN D  1 140 ? -68.666 13.532  22.981  1.00 56.38  ? 140  GLN D CA  1 
ATOM   13682 C  C   . GLN D  1 140 ? -68.982 14.613  24.021  1.00 56.42  ? 140  GLN D C   1 
ATOM   13683 O  O   . GLN D  1 140 ? -69.549 15.645  23.680  1.00 59.29  ? 140  GLN D O   1 
ATOM   13684 C  CB  . GLN D  1 140 ? -69.576 12.311  23.164  1.00 64.96  ? 140  GLN D CB  1 
ATOM   13685 C  CG  . GLN D  1 140 ? -71.059 12.620  23.006  1.00 71.99  ? 140  GLN D CG  1 
ATOM   13686 C  CD  . GLN D  1 140 ? -71.693 13.103  24.297  1.00 79.24  ? 140  GLN D CD  1 
ATOM   13687 O  OE1 . GLN D  1 140 ? -71.773 12.355  25.271  1.00 83.30  ? 140  GLN D OE1 1 
ATOM   13688 N  NE2 . GLN D  1 140 ? -72.132 14.360  24.318  1.00 79.85  ? 140  GLN D NE2 1 
ATOM   13689 N  N   . VAL D  1 141 ? -68.637 14.370  25.283  1.00 47.75  ? 141  VAL D N   1 
ATOM   13690 C  CA  . VAL D  1 141 ? -68.987 15.295  26.359  1.00 45.28  ? 141  VAL D CA  1 
ATOM   13691 C  C   . VAL D  1 141 ? -68.085 16.506  26.564  1.00 43.39  ? 141  VAL D C   1 
ATOM   13692 O  O   . VAL D  1 141 ? -68.575 17.563  26.928  1.00 44.74  ? 141  VAL D O   1 
ATOM   13693 C  CB  . VAL D  1 141 ? -69.308 14.591  27.704  1.00 44.78  ? 141  VAL D CB  1 
ATOM   13694 C  CG1 . VAL D  1 141 ? -70.745 14.110  27.691  1.00 63.92  ? 141  VAL D CG1 1 
ATOM   13695 C  CG2 . VAL D  1 141 ? -68.382 13.439  27.972  1.00 43.07  ? 141  VAL D CG2 1 
ATOM   13696 N  N   . GLU D  1 142 ? -66.782 16.389  26.349  1.00 45.53  ? 142  GLU D N   1 
ATOM   13697 C  CA  . GLU D  1 142 ? -65.977 17.600  26.484  1.00 48.62  ? 142  GLU D CA  1 
ATOM   13698 C  C   . GLU D  1 142 ? -65.703 18.261  25.142  1.00 47.45  ? 142  GLU D C   1 
ATOM   13699 O  O   . GLU D  1 142 ? -64.990 19.267  25.069  1.00 47.62  ? 142  GLU D O   1 
ATOM   13700 C  CB  . GLU D  1 142 ? -64.700 17.359  27.285  1.00 63.02  ? 142  GLU D CB  1 
ATOM   13701 C  CG  . GLU D  1 142 ? -64.962 17.102  28.763  1.00 69.70  ? 142  GLU D CG  1 
ATOM   13702 C  CD  . GLU D  1 142 ? -65.706 18.241  29.434  1.00 75.52  ? 142  GLU D CD  1 
ATOM   13703 O  OE1 . GLU D  1 142 ? -65.417 19.414  29.101  1.00 76.64  ? 142  GLU D OE1 1 
ATOM   13704 O  OE2 . GLU D  1 142 ? -66.579 17.959  30.289  1.00 77.82  ? 142  GLU D OE2 1 
ATOM   13705 N  N   . GLY D  1 143 ? -66.275 17.681  24.087  1.00 45.64  ? 143  GLY D N   1 
ATOM   13706 C  CA  . GLY D  1 143 ? -66.211 18.251  22.753  1.00 45.48  ? 143  GLY D CA  1 
ATOM   13707 C  C   . GLY D  1 143 ? -64.825 18.201  22.155  1.00 42.39  ? 143  GLY D C   1 
ATOM   13708 O  O   . GLY D  1 143 ? -64.470 19.051  21.337  1.00 41.52  ? 143  GLY D O   1 
ATOM   13709 N  N   . ALA D  1 144 ? -64.064 17.176  22.528  1.00 45.99  ? 144  ALA D N   1 
ATOM   13710 C  CA  . ALA D  1 144 ? -62.625 17.169  22.303  1.00 47.03  ? 144  ALA D CA  1 
ATOM   13711 C  C   . ALA D  1 144 ? -62.210 16.180  21.216  1.00 48.24  ? 144  ALA D C   1 
ATOM   13712 O  O   . ALA D  1 144 ? -62.935 15.227  20.931  1.00 47.40  ? 144  ALA D O   1 
ATOM   13713 C  CB  . ALA D  1 144 ? -61.899 16.878  23.597  1.00 34.78  ? 144  ALA D CB  1 
ATOM   13714 N  N   . VAL D  1 145 ? -61.074 16.452  20.571  1.00 53.88  ? 145  VAL D N   1 
ATOM   13715 C  CA  . VAL D  1 145 ? -60.476 15.524  19.606  1.00 50.80  ? 145  VAL D CA  1 
ATOM   13716 C  C   . VAL D  1 145 ? -59.356 14.723  20.255  1.00 49.67  ? 145  VAL D C   1 
ATOM   13717 O  O   . VAL D  1 145 ? -58.373 15.280  20.759  1.00 48.68  ? 145  VAL D O   1 
ATOM   13718 C  CB  . VAL D  1 145 ? -59.882 16.240  18.381  1.00 37.87  ? 145  VAL D CB  1 
ATOM   13719 C  CG1 . VAL D  1 145 ? -59.078 15.257  17.537  1.00 34.51  ? 145  VAL D CG1 1 
ATOM   13720 C  CG2 . VAL D  1 145 ? -60.966 16.902  17.560  1.00 38.20  ? 145  VAL D CG2 1 
ATOM   13721 N  N   . LEU D  1 146 ? -59.500 13.407  20.196  1.00 43.09  ? 146  LEU D N   1 
ATOM   13722 C  CA  . LEU D  1 146 ? -58.658 12.500  20.951  1.00 41.77  ? 146  LEU D CA  1 
ATOM   13723 C  C   . LEU D  1 146 ? -57.830 11.528  20.082  1.00 40.50  ? 146  LEU D C   1 
ATOM   13724 O  O   . LEU D  1 146 ? -58.387 10.667  19.401  1.00 41.65  ? 146  LEU D O   1 
ATOM   13725 C  CB  . LEU D  1 146 ? -59.551 11.718  21.902  1.00 40.62  ? 146  LEU D CB  1 
ATOM   13726 C  CG  . LEU D  1 146 ? -58.786 11.105  23.060  1.00 43.71  ? 146  LEU D CG  1 
ATOM   13727 C  CD1 . LEU D  1 146 ? -59.324 11.648  24.354  1.00 47.92  ? 146  LEU D CD1 1 
ATOM   13728 C  CD2 . LEU D  1 146 ? -58.911 9.610   23.020  1.00 44.17  ? 146  LEU D CD2 1 
ATOM   13729 N  N   . VAL D  1 147 ? -56.503 11.659  20.112  1.00 38.21  ? 147  VAL D N   1 
ATOM   13730 C  CA  . VAL D  1 147 ? -55.632 10.733  19.382  1.00 32.36  ? 147  VAL D CA  1 
ATOM   13731 C  C   . VAL D  1 147 ? -55.007 9.736   20.335  1.00 29.63  ? 147  VAL D C   1 
ATOM   13732 O  O   . VAL D  1 147 ? -54.698 10.067  21.478  1.00 30.07  ? 147  VAL D O   1 
ATOM   13733 C  CB  . VAL D  1 147 ? -54.477 11.440  18.634  1.00 25.48  ? 147  VAL D CB  1 
ATOM   13734 C  CG1 . VAL D  1 147 ? -53.976 10.567  17.507  1.00 25.00  ? 147  VAL D CG1 1 
ATOM   13735 C  CG2 . VAL D  1 147 ? -54.927 12.766  18.081  1.00 26.21  ? 147  VAL D CG2 1 
ATOM   13736 N  N   . SER D  1 148 ? -54.834 8.508   19.863  1.00 30.50  ? 148  SER D N   1 
ATOM   13737 C  CA  . SER D  1 148 ? -54.073 7.505   20.602  1.00 30.74  ? 148  SER D CA  1 
ATOM   13738 C  C   . SER D  1 148 ? -53.280 6.670   19.592  1.00 30.48  ? 148  SER D C   1 
ATOM   13739 O  O   . SER D  1 148 ? -53.801 6.347   18.535  1.00 30.59  ? 148  SER D O   1 
ATOM   13740 C  CB  . SER D  1 148 ? -55.003 6.633   21.457  1.00 25.87  ? 148  SER D CB  1 
ATOM   13741 O  OG  . SER D  1 148 ? -55.923 5.908   20.660  1.00 26.04  ? 148  SER D OG  1 
ATOM   13742 N  N   . MET D  1 149 ? -52.019 6.347   19.887  1.00 23.12  ? 149  MET D N   1 
ATOM   13743 C  CA  . MET D  1 149 ? -51.209 5.587   18.923  1.00 22.66  ? 149  MET D CA  1 
ATOM   13744 C  C   . MET D  1 149 ? -50.609 4.337   19.538  1.00 22.37  ? 149  MET D C   1 
ATOM   13745 O  O   . MET D  1 149 ? -50.512 4.233   20.751  1.00 22.30  ? 149  MET D O   1 
ATOM   13746 C  CB  . MET D  1 149 ? -50.089 6.444   18.322  1.00 22.04  ? 149  MET D CB  1 
ATOM   13747 C  CG  . MET D  1 149 ? -48.779 6.427   19.110  1.00 21.30  ? 149  MET D CG  1 
ATOM   13748 S  SD  . MET D  1 149 ? -48.856 7.385   20.632  1.00 21.27  ? 149  MET D SD  1 
ATOM   13749 C  CE  . MET D  1 149 ? -48.953 9.064   20.027  1.00 21.46  ? 149  MET D CE  1 
ATOM   13750 N  N   . ASN D  1 150 ? -50.249 3.379   18.692  1.00 24.08  ? 150  ASN D N   1 
ATOM   13751 C  CA  . ASN D  1 150 ? -49.460 2.234   19.123  1.00 26.24  ? 150  ASN D CA  1 
ATOM   13752 C  C   . ASN D  1 150 ? -47.995 2.574   18.957  1.00 25.33  ? 150  ASN D C   1 
ATOM   13753 O  O   . ASN D  1 150 ? -47.644 3.316   18.038  1.00 25.87  ? 150  ASN D O   1 
ATOM   13754 C  CB  . ASN D  1 150 ? -49.801 0.989   18.306  1.00 24.19  ? 150  ASN D CB  1 
ATOM   13755 C  CG  . ASN D  1 150 ? -51.125 0.373   18.708  1.00 25.86  ? 150  ASN D CG  1 
ATOM   13756 O  OD1 . ASN D  1 150 ? -51.841 0.909   19.554  1.00 27.03  ? 150  ASN D OD1 1 
ATOM   13757 N  ND2 . ASN D  1 150 ? -51.464 -0.757  18.098  1.00 26.02  ? 150  ASN D ND2 1 
ATOM   13758 N  N   . TYR D  1 151 ? -47.146 2.083   19.860  1.00 22.45  ? 151  TYR D N   1 
ATOM   13759 C  CA  . TYR D  1 151 ? -45.697 2.166   19.666  1.00 23.43  ? 151  TYR D CA  1 
ATOM   13760 C  C   . TYR D  1 151 ? -45.107 0.829   20.015  1.00 24.47  ? 151  TYR D C   1 
ATOM   13761 O  O   . TYR D  1 151 ? -45.653 0.113   20.844  1.00 25.48  ? 151  TYR D O   1 
ATOM   13762 C  CB  . TYR D  1 151 ? -45.047 3.254   20.521  1.00 19.94  ? 151  TYR D CB  1 
ATOM   13763 C  CG  . TYR D  1 151 ? -45.350 3.130   21.989  1.00 20.02  ? 151  TYR D CG  1 
ATOM   13764 C  CD1 . TYR D  1 151 ? -46.497 3.693   22.524  1.00 55.67  ? 151  TYR D CD1 1 
ATOM   13765 C  CD2 . TYR D  1 151 ? -44.502 2.455   22.842  1.00 20.97  ? 151  TYR D CD2 1 
ATOM   13766 C  CE1 . TYR D  1 151 ? -46.797 3.591   23.863  1.00 20.58  ? 151  TYR D CE1 1 
ATOM   13767 C  CE2 . TYR D  1 151 ? -44.795 2.347   24.187  1.00 22.08  ? 151  TYR D CE2 1 
ATOM   13768 C  CZ  . TYR D  1 151 ? -45.950 2.917   24.684  1.00 20.39  ? 151  TYR D CZ  1 
ATOM   13769 O  OH  . TYR D  1 151 ? -46.263 2.821   26.009  1.00 24.86  ? 151  TYR D OH  1 
ATOM   13770 N  N   . ARG D  1 152 ? -43.979 0.507   19.395  1.00 20.90  ? 152  ARG D N   1 
ATOM   13771 C  CA  . ARG D  1 152 ? -43.324 -0.768  19.621  1.00 23.62  ? 152  ARG D CA  1 
ATOM   13772 C  C   . ARG D  1 152 ? -42.791 -0.859  21.050  1.00 23.48  ? 152  ARG D C   1 
ATOM   13773 O  O   . ARG D  1 152 ? -41.996 -0.042  21.504  1.00 22.94  ? 152  ARG D O   1 
ATOM   13774 C  CB  . ARG D  1 152 ? -42.188 -0.941  18.618  1.00 20.47  ? 152  ARG D CB  1 
ATOM   13775 C  CG  . ARG D  1 152 ? -42.654 -1.385  17.260  1.00 23.57  ? 152  ARG D CG  1 
ATOM   13776 C  CD  . ARG D  1 152 ? -41.555 -1.272  16.257  1.00 22.01  ? 152  ARG D CD  1 
ATOM   13777 N  NE  . ARG D  1 152 ? -41.264 0.123   16.000  1.00 20.42  ? 152  ARG D NE  1 
ATOM   13778 C  CZ  . ARG D  1 152 ? -40.173 0.542   15.376  1.00 20.83  ? 152  ARG D CZ  1 
ATOM   13779 N  NH1 . ARG D  1 152 ? -39.268 -0.332  14.955  1.00 22.76  ? 152  ARG D NH1 1 
ATOM   13780 N  NH2 . ARG D  1 152 ? -39.976 1.834   15.180  1.00 20.07  ? 152  ARG D NH2 1 
ATOM   13781 N  N   . VAL D  1 153 ? -43.248 -1.865  21.765  1.00 20.83  ? 153  VAL D N   1 
ATOM   13782 C  CA  . VAL D  1 153 ? -42.811 -2.063  23.118  1.00 20.81  ? 153  VAL D CA  1 
ATOM   13783 C  C   . VAL D  1 153 ? -41.871 -3.254  23.107  1.00 22.96  ? 153  VAL D C   1 
ATOM   13784 O  O   . VAL D  1 153 ? -41.637 -3.852  22.052  1.00 23.93  ? 153  VAL D O   1 
ATOM   13785 C  CB  . VAL D  1 153 ? -44.010 -2.343  23.994  1.00 21.29  ? 153  VAL D CB  1 
ATOM   13786 C  CG1 . VAL D  1 153 ? -45.014 -1.216  23.835  1.00 21.15  ? 153  VAL D CG1 1 
ATOM   13787 C  CG2 . VAL D  1 153 ? -44.651 -3.655  23.584  1.00 24.76  ? 153  VAL D CG2 1 
ATOM   13788 N  N   . GLY D  1 154 ? -41.328 -3.602  24.269  1.00 24.84  ? 154  GLY D N   1 
ATOM   13789 C  CA  . GLY D  1 154 ? -40.456 -4.761  24.387  1.00 25.48  ? 154  GLY D CA  1 
ATOM   13790 C  C   . GLY D  1 154 ? -39.198 -4.707  23.535  1.00 24.89  ? 154  GLY D C   1 
ATOM   13791 O  O   . GLY D  1 154 ? -38.713 -3.632  23.206  1.00 20.95  ? 154  GLY D O   1 
ATOM   13792 N  N   . THR D  1 155 ? -38.676 -5.879  23.182  1.00 27.06  ? 155  THR D N   1 
ATOM   13793 C  CA  . THR D  1 155 ? -37.439 -5.982  22.421  1.00 25.92  ? 155  THR D CA  1 
ATOM   13794 C  C   . THR D  1 155 ? -37.558 -5.177  21.140  1.00 26.44  ? 155  THR D C   1 
ATOM   13795 O  O   . THR D  1 155 ? -36.638 -4.466  20.754  1.00 24.70  ? 155  THR D O   1 
ATOM   13796 C  CB  . THR D  1 155 ? -37.106 -7.446  22.094  1.00 23.20  ? 155  THR D CB  1 
ATOM   13797 O  OG1 . THR D  1 155 ? -38.166 -8.027  21.329  1.00 23.60  ? 155  THR D OG1 1 
ATOM   13798 C  CG2 . THR D  1 155 ? -36.978 -8.234  23.358  1.00 23.72  ? 155  THR D CG2 1 
ATOM   13799 N  N   . PHE D  1 156 ? -38.720 -5.261  20.507  1.00 39.50  ? 156  PHE D N   1 
ATOM   13800 C  CA  . PHE D  1 156 ? -38.935 -4.630  19.215  1.00 41.54  ? 156  PHE D CA  1 
ATOM   13801 C  C   . PHE D  1 156 ? -38.792 -3.134  19.314  1.00 41.63  ? 156  PHE D C   1 
ATOM   13802 O  O   . PHE D  1 156 ? -38.153 -2.512  18.470  1.00 44.89  ? 156  PHE D O   1 
ATOM   13803 C  CB  . PHE D  1 156 ? -40.300 -5.020  18.664  1.00 26.88  ? 156  PHE D CB  1 
ATOM   13804 C  CG  . PHE D  1 156 ? -40.553 -6.481  18.745  1.00 22.90  ? 156  PHE D CG  1 
ATOM   13805 C  CD1 . PHE D  1 156 ? -39.942 -7.348  17.858  1.00 24.85  ? 156  PHE D CD1 1 
ATOM   13806 C  CD2 . PHE D  1 156 ? -41.346 -7.003  19.743  1.00 23.22  ? 156  PHE D CD2 1 
ATOM   13807 C  CE1 . PHE D  1 156 ? -40.146 -8.711  17.946  1.00 24.68  ? 156  PHE D CE1 1 
ATOM   13808 C  CE2 . PHE D  1 156 ? -41.550 -8.363  19.832  1.00 24.14  ? 156  PHE D CE2 1 
ATOM   13809 C  CZ  . PHE D  1 156 ? -40.951 -9.216  18.930  1.00 24.74  ? 156  PHE D CZ  1 
ATOM   13810 N  N   . GLY D  1 157 ? -39.379 -2.559  20.352  1.00 31.86  ? 157  GLY D N   1 
ATOM   13811 C  CA  . GLY D  1 157 ? -39.266 -1.131  20.558  1.00 31.87  ? 157  GLY D CA  1 
ATOM   13812 C  C   . GLY D  1 157 ? -37.951 -0.649  21.140  1.00 31.25  ? 157  GLY D C   1 
ATOM   13813 O  O   . GLY D  1 157 ? -37.371 0.357   20.720  1.00 31.91  ? 157  GLY D O   1 
ATOM   13814 N  N   . PHE D  1 158 ? -37.522 -1.309  22.194  1.00 24.90  ? 158  PHE D N   1 
ATOM   13815 C  CA  . PHE D  1 158 ? -36.353 -0.833  22.892  1.00 21.90  ? 158  PHE D CA  1 
ATOM   13816 C  C   . PHE D  1 158 ? -35.025 -1.559  22.853  1.00 20.39  ? 158  PHE D C   1 
ATOM   13817 O  O   . PHE D  1 158 ? -34.092 -1.074  23.475  1.00 20.05  ? 158  PHE D O   1 
ATOM   13818 C  CB  . PHE D  1 158 ? -36.753 -0.328  24.262  1.00 23.41  ? 158  PHE D CB  1 
ATOM   13819 C  CG  . PHE D  1 158 ? -37.843 0.693   24.180  1.00 24.40  ? 158  PHE D CG  1 
ATOM   13820 C  CD1 . PHE D  1 158 ? -39.164 0.304   24.097  1.00 24.41  ? 158  PHE D CD1 1 
ATOM   13821 C  CD2 . PHE D  1 158 ? -37.539 2.032   24.098  1.00 24.62  ? 158  PHE D CD2 1 
ATOM   13822 C  CE1 . PHE D  1 158 ? -40.151 1.226   23.979  1.00 25.68  ? 158  PHE D CE1 1 
ATOM   13823 C  CE2 . PHE D  1 158 ? -38.523 2.955   23.988  1.00 24.06  ? 158  PHE D CE2 1 
ATOM   13824 C  CZ  . PHE D  1 158 ? -39.834 2.553   23.925  1.00 25.57  ? 158  PHE D CZ  1 
ATOM   13825 N  N   . LEU D  1 159 ? -34.928 -2.704  22.169  1.00 24.23  ? 159  LEU D N   1 
ATOM   13826 C  CA  . LEU D  1 159 ? -33.657 -3.444  22.133  1.00 25.42  ? 159  LEU D CA  1 
ATOM   13827 C  C   . LEU D  1 159 ? -32.633 -2.618  21.384  1.00 25.84  ? 159  LEU D C   1 
ATOM   13828 O  O   . LEU D  1 159 ? -32.891 -2.182  20.270  1.00 27.73  ? 159  LEU D O   1 
ATOM   13829 C  CB  . LEU D  1 159 ? -33.800 -4.821  21.490  1.00 22.02  ? 159  LEU D CB  1 
ATOM   13830 C  CG  . LEU D  1 159 ? -32.576 -5.744  21.524  1.00 24.24  ? 159  LEU D CG  1 
ATOM   13831 C  CD1 . LEU D  1 159 ? -33.057 -7.188  21.482  1.00 23.63  ? 159  LEU D CD1 1 
ATOM   13832 C  CD2 . LEU D  1 159 ? -31.542 -5.469  20.404  1.00 23.10  ? 159  LEU D CD2 1 
ATOM   13833 N  N   . ALA D  1 160 ? -31.473 -2.408  21.997  1.00 21.32  ? 160  ALA D N   1 
ATOM   13834 C  CA  . ALA D  1 160 ? -30.554 -1.378  21.531  1.00 21.28  ? 160  ALA D CA  1 
ATOM   13835 C  C   . ALA D  1 160 ? -29.124 -1.833  21.610  1.00 22.64  ? 160  ALA D C   1 
ATOM   13836 O  O   . ALA D  1 160 ? -28.689 -2.342  22.635  1.00 22.96  ? 160  ALA D O   1 
ATOM   13837 C  CB  . ALA D  1 160 ? -30.725 -0.106  22.356  1.00 20.57  ? 160  ALA D CB  1 
ATOM   13838 N  N   . LEU D  1 161 ? -28.386 -1.627  20.532  1.00 29.68  ? 161  LEU D N   1 
ATOM   13839 C  CA  . LEU D  1 161 ? -26.951 -1.844  20.557  1.00 32.68  ? 161  LEU D CA  1 
ATOM   13840 C  C   . LEU D  1 161 ? -26.315 -0.501  20.294  1.00 35.38  ? 161  LEU D C   1 
ATOM   13841 O  O   . LEU D  1 161 ? -25.933 -0.212  19.169  1.00 38.87  ? 161  LEU D O   1 
ATOM   13842 C  CB  . LEU D  1 161 ? -26.530 -2.850  19.492  1.00 25.70  ? 161  LEU D CB  1 
ATOM   13843 C  CG  . LEU D  1 161 ? -26.711 -4.309  19.884  1.00 25.30  ? 161  LEU D CG  1 
ATOM   13844 C  CD1 . LEU D  1 161 ? -26.051 -5.187  18.863  1.00 26.94  ? 161  LEU D CD1 1 
ATOM   13845 C  CD2 . LEU D  1 161 ? -26.103 -4.553  21.247  1.00 24.78  ? 161  LEU D CD2 1 
ATOM   13846 N  N   . PRO D  1 162 ? -26.194 0.320   21.347  1.00 30.64  ? 162  PRO D N   1 
ATOM   13847 C  CA  . PRO D  1 162 ? -25.901 1.751   21.265  1.00 31.48  ? 162  PRO D CA  1 
ATOM   13848 C  C   . PRO D  1 162 ? -24.745 2.034   20.337  1.00 36.04  ? 162  PRO D C   1 
ATOM   13849 O  O   . PRO D  1 162 ? -23.710 1.374   20.435  1.00 37.01  ? 162  PRO D O   1 
ATOM   13850 C  CB  . PRO D  1 162 ? -25.484 2.084   22.693  1.00 33.76  ? 162  PRO D CB  1 
ATOM   13851 C  CG  . PRO D  1 162 ? -26.268 1.145   23.526  1.00 33.08  ? 162  PRO D CG  1 
ATOM   13852 C  CD  . PRO D  1 162 ? -26.333 -0.128  22.743  1.00 33.69  ? 162  PRO D CD  1 
ATOM   13853 N  N   . GLY D  1 163 ? -24.924 3.001   19.442  1.00 39.21  ? 163  GLY D N   1 
ATOM   13854 C  CA  . GLY D  1 163 ? -23.883 3.350   18.490  1.00 43.21  ? 163  GLY D CA  1 
ATOM   13855 C  C   . GLY D  1 163 ? -24.094 2.730   17.125  1.00 46.93  ? 163  GLY D C   1 
ATOM   13856 O  O   . GLY D  1 163 ? -23.569 3.215   16.124  1.00 46.58  ? 163  GLY D O   1 
ATOM   13857 N  N   . SER D  1 164 ? -24.876 1.657   17.085  1.00 58.90  ? 164  SER D N   1 
ATOM   13858 C  CA  . SER D  1 164 ? -25.175 0.978   15.834  1.00 62.98  ? 164  SER D CA  1 
ATOM   13859 C  C   . SER D  1 164 ? -26.250 1.728   15.072  1.00 64.29  ? 164  SER D C   1 
ATOM   13860 O  O   . SER D  1 164 ? -27.141 2.347   15.664  1.00 62.03  ? 164  SER D O   1 
ATOM   13861 C  CB  . SER D  1 164 ? -25.671 -0.440  16.093  1.00 57.67  ? 164  SER D CB  1 
ATOM   13862 O  OG  . SER D  1 164 ? -27.046 -0.415  16.450  1.00 55.98  ? 164  SER D OG  1 
ATOM   13863 N  N   . ARG D  1 165 ? -26.145 1.670   13.750  1.00 54.27  ? 165  ARG D N   1 
ATOM   13864 C  CA  . ARG D  1 165 ? -27.164 2.202   12.866  1.00 54.96  ? 165  ARG D CA  1 
ATOM   13865 C  C   . ARG D  1 165 ? -28.313 1.200   12.751  1.00 43.96  ? 165  ARG D C   1 
ATOM   13866 O  O   . ARG D  1 165 ? -29.452 1.571   12.438  1.00 38.67  ? 165  ARG D O   1 
ATOM   13867 C  CB  . ARG D  1 165 ? -26.558 2.508   11.493  1.00 96.11  ? 165  ARG D CB  1 
ATOM   13868 C  CG  . ARG D  1 165 ? -25.603 1.437   10.972  1.00 107.47 ? 165  ARG D CG  1 
ATOM   13869 C  CD  . ARG D  1 165 ? -25.321 1.625   9.483   1.00 117.21 ? 165  ARG D CD  1 
ATOM   13870 N  NE  . ARG D  1 165 ? -24.654 2.896   9.201   1.00 124.19 ? 165  ARG D NE  1 
ATOM   13871 C  CZ  . ARG D  1 165 ? -24.583 3.458   7.997   1.00 127.91 ? 165  ARG D CZ  1 
ATOM   13872 N  NH1 . ARG D  1 165 ? -25.149 2.870   6.948   1.00 128.57 ? 165  ARG D NH1 1 
ATOM   13873 N  NH2 . ARG D  1 165 ? -23.951 4.616   7.842   1.00 128.61 ? 165  ARG D NH2 1 
ATOM   13874 N  N   . GLU D  1 166 ? -27.995 -0.063  13.036  1.00 44.23  ? 166  GLU D N   1 
ATOM   13875 C  CA  . GLU D  1 166 ? -28.895 -1.200  12.831  1.00 46.46  ? 166  GLU D CA  1 
ATOM   13876 C  C   . GLU D  1 166 ? -29.965 -1.408  13.909  1.00 40.67  ? 166  GLU D C   1 
ATOM   13877 O  O   . GLU D  1 166 ? -31.044 -1.940  13.620  1.00 40.37  ? 166  GLU D O   1 
ATOM   13878 C  CB  . GLU D  1 166 ? -28.071 -2.476  12.683  1.00 78.08  ? 166  GLU D CB  1 
ATOM   13879 C  CG  . GLU D  1 166 ? -27.062 -2.406  11.564  1.00 89.73  ? 166  GLU D CG  1 
ATOM   13880 C  CD  . GLU D  1 166 ? -27.721 -2.308  10.203  1.00 99.76  ? 166  GLU D CD  1 
ATOM   13881 O  OE1 . GLU D  1 166 ? -28.112 -1.185  9.804   1.00 100.82 ? 166  GLU D OE1 1 
ATOM   13882 O  OE2 . GLU D  1 166 ? -27.847 -3.359  9.533   1.00 105.38 ? 166  GLU D OE2 1 
ATOM   13883 N  N   . ALA D  1 167 ? -29.638 -1.044  15.150  1.00 34.98  ? 167  ALA D N   1 
ATOM   13884 C  CA  . ALA D  1 167 ? -30.587 -1.061  16.263  1.00 28.01  ? 167  ALA D CA  1 
ATOM   13885 C  C   . ALA D  1 167 ? -30.287 0.102   17.190  1.00 26.10  ? 167  ALA D C   1 
ATOM   13886 O  O   . ALA D  1 167 ? -29.759 -0.112  18.281  1.00 25.73  ? 167  ALA D O   1 
ATOM   13887 C  CB  . ALA D  1 167 ? -30.464 -2.352  17.021  1.00 31.07  ? 167  ALA D CB  1 
ATOM   13888 N  N   . PRO D  1 168 ? -30.602 1.337   16.760  1.00 28.33  ? 168  PRO D N   1 
ATOM   13889 C  CA  . PRO D  1 168 ? -30.100 2.537   17.430  1.00 27.25  ? 168  PRO D CA  1 
ATOM   13890 C  C   . PRO D  1 168 ? -30.732 2.750   18.788  1.00 28.02  ? 168  PRO D C   1 
ATOM   13891 O  O   . PRO D  1 168 ? -30.173 3.479   19.604  1.00 28.36  ? 168  PRO D O   1 
ATOM   13892 C  CB  . PRO D  1 168 ? -30.501 3.670   16.478  1.00 33.92  ? 168  PRO D CB  1 
ATOM   13893 C  CG  . PRO D  1 168 ? -30.804 3.017   15.195  1.00 37.44  ? 168  PRO D CG  1 
ATOM   13894 C  CD  . PRO D  1 168 ? -31.408 1.697   15.591  1.00 38.89  ? 168  PRO D CD  1 
ATOM   13895 N  N   . GLY D  1 169 ? -31.879 2.130   19.029  1.00 31.39  ? 169  GLY D N   1 
ATOM   13896 C  CA  . GLY D  1 169 ? -32.520 2.250   20.323  1.00 29.77  ? 169  GLY D CA  1 
ATOM   13897 C  C   . GLY D  1 169 ? -33.500 3.401   20.395  1.00 26.83  ? 169  GLY D C   1 
ATOM   13898 O  O   . GLY D  1 169 ? -33.436 4.346   19.601  1.00 26.76  ? 169  GLY D O   1 
ATOM   13899 N  N   . ASN D  1 170 ? -34.405 3.300   21.366  1.00 24.15  ? 170  ASN D N   1 
ATOM   13900 C  CA  . ASN D  1 170 ? -35.530 4.221   21.554  1.00 24.81  ? 170  ASN D CA  1 
ATOM   13901 C  C   . ASN D  1 170 ? -36.449 4.313   20.350  1.00 26.74  ? 170  ASN D C   1 
ATOM   13902 O  O   . ASN D  1 170 ? -37.152 5.311   20.190  1.00 18.53  ? 170  ASN D O   1 
ATOM   13903 C  CB  . ASN D  1 170 ? -35.073 5.637   21.915  1.00 23.46  ? 170  ASN D CB  1 
ATOM   13904 C  CG  . ASN D  1 170 ? -34.154 5.675   23.104  1.00 20.90  ? 170  ASN D CG  1 
ATOM   13905 O  OD1 . ASN D  1 170 ? -34.348 4.948   24.074  1.00 19.41  ? 170  ASN D OD1 1 
ATOM   13906 N  ND2 . ASN D  1 170 ? -33.145 6.540   23.040  1.00 18.53  ? 170  ASN D ND2 1 
ATOM   13907 N  N   . VAL D  1 171 ? -36.470 3.292   19.505  1.00 18.93  ? 171  VAL D N   1 
ATOM   13908 C  CA  . VAL D  1 171 ? -37.298 3.416   18.331  1.00 19.07  ? 171  VAL D CA  1 
ATOM   13909 C  C   . VAL D  1 171 ? -38.791 3.468   18.705  1.00 18.98  ? 171  VAL D C   1 
ATOM   13910 O  O   . VAL D  1 171 ? -39.593 4.022   17.963  1.00 19.06  ? 171  VAL D O   1 
ATOM   13911 C  CB  . VAL D  1 171 ? -36.958 2.372   17.251  1.00 19.51  ? 171  VAL D CB  1 
ATOM   13912 C  CG1 . VAL D  1 171 ? -35.542 2.576   16.776  1.00 19.72  ? 171  VAL D CG1 1 
ATOM   13913 C  CG2 . VAL D  1 171 ? -37.110 0.990   17.777  1.00 26.08  ? 171  VAL D CG2 1 
ATOM   13914 N  N   . GLY D  1 172 ? -39.155 2.938   19.871  1.00 18.92  ? 172  GLY D N   1 
ATOM   13915 C  CA  . GLY D  1 172 ? -40.524 3.042   20.347  1.00 18.97  ? 172  GLY D CA  1 
ATOM   13916 C  C   . GLY D  1 172 ? -40.918 4.499   20.516  1.00 18.86  ? 172  GLY D C   1 
ATOM   13917 O  O   . GLY D  1 172 ? -41.999 4.953   20.104  1.00 21.31  ? 172  GLY D O   1 
ATOM   13918 N  N   . LEU D  1 173 ? -40.020 5.254   21.123  1.00 24.47  ? 173  LEU D N   1 
ATOM   13919 C  CA  . LEU D  1 173 ? -40.208 6.683   21.279  1.00 25.01  ? 173  LEU D CA  1 
ATOM   13920 C  C   . LEU D  1 173 ? -40.269 7.387   19.915  1.00 27.10  ? 173  LEU D C   1 
ATOM   13921 O  O   . LEU D  1 173 ? -41.021 8.342   19.732  1.00 30.02  ? 173  LEU D O   1 
ATOM   13922 C  CB  . LEU D  1 173 ? -39.086 7.259   22.148  1.00 21.15  ? 173  LEU D CB  1 
ATOM   13923 C  CG  . LEU D  1 173 ? -39.125 6.753   23.589  1.00 21.81  ? 173  LEU D CG  1 
ATOM   13924 C  CD1 . LEU D  1 173 ? -38.082 7.455   24.447  1.00 18.11  ? 173  LEU D CD1 1 
ATOM   13925 C  CD2 . LEU D  1 173 ? -40.531 6.919   24.158  1.00 18.39  ? 173  LEU D CD2 1 
ATOM   13926 N  N   . LEU D  1 174 ? -39.483 6.912   18.957  1.00 21.68  ? 174  LEU D N   1 
ATOM   13927 C  CA  . LEU D  1 174 ? -39.495 7.496   17.625  1.00 18.93  ? 174  LEU D CA  1 
ATOM   13928 C  C   . LEU D  1 174 ? -40.830 7.237   16.922  1.00 21.04  ? 174  LEU D C   1 
ATOM   13929 O  O   . LEU D  1 174 ? -41.264 8.044   16.097  1.00 19.57  ? 174  LEU D O   1 
ATOM   13930 C  CB  . LEU D  1 174 ? -38.325 6.961   16.801  1.00 44.96  ? 174  LEU D CB  1 
ATOM   13931 C  CG  . LEU D  1 174 ? -36.952 7.357   17.304  1.00 19.00  ? 174  LEU D CG  1 
ATOM   13932 C  CD1 . LEU D  1 174 ? -35.942 7.040   16.265  1.00 19.35  ? 174  LEU D CD1 1 
ATOM   13933 C  CD2 . LEU D  1 174 ? -36.944 8.826   17.604  1.00 19.00  ? 174  LEU D CD2 1 
ATOM   13934 N  N   . ASP D  1 175 ? -41.462 6.106   17.250  1.00 27.55  ? 175  ASP D N   1 
ATOM   13935 C  CA  . ASP D  1 175 ? -42.831 5.809   16.827  1.00 19.54  ? 175  ASP D CA  1 
ATOM   13936 C  C   . ASP D  1 175 ? -43.791 6.842   17.385  1.00 19.64  ? 175  ASP D C   1 
ATOM   13937 O  O   . ASP D  1 175 ? -44.524 7.476   16.626  1.00 20.62  ? 175  ASP D O   1 
ATOM   13938 C  CB  . ASP D  1 175 ? -43.296 4.438   17.321  1.00 24.47  ? 175  ASP D CB  1 
ATOM   13939 C  CG  . ASP D  1 175 ? -42.516 3.309   16.718  1.00 27.24  ? 175  ASP D CG  1 
ATOM   13940 O  OD1 . ASP D  1 175 ? -41.845 3.548   15.691  1.00 29.22  ? 175  ASP D OD1 1 
ATOM   13941 O  OD2 . ASP D  1 175 ? -42.579 2.185   17.266  1.00 27.12  ? 175  ASP D OD2 1 
ATOM   13942 N  N   . GLN D  1 176 ? -43.806 6.992   18.711  1.00 25.13  ? 176  GLN D N   1 
ATOM   13943 C  CA  . GLN D  1 176 ? -44.681 7.986   19.327  1.00 19.65  ? 176  GLN D CA  1 
ATOM   13944 C  C   . GLN D  1 176 ? -44.499 9.335   18.648  1.00 27.52  ? 176  GLN D C   1 
ATOM   13945 O  O   . GLN D  1 176 ? -45.465 9.976   18.225  1.00 20.24  ? 176  GLN D O   1 
ATOM   13946 C  CB  . GLN D  1 176 ? -44.365 8.128   20.803  1.00 19.43  ? 176  GLN D CB  1 
ATOM   13947 C  CG  . GLN D  1 176 ? -44.324 6.820   21.533  1.00 19.35  ? 176  GLN D CG  1 
ATOM   13948 C  CD  . GLN D  1 176 ? -44.062 6.988   23.019  1.00 19.24  ? 176  GLN D CD  1 
ATOM   13949 O  OE1 . GLN D  1 176 ? -43.740 8.082   23.494  1.00 19.15  ? 176  GLN D OE1 1 
ATOM   13950 N  NE2 . GLN D  1 176 ? -44.209 5.897   23.765  1.00 19.33  ? 176  GLN D NE2 1 
ATOM   13951 N  N   . ARG D  1 177 ? -43.246 9.752   18.520  1.00 22.16  ? 177  ARG D N   1 
ATOM   13952 C  CA  . ARG D  1 177 ? -42.939 11.022  17.890  1.00 22.09  ? 177  ARG D CA  1 
ATOM   13953 C  C   . ARG D  1 177 ? -43.554 11.100  16.511  1.00 23.78  ? 177  ARG D C   1 
ATOM   13954 O  O   . ARG D  1 177 ? -44.258 12.048  16.225  1.00 26.50  ? 177  ARG D O   1 
ATOM   13955 C  CB  . ARG D  1 177 ? -41.434 11.275  17.794  1.00 25.62  ? 177  ARG D CB  1 
ATOM   13956 C  CG  . ARG D  1 177 ? -41.143 12.487  16.928  1.00 29.13  ? 177  ARG D CG  1 
ATOM   13957 C  CD  . ARG D  1 177 ? -39.703 12.826  16.886  1.00 19.88  ? 177  ARG D CD  1 
ATOM   13958 N  NE  . ARG D  1 177 ? -39.231 13.179  18.204  1.00 28.48  ? 177  ARG D NE  1 
ATOM   13959 C  CZ  . ARG D  1 177 ? -37.985 12.983  18.611  1.00 31.47  ? 177  ARG D CZ  1 
ATOM   13960 N  NH1 . ARG D  1 177 ? -37.093 12.425  17.788  1.00 30.34  ? 177  ARG D NH1 1 
ATOM   13961 N  NH2 . ARG D  1 177 ? -37.631 13.340  19.841  1.00 33.63  ? 177  ARG D NH2 1 
ATOM   13962 N  N   . LEU D  1 178 ? -43.295 10.109  15.659  1.00 28.55  ? 178  LEU D N   1 
ATOM   13963 C  CA  . LEU D  1 178 ? -43.878 10.094  14.318  1.00 20.61  ? 178  LEU D CA  1 
ATOM   13964 C  C   . LEU D  1 178 ? -45.405 10.223  14.346  1.00 21.03  ? 178  LEU D C   1 
ATOM   13965 O  O   . LEU D  1 178 ? -45.996 10.886  13.502  1.00 21.57  ? 178  LEU D O   1 
ATOM   13966 C  CB  . LEU D  1 178 ? -43.483 8.835   13.561  1.00 20.56  ? 178  LEU D CB  1 
ATOM   13967 C  CG  . LEU D  1 178 ? -43.830 8.938   12.086  1.00 21.11  ? 178  LEU D CG  1 
ATOM   13968 C  CD1 . LEU D  1 178 ? -43.044 10.092  11.469  1.00 21.34  ? 178  LEU D CD1 1 
ATOM   13969 C  CD2 . LEU D  1 178 ? -43.548 7.636   11.385  1.00 21.17  ? 178  LEU D CD2 1 
ATOM   13970 N  N   . ALA D  1 179 ? -46.048 9.608   15.325  1.00 20.91  ? 179  ALA D N   1 
ATOM   13971 C  CA  . ALA D  1 179 ? -47.480 9.778   15.452  1.00 21.45  ? 179  ALA D CA  1 
ATOM   13972 C  C   . ALA D  1 179 ? -47.793 11.229  15.787  1.00 22.24  ? 179  ALA D C   1 
ATOM   13973 O  O   . ALA D  1 179 ? -48.845 11.757  15.408  1.00 22.46  ? 179  ALA D O   1 
ATOM   13974 C  CB  . ALA D  1 179 ? -48.020 8.861   16.505  1.00 30.24  ? 179  ALA D CB  1 
ATOM   13975 N  N   . LEU D  1 180 ? -46.870 11.876  16.497  1.00 28.37  ? 180  LEU D N   1 
ATOM   13976 C  CA  . LEU D  1 180 ? -47.024 13.291  16.845  1.00 29.49  ? 180  LEU D CA  1 
ATOM   13977 C  C   . LEU D  1 180 ? -46.875 14.216  15.628  1.00 31.94  ? 180  LEU D C   1 
ATOM   13978 O  O   . LEU D  1 180 ? -47.650 15.155  15.477  1.00 36.82  ? 180  LEU D O   1 
ATOM   13979 C  CB  . LEU D  1 180 ? -46.069 13.686  17.980  1.00 21.36  ? 180  LEU D CB  1 
ATOM   13980 C  CG  . LEU D  1 180 ? -46.631 13.696  19.404  1.00 21.40  ? 180  LEU D CG  1 
ATOM   13981 C  CD1 . LEU D  1 180 ? -47.639 12.576  19.635  1.00 21.50  ? 180  LEU D CD1 1 
ATOM   13982 C  CD2 . LEU D  1 180 ? -45.495 13.607  20.398  1.00 20.82  ? 180  LEU D CD2 1 
ATOM   13983 N  N   . GLN D  1 181 ? -45.896 13.946  14.763  1.00 27.46  ? 181  GLN D N   1 
ATOM   13984 C  CA  . GLN D  1 181 ? -45.780 14.663  13.492  1.00 29.47  ? 181  GLN D CA  1 
ATOM   13985 C  C   . GLN D  1 181 ? -47.022 14.439  12.666  1.00 28.55  ? 181  GLN D C   1 
ATOM   13986 O  O   . GLN D  1 181 ? -47.524 15.386  12.061  1.00 32.17  ? 181  GLN D O   1 
ATOM   13987 C  CB  . GLN D  1 181 ? -44.583 14.202  12.674  1.00 43.81  ? 181  GLN D CB  1 
ATOM   13988 C  CG  . GLN D  1 181 ? -43.447 15.181  12.613  1.00 52.52  ? 181  GLN D CG  1 
ATOM   13989 C  CD  . GLN D  1 181 ? -42.152 14.560  13.110  1.00 60.63  ? 181  GLN D CD  1 
ATOM   13990 O  OE1 . GLN D  1 181 ? -41.951 13.340  13.016  1.00 61.39  ? 181  GLN D OE1 1 
ATOM   13991 N  NE2 . GLN D  1 181 ? -41.270 15.393  13.659  1.00 64.19  ? 181  GLN D NE2 1 
ATOM   13992 N  N   . TRP D  1 182 ? -47.507 13.193  12.624  1.00 29.32  ? 182  TRP D N   1 
ATOM   13993 C  CA  . TRP D  1 182 ? -48.753 12.886  11.917  1.00 28.85  ? 182  TRP D CA  1 
ATOM   13994 C  C   . TRP D  1 182 ? -49.814 13.808  12.447  1.00 29.29  ? 182  TRP D C   1 
ATOM   13995 O  O   . TRP D  1 182 ? -50.514 14.443  11.671  1.00 30.19  ? 182  TRP D O   1 
ATOM   13996 C  CB  . TRP D  1 182 ? -49.221 11.447  12.133  1.00 23.37  ? 182  TRP D CB  1 
ATOM   13997 C  CG  . TRP D  1 182 ? -50.331 11.018  11.200  1.00 24.09  ? 182  TRP D CG  1 
ATOM   13998 C  CD1 . TRP D  1 182 ? -50.181 10.434  9.981   1.00 31.23  ? 182  TRP D CD1 1 
ATOM   13999 C  CD2 . TRP D  1 182 ? -51.748 11.126  11.413  1.00 24.81  ? 182  TRP D CD2 1 
ATOM   14000 N  NE1 . TRP D  1 182 ? -51.412 10.168  9.414   1.00 29.20  ? 182  TRP D NE1 1 
ATOM   14001 C  CE2 . TRP D  1 182 ? -52.387 10.589  10.272  1.00 28.10  ? 182  TRP D CE2 1 
ATOM   14002 C  CE3 . TRP D  1 182 ? -52.536 11.628  12.446  1.00 25.13  ? 182  TRP D CE3 1 
ATOM   14003 C  CZ2 . TRP D  1 182 ? -53.769 10.542  10.144  1.00 26.30  ? 182  TRP D CZ2 1 
ATOM   14004 C  CZ3 . TRP D  1 182 ? -53.913 11.584  12.310  1.00 26.05  ? 182  TRP D CZ3 1 
ATOM   14005 C  CH2 . TRP D  1 182 ? -54.514 11.041  11.169  1.00 26.78  ? 182  TRP D CH2 1 
ATOM   14006 N  N   . VAL D  1 183 ? -49.922 13.895  13.770  1.00 24.00  ? 183  VAL D N   1 
ATOM   14007 C  CA  . VAL D  1 183 ? -50.950 14.731  14.370  1.00 30.05  ? 183  VAL D CA  1 
ATOM   14008 C  C   . VAL D  1 183 ? -50.794 16.155  13.864  1.00 27.84  ? 183  VAL D C   1 
ATOM   14009 O  O   . VAL D  1 183 ? -51.767 16.831  13.510  1.00 28.62  ? 183  VAL D O   1 
ATOM   14010 C  CB  . VAL D  1 183 ? -50.931 14.655  15.909  1.00 37.49  ? 183  VAL D CB  1 
ATOM   14011 C  CG1 . VAL D  1 183 ? -51.000 16.037  16.534  1.00 37.75  ? 183  VAL D CG1 1 
ATOM   14012 C  CG2 . VAL D  1 183 ? -52.097 13.827  16.378  1.00 39.34  ? 183  VAL D CG2 1 
ATOM   14013 N  N   . GLN D  1 184 ? -49.545 16.570  13.759  1.00 25.19  ? 184  GLN D N   1 
ATOM   14014 C  CA  . GLN D  1 184 ? -49.242 17.926  13.377  1.00 26.53  ? 184  GLN D CA  1 
ATOM   14015 C  C   . GLN D  1 184 ? -49.692 18.222  11.955  1.00 26.34  ? 184  GLN D C   1 
ATOM   14016 O  O   . GLN D  1 184 ? -50.202 19.300  11.685  1.00 27.31  ? 184  GLN D O   1 
ATOM   14017 C  CB  . GLN D  1 184 ? -47.743 18.197  13.566  1.00 34.02  ? 184  GLN D CB  1 
ATOM   14018 C  CG  . GLN D  1 184 ? -47.364 19.647  13.775  1.00 33.83  ? 184  GLN D CG  1 
ATOM   14019 C  CD  . GLN D  1 184 ? -47.928 20.230  15.053  1.00 34.74  ? 184  GLN D CD  1 
ATOM   14020 O  OE1 . GLN D  1 184 ? -48.883 19.710  15.643  1.00 30.02  ? 184  GLN D OE1 1 
ATOM   14021 N  NE2 . GLN D  1 184 ? -47.335 21.333  15.489  1.00 39.85  ? 184  GLN D NE2 1 
ATOM   14022 N  N   . GLU D  1 185 ? -49.509 17.273  11.047  1.00 27.89  ? 185  GLU D N   1 
ATOM   14023 C  CA  . GLU D  1 185 ? -49.895 17.493  9.655   1.00 34.53  ? 185  GLU D CA  1 
ATOM   14024 C  C   . GLU D  1 185 ? -51.390 17.289  9.385   1.00 34.85  ? 185  GLU D C   1 
ATOM   14025 O  O   . GLU D  1 185 ? -52.001 18.007  8.584   1.00 36.75  ? 185  GLU D O   1 
ATOM   14026 C  CB  . GLU D  1 185 ? -49.087 16.594  8.722   1.00 47.88  ? 185  GLU D CB  1 
ATOM   14027 C  CG  . GLU D  1 185 ? -47.622 16.934  8.653   1.00 57.43  ? 185  GLU D CG  1 
ATOM   14028 C  CD  . GLU D  1 185 ? -46.772 15.739  8.262   1.00 66.90  ? 185  GLU D CD  1 
ATOM   14029 O  OE1 . GLU D  1 185 ? -47.311 14.784  7.642   1.00 68.57  ? 185  GLU D OE1 1 
ATOM   14030 O  OE2 . GLU D  1 185 ? -45.563 15.751  8.596   1.00 69.92  ? 185  GLU D OE2 1 
ATOM   14031 N  N   . ASN D  1 186 ? -51.952 16.244  9.973   1.00 27.21  ? 186  ASN D N   1 
ATOM   14032 C  CA  . ASN D  1 186 ? -53.317 15.878  9.656   1.00 28.21  ? 186  ASN D CA  1 
ATOM   14033 C  C   . ASN D  1 186 ? -54.470 16.125  10.633  1.00 29.79  ? 186  ASN D C   1 
ATOM   14034 O  O   . ASN D  1 186 ? -55.636 15.983  10.242  1.00 29.46  ? 186  ASN D O   1 
ATOM   14035 C  CB  . ASN D  1 186 ? -53.302 14.437  9.187   1.00 41.84  ? 186  ASN D CB  1 
ATOM   14036 C  CG  . ASN D  1 186 ? -52.208 14.199  8.190   1.00 46.50  ? 186  ASN D CG  1 
ATOM   14037 O  OD1 . ASN D  1 186 ? -52.314 14.617  7.035   1.00 48.53  ? 186  ASN D OD1 1 
ATOM   14038 N  ND2 . ASN D  1 186 ? -51.122 13.569  8.635   1.00 47.30  ? 186  ASN D ND2 1 
ATOM   14039 N  N   . ILE D  1 187 ? -54.192 16.523  11.873  1.00 41.23  ? 187  ILE D N   1 
ATOM   14040 C  CA  . ILE D  1 187 ? -55.277 16.437  12.857  1.00 44.09  ? 187  ILE D CA  1 
ATOM   14041 C  C   . ILE D  1 187 ? -56.340 17.462  12.551  1.00 43.88  ? 187  ILE D C   1 
ATOM   14042 O  O   . ILE D  1 187 ? -57.478 17.316  12.957  1.00 44.63  ? 187  ILE D O   1 
ATOM   14043 C  CB  . ILE D  1 187 ? -54.812 16.559  14.328  1.00 45.07  ? 187  ILE D CB  1 
ATOM   14044 C  CG1 . ILE D  1 187 ? -55.925 16.098  15.284  1.00 42.86  ? 187  ILE D CG1 1 
ATOM   14045 C  CG2 . ILE D  1 187 ? -54.404 17.988  14.641  1.00 46.46  ? 187  ILE D CG2 1 
ATOM   14046 C  CD1 . ILE D  1 187 ? -56.633 14.826  14.870  1.00 38.92  ? 187  ILE D CD1 1 
ATOM   14047 N  N   . ALA D  1 188 ? -55.954 18.479  11.795  1.00 46.35  ? 188  ALA D N   1 
ATOM   14048 C  CA  . ALA D  1 188 ? -56.845 19.569  11.441  1.00 47.73  ? 188  ALA D CA  1 
ATOM   14049 C  C   . ALA D  1 188 ? -58.083 19.081  10.681  1.00 46.69  ? 188  ALA D C   1 
ATOM   14050 O  O   . ALA D  1 188 ? -59.199 19.540  10.930  1.00 47.06  ? 188  ALA D O   1 
ATOM   14051 C  CB  . ALA D  1 188 ? -56.084 20.611  10.631  1.00 48.89  ? 188  ALA D CB  1 
ATOM   14052 N  N   . ALA D  1 189 ? -57.886 18.134  9.771   1.00 45.71  ? 189  ALA D N   1 
ATOM   14053 C  CA  . ALA D  1 189 ? -58.982 17.655  8.943   1.00 43.65  ? 189  ALA D CA  1 
ATOM   14054 C  C   . ALA D  1 189 ? -60.077 16.997  9.749   1.00 44.05  ? 189  ALA D C   1 
ATOM   14055 O  O   . ALA D  1 189 ? -61.174 16.828  9.255   1.00 51.44  ? 189  ALA D O   1 
ATOM   14056 C  CB  . ALA D  1 189 ? -58.485 16.700  7.892   1.00 34.06  ? 189  ALA D CB  1 
ATOM   14057 N  N   . PHE D  1 190 ? -59.785 16.589  10.973  1.00 33.09  ? 190  PHE D N   1 
ATOM   14058 C  CA  . PHE D  1 190 ? -60.830 16.044  11.829  1.00 33.64  ? 190  PHE D CA  1 
ATOM   14059 C  C   . PHE D  1 190 ? -61.366 17.103  12.765  1.00 34.54  ? 190  PHE D C   1 
ATOM   14060 O  O   . PHE D  1 190 ? -62.170 16.797  13.644  1.00 42.46  ? 190  PHE D O   1 
ATOM   14061 C  CB  . PHE D  1 190 ? -60.332 14.872  12.665  1.00 35.27  ? 190  PHE D CB  1 
ATOM   14062 C  CG  . PHE D  1 190 ? -59.637 13.816  11.879  1.00 33.64  ? 190  PHE D CG  1 
ATOM   14063 C  CD1 . PHE D  1 190 ? -58.305 13.979  11.500  1.00 33.60  ? 190  PHE D CD1 1 
ATOM   14064 C  CD2 . PHE D  1 190 ? -60.299 12.649  11.542  1.00 33.12  ? 190  PHE D CD2 1 
ATOM   14065 C  CE1 . PHE D  1 190 ? -57.650 13.006  10.776  1.00 33.83  ? 190  PHE D CE1 1 
ATOM   14066 C  CE2 . PHE D  1 190 ? -59.656 11.671  10.822  1.00 35.24  ? 190  PHE D CE2 1 
ATOM   14067 C  CZ  . PHE D  1 190 ? -58.319 11.848  10.437  1.00 35.11  ? 190  PHE D CZ  1 
ATOM   14068 N  N   . GLY D  1 191 ? -60.888 18.333  12.609  1.00 34.75  ? 191  GLY D N   1 
ATOM   14069 C  CA  . GLY D  1 191 ? -61.311 19.416  13.478  1.00 39.44  ? 191  GLY D CA  1 
ATOM   14070 C  C   . GLY D  1 191 ? -60.438 19.594  14.706  1.00 38.10  ? 191  GLY D C   1 
ATOM   14071 O  O   . GLY D  1 191 ? -60.883 20.102  15.735  1.00 39.31  ? 191  GLY D O   1 
ATOM   14072 N  N   . GLY D  1 192 ? -59.191 19.158  14.612  1.00 44.05  ? 192  GLY D N   1 
ATOM   14073 C  CA  . GLY D  1 192 ? -58.242 19.383  15.682  1.00 45.86  ? 192  GLY D CA  1 
ATOM   14074 C  C   . GLY D  1 192 ? -57.531 20.710  15.505  1.00 47.96  ? 192  GLY D C   1 
ATOM   14075 O  O   . GLY D  1 192 ? -57.560 21.302  14.425  1.00 52.57  ? 192  GLY D O   1 
ATOM   14076 N  N   . ASP D  1 193 ? -56.908 21.192  16.572  1.00 32.14  ? 193  ASP D N   1 
ATOM   14077 C  CA  . ASP D  1 193 ? -56.051 22.353  16.468  1.00 32.63  ? 193  ASP D CA  1 
ATOM   14078 C  C   . ASP D  1 193 ? -54.609 21.886  16.590  1.00 30.71  ? 193  ASP D C   1 
ATOM   14079 O  O   . ASP D  1 193 ? -54.178 21.511  17.674  1.00 29.99  ? 193  ASP D O   1 
ATOM   14080 C  CB  . ASP D  1 193 ? -56.373 23.354  17.577  1.00 54.36  ? 193  ASP D CB  1 
ATOM   14081 C  CG  . ASP D  1 193 ? -55.624 24.681  17.417  1.00 61.27  ? 193  ASP D CG  1 
ATOM   14082 O  OD1 . ASP D  1 193 ? -54.448 24.679  16.982  1.00 60.14  ? 193  ASP D OD1 1 
ATOM   14083 O  OD2 . ASP D  1 193 ? -56.219 25.738  17.738  1.00 65.47  ? 193  ASP D OD2 1 
ATOM   14084 N  N   . PRO D  1 194 ? -53.857 21.910  15.477  1.00 36.08  ? 194  PRO D N   1 
ATOM   14085 C  CA  . PRO D  1 194 ? -52.422 21.620  15.464  1.00 38.03  ? 194  PRO D CA  1 
ATOM   14086 C  C   . PRO D  1 194 ? -51.655 22.419  16.498  1.00 42.23  ? 194  PRO D C   1 
ATOM   14087 O  O   . PRO D  1 194 ? -50.589 21.962  16.916  1.00 39.73  ? 194  PRO D O   1 
ATOM   14088 C  CB  . PRO D  1 194 ? -51.999 22.065  14.070  1.00 49.17  ? 194  PRO D CB  1 
ATOM   14089 C  CG  . PRO D  1 194 ? -53.177 21.741  13.246  1.00 51.82  ? 194  PRO D CG  1 
ATOM   14090 C  CD  . PRO D  1 194 ? -54.391 22.009  14.111  1.00 50.86  ? 194  PRO D CD  1 
ATOM   14091 N  N   . MET D  1 195 ? -52.166 23.589  16.883  1.00 60.26  ? 195  MET D N   1 
ATOM   14092 C  CA  . MET D  1 195 ? -51.485 24.418  17.877  1.00 61.58  ? 195  MET D CA  1 
ATOM   14093 C  C   . MET D  1 195 ? -51.981 24.296  19.329  1.00 59.99  ? 195  MET D C   1 
ATOM   14094 O  O   . MET D  1 195 ? -51.400 24.906  20.226  1.00 61.14  ? 195  MET D O   1 
ATOM   14095 C  CB  . MET D  1 195 ? -51.458 25.882  17.437  1.00 58.22  ? 195  MET D CB  1 
ATOM   14096 C  CG  . MET D  1 195 ? -50.484 26.176  16.313  1.00 56.26  ? 195  MET D CG  1 
ATOM   14097 S  SD  . MET D  1 195 ? -50.895 27.718  15.479  1.00 124.72 ? 195  MET D SD  1 
ATOM   14098 C  CE  . MET D  1 195 ? -52.611 27.436  15.013  1.00 40.40  ? 195  MET D CE  1 
ATOM   14099 N  N   . SER D  1 196 ? -53.046 23.543  19.582  1.00 46.74  ? 196  SER D N   1 
ATOM   14100 C  CA  . SER D  1 196 ? -53.283 23.121  20.959  1.00 47.08  ? 196  SER D CA  1 
ATOM   14101 C  C   . SER D  1 196 ? -53.274 21.602  21.077  1.00 46.22  ? 196  SER D C   1 
ATOM   14102 O  O   . SER D  1 196 ? -54.287 20.942  20.851  1.00 49.35  ? 196  SER D O   1 
ATOM   14103 C  CB  . SER D  1 196 ? -54.601 23.687  21.487  1.00 58.50  ? 196  SER D CB  1 
ATOM   14104 O  OG  . SER D  1 196 ? -54.949 23.097  22.725  1.00 59.70  ? 196  SER D OG  1 
ATOM   14105 N  N   . VAL D  1 197 ? -52.158 21.063  21.542  1.00 41.47  ? 197  VAL D N   1 
ATOM   14106 C  CA  . VAL D  1 197 ? -51.979 19.627  21.591  1.00 36.27  ? 197  VAL D CA  1 
ATOM   14107 C  C   . VAL D  1 197 ? -51.394 19.251  22.928  1.00 34.74  ? 197  VAL D C   1 
ATOM   14108 O  O   . VAL D  1 197 ? -50.275 19.645  23.250  1.00 35.99  ? 197  VAL D O   1 
ATOM   14109 C  CB  . VAL D  1 197 ? -51.045 19.159  20.479  1.00 29.01  ? 197  VAL D CB  1 
ATOM   14110 C  CG1 . VAL D  1 197 ? -50.565 17.766  20.754  1.00 24.99  ? 197  VAL D CG1 1 
ATOM   14111 C  CG2 . VAL D  1 197 ? -51.764 19.215  19.144  1.00 29.67  ? 197  VAL D CG2 1 
ATOM   14112 N  N   . THR D  1 198 ? -52.155 18.492  23.707  1.00 35.05  ? 198  THR D N   1 
ATOM   14113 C  CA  . THR D  1 198 ? -51.708 18.076  25.025  1.00 30.88  ? 198  THR D CA  1 
ATOM   14114 C  C   . THR D  1 198 ? -51.418 16.590  25.032  1.00 29.77  ? 198  THR D C   1 
ATOM   14115 O  O   . THR D  1 198 ? -52.299 15.780  24.721  1.00 30.02  ? 198  THR D O   1 
ATOM   14116 C  CB  . THR D  1 198 ? -52.772 18.336  26.085  1.00 27.02  ? 198  THR D CB  1 
ATOM   14117 O  OG1 . THR D  1 198 ? -53.108 19.727  26.106  1.00 28.05  ? 198  THR D OG1 1 
ATOM   14118 C  CG2 . THR D  1 198 ? -52.257 17.915  27.445  1.00 26.62  ? 198  THR D CG2 1 
ATOM   14119 N  N   . LEU D  1 199 ? -50.183 16.230  25.376  1.00 29.97  ? 199  LEU D N   1 
ATOM   14120 C  CA  . LEU D  1 199 ? -49.836 14.823  25.523  1.00 28.95  ? 199  LEU D CA  1 
ATOM   14121 C  C   . LEU D  1 199 ? -50.291 14.419  26.907  1.00 29.60  ? 199  LEU D C   1 
ATOM   14122 O  O   . LEU D  1 199 ? -50.174 15.197  27.849  1.00 29.29  ? 199  LEU D O   1 
ATOM   14123 C  CB  . LEU D  1 199 ? -48.331 14.610  25.416  1.00 22.44  ? 199  LEU D CB  1 
ATOM   14124 C  CG  . LEU D  1 199 ? -47.603 15.115  24.182  1.00 22.16  ? 199  LEU D CG  1 
ATOM   14125 C  CD1 . LEU D  1 199 ? -46.140 14.770  24.300  1.00 21.34  ? 199  LEU D CD1 1 
ATOM   14126 C  CD2 . LEU D  1 199 ? -48.200 14.487  22.961  1.00 22.22  ? 199  LEU D CD2 1 
ATOM   14127 N  N   . PHE D  1 200 ? -50.856 13.228  27.031  1.00 23.76  ? 200  PHE D N   1 
ATOM   14128 C  CA  . PHE D  1 200 ? -51.145 12.695  28.352  1.00 24.06  ? 200  PHE D CA  1 
ATOM   14129 C  C   . PHE D  1 200 ? -50.959 11.193  28.380  1.00 23.62  ? 200  PHE D C   1 
ATOM   14130 O  O   . PHE D  1 200 ? -51.347 10.488  27.450  1.00 23.59  ? 200  PHE D O   1 
ATOM   14131 C  CB  . PHE D  1 200 ? -52.506 13.179  28.918  1.00 25.31  ? 200  PHE D CB  1 
ATOM   14132 C  CG  . PHE D  1 200 ? -53.733 12.467  28.385  1.00 25.98  ? 200  PHE D CG  1 
ATOM   14133 C  CD1 . PHE D  1 200 ? -54.119 12.583  27.061  1.00 33.28  ? 200  PHE D CD1 1 
ATOM   14134 C  CD2 . PHE D  1 200 ? -54.558 11.759  29.243  1.00 26.73  ? 200  PHE D CD2 1 
ATOM   14135 C  CE1 . PHE D  1 200 ? -55.284 11.954  26.593  1.00 33.48  ? 200  PHE D CE1 1 
ATOM   14136 C  CE2 . PHE D  1 200 ? -55.719 11.134  28.781  1.00 27.51  ? 200  PHE D CE2 1 
ATOM   14137 C  CZ  . PHE D  1 200 ? -56.075 11.226  27.458  1.00 27.54  ? 200  PHE D CZ  1 
ATOM   14138 N  N   . GLY D  1 201 ? -50.326 10.703  29.435  1.00 25.48  ? 201  GLY D N   1 
ATOM   14139 C  CA  . GLY D  1 201 ? -50.086 9.280   29.513  1.00 24.99  ? 201  GLY D CA  1 
ATOM   14140 C  C   . GLY D  1 201 ? -49.966 8.788   30.932  1.00 29.22  ? 201  GLY D C   1 
ATOM   14141 O  O   . GLY D  1 201 ? -49.870 9.576   31.878  1.00 33.92  ? 201  GLY D O   1 
ATOM   14142 N  N   . GLU D  1 202 ? -49.954 7.471   31.083  1.00 32.52  ? 202  GLU D N   1 
ATOM   14143 C  CA  . GLU D  1 202 ? -49.879 6.869   32.402  1.00 35.13  ? 202  GLU D CA  1 
ATOM   14144 C  C   . GLU D  1 202 ? -48.732 5.845   32.482  1.00 32.83  ? 202  GLU D C   1 
ATOM   14145 O  O   . GLU D  1 202 ? -48.416 5.180   31.497  1.00 32.28  ? 202  GLU D O   1 
ATOM   14146 C  CB  . GLU D  1 202 ? -51.244 6.271   32.757  1.00 41.84  ? 202  GLU D CB  1 
ATOM   14147 C  CG  . GLU D  1 202 ? -51.350 5.705   34.135  1.00 45.59  ? 202  GLU D CG  1 
ATOM   14148 C  CD  . GLU D  1 202 ? -51.011 4.240   34.146  1.00 50.52  ? 202  GLU D CD  1 
ATOM   14149 O  OE1 . GLU D  1 202 ? -51.015 3.623   33.060  1.00 50.82  ? 202  GLU D OE1 1 
ATOM   14150 O  OE2 . GLU D  1 202 ? -50.734 3.702   35.234  1.00 53.84  ? 202  GLU D OE2 1 
ATOM   14151 N  N   . SER D  1 203 ? -48.099 5.755   33.651  1.00 27.84  ? 203  SER D N   1 
ATOM   14152 C  CA  . SER D  1 203 ? -46.971 4.848   33.899  1.00 28.97  ? 203  SER D CA  1 
ATOM   14153 C  C   . SER D  1 203 ? -45.803 5.064   32.923  1.00 27.54  ? 203  SER D C   1 
ATOM   14154 O  O   . SER D  1 203 ? -45.218 6.146   32.874  1.00 26.45  ? 203  SER D O   1 
ATOM   14155 C  CB  . SER D  1 203 ? -47.430 3.387   33.890  1.00 40.58  ? 203  SER D CB  1 
ATOM   14156 O  OG  . SER D  1 203 ? -46.531 2.560   34.614  1.00 43.57  ? 203  SER D OG  1 
ATOM   14157 N  N   . ALA D  1 204 ? -45.466 4.037   32.146  1.00 30.00  ? 204  ALA D N   1 
ATOM   14158 C  CA  . ALA D  1 204 ? -44.456 4.173   31.103  1.00 25.05  ? 204  ALA D CA  1 
ATOM   14159 C  C   . ALA D  1 204 ? -44.906 5.190   30.068  1.00 23.43  ? 204  ALA D C   1 
ATOM   14160 O  O   . ALA D  1 204 ? -44.090 5.820   29.409  1.00 21.78  ? 204  ALA D O   1 
ATOM   14161 C  CB  . ALA D  1 204 ? -44.198 2.846   30.433  1.00 20.62  ? 204  ALA D CB  1 
ATOM   14162 N  N   . GLY D  1 205 ? -46.214 5.338   29.911  1.00 20.96  ? 205  GLY D N   1 
ATOM   14163 C  CA  . GLY D  1 205 ? -46.730 6.333   28.998  1.00 20.94  ? 205  GLY D CA  1 
ATOM   14164 C  C   . GLY D  1 205 ? -46.375 7.719   29.487  1.00 22.50  ? 205  GLY D C   1 
ATOM   14165 O  O   . GLY D  1 205 ? -45.975 8.580   28.709  1.00 20.52  ? 205  GLY D O   1 
ATOM   14166 N  N   . ALA D  1 206 ? -46.519 7.935   30.786  1.00 21.21  ? 206  ALA D N   1 
ATOM   14167 C  CA  . ALA D  1 206 ? -46.201 9.228   31.355  1.00 21.24  ? 206  ALA D CA  1 
ATOM   14168 C  C   . ALA D  1 206 ? -44.689 9.435   31.349  1.00 20.56  ? 206  ALA D C   1 
ATOM   14169 O  O   . ALA D  1 206 ? -44.202 10.559  31.185  1.00 20.43  ? 206  ALA D O   1 
ATOM   14170 C  CB  . ALA D  1 206 ? -46.762 9.345   32.755  1.00 27.40  ? 206  ALA D CB  1 
ATOM   14171 N  N   . ALA D  1 207 ? -43.947 8.346   31.520  1.00 21.57  ? 207  ALA D N   1 
ATOM   14172 C  CA  . ALA D  1 207 ? -42.504 8.405   31.372  1.00 23.98  ? 207  ALA D CA  1 
ATOM   14173 C  C   . ALA D  1 207 ? -42.188 8.939   29.982  1.00 26.24  ? 207  ALA D C   1 
ATOM   14174 O  O   . ALA D  1 207 ? -41.337 9.804   29.822  1.00 27.92  ? 207  ALA D O   1 
ATOM   14175 C  CB  . ALA D  1 207 ? -41.884 7.032   31.571  1.00 20.06  ? 207  ALA D CB  1 
ATOM   14176 N  N   . SER D  1 208 ? -42.899 8.428   28.983  1.00 19.36  ? 208  SER D N   1 
ATOM   14177 C  CA  . SER D  1 208 ? -42.678 8.831   27.608  1.00 19.12  ? 208  SER D CA  1 
ATOM   14178 C  C   . SER D  1 208 ? -43.019 10.288  27.408  1.00 23.18  ? 208  SER D C   1 
ATOM   14179 O  O   . SER D  1 208 ? -42.284 10.991  26.732  1.00 25.10  ? 208  SER D O   1 
ATOM   14180 C  CB  . SER D  1 208 ? -43.498 7.975   26.659  1.00 19.24  ? 208  SER D CB  1 
ATOM   14181 O  OG  . SER D  1 208 ? -43.203 6.617   26.875  1.00 19.18  ? 208  SER D OG  1 
ATOM   14182 N  N   . VAL D  1 209 ? -44.134 10.737  27.980  1.00 22.25  ? 209  VAL D N   1 
ATOM   14183 C  CA  . VAL D  1 209 ? -44.526 12.140  27.882  1.00 23.47  ? 209  VAL D CA  1 
ATOM   14184 C  C   . VAL D  1 209 ? -43.397 12.999  28.442  1.00 25.53  ? 209  VAL D C   1 
ATOM   14185 O  O   . VAL D  1 209 ? -42.947 13.964  27.808  1.00 26.52  ? 209  VAL D O   1 
ATOM   14186 C  CB  . VAL D  1 209 ? -45.835 12.416  28.644  1.00 25.96  ? 209  VAL D CB  1 
ATOM   14187 C  CG1 . VAL D  1 209 ? -46.219 13.870  28.551  1.00 25.95  ? 209  VAL D CG1 1 
ATOM   14188 C  CG2 . VAL D  1 209 ? -46.945 11.567  28.088  1.00 28.53  ? 209  VAL D CG2 1 
ATOM   14189 N  N   . GLY D  1 210 ? -42.909 12.625  29.618  1.00 26.56  ? 210  GLY D N   1 
ATOM   14190 C  CA  . GLY D  1 210 ? -41.747 13.290  30.177  1.00 29.21  ? 210  GLY D CA  1 
ATOM   14191 C  C   . GLY D  1 210 ? -40.539 13.223  29.253  1.00 29.93  ? 210  GLY D C   1 
ATOM   14192 O  O   . GLY D  1 210 ? -39.711 14.126  29.197  1.00 19.47  ? 210  GLY D O   1 
ATOM   14193 N  N   . MET D  1 211 ? -40.452 12.146  28.497  1.00 19.07  ? 211  MET D N   1 
ATOM   14194 C  CA  . MET D  1 211 ? -39.320 11.934  27.638  1.00 18.74  ? 211  MET D CA  1 
ATOM   14195 C  C   . MET D  1 211 ? -39.387 12.836  26.390  1.00 19.54  ? 211  MET D C   1 
ATOM   14196 O  O   . MET D  1 211 ? -38.360 13.233  25.853  1.00 18.83  ? 211  MET D O   1 
ATOM   14197 C  CB  . MET D  1 211 ? -39.251 10.460  27.267  1.00 18.48  ? 211  MET D CB  1 
ATOM   14198 C  CG  . MET D  1 211 ? -37.853 9.942   27.100  1.00 18.26  ? 211  MET D CG  1 
ATOM   14199 S  SD  . MET D  1 211 ? -37.346 8.924   28.479  1.00 29.36  ? 211  MET D SD  1 
ATOM   14200 C  CE  . MET D  1 211 ? -38.898 8.154   28.892  1.00 20.99  ? 211  MET D CE  1 
ATOM   14201 N  N   . HIS D  1 212 ? -40.586 13.167  25.922  1.00 22.77  ? 212  HIS D N   1 
ATOM   14202 C  CA  . HIS D  1 212 ? -40.711 14.127  24.824  1.00 26.07  ? 212  HIS D CA  1 
ATOM   14203 C  C   . HIS D  1 212 ? -40.513 15.543  25.352  1.00 28.31  ? 212  HIS D C   1 
ATOM   14204 O  O   . HIS D  1 212 ? -40.038 16.410  24.629  1.00 31.33  ? 212  HIS D O   1 
ATOM   14205 C  CB  . HIS D  1 212 ? -42.064 14.026  24.097  1.00 19.69  ? 212  HIS D CB  1 
ATOM   14206 C  CG  . HIS D  1 212 ? -42.304 12.708  23.426  1.00 19.41  ? 212  HIS D CG  1 
ATOM   14207 N  ND1 . HIS D  1 212 ? -41.486 12.215  22.435  1.00 25.46  ? 212  HIS D ND1 1 
ATOM   14208 C  CD2 . HIS D  1 212 ? -43.286 11.791  23.593  1.00 24.05  ? 212  HIS D CD2 1 
ATOM   14209 C  CE1 . HIS D  1 212 ? -41.940 11.041  22.032  1.00 19.03  ? 212  HIS D CE1 1 
ATOM   14210 N  NE2 . HIS D  1 212 ? -43.032 10.761  22.719  1.00 23.64  ? 212  HIS D NE2 1 
ATOM   14211 N  N   . ILE D  1 213 ? -40.890 15.783  26.606  1.00 33.15  ? 213  ILE D N   1 
ATOM   14212 C  CA  . ILE D  1 213 ? -40.586 17.069  27.229  1.00 34.34  ? 213  ILE D CA  1 
ATOM   14213 C  C   . ILE D  1 213 ? -39.073 17.317  27.181  1.00 33.48  ? 213  ILE D C   1 
ATOM   14214 O  O   . ILE D  1 213 ? -38.616 18.432  26.964  1.00 35.86  ? 213  ILE D O   1 
ATOM   14215 C  CB  . ILE D  1 213 ? -41.073 17.130  28.692  1.00 30.00  ? 213  ILE D CB  1 
ATOM   14216 C  CG1 . ILE D  1 213 ? -42.591 17.089  28.748  1.00 21.20  ? 213  ILE D CG1 1 
ATOM   14217 C  CG2 . ILE D  1 213 ? -40.563 18.381  29.377  1.00 21.28  ? 213  ILE D CG2 1 
ATOM   14218 C  CD1 . ILE D  1 213 ? -43.136 17.100  30.122  1.00 21.59  ? 213  ILE D CD1 1 
ATOM   14219 N  N   . LEU D  1 214 ? -38.300 16.255  27.348  1.00 30.29  ? 214  LEU D N   1 
ATOM   14220 C  CA  . LEU D  1 214 ? -36.860 16.387  27.490  1.00 31.05  ? 214  LEU D CA  1 
ATOM   14221 C  C   . LEU D  1 214 ? -36.070 16.205  26.188  1.00 34.78  ? 214  LEU D C   1 
ATOM   14222 O  O   . LEU D  1 214 ? -34.838 16.304  26.184  1.00 39.24  ? 214  LEU D O   1 
ATOM   14223 C  CB  . LEU D  1 214 ? -36.365 15.399  28.545  1.00 24.94  ? 214  LEU D CB  1 
ATOM   14224 C  CG  . LEU D  1 214 ? -36.965 15.581  29.930  1.00 19.64  ? 214  LEU D CG  1 
ATOM   14225 C  CD1 . LEU D  1 214 ? -36.826 14.317  30.691  1.00 32.14  ? 214  LEU D CD1 1 
ATOM   14226 C  CD2 . LEU D  1 214 ? -36.234 16.654  30.643  1.00 20.06  ? 214  LEU D CD2 1 
ATOM   14227 N  N   . SER D  1 215 ? -36.767 15.925  25.090  1.00 26.33  ? 215  SER D N   1 
ATOM   14228 C  CA  . SER D  1 215 ? -36.098 15.639  23.818  1.00 26.62  ? 215  SER D CA  1 
ATOM   14229 C  C   . SER D  1 215 ? -36.422 16.738  22.848  1.00 25.48  ? 215  SER D C   1 
ATOM   14230 O  O   . SER D  1 215 ? -37.588 16.942  22.527  1.00 25.86  ? 215  SER D O   1 
ATOM   14231 C  CB  . SER D  1 215 ? -36.585 14.315  23.230  1.00 39.37  ? 215  SER D CB  1 
ATOM   14232 O  OG  . SER D  1 215 ? -35.891 14.011  22.030  1.00 42.16  ? 215  SER D OG  1 
ATOM   14233 N  N   . LEU D  1 216 ? -35.404 17.432  22.354  1.00 29.24  ? 216  LEU D N   1 
ATOM   14234 C  CA  . LEU D  1 216 ? -35.660 18.653  21.591  1.00 31.85  ? 216  LEU D CA  1 
ATOM   14235 C  C   . LEU D  1 216 ? -36.575 18.512  20.359  1.00 31.99  ? 216  LEU D C   1 
ATOM   14236 O  O   . LEU D  1 216 ? -37.575 19.225  20.270  1.00 34.09  ? 216  LEU D O   1 
ATOM   14237 C  CB  . LEU D  1 216 ? -34.372 19.414  21.273  1.00 33.33  ? 216  LEU D CB  1 
ATOM   14238 C  CG  . LEU D  1 216 ? -34.543 20.900  21.584  1.00 34.85  ? 216  LEU D CG  1 
ATOM   14239 C  CD1 . LEU D  1 216 ? -35.409 21.624  20.529  1.00 33.84  ? 216  LEU D CD1 1 
ATOM   14240 C  CD2 . LEU D  1 216 ? -35.125 21.057  22.990  1.00 33.95  ? 216  LEU D CD2 1 
ATOM   14241 N  N   . PRO D  1 217 ? -36.250 17.605  19.418  1.00 26.17  ? 217  PRO D N   1 
ATOM   14242 C  CA  . PRO D  1 217 ? -37.164 17.444  18.292  1.00 24.22  ? 217  PRO D CA  1 
ATOM   14243 C  C   . PRO D  1 217 ? -38.609 17.216  18.708  1.00 24.97  ? 217  PRO D C   1 
ATOM   14244 O  O   . PRO D  1 217 ? -39.493 17.726  18.021  1.00 32.13  ? 217  PRO D O   1 
ATOM   14245 C  CB  . PRO D  1 217 ? -36.613 16.226  17.548  1.00 36.34  ? 217  PRO D CB  1 
ATOM   14246 C  CG  . PRO D  1 217 ? -35.598 15.628  18.442  1.00 39.49  ? 217  PRO D CG  1 
ATOM   14247 C  CD  . PRO D  1 217 ? -35.063 16.755  19.255  1.00 40.35  ? 217  PRO D CD  1 
ATOM   14248 N  N   . SER D  1 218 ? -38.868 16.517  19.807  1.00 21.53  ? 218  SER D N   1 
ATOM   14249 C  CA  . SER D  1 218 ? -40.267 16.310  20.206  1.00 24.99  ? 218  SER D CA  1 
ATOM   14250 C  C   . SER D  1 218 ? -40.988 17.600  20.635  1.00 29.22  ? 218  SER D C   1 
ATOM   14251 O  O   . SER D  1 218 ? -42.205 17.731  20.453  1.00 21.43  ? 218  SER D O   1 
ATOM   14252 C  CB  . SER D  1 218 ? -40.396 15.238  21.295  1.00 20.05  ? 218  SER D CB  1 
ATOM   14253 O  OG  . SER D  1 218 ? -40.306 13.935  20.746  1.00 19.55  ? 218  SER D OG  1 
ATOM   14254 N  N   . ARG D  1 219 ? -40.222 18.550  21.168  1.00 36.09  ? 219  ARG D N   1 
ATOM   14255 C  CA  . ARG D  1 219 ? -40.774 19.695  21.887  1.00 39.37  ? 219  ARG D CA  1 
ATOM   14256 C  C   . ARG D  1 219 ? -41.831 20.507  21.149  1.00 39.73  ? 219  ARG D C   1 
ATOM   14257 O  O   . ARG D  1 219 ? -42.721 21.081  21.781  1.00 41.44  ? 219  ARG D O   1 
ATOM   14258 C  CB  . ARG D  1 219 ? -39.658 20.629  22.355  1.00 45.83  ? 219  ARG D CB  1 
ATOM   14259 C  CG  . ARG D  1 219 ? -39.210 20.395  23.793  1.00 50.77  ? 219  ARG D CG  1 
ATOM   14260 C  CD  . ARG D  1 219 ? -40.388 20.135  24.732  1.00 54.31  ? 219  ARG D CD  1 
ATOM   14261 N  NE  . ARG D  1 219 ? -41.265 21.292  24.906  1.00 59.23  ? 219  ARG D NE  1 
ATOM   14262 C  CZ  . ARG D  1 219 ? -41.152 22.181  25.891  1.00 62.54  ? 219  ARG D CZ  1 
ATOM   14263 N  NH1 . ARG D  1 219 ? -40.180 22.061  26.801  1.00 60.58  ? 219  ARG D NH1 1 
ATOM   14264 N  NH2 . ARG D  1 219 ? -42.012 23.195  25.960  1.00 64.54  ? 219  ARG D NH2 1 
ATOM   14265 N  N   . SER D  1 220 ? -41.724 20.566  19.825  1.00 39.19  ? 220  SER D N   1 
ATOM   14266 C  CA  . SER D  1 220 ? -42.595 21.422  19.025  1.00 38.51  ? 220  SER D CA  1 
ATOM   14267 C  C   . SER D  1 220 ? -43.803 20.676  18.501  1.00 38.55  ? 220  SER D C   1 
ATOM   14268 O  O   . SER D  1 220 ? -44.540 21.185  17.662  1.00 39.71  ? 220  SER D O   1 
ATOM   14269 C  CB  . SER D  1 220 ? -41.844 21.993  17.837  1.00 29.56  ? 220  SER D CB  1 
ATOM   14270 O  OG  . SER D  1 220 ? -41.670 20.981  16.869  1.00 27.55  ? 220  SER D OG  1 
ATOM   14271 N  N   . LEU D  1 221 ? -43.973 19.440  18.933  1.00 32.90  ? 221  LEU D N   1 
ATOM   14272 C  CA  . LEU D  1 221 ? -45.107 18.671  18.465  1.00 34.33  ? 221  LEU D CA  1 
ATOM   14273 C  C   . LEU D  1 221 ? -46.251 18.742  19.468  1.00 35.28  ? 221  LEU D C   1 
ATOM   14274 O  O   . LEU D  1 221 ? -47.336 18.222  19.222  1.00 35.12  ? 221  LEU D O   1 
ATOM   14275 C  CB  . LEU D  1 221 ? -44.683 17.227  18.185  1.00 29.89  ? 221  LEU D CB  1 
ATOM   14276 C  CG  . LEU D  1 221 ? -43.395 17.181  17.363  1.00 27.64  ? 221  LEU D CG  1 
ATOM   14277 C  CD1 . LEU D  1 221 ? -42.887 15.773  17.163  1.00 21.29  ? 221  LEU D CD1 1 
ATOM   14278 C  CD2 . LEU D  1 221 ? -43.661 17.849  16.040  1.00 28.29  ? 221  LEU D CD2 1 
ATOM   14279 N  N   . PHE D  1 222 ? -46.014 19.403  20.593  1.00 23.52  ? 222  PHE D N   1 
ATOM   14280 C  CA  . PHE D  1 222 ? -47.051 19.516  21.604  1.00 23.96  ? 222  PHE D CA  1 
ATOM   14281 C  C   . PHE D  1 222 ? -46.924 20.786  22.427  1.00 28.04  ? 222  PHE D C   1 
ATOM   14282 O  O   . PHE D  1 222 ? -46.032 21.596  22.193  1.00 28.12  ? 222  PHE D O   1 
ATOM   14283 C  CB  . PHE D  1 222 ? -47.077 18.285  22.502  1.00 23.27  ? 222  PHE D CB  1 
ATOM   14284 C  CG  . PHE D  1 222 ? -45.863 18.130  23.367  1.00 22.63  ? 222  PHE D CG  1 
ATOM   14285 C  CD1 . PHE D  1 222 ? -44.669 17.663  22.837  1.00 21.94  ? 222  PHE D CD1 1 
ATOM   14286 C  CD2 . PHE D  1 222 ? -45.921 18.420  24.719  1.00 22.80  ? 222  PHE D CD2 1 
ATOM   14287 C  CE1 . PHE D  1 222 ? -43.544 17.501  23.638  1.00 30.76  ? 222  PHE D CE1 1 
ATOM   14288 C  CE2 . PHE D  1 222 ? -44.804 18.260  25.520  1.00 22.28  ? 222  PHE D CE2 1 
ATOM   14289 C  CZ  . PHE D  1 222 ? -43.610 17.798  24.974  1.00 21.60  ? 222  PHE D CZ  1 
ATOM   14290 N  N   . HIS D  1 223 ? -47.853 20.968  23.362  1.00 39.90  ? 223  HIS D N   1 
ATOM   14291 C  CA  . HIS D  1 223 ? -48.002 22.225  24.094  1.00 39.75  ? 223  HIS D CA  1 
ATOM   14292 C  C   . HIS D  1 223 ? -48.106 22.029  25.597  1.00 41.89  ? 223  HIS D C   1 
ATOM   14293 O  O   . HIS D  1 223 ? -47.333 22.593  26.378  1.00 44.58  ? 223  HIS D O   1 
ATOM   14294 C  CB  . HIS D  1 223 ? -49.158 23.022  23.524  1.00 34.39  ? 223  HIS D CB  1 
ATOM   14295 C  CG  . HIS D  1 223 ? -49.032 23.241  22.051  1.00 37.44  ? 223  HIS D CG  1 
ATOM   14296 N  ND1 . HIS D  1 223 ? -49.745 22.511  21.124  1.00 37.97  ? 223  HIS D ND1 1 
ATOM   14297 C  CD2 . HIS D  1 223 ? -48.225 24.067  21.340  1.00 39.28  ? 223  HIS D CD2 1 
ATOM   14298 C  CE1 . HIS D  1 223 ? -49.400 22.895  19.908  1.00 39.00  ? 223  HIS D CE1 1 
ATOM   14299 N  NE2 . HIS D  1 223 ? -48.495 23.851  20.011  1.00 39.70  ? 223  HIS D NE2 1 
ATOM   14300 N  N   . ARG D  1 224 ? -49.102 21.258  26.000  1.00 34.33  ? 224  ARG D N   1 
ATOM   14301 C  CA  . ARG D  1 224 ? -49.244 20.891  27.397  1.00 36.27  ? 224  ARG D CA  1 
ATOM   14302 C  C   . ARG D  1 224 ? -48.906 19.402  27.640  1.00 35.34  ? 224  ARG D C   1 
ATOM   14303 O  O   . ARG D  1 224 ? -48.980 18.566  26.721  1.00 32.83  ? 224  ARG D O   1 
ATOM   14304 C  CB  . ARG D  1 224 ? -50.649 21.260  27.887  1.00 43.59  ? 224  ARG D CB  1 
ATOM   14305 C  CG  . ARG D  1 224 ? -50.836 22.766  28.055  1.00 46.58  ? 224  ARG D CG  1 
ATOM   14306 C  CD  . ARG D  1 224 ? -52.286 23.250  27.907  1.00 49.32  ? 224  ARG D CD  1 
ATOM   14307 N  NE  . ARG D  1 224 ? -52.670 23.579  26.531  1.00 52.92  ? 224  ARG D NE  1 
ATOM   14308 C  CZ  . ARG D  1 224 ? -52.115 24.548  25.798  1.00 57.25  ? 224  ARG D CZ  1 
ATOM   14309 N  NH1 . ARG D  1 224 ? -51.131 25.288  26.299  1.00 58.99  ? 224  ARG D NH1 1 
ATOM   14310 N  NH2 . ARG D  1 224 ? -52.534 24.775  24.552  1.00 58.02  ? 224  ARG D NH2 1 
ATOM   14311 N  N   . ALA D  1 225 ? -48.482 19.082  28.862  1.00 40.53  ? 225  ALA D N   1 
ATOM   14312 C  CA  . ALA D  1 225 ? -48.234 17.677  29.203  1.00 36.82  ? 225  ALA D CA  1 
ATOM   14313 C  C   . ALA D  1 225 ? -48.968 17.204  30.479  1.00 36.86  ? 225  ALA D C   1 
ATOM   14314 O  O   . ALA D  1 225 ? -49.169 17.978  31.413  1.00 37.02  ? 225  ALA D O   1 
ATOM   14315 C  CB  . ALA D  1 225 ? -46.734 17.415  29.295  1.00 23.17  ? 225  ALA D CB  1 
ATOM   14316 N  N   . VAL D  1 226 ? -49.381 15.936  30.499  1.00 30.30  ? 226  VAL D N   1 
ATOM   14317 C  CA  . VAL D  1 226 ? -49.982 15.313  31.682  1.00 24.83  ? 226  VAL D CA  1 
ATOM   14318 C  C   . VAL D  1 226 ? -49.337 13.952  31.977  1.00 24.05  ? 226  VAL D C   1 
ATOM   14319 O  O   . VAL D  1 226 ? -49.479 12.982  31.214  1.00 26.22  ? 226  VAL D O   1 
ATOM   14320 C  CB  . VAL D  1 226 ? -51.521 15.159  31.531  1.00 25.84  ? 226  VAL D CB  1 
ATOM   14321 C  CG1 . VAL D  1 226 ? -52.107 14.278  32.612  1.00 26.34  ? 226  VAL D CG1 1 
ATOM   14322 C  CG2 . VAL D  1 226 ? -52.181 16.498  31.556  1.00 26.87  ? 226  VAL D CG2 1 
ATOM   14323 N  N   . LEU D  1 227 ? -48.638 13.897  33.105  1.00 23.93  ? 227  LEU D N   1 
ATOM   14324 C  CA  . LEU D  1 227 ? -47.925 12.708  33.540  1.00 25.46  ? 227  LEU D CA  1 
ATOM   14325 C  C   . LEU D  1 227 ? -48.665 12.065  34.713  1.00 25.97  ? 227  LEU D C   1 
ATOM   14326 O  O   . LEU D  1 227 ? -48.667 12.576  35.860  1.00 24.61  ? 227  LEU D O   1 
ATOM   14327 C  CB  . LEU D  1 227 ? -46.478 13.054  33.927  1.00 22.71  ? 227  LEU D CB  1 
ATOM   14328 C  CG  . LEU D  1 227 ? -45.491 13.452  32.820  1.00 21.96  ? 227  LEU D CG  1 
ATOM   14329 C  CD1 . LEU D  1 227 ? -45.641 14.877  32.365  1.00 22.32  ? 227  LEU D CD1 1 
ATOM   14330 C  CD2 . LEU D  1 227 ? -44.094 13.235  33.290  1.00 21.41  ? 227  LEU D CD2 1 
ATOM   14331 N  N   . GLN D  1 228 ? -49.295 10.935  34.418  1.00 37.99  ? 228  GLN D N   1 
ATOM   14332 C  CA  . GLN D  1 228 ? -50.088 10.244  35.412  1.00 41.63  ? 228  GLN D CA  1 
ATOM   14333 C  C   . GLN D  1 228 ? -49.328 9.038   35.922  1.00 48.56  ? 228  GLN D C   1 
ATOM   14334 O  O   . GLN D  1 228 ? -49.146 8.070   35.190  1.00 53.10  ? 228  GLN D O   1 
ATOM   14335 C  CB  . GLN D  1 228 ? -51.409 9.795   34.805  1.00 29.92  ? 228  GLN D CB  1 
ATOM   14336 C  CG  . GLN D  1 228 ? -52.097 10.874  34.004  1.00 28.47  ? 228  GLN D CG  1 
ATOM   14337 C  CD  . GLN D  1 228 ? -53.472 10.463  33.513  1.00 32.92  ? 228  GLN D CD  1 
ATOM   14338 O  OE1 . GLN D  1 228 ? -54.048 11.120  32.651  1.00 34.95  ? 228  GLN D OE1 1 
ATOM   14339 N  NE2 . GLN D  1 228 ? -54.007 9.380   34.064  1.00 35.34  ? 228  GLN D NE2 1 
ATOM   14340 N  N   . SER D  1 229 ? -48.886 9.110   37.177  1.00 32.94  ? 229  SER D N   1 
ATOM   14341 C  CA  . SER D  1 229 ? -48.250 7.991   37.878  1.00 29.66  ? 229  SER D CA  1 
ATOM   14342 C  C   . SER D  1 229 ? -47.038 7.454   37.146  1.00 23.69  ? 229  SER D C   1 
ATOM   14343 O  O   . SER D  1 229 ? -46.855 6.244   37.044  1.00 23.61  ? 229  SER D O   1 
ATOM   14344 C  CB  . SER D  1 229 ? -49.252 6.857   38.118  1.00 43.34  ? 229  SER D CB  1 
ATOM   14345 O  OG  . SER D  1 229 ? -50.504 7.355   38.574  1.00 47.08  ? 229  SER D OG  1 
ATOM   14346 N  N   . GLY D  1 230 ? -46.224 8.361   36.626  1.00 23.00  ? 230  GLY D N   1 
ATOM   14347 C  CA  . GLY D  1 230 ? -44.991 7.972   35.974  1.00 26.97  ? 230  GLY D CA  1 
ATOM   14348 C  C   . GLY D  1 230 ? -44.145 9.161   35.564  1.00 25.01  ? 230  GLY D C   1 
ATOM   14349 O  O   . GLY D  1 230 ? -44.660 10.270  35.404  1.00 21.84  ? 230  GLY D O   1 
ATOM   14350 N  N   . THR D  1 231 ? -42.845 8.925   35.390  1.00 22.12  ? 231  THR D N   1 
ATOM   14351 C  CA  . THR D  1 231 ? -41.901 9.994   35.100  1.00 21.48  ? 231  THR D CA  1 
ATOM   14352 C  C   . THR D  1 231 ? -40.736 9.544   34.232  1.00 19.96  ? 231  THR D C   1 
ATOM   14353 O  O   . THR D  1 231 ? -40.379 8.376   34.242  1.00 23.54  ? 231  THR D O   1 
ATOM   14354 C  CB  . THR D  1 231 ? -41.302 10.470  36.385  1.00 22.68  ? 231  THR D CB  1 
ATOM   14355 O  OG1 . THR D  1 231 ? -41.118 9.335   37.242  1.00 23.43  ? 231  THR D OG1 1 
ATOM   14356 C  CG2 . THR D  1 231 ? -42.219 11.480  37.039  1.00 21.58  ? 231  THR D CG2 1 
ATOM   14357 N  N   . PRO D  1 232 ? -40.114 10.475  33.497  1.00 19.76  ? 232  PRO D N   1 
ATOM   14358 C  CA  . PRO D  1 232 ? -38.930 10.107  32.730  1.00 19.21  ? 232  PRO D CA  1 
ATOM   14359 C  C   . PRO D  1 232 ? -37.760 9.835   33.645  1.00 19.22  ? 232  PRO D C   1 
ATOM   14360 O  O   . PRO D  1 232 ? -36.858 9.100   33.267  1.00 19.00  ? 232  PRO D O   1 
ATOM   14361 C  CB  . PRO D  1 232 ? -38.648 11.359  31.913  1.00 19.13  ? 232  PRO D CB  1 
ATOM   14362 C  CG  . PRO D  1 232 ? -39.183 12.449  32.719  1.00 21.21  ? 232  PRO D CG  1 
ATOM   14363 C  CD  . PRO D  1 232 ? -40.434 11.901  33.332  1.00 23.22  ? 232  PRO D CD  1 
ATOM   14364 N  N   . ASN D  1 233 ? -37.756 10.417  34.834  1.00 25.35  ? 233  ASN D N   1 
ATOM   14365 C  CA  . ASN D  1 233 ? -36.662 10.152  35.758  1.00 31.38  ? 233  ASN D CA  1 
ATOM   14366 C  C   . ASN D  1 233 ? -36.986 8.968   36.654  1.00 33.54  ? 233  ASN D C   1 
ATOM   14367 O  O   . ASN D  1 233 ? -38.080 8.417   36.596  1.00 35.56  ? 233  ASN D O   1 
ATOM   14368 C  CB  . ASN D  1 233 ? -36.364 11.384  36.607  1.00 34.23  ? 233  ASN D CB  1 
ATOM   14369 C  CG  . ASN D  1 233 ? -37.596 11.919  37.285  1.00 36.54  ? 233  ASN D CG  1 
ATOM   14370 O  OD1 . ASN D  1 233 ? -38.672 11.896  36.709  1.00 36.77  ? 233  ASN D OD1 1 
ATOM   14371 N  ND2 . ASN D  1 233 ? -37.451 12.391  38.518  1.00 38.75  ? 233  ASN D ND2 1 
ATOM   14372 N  N   . GLY D  1 234 ? -36.042 8.590   37.503  1.00 40.11  ? 234  GLY D N   1 
ATOM   14373 C  CA  . GLY D  1 234 ? -36.285 7.507   38.432  1.00 41.20  ? 234  GLY D CA  1 
ATOM   14374 C  C   . GLY D  1 234 ? -35.567 6.212   38.119  1.00 40.06  ? 234  GLY D C   1 
ATOM   14375 O  O   . GLY D  1 234 ? -34.778 6.146   37.186  1.00 45.33  ? 234  GLY D O   1 
ATOM   14376 N  N   . PRO D  1 235 ? -35.836 5.173   38.914  1.00 25.35  ? 235  PRO D N   1 
ATOM   14377 C  CA  . PRO D  1 235 ? -35.197 3.866   38.780  1.00 26.69  ? 235  PRO D CA  1 
ATOM   14378 C  C   . PRO D  1 235 ? -35.472 3.162   37.457  1.00 29.21  ? 235  PRO D C   1 
ATOM   14379 O  O   . PRO D  1 235 ? -34.528 2.648   36.867  1.00 33.08  ? 235  PRO D O   1 
ATOM   14380 C  CB  . PRO D  1 235 ? -35.845 3.053   39.898  1.00 27.25  ? 235  PRO D CB  1 
ATOM   14381 C  CG  . PRO D  1 235 ? -37.159 3.717   40.155  1.00 21.93  ? 235  PRO D CG  1 
ATOM   14382 C  CD  . PRO D  1 235 ? -36.918 5.163   39.914  1.00 23.08  ? 235  PRO D CD  1 
ATOM   14383 N  N   . TRP D  1 236 ? -36.732 3.111   37.022  1.00 36.36  ? 236  TRP D N   1 
ATOM   14384 C  CA  . TRP D  1 236 ? -37.130 2.163   35.977  1.00 35.54  ? 236  TRP D CA  1 
ATOM   14385 C  C   . TRP D  1 236 ? -37.314 2.576   34.518  1.00 38.02  ? 236  TRP D C   1 
ATOM   14386 O  O   . TRP D  1 236 ? -37.489 1.706   33.669  1.00 39.95  ? 236  TRP D O   1 
ATOM   14387 C  CB  . TRP D  1 236 ? -38.431 1.517   36.398  1.00 22.07  ? 236  TRP D CB  1 
ATOM   14388 C  CG  . TRP D  1 236 ? -39.480 2.492   36.583  1.00 24.01  ? 236  TRP D CG  1 
ATOM   14389 C  CD1 . TRP D  1 236 ? -39.844 3.069   37.752  1.00 28.94  ? 236  TRP D CD1 1 
ATOM   14390 C  CD2 . TRP D  1 236 ? -40.335 3.035   35.574  1.00 29.43  ? 236  TRP D CD2 1 
ATOM   14391 N  NE1 . TRP D  1 236 ? -40.882 3.948   37.543  1.00 33.54  ? 236  TRP D NE1 1 
ATOM   14392 C  CE2 . TRP D  1 236 ? -41.206 3.941   36.212  1.00 33.72  ? 236  TRP D CE2 1 
ATOM   14393 C  CE3 . TRP D  1 236 ? -40.459 2.838   34.196  1.00 31.16  ? 236  TRP D CE3 1 
ATOM   14394 C  CZ2 . TRP D  1 236 ? -42.187 4.655   35.517  1.00 34.79  ? 236  TRP D CZ2 1 
ATOM   14395 C  CZ3 . TRP D  1 236 ? -41.433 3.551   33.504  1.00 32.63  ? 236  TRP D CZ3 1 
ATOM   14396 C  CH2 . TRP D  1 236 ? -42.288 4.441   34.167  1.00 33.69  ? 236  TRP D CH2 1 
ATOM   14397 N  N   . ALA D  1 237 ? -37.283 3.867   34.211  1.00 24.60  ? 237  ALA D N   1 
ATOM   14398 C  CA  . ALA D  1 237 ? -37.720 4.316   32.889  1.00 21.32  ? 237  ALA D CA  1 
ATOM   14399 C  C   . ALA D  1 237 ? -36.627 4.400   31.854  1.00 19.01  ? 237  ALA D C   1 
ATOM   14400 O  O   . ALA D  1 237 ? -36.920 4.543   30.684  1.00 18.78  ? 237  ALA D O   1 
ATOM   14401 C  CB  . ALA D  1 237 ? -38.449 5.645   32.986  1.00 24.86  ? 237  ALA D CB  1 
ATOM   14402 N  N   . THR D  1 238 ? -35.371 4.335   32.269  1.00 25.18  ? 238  THR D N   1 
ATOM   14403 C  CA  . THR D  1 238 ? -34.274 4.351   31.306  1.00 23.15  ? 238  THR D CA  1 
ATOM   14404 C  C   . THR D  1 238 ? -33.176 3.456   31.816  1.00 22.71  ? 238  THR D C   1 
ATOM   14405 O  O   . THR D  1 238 ? -33.038 3.308   33.038  1.00 24.07  ? 238  THR D O   1 
ATOM   14406 C  CB  . THR D  1 238 ? -33.649 5.759   31.113  1.00 23.16  ? 238  THR D CB  1 
ATOM   14407 O  OG1 . THR D  1 238 ? -32.890 6.114   32.276  1.00 23.48  ? 238  THR D OG1 1 
ATOM   14408 C  CG2 . THR D  1 238 ? -34.711 6.832   30.840  1.00 24.20  ? 238  THR D CG2 1 
ATOM   14409 N  N   . VAL D  1 239 ? -32.417 2.845   30.898  1.00 24.84  ? 239  VAL D N   1 
ATOM   14410 C  CA  . VAL D  1 239 ? -31.096 2.310   31.257  1.00 27.09  ? 239  VAL D CA  1 
ATOM   14411 C  C   . VAL D  1 239 ? -30.022 3.079   30.530  1.00 27.40  ? 239  VAL D C   1 
ATOM   14412 O  O   . VAL D  1 239 ? -30.310 3.956   29.713  1.00 25.32  ? 239  VAL D O   1 
ATOM   14413 C  CB  . VAL D  1 239 ? -30.866 0.815   30.925  1.00 29.94  ? 239  VAL D CB  1 
ATOM   14414 C  CG1 . VAL D  1 239 ? -31.948 -0.053  31.520  1.00 31.66  ? 239  VAL D CG1 1 
ATOM   14415 C  CG2 . VAL D  1 239 ? -30.762 0.617   29.443  1.00 31.13  ? 239  VAL D CG2 1 
ATOM   14416 N  N   . SER D  1 240 ? -28.778 2.723   30.824  1.00 34.63  ? 240  SER D N   1 
ATOM   14417 C  CA  . SER D  1 240 ? -27.638 3.380   30.225  1.00 33.54  ? 240  SER D CA  1 
ATOM   14418 C  C   . SER D  1 240 ? -27.305 2.703   28.912  1.00 36.49  ? 240  SER D C   1 
ATOM   14419 O  O   . SER D  1 240 ? -27.919 1.703   28.538  1.00 38.80  ? 240  SER D O   1 
ATOM   14420 C  CB  . SER D  1 240 ? -26.446 3.254   31.147  1.00 21.06  ? 240  SER D CB  1 
ATOM   14421 O  OG  . SER D  1 240 ? -26.028 1.910   31.190  1.00 21.62  ? 240  SER D OG  1 
ATOM   14422 N  N   . ALA D  1 241 ? -26.317 3.248   28.219  1.00 31.46  ? 241  ALA D N   1 
ATOM   14423 C  CA  . ALA D  1 241 ? -25.831 2.640   27.000  1.00 30.69  ? 241  ALA D CA  1 
ATOM   14424 C  C   . ALA D  1 241 ? -25.302 1.254   27.342  1.00 28.84  ? 241  ALA D C   1 
ATOM   14425 O  O   . ALA D  1 241 ? -25.592 0.264   26.654  1.00 29.27  ? 241  ALA D O   1 
ATOM   14426 C  CB  . ALA D  1 241 ? -24.730 3.497   26.409  1.00 33.95  ? 241  ALA D CB  1 
ATOM   14427 N  N   . GLY D  1 242 ? -24.541 1.193   28.430  1.00 22.45  ? 242  GLY D N   1 
ATOM   14428 C  CA  . GLY D  1 242 ? -23.910 -0.041  28.838  1.00 23.25  ? 242  GLY D CA  1 
ATOM   14429 C  C   . GLY D  1 242 ? -24.881 -1.185  29.066  1.00 23.20  ? 242  GLY D C   1 
ATOM   14430 O  O   . GLY D  1 242 ? -24.766 -2.256  28.468  1.00 23.74  ? 242  GLY D O   1 
ATOM   14431 N  N   . GLU D  1 243 ? -25.846 -0.952  29.941  1.00 24.26  ? 243  GLU D N   1 
ATOM   14432 C  CA  . GLU D  1 243 ? -26.849 -1.958  30.255  1.00 27.58  ? 243  GLU D CA  1 
ATOM   14433 C  C   . GLU D  1 243 ? -27.663 -2.337  29.012  1.00 29.47  ? 243  GLU D C   1 
ATOM   14434 O  O   . GLU D  1 243 ? -27.998 -3.503  28.812  1.00 22.89  ? 243  GLU D O   1 
ATOM   14435 C  CB  . GLU D  1 243 ? -27.757 -1.444  31.381  1.00 36.23  ? 243  GLU D CB  1 
ATOM   14436 C  CG  . GLU D  1 243 ? -28.612 -2.498  32.056  1.00 38.88  ? 243  GLU D CG  1 
ATOM   14437 C  CD  . GLU D  1 243 ? -27.814 -3.602  32.748  1.00 42.28  ? 243  GLU D CD  1 
ATOM   14438 O  OE1 . GLU D  1 243 ? -26.568 -3.498  32.883  1.00 43.80  ? 243  GLU D OE1 1 
ATOM   14439 O  OE2 . GLU D  1 243 ? -28.458 -4.589  33.163  1.00 43.65  ? 243  GLU D OE2 1 
ATOM   14440 N  N   . ALA D  1 244 ? -27.974 -1.349  28.179  1.00 26.72  ? 244  ALA D N   1 
ATOM   14441 C  CA  . ALA D  1 244 ? -28.653 -1.614  26.924  1.00 21.64  ? 244  ALA D CA  1 
ATOM   14442 C  C   . ALA D  1 244 ? -27.887 -2.699  26.178  1.00 24.16  ? 244  ALA D C   1 
ATOM   14443 O  O   . ALA D  1 244 ? -28.451 -3.743  25.831  1.00 22.77  ? 244  ALA D O   1 
ATOM   14444 C  CB  . ALA D  1 244 ? -28.733 -0.354  26.094  1.00 37.06  ? 244  ALA D CB  1 
ATOM   14445 N  N   . ARG D  1 245 ? -26.589 -2.464  25.972  1.00 27.90  ? 245  ARG D N   1 
ATOM   14446 C  CA  . ARG D  1 245 ? -25.752 -3.428  25.254  1.00 28.91  ? 245  ARG D CA  1 
ATOM   14447 C  C   . ARG D  1 245 ? -25.720 -4.771  25.962  1.00 24.61  ? 245  ARG D C   1 
ATOM   14448 O  O   . ARG D  1 245 ? -25.904 -5.794  25.330  1.00 25.17  ? 245  ARG D O   1 
ATOM   14449 C  CB  . ARG D  1 245 ? -24.342 -2.884  25.029  1.00 43.50  ? 245  ARG D CB  1 
ATOM   14450 C  CG  . ARG D  1 245 ? -23.264 -3.950  25.017  1.00 52.27  ? 245  ARG D CG  1 
ATOM   14451 C  CD  . ARG D  1 245 ? -22.061 -3.508  24.206  1.00 58.14  ? 245  ARG D CD  1 
ATOM   14452 N  NE  . ARG D  1 245 ? -22.434 -3.296  22.811  1.00 61.65  ? 245  ARG D NE  1 
ATOM   14453 C  CZ  . ARG D  1 245 ? -22.151 -4.137  21.820  1.00 66.30  ? 245  ARG D CZ  1 
ATOM   14454 N  NH1 . ARG D  1 245 ? -21.467 -5.257  22.046  1.00 65.78  ? 245  ARG D NH1 1 
ATOM   14455 N  NH2 . ARG D  1 245 ? -22.552 -3.845  20.592  1.00 68.42  ? 245  ARG D NH2 1 
ATOM   14456 N  N   . ARG D  1 246 ? -25.519 -4.753  27.276  1.00 29.42  ? 246  ARG D N   1 
ATOM   14457 C  CA  . ARG D  1 246 ? -25.473 -5.968  28.083  1.00 29.32  ? 246  ARG D CA  1 
ATOM   14458 C  C   . ARG D  1 246 ? -26.707 -6.828  27.807  1.00 26.62  ? 246  ARG D C   1 
ATOM   14459 O  O   . ARG D  1 246 ? -26.607 -8.013  27.472  1.00 28.09  ? 246  ARG D O   1 
ATOM   14460 C  CB  . ARG D  1 246 ? -25.400 -5.597  29.572  1.00 39.02  ? 246  ARG D CB  1 
ATOM   14461 C  CG  . ARG D  1 246 ? -24.568 -6.528  30.455  1.00 46.08  ? 246  ARG D CG  1 
ATOM   14462 C  CD  . ARG D  1 246 ? -25.367 -7.699  31.028  1.00 52.32  ? 246  ARG D CD  1 
ATOM   14463 N  NE  . ARG D  1 246 ? -26.497 -7.249  31.841  1.00 57.06  ? 246  ARG D NE  1 
ATOM   14464 C  CZ  . ARG D  1 246 ? -27.416 -8.055  32.373  1.00 61.91  ? 246  ARG D CZ  1 
ATOM   14465 N  NH1 . ARG D  1 246 ? -27.350 -9.368  32.200  1.00 65.01  ? 246  ARG D NH1 1 
ATOM   14466 N  NH2 . ARG D  1 246 ? -28.412 -7.546  33.080  1.00 62.11  ? 246  ARG D NH2 1 
ATOM   14467 N  N   . ARG D  1 247 ? -27.872 -6.204  27.901  1.00 24.50  ? 247  ARG D N   1 
ATOM   14468 C  CA  . ARG D  1 247 ? -29.129 -6.916  27.846  1.00 24.49  ? 247  ARG D CA  1 
ATOM   14469 C  C   . ARG D  1 247 ? -29.396 -7.380  26.444  1.00 27.36  ? 247  ARG D C   1 
ATOM   14470 O  O   . ARG D  1 247 ? -29.889 -8.483  26.244  1.00 28.43  ? 247  ARG D O   1 
ATOM   14471 C  CB  . ARG D  1 247 ? -30.262 -6.013  28.314  1.00 23.55  ? 247  ARG D CB  1 
ATOM   14472 C  CG  . ARG D  1 247 ? -30.179 -5.669  29.772  1.00 23.50  ? 247  ARG D CG  1 
ATOM   14473 C  CD  . ARG D  1 247 ? -31.234 -4.675  30.183  1.00 25.49  ? 247  ARG D CD  1 
ATOM   14474 N  NE  . ARG D  1 247 ? -31.078 -4.309  31.587  1.00 22.72  ? 247  ARG D NE  1 
ATOM   14475 C  CZ  . ARG D  1 247 ? -31.941 -3.561  32.261  1.00 27.21  ? 247  ARG D CZ  1 
ATOM   14476 N  NH1 . ARG D  1 247 ? -33.032 -3.115  31.665  1.00 28.14  ? 247  ARG D NH1 1 
ATOM   14477 N  NH2 . ARG D  1 247 ? -31.723 -3.269  33.531  1.00 27.97  ? 247  ARG D NH2 1 
ATOM   14478 N  N   . ALA D  1 248 ? -29.073 -6.533  25.471  1.00 24.21  ? 248  ALA D N   1 
ATOM   14479 C  CA  . ALA D  1 248 ? -29.344 -6.845  24.075  1.00 31.14  ? 248  ALA D CA  1 
ATOM   14480 C  C   . ALA D  1 248 ? -28.484 -8.024  23.653  1.00 33.18  ? 248  ALA D C   1 
ATOM   14481 O  O   . ALA D  1 248 ? -28.974 -9.013  23.119  1.00 26.12  ? 248  ALA D O   1 
ATOM   14482 C  CB  . ALA D  1 248 ? -29.065 -5.643  23.209  1.00 23.76  ? 248  ALA D CB  1 
ATOM   14483 N  N   . THR D  1 249 ? -27.196 -7.904  23.926  1.00 26.03  ? 249  THR D N   1 
ATOM   14484 C  CA  . THR D  1 249 ? -26.236 -8.961  23.700  1.00 27.32  ? 249  THR D CA  1 
ATOM   14485 C  C   . THR D  1 249 ? -26.650 -10.296 24.323  1.00 28.13  ? 249  THR D C   1 
ATOM   14486 O  O   . THR D  1 249 ? -26.634 -11.327 23.655  1.00 29.06  ? 249  THR D O   1 
ATOM   14487 C  CB  . THR D  1 249 ? -24.870 -8.549  24.263  1.00 43.54  ? 249  THR D CB  1 
ATOM   14488 O  OG1 . THR D  1 249 ? -24.287 -7.561  23.408  1.00 42.87  ? 249  THR D OG1 1 
ATOM   14489 C  CG2 . THR D  1 249 ? -23.943 -9.743  24.353  1.00 48.41  ? 249  THR D CG2 1 
ATOM   14490 N  N   . LEU D  1 250 ? -27.005 -10.276 25.604  1.00 27.89  ? 250  LEU D N   1 
ATOM   14491 C  CA  . LEU D  1 250 ? -27.414 -11.491 26.316  1.00 28.74  ? 250  LEU D CA  1 
ATOM   14492 C  C   . LEU D  1 250 ? -28.686 -12.129 25.759  1.00 28.76  ? 250  LEU D C   1 
ATOM   14493 O  O   . LEU D  1 250 ? -28.748 -13.347 25.583  1.00 29.88  ? 250  LEU D O   1 
ATOM   14494 C  CB  . LEU D  1 250 ? -27.599 -11.181 27.800  1.00 31.48  ? 250  LEU D CB  1 
ATOM   14495 C  CG  . LEU D  1 250 ? -28.438 -12.137 28.634  1.00 29.02  ? 250  LEU D CG  1 
ATOM   14496 C  CD1 . LEU D  1 250 ? -27.684 -13.421 28.804  1.00 30.57  ? 250  LEU D CD1 1 
ATOM   14497 C  CD2 . LEU D  1 250 ? -28.740 -11.513 29.974  1.00 28.48  ? 250  LEU D CD2 1 
ATOM   14498 N  N   . LEU D  1 251 ? -29.699 -11.306 25.496  1.00 27.63  ? 251  LEU D N   1 
ATOM   14499 C  CA  . LEU D  1 251 ? -30.946 -11.800 24.923  1.00 27.64  ? 251  LEU D CA  1 
ATOM   14500 C  C   . LEU D  1 251 ? -30.676 -12.422 23.580  1.00 28.31  ? 251  LEU D C   1 
ATOM   14501 O  O   . LEU D  1 251 ? -31.247 -13.454 23.231  1.00 30.09  ? 251  LEU D O   1 
ATOM   14502 C  CB  . LEU D  1 251 ? -31.967 -10.690 24.723  1.00 31.02  ? 251  LEU D CB  1 
ATOM   14503 C  CG  . LEU D  1 251 ? -33.203 -11.319 24.079  1.00 29.86  ? 251  LEU D CG  1 
ATOM   14504 C  CD1 . LEU D  1 251 ? -34.388 -11.235 25.007  1.00 32.01  ? 251  LEU D CD1 1 
ATOM   14505 C  CD2 . LEU D  1 251 ? -33.501 -10.691 22.754  1.00 28.58  ? 251  LEU D CD2 1 
ATOM   14506 N  N   . ALA D  1 252 ? -29.812 -11.768 22.818  1.00 31.73  ? 252  ALA D N   1 
ATOM   14507 C  CA  . ALA D  1 252 ? -29.312 -12.329 21.579  1.00 33.97  ? 252  ALA D CA  1 
ATOM   14508 C  C   . ALA D  1 252 ? -28.690 -13.707 21.829  1.00 35.84  ? 252  ALA D C   1 
ATOM   14509 O  O   . ALA D  1 252 ? -28.945 -14.657 21.094  1.00 36.96  ? 252  ALA D O   1 
ATOM   14510 C  CB  . ALA D  1 252 ? -28.303 -11.405 20.997  1.00 28.58  ? 252  ALA D CB  1 
ATOM   14511 N  N   . ARG D  1 253 ? -27.877 -13.811 22.876  1.00 30.80  ? 253  ARG D N   1 
ATOM   14512 C  CA  . ARG D  1 253 ? -27.182 -15.051 23.176  1.00 32.38  ? 253  ARG D CA  1 
ATOM   14513 C  C   . ARG D  1 253 ? -28.178 -16.171 23.393  1.00 33.07  ? 253  ARG D C   1 
ATOM   14514 O  O   . ARG D  1 253 ? -27.964 -17.294 22.950  1.00 42.01  ? 253  ARG D O   1 
ATOM   14515 C  CB  . ARG D  1 253 ? -26.285 -14.883 24.408  1.00 39.06  ? 253  ARG D CB  1 
ATOM   14516 C  CG  . ARG D  1 253 ? -25.152 -15.924 24.547  1.00 41.91  ? 253  ARG D CG  1 
ATOM   14517 C  CD  . ARG D  1 253 ? -23.765 -15.277 24.544  1.00 41.06  ? 253  ARG D CD  1 
ATOM   14518 N  NE  . ARG D  1 253 ? -23.844 -13.882 24.961  1.00 40.25  ? 253  ARG D NE  1 
ATOM   14519 C  CZ  . ARG D  1 253 ? -23.995 -13.499 26.223  1.00 41.07  ? 253  ARG D CZ  1 
ATOM   14520 N  NH1 . ARG D  1 253 ? -24.085 -14.424 27.167  1.00 44.51  ? 253  ARG D NH1 1 
ATOM   14521 N  NH2 . ARG D  1 253 ? -24.070 -12.208 26.542  1.00 38.69  ? 253  ARG D NH2 1 
ATOM   14522 N  N   . LEU D  1 254 ? -29.282 -15.853 24.055  1.00 41.81  ? 254  LEU D N   1 
ATOM   14523 C  CA  . LEU D  1 254 ? -30.286 -16.869 24.365  1.00 42.33  ? 254  LEU D CA  1 
ATOM   14524 C  C   . LEU D  1 254 ? -31.067 -17.409 23.159  1.00 43.28  ? 254  LEU D C   1 
ATOM   14525 O  O   . LEU D  1 254 ? -31.514 -18.558 23.166  1.00 45.61  ? 254  LEU D O   1 
ATOM   14526 C  CB  . LEU D  1 254 ? -31.232 -16.360 25.442  1.00 32.09  ? 254  LEU D CB  1 
ATOM   14527 C  CG  . LEU D  1 254 ? -30.458 -16.150 26.735  1.00 32.18  ? 254  LEU D CG  1 
ATOM   14528 C  CD1 . LEU D  1 254 ? -31.212 -15.236 27.666  1.00 31.05  ? 254  LEU D CD1 1 
ATOM   14529 C  CD2 . LEU D  1 254 ? -30.223 -17.481 27.381  1.00 33.80  ? 254  LEU D CD2 1 
ATOM   14530 N  N   . VAL D  1 255 ? -31.225 -16.601 22.116  1.00 41.65  ? 255  VAL D N   1 
ATOM   14531 C  CA  . VAL D  1 255 ? -31.941 -17.071 20.928  1.00 39.83  ? 255  VAL D CA  1 
ATOM   14532 C  C   . VAL D  1 255 ? -31.008 -17.731 19.925  1.00 42.21  ? 255  VAL D C   1 
ATOM   14533 O  O   . VAL D  1 255 ? -31.411 -18.075 18.815  1.00 37.93  ? 255  VAL D O   1 
ATOM   14534 C  CB  . VAL D  1 255 ? -32.765 -15.965 20.263  1.00 32.22  ? 255  VAL D CB  1 
ATOM   14535 C  CG1 . VAL D  1 255 ? -34.001 -15.706 21.086  1.00 31.05  ? 255  VAL D CG1 1 
ATOM   14536 C  CG2 . VAL D  1 255 ? -31.941 -14.691 20.090  1.00 30.34  ? 255  VAL D CG2 1 
ATOM   14537 N  N   . GLY D  1 256 ? -29.752 -17.886 20.326  1.00 62.54  ? 256  GLY D N   1 
ATOM   14538 C  CA  . GLY D  1 256 ? -28.766 -18.561 19.509  1.00 70.78  ? 256  GLY D CA  1 
ATOM   14539 C  C   . GLY D  1 256 ? -28.123 -17.646 18.493  1.00 73.96  ? 256  GLY D C   1 
ATOM   14540 O  O   . GLY D  1 256 ? -27.431 -18.108 17.583  1.00 75.20  ? 256  GLY D O   1 
ATOM   14541 N  N   . CYS D  1 257 ? -28.342 -16.344 18.647  1.00 71.07  ? 257  CYS D N   1 
ATOM   14542 C  CA  . CYS D  1 257 ? -27.713 -15.376 17.761  1.00 69.55  ? 257  CYS D CA  1 
ATOM   14543 C  C   . CYS D  1 257 ? -26.207 -15.322 17.951  1.00 76.20  ? 257  CYS D C   1 
ATOM   14544 O  O   . CYS D  1 257 ? -25.694 -16.025 18.813  1.00 82.21  ? 257  CYS D O   1 
ATOM   14545 C  CB  . CYS D  1 257 ? -28.423 -14.044 17.792  1.00 50.60  ? 257  CYS D CB  1 
ATOM   14546 S  SG  . CYS D  1 257 ? -29.872 -14.204 16.724  1.00 95.05  ? 257  CYS D SG  1 
ATOM   14547 N  N   . PRO D  1 258 ? -25.506 -14.407 17.268  1.00 82.03  ? 258  PRO D N   1 
ATOM   14548 C  CA  . PRO D  1 258 ? -24.586 -14.947 16.256  1.00 85.53  ? 258  PRO D CA  1 
ATOM   14549 C  C   . PRO D  1 258 ? -23.887 -16.239 16.667  1.00 89.46  ? 258  PRO D C   1 
ATOM   14550 O  O   . PRO D  1 258 ? -23.245 -16.291 17.720  1.00 91.15  ? 258  PRO D O   1 
ATOM   14551 C  CB  . PRO D  1 258 ? -23.538 -13.839 16.142  1.00 58.77  ? 258  PRO D CB  1 
ATOM   14552 C  CG  . PRO D  1 258 ? -23.598 -13.131 17.464  1.00 55.85  ? 258  PRO D CG  1 
ATOM   14553 C  CD  . PRO D  1 258 ? -25.059 -13.093 17.751  1.00 54.70  ? 258  PRO D CD  1 
ATOM   14554 N  N   . PRO D  1 259 ? -24.001 -17.272 15.803  1.00 77.52  ? 259  PRO D N   1 
ATOM   14555 C  CA  . PRO D  1 259 ? -23.753 -18.679 16.178  1.00 80.35  ? 259  PRO D CA  1 
ATOM   14556 C  C   . PRO D  1 259 ? -22.327 -19.096 16.603  1.00 85.12  ? 259  PRO D C   1 
ATOM   14557 O  O   . PRO D  1 259 ? -21.333 -18.926 15.877  1.00 81.23  ? 259  PRO D O   1 
ATOM   14558 C  CB  . PRO D  1 259 ? -24.211 -19.462 14.934  1.00 63.13  ? 259  PRO D CB  1 
ATOM   14559 C  CG  . PRO D  1 259 ? -24.278 -18.438 13.821  1.00 60.67  ? 259  PRO D CG  1 
ATOM   14560 C  CD  . PRO D  1 259 ? -24.634 -17.150 14.476  1.00 58.71  ? 259  PRO D CD  1 
ATOM   14561 N  N   . GLY D  1 260 ? -22.280 -19.639 17.822  1.00 100.83 ? 260  GLY D N   1 
ATOM   14562 C  CA  . GLY D  1 260 ? -21.163 -20.365 18.417  1.00 107.05 ? 260  GLY D CA  1 
ATOM   14563 C  C   . GLY D  1 260 ? -20.097 -19.434 18.971  1.00 109.59 ? 260  GLY D C   1 
ATOM   14564 O  O   . GLY D  1 260 ? -19.479 -19.684 20.011  1.00 109.28 ? 260  GLY D O   1 
ATOM   14565 N  N   . GLY D  1 261 ? -19.904 -18.343 18.240  1.00 103.06 ? 261  GLY D N   1 
ATOM   14566 C  CA  . GLY D  1 261 ? -19.380 -17.082 18.716  1.00 98.36  ? 261  GLY D CA  1 
ATOM   14567 C  C   . GLY D  1 261 ? -19.154 -16.290 17.444  1.00 93.60  ? 261  GLY D C   1 
ATOM   14568 O  O   . GLY D  1 261 ? -18.801 -16.852 16.401  1.00 90.21  ? 261  GLY D O   1 
ATOM   14569 N  N   . ALA D  1 262 ? -19.341 -14.985 17.528  1.00 94.76  ? 262  ALA D N   1 
ATOM   14570 C  CA  . ALA D  1 262 ? -18.962 -14.072 16.466  1.00 93.08  ? 262  ALA D CA  1 
ATOM   14571 C  C   . ALA D  1 262 ? -18.364 -12.890 17.163  1.00 92.41  ? 262  ALA D C   1 
ATOM   14572 O  O   . ALA D  1 262 ? -17.204 -12.553 16.956  1.00 94.55  ? 262  ALA D O   1 
ATOM   14573 C  CB  . ALA D  1 262 ? -20.150 -13.654 15.612  1.00 77.69  ? 262  ALA D CB  1 
ATOM   14574 N  N   . GLY D  1 263 ? -19.211 -12.254 17.974  1.00 77.96  ? 263  GLY D N   1 
ATOM   14575 C  CA  . GLY D  1 263 ? -18.918 -10.983 18.608  1.00 75.37  ? 263  GLY D CA  1 
ATOM   14576 C  C   . GLY D  1 263 ? -18.747 -10.019 17.465  1.00 75.17  ? 263  GLY D C   1 
ATOM   14577 O  O   . GLY D  1 263 ? -19.412 -10.166 16.428  1.00 72.62  ? 263  GLY D O   1 
ATOM   14578 N  N   . GLY D  1 264 ? -17.847 -9.055  17.625  1.00 88.41  ? 264  GLY D N   1 
ATOM   14579 C  CA  . GLY D  1 264 ? -17.416 -8.303  16.468  1.00 89.50  ? 264  GLY D CA  1 
ATOM   14580 C  C   . GLY D  1 264 ? -18.573 -7.517  15.912  1.00 86.84  ? 264  GLY D C   1 
ATOM   14581 O  O   . GLY D  1 264 ? -19.086 -6.593  16.550  1.00 84.50  ? 264  GLY D O   1 
ATOM   14582 N  N   . ASN D  1 265 ? -18.943 -7.867  14.685  1.00 83.17  ? 265  ASN D N   1 
ATOM   14583 C  CA  . ASN D  1 265 ? -20.061 -7.234  14.027  1.00 83.88  ? 265  ASN D CA  1 
ATOM   14584 C  C   . ASN D  1 265 ? -21.338 -7.305  14.861  1.00 77.14  ? 265  ASN D C   1 
ATOM   14585 O  O   . ASN D  1 265 ? -21.833 -8.386  15.194  1.00 78.25  ? 265  ASN D O   1 
ATOM   14586 C  CB  . ASN D  1 265 ? -20.300 -7.909  12.676  1.00 99.93  ? 265  ASN D CB  1 
ATOM   14587 C  CG  . ASN D  1 265 ? -19.903 -7.035  11.508  1.00 106.94 ? 265  ASN D CG  1 
ATOM   14588 O  OD1 . ASN D  1 265 ? -19.735 -5.822  11.655  1.00 108.71 ? 265  ASN D OD1 1 
ATOM   14589 N  ND2 . ASN D  1 265 ? -19.768 -7.642  10.332  1.00 110.00 ? 265  ASN D ND2 1 
ATOM   14590 N  N   . ASP D  1 266 ? -21.871 -6.129  15.174  1.00 56.43  ? 266  ASP D N   1 
ATOM   14591 C  CA  . ASP D  1 266 ? -23.209 -6.011  15.700  1.00 48.49  ? 266  ASP D CA  1 
ATOM   14592 C  C   . ASP D  1 266 ? -24.105 -6.155  14.506  1.00 46.27  ? 266  ASP D C   1 
ATOM   14593 O  O   . ASP D  1 266 ? -25.230 -6.602  14.629  1.00 46.42  ? 266  ASP D O   1 
ATOM   14594 C  CB  . ASP D  1 266 ? -23.451 -4.622  16.271  1.00 59.29  ? 266  ASP D CB  1 
ATOM   14595 C  CG  . ASP D  1 266 ? -22.754 -4.401  17.574  1.00 62.22  ? 266  ASP D CG  1 
ATOM   14596 O  OD1 . ASP D  1 266 ? -21.811 -5.168  17.870  1.00 65.38  ? 266  ASP D OD1 1 
ATOM   14597 O  OD2 . ASP D  1 266 ? -23.147 -3.451  18.295  1.00 60.93  ? 266  ASP D OD2 1 
ATOM   14598 N  N   . THR D  1 267 ? -23.615 -5.732  13.345  1.00 58.33  ? 267  THR D N   1 
ATOM   14599 C  CA  . THR D  1 267 ? -24.442 -5.751  12.151  1.00 55.42  ? 267  THR D CA  1 
ATOM   14600 C  C   . THR D  1 267 ? -24.854 -7.184  11.886  1.00 56.85  ? 267  THR D C   1 
ATOM   14601 O  O   . THR D  1 267 ? -26.011 -7.450  11.532  1.00 56.61  ? 267  THR D O   1 
ATOM   14602 C  CB  . THR D  1 267 ? -23.738 -5.137  10.927  1.00 34.47  ? 267  THR D CB  1 
ATOM   14603 O  OG1 . THR D  1 267 ? -23.395 -3.772  11.208  1.00 30.03  ? 267  THR D OG1 1 
ATOM   14604 C  CG2 . THR D  1 267 ? -24.666 -5.175  9.719   1.00 32.42  ? 267  THR D CG2 1 
ATOM   14605 N  N   . GLU D  1 268 ? -23.914 -8.099  12.122  1.00 43.37  ? 268  GLU D N   1 
ATOM   14606 C  CA  . GLU D  1 268 ? -24.158 -9.527  11.954  1.00 47.70  ? 268  GLU D CA  1 
ATOM   14607 C  C   . GLU D  1 268 ? -25.050 -10.091 13.066  1.00 44.40  ? 268  GLU D C   1 
ATOM   14608 O  O   . GLU D  1 268 ? -25.936 -10.920 12.809  1.00 43.07  ? 268  GLU D O   1 
ATOM   14609 C  CB  . GLU D  1 268 ? -22.837 -10.288 11.885  1.00 85.58  ? 268  GLU D CB  1 
ATOM   14610 C  CG  . GLU D  1 268 ? -22.956 -11.693 11.329  1.00 96.98  ? 268  GLU D CG  1 
ATOM   14611 C  CD  . GLU D  1 268 ? -21.628 -12.433 11.348  1.00 106.98 ? 268  GLU D CD  1 
ATOM   14612 O  OE1 . GLU D  1 268 ? -21.242 -12.949 12.427  1.00 108.15 ? 268  GLU D OE1 1 
ATOM   14613 O  OE2 . GLU D  1 268 ? -20.974 -12.492 10.281  1.00 111.58 ? 268  GLU D OE2 1 
ATOM   14614 N  N   . LEU D  1 269 ? -24.815 -9.644  14.299  1.00 50.87  ? 269  LEU D N   1 
ATOM   14615 C  CA  . LEU D  1 269 ? -25.694 -9.998  15.413  1.00 44.75  ? 269  LEU D CA  1 
ATOM   14616 C  C   . LEU D  1 269 ? -27.156 -9.605  15.110  1.00 39.43  ? 269  LEU D C   1 
ATOM   14617 O  O   . LEU D  1 269 ? -28.004 -10.480 14.970  1.00 39.32  ? 269  LEU D O   1 
ATOM   14618 C  CB  . LEU D  1 269 ? -25.161 -9.422  16.747  1.00 33.22  ? 269  LEU D CB  1 
ATOM   14619 C  CG  . LEU D  1 269 ? -26.055 -9.119  17.968  1.00 31.74  ? 269  LEU D CG  1 
ATOM   14620 C  CD1 . LEU D  1 269 ? -27.112 -10.151 18.192  1.00 28.66  ? 269  LEU D CD1 1 
ATOM   14621 C  CD2 . LEU D  1 269 ? -25.227 -8.991  19.229  1.00 28.62  ? 269  LEU D CD2 1 
ATOM   14622 N  N   . ILE D  1 270 ? -27.433 -8.305  15.002  1.00 34.97  ? 270  ILE D N   1 
ATOM   14623 C  CA  . ILE D  1 270 ? -28.771 -7.788  14.694  1.00 35.42  ? 270  ILE D CA  1 
ATOM   14624 C  C   . ILE D  1 270 ? -29.339 -8.411  13.427  1.00 35.01  ? 270  ILE D C   1 
ATOM   14625 O  O   . ILE D  1 270 ? -30.568 -8.569  13.283  1.00 29.76  ? 270  ILE D O   1 
ATOM   14626 C  CB  . ILE D  1 270 ? -28.761 -6.260  14.498  1.00 33.93  ? 270  ILE D CB  1 
ATOM   14627 C  CG1 . ILE D  1 270 ? -28.034 -5.578  15.651  1.00 36.83  ? 270  ILE D CG1 1 
ATOM   14628 C  CG2 . ILE D  1 270 ? -30.181 -5.730  14.399  1.00 28.78  ? 270  ILE D CG2 1 
ATOM   14629 C  CD1 . ILE D  1 270 ? -28.765 -5.719  16.956  1.00 38.71  ? 270  ILE D CD1 1 
ATOM   14630 N  N   . ALA D  1 271 ? -28.437 -8.747  12.504  1.00 34.17  ? 271  ALA D N   1 
ATOM   14631 C  CA  . ALA D  1 271 ? -28.821 -9.505  11.328  1.00 34.50  ? 271  ALA D CA  1 
ATOM   14632 C  C   . ALA D  1 271 ? -29.498 -10.802 11.758  1.00 35.83  ? 271  ALA D C   1 
ATOM   14633 O  O   . ALA D  1 271 ? -30.690 -10.996 11.498  1.00 29.70  ? 271  ALA D O   1 
ATOM   14634 C  CB  . ALA D  1 271 ? -27.632 -9.797  10.494  1.00 37.17  ? 271  ALA D CB  1 
ATOM   14635 N  N   . CYS D  1 272 ? -28.732 -11.670 12.427  1.00 41.41  ? 272  CYS D N   1 
ATOM   14636 C  CA  . CYS D  1 272 ? -29.240 -12.960 12.919  1.00 41.39  ? 272  CYS D CA  1 
ATOM   14637 C  C   . CYS D  1 272 ? -30.556 -12.790 13.674  1.00 38.42  ? 272  CYS D C   1 
ATOM   14638 O  O   . CYS D  1 272 ? -31.521 -13.519 13.439  1.00 36.86  ? 272  CYS D O   1 
ATOM   14639 C  CB  . CYS D  1 272 ? -28.196 -13.665 13.808  1.00 39.93  ? 272  CYS D CB  1 
ATOM   14640 S  SG  . CYS D  1 272 ? -28.882 -14.836 15.047  1.00 93.86  ? 272  CYS D SG  1 
ATOM   14641 N  N   . LEU D  1 273 ? -30.573 -11.803 14.568  1.00 34.14  ? 273  LEU D N   1 
ATOM   14642 C  CA  . LEU D  1 273 ? -31.731 -11.481 15.384  1.00 31.50  ? 273  LEU D CA  1 
ATOM   14643 C  C   . LEU D  1 273 ? -32.957 -11.223 14.531  1.00 31.42  ? 273  LEU D C   1 
ATOM   14644 O  O   . LEU D  1 273 ? -34.049 -11.698 14.853  1.00 30.99  ? 273  LEU D O   1 
ATOM   14645 C  CB  . LEU D  1 273 ? -31.434 -10.251 16.227  1.00 27.26  ? 273  LEU D CB  1 
ATOM   14646 C  CG  . LEU D  1 273 ? -31.255 -10.489 17.719  1.00 31.71  ? 273  LEU D CG  1 
ATOM   14647 C  CD1 . LEU D  1 273 ? -30.789 -9.207  18.392  1.00 29.70  ? 273  LEU D CD1 1 
ATOM   14648 C  CD2 . LEU D  1 273 ? -32.562 -10.977 18.322  1.00 31.12  ? 273  LEU D CD2 1 
ATOM   14649 N  N   . ARG D  1 274 ? -32.766 -10.487 13.432  1.00 36.96  ? 274  ARG D N   1 
ATOM   14650 C  CA  . ARG D  1 274 ? -33.874 -10.054 12.571  1.00 36.74  ? 274  ARG D CA  1 
ATOM   14651 C  C   . ARG D  1 274 ? -34.579 -11.227 11.892  1.00 38.39  ? 274  ARG D C   1 
ATOM   14652 O  O   . ARG D  1 274 ? -35.632 -11.057 11.269  1.00 38.10  ? 274  ARG D O   1 
ATOM   14653 C  CB  . ARG D  1 274 ? -33.366 -9.071  11.517  1.00 34.46  ? 274  ARG D CB  1 
ATOM   14654 C  CG  . ARG D  1 274 ? -33.744 -7.624  11.764  1.00 36.65  ? 274  ARG D CG  1 
ATOM   14655 C  CD  . ARG D  1 274 ? -33.383 -6.742  10.563  1.00 41.04  ? 274  ARG D CD  1 
ATOM   14656 N  NE  . ARG D  1 274 ? -32.065 -6.112  10.660  1.00 44.13  ? 274  ARG D NE  1 
ATOM   14657 C  CZ  . ARG D  1 274 ? -31.863 -4.811  10.875  1.00 46.34  ? 274  ARG D CZ  1 
ATOM   14658 N  NH1 . ARG D  1 274 ? -32.885 -3.976  11.019  1.00 44.58  ? 274  ARG D NH1 1 
ATOM   14659 N  NH2 . ARG D  1 274 ? -30.629 -4.340  10.950  1.00 49.10  ? 274  ARG D NH2 1 
ATOM   14660 N  N   . THR D  1 275 ? -33.963 -12.404 12.008  1.00 34.39  ? 275  THR D N   1 
ATOM   14661 C  CA  . THR D  1 275 ? -34.429 -13.634 11.385  1.00 35.35  ? 275  THR D CA  1 
ATOM   14662 C  C   . THR D  1 275 ? -35.209 -14.556 12.320  1.00 38.41  ? 275  THR D C   1 
ATOM   14663 O  O   . THR D  1 275 ? -35.686 -15.604 11.893  1.00 42.85  ? 275  THR D O   1 
ATOM   14664 C  CB  . THR D  1 275 ? -33.243 -14.427 10.840  1.00 31.97  ? 275  THR D CB  1 
ATOM   14665 O  OG1 . THR D  1 275 ? -32.601 -15.116 11.915  1.00 32.47  ? 275  THR D OG1 1 
ATOM   14666 C  CG2 . THR D  1 275 ? -32.242 -13.491 10.188  1.00 37.59  ? 275  THR D CG2 1 
ATOM   14667 N  N   . ARG D  1 276 ? -35.327 -14.189 13.592  1.00 32.35  ? 276  ARG D N   1 
ATOM   14668 C  CA  . ARG D  1 276 ? -36.096 -14.993 14.536  1.00 30.62  ? 276  ARG D CA  1 
ATOM   14669 C  C   . ARG D  1 276 ? -37.540 -14.545 14.555  1.00 29.97  ? 276  ARG D C   1 
ATOM   14670 O  O   . ARG D  1 276 ? -37.822 -13.345 14.532  1.00 28.83  ? 276  ARG D O   1 
ATOM   14671 C  CB  . ARG D  1 276 ? -35.535 -14.839 15.938  1.00 35.26  ? 276  ARG D CB  1 
ATOM   14672 C  CG  . ARG D  1 276 ? -34.109 -15.300 16.073  1.00 38.19  ? 276  ARG D CG  1 
ATOM   14673 C  CD  . ARG D  1 276 ? -34.042 -16.772 16.378  1.00 42.33  ? 276  ARG D CD  1 
ATOM   14674 N  NE  . ARG D  1 276 ? -32.664 -17.239 16.414  1.00 47.76  ? 276  ARG D NE  1 
ATOM   14675 C  CZ  . ARG D  1 276 ? -31.990 -17.619 15.335  1.00 53.45  ? 276  ARG D CZ  1 
ATOM   14676 N  NH1 . ARG D  1 276 ? -32.580 -17.577 14.145  1.00 54.02  ? 276  ARG D NH1 1 
ATOM   14677 N  NH2 . ARG D  1 276 ? -30.734 -18.046 15.444  1.00 56.34  ? 276  ARG D NH2 1 
ATOM   14678 N  N   . PRO D  1 277 ? -38.470 -15.503 14.612  1.00 35.72  ? 277  PRO D N   1 
ATOM   14679 C  CA  . PRO D  1 277 ? -39.890 -15.169 14.783  1.00 35.76  ? 277  PRO D CA  1 
ATOM   14680 C  C   . PRO D  1 277 ? -40.090 -14.329 16.041  1.00 35.81  ? 277  PRO D C   1 
ATOM   14681 O  O   . PRO D  1 277 ? -39.308 -14.462 16.980  1.00 39.13  ? 277  PRO D O   1 
ATOM   14682 C  CB  . PRO D  1 277 ? -40.565 -16.539 14.924  1.00 31.77  ? 277  PRO D CB  1 
ATOM   14683 C  CG  . PRO D  1 277 ? -39.471 -17.503 15.177  1.00 32.75  ? 277  PRO D CG  1 
ATOM   14684 C  CD  . PRO D  1 277 ? -38.237 -16.949 14.554  1.00 32.34  ? 277  PRO D CD  1 
ATOM   14685 N  N   . ALA D  1 278 ? -41.092 -13.463 16.054  1.00 28.92  ? 278  ALA D N   1 
ATOM   14686 C  CA  . ALA D  1 278 ? -41.217 -12.493 17.140  1.00 28.28  ? 278  ALA D CA  1 
ATOM   14687 C  C   . ALA D  1 278 ? -41.366 -13.188 18.483  1.00 29.76  ? 278  ALA D C   1 
ATOM   14688 O  O   . ALA D  1 278 ? -40.750 -12.792 19.495  1.00 29.99  ? 278  ALA D O   1 
ATOM   14689 C  CB  . ALA D  1 278 ? -42.397 -11.558 16.893  1.00 27.32  ? 278  ALA D CB  1 
ATOM   14690 N  N   . GLN D  1 279 ? -42.169 -14.245 18.482  1.00 35.95  ? 279  GLN D N   1 
ATOM   14691 C  CA  . GLN D  1 279 ? -42.511 -14.910 19.726  1.00 39.94  ? 279  GLN D CA  1 
ATOM   14692 C  C   . GLN D  1 279 ? -41.272 -15.527 20.380  1.00 42.32  ? 279  GLN D C   1 
ATOM   14693 O  O   . GLN D  1 279 ? -41.190 -15.607 21.602  1.00 45.08  ? 279  GLN D O   1 
ATOM   14694 C  CB  . GLN D  1 279 ? -43.617 -15.941 19.503  1.00 43.75  ? 279  GLN D CB  1 
ATOM   14695 C  CG  . GLN D  1 279 ? -44.256 -16.443 20.784  1.00 47.25  ? 279  GLN D CG  1 
ATOM   14696 C  CD  . GLN D  1 279 ? -44.618 -15.323 21.737  1.00 49.51  ? 279  GLN D CD  1 
ATOM   14697 O  OE1 . GLN D  1 279 ? -45.342 -14.391 21.383  1.00 50.76  ? 279  GLN D OE1 1 
ATOM   14698 N  NE2 . GLN D  1 279 ? -44.111 -15.409 22.959  1.00 50.51  ? 279  GLN D NE2 1 
ATOM   14699 N  N   . ASP D  1 280 ? -40.302 -15.934 19.562  1.00 33.13  ? 280  ASP D N   1 
ATOM   14700 C  CA  . ASP D  1 280 ? -39.025 -16.421 20.066  1.00 32.80  ? 280  ASP D CA  1 
ATOM   14701 C  C   . ASP D  1 280 ? -38.308 -15.346 20.856  1.00 30.73  ? 280  ASP D C   1 
ATOM   14702 O  O   . ASP D  1 280 ? -37.771 -15.616 21.929  1.00 33.07  ? 280  ASP D O   1 
ATOM   14703 C  CB  . ASP D  1 280 ? -38.142 -16.931 18.935  1.00 49.37  ? 280  ASP D CB  1 
ATOM   14704 C  CG  . ASP D  1 280 ? -38.580 -18.294 18.436  1.00 60.98  ? 280  ASP D CG  1 
ATOM   14705 O  OD1 . ASP D  1 280 ? -39.699 -18.718 18.820  1.00 63.23  ? 280  ASP D OD1 1 
ATOM   14706 O  OD2 . ASP D  1 280 ? -37.815 -18.934 17.667  1.00 66.10  ? 280  ASP D OD2 1 
ATOM   14707 N  N   . LEU D  1 281 ? -38.302 -14.123 20.343  1.00 28.68  ? 281  LEU D N   1 
ATOM   14708 C  CA  . LEU D  1 281 ? -37.705 -13.024 21.093  1.00 29.65  ? 281  LEU D CA  1 
ATOM   14709 C  C   . LEU D  1 281 ? -38.420 -12.835 22.425  1.00 29.44  ? 281  LEU D C   1 
ATOM   14710 O  O   . LEU D  1 281 ? -37.790 -12.879 23.490  1.00 27.48  ? 281  LEU D O   1 
ATOM   14711 C  CB  . LEU D  1 281 ? -37.721 -11.733 20.278  1.00 26.54  ? 281  LEU D CB  1 
ATOM   14712 C  CG  . LEU D  1 281 ? -36.366 -11.344 19.692  1.00 26.36  ? 281  LEU D CG  1 
ATOM   14713 C  CD1 . LEU D  1 281 ? -35.537 -12.566 19.359  1.00 27.56  ? 281  LEU D CD1 1 
ATOM   14714 C  CD2 . LEU D  1 281 ? -36.571 -10.490 18.459  1.00 25.79  ? 281  LEU D CD2 1 
ATOM   14715 N  N   . VAL D  1 282 ? -39.740 -12.669 22.359  1.00 32.79  ? 282  VAL D N   1 
ATOM   14716 C  CA  . VAL D  1 282 ? -40.544 -12.451 23.570  1.00 32.47  ? 282  VAL D CA  1 
ATOM   14717 C  C   . VAL D  1 282 ? -40.402 -13.544 24.637  1.00 33.08  ? 282  VAL D C   1 
ATOM   14718 O  O   . VAL D  1 282 ? -40.412 -13.250 25.836  1.00 34.48  ? 282  VAL D O   1 
ATOM   14719 C  CB  . VAL D  1 282 ? -42.030 -12.212 23.222  1.00 34.42  ? 282  VAL D CB  1 
ATOM   14720 C  CG1 . VAL D  1 282 ? -42.951 -12.635 24.353  1.00 33.77  ? 282  VAL D CG1 1 
ATOM   14721 C  CG2 . VAL D  1 282 ? -42.239 -10.757 22.897  1.00 37.78  ? 282  VAL D CG2 1 
ATOM   14722 N  N   . ASP D  1 283 ? -40.251 -14.793 24.207  1.00 31.27  ? 283  ASP D N   1 
ATOM   14723 C  CA  . ASP D  1 283 ? -40.067 -15.892 25.146  1.00 34.63  ? 283  ASP D CA  1 
ATOM   14724 C  C   . ASP D  1 283 ? -38.866 -15.642 26.054  1.00 40.72  ? 283  ASP D C   1 
ATOM   14725 O  O   . ASP D  1 283 ? -39.015 -15.540 27.268  1.00 45.42  ? 283  ASP D O   1 
ATOM   14726 C  CB  . ASP D  1 283 ? -39.920 -17.226 24.416  1.00 37.62  ? 283  ASP D CB  1 
ATOM   14727 C  CG  . ASP D  1 283 ? -41.243 -17.743 23.893  1.00 41.37  ? 283  ASP D CG  1 
ATOM   14728 O  OD1 . ASP D  1 283 ? -42.273 -17.173 24.308  1.00 43.21  ? 283  ASP D OD1 1 
ATOM   14729 O  OD2 . ASP D  1 283 ? -41.259 -18.709 23.086  1.00 42.29  ? 283  ASP D OD2 1 
ATOM   14730 N  N   . HIS D  1 284 ? -37.688 -15.461 25.474  1.00 31.45  ? 284  HIS D N   1 
ATOM   14731 C  CA  . HIS D  1 284 ? -36.507 -15.267 26.298  1.00 34.48  ? 284  HIS D CA  1 
ATOM   14732 C  C   . HIS D  1 284 ? -36.416 -13.821 26.781  1.00 32.01  ? 284  HIS D C   1 
ATOM   14733 O  O   . HIS D  1 284 ? -35.429 -13.432 27.402  1.00 32.07  ? 284  HIS D O   1 
ATOM   14734 C  CB  . HIS D  1 284 ? -35.240 -15.659 25.542  1.00 61.32  ? 284  HIS D CB  1 
ATOM   14735 C  CG  . HIS D  1 284 ? -35.274 -17.051 25.007  1.00 73.50  ? 284  HIS D CG  1 
ATOM   14736 N  ND1 . HIS D  1 284 ? -35.694 -17.345 23.727  1.00 79.28  ? 284  HIS D ND1 1 
ATOM   14737 C  CD2 . HIS D  1 284 ? -34.964 -18.235 25.584  1.00 79.84  ? 284  HIS D CD2 1 
ATOM   14738 C  CE1 . HIS D  1 284 ? -35.629 -18.650 23.532  1.00 82.74  ? 284  HIS D CE1 1 
ATOM   14739 N  NE2 . HIS D  1 284 ? -35.191 -19.213 24.643  1.00 84.63  ? 284  HIS D NE2 1 
ATOM   14740 N  N   . GLU D  1 285 ? -37.421 -13.006 26.469  1.00 27.81  ? 285  GLU D N   1 
ATOM   14741 C  CA  . GLU D  1 285 ? -37.393 -11.613 26.925  1.00 27.66  ? 285  GLU D CA  1 
ATOM   14742 C  C   . GLU D  1 285 ? -37.348 -11.527 28.429  1.00 33.75  ? 285  GLU D C   1 
ATOM   14743 O  O   . GLU D  1 285 ? -36.657 -10.669 28.964  1.00 26.10  ? 285  GLU D O   1 
ATOM   14744 C  CB  . GLU D  1 285 ? -38.575 -10.802 26.393  1.00 56.55  ? 285  GLU D CB  1 
ATOM   14745 C  CG  . GLU D  1 285 ? -38.570 -9.330  26.778  1.00 54.44  ? 285  GLU D CG  1 
ATOM   14746 C  CD  . GLU D  1 285 ? -39.887 -8.680  26.438  1.00 53.39  ? 285  GLU D CD  1 
ATOM   14747 O  OE1 . GLU D  1 285 ? -40.846 -8.844  27.219  1.00 53.98  ? 285  GLU D OE1 1 
ATOM   14748 O  OE2 . GLU D  1 285 ? -39.975 -8.037  25.376  1.00 51.78  ? 285  GLU D OE2 1 
ATOM   14749 N  N   . TRP D  1 286 ? -38.046 -12.417 29.136  1.00 77.93  ? 286  TRP D N   1 
ATOM   14750 C  CA  . TRP D  1 286 ? -37.818 -12.373 30.565  1.00 84.17  ? 286  TRP D CA  1 
ATOM   14751 C  C   . TRP D  1 286 ? -36.802 -13.463 30.920  1.00 83.23  ? 286  TRP D C   1 
ATOM   14752 O  O   . TRP D  1 286 ? -37.129 -14.586 31.322  1.00 84.16  ? 286  TRP D O   1 
ATOM   14753 C  CB  . TRP D  1 286 ? -39.136 -12.545 31.346  1.00 82.88  ? 286  TRP D CB  1 
ATOM   14754 C  CG  . TRP D  1 286 ? -40.129 -11.427 31.125  1.00 87.56  ? 286  TRP D CG  1 
ATOM   14755 C  CD1 . TRP D  1 286 ? -41.188 -11.427 30.261  1.00 87.79  ? 286  TRP D CD1 1 
ATOM   14756 C  CD2 . TRP D  1 286 ? -40.142 -10.139 31.775  1.00 93.13  ? 286  TRP D CD2 1 
ATOM   14757 N  NE1 . TRP D  1 286 ? -41.859 -10.226 30.332  1.00 88.19  ? 286  TRP D NE1 1 
ATOM   14758 C  CE2 . TRP D  1 286 ? -41.241 -9.425  31.246  1.00 92.53  ? 286  TRP D CE2 1 
ATOM   14759 C  CE3 . TRP D  1 286 ? -39.333 -9.528  32.744  1.00 96.40  ? 286  TRP D CE3 1 
ATOM   14760 C  CZ2 . TRP D  1 286 ? -41.546 -8.113  31.668  1.00 95.07  ? 286  TRP D CZ2 1 
ATOM   14761 C  CZ3 . TRP D  1 286 ? -39.644 -8.218  33.158  1.00 95.55  ? 286  TRP D CZ3 1 
ATOM   14762 C  CH2 . TRP D  1 286 ? -40.738 -7.533  32.618  1.00 94.82  ? 286  TRP D CH2 1 
ATOM   14763 N  N   . HIS D  1 287 ? -35.545 -13.053 30.789  1.00 59.80  ? 287  HIS D N   1 
ATOM   14764 C  CA  . HIS D  1 287 ? -34.359 -13.715 31.299  1.00 61.02  ? 287  HIS D CA  1 
ATOM   14765 C  C   . HIS D  1 287 ? -33.436 -12.592 31.734  1.00 59.07  ? 287  HIS D C   1 
ATOM   14766 O  O   . HIS D  1 287 ? -33.075 -12.459 32.905  1.00 62.93  ? 287  HIS D O   1 
ATOM   14767 C  CB  . HIS D  1 287 ? -33.691 -14.615 30.259  1.00 87.14  ? 287  HIS D CB  1 
ATOM   14768 C  CG  . HIS D  1 287 ? -34.192 -16.033 30.276  1.00 98.05  ? 287  HIS D CG  1 
ATOM   14769 N  ND1 . HIS D  1 287 ? -35.421 -16.383 30.788  1.00 101.72 ? 287  HIS D ND1 1 
ATOM   14770 C  CD2 . HIS D  1 287 ? -33.620 -17.184 29.842  1.00 102.56 ? 287  HIS D CD2 1 
ATOM   14771 C  CE1 . HIS D  1 287 ? -35.590 -17.692 30.666  1.00 103.92 ? 287  HIS D CE1 1 
ATOM   14772 N  NE2 . HIS D  1 287 ? -34.515 -18.198 30.094  1.00 104.05 ? 287  HIS D NE2 1 
ATOM   14773 N  N   . VAL D  1 288 ? -33.099 -11.767 30.747  1.00 58.64  ? 288  VAL D N   1 
ATOM   14774 C  CA  . VAL D  1 288 ? -32.033 -10.771 30.808  1.00 59.43  ? 288  VAL D CA  1 
ATOM   14775 C  C   . VAL D  1 288 ? -31.976 -9.853  32.035  1.00 66.85  ? 288  VAL D C   1 
ATOM   14776 O  O   . VAL D  1 288 ? -30.903 -9.312  32.341  1.00 67.90  ? 288  VAL D O   1 
ATOM   14777 C  CB  . VAL D  1 288 ? -32.101 -9.862  29.581  1.00 48.92  ? 288  VAL D CB  1 
ATOM   14778 C  CG1 . VAL D  1 288 ? -32.052 -10.692 28.330  1.00 49.42  ? 288  VAL D CG1 1 
ATOM   14779 C  CG2 . VAL D  1 288 ? -33.381 -9.037  29.609  1.00 45.46  ? 288  VAL D CG2 1 
ATOM   14780 N  N   . LEU D  1 289 ? -33.119 -9.651  32.699  1.00 70.72  ? 289  LEU D N   1 
ATOM   14781 C  CA  . LEU D  1 289 ? -33.201 -8.851  33.919  1.00 71.81  ? 289  LEU D CA  1 
ATOM   14782 C  C   . LEU D  1 289 ? -32.172 -9.334  34.927  1.00 77.68  ? 289  LEU D C   1 
ATOM   14783 O  O   . LEU D  1 289 ? -32.223 -10.499 35.338  1.00 78.59  ? 289  LEU D O   1 
ATOM   14784 C  CB  . LEU D  1 289 ? -34.581 -9.005  34.545  1.00 74.59  ? 289  LEU D CB  1 
ATOM   14785 C  CG  . LEU D  1 289 ? -35.597 -7.882  34.369  1.00 74.94  ? 289  LEU D CG  1 
ATOM   14786 C  CD1 . LEU D  1 289 ? -36.840 -8.163  35.218  1.00 75.49  ? 289  LEU D CD1 1 
ATOM   14787 C  CD2 . LEU D  1 289 ? -34.970 -6.547  34.733  1.00 74.28  ? 289  LEU D CD2 1 
ATOM   14788 N  N   . PRO D  1 290 ? -31.260 -8.426  35.353  1.00 89.73  ? 290  PRO D N   1 
ATOM   14789 C  CA  . PRO D  1 290 ? -30.035 -8.682  36.141  1.00 90.95  ? 290  PRO D CA  1 
ATOM   14790 C  C   . PRO D  1 290 ? -30.251 -9.474  37.425  1.00 94.07  ? 290  PRO D C   1 
ATOM   14791 O  O   . PRO D  1 290 ? -29.489 -10.396 37.735  1.00 93.38  ? 290  PRO D O   1 
ATOM   14792 C  CB  . PRO D  1 290 ? -29.522 -7.270  36.480  1.00 77.60  ? 290  PRO D CB  1 
ATOM   14793 C  CG  . PRO D  1 290 ? -30.673 -6.343  36.208  1.00 76.40  ? 290  PRO D CG  1 
ATOM   14794 C  CD  . PRO D  1 290 ? -31.437 -6.986  35.088  1.00 78.07  ? 290  PRO D CD  1 
ATOM   14795 N  N   . GLN D  1 291 ? -31.283 -9.102  38.170  1.00 104.70 ? 291  GLN D N   1 
ATOM   14796 C  CA  . GLN D  1 291 ? -31.625 -9.809  39.391  1.00 108.18 ? 291  GLN D CA  1 
ATOM   14797 C  C   . GLN D  1 291 ? -33.144 -9.878  39.566  1.00 110.63 ? 291  GLN D C   1 
ATOM   14798 O  O   . GLN D  1 291 ? -33.892 -9.170  38.881  1.00 108.86 ? 291  GLN D O   1 
ATOM   14799 C  CB  . GLN D  1 291 ? -30.932 -9.173  40.611  1.00 90.47  ? 291  GLN D CB  1 
ATOM   14800 C  CG  . GLN D  1 291 ? -31.462 -7.805  41.042  1.00 86.11  ? 291  GLN D CG  1 
ATOM   14801 C  CD  . GLN D  1 291 ? -31.074 -6.670  40.105  1.00 81.92  ? 291  GLN D CD  1 
ATOM   14802 O  OE1 . GLN D  1 291 ? -31.831 -6.318  39.194  1.00 81.51  ? 291  GLN D OE1 1 
ATOM   14803 N  NE2 . GLN D  1 291 ? -29.903 -6.077  40.339  1.00 78.92  ? 291  GLN D NE2 1 
ATOM   14804 N  N   . GLU D  1 292 ? -33.585 -10.752 40.468  1.00 108.70 ? 292  GLU D N   1 
ATOM   14805 C  CA  . GLU D  1 292 ? -35.000 -10.918 40.760  1.00 106.25 ? 292  GLU D CA  1 
ATOM   14806 C  C   . GLU D  1 292 ? -35.587 -9.572  41.171  1.00 99.34  ? 292  GLU D C   1 
ATOM   14807 O  O   . GLU D  1 292 ? -35.164 -8.967  42.162  1.00 98.08  ? 292  GLU D O   1 
ATOM   14808 C  CB  . GLU D  1 292 ? -35.157 -11.923 41.902  1.00 105.55 ? 292  GLU D CB  1 
ATOM   14809 C  CG  . GLU D  1 292 ? -36.579 -12.351 42.186  1.00 108.74 ? 292  GLU D CG  1 
ATOM   14810 C  CD  . GLU D  1 292 ? -36.665 -13.325 43.345  1.00 112.69 ? 292  GLU D CD  1 
ATOM   14811 O  OE1 . GLU D  1 292 ? -35.693 -13.401 44.132  1.00 113.52 ? 292  GLU D OE1 1 
ATOM   14812 O  OE2 . GLU D  1 292 ? -37.701 -14.017 43.463  1.00 114.31 ? 292  GLU D OE2 1 
ATOM   14813 N  N   . SER D  1 293 ? -36.592 -9.123  40.425  1.00 71.27  ? 293  SER D N   1 
ATOM   14814 C  CA  . SER D  1 293 ? -37.136 -7.788  40.635  1.00 63.62  ? 293  SER D CA  1 
ATOM   14815 C  C   . SER D  1 293 ? -38.630 -7.661  40.349  1.00 58.82  ? 293  SER D C   1 
ATOM   14816 O  O   . SER D  1 293 ? -39.257 -8.522  39.715  1.00 53.91  ? 293  SER D O   1 
ATOM   14817 C  CB  . SER D  1 293 ? -36.344 -6.737  39.834  1.00 74.70  ? 293  SER D CB  1 
ATOM   14818 O  OG  . SER D  1 293 ? -36.335 -7.019  38.443  1.00 74.39  ? 293  SER D OG  1 
ATOM   14819 N  N   . ILE D  1 294 ? -39.185 -6.576  40.877  1.00 84.63  ? 294  ILE D N   1 
ATOM   14820 C  CA  . ILE D  1 294 ? -40.511 -6.104  40.516  1.00 84.89  ? 294  ILE D CA  1 
ATOM   14821 C  C   . ILE D  1 294 ? -40.443 -4.591  40.233  1.00 78.59  ? 294  ILE D C   1 
ATOM   14822 O  O   . ILE D  1 294 ? -39.680 -3.851  40.867  1.00 74.99  ? 294  ILE D O   1 
ATOM   14823 C  CB  . ILE D  1 294 ? -41.594 -6.442  41.596  1.00 85.70  ? 294  ILE D CB  1 
ATOM   14824 C  CG1 . ILE D  1 294 ? -41.330 -5.677  42.902  1.00 85.00  ? 294  ILE D CG1 1 
ATOM   14825 C  CG2 . ILE D  1 294 ? -41.706 -7.967  41.815  1.00 84.58  ? 294  ILE D CG2 1 
ATOM   14826 C  CD1 . ILE D  1 294 ? -42.582 -5.401  43.721  1.00 83.77  ? 294  ILE D CD1 1 
ATOM   14827 N  N   . PHE D  1 295 ? -41.250 -4.152  39.276  1.00 63.96  ? 295  PHE D N   1 
ATOM   14828 C  CA  . PHE D  1 295 ? -41.186 -2.794  38.747  1.00 65.60  ? 295  PHE D CA  1 
ATOM   14829 C  C   . PHE D  1 295 ? -39.792 -2.493  38.188  1.00 69.45  ? 295  PHE D C   1 
ATOM   14830 O  O   . PHE D  1 295 ? -39.249 -1.413  38.394  1.00 71.13  ? 295  PHE D O   1 
ATOM   14831 C  CB  . PHE D  1 295 ? -41.659 -1.727  39.767  1.00 68.80  ? 295  PHE D CB  1 
ATOM   14832 C  CG  . PHE D  1 295 ? -42.474 -0.579  39.146  1.00 67.50  ? 295  PHE D CG  1 
ATOM   14833 C  CD1 . PHE D  1 295 ? -42.364 -0.263  37.795  1.00 65.40  ? 295  PHE D CD1 1 
ATOM   14834 C  CD2 . PHE D  1 295 ? -43.348 0.174   39.916  1.00 65.49  ? 295  PHE D CD2 1 
ATOM   14835 C  CE1 . PHE D  1 295 ? -43.106 0.770   37.219  1.00 60.75  ? 295  PHE D CE1 1 
ATOM   14836 C  CE2 . PHE D  1 295 ? -44.077 1.218   39.345  1.00 62.75  ? 295  PHE D CE2 1 
ATOM   14837 C  CZ  . PHE D  1 295 ? -43.955 1.503   37.991  1.00 60.78  ? 295  PHE D CZ  1 
ATOM   14838 N  N   . ARG D  1 296 ? -39.213 -3.472  37.500  1.00 97.60  ? 296  ARG D N   1 
ATOM   14839 C  CA  . ARG D  1 296 ? -38.104 -3.226  36.582  1.00 98.94  ? 296  ARG D CA  1 
ATOM   14840 C  C   . ARG D  1 296 ? -38.482 -3.926  35.282  1.00 103.51 ? 296  ARG D C   1 
ATOM   14841 O  O   . ARG D  1 296 ? -39.221 -4.913  35.289  1.00 111.32 ? 296  ARG D O   1 
ATOM   14842 C  CB  . ARG D  1 296 ? -36.771 -3.755  37.126  1.00 68.03  ? 296  ARG D CB  1 
ATOM   14843 C  CG  . ARG D  1 296 ? -36.298 -3.088  38.417  1.00 67.81  ? 296  ARG D CG  1 
ATOM   14844 C  CD  . ARG D  1 296 ? -35.983 -1.597  38.222  1.00 67.66  ? 296  ARG D CD  1 
ATOM   14845 N  NE  . ARG D  1 296 ? -35.706 -0.885  39.475  1.00 67.37  ? 296  ARG D NE  1 
ATOM   14846 C  CZ  . ARG D  1 296 ? -36.614 -0.636  40.421  1.00 68.50  ? 296  ARG D CZ  1 
ATOM   14847 N  NH1 . ARG D  1 296 ? -37.866 -1.047  40.282  1.00 70.01  ? 296  ARG D NH1 1 
ATOM   14848 N  NH2 . ARG D  1 296 ? -36.274 0.011   41.526  1.00 68.89  ? 296  ARG D NH2 1 
ATOM   14849 N  N   . PHE D  1 297 ? -37.999 -3.422  34.159  1.00 74.09  ? 297  PHE D N   1 
ATOM   14850 C  CA  . PHE D  1 297 ? -38.434 -3.971  32.890  1.00 67.96  ? 297  PHE D CA  1 
ATOM   14851 C  C   . PHE D  1 297 ? -37.225 -4.185  32.016  1.00 62.85  ? 297  PHE D C   1 
ATOM   14852 O  O   . PHE D  1 297 ? -36.281 -3.397  32.074  1.00 66.09  ? 297  PHE D O   1 
ATOM   14853 C  CB  . PHE D  1 297 ? -39.371 -2.988  32.223  1.00 75.71  ? 297  PHE D CB  1 
ATOM   14854 C  CG  . PHE D  1 297 ? -40.374 -2.375  33.158  1.00 77.78  ? 297  PHE D CG  1 
ATOM   14855 C  CD1 . PHE D  1 297 ? -41.588 -2.986  33.378  1.00 79.25  ? 297  PHE D CD1 1 
ATOM   14856 C  CD2 . PHE D  1 297 ? -40.114 -1.184  33.808  1.00 76.85  ? 297  PHE D CD2 1 
ATOM   14857 C  CE1 . PHE D  1 297 ? -42.534 -2.429  34.221  1.00 77.51  ? 297  PHE D CE1 1 
ATOM   14858 C  CE2 . PHE D  1 297 ? -41.059 -0.630  34.656  1.00 75.69  ? 297  PHE D CE2 1 
ATOM   14859 C  CZ  . PHE D  1 297 ? -42.271 -1.258  34.847  1.00 74.80  ? 297  PHE D CZ  1 
ATOM   14860 N  N   . SER D  1 298 ? -37.255 -5.240  31.203  1.00 48.05  ? 298  SER D N   1 
ATOM   14861 C  CA  . SER D  1 298 ? -36.090 -5.644  30.400  1.00 39.15  ? 298  SER D CA  1 
ATOM   14862 C  C   . SER D  1 298 ? -35.508 -4.570  29.469  1.00 27.67  ? 298  SER D C   1 
ATOM   14863 O  O   . SER D  1 298 ? -34.370 -4.142  29.647  1.00 22.41  ? 298  SER D O   1 
ATOM   14864 C  CB  . SER D  1 298 ? -36.410 -6.908  29.609  1.00 54.55  ? 298  SER D CB  1 
ATOM   14865 O  OG  . SER D  1 298 ? -36.652 -7.987  30.490  1.00 57.99  ? 298  SER D OG  1 
ATOM   14866 N  N   . PHE D  1 299 ? -36.286 -4.149  28.474  1.00 32.14  ? 299  PHE D N   1 
ATOM   14867 C  CA  . PHE D  1 299 ? -35.823 -3.169  27.497  1.00 27.05  ? 299  PHE D CA  1 
ATOM   14868 C  C   . PHE D  1 299 ? -36.613 -1.874  27.580  1.00 25.19  ? 299  PHE D C   1 
ATOM   14869 O  O   . PHE D  1 299 ? -37.825 -1.873  27.404  1.00 26.12  ? 299  PHE D O   1 
ATOM   14870 C  CB  . PHE D  1 299 ? -35.925 -3.764  26.100  1.00 23.41  ? 299  PHE D CB  1 
ATOM   14871 C  CG  . PHE D  1 299 ? -35.114 -5.016  25.927  1.00 26.51  ? 299  PHE D CG  1 
ATOM   14872 C  CD1 . PHE D  1 299 ? -33.760 -4.946  25.607  1.00 27.50  ? 299  PHE D CD1 1 
ATOM   14873 C  CD2 . PHE D  1 299 ? -35.690 -6.263  26.102  1.00 30.19  ? 299  PHE D CD2 1 
ATOM   14874 C  CE1 . PHE D  1 299 ? -32.991 -6.102  25.452  1.00 29.41  ? 299  PHE D CE1 1 
ATOM   14875 C  CE2 . PHE D  1 299 ? -34.922 -7.428  25.947  1.00 32.84  ? 299  PHE D CE2 1 
ATOM   14876 C  CZ  . PHE D  1 299 ? -33.572 -7.343  25.620  1.00 31.39  ? 299  PHE D CZ  1 
ATOM   14877 N  N   . VAL D  1 300 ? -35.927 -0.772  27.858  1.00 22.70  ? 300  VAL D N   1 
ATOM   14878 C  CA  . VAL D  1 300 ? -36.585 0.522   28.072  1.00 22.97  ? 300  VAL D CA  1 
ATOM   14879 C  C   . VAL D  1 300 ? -35.816 1.614   27.326  1.00 23.66  ? 300  VAL D C   1 
ATOM   14880 O  O   . VAL D  1 300 ? -34.807 1.302   26.678  1.00 22.99  ? 300  VAL D O   1 
ATOM   14881 C  CB  . VAL D  1 300 ? -36.568 0.870   29.541  1.00 19.48  ? 300  VAL D CB  1 
ATOM   14882 C  CG1 . VAL D  1 300 ? -37.416 -0.112  30.327  1.00 19.98  ? 300  VAL D CG1 1 
ATOM   14883 C  CG2 . VAL D  1 300 ? -35.128 0.895   30.019  1.00 19.56  ? 300  VAL D CG2 1 
ATOM   14884 N  N   . PRO D  1 301 ? -36.280 2.889   27.395  1.00 24.53  ? 301  PRO D N   1 
ATOM   14885 C  CA  . PRO D  1 301 ? -35.456 3.938   26.776  1.00 22.95  ? 301  PRO D CA  1 
ATOM   14886 C  C   . PRO D  1 301 ? -33.975 3.919   27.189  1.00 20.47  ? 301  PRO D C   1 
ATOM   14887 O  O   . PRO D  1 301 ? -33.633 3.642   28.334  1.00 19.71  ? 301  PRO D O   1 
ATOM   14888 C  CB  . PRO D  1 301 ? -36.144 5.226   27.234  1.00 18.27  ? 301  PRO D CB  1 
ATOM   14889 C  CG  . PRO D  1 301 ? -37.568 4.858   27.289  1.00 18.35  ? 301  PRO D CG  1 
ATOM   14890 C  CD  . PRO D  1 301 ? -37.631 3.402   27.710  1.00 18.63  ? 301  PRO D CD  1 
ATOM   14891 N  N   . VAL D  1 302 ? -33.099 4.181   26.230  1.00 18.66  ? 302  VAL D N   1 
ATOM   14892 C  CA  . VAL D  1 302 ? -31.671 4.190   26.489  1.00 18.94  ? 302  VAL D CA  1 
ATOM   14893 C  C   . VAL D  1 302 ? -31.199 5.633   26.536  1.00 22.77  ? 302  VAL D C   1 
ATOM   14894 O  O   . VAL D  1 302 ? -31.694 6.474   25.788  1.00 18.66  ? 302  VAL D O   1 
ATOM   14895 C  CB  . VAL D  1 302 ? -30.896 3.424   25.390  1.00 19.30  ? 302  VAL D CB  1 
ATOM   14896 C  CG1 . VAL D  1 302 ? -31.120 4.057   24.027  1.00 19.19  ? 302  VAL D CG1 1 
ATOM   14897 C  CG2 . VAL D  1 302 ? -29.410 3.362   25.713  1.00 19.75  ? 302  VAL D CG2 1 
ATOM   14898 N  N   . VAL D  1 303 ? -30.239 5.932   27.408  1.00 25.36  ? 303  VAL D N   1 
ATOM   14899 C  CA  . VAL D  1 303 ? -29.645 7.255   27.397  1.00 22.86  ? 303  VAL D CA  1 
ATOM   14900 C  C   . VAL D  1 303 ? -28.466 7.105   26.436  1.00 24.45  ? 303  VAL D C   1 
ATOM   14901 O  O   . VAL D  1 303 ? -27.370 6.639   26.789  1.00 21.98  ? 303  VAL D O   1 
ATOM   14902 C  CB  . VAL D  1 303 ? -29.196 7.608   28.820  1.00 24.03  ? 303  VAL D CB  1 
ATOM   14903 C  CG1 . VAL D  1 303 ? -28.245 8.789   28.845  1.00 26.60  ? 303  VAL D CG1 1 
ATOM   14904 C  CG2 . VAL D  1 303 ? -30.418 7.865   29.692  1.00 22.81  ? 303  VAL D CG2 1 
ATOM   14905 N  N   . ASP D  1 304 ? -28.740 7.524   25.202  1.00 27.64  ? 304  ASP D N   1 
ATOM   14906 C  CA  . ASP D  1 304 ? -27.902 7.235   24.044  1.00 28.00  ? 304  ASP D CA  1 
ATOM   14907 C  C   . ASP D  1 304 ? -27.080 8.406   23.547  1.00 25.96  ? 304  ASP D C   1 
ATOM   14908 O  O   . ASP D  1 304 ? -26.328 8.271   22.593  1.00 27.83  ? 304  ASP D O   1 
ATOM   14909 C  CB  . ASP D  1 304 ? -28.780 6.694   22.908  1.00 36.14  ? 304  ASP D CB  1 
ATOM   14910 C  CG  . ASP D  1 304 ? -29.936 7.634   22.554  1.00 37.09  ? 304  ASP D CG  1 
ATOM   14911 O  OD1 . ASP D  1 304 ? -30.107 8.659   23.262  1.00 37.90  ? 304  ASP D OD1 1 
ATOM   14912 O  OD2 . ASP D  1 304 ? -30.669 7.345   21.571  1.00 34.87  ? 304  ASP D OD2 1 
ATOM   14913 N  N   . GLY D  1 305 ? -27.269 9.567   24.155  1.00 25.75  ? 305  GLY D N   1 
ATOM   14914 C  CA  . GLY D  1 305 ? -26.701 10.797  23.637  1.00 28.32  ? 305  GLY D CA  1 
ATOM   14915 C  C   . GLY D  1 305 ? -27.455 11.412  22.464  1.00 30.65  ? 305  GLY D C   1 
ATOM   14916 O  O   . GLY D  1 305 ? -27.168 12.539  22.056  1.00 32.29  ? 305  GLY D O   1 
ATOM   14917 N  N   . ASP D  1 306 ? -28.430 10.684  21.932  1.00 31.58  ? 306  ASP D N   1 
ATOM   14918 C  CA  . ASP D  1 306 ? -29.165 11.123  20.744  1.00 35.47  ? 306  ASP D CA  1 
ATOM   14919 C  C   . ASP D  1 306 ? -30.525 11.704  21.153  1.00 30.03  ? 306  ASP D C   1 
ATOM   14920 O  O   . ASP D  1 306 ? -30.709 12.931  21.193  1.00 23.43  ? 306  ASP D O   1 
ATOM   14921 C  CB  . ASP D  1 306 ? -29.366 9.910   19.813  1.00 49.11  ? 306  ASP D CB  1 
ATOM   14922 C  CG  . ASP D  1 306 ? -29.892 10.276  18.425  1.00 50.34  ? 306  ASP D CG  1 
ATOM   14923 O  OD1 . ASP D  1 306 ? -30.739 11.185  18.296  1.00 49.73  ? 306  ASP D OD1 1 
ATOM   14924 O  OD2 . ASP D  1 306 ? -29.466 9.615   17.454  1.00 50.80  ? 306  ASP D OD2 1 
ATOM   14925 N  N   . PHE D  1 307 ? -31.454 10.802  21.477  1.00 34.54  ? 307  PHE D N   1 
ATOM   14926 C  CA  . PHE D  1 307 ? -32.828 11.150  21.826  1.00 32.72  ? 307  PHE D CA  1 
ATOM   14927 C  C   . PHE D  1 307 ? -32.825 11.774  23.194  1.00 35.57  ? 307  PHE D C   1 
ATOM   14928 O  O   . PHE D  1 307 ? -33.405 12.834  23.415  1.00 37.30  ? 307  PHE D O   1 
ATOM   14929 C  CB  . PHE D  1 307 ? -33.696 9.900   21.855  1.00 18.66  ? 307  PHE D CB  1 
ATOM   14930 C  CG  . PHE D  1 307 ? -35.163 10.192  21.950  1.00 18.49  ? 307  PHE D CG  1 
ATOM   14931 C  CD1 . PHE D  1 307 ? -35.733 10.606  23.150  1.00 18.37  ? 307  PHE D CD1 1 
ATOM   14932 C  CD2 . PHE D  1 307 ? -35.979 10.045  20.847  1.00 18.56  ? 307  PHE D CD2 1 
ATOM   14933 C  CE1 . PHE D  1 307 ? -37.082 10.873  23.242  1.00 18.37  ? 307  PHE D CE1 1 
ATOM   14934 C  CE2 . PHE D  1 307 ? -37.317 10.302  20.939  1.00 18.53  ? 307  PHE D CE2 1 
ATOM   14935 C  CZ  . PHE D  1 307 ? -37.867 10.723  22.143  1.00 18.46  ? 307  PHE D CZ  1 
ATOM   14936 N  N   . LEU D  1 308 ? -32.179 11.083  24.121  1.00 36.79  ? 308  LEU D N   1 
ATOM   14937 C  CA  . LEU D  1 308 ? -31.859 11.661  25.412  1.00 36.12  ? 308  LEU D CA  1 
ATOM   14938 C  C   . LEU D  1 308 ? -30.419 12.156  25.357  1.00 34.15  ? 308  LEU D C   1 
ATOM   14939 O  O   . LEU D  1 308 ? -29.491 11.366  25.184  1.00 29.68  ? 308  LEU D O   1 
ATOM   14940 C  CB  . LEU D  1 308 ? -32.074 10.637  26.524  1.00 24.84  ? 308  LEU D CB  1 
ATOM   14941 C  CG  . LEU D  1 308 ? -33.549 10.224  26.605  1.00 22.81  ? 308  LEU D CG  1 
ATOM   14942 C  CD1 . LEU D  1 308 ? -33.760 9.239   27.723  1.00 23.30  ? 308  LEU D CD1 1 
ATOM   14943 C  CD2 . LEU D  1 308 ? -34.465 11.432  26.780  1.00 18.44  ? 308  LEU D CD2 1 
ATOM   14944 N  N   . SER D  1 309 ? -30.260 13.474  25.472  1.00 32.54  ? 309  SER D N   1 
ATOM   14945 C  CA  . SER D  1 309 ? -28.974 14.139  25.296  1.00 34.52  ? 309  SER D CA  1 
ATOM   14946 C  C   . SER D  1 309 ? -28.053 13.912  26.482  1.00 33.75  ? 309  SER D C   1 
ATOM   14947 O  O   . SER D  1 309 ? -26.835 13.913  26.335  1.00 32.62  ? 309  SER D O   1 
ATOM   14948 C  CB  . SER D  1 309 ? -29.178 15.640  25.085  1.00 39.23  ? 309  SER D CB  1 
ATOM   14949 O  OG  . SER D  1 309 ? -29.595 16.279  26.275  1.00 39.56  ? 309  SER D OG  1 
ATOM   14950 N  N   . ASP D  1 310 ? -28.657 13.743  27.655  1.00 33.37  ? 310  ASP D N   1 
ATOM   14951 C  CA  . ASP D  1 310 ? -27.971 13.334  28.874  1.00 36.68  ? 310  ASP D CA  1 
ATOM   14952 C  C   . ASP D  1 310 ? -28.989 12.467  29.604  1.00 33.66  ? 310  ASP D C   1 
ATOM   14953 O  O   . ASP D  1 310 ? -30.036 12.138  29.041  1.00 34.19  ? 310  ASP D O   1 
ATOM   14954 C  CB  . ASP D  1 310 ? -27.596 14.557  29.723  1.00 57.54  ? 310  ASP D CB  1 
ATOM   14955 C  CG  . ASP D  1 310 ? -26.388 14.309  30.637  1.00 63.84  ? 310  ASP D CG  1 
ATOM   14956 O  OD1 . ASP D  1 310 ? -26.299 13.235  31.265  1.00 66.28  ? 310  ASP D OD1 1 
ATOM   14957 O  OD2 . ASP D  1 310 ? -25.522 15.204  30.733  1.00 64.76  ? 310  ASP D OD2 1 
ATOM   14958 N  N   . THR D  1 311 ? -28.700 12.088  30.844  1.00 31.61  ? 311  THR D N   1 
ATOM   14959 C  CA  . THR D  1 311 ? -29.662 11.337  31.636  1.00 28.95  ? 311  THR D CA  1 
ATOM   14960 C  C   . THR D  1 311 ? -30.842 12.250  31.859  1.00 25.88  ? 311  THR D C   1 
ATOM   14961 O  O   . THR D  1 311 ? -30.680 13.465  31.853  1.00 25.02  ? 311  THR D O   1 
ATOM   14962 C  CB  . THR D  1 311 ? -29.125 11.026  33.021  1.00 35.93  ? 311  THR D CB  1 
ATOM   14963 O  OG1 . THR D  1 311 ? -29.652 11.991  33.936  1.00 38.70  ? 311  THR D OG1 1 
ATOM   14964 C  CG2 . THR D  1 311 ? -27.608 11.088  33.048  1.00 36.07  ? 311  THR D CG2 1 
ATOM   14965 N  N   . PRO D  1 312 ? -32.033 11.678  32.072  1.00 25.88  ? 312  PRO D N   1 
ATOM   14966 C  CA  . PRO D  1 312 ? -33.189 12.521  32.394  1.00 24.93  ? 312  PRO D CA  1 
ATOM   14967 C  C   . PRO D  1 312 ? -33.010 13.342  33.682  1.00 26.81  ? 312  PRO D C   1 
ATOM   14968 O  O   . PRO D  1 312 ? -33.463 14.490  33.701  1.00 26.02  ? 312  PRO D O   1 
ATOM   14969 C  CB  . PRO D  1 312 ? -34.346 11.516  32.525  1.00 27.22  ? 312  PRO D CB  1 
ATOM   14970 C  CG  . PRO D  1 312 ? -33.698 10.196  32.708  1.00 30.16  ? 312  PRO D CG  1 
ATOM   14971 C  CD  . PRO D  1 312 ? -32.402 10.260  31.953  1.00 30.41  ? 312  PRO D CD  1 
ATOM   14972 N  N   . GLU D  1 313 ? -32.362 12.797  34.717  1.00 37.77  ? 313  GLU D N   1 
ATOM   14973 C  CA  . GLU D  1 313 ? -32.175 13.554  35.970  1.00 37.83  ? 313  GLU D CA  1 
ATOM   14974 C  C   . GLU D  1 313 ? -31.355 14.807  35.706  1.00 34.54  ? 313  GLU D C   1 
ATOM   14975 O  O   . GLU D  1 313 ? -31.618 15.855  36.277  1.00 39.47  ? 313  GLU D O   1 
ATOM   14976 C  CB  . GLU D  1 313 ? -31.573 12.707  37.109  1.00 33.24  ? 313  GLU D CB  1 
ATOM   14977 C  CG  . GLU D  1 313 ? -31.150 11.269  36.710  1.00 108.24 ? 313  GLU D CG  1 
ATOM   14978 C  CD  . GLU D  1 313 ? -32.279 10.220  36.764  1.00 105.46 ? 313  GLU D CD  1 
ATOM   14979 O  OE1 . GLU D  1 313 ? -33.251 10.402  37.534  1.00 105.65 ? 313  GLU D OE1 1 
ATOM   14980 O  OE2 . GLU D  1 313 ? -32.177 9.198   36.043  1.00 102.02 ? 313  GLU D OE2 1 
ATOM   14981 N  N   . ALA D  1 314 ? -30.392 14.697  34.801  1.00 20.49  ? 314  ALA D N   1 
ATOM   14982 C  CA  . ALA D  1 314 ? -29.652 15.853  34.296  1.00 20.88  ? 314  ALA D CA  1 
ATOM   14983 C  C   . ALA D  1 314 ? -30.544 16.896  33.594  1.00 24.74  ? 314  ALA D C   1 
ATOM   14984 O  O   . ALA D  1 314 ? -30.546 18.086  33.935  1.00 27.69  ? 314  ALA D O   1 
ATOM   14985 C  CB  . ALA D  1 314 ? -28.579 15.383  33.340  1.00 20.86  ? 314  ALA D CB  1 
ATOM   14986 N  N   . LEU D  1 315 ? -31.288 16.448  32.594  1.00 30.92  ? 315  LEU D N   1 
ATOM   14987 C  CA  . LEU D  1 315 ? -32.079 17.360  31.790  1.00 30.31  ? 315  LEU D CA  1 
ATOM   14988 C  C   . LEU D  1 315 ? -33.144 18.045  32.613  1.00 30.61  ? 315  LEU D C   1 
ATOM   14989 O  O   . LEU D  1 315 ? -33.480 19.191  32.337  1.00 34.29  ? 315  LEU D O   1 
ATOM   14990 C  CB  . LEU D  1 315 ? -32.719 16.625  30.627  1.00 20.16  ? 315  LEU D CB  1 
ATOM   14991 C  CG  . LEU D  1 315 ? -31.706 15.729  29.940  1.00 19.94  ? 315  LEU D CG  1 
ATOM   14992 C  CD1 . LEU D  1 315 ? -32.395 14.941  28.861  1.00 45.29  ? 315  LEU D CD1 1 
ATOM   14993 C  CD2 . LEU D  1 315 ? -30.575 16.558  29.383  1.00 25.44  ? 315  LEU D CD2 1 
ATOM   14994 N  N   . ILE D  1 316 ? -33.686 17.360  33.615  1.00 22.25  ? 316  ILE D N   1 
ATOM   14995 C  CA  . ILE D  1 316 ? -34.638 18.038  34.480  1.00 27.12  ? 316  ILE D CA  1 
ATOM   14996 C  C   . ILE D  1 316 ? -33.909 18.932  35.474  1.00 36.02  ? 316  ILE D C   1 
ATOM   14997 O  O   . ILE D  1 316 ? -34.464 19.942  35.924  1.00 39.76  ? 316  ILE D O   1 
ATOM   14998 C  CB  . ILE D  1 316 ? -35.612 17.104  35.222  1.00 29.26  ? 316  ILE D CB  1 
ATOM   14999 C  CG1 . ILE D  1 316 ? -34.856 16.047  36.010  1.00 29.04  ? 316  ILE D CG1 1 
ATOM   15000 C  CG2 . ILE D  1 316 ? -36.603 16.478  34.264  1.00 28.86  ? 316  ILE D CG2 1 
ATOM   15001 C  CD1 . ILE D  1 316 ? -35.737 15.269  36.955  1.00 29.69  ? 316  ILE D CD1 1 
ATOM   15002 N  N   . ASN D  1 317 ? -32.668 18.573  35.807  1.00 42.88  ? 317  ASN D N   1 
ATOM   15003 C  CA  . ASN D  1 317 ? -31.845 19.417  36.679  1.00 46.52  ? 317  ASN D CA  1 
ATOM   15004 C  C   . ASN D  1 317 ? -31.539 20.775  36.074  1.00 45.01  ? 317  ASN D C   1 
ATOM   15005 O  O   . ASN D  1 317 ? -31.442 21.762  36.797  1.00 43.13  ? 317  ASN D O   1 
ATOM   15006 C  CB  . ASN D  1 317 ? -30.522 18.739  37.012  1.00 67.92  ? 317  ASN D CB  1 
ATOM   15007 C  CG  . ASN D  1 317 ? -30.506 18.141  38.389  1.00 74.90  ? 317  ASN D CG  1 
ATOM   15008 O  OD1 . ASN D  1 317 ? -31.526 18.121  39.092  1.00 75.04  ? 317  ASN D OD1 1 
ATOM   15009 N  ND2 . ASN D  1 317 ? -29.340 17.632  38.790  1.00 78.86  ? 317  ASN D ND2 1 
ATOM   15010 N  N   . THR D  1 318 ? -31.380 20.826  34.752  1.00 46.28  ? 318  THR D N   1 
ATOM   15011 C  CA  . THR D  1 318 ? -30.919 22.063  34.122  1.00 49.64  ? 318  THR D CA  1 
ATOM   15012 C  C   . THR D  1 318 ? -31.873 22.813  33.173  1.00 52.46  ? 318  THR D C   1 
ATOM   15013 O  O   . THR D  1 318 ? -32.309 23.914  33.502  1.00 55.76  ? 318  THR D O   1 
ATOM   15014 C  CB  . THR D  1 318 ? -29.549 21.880  33.462  1.00 59.58  ? 318  THR D CB  1 
ATOM   15015 O  OG1 . THR D  1 318 ? -29.462 20.562  32.911  1.00 62.53  ? 318  THR D OG1 1 
ATOM   15016 C  CG2 . THR D  1 318 ? -28.447 22.067  34.493  1.00 59.47  ? 318  THR D CG2 1 
ATOM   15017 N  N   . GLY D  1 319 ? -32.219 22.231  32.028  1.00 57.85  ? 319  GLY D N   1 
ATOM   15018 C  CA  . GLY D  1 319 ? -32.827 22.994  30.940  1.00 62.48  ? 319  GLY D CA  1 
ATOM   15019 C  C   . GLY D  1 319 ? -34.054 23.854  31.261  1.00 65.92  ? 319  GLY D C   1 
ATOM   15020 O  O   . GLY D  1 319 ? -34.767 23.594  32.233  1.00 64.81  ? 319  GLY D O   1 
ATOM   15021 N  N   . ASP D  1 320 ? -34.289 24.884  30.439  1.00 71.00  ? 320  ASP D N   1 
ATOM   15022 C  CA  . ASP D  1 320 ? -35.299 25.916  30.719  1.00 71.49  ? 320  ASP D CA  1 
ATOM   15023 C  C   . ASP D  1 320 ? -36.740 25.495  30.415  1.00 69.58  ? 320  ASP D C   1 
ATOM   15024 O  O   . ASP D  1 320 ? -37.117 25.220  29.271  1.00 69.29  ? 320  ASP D O   1 
ATOM   15025 C  CB  . ASP D  1 320 ? -34.981 27.205  29.948  1.00 75.25  ? 320  ASP D CB  1 
ATOM   15026 C  CG  . ASP D  1 320 ? -35.868 28.370  30.367  1.00 78.89  ? 320  ASP D CG  1 
ATOM   15027 O  OD1 . ASP D  1 320 ? -36.272 28.398  31.547  1.00 80.71  ? 320  ASP D OD1 1 
ATOM   15028 O  OD2 . ASP D  1 320 ? -36.162 29.256  29.529  1.00 79.94  ? 320  ASP D OD2 1 
ATOM   15029 N  N   . PHE D  1 321 ? -37.539 25.454  31.471  1.00 61.91  ? 321  PHE D N   1 
ATOM   15030 C  CA  . PHE D  1 321 ? -38.944 25.075  31.387  1.00 60.02  ? 321  PHE D CA  1 
ATOM   15031 C  C   . PHE D  1 321 ? -39.939 26.234  31.396  1.00 64.70  ? 321  PHE D C   1 
ATOM   15032 O  O   . PHE D  1 321 ? -41.141 26.020  31.576  1.00 64.77  ? 321  PHE D O   1 
ATOM   15033 C  CB  . PHE D  1 321 ? -39.269 23.937  32.353  1.00 55.08  ? 321  PHE D CB  1 
ATOM   15034 C  CG  . PHE D  1 321 ? -38.447 22.700  32.088  1.00 49.99  ? 321  PHE D CG  1 
ATOM   15035 C  CD1 . PHE D  1 321 ? -38.282 22.238  30.791  1.00 47.12  ? 321  PHE D CD1 1 
ATOM   15036 C  CD2 . PHE D  1 321 ? -37.787 22.043  33.118  1.00 47.01  ? 321  PHE D CD2 1 
ATOM   15037 C  CE1 . PHE D  1 321 ? -37.516 21.131  30.536  1.00 44.15  ? 321  PHE D CE1 1 
ATOM   15038 C  CE2 . PHE D  1 321 ? -37.012 20.933  32.865  1.00 42.53  ? 321  PHE D CE2 1 
ATOM   15039 C  CZ  . PHE D  1 321 ? -36.877 20.477  31.577  1.00 41.62  ? 321  PHE D CZ  1 
ATOM   15040 N  N   . GLN D  1 322 ? -39.413 27.453  31.258  1.00 72.49  ? 322  GLN D N   1 
ATOM   15041 C  CA  . GLN D  1 322 ? -40.224 28.668  31.184  1.00 76.42  ? 322  GLN D CA  1 
ATOM   15042 C  C   . GLN D  1 322 ? -41.344 28.436  30.188  1.00 76.42  ? 322  GLN D C   1 
ATOM   15043 O  O   . GLN D  1 322 ? -41.113 27.876  29.114  1.00 75.87  ? 322  GLN D O   1 
ATOM   15044 C  CB  . GLN D  1 322 ? -39.373 29.860  30.714  1.00 86.99  ? 322  GLN D CB  1 
ATOM   15045 C  CG  . GLN D  1 322 ? -38.526 30.523  31.792  1.00 92.23  ? 322  GLN D CG  1 
ATOM   15046 C  CD  . GLN D  1 322 ? -39.356 31.288  32.814  1.00 99.11  ? 322  GLN D CD  1 
ATOM   15047 O  OE1 . GLN D  1 322 ? -40.535 31.574  32.585  1.00 102.76 ? 322  GLN D OE1 1 
ATOM   15048 N  NE2 . GLN D  1 322 ? -38.743 31.625  33.947  1.00 100.07 ? 322  GLN D NE2 1 
ATOM   15049 N  N   . ASP D  1 323 ? -42.555 28.843  30.562  1.00 88.54  ? 323  ASP D N   1 
ATOM   15050 C  CA  . ASP D  1 323 ? -43.768 28.509  29.804  1.00 89.69  ? 323  ASP D CA  1 
ATOM   15051 C  C   . ASP D  1 323 ? -43.796 27.057  29.280  1.00 84.55  ? 323  ASP D C   1 
ATOM   15052 O  O   . ASP D  1 323 ? -43.656 26.778  28.081  1.00 83.00  ? 323  ASP D O   1 
ATOM   15053 C  CB  . ASP D  1 323 ? -44.166 29.565  28.740  1.00 153.37 ? 323  ASP D CB  1 
ATOM   15054 C  CG  . ASP D  1 323 ? -43.041 29.909  27.773  1.00 152.96 ? 323  ASP D CG  1 
ATOM   15055 O  OD1 . ASP D  1 323 ? -42.839 29.157  26.794  1.00 152.06 ? 323  ASP D OD1 1 
ATOM   15056 O  OD2 . ASP D  1 323 ? -42.381 30.953  27.976  1.00 153.25 ? 323  ASP D OD2 1 
ATOM   15057 N  N   . LEU D  1 324 ? -43.915 26.146  30.237  1.00 66.50  ? 324  LEU D N   1 
ATOM   15058 C  CA  . LEU D  1 324 ? -44.335 24.787  29.984  1.00 54.52  ? 324  LEU D CA  1 
ATOM   15059 C  C   . LEU D  1 324 ? -45.420 24.505  31.001  1.00 49.62  ? 324  LEU D C   1 
ATOM   15060 O  O   . LEU D  1 324 ? -45.237 24.748  32.188  1.00 52.06  ? 324  LEU D O   1 
ATOM   15061 C  CB  . LEU D  1 324 ? -43.184 23.810  30.189  1.00 35.88  ? 324  LEU D CB  1 
ATOM   15062 C  CG  . LEU D  1 324 ? -43.654 22.350  30.170  1.00 31.47  ? 324  LEU D CG  1 
ATOM   15063 C  CD1 . LEU D  1 324 ? -44.427 22.029  28.884  1.00 31.93  ? 324  LEU D CD1 1 
ATOM   15064 C  CD2 . LEU D  1 324 ? -42.498 21.376  30.370  1.00 26.78  ? 324  LEU D CD2 1 
ATOM   15065 N  N   . GLN D  1 325 ? -46.556 24.004  30.551  1.00 33.52  ? 325  GLN D N   1 
ATOM   15066 C  CA  . GLN D  1 325 ? -47.608 23.671  31.494  1.00 35.13  ? 325  GLN D CA  1 
ATOM   15067 C  C   . GLN D  1 325 ? -47.698 22.171  31.690  1.00 31.78  ? 325  GLN D C   1 
ATOM   15068 O  O   . GLN D  1 325 ? -47.844 21.398  30.725  1.00 33.80  ? 325  GLN D O   1 
ATOM   15069 C  CB  . GLN D  1 325 ? -48.938 24.249  31.037  1.00 62.23  ? 325  GLN D CB  1 
ATOM   15070 C  CG  . GLN D  1 325 ? -48.951 25.761  31.042  1.00 69.67  ? 325  GLN D CG  1 
ATOM   15071 C  CD  . GLN D  1 325 ? -50.007 26.335  30.130  1.00 75.64  ? 325  GLN D CD  1 
ATOM   15072 O  OE1 . GLN D  1 325 ? -50.048 26.034  28.933  1.00 75.12  ? 325  GLN D OE1 1 
ATOM   15073 N  NE2 . GLN D  1 325 ? -50.876 27.171  30.691  1.00 79.92  ? 325  GLN D NE2 1 
ATOM   15074 N  N   . VAL D  1 326 ? -47.599 21.758  32.945  1.00 41.75  ? 326  VAL D N   1 
ATOM   15075 C  CA  . VAL D  1 326 ? -47.530 20.344  33.264  1.00 41.43  ? 326  VAL D CA  1 
ATOM   15076 C  C   . VAL D  1 326 ? -48.498 19.976  34.368  1.00 43.65  ? 326  VAL D C   1 
ATOM   15077 O  O   . VAL D  1 326 ? -48.573 20.656  35.382  1.00 46.53  ? 326  VAL D O   1 
ATOM   15078 C  CB  . VAL D  1 326 ? -46.117 19.946  33.701  1.00 25.86  ? 326  VAL D CB  1 
ATOM   15079 C  CG1 . VAL D  1 326 ? -46.093 18.505  34.123  1.00 24.49  ? 326  VAL D CG1 1 
ATOM   15080 C  CG2 . VAL D  1 326 ? -45.147 20.162  32.570  1.00 24.43  ? 326  VAL D CG2 1 
ATOM   15081 N  N   . LEU D  1 327 ? -49.244 18.899  34.161  1.00 26.61  ? 327  LEU D N   1 
ATOM   15082 C  CA  . LEU D  1 327 ? -50.072 18.333  35.213  1.00 27.29  ? 327  LEU D CA  1 
ATOM   15083 C  C   . LEU D  1 327 ? -49.538 16.939  35.579  1.00 26.44  ? 327  LEU D C   1 
ATOM   15084 O  O   . LEU D  1 327 ? -49.542 16.041  34.752  1.00 25.78  ? 327  LEU D O   1 
ATOM   15085 C  CB  . LEU D  1 327 ? -51.541 18.288  34.761  1.00 28.22  ? 327  LEU D CB  1 
ATOM   15086 C  CG  . LEU D  1 327 ? -52.536 17.473  35.587  1.00 28.98  ? 327  LEU D CG  1 
ATOM   15087 C  CD1 . LEU D  1 327 ? -52.789 18.117  36.930  1.00 30.07  ? 327  LEU D CD1 1 
ATOM   15088 C  CD2 . LEU D  1 327 ? -53.814 17.300  34.823  1.00 29.71  ? 327  LEU D CD2 1 
ATOM   15089 N  N   . VAL D  1 328 ? -49.071 16.773  36.814  1.00 26.54  ? 328  VAL D N   1 
ATOM   15090 C  CA  . VAL D  1 328 ? -48.536 15.504  37.283  1.00 25.91  ? 328  VAL D CA  1 
ATOM   15091 C  C   . VAL D  1 328 ? -49.357 14.954  38.429  1.00 26.82  ? 328  VAL D C   1 
ATOM   15092 O  O   . VAL D  1 328 ? -50.096 15.690  39.095  1.00 27.93  ? 328  VAL D O   1 
ATOM   15093 C  CB  . VAL D  1 328 ? -47.134 15.672  37.808  1.00 25.30  ? 328  VAL D CB  1 
ATOM   15094 C  CG1 . VAL D  1 328 ? -46.264 16.137  36.717  1.00 39.00  ? 328  VAL D CG1 1 
ATOM   15095 C  CG2 . VAL D  1 328 ? -47.124 16.684  38.899  1.00 26.14  ? 328  VAL D CG2 1 
ATOM   15096 N  N   . GLY D  1 329 ? -49.251 13.653  38.671  1.00 26.50  ? 329  GLY D N   1 
ATOM   15097 C  CA  . GLY D  1 329 ? -49.932 13.135  39.848  1.00 27.48  ? 329  GLY D CA  1 
ATOM   15098 C  C   . GLY D  1 329 ? -49.814 11.653  40.101  1.00 31.44  ? 329  GLY D C   1 
ATOM   15099 O  O   . GLY D  1 329 ? -49.332 10.924  39.248  1.00 35.53  ? 329  GLY D O   1 
ATOM   15100 N  N   . VAL D  1 330 ? -50.270 11.198  41.266  1.00 29.39  ? 330  VAL D N   1 
ATOM   15101 C  CA  . VAL D  1 330 ? -50.112 9.784   41.629  1.00 28.86  ? 330  VAL D CA  1 
ATOM   15102 C  C   . VAL D  1 330 ? -51.398 9.189   42.207  1.00 30.38  ? 330  VAL D C   1 
ATOM   15103 O  O   . VAL D  1 330 ? -52.224 9.932   42.712  1.00 32.69  ? 330  VAL D O   1 
ATOM   15104 C  CB  . VAL D  1 330 ? -48.972 9.618   42.648  1.00 27.89  ? 330  VAL D CB  1 
ATOM   15105 C  CG1 . VAL D  1 330 ? -47.628 9.854   41.984  1.00 26.57  ? 330  VAL D CG1 1 
ATOM   15106 C  CG2 . VAL D  1 330 ? -49.162 10.577  43.796  1.00 28.82  ? 330  VAL D CG2 1 
ATOM   15107 N  N   . VAL D  1 331 ? -51.581 7.868   42.127  1.00 30.32  ? 331  VAL D N   1 
ATOM   15108 C  CA  . VAL D  1 331 ? -52.735 7.224   42.780  1.00 36.00  ? 331  VAL D CA  1 
ATOM   15109 C  C   . VAL D  1 331 ? -52.442 7.060   44.270  1.00 44.22  ? 331  VAL D C   1 
ATOM   15110 O  O   . VAL D  1 331 ? -51.334 7.366   44.708  1.00 47.92  ? 331  VAL D O   1 
ATOM   15111 C  CB  . VAL D  1 331 ? -53.057 5.831   42.194  1.00 37.79  ? 331  VAL D CB  1 
ATOM   15112 C  CG1 . VAL D  1 331 ? -53.273 5.901   40.699  1.00 38.40  ? 331  VAL D CG1 1 
ATOM   15113 C  CG2 . VAL D  1 331 ? -51.959 4.835   42.528  1.00 36.73  ? 331  VAL D CG2 1 
ATOM   15114 N  N   . LYS D  1 332 ? -53.402 6.566   45.054  1.00 56.22  ? 332  LYS D N   1 
ATOM   15115 C  CA  . LYS D  1 332 ? -53.191 6.524   46.503  1.00 56.99  ? 332  LYS D CA  1 
ATOM   15116 C  C   . LYS D  1 332 ? -52.038 5.609   46.881  1.00 58.65  ? 332  LYS D C   1 
ATOM   15117 O  O   . LYS D  1 332 ? -51.063 6.065   47.470  1.00 59.99  ? 332  LYS D O   1 
ATOM   15118 C  CB  . LYS D  1 332 ? -54.458 6.172   47.298  1.00 45.15  ? 332  LYS D CB  1 
ATOM   15119 C  CG  . LYS D  1 332 ? -54.496 6.870   48.687  1.00 42.52  ? 332  LYS D CG  1 
ATOM   15120 C  CD  . LYS D  1 332 ? -55.608 6.369   49.630  1.00 43.86  ? 332  LYS D CD  1 
ATOM   15121 C  CE  . LYS D  1 332 ? -55.181 5.137   50.459  1.00 44.57  ? 332  LYS D CE  1 
ATOM   15122 N  NZ  . LYS D  1 332 ? -55.998 3.886   50.184  1.00 43.65  ? 332  LYS D NZ  1 
ATOM   15123 N  N   . ASP D  1 333 ? -52.131 4.330   46.535  1.00 53.62  ? 333  ASP D N   1 
ATOM   15124 C  CA  . ASP D  1 333 ? -51.015 3.419   46.785  1.00 54.16  ? 333  ASP D CA  1 
ATOM   15125 C  C   . ASP D  1 333 ? -50.537 2.778   45.492  1.00 48.51  ? 333  ASP D C   1 
ATOM   15126 O  O   . ASP D  1 333 ? -51.156 1.845   44.987  1.00 45.91  ? 333  ASP D O   1 
ATOM   15127 C  CB  . ASP D  1 333 ? -51.441 2.336   47.780  1.00 63.57  ? 333  ASP D CB  1 
ATOM   15128 C  CG  . ASP D  1 333 ? -52.913 2.455   48.176  1.00 69.79  ? 333  ASP D CG  1 
ATOM   15129 O  OD1 . ASP D  1 333 ? -53.724 2.948   47.357  1.00 69.06  ? 333  ASP D OD1 1 
ATOM   15130 O  OD2 . ASP D  1 333 ? -53.259 2.062   49.311  1.00 74.73  ? 333  ASP D OD2 1 
ATOM   15131 N  N   . GLU D  1 334 ? -49.387 3.223   45.006  1.00 48.32  ? 334  GLU D N   1 
ATOM   15132 C  CA  . GLU D  1 334 ? -48.912 2.787   43.702  1.00 46.40  ? 334  GLU D CA  1 
ATOM   15133 C  C   . GLU D  1 334 ? -48.296 1.401   43.774  1.00 47.51  ? 334  GLU D C   1 
ATOM   15134 O  O   . GLU D  1 334 ? -48.239 0.685   42.776  1.00 49.10  ? 334  GLU D O   1 
ATOM   15135 C  CB  . GLU D  1 334 ? -47.885 3.773   43.151  1.00 43.97  ? 334  GLU D CB  1 
ATOM   15136 C  CG  . GLU D  1 334 ? -48.409 5.179   42.951  1.00 45.47  ? 334  GLU D CG  1 
ATOM   15137 C  CD  . GLU D  1 334 ? -48.748 5.478   41.501  1.00 45.10  ? 334  GLU D CD  1 
ATOM   15138 O  OE1 . GLU D  1 334 ? -48.399 4.650   40.630  1.00 45.21  ? 334  GLU D OE1 1 
ATOM   15139 O  OE2 . GLU D  1 334 ? -49.356 6.544   41.237  1.00 43.70  ? 334  GLU D OE2 1 
ATOM   15140 N  N   . GLY D  1 335 ? -47.840 1.022   44.960  1.00 42.36  ? 335  GLY D N   1 
ATOM   15141 C  CA  . GLY D  1 335 ? -47.046 -0.182  45.105  1.00 44.64  ? 335  GLY D CA  1 
ATOM   15142 C  C   . GLY D  1 335 ? -47.795 -1.502  45.203  1.00 48.64  ? 335  GLY D C   1 
ATOM   15143 O  O   . GLY D  1 335 ? -47.221 -2.565  44.952  1.00 51.17  ? 335  GLY D O   1 
ATOM   15144 N  N   . SER D  1 336 ? -49.068 -1.450  45.577  1.00 52.23  ? 336  SER D N   1 
ATOM   15145 C  CA  . SER D  1 336 ? -49.819 -2.671  45.835  1.00 52.58  ? 336  SER D CA  1 
ATOM   15146 C  C   . SER D  1 336 ? -49.898 -3.556  44.606  1.00 53.04  ? 336  SER D C   1 
ATOM   15147 O  O   . SER D  1 336 ? -49.640 -4.757  44.694  1.00 54.15  ? 336  SER D O   1 
ATOM   15148 C  CB  . SER D  1 336 ? -51.222 -2.337  46.326  1.00 56.97  ? 336  SER D CB  1 
ATOM   15149 O  OG  . SER D  1 336 ? -51.768 -1.289  45.549  1.00 58.47  ? 336  SER D OG  1 
ATOM   15150 N  N   . TYR D  1 337 ? -50.234 -2.952  43.465  1.00 56.84  ? 337  TYR D N   1 
ATOM   15151 C  CA  . TYR D  1 337 ? -50.460 -3.694  42.223  1.00 56.98  ? 337  TYR D CA  1 
ATOM   15152 C  C   . TYR D  1 337 ? -49.311 -4.642  41.898  1.00 54.47  ? 337  TYR D C   1 
ATOM   15153 O  O   . TYR D  1 337 ? -49.542 -5.770  41.479  1.00 56.69  ? 337  TYR D O   1 
ATOM   15154 C  CB  . TYR D  1 337 ? -50.724 -2.744  41.041  1.00 60.87  ? 337  TYR D CB  1 
ATOM   15155 C  CG  . TYR D  1 337 ? -50.919 -3.450  39.712  1.00 63.30  ? 337  TYR D CG  1 
ATOM   15156 C  CD1 . TYR D  1 337 ? -49.829 -3.831  38.940  1.00 65.36  ? 337  TYR D CD1 1 
ATOM   15157 C  CD2 . TYR D  1 337 ? -52.186 -3.724  39.229  1.00 66.48  ? 337  TYR D CD2 1 
ATOM   15158 C  CE1 . TYR D  1 337 ? -49.989 -4.479  37.741  1.00 69.31  ? 337  TYR D CE1 1 
ATOM   15159 C  CE2 . TYR D  1 337 ? -52.362 -4.374  38.020  1.00 71.58  ? 337  TYR D CE2 1 
ATOM   15160 C  CZ  . TYR D  1 337 ? -51.254 -4.752  37.277  1.00 73.92  ? 337  TYR D CZ  1 
ATOM   15161 O  OH  . TYR D  1 337 ? -51.404 -5.405  36.063  1.00 77.44  ? 337  TYR D OH  1 
ATOM   15162 N  N   . PHE D  1 338 ? -48.081 -4.183  42.104  1.00 48.34  ? 338  PHE D N   1 
ATOM   15163 C  CA  . PHE D  1 338 ? -46.902 -4.953  41.721  1.00 44.40  ? 338  PHE D CA  1 
ATOM   15164 C  C   . PHE D  1 338 ? -46.559 -6.063  42.694  1.00 43.44  ? 338  PHE D C   1 
ATOM   15165 O  O   . PHE D  1 338 ? -45.978 -7.066  42.296  1.00 46.89  ? 338  PHE D O   1 
ATOM   15166 C  CB  . PHE D  1 338 ? -45.695 -4.031  41.512  1.00 44.82  ? 338  PHE D CB  1 
ATOM   15167 C  CG  . PHE D  1 338 ? -45.986 -2.900  40.603  1.00 48.66  ? 338  PHE D CG  1 
ATOM   15168 C  CD1 . PHE D  1 338 ? -45.985 -3.089  39.235  1.00 51.61  ? 338  PHE D CD1 1 
ATOM   15169 C  CD2 . PHE D  1 338 ? -46.326 -1.661  41.110  1.00 52.16  ? 338  PHE D CD2 1 
ATOM   15170 C  CE1 . PHE D  1 338 ? -46.294 -2.054  38.381  1.00 54.27  ? 338  PHE D CE1 1 
ATOM   15171 C  CE2 . PHE D  1 338 ? -46.639 -0.620  40.270  1.00 54.67  ? 338  PHE D CE2 1 
ATOM   15172 C  CZ  . PHE D  1 338 ? -46.621 -0.815  38.899  1.00 55.92  ? 338  PHE D CZ  1 
ATOM   15173 N  N   . LEU D  1 339 ? -46.919 -5.897  43.960  1.00 39.03  ? 339  LEU D N   1 
ATOM   15174 C  CA  . LEU D  1 339 ? -46.479 -6.837  44.981  1.00 40.70  ? 339  LEU D CA  1 
ATOM   15175 C  C   . LEU D  1 339 ? -46.821 -8.299  44.669  1.00 44.72  ? 339  LEU D C   1 
ATOM   15176 O  O   . LEU D  1 339 ? -46.037 -9.200  44.985  1.00 45.67  ? 339  LEU D O   1 
ATOM   15177 C  CB  . LEU D  1 339 ? -46.995 -6.420  46.352  1.00 43.97  ? 339  LEU D CB  1 
ATOM   15178 C  CG  . LEU D  1 339 ? -46.360 -5.120  46.845  1.00 41.88  ? 339  LEU D CG  1 
ATOM   15179 C  CD1 . LEU D  1 339 ? -46.972 -4.709  48.158  1.00 44.38  ? 339  LEU D CD1 1 
ATOM   15180 C  CD2 . LEU D  1 339 ? -44.870 -5.276  47.000  1.00 38.65  ? 339  LEU D CD2 1 
ATOM   15181 N  N   . VAL D  1 340 ? -47.958 -8.530  44.011  1.00 45.74  ? 340  VAL D N   1 
ATOM   15182 C  CA  . VAL D  1 340 ? -48.364 -9.891  43.637  1.00 47.63  ? 340  VAL D CA  1 
ATOM   15183 C  C   . VAL D  1 340 ? -47.465 -10.528 42.580  1.00 48.99  ? 340  VAL D C   1 
ATOM   15184 O  O   . VAL D  1 340 ? -47.556 -11.726 42.314  1.00 49.00  ? 340  VAL D O   1 
ATOM   15185 C  CB  . VAL D  1 340 ? -49.815 -9.933  43.132  1.00 42.77  ? 340  VAL D CB  1 
ATOM   15186 C  CG1 . VAL D  1 340 ? -50.775 -9.953  44.300  1.00 47.85  ? 340  VAL D CG1 1 
ATOM   15187 C  CG2 . VAL D  1 340 ? -50.096 -8.753  42.239  1.00 37.89  ? 340  VAL D CG2 1 
ATOM   15188 N  N   . TYR D  1 341 ? -46.582 -9.712  42.013  1.00 52.80  ? 341  TYR D N   1 
ATOM   15189 C  CA  . TYR D  1 341 ? -45.726 -10.072 40.882  1.00 53.56  ? 341  TYR D CA  1 
ATOM   15190 C  C   . TYR D  1 341 ? -44.396 -10.711 41.283  1.00 58.64  ? 341  TYR D C   1 
ATOM   15191 O  O   . TYR D  1 341 ? -43.446 -10.749 40.501  1.00 60.06  ? 341  TYR D O   1 
ATOM   15192 C  CB  . TYR D  1 341 ? -45.604 -8.947  39.839  1.00 47.34  ? 341  TYR D CB  1 
ATOM   15193 C  CG  . TYR D  1 341 ? -46.838 -8.870  38.964  1.00 49.79  ? 341  TYR D CG  1 
ATOM   15194 C  CD1 . TYR D  1 341 ? -48.009 -8.318  39.450  1.00 55.59  ? 341  TYR D CD1 1 
ATOM   15195 C  CD2 . TYR D  1 341 ? -46.850 -9.387  37.672  1.00 49.74  ? 341  TYR D CD2 1 
ATOM   15196 C  CE1 . TYR D  1 341 ? -49.162 -8.261  38.680  1.00 57.54  ? 341  TYR D CE1 1 
ATOM   15197 C  CE2 . TYR D  1 341 ? -47.998 -9.336  36.886  1.00 51.40  ? 341  TYR D CE2 1 
ATOM   15198 C  CZ  . TYR D  1 341 ? -49.155 -8.768  37.404  1.00 56.21  ? 341  TYR D CZ  1 
ATOM   15199 O  OH  . TYR D  1 341 ? -50.321 -8.688  36.667  1.00 58.38  ? 341  TYR D OH  1 
ATOM   15200 N  N   . GLY D  1 342 ? -44.340 -11.218 42.509  1.00 66.22  ? 342  GLY D N   1 
ATOM   15201 C  CA  . GLY D  1 342 ? -43.126 -11.827 43.008  1.00 70.16  ? 342  GLY D CA  1 
ATOM   15202 C  C   . GLY D  1 342 ? -42.432 -11.282 44.236  1.00 73.61  ? 342  GLY D C   1 
ATOM   15203 O  O   . GLY D  1 342 ? -41.275 -11.619 44.491  1.00 76.79  ? 342  GLY D O   1 
ATOM   15204 N  N   . VAL D  1 343 ? -43.115 -10.443 45.005  1.00 81.83  ? 343  VAL D N   1 
ATOM   15205 C  CA  . VAL D  1 343 ? -42.776 -10.377 46.424  1.00 77.59  ? 343  VAL D CA  1 
ATOM   15206 C  C   . VAL D  1 343 ? -43.536 -11.474 47.155  1.00 77.67  ? 343  VAL D C   1 
ATOM   15207 O  O   . VAL D  1 343 ? -44.766 -11.503 47.130  1.00 82.02  ? 343  VAL D O   1 
ATOM   15208 C  CB  . VAL D  1 343 ? -43.142 -9.054  47.075  1.00 50.48  ? 343  VAL D CB  1 
ATOM   15209 C  CG1 . VAL D  1 343 ? -42.695 -9.065  48.541  1.00 47.27  ? 343  VAL D CG1 1 
ATOM   15210 C  CG2 . VAL D  1 343 ? -42.506 -7.917  46.321  1.00 48.62  ? 343  VAL D CG2 1 
ATOM   15211 N  N   . PRO D  1 344 ? -42.802 -12.385 47.803  1.00 55.57  ? 344  PRO D N   1 
ATOM   15212 C  CA  . PRO D  1 344 ? -43.385 -13.517 48.531  1.00 55.49  ? 344  PRO D CA  1 
ATOM   15213 C  C   . PRO D  1 344 ? -44.386 -13.097 49.610  1.00 56.06  ? 344  PRO D C   1 
ATOM   15214 O  O   . PRO D  1 344 ? -44.070 -12.249 50.444  1.00 55.86  ? 344  PRO D O   1 
ATOM   15215 C  CB  . PRO D  1 344 ? -42.164 -14.165 49.189  1.00 46.04  ? 344  PRO D CB  1 
ATOM   15216 C  CG  . PRO D  1 344 ? -41.047 -13.838 48.285  1.00 44.20  ? 344  PRO D CG  1 
ATOM   15217 C  CD  . PRO D  1 344 ? -41.336 -12.463 47.750  1.00 43.11  ? 344  PRO D CD  1 
ATOM   15218 N  N   . GLY D  1 345 ? -45.572 -13.704 49.595  1.00 59.24  ? 345  GLY D N   1 
ATOM   15219 C  CA  . GLY D  1 345 ? -46.566 -13.469 50.628  1.00 61.09  ? 345  GLY D CA  1 
ATOM   15220 C  C   . GLY D  1 345 ? -47.754 -12.649 50.174  1.00 60.37  ? 345  GLY D C   1 
ATOM   15221 O  O   . GLY D  1 345 ? -48.753 -12.535 50.886  1.00 63.23  ? 345  GLY D O   1 
ATOM   15222 N  N   . PHE D  1 346 ? -47.639 -12.074 48.984  1.00 53.87  ? 346  PHE D N   1 
ATOM   15223 C  CA  . PHE D  1 346 ? -48.692 -11.240 48.432  1.00 52.41  ? 346  PHE D CA  1 
ATOM   15224 C  C   . PHE D  1 346 ? -49.410 -11.964 47.299  1.00 55.02  ? 346  PHE D C   1 
ATOM   15225 O  O   . PHE D  1 346 ? -48.808 -12.317 46.277  1.00 55.91  ? 346  PHE D O   1 
ATOM   15226 C  CB  . PHE D  1 346 ? -48.117 -9.912  47.920  1.00 44.83  ? 346  PHE D CB  1 
ATOM   15227 C  CG  . PHE D  1 346 ? -47.579 -9.018  49.005  1.00 43.50  ? 346  PHE D CG  1 
ATOM   15228 C  CD1 . PHE D  1 346 ? -46.335 -9.256  49.571  1.00 41.67  ? 346  PHE D CD1 1 
ATOM   15229 C  CD2 . PHE D  1 346 ? -48.315 -7.930  49.453  1.00 43.64  ? 346  PHE D CD2 1 
ATOM   15230 C  CE1 . PHE D  1 346 ? -45.841 -8.435  50.568  1.00 40.63  ? 346  PHE D CE1 1 
ATOM   15231 C  CE2 . PHE D  1 346 ? -47.821 -7.107  50.454  1.00 42.05  ? 346  PHE D CE2 1 
ATOM   15232 C  CZ  . PHE D  1 346 ? -46.584 -7.361  51.009  1.00 40.83  ? 346  PHE D CZ  1 
ATOM   15233 N  N   . SER D  1 347 ? -50.703 -12.188 47.489  1.00 56.60  ? 347  SER D N   1 
ATOM   15234 C  CA  . SER D  1 347 ? -51.555 -12.732 46.443  1.00 55.59  ? 347  SER D CA  1 
ATOM   15235 C  C   . SER D  1 347 ? -52.777 -11.836 46.393  1.00 49.81  ? 347  SER D C   1 
ATOM   15236 O  O   . SER D  1 347 ? -52.992 -11.038 47.305  1.00 49.60  ? 347  SER D O   1 
ATOM   15237 C  CB  . SER D  1 347 ? -51.953 -14.170 46.776  1.00 70.62  ? 347  SER D CB  1 
ATOM   15238 O  OG  . SER D  1 347 ? -52.834 -14.714 45.811  1.00 73.39  ? 347  SER D OG  1 
ATOM   15239 N  N   . LYS D  1 348 ? -53.571 -11.936 45.336  1.00 44.80  ? 348  LYS D N   1 
ATOM   15240 C  CA  . LYS D  1 348 ? -54.800 -11.157 45.289  1.00 45.37  ? 348  LYS D CA  1 
ATOM   15241 C  C   . LYS D  1 348 ? -55.821 -11.792 46.220  1.00 48.45  ? 348  LYS D C   1 
ATOM   15242 O  O   . LYS D  1 348 ? -56.769 -11.141 46.647  1.00 49.30  ? 348  LYS D O   1 
ATOM   15243 C  CB  . LYS D  1 348 ? -55.363 -11.051 43.862  1.00 42.59  ? 348  LYS D CB  1 
ATOM   15244 C  CG  . LYS D  1 348 ? -55.972 -12.336 43.333  1.00 49.75  ? 348  LYS D CG  1 
ATOM   15245 C  CD  . LYS D  1 348 ? -56.648 -12.137 41.978  1.00 49.07  ? 348  LYS D CD  1 
ATOM   15246 C  CE  . LYS D  1 348 ? -57.140 -13.468 41.368  1.00 50.52  ? 348  LYS D CE  1 
ATOM   15247 N  NZ  . LYS D  1 348 ? -58.146 -14.204 42.203  1.00 52.22  ? 348  LYS D NZ  1 
ATOM   15248 N  N   . ASP D  1 349 ? -55.630 -13.072 46.521  1.00 54.71  ? 349  ASP D N   1 
ATOM   15249 C  CA  . ASP D  1 349 ? -56.642 -13.841 47.250  1.00 64.27  ? 349  ASP D CA  1 
ATOM   15250 C  C   . ASP D  1 349 ? -56.669 -13.766 48.803  1.00 75.98  ? 349  ASP D C   1 
ATOM   15251 O  O   . ASP D  1 349 ? -57.745 -13.617 49.386  1.00 77.65  ? 349  ASP D O   1 
ATOM   15252 C  CB  . ASP D  1 349 ? -56.688 -15.271 46.700  1.00 78.05  ? 349  ASP D CB  1 
ATOM   15253 C  CG  . ASP D  1 349 ? -56.998 -15.299 45.197  1.00 81.13  ? 349  ASP D CG  1 
ATOM   15254 O  OD1 . ASP D  1 349 ? -57.917 -14.565 44.766  1.00 83.02  ? 349  ASP D OD1 1 
ATOM   15255 O  OD2 . ASP D  1 349 ? -56.318 -16.030 44.442  1.00 80.53  ? 349  ASP D OD2 1 
ATOM   15256 N  N   . ASN D  1 350 ? -55.509 -13.854 49.462  1.00 66.62  ? 350  ASN D N   1 
ATOM   15257 C  CA  . ASN D  1 350 ? -55.437 -13.592 50.907  1.00 63.30  ? 350  ASN D CA  1 
ATOM   15258 C  C   . ASN D  1 350 ? -55.266 -12.091 51.176  1.00 60.61  ? 350  ASN D C   1 
ATOM   15259 O  O   . ASN D  1 350 ? -55.177 -11.308 50.240  1.00 58.33  ? 350  ASN D O   1 
ATOM   15260 C  CB  . ASN D  1 350 ? -54.377 -14.470 51.636  1.00 72.00  ? 350  ASN D CB  1 
ATOM   15261 C  CG  . ASN D  1 350 ? -53.027 -14.567 50.897  1.00 72.38  ? 350  ASN D CG  1 
ATOM   15262 O  OD1 . ASN D  1 350 ? -52.903 -14.144 49.751  1.00 70.49  ? 350  ASN D OD1 1 
ATOM   15263 N  ND2 . ASN D  1 350 ? -52.006 -15.126 51.580  1.00 77.47  ? 350  ASN D ND2 1 
ATOM   15264 N  N   . GLU D  1 351 ? -55.242 -11.675 52.436  1.00 65.20  ? 351  GLU D N   1 
ATOM   15265 C  CA  . GLU D  1 351 ? -55.009 -10.262 52.741  1.00 66.66  ? 351  GLU D CA  1 
ATOM   15266 C  C   . GLU D  1 351 ? -53.514 -9.987  52.833  1.00 62.21  ? 351  GLU D C   1 
ATOM   15267 O  O   . GLU D  1 351 ? -53.090 -8.867  53.132  1.00 58.57  ? 351  GLU D O   1 
ATOM   15268 C  CB  . GLU D  1 351 ? -55.694 -9.852  54.037  1.00 86.24  ? 351  GLU D CB  1 
ATOM   15269 C  CG  . GLU D  1 351 ? -57.195 -9.814  53.944  1.00 93.58  ? 351  GLU D CG  1 
ATOM   15270 C  CD  . GLU D  1 351 ? -57.852 -9.958  55.302  1.00 101.42 ? 351  GLU D CD  1 
ATOM   15271 O  OE1 . GLU D  1 351 ? -57.122 -10.030 56.319  1.00 101.91 ? 351  GLU D OE1 1 
ATOM   15272 O  OE2 . GLU D  1 351 ? -59.101 -10.005 55.349  1.00 105.61 ? 351  GLU D OE2 1 
ATOM   15273 N  N   . SER D  1 352 ? -52.729 -11.036 52.600  1.00 64.35  ? 352  SER D N   1 
ATOM   15274 C  CA  . SER D  1 352 ? -51.283 -10.923 52.480  1.00 61.22  ? 352  SER D CA  1 
ATOM   15275 C  C   . SER D  1 352 ? -50.627 -10.280 53.697  1.00 56.09  ? 352  SER D C   1 
ATOM   15276 O  O   . SER D  1 352 ? -49.740 -9.451  53.550  1.00 53.85  ? 352  SER D O   1 
ATOM   15277 C  CB  . SER D  1 352 ? -50.927 -10.125 51.217  1.00 70.12  ? 352  SER D CB  1 
ATOM   15278 O  OG  . SER D  1 352 ? -51.559 -10.655 50.061  1.00 70.99  ? 352  SER D OG  1 
ATOM   15279 N  N   . LEU D  1 353 ? -51.074 -10.633 54.895  1.00 48.68  ? 353  LEU D N   1 
ATOM   15280 C  CA  . LEU D  1 353 ? -50.395 -10.177 56.097  1.00 48.75  ? 353  LEU D CA  1 
ATOM   15281 C  C   . LEU D  1 353 ? -49.067 -10.897 56.061  1.00 51.82  ? 353  LEU D C   1 
ATOM   15282 O  O   . LEU D  1 353 ? -49.039 -12.094 55.834  1.00 56.72  ? 353  LEU D O   1 
ATOM   15283 C  CB  . LEU D  1 353 ? -51.184 -10.564 57.344  1.00 51.19  ? 353  LEU D CB  1 
ATOM   15284 C  CG  . LEU D  1 353 ? -52.702 -10.293 57.361  1.00 57.70  ? 353  LEU D CG  1 
ATOM   15285 C  CD1 . LEU D  1 353 ? -53.342 -10.734 58.684  1.00 60.78  ? 353  LEU D CD1 1 
ATOM   15286 C  CD2 . LEU D  1 353 ? -53.053 -8.839  57.069  1.00 54.92  ? 353  LEU D CD2 1 
ATOM   15287 N  N   . ILE D  1 354 ? -47.964 -10.180 56.237  1.00 51.12  ? 354  ILE D N   1 
ATOM   15288 C  CA  . ILE D  1 354 ? -46.643 -10.784 56.052  1.00 48.68  ? 354  ILE D CA  1 
ATOM   15289 C  C   . ILE D  1 354 ? -45.853 -10.763 57.340  1.00 50.69  ? 354  ILE D C   1 
ATOM   15290 O  O   . ILE D  1 354 ? -46.149 -9.972  58.240  1.00 51.56  ? 354  ILE D O   1 
ATOM   15291 C  CB  . ILE D  1 354 ? -45.806 -10.068 54.962  1.00 45.14  ? 354  ILE D CB  1 
ATOM   15292 C  CG1 . ILE D  1 354 ? -45.816 -8.555  55.177  1.00 45.46  ? 354  ILE D CG1 1 
ATOM   15293 C  CG2 . ILE D  1 354 ? -46.328 -10.394 53.584  1.00 43.77  ? 354  ILE D CG2 1 
ATOM   15294 C  CD1 . ILE D  1 354 ? -44.949 -7.793  54.205  1.00 40.81  ? 354  ILE D CD1 1 
ATOM   15295 N  N   . SER D  1 355 ? -44.852 -11.637 57.428  1.00 56.39  ? 355  SER D N   1 
ATOM   15296 C  CA  . SER D  1 355 ? -43.988 -11.686 58.604  1.00 60.42  ? 355  SER D CA  1 
ATOM   15297 C  C   . SER D  1 355 ? -42.911 -10.630 58.485  1.00 56.00  ? 355  SER D C   1 
ATOM   15298 O  O   . SER D  1 355 ? -42.787 -9.974  57.445  1.00 51.16  ? 355  SER D O   1 
ATOM   15299 C  CB  . SER D  1 355 ? -43.324 -13.058 58.730  1.00 73.11  ? 355  SER D CB  1 
ATOM   15300 O  OG  . SER D  1 355 ? -42.392 -13.276 57.683  1.00 72.43  ? 355  SER D OG  1 
ATOM   15301 N  N   . ARG D  1 356 ? -42.103 -10.484 59.528  1.00 56.31  ? 356  ARG D N   1 
ATOM   15302 C  CA  . ARG D  1 356 ? -41.036 -9.506  59.448  1.00 55.40  ? 356  ARG D CA  1 
ATOM   15303 C  C   . ARG D  1 356 ? -40.012 -9.944  58.423  1.00 54.28  ? 356  ARG D C   1 
ATOM   15304 O  O   . ARG D  1 356 ? -39.621 -9.162  57.564  1.00 51.86  ? 356  ARG D O   1 
ATOM   15305 C  CB  . ARG D  1 356 ? -40.367 -9.251  60.793  1.00 61.30  ? 356  ARG D CB  1 
ATOM   15306 C  CG  . ARG D  1 356 ? -39.195 -8.292  60.657  1.00 59.68  ? 356  ARG D CG  1 
ATOM   15307 C  CD  . ARG D  1 356 ? -39.087 -7.328  61.816  1.00 61.01  ? 356  ARG D CD  1 
ATOM   15308 N  NE  . ARG D  1 356 ? -38.330 -6.142  61.431  1.00 60.72  ? 356  ARG D NE  1 
ATOM   15309 C  CZ  . ARG D  1 356 ? -38.882 -4.987  61.079  1.00 59.85  ? 356  ARG D CZ  1 
ATOM   15310 N  NH1 . ARG D  1 356 ? -40.199 -4.858  61.081  1.00 59.95  ? 356  ARG D NH1 1 
ATOM   15311 N  NH2 . ARG D  1 356 ? -38.116 -3.961  60.738  1.00 58.84  ? 356  ARG D NH2 1 
ATOM   15312 N  N   . ALA D  1 357 ? -39.593 -11.202 58.505  1.00 57.53  ? 357  ALA D N   1 
ATOM   15313 C  CA  . ALA D  1 357 ? -38.611 -11.734 57.568  1.00 58.49  ? 357  ALA D CA  1 
ATOM   15314 C  C   . ALA D  1 357 ? -39.104 -11.597 56.131  1.00 57.04  ? 357  ALA D C   1 
ATOM   15315 O  O   . ALA D  1 357 ? -38.308 -11.394 55.198  1.00 56.27  ? 357  ALA D O   1 
ATOM   15316 C  CB  . ALA D  1 357 ? -38.299 -13.177 57.894  1.00 65.82  ? 357  ALA D CB  1 
ATOM   15317 N  N   . GLN D  1 358 ? -40.422 -11.686 55.968  1.00 58.39  ? 358  GLN D N   1 
ATOM   15318 C  CA  . GLN D  1 358 ? -41.049 -11.509 54.666  1.00 58.36  ? 358  GLN D CA  1 
ATOM   15319 C  C   . GLN D  1 358 ? -40.874 -10.085 54.169  1.00 56.22  ? 358  GLN D C   1 
ATOM   15320 O  O   . GLN D  1 358 ? -40.486 -9.872  53.021  1.00 54.20  ? 358  GLN D O   1 
ATOM   15321 C  CB  . GLN D  1 358 ? -42.530 -11.886 54.704  1.00 59.76  ? 358  GLN D CB  1 
ATOM   15322 C  CG  . GLN D  1 358 ? -42.779 -13.376 54.545  1.00 59.76  ? 358  GLN D CG  1 
ATOM   15323 C  CD  . GLN D  1 358 ? -44.230 -13.696 54.282  1.00 59.34  ? 358  GLN D CD  1 
ATOM   15324 O  OE1 . GLN D  1 358 ? -45.083 -13.578 55.166  1.00 60.85  ? 358  GLN D OE1 1 
ATOM   15325 N  NE2 . GLN D  1 358 ? -44.522 -14.102 53.059  1.00 57.89  ? 358  GLN D NE2 1 
ATOM   15326 N  N   . PHE D  1 359 ? -41.152 -9.116  55.034  1.00 62.60  ? 359  PHE D N   1 
ATOM   15327 C  CA  . PHE D  1 359 ? -40.937 -7.712  54.694  1.00 62.12  ? 359  PHE D CA  1 
ATOM   15328 C  C   . PHE D  1 359 ? -39.461 -7.401  54.384  1.00 61.34  ? 359  PHE D C   1 
ATOM   15329 O  O   . PHE D  1 359 ? -39.152 -6.687  53.419  1.00 61.16  ? 359  PHE D O   1 
ATOM   15330 C  CB  . PHE D  1 359 ? -41.473 -6.813  55.810  1.00 47.78  ? 359  PHE D CB  1 
ATOM   15331 C  CG  . PHE D  1 359 ? -41.082 -5.368  55.678  1.00 38.45  ? 359  PHE D CG  1 
ATOM   15332 C  CD1 . PHE D  1 359 ? -41.807 -4.512  54.872  1.00 55.14  ? 359  PHE D CD1 1 
ATOM   15333 C  CD2 . PHE D  1 359 ? -39.998 -4.865  56.376  1.00 38.34  ? 359  PHE D CD2 1 
ATOM   15334 C  CE1 . PHE D  1 359 ? -41.452 -3.184  54.754  1.00 36.33  ? 359  PHE D CE1 1 
ATOM   15335 C  CE2 . PHE D  1 359 ? -39.638 -3.542  56.263  1.00 37.24  ? 359  PHE D CE2 1 
ATOM   15336 C  CZ  . PHE D  1 359 ? -40.366 -2.701  55.453  1.00 36.25  ? 359  PHE D CZ  1 
ATOM   15337 N  N   . LEU D  1 360 ? -38.556 -7.949  55.192  1.00 55.72  ? 360  LEU D N   1 
ATOM   15338 C  CA  . LEU D  1 360 ? -37.120 -7.762  54.985  1.00 52.95  ? 360  LEU D CA  1 
ATOM   15339 C  C   . LEU D  1 360 ? -36.655 -8.260  53.632  1.00 52.91  ? 360  LEU D C   1 
ATOM   15340 O  O   . LEU D  1 360 ? -35.955 -7.540  52.917  1.00 54.65  ? 360  LEU D O   1 
ATOM   15341 C  CB  . LEU D  1 360 ? -36.322 -8.470  56.063  1.00 45.32  ? 360  LEU D CB  1 
ATOM   15342 C  CG  . LEU D  1 360 ? -36.667 -7.981  57.458  1.00 46.85  ? 360  LEU D CG  1 
ATOM   15343 C  CD1 . LEU D  1 360 ? -35.685 -8.556  58.480  1.00 50.38  ? 360  LEU D CD1 1 
ATOM   15344 C  CD2 . LEU D  1 360 ? -36.686 -6.462  57.479  1.00 45.27  ? 360  LEU D CD2 1 
ATOM   15345 N  N   . ALA D  1 361 ? -37.029 -9.493  53.290  1.00 42.86  ? 361  ALA D N   1 
ATOM   15346 C  CA  . ALA D  1 361 ? -36.695 -10.042 51.977  1.00 40.89  ? 361  ALA D CA  1 
ATOM   15347 C  C   . ALA D  1 361 ? -37.368 -9.252  50.846  1.00 41.93  ? 361  ALA D C   1 
ATOM   15348 O  O   . ALA D  1 361 ? -36.790 -9.037  49.764  1.00 34.67  ? 361  ALA D O   1 
ATOM   15349 C  CB  . ALA D  1 361 ? -37.081 -11.498 51.911  1.00 47.85  ? 361  ALA D CB  1 
ATOM   15350 N  N   . GLY D  1 362 ? -38.592 -8.813  51.112  1.00 36.00  ? 362  GLY D N   1 
ATOM   15351 C  CA  . GLY D  1 362 ? -39.357 -8.054  50.141  1.00 35.03  ? 362  GLY D CA  1 
ATOM   15352 C  C   . GLY D  1 362 ? -38.723 -6.721  49.793  1.00 33.32  ? 362  GLY D C   1 
ATOM   15353 O  O   . GLY D  1 362 ? -38.872 -6.227  48.669  1.00 32.14  ? 362  GLY D O   1 
ATOM   15354 N  N   . VAL D  1 363 ? -38.021 -6.131  50.758  1.00 34.26  ? 363  VAL D N   1 
ATOM   15355 C  CA  . VAL D  1 363 ? -37.292 -4.891  50.495  1.00 34.47  ? 363  VAL D CA  1 
ATOM   15356 C  C   . VAL D  1 363 ? -36.102 -5.108  49.547  1.00 34.91  ? 363  VAL D C   1 
ATOM   15357 O  O   . VAL D  1 363 ? -35.828 -4.269  48.691  1.00 30.21  ? 363  VAL D O   1 
ATOM   15358 C  CB  . VAL D  1 363 ? -36.867 -4.190  51.794  1.00 32.75  ? 363  VAL D CB  1 
ATOM   15359 C  CG1 . VAL D  1 363 ? -35.916 -3.033  51.502  1.00 31.63  ? 363  VAL D CG1 1 
ATOM   15360 C  CG2 . VAL D  1 363 ? -38.106 -3.707  52.537  1.00 33.39  ? 363  VAL D CG2 1 
ATOM   15361 N  N   . ARG D  1 364 ? -35.416 -6.240  49.671  1.00 42.47  ? 364  ARG D N   1 
ATOM   15362 C  CA  . ARG D  1 364 ? -34.380 -6.581  48.699  1.00 44.71  ? 364  ARG D CA  1 
ATOM   15363 C  C   . ARG D  1 364 ? -35.004 -6.835  47.330  1.00 46.54  ? 364  ARG D C   1 
ATOM   15364 O  O   . ARG D  1 364 ? -34.414 -6.503  46.296  1.00 47.69  ? 364  ARG D O   1 
ATOM   15365 C  CB  . ARG D  1 364 ? -33.568 -7.804  49.137  1.00 44.36  ? 364  ARG D CB  1 
ATOM   15366 C  CG  . ARG D  1 364 ? -32.932 -7.693  50.524  1.00 47.86  ? 364  ARG D CG  1 
ATOM   15367 C  CD  . ARG D  1 364 ? -32.269 -6.348  50.761  1.00 48.13  ? 364  ARG D CD  1 
ATOM   15368 N  NE  . ARG D  1 364 ? -31.005 -6.175  50.047  1.00 49.97  ? 364  ARG D NE  1 
ATOM   15369 C  CZ  . ARG D  1 364 ? -29.807 -6.421  50.577  1.00 54.69  ? 364  ARG D CZ  1 
ATOM   15370 N  NH1 . ARG D  1 364 ? -29.712 -6.868  51.829  1.00 57.86  ? 364  ARG D NH1 1 
ATOM   15371 N  NH2 . ARG D  1 364 ? -28.700 -6.222  49.862  1.00 54.13  ? 364  ARG D NH2 1 
ATOM   15372 N  N   . ILE D  1 365 ? -36.203 -7.419  47.325  1.00 46.73  ? 365  ILE D N   1 
ATOM   15373 C  CA  . ILE D  1 365 ? -36.879 -7.736  46.058  1.00 45.59  ? 365  ILE D CA  1 
ATOM   15374 C  C   . ILE D  1 365 ? -37.389 -6.494  45.307  1.00 41.90  ? 365  ILE D C   1 
ATOM   15375 O  O   . ILE D  1 365 ? -37.360 -6.453  44.078  1.00 40.27  ? 365  ILE D O   1 
ATOM   15376 C  CB  . ILE D  1 365 ? -38.005 -8.801  46.240  1.00 40.71  ? 365  ILE D CB  1 
ATOM   15377 C  CG1 . ILE D  1 365 ? -37.436 -10.221 46.143  1.00 44.96  ? 365  ILE D CG1 1 
ATOM   15378 C  CG2 . ILE D  1 365 ? -39.048 -8.691  45.158  1.00 37.43  ? 365  ILE D CG2 1 
ATOM   15379 C  CD1 . ILE D  1 365 ? -36.304 -10.548 47.126  1.00 46.64  ? 365  ILE D CD1 1 
ATOM   15380 N  N   . GLY D  1 366 ? -37.830 -5.479  46.047  1.00 39.47  ? 366  GLY D N   1 
ATOM   15381 C  CA  . GLY D  1 366 ? -38.380 -4.273  45.439  1.00 41.22  ? 366  GLY D CA  1 
ATOM   15382 C  C   . GLY D  1 366 ? -37.395 -3.134  45.214  1.00 43.03  ? 366  GLY D C   1 
ATOM   15383 O  O   . GLY D  1 366 ? -37.633 -2.238  44.389  1.00 45.00  ? 366  GLY D O   1 
ATOM   15384 N  N   . VAL D  1 367 ? -36.292 -3.158  45.960  1.00 46.72  ? 367  VAL D N   1 
ATOM   15385 C  CA  . VAL D  1 367 ? -35.195 -2.225  45.751  1.00 43.29  ? 367  VAL D CA  1 
ATOM   15386 C  C   . VAL D  1 367 ? -33.946 -3.036  45.444  1.00 49.28  ? 367  VAL D C   1 
ATOM   15387 O  O   . VAL D  1 367 ? -33.102 -3.224  46.322  1.00 52.82  ? 367  VAL D O   1 
ATOM   15388 C  CB  . VAL D  1 367 ? -34.918 -1.372  46.997  1.00 30.30  ? 367  VAL D CB  1 
ATOM   15389 C  CG1 . VAL D  1 367 ? -34.047 -0.211  46.640  1.00 26.48  ? 367  VAL D CG1 1 
ATOM   15390 C  CG2 . VAL D  1 367 ? -36.206 -0.879  47.601  1.00 29.26  ? 367  VAL D CG2 1 
ATOM   15391 N  N   . PRO D  1 368 ? -33.831 -3.541  44.201  1.00 37.75  ? 368  PRO D N   1 
ATOM   15392 C  CA  . PRO D  1 368 ? -32.689 -4.348  43.750  1.00 38.62  ? 368  PRO D CA  1 
ATOM   15393 C  C   . PRO D  1 368 ? -31.439 -3.476  43.716  1.00 38.18  ? 368  PRO D C   1 
ATOM   15394 O  O   . PRO D  1 368 ? -30.315 -3.939  43.988  1.00 31.88  ? 368  PRO D O   1 
ATOM   15395 C  CB  . PRO D  1 368 ? -33.079 -4.732  42.322  1.00 48.48  ? 368  PRO D CB  1 
ATOM   15396 C  CG  . PRO D  1 368 ? -34.543 -4.436  42.207  1.00 47.80  ? 368  PRO D CG  1 
ATOM   15397 C  CD  . PRO D  1 368 ? -34.776 -3.283  43.105  1.00 46.39  ? 368  PRO D CD  1 
ATOM   15398 N  N   . GLN D  1 369 ? -31.691 -2.200  43.408  1.00 50.96  ? 369  GLN D N   1 
ATOM   15399 C  CA  . GLN D  1 369 ? -30.720 -1.113  43.403  1.00 52.58  ? 369  GLN D CA  1 
ATOM   15400 C  C   . GLN D  1 369 ? -29.848 -1.180  44.657  1.00 49.76  ? 369  GLN D C   1 
ATOM   15401 O  O   . GLN D  1 369 ? -28.641 -0.948  44.617  1.00 49.99  ? 369  GLN D O   1 
ATOM   15402 C  CB  . GLN D  1 369 ? -31.499 0.224   43.409  1.00 60.74  ? 369  GLN D CB  1 
ATOM   15403 C  CG  . GLN D  1 369 ? -31.847 0.855   42.047  1.00 68.53  ? 369  GLN D CG  1 
ATOM   15404 C  CD  . GLN D  1 369 ? -32.698 -0.037  41.133  1.00 76.16  ? 369  GLN D CD  1 
ATOM   15405 O  OE1 . GLN D  1 369 ? -33.131 -1.118  41.533  1.00 81.34  ? 369  GLN D OE1 1 
ATOM   15406 N  NE2 . GLN D  1 369 ? -32.939 0.423   39.892  1.00 73.33  ? 369  GLN D NE2 1 
ATOM   15407 N  N   . ALA D  1 370 ? -30.484 -1.528  45.769  1.00 43.81  ? 370  ALA D N   1 
ATOM   15408 C  CA  . ALA D  1 370 ? -29.920 -1.361  47.095  1.00 38.90  ? 370  ALA D CA  1 
ATOM   15409 C  C   . ALA D  1 370 ? -28.770 -2.293  47.420  1.00 41.23  ? 370  ALA D C   1 
ATOM   15410 O  O   . ALA D  1 370 ? -28.818 -3.484  47.125  1.00 41.82  ? 370  ALA D O   1 
ATOM   15411 C  CB  . ALA D  1 370 ? -31.014 -1.518  48.130  1.00 28.09  ? 370  ALA D CB  1 
ATOM   15412 N  N   . SER D  1 371 ? -27.746 -1.728  48.054  1.00 39.69  ? 371  SER D N   1 
ATOM   15413 C  CA  . SER D  1 371 ? -26.713 -2.513  48.710  1.00 43.99  ? 371  SER D CA  1 
ATOM   15414 C  C   . SER D  1 371 ? -27.290 -3.035  50.017  1.00 46.89  ? 371  SER D C   1 
ATOM   15415 O  O   . SER D  1 371 ? -28.470 -2.857  50.283  1.00 45.37  ? 371  SER D O   1 
ATOM   15416 C  CB  . SER D  1 371 ? -25.461 -1.660  48.981  1.00 52.92  ? 371  SER D CB  1 
ATOM   15417 O  OG  . SER D  1 371 ? -25.682 -0.663  49.965  1.00 52.58  ? 371  SER D OG  1 
ATOM   15418 N  N   . ASP D  1 372 ? -26.465 -3.683  50.832  1.00 61.98  ? 372  ASP D N   1 
ATOM   15419 C  CA  . ASP D  1 372 ? -26.904 -4.119  52.155  1.00 64.01  ? 372  ASP D CA  1 
ATOM   15420 C  C   . ASP D  1 372 ? -27.349 -2.901  52.975  1.00 60.69  ? 372  ASP D C   1 
ATOM   15421 O  O   . ASP D  1 372 ? -28.493 -2.833  53.445  1.00 60.99  ? 372  ASP D O   1 
ATOM   15422 C  CB  . ASP D  1 372 ? -25.775 -4.871  52.887  1.00 63.12  ? 372  ASP D CB  1 
ATOM   15423 C  CG  . ASP D  1 372 ? -25.458 -6.242  52.269  1.00 61.68  ? 372  ASP D CG  1 
ATOM   15424 O  OD1 . ASP D  1 372 ? -25.912 -6.507  51.128  1.00 62.46  ? 372  ASP D OD1 1 
ATOM   15425 O  OD2 . ASP D  1 372 ? -24.740 -7.044  52.925  1.00 56.86  ? 372  ASP D OD2 1 
ATOM   15426 N  N   . LEU D  1 373 ? -26.444 -1.930  53.114  1.00 54.33  ? 373  LEU D N   1 
ATOM   15427 C  CA  . LEU D  1 373 ? -26.662 -0.771  53.988  1.00 50.77  ? 373  LEU D CA  1 
ATOM   15428 C  C   . LEU D  1 373 ? -27.838 0.100   53.550  1.00 47.00  ? 373  LEU D C   1 
ATOM   15429 O  O   . LEU D  1 373 ? -28.562 0.646   54.383  1.00 47.63  ? 373  LEU D O   1 
ATOM   15430 C  CB  . LEU D  1 373 ? -25.384 0.078   54.115  1.00 32.58  ? 373  LEU D CB  1 
ATOM   15431 C  CG  . LEU D  1 373 ? -25.362 1.271   55.089  1.00 32.82  ? 373  LEU D CG  1 
ATOM   15432 C  CD1 . LEU D  1 373 ? -25.561 0.850   56.555  1.00 34.16  ? 373  LEU D CD1 1 
ATOM   15433 C  CD2 . LEU D  1 373 ? -24.072 2.065   54.924  1.00 32.74  ? 373  LEU D CD2 1 
ATOM   15434 N  N   . ALA D  1 374 ? -28.027 0.232   52.245  1.00 42.51  ? 374  ALA D N   1 
ATOM   15435 C  CA  . ALA D  1 374 ? -29.119 1.046   51.742  1.00 39.47  ? 374  ALA D CA  1 
ATOM   15436 C  C   . ALA D  1 374 ? -30.444 0.394   52.102  1.00 38.55  ? 374  ALA D C   1 
ATOM   15437 O  O   . ALA D  1 374 ? -31.406 1.076   52.471  1.00 37.08  ? 374  ALA D O   1 
ATOM   15438 C  CB  . ALA D  1 374 ? -29.007 1.224   50.253  1.00 35.51  ? 374  ALA D CB  1 
ATOM   15439 N  N   . ALA D  1 375 ? -30.481 -0.932  52.002  1.00 32.55  ? 375  ALA D N   1 
ATOM   15440 C  CA  . ALA D  1 375 ? -31.665 -1.699  52.373  1.00 33.33  ? 375  ALA D CA  1 
ATOM   15441 C  C   . ALA D  1 375 ? -31.940 -1.585  53.866  1.00 36.56  ? 375  ALA D C   1 
ATOM   15442 O  O   . ALA D  1 375 ? -33.085 -1.496  54.296  1.00 36.00  ? 375  ALA D O   1 
ATOM   15443 C  CB  . ALA D  1 375 ? -31.481 -3.137  51.993  1.00 35.10  ? 375  ALA D CB  1 
ATOM   15444 N  N   . GLU D  1 376 ? -30.881 -1.594  54.659  1.00 39.62  ? 376  GLU D N   1 
ATOM   15445 C  CA  . GLU D  1 376 ? -31.042 -1.388  56.082  1.00 45.30  ? 376  GLU D CA  1 
ATOM   15446 C  C   . GLU D  1 376 ? -31.606 0.003   56.364  1.00 40.99  ? 376  GLU D C   1 
ATOM   15447 O  O   . GLU D  1 376 ? -32.367 0.199   57.307  1.00 40.24  ? 376  GLU D O   1 
ATOM   15448 C  CB  . GLU D  1 376 ? -29.708 -1.571  56.786  1.00 78.62  ? 376  GLU D CB  1 
ATOM   15449 C  CG  . GLU D  1 376 ? -29.826 -1.641  58.281  1.00 90.54  ? 376  GLU D CG  1 
ATOM   15450 C  CD  . GLU D  1 376 ? -28.948 -2.720  58.851  1.00 100.16 ? 376  GLU D CD  1 
ATOM   15451 O  OE1 . GLU D  1 376 ? -28.367 -3.489  58.043  1.00 99.92  ? 376  GLU D OE1 1 
ATOM   15452 O  OE2 . GLU D  1 376 ? -28.840 -2.793  60.097  1.00 105.47 ? 376  GLU D OE2 1 
ATOM   15453 N  N   . ALA D  1 377 ? -31.225 0.976   55.546  1.00 45.99  ? 377  ALA D N   1 
ATOM   15454 C  CA  . ALA D  1 377 ? -31.757 2.319   55.701  1.00 43.28  ? 377  ALA D CA  1 
ATOM   15455 C  C   . ALA D  1 377 ? -33.248 2.323   55.361  1.00 43.72  ? 377  ALA D C   1 
ATOM   15456 O  O   . ALA D  1 377 ? -34.061 2.923   56.065  1.00 44.79  ? 377  ALA D O   1 
ATOM   15457 C  CB  . ALA D  1 377 ? -30.996 3.298   54.827  1.00 31.09  ? 377  ALA D CB  1 
ATOM   15458 N  N   . VAL D  1 378 ? -33.605 1.637   54.282  1.00 38.97  ? 378  VAL D N   1 
ATOM   15459 C  CA  . VAL D  1 378 ? -34.994 1.587   53.847  1.00 37.30  ? 378  VAL D CA  1 
ATOM   15460 C  C   . VAL D  1 378 ? -35.863 0.908   54.901  1.00 39.04  ? 378  VAL D C   1 
ATOM   15461 O  O   . VAL D  1 378 ? -36.996 1.333   55.168  1.00 40.60  ? 378  VAL D O   1 
ATOM   15462 C  CB  . VAL D  1 378 ? -35.130 0.861   52.504  1.00 30.38  ? 378  VAL D CB  1 
ATOM   15463 C  CG1 . VAL D  1 378 ? -36.595 0.735   52.121  1.00 30.40  ? 378  VAL D CG1 1 
ATOM   15464 C  CG2 . VAL D  1 378 ? -34.369 1.608   51.445  1.00 29.15  ? 378  VAL D CG2 1 
ATOM   15465 N  N   . VAL D  1 379 ? -35.321 -0.141  55.510  1.00 33.44  ? 379  VAL D N   1 
ATOM   15466 C  CA  . VAL D  1 379 ? -36.047 -0.858  56.536  1.00 34.89  ? 379  VAL D CA  1 
ATOM   15467 C  C   . VAL D  1 379 ? -36.195 0.051   57.731  1.00 35.65  ? 379  VAL D C   1 
ATOM   15468 O  O   . VAL D  1 379 ? -37.296 0.196   58.253  1.00 43.74  ? 379  VAL D O   1 
ATOM   15469 C  CB  . VAL D  1 379 ? -35.374 -2.182  56.919  1.00 35.81  ? 379  VAL D CB  1 
ATOM   15470 C  CG1 . VAL D  1 379 ? -35.822 -2.639  58.292  1.00 37.52  ? 379  VAL D CG1 1 
ATOM   15471 C  CG2 . VAL D  1 379 ? -35.712 -3.232  55.903  1.00 35.53  ? 379  VAL D CG2 1 
ATOM   15472 N  N   . LEU D  1 380 ? -35.102 0.693   58.135  1.00 38.94  ? 380  LEU D N   1 
ATOM   15473 C  CA  . LEU D  1 380 ? -35.141 1.604   59.273  1.00 36.26  ? 380  LEU D CA  1 
ATOM   15474 C  C   . LEU D  1 380 ? -36.239 2.626   59.067  1.00 35.94  ? 380  LEU D C   1 
ATOM   15475 O  O   . LEU D  1 380 ? -37.011 2.919   59.980  1.00 38.69  ? 380  LEU D O   1 
ATOM   15476 C  CB  . LEU D  1 380 ? -33.812 2.327   59.465  1.00 35.92  ? 380  LEU D CB  1 
ATOM   15477 C  CG  . LEU D  1 380 ? -33.982 3.623   60.272  1.00 37.08  ? 380  LEU D CG  1 
ATOM   15478 C  CD1 . LEU D  1 380 ? -34.310 3.337   61.724  1.00 38.00  ? 380  LEU D CD1 1 
ATOM   15479 C  CD2 . LEU D  1 380 ? -32.767 4.511   60.185  1.00 38.07  ? 380  LEU D CD2 1 
ATOM   15480 N  N   . HIS D  1 381 ? -36.329 3.141   57.849  1.00 34.58  ? 381  HIS D N   1 
ATOM   15481 C  CA  . HIS D  1 381 ? -37.307 4.172   57.551  1.00 34.57  ? 381  HIS D CA  1 
ATOM   15482 C  C   . HIS D  1 381 ? -38.736 3.662   57.595  1.00 34.95  ? 381  HIS D C   1 
ATOM   15483 O  O   . HIS D  1 381 ? -39.581 4.260   58.243  1.00 35.77  ? 381  HIS D O   1 
ATOM   15484 C  CB  . HIS D  1 381 ? -37.029 4.800   56.196  1.00 44.59  ? 381  HIS D CB  1 
ATOM   15485 C  CG  . HIS D  1 381 ? -37.567 6.189   56.058  1.00 45.03  ? 381  HIS D CG  1 
ATOM   15486 N  ND1 . HIS D  1 381 ? -36.843 7.306   56.426  1.00 46.07  ? 381  HIS D ND1 1 
ATOM   15487 C  CD2 . HIS D  1 381 ? -38.757 6.641   55.597  1.00 43.25  ? 381  HIS D CD2 1 
ATOM   15488 C  CE1 . HIS D  1 381 ? -37.563 8.388   56.186  1.00 45.81  ? 381  HIS D CE1 1 
ATOM   15489 N  NE2 . HIS D  1 381 ? -38.727 8.012   55.682  1.00 44.54  ? 381  HIS D NE2 1 
ATOM   15490 N  N   . TYR D  1 382 ? -39.005 2.553   56.921  1.00 34.74  ? 382  TYR D N   1 
ATOM   15491 C  CA  . TYR D  1 382 ? -40.384 2.102   56.768  1.00 35.31  ? 382  TYR D CA  1 
ATOM   15492 C  C   . TYR D  1 382 ? -40.970 1.240   57.894  1.00 49.94  ? 382  TYR D C   1 
ATOM   15493 O  O   . TYR D  1 382 ? -42.189 1.029   57.947  1.00 37.79  ? 382  TYR D O   1 
ATOM   15494 C  CB  . TYR D  1 382 ? -40.558 1.416   55.428  1.00 34.35  ? 382  TYR D CB  1 
ATOM   15495 C  CG  . TYR D  1 382 ? -40.662 2.385   54.289  1.00 32.99  ? 382  TYR D CG  1 
ATOM   15496 C  CD1 . TYR D  1 382 ? -39.530 2.827   53.628  1.00 31.80  ? 382  TYR D CD1 1 
ATOM   15497 C  CD2 . TYR D  1 382 ? -41.895 2.859   53.873  1.00 33.02  ? 382  TYR D CD2 1 
ATOM   15498 C  CE1 . TYR D  1 382 ? -39.624 3.717   52.572  1.00 31.21  ? 382  TYR D CE1 1 
ATOM   15499 C  CE2 . TYR D  1 382 ? -42.002 3.744   52.821  1.00 31.88  ? 382  TYR D CE2 1 
ATOM   15500 C  CZ  . TYR D  1 382 ? -40.865 4.173   52.175  1.00 30.70  ? 382  TYR D CZ  1 
ATOM   15501 O  OH  . TYR D  1 382 ? -40.964 5.062   51.131  1.00 29.68  ? 382  TYR D OH  1 
ATOM   15502 N  N   . THR D  1 383 ? -40.116 0.758   58.792  1.00 37.77  ? 383  THR D N   1 
ATOM   15503 C  CA  . THR D  1 383 ? -40.571 0.008   59.964  1.00 39.56  ? 383  THR D CA  1 
ATOM   15504 C  C   . THR D  1 383 ? -41.191 0.917   61.023  1.00 40.64  ? 383  THR D C   1 
ATOM   15505 O  O   . THR D  1 383 ? -40.640 1.964   61.335  1.00 46.65  ? 383  THR D O   1 
ATOM   15506 C  CB  . THR D  1 383 ? -39.401 -0.761  60.608  1.00 43.55  ? 383  THR D CB  1 
ATOM   15507 O  OG1 . THR D  1 383 ? -39.032 -1.851  59.763  1.00 44.36  ? 383  THR D OG1 1 
ATOM   15508 C  CG2 . THR D  1 383 ? -39.787 -1.317  61.954  1.00 42.08  ? 383  THR D CG2 1 
ATOM   15509 N  N   . ASP D  1 384 ? -42.336 0.531   61.574  1.00 42.05  ? 384  ASP D N   1 
ATOM   15510 C  CA  . ASP D  1 384 ? -42.811 1.184   62.786  1.00 43.46  ? 384  ASP D CA  1 
ATOM   15511 C  C   . ASP D  1 384 ? -42.177 0.415   63.928  1.00 44.79  ? 384  ASP D C   1 
ATOM   15512 O  O   . ASP D  1 384 ? -42.460 -0.765  64.138  1.00 45.78  ? 384  ASP D O   1 
ATOM   15513 C  CB  . ASP D  1 384 ? -44.342 1.167   62.886  1.00 56.46  ? 384  ASP D CB  1 
ATOM   15514 C  CG  . ASP D  1 384 ? -44.854 1.417   64.307  1.00 60.90  ? 384  ASP D CG  1 
ATOM   15515 O  OD1 . ASP D  1 384 ? -44.185 2.124   65.099  1.00 61.52  ? 384  ASP D OD1 1 
ATOM   15516 O  OD2 . ASP D  1 384 ? -45.945 0.897   64.631  1.00 63.87  ? 384  ASP D OD2 1 
ATOM   15517 N  N   . TRP D  1 385 ? -41.315 1.103   64.666  1.00 48.45  ? 385  TRP D N   1 
ATOM   15518 C  CA  . TRP D  1 385 ? -40.448 0.456   65.631  1.00 47.31  ? 385  TRP D CA  1 
ATOM   15519 C  C   . TRP D  1 385 ? -41.148 0.225   66.937  1.00 49.32  ? 385  TRP D C   1 
ATOM   15520 O  O   . TRP D  1 385 ? -40.676 -0.538  67.783  1.00 50.24  ? 385  TRP D O   1 
ATOM   15521 C  CB  . TRP D  1 385 ? -39.205 1.290   65.831  1.00 45.19  ? 385  TRP D CB  1 
ATOM   15522 C  CG  . TRP D  1 385 ? -38.336 1.169   64.683  1.00 43.45  ? 385  TRP D CG  1 
ATOM   15523 C  CD1 . TRP D  1 385 ? -38.206 2.048   63.665  1.00 41.83  ? 385  TRP D CD1 1 
ATOM   15524 C  CD2 . TRP D  1 385 ? -37.486 0.066   64.381  1.00 43.26  ? 385  TRP D CD2 1 
ATOM   15525 N  NE1 . TRP D  1 385 ? -37.304 1.574   62.747  1.00 40.62  ? 385  TRP D NE1 1 
ATOM   15526 C  CE2 . TRP D  1 385 ? -36.846 0.354   63.170  1.00 41.48  ? 385  TRP D CE2 1 
ATOM   15527 C  CE3 . TRP D  1 385 ? -37.194 -1.135  65.028  1.00 44.54  ? 385  TRP D CE3 1 
ATOM   15528 C  CZ2 . TRP D  1 385 ? -35.929 -0.513  62.587  1.00 40.96  ? 385  TRP D CZ2 1 
ATOM   15529 C  CZ3 . TRP D  1 385 ? -36.286 -1.989  64.457  1.00 44.03  ? 385  TRP D CZ3 1 
ATOM   15530 C  CH2 . TRP D  1 385 ? -35.663 -1.678  63.247  1.00 42.52  ? 385  TRP D CH2 1 
ATOM   15531 N  N   . LEU D  1 386 ? -42.284 0.885   67.101  1.00 55.58  ? 386  LEU D N   1 
ATOM   15532 C  CA  . LEU D  1 386 ? -43.125 0.596   68.238  1.00 62.63  ? 386  LEU D CA  1 
ATOM   15533 C  C   . LEU D  1 386 ? -43.779 -0.787  68.047  1.00 66.30  ? 386  LEU D C   1 
ATOM   15534 O  O   . LEU D  1 386 ? -44.022 -1.505  69.029  1.00 68.90  ? 386  LEU D O   1 
ATOM   15535 C  CB  . LEU D  1 386 ? -44.154 1.709   68.434  1.00 68.06  ? 386  LEU D CB  1 
ATOM   15536 C  CG  . LEU D  1 386 ? -44.584 1.972   69.883  1.00 74.65  ? 386  LEU D CG  1 
ATOM   15537 C  CD1 . LEU D  1 386 ? -46.044 1.588   70.107  1.00 78.27  ? 386  LEU D CD1 1 
ATOM   15538 C  CD2 . LEU D  1 386 ? -43.687 1.239   70.874  1.00 75.99  ? 386  LEU D CD2 1 
ATOM   15539 N  N   . HIS D  1 387 ? -44.025 -1.158  66.781  1.00 58.54  ? 387  HIS D N   1 
ATOM   15540 C  CA  . HIS D  1 387 ? -44.627 -2.449  66.409  1.00 55.71  ? 387  HIS D CA  1 
ATOM   15541 C  C   . HIS D  1 387 ? -43.912 -3.080  65.227  1.00 50.55  ? 387  HIS D C   1 
ATOM   15542 O  O   . HIS D  1 387 ? -44.446 -3.080  64.125  1.00 51.45  ? 387  HIS D O   1 
ATOM   15543 C  CB  . HIS D  1 387 ? -46.094 -2.265  66.014  1.00 63.84  ? 387  HIS D CB  1 
ATOM   15544 C  CG  . HIS D  1 387 ? -46.928 -1.611  67.066  1.00 71.03  ? 387  HIS D CG  1 
ATOM   15545 N  ND1 . HIS D  1 387 ? -47.109 -2.158  68.320  1.00 76.71  ? 387  HIS D ND1 1 
ATOM   15546 C  CD2 . HIS D  1 387 ? -47.636 -0.457  67.053  1.00 73.09  ? 387  HIS D CD2 1 
ATOM   15547 C  CE1 . HIS D  1 387 ? -47.886 -1.366  69.036  1.00 79.08  ? 387  HIS D CE1 1 
ATOM   15548 N  NE2 . HIS D  1 387 ? -48.219 -0.326  68.290  1.00 78.15  ? 387  HIS D NE2 1 
ATOM   15549 N  N   . PRO D  1 388 ? -42.717 -3.638  65.446  1.00 49.23  ? 388  PRO D N   1 
ATOM   15550 C  CA  . PRO D  1 388 ? -41.883 -4.118  64.337  1.00 47.65  ? 388  PRO D CA  1 
ATOM   15551 C  C   . PRO D  1 388 ? -42.499 -5.323  63.640  1.00 49.71  ? 388  PRO D C   1 
ATOM   15552 O  O   . PRO D  1 388 ? -42.234 -5.553  62.457  1.00 46.54  ? 388  PRO D O   1 
ATOM   15553 C  CB  . PRO D  1 388 ? -40.588 -4.566  65.029  1.00 54.10  ? 388  PRO D CB  1 
ATOM   15554 C  CG  . PRO D  1 388 ? -40.698 -4.109  66.446  1.00 57.26  ? 388  PRO D CG  1 
ATOM   15555 C  CD  . PRO D  1 388 ? -42.156 -4.017  66.746  1.00 56.78  ? 388  PRO D CD  1 
ATOM   15556 N  N   . GLU D  1 389 ? -43.302 -6.085  64.385  1.00 61.78  ? 389  GLU D N   1 
ATOM   15557 C  CA  . GLU D  1 389 ? -43.840 -7.364  63.916  1.00 61.79  ? 389  GLU D CA  1 
ATOM   15558 C  C   . GLU D  1 389 ? -45.197 -7.282  63.232  1.00 55.09  ? 389  GLU D C   1 
ATOM   15559 O  O   . GLU D  1 389 ? -45.624 -8.264  62.639  1.00 52.93  ? 389  GLU D O   1 
ATOM   15560 C  CB  . GLU D  1 389 ? -43.948 -8.371  65.078  1.00 77.51  ? 389  GLU D CB  1 
ATOM   15561 C  CG  . GLU D  1 389 ? -42.631 -8.721  65.761  1.00 82.97  ? 389  GLU D CG  1 
ATOM   15562 C  CD  . GLU D  1 389 ? -41.582 -9.211  64.781  1.00 84.79  ? 389  GLU D CD  1 
ATOM   15563 O  OE1 . GLU D  1 389 ? -41.950 -9.919  63.819  1.00 84.61  ? 389  GLU D OE1 1 
ATOM   15564 O  OE2 . GLU D  1 389 ? -40.391 -8.878  64.965  1.00 85.50  ? 389  GLU D OE2 1 
ATOM   15565 N  N   . ASP D  1 390 ? -45.872 -6.136  63.309  1.00 52.00  ? 390  ASP D N   1 
ATOM   15566 C  CA  . ASP D  1 390 ? -47.258 -6.066  62.848  1.00 56.81  ? 390  ASP D CA  1 
ATOM   15567 C  C   . ASP D  1 390 ? -47.356 -6.445  61.386  1.00 58.32  ? 390  ASP D C   1 
ATOM   15568 O  O   . ASP D  1 390 ? -46.801 -5.762  60.528  1.00 58.38  ? 390  ASP D O   1 
ATOM   15569 C  CB  . ASP D  1 390 ? -47.858 -4.677  63.059  1.00 68.44  ? 390  ASP D CB  1 
ATOM   15570 C  CG  . ASP D  1 390 ? -49.307 -4.579  62.567  1.00 73.02  ? 390  ASP D CG  1 
ATOM   15571 O  OD1 . ASP D  1 390 ? -49.965 -5.628  62.387  1.00 74.46  ? 390  ASP D OD1 1 
ATOM   15572 O  OD2 . ASP D  1 390 ? -49.797 -3.444  62.371  1.00 74.65  ? 390  ASP D OD2 1 
ATOM   15573 N  N   . PRO D  1 391 ? -48.069 -7.543  61.100  1.00 74.57  ? 391  PRO D N   1 
ATOM   15574 C  CA  . PRO D  1 391 ? -48.175 -8.033  59.729  1.00 73.74  ? 391  PRO D CA  1 
ATOM   15575 C  C   . PRO D  1 391 ? -48.867 -7.015  58.853  1.00 73.98  ? 391  PRO D C   1 
ATOM   15576 O  O   . PRO D  1 391 ? -48.395 -6.767  57.749  1.00 76.58  ? 391  PRO D O   1 
ATOM   15577 C  CB  . PRO D  1 391 ? -49.042 -9.277  59.879  1.00 55.43  ? 391  PRO D CB  1 
ATOM   15578 C  CG  . PRO D  1 391 ? -48.817 -9.717  61.288  1.00 53.06  ? 391  PRO D CG  1 
ATOM   15579 C  CD  . PRO D  1 391 ? -48.721 -8.451  62.056  1.00 56.56  ? 391  PRO D CD  1 
ATOM   15580 N  N   . THR D  1 392 ? -49.944 -6.418  59.350  1.00 49.22  ? 392  THR D N   1 
ATOM   15581 C  CA  . THR D  1 392 ? -50.703 -5.433  58.583  1.00 48.13  ? 392  THR D CA  1 
ATOM   15582 C  C   . THR D  1 392 ? -49.849 -4.232  58.185  1.00 46.13  ? 392  THR D C   1 
ATOM   15583 O  O   . THR D  1 392 ? -49.771 -3.865  57.001  1.00 44.52  ? 392  THR D O   1 
ATOM   15584 C  CB  . THR D  1 392 ? -51.905 -4.943  59.387  1.00 66.23  ? 392  THR D CB  1 
ATOM   15585 O  OG1 . THR D  1 392 ? -52.523 -6.067  60.022  1.00 71.62  ? 392  THR D OG1 1 
ATOM   15586 C  CG2 . THR D  1 392 ? -52.916 -4.231  58.487  1.00 64.94  ? 392  THR D CG2 1 
ATOM   15587 N  N   . HIS D  1 393 ? -49.206 -3.623  59.177  1.00 48.86  ? 393  HIS D N   1 
ATOM   15588 C  CA  . HIS D  1 393 ? -48.298 -2.514  58.913  1.00 49.87  ? 393  HIS D CA  1 
ATOM   15589 C  C   . HIS D  1 393 ? -47.186 -2.919  57.939  1.00 45.62  ? 393  HIS D C   1 
ATOM   15590 O  O   . HIS D  1 393 ? -46.880 -2.187  57.011  1.00 43.05  ? 393  HIS D O   1 
ATOM   15591 C  CB  . HIS D  1 393 ? -47.690 -1.948  60.205  1.00 64.28  ? 393  HIS D CB  1 
ATOM   15592 C  CG  . HIS D  1 393 ? -46.682 -0.872  59.957  1.00 67.66  ? 393  HIS D CG  1 
ATOM   15593 N  ND1 . HIS D  1 393 ? -47.029 0.372   59.474  1.00 69.26  ? 393  HIS D ND1 1 
ATOM   15594 C  CD2 . HIS D  1 393 ? -45.334 -0.869  60.071  1.00 69.26  ? 393  HIS D CD2 1 
ATOM   15595 C  CE1 . HIS D  1 393 ? -45.940 1.103   59.318  1.00 69.47  ? 393  HIS D CE1 1 
ATOM   15596 N  NE2 . HIS D  1 393 ? -44.897 0.373   59.672  1.00 70.39  ? 393  HIS D NE2 1 
ATOM   15597 N  N   . LEU D  1 394 ? -46.588 -4.084  58.153  1.00 52.27  ? 394  LEU D N   1 
ATOM   15598 C  CA  . LEU D  1 394 ? -45.552 -4.574  57.258  1.00 48.59  ? 394  LEU D CA  1 
ATOM   15599 C  C   . LEU D  1 394 ? -46.033 -4.622  55.814  1.00 47.73  ? 394  LEU D C   1 
ATOM   15600 O  O   . LEU D  1 394 ? -45.363 -4.142  54.906  1.00 47.14  ? 394  LEU D O   1 
ATOM   15601 C  CB  . LEU D  1 394 ? -45.095 -5.955  57.701  1.00 43.14  ? 394  LEU D CB  1 
ATOM   15602 C  CG  . LEU D  1 394 ? -44.181 -5.882  58.910  1.00 43.83  ? 394  LEU D CG  1 
ATOM   15603 C  CD1 . LEU D  1 394 ? -43.817 -7.267  59.370  1.00 45.16  ? 394  LEU D CD1 1 
ATOM   15604 C  CD2 . LEU D  1 394 ? -42.954 -5.088  58.544  1.00 42.16  ? 394  LEU D CD2 1 
ATOM   15605 N  N   . ARG D  1 395 ? -47.209 -5.197  55.617  1.00 43.35  ? 395  ARG D N   1 
ATOM   15606 C  CA  . ARG D  1 395 ? -47.800 -5.331  54.297  1.00 43.55  ? 395  ARG D CA  1 
ATOM   15607 C  C   . ARG D  1 395 ? -47.976 -3.958  53.641  1.00 39.65  ? 395  ARG D C   1 
ATOM   15608 O  O   . ARG D  1 395 ? -47.412 -3.677  52.566  1.00 38.03  ? 395  ARG D O   1 
ATOM   15609 C  CB  . ARG D  1 395 ? -49.137 -6.054  54.439  1.00 42.70  ? 395  ARG D CB  1 
ATOM   15610 C  CG  . ARG D  1 395 ? -49.834 -6.333  53.159  1.00 42.17  ? 395  ARG D CG  1 
ATOM   15611 C  CD  . ARG D  1 395 ? -51.066 -5.484  53.061  1.00 42.54  ? 395  ARG D CD  1 
ATOM   15612 N  NE  . ARG D  1 395 ? -52.193 -6.063  53.770  1.00 44.67  ? 395  ARG D NE  1 
ATOM   15613 C  CZ  . ARG D  1 395 ? -53.169 -5.333  54.289  1.00 48.25  ? 395  ARG D CZ  1 
ATOM   15614 N  NH1 . ARG D  1 395 ? -53.115 -4.015  54.178  1.00 46.77  ? 395  ARG D NH1 1 
ATOM   15615 N  NH2 . ARG D  1 395 ? -54.188 -5.908  54.923  1.00 50.58  ? 395  ARG D NH2 1 
ATOM   15616 N  N   . ASP D  1 396 ? -48.718 -3.082  54.308  1.00 40.37  ? 396  ASP D N   1 
ATOM   15617 C  CA  . ASP D  1 396 ? -48.950 -1.758  53.745  1.00 41.19  ? 396  ASP D CA  1 
ATOM   15618 C  C   . ASP D  1 396 ? -47.648 -0.979  53.513  1.00 38.27  ? 396  ASP D C   1 
ATOM   15619 O  O   . ASP D  1 396 ? -47.542 -0.187  52.572  1.00 36.37  ? 396  ASP D O   1 
ATOM   15620 C  CB  . ASP D  1 396 ? -49.944 -0.967  54.600  1.00 56.95  ? 396  ASP D CB  1 
ATOM   15621 C  CG  . ASP D  1 396 ? -51.344 -1.549  54.534  1.00 65.90  ? 396  ASP D CG  1 
ATOM   15622 O  OD1 . ASP D  1 396 ? -51.592 -2.537  55.250  1.00 70.61  ? 396  ASP D OD1 1 
ATOM   15623 O  OD2 . ASP D  1 396 ? -52.192 -1.052  53.752  1.00 68.42  ? 396  ASP D OD2 1 
ATOM   15624 N  N   . ALA D  1 397 ? -46.650 -1.232  54.354  1.00 40.88  ? 397  ALA D N   1 
ATOM   15625 C  CA  . ALA D  1 397 ? -45.388 -0.511  54.287  1.00 39.71  ? 397  ALA D CA  1 
ATOM   15626 C  C   . ALA D  1 397 ? -44.526 -1.050  53.159  1.00 35.32  ? 397  ALA D C   1 
ATOM   15627 O  O   . ALA D  1 397 ? -43.683 -0.349  52.634  1.00 34.82  ? 397  ALA D O   1 
ATOM   15628 C  CB  . ALA D  1 397 ? -44.649 -0.572  55.619  1.00 37.53  ? 397  ALA D CB  1 
ATOM   15629 N  N   . MET D  1 398 ? -44.739 -2.297  52.779  1.00 35.72  ? 398  MET D N   1 
ATOM   15630 C  CA  . MET D  1 398 ? -44.030 -2.843  51.640  1.00 34.58  ? 398  MET D CA  1 
ATOM   15631 C  C   . MET D  1 398 ? -44.636 -2.227  50.376  1.00 33.50  ? 398  MET D C   1 
ATOM   15632 O  O   . MET D  1 398 ? -43.922 -1.862  49.408  1.00 32.12  ? 398  MET D O   1 
ATOM   15633 C  CB  . MET D  1 398 ? -44.150 -4.366  51.641  1.00 35.54  ? 398  MET D CB  1 
ATOM   15634 C  CG  . MET D  1 398 ? -43.506 -5.065  50.458  1.00 34.62  ? 398  MET D CG  1 
ATOM   15635 S  SD  . MET D  1 398 ? -41.731 -5.263  50.649  1.00 44.74  ? 398  MET D SD  1 
ATOM   15636 C  CE  . MET D  1 398 ? -41.107 -3.804  49.825  1.00 44.12  ? 398  MET D CE  1 
ATOM   15637 N  N   . SER D  1 399 ? -45.962 -2.094  50.401  1.00 34.25  ? 399  SER D N   1 
ATOM   15638 C  CA  . SER D  1 399 ? -46.663 -1.378  49.336  1.00 33.44  ? 399  SER D CA  1 
ATOM   15639 C  C   . SER D  1 399 ? -46.023 -0.001  49.231  1.00 32.34  ? 399  SER D C   1 
ATOM   15640 O  O   . SER D  1 399 ? -45.739 0.499   48.135  1.00 31.09  ? 399  SER D O   1 
ATOM   15641 C  CB  . SER D  1 399 ? -48.173 -1.285  49.648  1.00 34.70  ? 399  SER D CB  1 
ATOM   15642 O  OG  . SER D  1 399 ? -48.882 -0.384  48.802  1.00 34.12  ? 399  SER D OG  1 
ATOM   15643 N  N   . ALA D  1 400 ? -45.754 0.579   50.398  1.00 32.91  ? 400  ALA D N   1 
ATOM   15644 C  CA  . ALA D  1 400 ? -45.239 1.935   50.486  1.00 32.18  ? 400  ALA D CA  1 
ATOM   15645 C  C   . ALA D  1 400 ? -43.862 2.047   49.869  1.00 30.85  ? 400  ALA D C   1 
ATOM   15646 O  O   . ALA D  1 400 ? -43.647 2.903   49.026  1.00 29.80  ? 400  ALA D O   1 
ATOM   15647 C  CB  . ALA D  1 400 ? -45.215 2.402   51.920  1.00 51.82  ? 400  ALA D CB  1 
ATOM   15648 N  N   . VAL D  1 401 ? -42.936 1.186   50.298  1.00 31.81  ? 401  VAL D N   1 
ATOM   15649 C  CA  . VAL D  1 401 ? -41.583 1.146   49.742  1.00 31.46  ? 401  VAL D CA  1 
ATOM   15650 C  C   . VAL D  1 401 ? -41.657 1.120   48.222  1.00 28.83  ? 401  VAL D C   1 
ATOM   15651 O  O   . VAL D  1 401 ? -41.225 2.073   47.563  1.00 27.85  ? 401  VAL D O   1 
ATOM   15652 C  CB  . VAL D  1 401 ? -40.761 -0.046  50.269  1.00 30.52  ? 401  VAL D CB  1 
ATOM   15653 C  CG1 . VAL D  1 401 ? -39.396 -0.047  49.652  1.00 29.54  ? 401  VAL D CG1 1 
ATOM   15654 C  CG2 . VAL D  1 401 ? -40.624 0.038   51.749  1.00 31.64  ? 401  VAL D CG2 1 
ATOM   15655 N  N   . VAL D  1 402 ? -42.254 0.063   47.674  1.00 29.09  ? 402  VAL D N   1 
ATOM   15656 C  CA  . VAL D  1 402 ? -42.358 -0.052  46.218  1.00 28.14  ? 402  VAL D CA  1 
ATOM   15657 C  C   . VAL D  1 402 ? -42.905 1.218   45.546  1.00 34.17  ? 402  VAL D C   1 
ATOM   15658 O  O   . VAL D  1 402 ? -42.276 1.790   44.636  1.00 26.37  ? 402  VAL D O   1 
ATOM   15659 C  CB  . VAL D  1 402 ? -43.228 -1.259  45.816  1.00 29.60  ? 402  VAL D CB  1 
ATOM   15660 C  CG1 . VAL D  1 402 ? -43.718 -1.114  44.383  1.00 29.23  ? 402  VAL D CG1 1 
ATOM   15661 C  CG2 . VAL D  1 402 ? -42.453 -2.558  45.995  1.00 30.02  ? 402  VAL D CG2 1 
ATOM   15662 N  N   . GLY D  1 403 ? -44.061 1.666   46.026  1.00 36.57  ? 403  GLY D N   1 
ATOM   15663 C  CA  . GLY D  1 403 ? -44.723 2.838   45.483  1.00 38.03  ? 403  GLY D CA  1 
ATOM   15664 C  C   . GLY D  1 403 ? -43.901 4.115   45.505  1.00 39.13  ? 403  GLY D C   1 
ATOM   15665 O  O   . GLY D  1 403 ? -43.860 4.838   44.518  1.00 40.16  ? 403  GLY D O   1 
ATOM   15666 N  N   . ASP D  1 404 ? -43.247 4.398   46.627  1.00 39.45  ? 404  ASP D N   1 
ATOM   15667 C  CA  . ASP D  1 404 ? -42.509 5.641   46.786  1.00 37.68  ? 404  ASP D CA  1 
ATOM   15668 C  C   . ASP D  1 404 ? -41.278 5.620   45.921  1.00 37.13  ? 404  ASP D C   1 
ATOM   15669 O  O   . ASP D  1 404 ? -40.965 6.586   45.228  1.00 39.00  ? 404  ASP D O   1 
ATOM   15670 C  CB  . ASP D  1 404 ? -42.087 5.829   48.234  1.00 36.50  ? 404  ASP D CB  1 
ATOM   15671 C  CG  . ASP D  1 404 ? -43.257 5.794   49.181  1.00 42.11  ? 404  ASP D CG  1 
ATOM   15672 O  OD1 . ASP D  1 404 ? -44.396 6.050   48.723  1.00 43.89  ? 404  ASP D OD1 1 
ATOM   15673 O  OD2 . ASP D  1 404 ? -43.041 5.504   50.381  1.00 44.37  ? 404  ASP D OD2 1 
ATOM   15674 N  N   . HIS D  1 405 ? -40.572 4.503   45.959  1.00 29.65  ? 405  HIS D N   1 
ATOM   15675 C  CA  . HIS D  1 405 ? -39.309 4.422   45.245  1.00 26.57  ? 405  HIS D CA  1 
ATOM   15676 C  C   . HIS D  1 405 ? -39.476 4.481   43.731  1.00 25.21  ? 405  HIS D C   1 
ATOM   15677 O  O   . HIS D  1 405 ? -38.709 5.156   43.052  1.00 23.41  ? 405  HIS D O   1 
ATOM   15678 C  CB  . HIS D  1 405 ? -38.568 3.157   45.642  1.00 27.55  ? 405  HIS D CB  1 
ATOM   15679 C  CG  . HIS D  1 405 ? -37.351 2.904   44.822  1.00 28.58  ? 405  HIS D CG  1 
ATOM   15680 N  ND1 . HIS D  1 405 ? -36.442 3.893   44.532  1.00 30.12  ? 405  HIS D ND1 1 
ATOM   15681 C  CD2 . HIS D  1 405 ? -36.901 1.776   44.225  1.00 30.52  ? 405  HIS D CD2 1 
ATOM   15682 C  CE1 . HIS D  1 405 ? -35.464 3.381   43.800  1.00 32.00  ? 405  HIS D CE1 1 
ATOM   15683 N  NE2 . HIS D  1 405 ? -35.719 2.102   43.601  1.00 32.20  ? 405  HIS D NE2 1 
ATOM   15684 N  N   . ASN D  1 406 ? -40.455 3.742   43.208  1.00 25.97  ? 406  ASN D N   1 
ATOM   15685 C  CA  . ASN D  1 406 ? -40.709 3.715   41.763  1.00 23.57  ? 406  ASN D CA  1 
ATOM   15686 C  C   . ASN D  1 406 ? -41.575 4.824   41.160  1.00 25.56  ? 406  ASN D C   1 
ATOM   15687 O  O   . ASN D  1 406 ? -41.343 5.240   40.031  1.00 22.97  ? 406  ASN D O   1 
ATOM   15688 C  CB  . ASN D  1 406 ? -41.232 2.352   41.361  1.00 23.88  ? 406  ASN D CB  1 
ATOM   15689 C  CG  . ASN D  1 406 ? -40.199 1.284   41.544  1.00 33.60  ? 406  ASN D CG  1 
ATOM   15690 O  OD1 . ASN D  1 406 ? -39.112 1.385   40.984  1.00 35.83  ? 406  ASN D OD1 1 
ATOM   15691 N  ND2 . ASN D  1 406 ? -40.499 0.274   42.363  1.00 30.71  ? 406  ASN D ND2 1 
ATOM   15692 N  N   . VAL D  1 407 ? -42.582 5.287   41.894  1.00 24.03  ? 407  VAL D N   1 
ATOM   15693 C  CA  . VAL D  1 407 ? -43.486 6.301   41.360  1.00 32.53  ? 407  VAL D CA  1 
ATOM   15694 C  C   . VAL D  1 407 ? -43.463 7.622   42.132  1.00 30.59  ? 407  VAL D C   1 
ATOM   15695 O  O   . VAL D  1 407 ? -42.908 8.602   41.650  1.00 30.25  ? 407  VAL D O   1 
ATOM   15696 C  CB  . VAL D  1 407 ? -44.943 5.806   41.293  1.00 24.73  ? 407  VAL D CB  1 
ATOM   15697 C  CG1 . VAL D  1 407 ? -45.825 6.889   40.699  1.00 24.77  ? 407  VAL D CG1 1 
ATOM   15698 C  CG2 . VAL D  1 407 ? -45.044 4.514   40.497  1.00 24.54  ? 407  VAL D CG2 1 
ATOM   15699 N  N   . VAL D  1 408 ? -44.053 7.635   43.329  1.00 32.93  ? 408  VAL D N   1 
ATOM   15700 C  CA  . VAL D  1 408 ? -44.333 8.878   44.061  1.00 34.60  ? 408  VAL D CA  1 
ATOM   15701 C  C   . VAL D  1 408 ? -43.136 9.819   44.185  1.00 34.01  ? 408  VAL D C   1 
ATOM   15702 O  O   . VAL D  1 408 ? -43.219 10.978  43.806  1.00 34.88  ? 408  VAL D O   1 
ATOM   15703 C  CB  . VAL D  1 408 ? -44.910 8.622   45.479  1.00 27.07  ? 408  VAL D CB  1 
ATOM   15704 C  CG1 . VAL D  1 408 ? -44.934 9.908   46.265  1.00 27.63  ? 408  VAL D CG1 1 
ATOM   15705 C  CG2 . VAL D  1 408 ? -46.308 8.037   45.401  1.00 27.86  ? 408  VAL D CG2 1 
ATOM   15706 N  N   . CYS D  1 409 ? -42.018 9.322   44.698  1.00 27.29  ? 409  CYS D N   1 
ATOM   15707 C  CA  . CYS D  1 409 ? -40.857 10.183  44.907  1.00 26.43  ? 409  CYS D CA  1 
ATOM   15708 C  C   . CYS D  1 409 ? -40.224 10.736  43.625  1.00 27.09  ? 409  CYS D C   1 
ATOM   15709 O  O   . CYS D  1 409 ? -39.888 11.913  43.577  1.00 23.88  ? 409  CYS D O   1 
ATOM   15710 C  CB  . CYS D  1 409 ? -39.837 9.522   45.835  1.00 31.92  ? 409  CYS D CB  1 
ATOM   15711 S  SG  . CYS D  1 409 ? -40.391 9.529   47.548  1.00 39.73  ? 409  CYS D SG  1 
ATOM   15712 N  N   . PRO D  1 410 ? -40.054 9.895   42.589  1.00 33.64  ? 410  PRO D N   1 
ATOM   15713 C  CA  . PRO D  1 410 ? -39.743 10.450  41.267  1.00 32.25  ? 410  PRO D CA  1 
ATOM   15714 C  C   . PRO D  1 410 ? -40.720 11.536  40.789  1.00 30.97  ? 410  PRO D C   1 
ATOM   15715 O  O   . PRO D  1 410 ? -40.249 12.541  40.273  1.00 31.47  ? 410  PRO D O   1 
ATOM   15716 C  CB  . PRO D  1 410 ? -39.834 9.227   40.361  1.00 29.42  ? 410  PRO D CB  1 
ATOM   15717 C  CG  . PRO D  1 410 ? -39.380 8.115   41.233  1.00 30.01  ? 410  PRO D CG  1 
ATOM   15718 C  CD  . PRO D  1 410 ? -39.872 8.431   42.616  1.00 31.02  ? 410  PRO D CD  1 
ATOM   15719 N  N   . VAL D  1 411 ? -42.030 11.341  40.949  1.00 29.50  ? 411  VAL D N   1 
ATOM   15720 C  CA  . VAL D  1 411 ? -43.017 12.346  40.544  1.00 23.56  ? 411  VAL D CA  1 
ATOM   15721 C  C   . VAL D  1 411 ? -42.794 13.635  41.301  1.00 24.09  ? 411  VAL D C   1 
ATOM   15722 O  O   . VAL D  1 411 ? -42.831 14.715  40.739  1.00 24.10  ? 411  VAL D O   1 
ATOM   15723 C  CB  . VAL D  1 411 ? -44.455 11.887  40.822  1.00 24.81  ? 411  VAL D CB  1 
ATOM   15724 C  CG1 . VAL D  1 411 ? -45.432 13.027  40.597  1.00 24.91  ? 411  VAL D CG1 1 
ATOM   15725 C  CG2 . VAL D  1 411 ? -44.808 10.706  39.955  1.00 23.90  ? 411  VAL D CG2 1 
ATOM   15726 N  N   . ALA D  1 412 ? -42.551 13.497  42.593  1.00 27.50  ? 412  ALA D N   1 
ATOM   15727 C  CA  . ALA D  1 412 ? -42.259 14.619  43.462  1.00 30.16  ? 412  ALA D CA  1 
ATOM   15728 C  C   . ALA D  1 412 ? -41.016 15.375  43.000  1.00 32.07  ? 412  ALA D C   1 
ATOM   15729 O  O   . ALA D  1 412 ? -41.033 16.607  42.880  1.00 35.46  ? 412  ALA D O   1 
ATOM   15730 C  CB  . ALA D  1 412 ? -42.070 14.123  44.868  1.00 25.86  ? 412  ALA D CB  1 
ATOM   15731 N  N   . GLN D  1 413 ? -39.937 14.634  42.751  1.00 23.98  ? 413  GLN D N   1 
ATOM   15732 C  CA  . GLN D  1 413 ? -38.703 15.219  42.250  1.00 23.52  ? 413  GLN D CA  1 
ATOM   15733 C  C   . GLN D  1 413 ? -38.937 15.972  40.948  1.00 23.47  ? 413  GLN D C   1 
ATOM   15734 O  O   . GLN D  1 413 ? -38.456 17.087  40.787  1.00 25.06  ? 413  GLN D O   1 
ATOM   15735 C  CB  . GLN D  1 413 ? -37.635 14.160  42.040  1.00 35.06  ? 413  GLN D CB  1 
ATOM   15736 C  CG  . GLN D  1 413 ? -36.289 14.770  41.749  1.00 44.71  ? 413  GLN D CG  1 
ATOM   15737 C  CD  . GLN D  1 413 ? -35.220 13.733  41.480  1.00 55.23  ? 413  GLN D CD  1 
ATOM   15738 O  OE1 . GLN D  1 413 ? -35.327 12.940  40.535  1.00 58.41  ? 413  GLN D OE1 1 
ATOM   15739 N  NE2 . GLN D  1 413 ? -34.175 13.728  42.314  1.00 58.39  ? 413  GLN D NE2 1 
ATOM   15740 N  N   . LEU D  1 414 ? -39.690 15.371  40.028  1.00 28.23  ? 414  LEU D N   1 
ATOM   15741 C  CA  . LEU D  1 414 ? -40.006 16.020  38.758  1.00 27.58  ? 414  LEU D CA  1 
ATOM   15742 C  C   . LEU D  1 414 ? -40.783 17.312  38.965  1.00 31.40  ? 414  LEU D C   1 
ATOM   15743 O  O   . LEU D  1 414 ? -40.430 18.341  38.398  1.00 33.40  ? 414  LEU D O   1 
ATOM   15744 C  CB  . LEU D  1 414 ? -40.807 15.100  37.842  1.00 25.02  ? 414  LEU D CB  1 
ATOM   15745 C  CG  . LEU D  1 414 ? -41.038 15.683  36.449  1.00 25.94  ? 414  LEU D CG  1 
ATOM   15746 C  CD1 . LEU D  1 414 ? -39.741 15.682  35.639  1.00 21.31  ? 414  LEU D CD1 1 
ATOM   15747 C  CD2 . LEU D  1 414 ? -42.117 14.916  35.746  1.00 21.83  ? 414  LEU D CD2 1 
ATOM   15748 N  N   . ALA D  1 415 ? -41.844 17.261  39.767  1.00 36.34  ? 415  ALA D N   1 
ATOM   15749 C  CA  . ALA D  1 415 ? -42.654 18.453  40.008  1.00 37.04  ? 415  ALA D CA  1 
ATOM   15750 C  C   . ALA D  1 415 ? -41.751 19.547  40.520  1.00 34.62  ? 415  ALA D C   1 
ATOM   15751 O  O   . ALA D  1 415 ? -41.756 20.653  39.997  1.00 37.63  ? 415  ALA D O   1 
ATOM   15752 C  CB  . ALA D  1 415 ? -43.770 18.176  41.000  1.00 25.88  ? 415  ALA D CB  1 
ATOM   15753 N  N   . GLY D  1 416 ? -40.946 19.208  41.519  1.00 26.14  ? 416  GLY D N   1 
ATOM   15754 C  CA  . GLY D  1 416 ? -40.017 20.150  42.109  1.00 25.79  ? 416  GLY D CA  1 
ATOM   15755 C  C   . GLY D  1 416 ? -39.077 20.791  41.105  1.00 25.81  ? 416  GLY D C   1 
ATOM   15756 O  O   . GLY D  1 416 ? -38.946 22.013  41.074  1.00 27.58  ? 416  GLY D O   1 
ATOM   15757 N  N   . ARG D  1 417 ? -38.420 19.978  40.285  1.00 26.63  ? 417  ARG D N   1 
ATOM   15758 C  CA  . ARG D  1 417 ? -37.450 20.509  39.333  1.00 31.82  ? 417  ARG D CA  1 
ATOM   15759 C  C   . ARG D  1 417 ? -38.132 21.371  38.270  1.00 32.77  ? 417  ARG D C   1 
ATOM   15760 O  O   . ARG D  1 417 ? -37.687 22.480  37.987  1.00 33.65  ? 417  ARG D O   1 
ATOM   15761 C  CB  . ARG D  1 417 ? -36.630 19.386  38.687  1.00 48.11  ? 417  ARG D CB  1 
ATOM   15762 C  CG  . ARG D  1 417 ? -35.902 18.487  39.676  1.00 57.86  ? 417  ARG D CG  1 
ATOM   15763 C  CD  . ARG D  1 417 ? -34.468 18.915  39.875  1.00 67.99  ? 417  ARG D CD  1 
ATOM   15764 N  NE  . ARG D  1 417 ? -34.339 20.364  39.792  1.00 77.15  ? 417  ARG D NE  1 
ATOM   15765 C  CZ  . ARG D  1 417 ? -33.186 21.019  39.841  1.00 82.07  ? 417  ARG D CZ  1 
ATOM   15766 N  NH1 . ARG D  1 417 ? -32.046 20.351  39.980  1.00 83.34  ? 417  ARG D NH1 1 
ATOM   15767 N  NH2 . ARG D  1 417 ? -33.179 22.344  39.750  1.00 82.47  ? 417  ARG D NH2 1 
ATOM   15768 N  N   . LEU D  1 418 ? -39.216 20.865  37.693  1.00 36.15  ? 418  LEU D N   1 
ATOM   15769 C  CA  . LEU D  1 418 ? -39.940 21.606  36.667  1.00 37.90  ? 418  LEU D CA  1 
ATOM   15770 C  C   . LEU D  1 418 ? -40.418 22.943  37.224  1.00 43.96  ? 418  LEU D C   1 
ATOM   15771 O  O   . LEU D  1 418 ? -40.408 23.955  36.528  1.00 49.14  ? 418  LEU D O   1 
ATOM   15772 C  CB  . LEU D  1 418 ? -41.133 20.799  36.135  1.00 24.14  ? 418  LEU D CB  1 
ATOM   15773 C  CG  . LEU D  1 418 ? -40.885 19.476  35.402  1.00 23.13  ? 418  LEU D CG  1 
ATOM   15774 C  CD1 . LEU D  1 418 ? -42.138 18.990  34.674  1.00 23.11  ? 418  LEU D CD1 1 
ATOM   15775 C  CD2 . LEU D  1 418 ? -39.700 19.608  34.458  1.00 22.61  ? 418  LEU D CD2 1 
ATOM   15776 N  N   . ALA D  1 419 ? -40.833 22.942  38.484  1.00 37.94  ? 419  ALA D N   1 
ATOM   15777 C  CA  . ALA D  1 419 ? -41.269 24.166  39.130  1.00 36.70  ? 419  ALA D CA  1 
ATOM   15778 C  C   . ALA D  1 419 ? -40.090 25.109  39.258  1.00 38.18  ? 419  ALA D C   1 
ATOM   15779 O  O   . ALA D  1 419 ? -40.169 26.265  38.859  1.00 41.30  ? 419  ALA D O   1 
ATOM   15780 C  CB  . ALA D  1 419 ? -41.856 23.869  40.488  1.00 44.61  ? 419  ALA D CB  1 
ATOM   15781 N  N   . ALA D  1 420 ? -38.990 24.601  39.796  1.00 45.37  ? 420  ALA D N   1 
ATOM   15782 C  CA  . ALA D  1 420 ? -37.775 25.395  39.988  1.00 49.87  ? 420  ALA D CA  1 
ATOM   15783 C  C   . ALA D  1 420 ? -37.218 25.988  38.685  1.00 46.15  ? 420  ALA D C   1 
ATOM   15784 O  O   . ALA D  1 420 ? -36.549 27.026  38.685  1.00 46.51  ? 420  ALA D O   1 
ATOM   15785 C  CB  . ALA D  1 420 ? -36.710 24.554  40.680  1.00 61.96  ? 420  ALA D CB  1 
ATOM   15786 N  N   . GLN D  1 421 ? -37.494 25.314  37.578  1.00 31.58  ? 421  GLN D N   1 
ATOM   15787 C  CA  . GLN D  1 421 ? -37.081 25.793  36.273  1.00 31.84  ? 421  GLN D CA  1 
ATOM   15788 C  C   . GLN D  1 421 ? -38.190 26.640  35.653  1.00 31.31  ? 421  GLN D C   1 
ATOM   15789 O  O   . GLN D  1 421 ? -38.166 26.946  34.459  1.00 27.72  ? 421  GLN D O   1 
ATOM   15790 C  CB  . GLN D  1 421 ? -36.634 24.650  35.368  1.00 49.94  ? 421  GLN D CB  1 
ATOM   15791 C  CG  . GLN D  1 421 ? -35.128 24.617  35.129  1.00 52.38  ? 421  GLN D CG  1 
ATOM   15792 C  CD  . GLN D  1 421 ? -34.330 24.235  36.361  1.00 53.91  ? 421  GLN D CD  1 
ATOM   15793 O  OE1 . GLN D  1 421 ? -34.765 23.428  37.180  1.00 53.38  ? 421  GLN D OE1 1 
ATOM   15794 N  NE2 . GLN D  1 421 ? -33.145 24.813  36.490  1.00 55.35  ? 421  GLN D NE2 1 
ATOM   15795 N  N   . GLY D  1 422 ? -39.195 26.952  36.471  1.00 51.76  ? 422  GLY D N   1 
ATOM   15796 C  CA  . GLY D  1 422 ? -40.190 27.958  36.140  1.00 54.41  ? 422  GLY D CA  1 
ATOM   15797 C  C   . GLY D  1 422 ? -41.274 27.497  35.195  1.00 53.08  ? 422  GLY D C   1 
ATOM   15798 O  O   . GLY D  1 422 ? -41.668 28.213  34.278  1.00 54.90  ? 422  GLY D O   1 
ATOM   15799 N  N   . ALA D  1 423 ? -41.759 26.286  35.418  1.00 41.44  ? 423  ALA D N   1 
ATOM   15800 C  CA  . ALA D  1 423 ? -42.855 25.772  34.626  1.00 37.72  ? 423  ALA D CA  1 
ATOM   15801 C  C   . ALA D  1 423 ? -44.089 25.785  35.502  1.00 38.82  ? 423  ALA D C   1 
ATOM   15802 O  O   . ALA D  1 423 ? -43.980 25.579  36.714  1.00 42.18  ? 423  ALA D O   1 
ATOM   15803 C  CB  . ALA D  1 423 ? -42.546 24.371  34.155  1.00 28.92  ? 423  ALA D CB  1 
ATOM   15804 N  N   . ARG D  1 424 ? -45.250 26.062  34.910  1.00 30.60  ? 424  ARG D N   1 
ATOM   15805 C  CA  . ARG D  1 424 ? -46.492 25.964  35.665  1.00 36.73  ? 424  ARG D CA  1 
ATOM   15806 C  C   . ARG D  1 424 ? -46.805 24.481  35.819  1.00 35.83  ? 424  ARG D C   1 
ATOM   15807 O  O   . ARG D  1 424 ? -46.671 23.703  34.867  1.00 34.15  ? 424  ARG D O   1 
ATOM   15808 C  CB  . ARG D  1 424 ? -47.645 26.724  35.005  1.00 61.55  ? 424  ARG D CB  1 
ATOM   15809 C  CG  . ARG D  1 424 ? -48.683 27.257  35.996  1.00 70.02  ? 424  ARG D CG  1 
ATOM   15810 C  CD  . ARG D  1 424 ? -49.898 27.821  35.280  1.00 78.66  ? 424  ARG D CD  1 
ATOM   15811 N  NE  . ARG D  1 424 ? -49.524 28.781  34.244  1.00 86.67  ? 424  ARG D NE  1 
ATOM   15812 C  CZ  . ARG D  1 424 ? -49.425 30.093  34.442  1.00 94.70  ? 424  ARG D CZ  1 
ATOM   15813 N  NH1 . ARG D  1 424 ? -49.679 30.606  35.644  1.00 98.26  ? 424  ARG D NH1 1 
ATOM   15814 N  NH2 . ARG D  1 424 ? -49.075 30.896  33.441  1.00 95.54  ? 424  ARG D NH2 1 
ATOM   15815 N  N   . VAL D  1 425 ? -47.171 24.091  37.036  1.00 32.22  ? 425  VAL D N   1 
ATOM   15816 C  CA  . VAL D  1 425 ? -47.231 22.692  37.413  1.00 28.67  ? 425  VAL D CA  1 
ATOM   15817 C  C   . VAL D  1 425 ? -48.418 22.518  38.323  1.00 29.72  ? 425  VAL D C   1 
ATOM   15818 O  O   . VAL D  1 425 ? -48.572 23.276  39.262  1.00 30.75  ? 425  VAL D O   1 
ATOM   15819 C  CB  . VAL D  1 425 ? -45.938 22.279  38.189  1.00 32.21  ? 425  VAL D CB  1 
ATOM   15820 C  CG1 . VAL D  1 425 ? -46.024 20.849  38.687  1.00 31.61  ? 425  VAL D CG1 1 
ATOM   15821 C  CG2 . VAL D  1 425 ? -44.682 22.467  37.335  1.00 31.46  ? 425  VAL D CG2 1 
ATOM   15822 N  N   . TYR D  1 426 ? -49.256 21.527  38.053  1.00 44.41  ? 426  TYR D N   1 
ATOM   15823 C  CA  . TYR D  1 426 ? -50.307 21.138  38.991  1.00 44.05  ? 426  TYR D CA  1 
ATOM   15824 C  C   . TYR D  1 426 ? -50.098 19.691  39.438  1.00 43.68  ? 426  TYR D C   1 
ATOM   15825 O  O   . TYR D  1 426 ? -49.614 18.870  38.673  1.00 43.49  ? 426  TYR D O   1 
ATOM   15826 C  CB  . TYR D  1 426 ? -51.684 21.302  38.362  1.00 33.77  ? 426  TYR D CB  1 
ATOM   15827 C  CG  . TYR D  1 426 ? -52.003 22.718  37.949  1.00 33.13  ? 426  TYR D CG  1 
ATOM   15828 C  CD1 . TYR D  1 426 ? -51.634 23.194  36.703  1.00 33.23  ? 426  TYR D CD1 1 
ATOM   15829 C  CD2 . TYR D  1 426 ? -52.676 23.580  38.803  1.00 35.60  ? 426  TYR D CD2 1 
ATOM   15830 C  CE1 . TYR D  1 426 ? -51.925 24.486  36.309  1.00 35.89  ? 426  TYR D CE1 1 
ATOM   15831 C  CE2 . TYR D  1 426 ? -52.969 24.884  38.421  1.00 37.93  ? 426  TYR D CE2 1 
ATOM   15832 C  CZ  . TYR D  1 426 ? -52.592 25.329  37.167  1.00 38.13  ? 426  TYR D CZ  1 
ATOM   15833 O  OH  . TYR D  1 426 ? -52.875 26.621  36.765  1.00 39.69  ? 426  TYR D OH  1 
ATOM   15834 N  N   . ALA D  1 427 ? -50.449 19.371  40.677  1.00 33.39  ? 427  ALA D N   1 
ATOM   15835 C  CA  . ALA D  1 427 ? -50.183 18.034  41.195  1.00 33.01  ? 427  ALA D CA  1 
ATOM   15836 C  C   . ALA D  1 427 ? -51.423 17.443  41.851  1.00 34.98  ? 427  ALA D C   1 
ATOM   15837 O  O   . ALA D  1 427 ? -52.113 18.118  42.615  1.00 32.50  ? 427  ALA D O   1 
ATOM   15838 C  CB  . ALA D  1 427 ? -49.011 18.055  42.161  1.00 29.67  ? 427  ALA D CB  1 
ATOM   15839 N  N   . TYR D  1 428 ? -51.718 16.185  41.532  1.00 41.36  ? 428  TYR D N   1 
ATOM   15840 C  CA  . TYR D  1 428 ? -52.894 15.524  42.099  1.00 42.95  ? 428  TYR D CA  1 
ATOM   15841 C  C   . TYR D  1 428 ? -52.530 14.255  42.865  1.00 42.54  ? 428  TYR D C   1 
ATOM   15842 O  O   . TYR D  1 428 ? -51.544 13.574  42.552  1.00 41.06  ? 428  TYR D O   1 
ATOM   15843 C  CB  . TYR D  1 428 ? -53.942 15.198  41.004  1.00 47.43  ? 428  TYR D CB  1 
ATOM   15844 C  CG  . TYR D  1 428 ? -53.543 14.072  40.057  1.00 42.57  ? 428  TYR D CG  1 
ATOM   15845 C  CD1 . TYR D  1 428 ? -53.598 12.747  40.471  1.00 42.06  ? 428  TYR D CD1 1 
ATOM   15846 C  CD2 . TYR D  1 428 ? -53.129 14.335  38.755  1.00 36.96  ? 428  TYR D CD2 1 
ATOM   15847 C  CE1 . TYR D  1 428 ? -53.219 11.727  39.655  1.00 40.35  ? 428  TYR D CE1 1 
ATOM   15848 C  CE2 . TYR D  1 428 ? -52.767 13.309  37.913  1.00 35.46  ? 428  TYR D CE2 1 
ATOM   15849 C  CZ  . TYR D  1 428 ? -52.807 11.995  38.375  1.00 37.25  ? 428  TYR D CZ  1 
ATOM   15850 O  OH  . TYR D  1 428 ? -52.439 10.914  37.585  1.00 34.45  ? 428  TYR D OH  1 
ATOM   15851 N  N   . ILE D  1 429 ? -53.355 13.917  43.845  1.00 45.28  ? 429  ILE D N   1 
ATOM   15852 C  CA  . ILE D  1 429 ? -53.310 12.582  44.421  1.00 48.42  ? 429  ILE D CA  1 
ATOM   15853 C  C   . ILE D  1 429 ? -54.707 11.972  44.273  1.00 51.82  ? 429  ILE D C   1 
ATOM   15854 O  O   . ILE D  1 429 ? -55.689 12.522  44.759  1.00 56.19  ? 429  ILE D O   1 
ATOM   15855 C  CB  . ILE D  1 429 ? -52.734 12.568  45.881  1.00 49.38  ? 429  ILE D CB  1 
ATOM   15856 C  CG1 . ILE D  1 429 ? -52.089 11.221  46.201  1.00 47.29  ? 429  ILE D CG1 1 
ATOM   15857 C  CG2 . ILE D  1 429 ? -53.776 12.943  46.936  1.00 51.26  ? 429  ILE D CG2 1 
ATOM   15858 C  CD1 . ILE D  1 429 ? -51.498 11.168  47.573  1.00 46.93  ? 429  ILE D CD1 1 
ATOM   15859 N  N   . PHE D  1 430 ? -54.795 10.862  43.548  1.00 53.77  ? 430  PHE D N   1 
ATOM   15860 C  CA  . PHE D  1 430 ? -56.079 10.281  43.191  1.00 54.37  ? 430  PHE D CA  1 
ATOM   15861 C  C   . PHE D  1 430 ? -56.471 9.255   44.236  1.00 58.94  ? 430  PHE D C   1 
ATOM   15862 O  O   . PHE D  1 430 ? -55.839 8.206   44.337  1.00 61.64  ? 430  PHE D O   1 
ATOM   15863 C  CB  . PHE D  1 430 ? -55.967 9.607   41.830  1.00 40.36  ? 430  PHE D CB  1 
ATOM   15864 C  CG  . PHE D  1 430 ? -57.281 9.104   41.282  1.00 38.93  ? 430  PHE D CG  1 
ATOM   15865 C  CD1 . PHE D  1 430 ? -58.117 9.946   40.564  1.00 36.08  ? 430  PHE D CD1 1 
ATOM   15866 C  CD2 . PHE D  1 430 ? -57.669 7.783   41.466  1.00 39.31  ? 430  PHE D CD2 1 
ATOM   15867 C  CE1 . PHE D  1 430 ? -59.306 9.484   40.049  1.00 36.07  ? 430  PHE D CE1 1 
ATOM   15868 C  CE2 . PHE D  1 430 ? -58.869 7.316   40.950  1.00 38.71  ? 430  PHE D CE2 1 
ATOM   15869 C  CZ  . PHE D  1 430 ? -59.684 8.167   40.243  1.00 38.01  ? 430  PHE D CZ  1 
ATOM   15870 N  N   . GLU D  1 431 ? -57.496 9.580   45.025  1.00 53.73  ? 431  GLU D N   1 
ATOM   15871 C  CA  . GLU D  1 431 ? -57.912 8.755   46.167  1.00 52.92  ? 431  GLU D CA  1 
ATOM   15872 C  C   . GLU D  1 431 ? -59.149 7.838   46.042  1.00 51.77  ? 431  GLU D C   1 
ATOM   15873 O  O   . GLU D  1 431 ? -59.478 7.118   46.991  1.00 53.38  ? 431  GLU D O   1 
ATOM   15874 C  CB  . GLU D  1 431 ? -58.015 9.625   47.422  1.00 55.83  ? 431  GLU D CB  1 
ATOM   15875 C  CG  . GLU D  1 431 ? -56.690 10.251  47.810  1.00 56.94  ? 431  GLU D CG  1 
ATOM   15876 C  CD  . GLU D  1 431 ? -56.758 11.039  49.103  1.00 58.82  ? 431  GLU D CD  1 
ATOM   15877 O  OE1 . GLU D  1 431 ? -57.809 11.664  49.374  1.00 60.08  ? 431  GLU D OE1 1 
ATOM   15878 O  OE2 . GLU D  1 431 ? -55.752 11.027  49.846  1.00 57.77  ? 431  GLU D OE2 1 
ATOM   15879 N  N   . HIS D  1 432 ? -59.842 7.853   44.906  1.00 44.53  ? 432  HIS D N   1 
ATOM   15880 C  CA  . HIS D  1 432 ? -61.082 7.079   44.806  1.00 42.24  ? 432  HIS D CA  1 
ATOM   15881 C  C   . HIS D  1 432 ? -60.888 5.681   44.226  1.00 41.01  ? 432  HIS D C   1 
ATOM   15882 O  O   . HIS D  1 432 ? -60.559 5.525   43.048  1.00 39.71  ? 432  HIS D O   1 
ATOM   15883 C  CB  . HIS D  1 432 ? -62.154 7.822   43.999  1.00 44.41  ? 432  HIS D CB  1 
ATOM   15884 C  CG  . HIS D  1 432 ? -63.377 6.996   43.731  1.00 48.35  ? 432  HIS D CG  1 
ATOM   15885 N  ND1 . HIS D  1 432 ? -64.376 6.813   44.667  1.00 50.45  ? 432  HIS D ND1 1 
ATOM   15886 C  CD2 . HIS D  1 432 ? -63.751 6.281   42.642  1.00 49.18  ? 432  HIS D CD2 1 
ATOM   15887 C  CE1 . HIS D  1 432 ? -65.313 6.030   44.162  1.00 50.52  ? 432  HIS D CE1 1 
ATOM   15888 N  NE2 . HIS D  1 432 ? -64.957 5.691   42.934  1.00 49.75  ? 432  HIS D NE2 1 
ATOM   15889 N  N   . ARG D  1 433 ? -61.103 4.667   45.058  1.00 43.59  ? 433  ARG D N   1 
ATOM   15890 C  CA  . ARG D  1 433 ? -61.164 3.291   44.582  1.00 45.49  ? 433  ARG D CA  1 
ATOM   15891 C  C   . ARG D  1 433 ? -62.523 3.059   43.915  1.00 51.49  ? 433  ARG D C   1 
ATOM   15892 O  O   . ARG D  1 433 ? -63.574 3.280   44.524  1.00 55.24  ? 433  ARG D O   1 
ATOM   15893 C  CB  . ARG D  1 433 ? -60.961 2.319   45.748  1.00 48.83  ? 433  ARG D CB  1 
ATOM   15894 C  CG  . ARG D  1 433 ? -61.190 0.846   45.418  1.00 51.99  ? 433  ARG D CG  1 
ATOM   15895 C  CD  . ARG D  1 433 ? -61.190 -0.002  46.691  1.00 56.35  ? 433  ARG D CD  1 
ATOM   15896 N  NE  . ARG D  1 433 ? -61.465 -1.421  46.456  1.00 59.22  ? 433  ARG D NE  1 
ATOM   15897 C  CZ  . ARG D  1 433 ? -60.536 -2.375  46.447  1.00 58.83  ? 433  ARG D CZ  1 
ATOM   15898 N  NH1 . ARG D  1 433 ? -59.264 -2.066  46.654  1.00 55.91  ? 433  ARG D NH1 1 
ATOM   15899 N  NH2 . ARG D  1 433 ? -60.877 -3.640  46.231  1.00 60.35  ? 433  ARG D NH2 1 
ATOM   15900 N  N   . ALA D  1 434 ? -62.508 2.628   42.659  1.00 58.15  ? 434  ALA D N   1 
ATOM   15901 C  CA  . ALA D  1 434 ? -63.754 2.382   41.941  1.00 58.82  ? 434  ALA D CA  1 
ATOM   15902 C  C   . ALA D  1 434 ? -64.558 1.241   42.574  1.00 59.72  ? 434  ALA D C   1 
ATOM   15903 O  O   . ALA D  1 434 ? -64.000 0.223   42.993  1.00 60.01  ? 434  ALA D O   1 
ATOM   15904 C  CB  . ALA D  1 434 ? -63.473 2.095   40.479  1.00 52.78  ? 434  ALA D CB  1 
ATOM   15905 N  N   . SER D  1 435 ? -65.874 1.426   42.640  1.00 48.04  ? 435  SER D N   1 
ATOM   15906 C  CA  . SER D  1 435 ? -66.775 0.428   43.202  1.00 51.23  ? 435  SER D CA  1 
ATOM   15907 C  C   . SER D  1 435 ? -66.700 -0.879  42.423  1.00 53.90  ? 435  SER D C   1 
ATOM   15908 O  O   . SER D  1 435 ? -66.855 -1.966  42.985  1.00 53.63  ? 435  SER D O   1 
ATOM   15909 C  CB  . SER D  1 435 ? -68.211 0.947   43.166  1.00 65.67  ? 435  SER D CB  1 
ATOM   15910 O  OG  . SER D  1 435 ? -68.719 0.962   41.840  1.00 66.37  ? 435  SER D OG  1 
ATOM   15911 N  N   . THR D  1 436 ? -66.451 -0.753  41.124  1.00 72.09  ? 436  THR D N   1 
ATOM   15912 C  CA  . THR D  1 436 ? -66.453 -1.871  40.194  1.00 75.81  ? 436  THR D CA  1 
ATOM   15913 C  C   . THR D  1 436 ? -65.115 -2.578  40.163  1.00 75.59  ? 436  THR D C   1 
ATOM   15914 O  O   . THR D  1 436 ? -64.913 -3.493  39.365  1.00 77.93  ? 436  THR D O   1 
ATOM   15915 C  CB  . THR D  1 436 ? -66.700 -1.379  38.773  1.00 79.35  ? 436  THR D CB  1 
ATOM   15916 O  OG1 . THR D  1 436 ? -65.582 -0.583  38.347  1.00 77.54  ? 436  THR D OG1 1 
ATOM   15917 C  CG2 . THR D  1 436 ? -67.977 -0.553  38.716  1.00 81.79  ? 436  THR D CG2 1 
ATOM   15918 N  N   . LEU D  1 437 ? -64.190 -2.137  41.006  1.00 60.84  ? 437  LEU D N   1 
ATOM   15919 C  CA  . LEU D  1 437 ? -62.847 -2.693  40.999  1.00 56.57  ? 437  LEU D CA  1 
ATOM   15920 C  C   . LEU D  1 437 ? -62.864 -4.174  41.386  1.00 53.01  ? 437  LEU D C   1 
ATOM   15921 O  O   . LEU D  1 437 ? -63.802 -4.652  42.022  1.00 52.73  ? 437  LEU D O   1 
ATOM   15922 C  CB  . LEU D  1 437 ? -61.930 -1.887  41.916  1.00 66.71  ? 437  LEU D CB  1 
ATOM   15923 C  CG  . LEU D  1 437 ? -60.434 -2.004  41.637  1.00 67.83  ? 437  LEU D CG  1 
ATOM   15924 C  CD1 . LEU D  1 437 ? -59.788 -0.637  41.701  1.00 68.35  ? 437  LEU D CD1 1 
ATOM   15925 C  CD2 . LEU D  1 437 ? -59.791 -2.940  42.635  1.00 68.14  ? 437  LEU D CD2 1 
ATOM   15926 N  N   . THR D  1 438 ? -61.821 -4.887  40.978  1.00 56.92  ? 438  THR D N   1 
ATOM   15927 C  CA  . THR D  1 438 ? -61.741 -6.343  41.081  1.00 55.75  ? 438  THR D CA  1 
ATOM   15928 C  C   . THR D  1 438 ? -60.792 -6.804  42.172  1.00 57.77  ? 438  THR D C   1 
ATOM   15929 O  O   . THR D  1 438 ? -61.126 -7.694  42.956  1.00 61.58  ? 438  THR D O   1 
ATOM   15930 C  CB  . THR D  1 438 ? -61.360 -6.992  39.775  1.00 43.09  ? 438  THR D CB  1 
ATOM   15931 O  OG1 . THR D  1 438 ? -61.768 -6.141  38.695  1.00 42.31  ? 438  THR D OG1 1 
ATOM   15932 C  CG2 . THR D  1 438 ? -62.049 -8.334  39.674  1.00 44.79  ? 438  THR D CG2 1 
ATOM   15933 N  N   . TRP D  1 439 ? -59.576 -6.261  42.134  1.00 54.90  ? 439  TRP D N   1 
ATOM   15934 C  CA  . TRP D  1 439 ? -58.517 -6.561  43.098  1.00 52.81  ? 439  TRP D CA  1 
ATOM   15935 C  C   . TRP D  1 439 ? -58.980 -6.428  44.557  1.00 52.50  ? 439  TRP D C   1 
ATOM   15936 O  O   . TRP D  1 439 ? -59.956 -5.724  44.852  1.00 49.78  ? 439  TRP D O   1 
ATOM   15937 C  CB  . TRP D  1 439 ? -57.357 -5.588  42.896  1.00 43.09  ? 439  TRP D CB  1 
ATOM   15938 C  CG  . TRP D  1 439 ? -56.689 -5.671  41.594  1.00 40.50  ? 439  TRP D CG  1 
ATOM   15939 C  CD1 . TRP D  1 439 ? -56.873 -4.844  40.526  1.00 40.36  ? 439  TRP D CD1 1 
ATOM   15940 C  CD2 . TRP D  1 439 ? -55.695 -6.617  41.206  1.00 39.31  ? 439  TRP D CD2 1 
ATOM   15941 N  NE1 . TRP D  1 439 ? -56.053 -5.223  39.486  1.00 39.49  ? 439  TRP D NE1 1 
ATOM   15942 C  CE2 . TRP D  1 439 ? -55.320 -6.313  39.879  1.00 39.06  ? 439  TRP D CE2 1 
ATOM   15943 C  CE3 . TRP D  1 439 ? -55.089 -7.699  41.846  1.00 39.28  ? 439  TRP D CE3 1 
ATOM   15944 C  CZ2 . TRP D  1 439 ? -54.366 -7.049  39.182  1.00 35.29  ? 439  TRP D CZ2 1 
ATOM   15945 C  CZ3 . TRP D  1 439 ? -54.139 -8.428  41.153  1.00 39.10  ? 439  TRP D CZ3 1 
ATOM   15946 C  CH2 . TRP D  1 439 ? -53.786 -8.099  39.835  1.00 38.27  ? 439  TRP D CH2 1 
ATOM   15947 N  N   . PRO D  1 440 ? -58.279 -7.118  45.477  1.00 47.48  ? 440  PRO D N   1 
ATOM   15948 C  CA  . PRO D  1 440 ? -58.639 -7.165  46.899  1.00 49.50  ? 440  PRO D CA  1 
ATOM   15949 C  C   . PRO D  1 440 ? -58.721 -5.809  47.584  1.00 45.42  ? 440  PRO D C   1 
ATOM   15950 O  O   . PRO D  1 440 ? -58.151 -4.823  47.121  1.00 43.74  ? 440  PRO D O   1 
ATOM   15951 C  CB  . PRO D  1 440 ? -57.494 -7.976  47.522  1.00 49.54  ? 440  PRO D CB  1 
ATOM   15952 C  CG  . PRO D  1 440 ? -56.389 -7.934  46.525  1.00 46.15  ? 440  PRO D CG  1 
ATOM   15953 C  CD  . PRO D  1 440 ? -57.083 -7.937  45.207  1.00 46.54  ? 440  PRO D CD  1 
ATOM   15954 N  N   . LEU D  1 441 ? -59.438 -5.787  48.700  1.00 48.64  ? 441  LEU D N   1 
ATOM   15955 C  CA  . LEU D  1 441 ? -59.608 -4.585  49.507  1.00 51.66  ? 441  LEU D CA  1 
ATOM   15956 C  C   . LEU D  1 441 ? -58.264 -3.997  49.951  1.00 49.78  ? 441  LEU D C   1 
ATOM   15957 O  O   . LEU D  1 441 ? -58.100 -2.777  50.042  1.00 45.25  ? 441  LEU D O   1 
ATOM   15958 C  CB  . LEU D  1 441 ? -60.473 -4.923  50.730  1.00 70.42  ? 441  LEU D CB  1 
ATOM   15959 C  CG  . LEU D  1 441 ? -61.213 -3.819  51.497  1.00 72.82  ? 441  LEU D CG  1 
ATOM   15960 C  CD1 . LEU D  1 441 ? -60.354 -3.244  52.637  1.00 73.30  ? 441  LEU D CD1 1 
ATOM   15961 C  CD2 . LEU D  1 441 ? -61.701 -2.721  50.540  1.00 70.33  ? 441  LEU D CD2 1 
ATOM   15962 N  N   . TRP D  1 442 ? -57.303 -4.873  50.213  1.00 54.77  ? 442  TRP D N   1 
ATOM   15963 C  CA  . TRP D  1 442 ? -56.042 -4.451  50.798  1.00 54.57  ? 442  TRP D CA  1 
ATOM   15964 C  C   . TRP D  1 442 ? -55.167 -3.634  49.858  1.00 53.58  ? 442  TRP D C   1 
ATOM   15965 O  O   . TRP D  1 442 ? -54.225 -2.965  50.301  1.00 54.07  ? 442  TRP D O   1 
ATOM   15966 C  CB  . TRP D  1 442 ? -55.262 -5.650  51.351  1.00 59.62  ? 442  TRP D CB  1 
ATOM   15967 C  CG  . TRP D  1 442 ? -54.620 -6.561  50.331  1.00 60.54  ? 442  TRP D CG  1 
ATOM   15968 C  CD1 . TRP D  1 442 ? -55.070 -7.789  49.937  1.00 63.70  ? 442  TRP D CD1 1 
ATOM   15969 C  CD2 . TRP D  1 442 ? -53.390 -6.337  49.613  1.00 55.83  ? 442  TRP D CD2 1 
ATOM   15970 N  NE1 . TRP D  1 442 ? -54.208 -8.334  49.011  1.00 62.21  ? 442  TRP D NE1 1 
ATOM   15971 C  CE2 . TRP D  1 442 ? -53.171 -7.461  48.798  1.00 57.29  ? 442  TRP D CE2 1 
ATOM   15972 C  CE3 . TRP D  1 442 ? -52.461 -5.296  49.578  1.00 49.77  ? 442  TRP D CE3 1 
ATOM   15973 C  CZ2 . TRP D  1 442 ? -52.068 -7.570  47.963  1.00 53.07  ? 442  TRP D CZ2 1 
ATOM   15974 C  CZ3 . TRP D  1 442 ? -51.378 -5.406  48.750  1.00 46.65  ? 442  TRP D CZ3 1 
ATOM   15975 C  CH2 . TRP D  1 442 ? -51.185 -6.532  47.957  1.00 48.63  ? 442  TRP D CH2 1 
ATOM   15976 N  N   . MET D  1 443 ? -55.485 -3.674  48.568  1.00 56.92  ? 443  MET D N   1 
ATOM   15977 C  CA  . MET D  1 443 ? -54.651 -3.029  47.555  1.00 54.00  ? 443  MET D CA  1 
ATOM   15978 C  C   . MET D  1 443 ? -55.012 -1.562  47.327  1.00 50.77  ? 443  MET D C   1 
ATOM   15979 O  O   . MET D  1 443 ? -54.482 -0.918  46.425  1.00 49.37  ? 443  MET D O   1 
ATOM   15980 C  CB  . MET D  1 443 ? -54.722 -3.787  46.235  1.00 44.55  ? 443  MET D CB  1 
ATOM   15981 C  CG  . MET D  1 443 ? -53.869 -5.019  46.178  1.00 38.57  ? 443  MET D CG  1 
ATOM   15982 S  SD  . MET D  1 443 ? -54.047 -5.753  44.543  1.00 50.24  ? 443  MET D SD  1 
ATOM   15983 C  CE  . MET D  1 443 ? -52.732 -6.971  44.593  1.00 37.54  ? 443  MET D CE  1 
ATOM   15984 N  N   . GLY D  1 444 ? -55.931 -1.049  48.133  1.00 46.04  ? 444  GLY D N   1 
ATOM   15985 C  CA  . GLY D  1 444 ? -56.266 0.359   48.088  1.00 47.11  ? 444  GLY D CA  1 
ATOM   15986 C  C   . GLY D  1 444 ? -56.736 0.806   46.719  1.00 46.50  ? 444  GLY D C   1 
ATOM   15987 O  O   . GLY D  1 444 ? -57.693 0.261   46.165  1.00 46.63  ? 444  GLY D O   1 
ATOM   15988 N  N   . VAL D  1 445 ? -56.042 1.801   46.177  1.00 46.45  ? 445  VAL D N   1 
ATOM   15989 C  CA  . VAL D  1 445 ? -56.361 2.363   44.878  1.00 44.91  ? 445  VAL D CA  1 
ATOM   15990 C  C   . VAL D  1 445 ? -55.142 2.068   44.053  1.00 45.67  ? 445  VAL D C   1 
ATOM   15991 O  O   . VAL D  1 445 ? -54.219 2.865   44.008  1.00 48.08  ? 445  VAL D O   1 
ATOM   15992 C  CB  . VAL D  1 445 ? -56.558 3.894   44.953  1.00 36.74  ? 445  VAL D CB  1 
ATOM   15993 C  CG1 . VAL D  1 445 ? -56.972 4.460   43.607  1.00 36.07  ? 445  VAL D CG1 1 
ATOM   15994 C  CG2 . VAL D  1 445 ? -57.597 4.239   45.991  1.00 38.65  ? 445  VAL D CG2 1 
ATOM   15995 N  N   . PRO D  1 446 ? -55.115 0.891   43.430  1.00 34.89  ? 446  PRO D N   1 
ATOM   15996 C  CA  . PRO D  1 446 ? -53.930 0.396   42.732  1.00 37.76  ? 446  PRO D CA  1 
ATOM   15997 C  C   . PRO D  1 446 ? -53.469 1.273   41.575  1.00 35.94  ? 446  PRO D C   1 
ATOM   15998 O  O   . PRO D  1 446 ? -54.228 2.077   41.025  1.00 36.60  ? 446  PRO D O   1 
ATOM   15999 C  CB  . PRO D  1 446 ? -54.385 -0.961  42.201  1.00 34.00  ? 446  PRO D CB  1 
ATOM   16000 C  CG  . PRO D  1 446 ? -55.455 -1.370  43.125  1.00 35.86  ? 446  PRO D CG  1 
ATOM   16001 C  CD  . PRO D  1 446 ? -56.184 -0.112  43.450  1.00 36.34  ? 446  PRO D CD  1 
ATOM   16002 N  N   . HIS D  1 447 ? -52.206 1.088   41.220  1.00 34.79  ? 447  HIS D N   1 
ATOM   16003 C  CA  . HIS D  1 447 ? -51.586 1.755   40.093  1.00 34.61  ? 447  HIS D CA  1 
ATOM   16004 C  C   . HIS D  1 447 ? -52.451 1.593   38.836  1.00 38.08  ? 447  HIS D C   1 
ATOM   16005 O  O   . HIS D  1 447 ? -52.927 0.501   38.511  1.00 37.78  ? 447  HIS D O   1 
ATOM   16006 C  CB  . HIS D  1 447 ? -50.199 1.135   39.897  1.00 31.11  ? 447  HIS D CB  1 
ATOM   16007 C  CG  . HIS D  1 447 ? -49.452 1.651   38.712  1.00 30.06  ? 447  HIS D CG  1 
ATOM   16008 N  ND1 . HIS D  1 447 ? -49.015 2.955   38.615  1.00 33.58  ? 447  HIS D ND1 1 
ATOM   16009 C  CD2 . HIS D  1 447 ? -49.035 1.029   37.584  1.00 29.21  ? 447  HIS D CD2 1 
ATOM   16010 C  CE1 . HIS D  1 447 ? -48.372 3.118   37.472  1.00 33.07  ? 447  HIS D CE1 1 
ATOM   16011 N  NE2 . HIS D  1 447 ? -48.370 1.963   36.828  1.00 31.34  ? 447  HIS D NE2 1 
ATOM   16012 N  N   . GLY D  1 448 ? -52.697 2.700   38.154  1.00 49.36  ? 448  GLY D N   1 
ATOM   16013 C  CA  . GLY D  1 448 ? -53.413 2.645   36.900  1.00 48.49  ? 448  GLY D CA  1 
ATOM   16014 C  C   . GLY D  1 448 ? -54.920 2.740   36.998  1.00 50.45  ? 448  GLY D C   1 
ATOM   16015 O  O   . GLY D  1 448 ? -55.589 2.779   35.968  1.00 54.16  ? 448  GLY D O   1 
ATOM   16016 N  N   . TYR D  1 449 ? -55.471 2.797   38.208  1.00 34.83  ? 449  TYR D N   1 
ATOM   16017 C  CA  . TYR D  1 449 ? -56.933 2.741   38.348  1.00 34.07  ? 449  TYR D CA  1 
ATOM   16018 C  C   . TYR D  1 449 ? -57.686 4.072   38.337  1.00 33.68  ? 449  TYR D C   1 
ATOM   16019 O  O   . TYR D  1 449 ? -58.880 4.126   38.645  1.00 34.92  ? 449  TYR D O   1 
ATOM   16020 C  CB  . TYR D  1 449 ? -57.386 1.762   39.435  1.00 41.94  ? 449  TYR D CB  1 
ATOM   16021 C  CG  . TYR D  1 449 ? -57.168 0.341   38.961  1.00 45.56  ? 449  TYR D CG  1 
ATOM   16022 C  CD1 . TYR D  1 449 ? -55.921 -0.261  39.091  1.00 48.94  ? 449  TYR D CD1 1 
ATOM   16023 C  CD2 . TYR D  1 449 ? -58.178 -0.376  38.316  1.00 44.97  ? 449  TYR D CD2 1 
ATOM   16024 C  CE1 . TYR D  1 449 ? -55.690 -1.550  38.632  1.00 50.44  ? 449  TYR D CE1 1 
ATOM   16025 C  CE2 . TYR D  1 449 ? -57.958 -1.669  37.855  1.00 46.04  ? 449  TYR D CE2 1 
ATOM   16026 C  CZ  . TYR D  1 449 ? -56.707 -2.249  38.018  1.00 49.21  ? 449  TYR D CZ  1 
ATOM   16027 O  OH  . TYR D  1 449 ? -56.435 -3.526  37.572  1.00 49.54  ? 449  TYR D OH  1 
ATOM   16028 N  N   . GLU D  1 450 ? -56.967 5.143   38.011  1.00 51.09  ? 450  GLU D N   1 
ATOM   16029 C  CA  . GLU D  1 450 ? -57.602 6.426   37.728  1.00 53.94  ? 450  GLU D CA  1 
ATOM   16030 C  C   . GLU D  1 450 ? -57.955 6.601   36.251  1.00 56.06  ? 450  GLU D C   1 
ATOM   16031 O  O   . GLU D  1 450 ? -58.716 7.508   35.913  1.00 60.60  ? 450  GLU D O   1 
ATOM   16032 C  CB  . GLU D  1 450 ? -56.689 7.580   38.145  1.00 41.44  ? 450  GLU D CB  1 
ATOM   16033 C  CG  . GLU D  1 450 ? -55.659 7.987   37.098  1.00 40.46  ? 450  GLU D CG  1 
ATOM   16034 C  CD  . GLU D  1 450 ? -54.452 7.059   37.061  1.00 42.97  ? 450  GLU D CD  1 
ATOM   16035 O  OE1 . GLU D  1 450 ? -54.640 5.831   37.213  1.00 42.46  ? 450  GLU D OE1 1 
ATOM   16036 O  OE2 . GLU D  1 450 ? -53.311 7.558   36.890  1.00 44.84  ? 450  GLU D OE2 1 
ATOM   16037 N  N   . ILE D  1 451 ? -57.421 5.743   35.378  1.00 42.76  ? 451  ILE D N   1 
ATOM   16038 C  CA  . ILE D  1 451 ? -57.569 5.940   33.930  1.00 37.63  ? 451  ILE D CA  1 
ATOM   16039 C  C   . ILE D  1 451 ? -59.023 5.911   33.486  1.00 37.51  ? 451  ILE D C   1 
ATOM   16040 O  O   . ILE D  1 451 ? -59.493 6.830   32.805  1.00 35.56  ? 451  ILE D O   1 
ATOM   16041 C  CB  . ILE D  1 451 ? -56.804 4.899   33.112  1.00 29.78  ? 451  ILE D CB  1 
ATOM   16042 C  CG1 . ILE D  1 451 ? -55.338 4.887   33.512  1.00 28.55  ? 451  ILE D CG1 1 
ATOM   16043 C  CG2 . ILE D  1 451 ? -56.937 5.188   31.624  1.00 29.28  ? 451  ILE D CG2 1 
ATOM   16044 C  CD1 . ILE D  1 451 ? -54.521 3.963   32.679  1.00 27.60  ? 451  ILE D CD1 1 
ATOM   16045 N  N   . GLU D  1 452 ? -59.731 4.858   33.890  1.00 44.34  ? 452  GLU D N   1 
ATOM   16046 C  CA  . GLU D  1 452 ? -61.121 4.653   33.499  1.00 47.15  ? 452  GLU D CA  1 
ATOM   16047 C  C   . GLU D  1 452 ? -61.977 5.873   33.822  1.00 50.96  ? 452  GLU D C   1 
ATOM   16048 O  O   . GLU D  1 452 ? -62.945 6.168   33.124  1.00 55.50  ? 452  GLU D O   1 
ATOM   16049 C  CB  . GLU D  1 452 ? -61.677 3.400   34.173  1.00 39.33  ? 452  GLU D CB  1 
ATOM   16050 C  CG  . GLU D  1 452 ? -61.487 3.380   35.679  1.00 42.23  ? 452  GLU D CG  1 
ATOM   16051 C  CD  . GLU D  1 452 ? -61.391 1.974   36.243  1.00 46.66  ? 452  GLU D CD  1 
ATOM   16052 O  OE1 . GLU D  1 452 ? -60.268 1.429   36.265  1.00 47.18  ? 452  GLU D OE1 1 
ATOM   16053 O  OE2 . GLU D  1 452 ? -62.430 1.411   36.664  1.00 50.48  ? 452  GLU D OE2 1 
ATOM   16054 N  N   . PHE D  1 453 ? -61.600 6.594   34.869  1.00 41.06  ? 453  PHE D N   1 
ATOM   16055 C  CA  . PHE D  1 453 ? -62.321 7.796   35.245  1.00 40.66  ? 453  PHE D CA  1 
ATOM   16056 C  C   . PHE D  1 453 ? -61.944 8.974   34.369  1.00 41.52  ? 453  PHE D C   1 
ATOM   16057 O  O   . PHE D  1 453 ? -62.815 9.742   33.962  1.00 43.70  ? 453  PHE D O   1 
ATOM   16058 C  CB  . PHE D  1 453 ? -62.089 8.126   36.711  1.00 42.08  ? 453  PHE D CB  1 
ATOM   16059 C  CG  . PHE D  1 453 ? -62.779 7.196   37.641  1.00 45.42  ? 453  PHE D CG  1 
ATOM   16060 C  CD1 . PHE D  1 453 ? -62.157 6.039   38.067  1.00 47.90  ? 453  PHE D CD1 1 
ATOM   16061 C  CD2 . PHE D  1 453 ? -64.062 7.458   38.070  1.00 49.02  ? 453  PHE D CD2 1 
ATOM   16062 C  CE1 . PHE D  1 453 ? -62.804 5.163   38.923  1.00 51.00  ? 453  PHE D CE1 1 
ATOM   16063 C  CE2 . PHE D  1 453 ? -64.717 6.590   38.928  1.00 51.96  ? 453  PHE D CE2 1 
ATOM   16064 C  CZ  . PHE D  1 453 ? -64.088 5.440   39.356  1.00 51.97  ? 453  PHE D CZ  1 
ATOM   16065 N  N   . ILE D  1 454 ? -60.654 9.120   34.079  1.00 36.66  ? 454  ILE D N   1 
ATOM   16066 C  CA  . ILE D  1 454 ? -60.204 10.234  33.256  1.00 33.57  ? 454  ILE D CA  1 
ATOM   16067 C  C   . ILE D  1 454 ? -60.813 10.107  31.876  1.00 33.68  ? 454  ILE D C   1 
ATOM   16068 O  O   . ILE D  1 454 ? -61.163 11.103  31.255  1.00 34.01  ? 454  ILE D O   1 
ATOM   16069 C  CB  . ILE D  1 454 ? -58.682 10.295  33.123  1.00 33.32  ? 454  ILE D CB  1 
ATOM   16070 C  CG1 . ILE D  1 454 ? -58.024 10.291  34.498  1.00 31.70  ? 454  ILE D CG1 1 
ATOM   16071 C  CG2 . ILE D  1 454 ? -58.267 11.535  32.365  1.00 31.27  ? 454  ILE D CG2 1 
ATOM   16072 C  CD1 . ILE D  1 454 ? -58.513 11.384  35.370  1.00 32.81  ? 454  ILE D CD1 1 
ATOM   16073 N  N   . PHE D  1 455 ? -60.966 8.877   31.399  1.00 37.37  ? 455  PHE D N   1 
ATOM   16074 C  CA  . PHE D  1 455 ? -61.633 8.664   30.119  1.00 40.10  ? 455  PHE D CA  1 
ATOM   16075 C  C   . PHE D  1 455 ? -63.155 8.744   30.218  1.00 42.80  ? 455  PHE D C   1 
ATOM   16076 O  O   . PHE D  1 455 ? -63.829 8.955   29.221  1.00 44.34  ? 455  PHE D O   1 
ATOM   16077 C  CB  . PHE D  1 455 ? -61.174 7.361   29.464  1.00 37.57  ? 455  PHE D CB  1 
ATOM   16078 C  CG  . PHE D  1 455 ? -59.857 7.493   28.750  1.00 37.84  ? 455  PHE D CG  1 
ATOM   16079 C  CD1 . PHE D  1 455 ? -58.656 7.281   29.427  1.00 38.70  ? 455  PHE D CD1 1 
ATOM   16080 C  CD2 . PHE D  1 455 ? -59.813 7.870   27.412  1.00 33.90  ? 455  PHE D CD2 1 
ATOM   16081 C  CE1 . PHE D  1 455 ? -57.441 7.422   28.778  1.00 34.64  ? 455  PHE D CE1 1 
ATOM   16082 C  CE2 . PHE D  1 455 ? -58.609 8.011   26.762  1.00 30.57  ? 455  PHE D CE2 1 
ATOM   16083 C  CZ  . PHE D  1 455 ? -57.420 7.791   27.447  1.00 31.65  ? 455  PHE D CZ  1 
ATOM   16084 N  N   . GLY D  1 456 ? -63.690 8.583   31.422  1.00 44.40  ? 456  GLY D N   1 
ATOM   16085 C  CA  . GLY D  1 456 ? -65.106 8.792   31.647  1.00 47.16  ? 456  GLY D CA  1 
ATOM   16086 C  C   . GLY D  1 456 ? -66.009 7.585   31.442  1.00 49.59  ? 456  GLY D C   1 
ATOM   16087 O  O   . GLY D  1 456 ? -67.217 7.734   31.224  1.00 52.37  ? 456  GLY D O   1 
ATOM   16088 N  N   . LEU D  1 457 ? -65.439 6.388   31.524  1.00 47.94  ? 457  LEU D N   1 
ATOM   16089 C  CA  . LEU D  1 457 ? -66.231 5.153   31.462  1.00 48.57  ? 457  LEU D CA  1 
ATOM   16090 C  C   . LEU D  1 457 ? -67.493 5.109   32.351  1.00 54.56  ? 457  LEU D C   1 
ATOM   16091 O  O   . LEU D  1 457 ? -68.510 4.579   31.921  1.00 56.74  ? 457  LEU D O   1 
ATOM   16092 C  CB  . LEU D  1 457 ? -65.358 3.919   31.725  1.00 39.33  ? 457  LEU D CB  1 
ATOM   16093 C  CG  . LEU D  1 457 ? -64.612 3.319   30.536  1.00 37.89  ? 457  LEU D CG  1 
ATOM   16094 C  CD1 . LEU D  1 457 ? -63.847 4.379   29.759  1.00 36.45  ? 457  LEU D CD1 1 
ATOM   16095 C  CD2 . LEU D  1 457 ? -63.660 2.262   31.040  1.00 37.05  ? 457  LEU D CD2 1 
ATOM   16096 N  N   . PRO D  1 458 ? -67.438 5.650   33.587  1.00 61.43  ? 458  PRO D N   1 
ATOM   16097 C  CA  . PRO D  1 458 ? -68.654 5.630   34.409  1.00 65.79  ? 458  PRO D CA  1 
ATOM   16098 C  C   . PRO D  1 458 ? -69.891 6.234   33.744  1.00 70.41  ? 458  PRO D C   1 
ATOM   16099 O  O   . PRO D  1 458 ? -71.006 5.910   34.163  1.00 75.10  ? 458  PRO D O   1 
ATOM   16100 C  CB  . PRO D  1 458 ? -68.261 6.473   35.616  1.00 65.72  ? 458  PRO D CB  1 
ATOM   16101 C  CG  . PRO D  1 458 ? -66.812 6.223   35.770  1.00 63.46  ? 458  PRO D CG  1 
ATOM   16102 C  CD  . PRO D  1 458 ? -66.259 6.040   34.388  1.00 61.05  ? 458  PRO D CD  1 
ATOM   16103 N  N   . LEU D  1 459 ? -69.701 7.083   32.735  1.00 59.03  ? 459  LEU D N   1 
ATOM   16104 C  CA  . LEU D  1 459 ? -70.820 7.678   32.007  1.00 58.32  ? 459  LEU D CA  1 
ATOM   16105 C  C   . LEU D  1 459 ? -71.635 6.646   31.239  1.00 58.56  ? 459  LEU D C   1 
ATOM   16106 O  O   . LEU D  1 459 ? -72.800 6.875   30.936  1.00 61.36  ? 459  LEU D O   1 
ATOM   16107 C  CB  . LEU D  1 459 ? -70.317 8.739   31.047  1.00 46.30  ? 459  LEU D CB  1 
ATOM   16108 C  CG  . LEU D  1 459 ? -69.577 9.879   31.726  1.00 45.59  ? 459  LEU D CG  1 
ATOM   16109 C  CD1 . LEU D  1 459 ? -68.742 10.638  30.706  1.00 43.96  ? 459  LEU D CD1 1 
ATOM   16110 C  CD2 . LEU D  1 459 ? -70.570 10.795  32.400  1.00 47.67  ? 459  LEU D CD2 1 
ATOM   16111 N  N   . ASP D  1 460 ? -71.014 5.515   30.925  1.00 54.35  ? 460  ASP D N   1 
ATOM   16112 C  CA  . ASP D  1 460 ? -71.680 4.409   30.243  1.00 59.47  ? 460  ASP D CA  1 
ATOM   16113 C  C   . ASP D  1 460 ? -72.481 3.578   31.250  1.00 62.84  ? 460  ASP D C   1 
ATOM   16114 O  O   . ASP D  1 460 ? -71.906 2.977   32.160  1.00 64.66  ? 460  ASP D O   1 
ATOM   16115 C  CB  . ASP D  1 460 ? -70.627 3.537   29.572  1.00 72.42  ? 460  ASP D CB  1 
ATOM   16116 C  CG  . ASP D  1 460 ? -71.223 2.473   28.693  1.00 77.38  ? 460  ASP D CG  1 
ATOM   16117 O  OD1 . ASP D  1 460 ? -71.749 1.478   29.231  1.00 80.35  ? 460  ASP D OD1 1 
ATOM   16118 O  OD2 . ASP D  1 460 ? -71.143 2.628   27.458  1.00 78.51  ? 460  ASP D OD2 1 
ATOM   16119 N  N   . PRO D  1 461 ? -73.816 3.549   31.096  1.00 67.03  ? 461  PRO D N   1 
ATOM   16120 C  CA  . PRO D  1 461 ? -74.723 2.952   32.087  1.00 67.96  ? 461  PRO D CA  1 
ATOM   16121 C  C   . PRO D  1 461 ? -74.653 1.428   32.151  1.00 67.66  ? 461  PRO D C   1 
ATOM   16122 O  O   . PRO D  1 461 ? -75.074 0.824   33.140  1.00 68.06  ? 461  PRO D O   1 
ATOM   16123 C  CB  . PRO D  1 461 ? -76.107 3.411   31.617  1.00 74.73  ? 461  PRO D CB  1 
ATOM   16124 C  CG  . PRO D  1 461 ? -75.838 4.563   30.682  1.00 74.18  ? 461  PRO D CG  1 
ATOM   16125 C  CD  . PRO D  1 461 ? -74.561 4.199   30.008  1.00 71.52  ? 461  PRO D CD  1 
ATOM   16126 N  N   . SER D  1 462 ? -74.124 0.813   31.103  1.00 71.61  ? 462  SER D N   1 
ATOM   16127 C  CA  . SER D  1 462 ? -73.959 -0.633  31.078  1.00 76.21  ? 462  SER D CA  1 
ATOM   16128 C  C   . SER D  1 462 ? -72.765 -1.083  31.923  1.00 78.91  ? 462  SER D C   1 
ATOM   16129 O  O   . SER D  1 462 ? -72.510 -2.282  32.063  1.00 79.61  ? 462  SER D O   1 
ATOM   16130 C  CB  . SER D  1 462 ? -73.804 -1.128  29.637  1.00 78.17  ? 462  SER D CB  1 
ATOM   16131 O  OG  . SER D  1 462 ? -72.732 -0.477  28.974  1.00 75.40  ? 462  SER D OG  1 
ATOM   16132 N  N   . LEU D  1 463 ? -72.022 -0.119  32.461  1.00 95.32  ? 463  LEU D N   1 
ATOM   16133 C  CA  . LEU D  1 463 ? -70.792 -0.421  33.189  1.00 94.40  ? 463  LEU D CA  1 
ATOM   16134 C  C   . LEU D  1 463 ? -70.949 -0.507  34.703  1.00 99.12  ? 463  LEU D C   1 
ATOM   16135 O  O   . LEU D  1 463 ? -69.990 -0.833  35.410  1.00 101.11 ? 463  LEU D O   1 
ATOM   16136 C  CB  . LEU D  1 463 ? -69.698 0.583   32.832  1.00 64.43  ? 463  LEU D CB  1 
ATOM   16137 C  CG  . LEU D  1 463 ? -69.321 0.548   31.356  1.00 59.58  ? 463  LEU D CG  1 
ATOM   16138 C  CD1 . LEU D  1 463 ? -68.041 1.331   31.105  1.00 57.26  ? 463  LEU D CD1 1 
ATOM   16139 C  CD2 . LEU D  1 463 ? -69.184 -0.896  30.904  1.00 58.47  ? 463  LEU D CD2 1 
ATOM   16140 N  N   . ASN D  1 464 ? -72.151 -0.215  35.192  1.00 71.12  ? 464  ASN D N   1 
ATOM   16141 C  CA  . ASN D  1 464 ? -72.487 -0.434  36.598  1.00 73.69  ? 464  ASN D CA  1 
ATOM   16142 C  C   . ASN D  1 464 ? -71.682 0.419   37.594  1.00 66.83  ? 464  ASN D C   1 
ATOM   16143 O  O   . ASN D  1 464 ? -71.451 0.013   38.738  1.00 65.56  ? 464  ASN D O   1 
ATOM   16144 C  CB  . ASN D  1 464 ? -72.387 -1.931  36.948  1.00 104.50 ? 464  ASN D CB  1 
ATOM   16145 C  CG  . ASN D  1 464 ? -73.280 -2.804  36.064  1.00 116.30 ? 464  ASN D CG  1 
ATOM   16146 O  OD1 . ASN D  1 464 ? -73.810 -2.344  35.048  1.00 118.00 ? 464  ASN D OD1 1 
ATOM   16147 N  ND2 . ASN D  1 464 ? -73.453 -4.071  36.457  1.00 125.52 ? 464  ASN D ND2 1 
ATOM   16148 N  N   . TYR D  1 465 ? -71.244 1.596   37.160  1.00 71.88  ? 465  TYR D N   1 
ATOM   16149 C  CA  . TYR D  1 465 ? -70.618 2.532   38.084  1.00 68.75  ? 465  TYR D CA  1 
ATOM   16150 C  C   . TYR D  1 465 ? -71.754 3.213   38.818  1.00 67.28  ? 465  TYR D C   1 
ATOM   16151 O  O   . TYR D  1 465 ? -72.865 3.277   38.294  1.00 69.54  ? 465  TYR D O   1 
ATOM   16152 C  CB  . TYR D  1 465 ? -69.739 3.558   37.351  1.00 72.06  ? 465  TYR D CB  1 
ATOM   16153 C  CG  . TYR D  1 465 ? -68.408 3.010   36.860  1.00 70.72  ? 465  TYR D CG  1 
ATOM   16154 C  CD1 . TYR D  1 465 ? -68.297 2.405   35.612  1.00 70.88  ? 465  TYR D CD1 1 
ATOM   16155 C  CD2 . TYR D  1 465 ? -67.261 3.095   37.643  1.00 70.16  ? 465  TYR D CD2 1 
ATOM   16156 C  CE1 . TYR D  1 465 ? -67.078 1.898   35.156  1.00 69.68  ? 465  TYR D CE1 1 
ATOM   16157 C  CE2 . TYR D  1 465 ? -66.032 2.588   37.194  1.00 68.41  ? 465  TYR D CE2 1 
ATOM   16158 C  CZ  . TYR D  1 465 ? -65.949 1.993   35.949  1.00 67.36  ? 465  TYR D CZ  1 
ATOM   16159 O  OH  . TYR D  1 465 ? -64.749 1.488   35.491  1.00 63.15  ? 465  TYR D OH  1 
ATOM   16160 N  N   . THR D  1 466 ? -71.489 3.699   40.030  1.00 54.21  ? 466  THR D N   1 
ATOM   16161 C  CA  . THR D  1 466 ? -72.504 4.405   40.814  1.00 56.17  ? 466  THR D CA  1 
ATOM   16162 C  C   . THR D  1 466 ? -72.676 5.846   40.349  1.00 55.99  ? 466  THR D C   1 
ATOM   16163 O  O   . THR D  1 466 ? -71.935 6.328   39.498  1.00 54.02  ? 466  THR D O   1 
ATOM   16164 C  CB  . THR D  1 466 ? -72.127 4.436   42.286  1.00 75.22  ? 466  THR D CB  1 
ATOM   16165 O  OG1 . THR D  1 466 ? -71.128 5.443   42.492  1.00 75.89  ? 466  THR D OG1 1 
ATOM   16166 C  CG2 . THR D  1 466 ? -71.583 3.078   42.708  1.00 75.89  ? 466  THR D CG2 1 
ATOM   16167 N  N   . THR D  1 467 ? -73.640 6.548   40.928  1.00 69.81  ? 467  THR D N   1 
ATOM   16168 C  CA  . THR D  1 467 ? -73.984 7.871   40.417  1.00 73.15  ? 467  THR D CA  1 
ATOM   16169 C  C   . THR D  1 467 ? -72.998 8.932   40.918  1.00 74.41  ? 467  THR D C   1 
ATOM   16170 O  O   . THR D  1 467 ? -72.719 9.927   40.223  1.00 72.44  ? 467  THR D O   1 
ATOM   16171 C  CB  . THR D  1 467 ? -75.463 8.220   40.693  1.00 83.43  ? 467  THR D CB  1 
ATOM   16172 O  OG1 . THR D  1 467 ? -75.997 7.293   41.647  1.00 87.34  ? 467  THR D OG1 1 
ATOM   16173 C  CG2 . THR D  1 467 ? -76.281 8.107   39.402  1.00 83.00  ? 467  THR D CG2 1 
ATOM   16174 N  N   . GLU D  1 468 ? -72.453 8.690   42.111  1.00 85.97  ? 468  GLU D N   1 
ATOM   16175 C  CA  . GLU D  1 468 ? -71.322 9.466   42.612  1.00 85.86  ? 468  GLU D CA  1 
ATOM   16176 C  C   . GLU D  1 468 ? -70.224 9.360   41.584  1.00 79.04  ? 468  GLU D C   1 
ATOM   16177 O  O   . GLU D  1 468 ? -69.734 10.362  41.076  1.00 77.97  ? 468  GLU D O   1 
ATOM   16178 C  CB  . GLU D  1 468 ? -70.791 8.903   43.934  1.00 93.88  ? 468  GLU D CB  1 
ATOM   16179 C  CG  . GLU D  1 468 ? -71.570 9.289   45.175  1.00 100.69 ? 468  GLU D CG  1 
ATOM   16180 C  CD  . GLU D  1 468 ? -72.719 8.336   45.473  1.00 107.15 ? 468  GLU D CD  1 
ATOM   16181 O  OE1 . GLU D  1 468 ? -73.016 7.447   44.636  1.00 106.74 ? 468  GLU D OE1 1 
ATOM   16182 O  OE2 . GLU D  1 468 ? -73.328 8.478   46.556  1.00 111.37 ? 468  GLU D OE2 1 
ATOM   16183 N  N   . GLU D  1 469 ? -69.860 8.120   41.275  1.00 68.81  ? 469  GLU D N   1 
ATOM   16184 C  CA  . GLU D  1 469 ? -68.768 7.836   40.356  1.00 62.44  ? 469  GLU D CA  1 
ATOM   16185 C  C   . GLU D  1 469 ? -68.940 8.509   39.001  1.00 58.93  ? 469  GLU D C   1 
ATOM   16186 O  O   . GLU D  1 469 ? -67.966 8.974   38.417  1.00 56.42  ? 469  GLU D O   1 
ATOM   16187 C  CB  . GLU D  1 469 ? -68.582 6.329   40.201  1.00 50.34  ? 469  GLU D CB  1 
ATOM   16188 C  CG  . GLU D  1 469 ? -68.186 5.663   41.493  1.00 49.33  ? 469  GLU D CG  1 
ATOM   16189 C  CD  . GLU D  1 469 ? -67.816 4.219   41.306  1.00 49.38  ? 469  GLU D CD  1 
ATOM   16190 O  OE1 . GLU D  1 469 ? -68.624 3.483   40.709  1.00 50.87  ? 469  GLU D OE1 1 
ATOM   16191 O  OE2 . GLU D  1 469 ? -66.714 3.820   41.745  1.00 47.57  ? 469  GLU D OE2 1 
ATOM   16192 N  N   . ARG D  1 470 ? -70.175 8.567   38.510  1.00 52.80  ? 470  ARG D N   1 
ATOM   16193 C  CA  . ARG D  1 470 ? -70.454 9.245   37.253  1.00 54.26  ? 470  ARG D CA  1 
ATOM   16194 C  C   . ARG D  1 470 ? -70.171 10.737  37.419  1.00 53.19  ? 470  ARG D C   1 
ATOM   16195 O  O   . ARG D  1 470 ? -69.426 11.331  36.624  1.00 50.32  ? 470  ARG D O   1 
ATOM   16196 C  CB  . ARG D  1 470 ? -71.902 9.012   36.815  1.00 77.83  ? 470  ARG D CB  1 
ATOM   16197 C  CG  . ARG D  1 470 ? -72.194 9.417   35.376  1.00 83.89  ? 470  ARG D CG  1 
ATOM   16198 C  CD  . ARG D  1 470 ? -73.361 10.401  35.277  1.00 91.71  ? 470  ARG D CD  1 
ATOM   16199 N  NE  . ARG D  1 470 ? -74.625 9.818   35.721  1.00 99.94  ? 470  ARG D NE  1 
ATOM   16200 C  CZ  . ARG D  1 470 ? -75.720 10.523  36.003  1.00 106.35 ? 470  ARG D CZ  1 
ATOM   16201 N  NH1 . ARG D  1 470 ? -75.710 11.848  35.891  1.00 107.59 ? 470  ARG D NH1 1 
ATOM   16202 N  NH2 . ARG D  1 470 ? -76.827 9.905   36.407  1.00 109.16 ? 470  ARG D NH2 1 
ATOM   16203 N  N   . ILE D  1 471 ? -70.741 11.335  38.467  1.00 67.94  ? 471  ILE D N   1 
ATOM   16204 C  CA  . ILE D  1 471 ? -70.598 12.779  38.698  1.00 70.59  ? 471  ILE D CA  1 
ATOM   16205 C  C   . ILE D  1 471 ? -69.113 13.180  38.806  1.00 69.05  ? 471  ILE D C   1 
ATOM   16206 O  O   . ILE D  1 471 ? -68.661 14.207  38.256  1.00 66.41  ? 471  ILE D O   1 
ATOM   16207 C  CB  . ILE D  1 471 ? -71.461 13.235  39.928  1.00 58.80  ? 471  ILE D CB  1 
ATOM   16208 C  CG1 . ILE D  1 471 ? -72.227 14.518  39.607  1.00 61.73  ? 471  ILE D CG1 1 
ATOM   16209 C  CG2 . ILE D  1 471 ? -70.639 13.369  41.210  1.00 57.72  ? 471  ILE D CG2 1 
ATOM   16210 C  CD1 . ILE D  1 471 ? -73.055 14.420  38.350  1.00 63.91  ? 471  ILE D CD1 1 
ATOM   16211 N  N   . PHE D  1 472 ? -68.364 12.298  39.464  1.00 71.64  ? 472  PHE D N   1 
ATOM   16212 C  CA  . PHE D  1 472 ? -66.940 12.427  39.721  1.00 66.62  ? 472  PHE D CA  1 
ATOM   16213 C  C   . PHE D  1 472 ? -66.177 12.295  38.412  1.00 64.26  ? 472  PHE D C   1 
ATOM   16214 O  O   . PHE D  1 472 ? -65.233 13.047  38.147  1.00 61.40  ? 472  PHE D O   1 
ATOM   16215 C  CB  . PHE D  1 472 ? -66.539 11.326  40.716  1.00 53.00  ? 472  PHE D CB  1 
ATOM   16216 C  CG  . PHE D  1 472 ? -65.058 11.193  40.942  1.00 50.10  ? 472  PHE D CG  1 
ATOM   16217 C  CD1 . PHE D  1 472 ? -64.281 12.295  41.275  1.00 48.74  ? 472  PHE D CD1 1 
ATOM   16218 C  CD2 . PHE D  1 472 ? -64.447 9.947   40.865  1.00 49.22  ? 472  PHE D CD2 1 
ATOM   16219 C  CE1 . PHE D  1 472 ? -62.918 12.158  41.500  1.00 43.97  ? 472  PHE D CE1 1 
ATOM   16220 C  CE2 . PHE D  1 472 ? -63.089 9.808   41.086  1.00 41.58  ? 472  PHE D CE2 1 
ATOM   16221 C  CZ  . PHE D  1 472 ? -62.327 10.914  41.407  1.00 41.57  ? 472  PHE D CZ  1 
ATOM   16222 N  N   . ALA D  1 473 ? -66.617 11.344  37.590  1.00 64.53  ? 473  ALA D N   1 
ATOM   16223 C  CA  . ALA D  1 473 ? -65.999 11.075  36.301  1.00 61.54  ? 473  ALA D CA  1 
ATOM   16224 C  C   . ALA D  1 473 ? -66.060 12.319  35.444  1.00 65.12  ? 473  ALA D C   1 
ATOM   16225 O  O   . ALA D  1 473 ? -65.018 12.842  35.021  1.00 65.47  ? 473  ALA D O   1 
ATOM   16226 C  CB  . ALA D  1 473 ? -66.684 9.912   35.602  1.00 43.22  ? 473  ALA D CB  1 
ATOM   16227 N  N   . GLN D  1 474 ? -67.272 12.819  35.215  1.00 68.88  ? 474  GLN D N   1 
ATOM   16228 C  CA  . GLN D  1 474 ? -67.390 14.016  34.391  1.00 70.71  ? 474  GLN D CA  1 
ATOM   16229 C  C   . GLN D  1 474 ? -66.653 15.197  35.008  1.00 73.22  ? 474  GLN D C   1 
ATOM   16230 O  O   . GLN D  1 474 ? -66.114 16.037  34.281  1.00 75.09  ? 474  GLN D O   1 
ATOM   16231 C  CB  . GLN D  1 474 ? -68.838 14.360  34.023  1.00 59.92  ? 474  GLN D CB  1 
ATOM   16232 C  CG  . GLN D  1 474 ? -69.872 14.089  35.085  1.00 62.61  ? 474  GLN D CG  1 
ATOM   16233 C  CD  . GLN D  1 474 ? -71.285 14.119  34.517  1.00 64.84  ? 474  GLN D CD  1 
ATOM   16234 O  OE1 . GLN D  1 474 ? -72.275 13.987  35.250  1.00 67.55  ? 474  GLN D OE1 1 
ATOM   16235 N  NE2 . GLN D  1 474 ? -71.384 14.289  33.199  1.00 61.97  ? 474  GLN D NE2 1 
ATOM   16236 N  N   . ARG D  1 475 ? -66.593 15.242  36.337  1.00 72.62  ? 475  ARG D N   1 
ATOM   16237 C  CA  . ARG D  1 475 ? -65.781 16.266  36.988  1.00 71.71  ? 475  ARG D CA  1 
ATOM   16238 C  C   . ARG D  1 475 ? -64.325 16.197  36.537  1.00 68.95  ? 475  ARG D C   1 
ATOM   16239 O  O   . ARG D  1 475 ? -63.730 17.216  36.152  1.00 69.95  ? 475  ARG D O   1 
ATOM   16240 C  CB  . ARG D  1 475 ? -65.860 16.145  38.505  1.00 67.42  ? 475  ARG D CB  1 
ATOM   16241 C  CG  . ARG D  1 475 ? -64.898 17.049  39.237  1.00 67.05  ? 475  ARG D CG  1 
ATOM   16242 C  CD  . ARG D  1 475 ? -65.365 17.243  40.656  1.00 70.95  ? 475  ARG D CD  1 
ATOM   16243 N  NE  . ARG D  1 475 ? -64.249 17.420  41.573  1.00 73.43  ? 475  ARG D NE  1 
ATOM   16244 C  CZ  . ARG D  1 475 ? -63.991 16.613  42.597  1.00 74.52  ? 475  ARG D CZ  1 
ATOM   16245 N  NH1 . ARG D  1 475 ? -64.778 15.570  42.841  1.00 74.04  ? 475  ARG D NH1 1 
ATOM   16246 N  NH2 . ARG D  1 475 ? -62.948 16.855  43.380  1.00 74.80  ? 475  ARG D NH2 1 
ATOM   16247 N  N   . LEU D  1 476 ? -63.759 14.992  36.575  1.00 60.37  ? 476  LEU D N   1 
ATOM   16248 C  CA  . LEU D  1 476 ? -62.356 14.805  36.213  1.00 54.51  ? 476  LEU D CA  1 
ATOM   16249 C  C   . LEU D  1 476 ? -62.096 15.103  34.739  1.00 52.24  ? 476  LEU D C   1 
ATOM   16250 O  O   . LEU D  1 476 ? -61.074 15.711  34.395  1.00 49.89  ? 476  LEU D O   1 
ATOM   16251 C  CB  . LEU D  1 476 ? -61.845 13.411  36.603  1.00 39.42  ? 476  LEU D CB  1 
ATOM   16252 C  CG  . LEU D  1 476 ? -61.460 13.241  38.082  1.00 38.14  ? 476  LEU D CG  1 
ATOM   16253 C  CD1 . LEU D  1 476 ? -60.338 12.235  38.273  1.00 36.63  ? 476  LEU D CD1 1 
ATOM   16254 C  CD2 . LEU D  1 476 ? -61.087 14.565  38.712  1.00 38.42  ? 476  LEU D CD2 1 
ATOM   16255 N  N   . MET D  1 477 ? -63.025 14.694  33.877  1.00 52.31  ? 477  MET D N   1 
ATOM   16256 C  CA  . MET D  1 477 ? -62.926 15.029  32.457  1.00 50.38  ? 477  MET D CA  1 
ATOM   16257 C  C   . MET D  1 477 ? -62.891 16.534  32.261  1.00 52.36  ? 477  MET D C   1 
ATOM   16258 O  O   . MET D  1 477 ? -62.077 17.050  31.485  1.00 51.50  ? 477  MET D O   1 
ATOM   16259 C  CB  . MET D  1 477 ? -64.087 14.440  31.668  1.00 41.02  ? 477  MET D CB  1 
ATOM   16260 C  CG  . MET D  1 477 ? -64.161 12.936  31.735  1.00 40.68  ? 477  MET D CG  1 
ATOM   16261 S  SD  . MET D  1 477 ? -65.436 12.326  30.642  1.00 63.19  ? 477  MET D SD  1 
ATOM   16262 C  CE  . MET D  1 477 ? -66.685 13.568  30.948  1.00 103.71 ? 477  MET D CE  1 
ATOM   16263 N  N   . LYS D  1 478 ? -63.777 17.231  32.971  1.00 57.72  ? 478  LYS D N   1 
ATOM   16264 C  CA  . LYS D  1 478 ? -63.770 18.687  32.971  1.00 61.01  ? 478  LYS D CA  1 
ATOM   16265 C  C   . LYS D  1 478 ? -62.390 19.212  33.339  1.00 60.45  ? 478  LYS D C   1 
ATOM   16266 O  O   . LYS D  1 478 ? -61.860 20.078  32.636  1.00 62.14  ? 478  LYS D O   1 
ATOM   16267 C  CB  . LYS D  1 478 ? -64.824 19.257  33.928  1.00 66.97  ? 478  LYS D CB  1 
ATOM   16268 C  CG  . LYS D  1 478 ? -66.247 19.311  33.357  1.00 70.94  ? 478  LYS D CG  1 
ATOM   16269 C  CD  . LYS D  1 478 ? -66.415 20.408  32.307  1.00 70.45  ? 478  LYS D CD  1 
ATOM   16270 C  CE  . LYS D  1 478 ? -66.234 21.791  32.904  1.00 69.91  ? 478  LYS D CE  1 
ATOM   16271 N  NZ  . LYS D  1 478 ? -66.282 22.828  31.841  1.00 70.14  ? 478  LYS D NZ  1 
ATOM   16272 N  N   . TYR D  1 479 ? -61.803 18.679  34.419  1.00 49.03  ? 479  TYR D N   1 
ATOM   16273 C  CA  . TYR D  1 479 ? -60.474 19.137  34.856  1.00 42.17  ? 479  TYR D CA  1 
ATOM   16274 C  C   . TYR D  1 479 ? -59.472 18.996  33.733  1.00 38.18  ? 479  TYR D C   1 
ATOM   16275 O  O   . TYR D  1 479 ? -58.870 19.981  33.303  1.00 35.55  ? 479  TYR D O   1 
ATOM   16276 C  CB  . TYR D  1 479 ? -59.965 18.362  36.072  1.00 41.34  ? 479  TYR D CB  1 
ATOM   16277 C  CG  . TYR D  1 479 ? -60.600 18.752  37.382  1.00 46.68  ? 479  TYR D CG  1 
ATOM   16278 C  CD1 . TYR D  1 479 ? -61.430 19.858  37.479  1.00 51.26  ? 479  TYR D CD1 1 
ATOM   16279 C  CD2 . TYR D  1 479 ? -60.371 18.008  38.527  1.00 49.04  ? 479  TYR D CD2 1 
ATOM   16280 C  CE1 . TYR D  1 479 ? -62.023 20.207  38.682  1.00 54.05  ? 479  TYR D CE1 1 
ATOM   16281 C  CE2 . TYR D  1 479 ? -60.954 18.349  39.736  1.00 51.97  ? 479  TYR D CE2 1 
ATOM   16282 C  CZ  . TYR D  1 479 ? -61.778 19.450  39.810  1.00 53.99  ? 479  TYR D CZ  1 
ATOM   16283 O  OH  . TYR D  1 479 ? -62.354 19.788  41.018  1.00 55.92  ? 479  TYR D OH  1 
ATOM   16284 N  N   . TRP D  1 480 ? -59.335 17.764  33.246  1.00 39.96  ? 480  TRP D N   1 
ATOM   16285 C  CA  . TRP D  1 480 ? -58.308 17.401  32.268  1.00 37.44  ? 480  TRP D CA  1 
ATOM   16286 C  C   . TRP D  1 480 ? -58.413 18.187  30.979  1.00 37.72  ? 480  TRP D C   1 
ATOM   16287 O  O   . TRP D  1 480 ? -57.414 18.710  30.488  1.00 35.37  ? 480  TRP D O   1 
ATOM   16288 C  CB  . TRP D  1 480 ? -58.400 15.919  31.933  1.00 32.55  ? 480  TRP D CB  1 
ATOM   16289 C  CG  . TRP D  1 480 ? -57.375 15.046  32.580  1.00 31.38  ? 480  TRP D CG  1 
ATOM   16290 C  CD1 . TRP D  1 480 ? -56.531 14.185  31.950  1.00 30.02  ? 480  TRP D CD1 1 
ATOM   16291 C  CD2 . TRP D  1 480 ? -57.106 14.922  33.983  1.00 36.62  ? 480  TRP D CD2 1 
ATOM   16292 N  NE1 . TRP D  1 480 ? -55.755 13.526  32.867  1.00 34.21  ? 480  TRP D NE1 1 
ATOM   16293 C  CE2 . TRP D  1 480 ? -56.082 13.965  34.124  1.00 36.08  ? 480  TRP D CE2 1 
ATOM   16294 C  CE3 . TRP D  1 480 ? -57.634 15.523  35.134  1.00 32.88  ? 480  TRP D CE3 1 
ATOM   16295 C  CZ2 . TRP D  1 480 ? -55.560 13.605  35.375  1.00 37.44  ? 480  TRP D CZ2 1 
ATOM   16296 C  CZ3 . TRP D  1 480 ? -57.124 15.162  36.370  1.00 32.78  ? 480  TRP D CZ3 1 
ATOM   16297 C  CH2 . TRP D  1 480 ? -56.093 14.217  36.481  1.00 39.91  ? 480  TRP D CH2 1 
ATOM   16298 N  N   . THR D  1 481 ? -59.617 18.252  30.420  1.00 41.68  ? 481  THR D N   1 
ATOM   16299 C  CA  . THR D  1 481 ? -59.806 18.972  29.168  1.00 44.89  ? 481  THR D CA  1 
ATOM   16300 C  C   . THR D  1 481 ? -59.689 20.480  29.359  1.00 50.19  ? 481  THR D C   1 
ATOM   16301 O  O   . THR D  1 481 ? -59.310 21.191  28.428  1.00 50.78  ? 481  THR D O   1 
ATOM   16302 C  CB  . THR D  1 481 ? -61.142 18.643  28.516  1.00 45.45  ? 481  THR D CB  1 
ATOM   16303 O  OG1 . THR D  1 481 ? -62.212 19.038  29.388  1.00 47.83  ? 481  THR D OG1 1 
ATOM   16304 C  CG2 . THR D  1 481 ? -61.214 17.153  28.227  1.00 43.60  ? 481  THR D CG2 1 
ATOM   16305 N  N   . ASN D  1 482 ? -60.016 20.971  30.555  1.00 54.61  ? 482  ASN D N   1 
ATOM   16306 C  CA  . ASN D  1 482 ? -59.742 22.371  30.880  1.00 56.16  ? 482  ASN D CA  1 
ATOM   16307 C  C   . ASN D  1 482 ? -58.247 22.640  30.856  1.00 54.41  ? 482  ASN D C   1 
ATOM   16308 O  O   . ASN D  1 482 ? -57.803 23.679  30.370  1.00 51.90  ? 482  ASN D O   1 
ATOM   16309 C  CB  . ASN D  1 482 ? -60.318 22.767  32.239  1.00 62.83  ? 482  ASN D CB  1 
ATOM   16310 C  CG  . ASN D  1 482 ? -61.755 23.221  32.149  1.00 69.93  ? 482  ASN D CG  1 
ATOM   16311 O  OD1 . ASN D  1 482 ? -62.271 23.491  31.057  1.00 72.44  ? 482  ASN D OD1 1 
ATOM   16312 N  ND2 . ASN D  1 482 ? -62.415 23.318  33.300  1.00 72.44  ? 482  ASN D ND2 1 
ATOM   16313 N  N   . PHE D  1 483 ? -57.471 21.698  31.384  1.00 64.75  ? 483  PHE D N   1 
ATOM   16314 C  CA  . PHE D  1 483 ? -56.023 21.831  31.339  1.00 61.29  ? 483  PHE D CA  1 
ATOM   16315 C  C   . PHE D  1 483 ? -55.580 21.826  29.896  1.00 60.30  ? 483  PHE D C   1 
ATOM   16316 O  O   . PHE D  1 483 ? -54.798 22.673  29.482  1.00 62.23  ? 483  PHE D O   1 
ATOM   16317 C  CB  . PHE D  1 483 ? -55.319 20.710  32.101  1.00 47.99  ? 483  PHE D CB  1 
ATOM   16318 C  CG  . PHE D  1 483 ? -53.821 20.768  31.994  1.00 47.22  ? 483  PHE D CG  1 
ATOM   16319 C  CD1 . PHE D  1 483 ? -53.104 21.735  32.673  1.00 48.45  ? 483  PHE D CD1 1 
ATOM   16320 C  CD2 . PHE D  1 483 ? -53.130 19.871  31.198  1.00 45.94  ? 483  PHE D CD2 1 
ATOM   16321 C  CE1 . PHE D  1 483 ? -51.717 21.795  32.565  1.00 47.86  ? 483  PHE D CE1 1 
ATOM   16322 C  CE2 . PHE D  1 483 ? -51.749 19.927  31.089  1.00 44.87  ? 483  PHE D CE2 1 
ATOM   16323 C  CZ  . PHE D  1 483 ? -51.044 20.887  31.775  1.00 45.91  ? 483  PHE D CZ  1 
ATOM   16324 N  N   . ALA D  1 484 ? -56.105 20.874  29.135  1.00 51.36  ? 484  ALA D N   1 
ATOM   16325 C  CA  . ALA D  1 484 ? -55.749 20.707  27.733  1.00 49.17  ? 484  ALA D CA  1 
ATOM   16326 C  C   . ALA D  1 484 ? -55.969 22.000  26.964  1.00 54.31  ? 484  ALA D C   1 
ATOM   16327 O  O   . ALA D  1 484 ? -55.120 22.422  26.175  1.00 54.38  ? 484  ALA D O   1 
ATOM   16328 C  CB  . ALA D  1 484 ? -56.565 19.594  27.125  1.00 31.15  ? 484  ALA D CB  1 
ATOM   16329 N  N   . ARG D  1 485 ? -57.109 22.628  27.239  1.00 45.03  ? 485  ARG D N   1 
ATOM   16330 C  CA  . ARG D  1 485 ? -57.575 23.817  26.538  1.00 46.33  ? 485  ARG D CA  1 
ATOM   16331 C  C   . ARG D  1 485 ? -56.808 25.069  26.976  1.00 45.16  ? 485  ARG D C   1 
ATOM   16332 O  O   . ARG D  1 485 ? -56.106 25.682  26.171  1.00 43.88  ? 485  ARG D O   1 
ATOM   16333 C  CB  . ARG D  1 485 ? -59.070 23.977  26.811  1.00 68.68  ? 485  ARG D CB  1 
ATOM   16334 C  CG  . ARG D  1 485 ? -59.776 25.091  26.076  1.00 77.61  ? 485  ARG D CG  1 
ATOM   16335 C  CD  . ARG D  1 485 ? -61.181 25.333  26.662  1.00 86.00  ? 485  ARG D CD  1 
ATOM   16336 N  NE  . ARG D  1 485 ? -61.690 24.209  27.460  1.00 91.48  ? 485  ARG D NE  1 
ATOM   16337 C  CZ  . ARG D  1 485 ? -62.356 23.159  26.972  1.00 93.84  ? 485  ARG D CZ  1 
ATOM   16338 N  NH1 . ARG D  1 485 ? -62.599 23.055  25.667  1.00 93.23  ? 485  ARG D NH1 1 
ATOM   16339 N  NH2 . ARG D  1 485 ? -62.774 22.200  27.795  1.00 93.78  ? 485  ARG D NH2 1 
ATOM   16340 N  N   . THR D  1 486 ? -56.972 25.459  28.242  1.00 50.59  ? 486  THR D N   1 
ATOM   16341 C  CA  . THR D  1 486 ? -56.371 26.688  28.778  1.00 51.83  ? 486  THR D CA  1 
ATOM   16342 C  C   . THR D  1 486 ? -55.024 26.560  29.471  1.00 46.47  ? 486  THR D C   1 
ATOM   16343 O  O   . THR D  1 486 ? -54.349 27.566  29.657  1.00 45.66  ? 486  THR D O   1 
ATOM   16344 C  CB  . THR D  1 486 ? -57.275 27.330  29.847  1.00 74.10  ? 486  THR D CB  1 
ATOM   16345 O  OG1 . THR D  1 486 ? -57.072 26.664  31.100  1.00 72.73  ? 486  THR D OG1 1 
ATOM   16346 C  CG2 . THR D  1 486 ? -58.756 27.254  29.450  1.00 81.48  ? 486  THR D CG2 1 
ATOM   16347 N  N   . GLY D  1 487 ? -54.628 25.343  29.843  1.00 43.13  ? 487  GLY D N   1 
ATOM   16348 C  CA  . GLY D  1 487 ? -53.440 25.145  30.669  1.00 40.65  ? 487  GLY D CA  1 
ATOM   16349 C  C   . GLY D  1 487 ? -53.652 25.333  32.170  1.00 41.83  ? 487  GLY D C   1 
ATOM   16350 O  O   . GLY D  1 487 ? -52.702 25.513  32.929  1.00 37.76  ? 487  GLY D O   1 
ATOM   16351 N  N   . ASP D  1 488 ? -54.907 25.319  32.600  1.00 57.17  ? 488  ASP D N   1 
ATOM   16352 C  CA  . ASP D  1 488 ? -55.228 25.391  34.015  1.00 60.70  ? 488  ASP D CA  1 
ATOM   16353 C  C   . ASP D  1 488 ? -56.359 24.402  34.215  1.00 56.91  ? 488  ASP D C   1 
ATOM   16354 O  O   . ASP D  1 488 ? -57.322 24.414  33.454  1.00 60.20  ? 488  ASP D O   1 
ATOM   16355 C  CB  . ASP D  1 488 ? -55.706 26.817  34.313  1.00 70.43  ? 488  ASP D CB  1 
ATOM   16356 C  CG  . ASP D  1 488 ? -56.010 27.062  35.776  1.00 78.04  ? 488  ASP D CG  1 
ATOM   16357 O  OD1 . ASP D  1 488 ? -56.625 26.191  36.423  1.00 81.25  ? 488  ASP D OD1 1 
ATOM   16358 O  OD2 . ASP D  1 488 ? -55.654 28.155  36.274  1.00 80.01  ? 488  ASP D OD2 1 
ATOM   16359 N  N   . PRO D  1 489 ? -56.284 23.580  35.268  1.00 42.60  ? 489  PRO D N   1 
ATOM   16360 C  CA  . PRO D  1 489 ? -57.356 22.598  35.472  1.00 43.45  ? 489  PRO D CA  1 
ATOM   16361 C  C   . PRO D  1 489 ? -58.729 23.177  35.863  1.00 49.19  ? 489  PRO D C   1 
ATOM   16362 O  O   . PRO D  1 489 ? -59.747 22.627  35.432  1.00 50.95  ? 489  PRO D O   1 
ATOM   16363 C  CB  . PRO D  1 489 ? -56.801 21.680  36.577  1.00 35.73  ? 489  PRO D CB  1 
ATOM   16364 C  CG  . PRO D  1 489 ? -55.626 22.396  37.150  1.00 35.24  ? 489  PRO D CG  1 
ATOM   16365 C  CD  . PRO D  1 489 ? -55.081 23.241  36.040  1.00 34.78  ? 489  PRO D CD  1 
ATOM   16366 N  N   . ASN D  1 490 ? -58.768 24.248  36.655  1.00 48.93  ? 490  ASN D N   1 
ATOM   16367 C  CA  . ASN D  1 490 ? -60.051 24.699  37.202  1.00 53.49  ? 490  ASN D CA  1 
ATOM   16368 C  C   . ASN D  1 490 ? -60.923 25.492  36.246  1.00 62.04  ? 490  ASN D C   1 
ATOM   16369 O  O   . ASN D  1 490 ? -60.436 26.077  35.275  1.00 59.26  ? 490  ASN D O   1 
ATOM   16370 C  CB  . ASN D  1 490 ? -59.931 25.420  38.563  1.00 51.89  ? 490  ASN D CB  1 
ATOM   16371 C  CG  . ASN D  1 490 ? -58.540 25.933  38.842  1.00 46.40  ? 490  ASN D CG  1 
ATOM   16372 O  OD1 . ASN D  1 490 ? -57.893 25.491  39.779  1.00 41.75  ? 490  ASN D OD1 1 
ATOM   16373 N  ND2 . ASN D  1 490 ? -58.078 26.877  38.040  1.00 47.03  ? 490  ASN D ND2 1 
ATOM   16374 N  N   . ASP D  1 491 ? -62.223 25.476  36.542  1.00 84.87  ? 491  ASP D N   1 
ATOM   16375 C  CA  . ASP D  1 491 ? -63.231 26.218  35.798  1.00 93.43  ? 491  ASP D CA  1 
ATOM   16376 C  C   . ASP D  1 491 ? -62.961 27.721  35.818  1.00 95.41  ? 491  ASP D C   1 
ATOM   16377 O  O   . ASP D  1 491 ? -62.763 28.308  36.887  1.00 95.45  ? 491  ASP D O   1 
ATOM   16378 C  CB  . ASP D  1 491 ? -64.618 25.930  36.376  1.00 108.75 ? 491  ASP D CB  1 
ATOM   16379 C  CG  . ASP D  1 491 ? -65.553 25.295  35.364  1.00 114.50 ? 491  ASP D CG  1 
ATOM   16380 O  OD1 . ASP D  1 491 ? -65.792 25.909  34.299  1.00 116.09 ? 491  ASP D OD1 1 
ATOM   16381 O  OD2 . ASP D  1 491 ? -66.053 24.183  35.639  1.00 116.56 ? 491  ASP D OD2 1 
ATOM   16382 N  N   . PRO D  1 492 ? -62.942 28.343  34.629  1.00 89.66  ? 492  PRO D N   1 
ATOM   16383 C  CA  . PRO D  1 492 ? -62.686 29.780  34.478  1.00 92.64  ? 492  PRO D CA  1 
ATOM   16384 C  C   . PRO D  1 492 ? -63.797 30.610  35.108  1.00 97.72  ? 492  PRO D C   1 
ATOM   16385 O  O   . PRO D  1 492 ? -63.524 31.566  35.838  1.00 96.34  ? 492  PRO D O   1 
ATOM   16386 C  CB  . PRO D  1 492 ? -62.692 29.987  32.958  1.00 94.11  ? 492  PRO D CB  1 
ATOM   16387 C  CG  . PRO D  1 492 ? -62.619 28.609  32.353  1.00 91.42  ? 492  PRO D CG  1 
ATOM   16388 C  CD  . PRO D  1 492 ? -63.268 27.704  33.340  1.00 90.99  ? 492  PRO D CD  1 
ATOM   16389 N  N   . ARG D  1 493 ? -65.042 30.219  34.835  0.91 117.57 ? 493  ARG D N   1 
ATOM   16390 C  CA  . ARG D  1 493 ? -66.211 30.953  35.314  0.91 124.68 ? 493  ARG D CA  1 
ATOM   16391 C  C   . ARG D  1 493 ? -66.458 30.745  36.800  0.91 130.65 ? 493  ARG D C   1 
ATOM   16392 O  O   . ARG D  1 493 ? -66.639 31.721  37.532  0.91 134.53 ? 493  ARG D O   1 
ATOM   16393 C  CB  . ARG D  1 493 ? -67.478 30.586  34.536  0.91 113.29 ? 493  ARG D CB  1 
ATOM   16394 C  CG  . ARG D  1 493 ? -67.528 31.084  33.103  0.91 113.16 ? 493  ARG D CG  1 
ATOM   16395 C  CD  . ARG D  1 493 ? -67.395 29.924  32.136  0.91 112.31 ? 493  ARG D CD  1 
ATOM   16396 N  NE  . ARG D  1 493 ? -67.652 28.647  32.799  0.91 112.70 ? 493  ARG D NE  1 
ATOM   16397 C  CZ  . ARG D  1 493 ? -68.845 28.064  32.881  0.91 114.17 ? 493  ARG D CZ  1 
ATOM   16398 N  NH1 . ARG D  1 493 ? -69.913 28.642  32.338  0.91 115.36 ? 493  ARG D NH1 1 
ATOM   16399 N  NH2 . ARG D  1 493 ? -68.967 26.902  33.513  0.91 113.60 ? 493  ARG D NH2 1 
ATOM   16400 N  N   . ASP D  1 494 ? -66.424 29.498  37.272  0.89 124.96 ? 494  ASP D N   1 
ATOM   16401 C  CA  . ASP D  1 494 ? -66.773 29.299  38.667  0.89 125.28 ? 494  ASP D CA  1 
ATOM   16402 C  C   . ASP D  1 494 ? -65.451 29.550  39.332  0.89 124.30 ? 494  ASP D C   1 
ATOM   16403 O  O   . ASP D  1 494 ? -64.613 28.653  39.452  0.89 121.46 ? 494  ASP D O   1 
ATOM   16404 C  CB  . ASP D  1 494 ? -67.189 27.840  38.941  0.89 115.38 ? 494  ASP D CB  1 
ATOM   16405 C  CG  . ASP D  1 494 ? -67.997 27.209  37.791  0.89 113.45 ? 494  ASP D CG  1 
ATOM   16406 O  OD1 . ASP D  1 494 ? -67.985 27.741  36.656  0.89 112.54 ? 494  ASP D OD1 1 
ATOM   16407 O  OD2 . ASP D  1 494 ? -68.643 26.161  38.026  0.89 112.37 ? 494  ASP D OD2 1 
ATOM   16408 N  N   . SER D  1 495 ? -65.298 30.779  39.815  0.91 129.36 ? 495  SER D N   1 
ATOM   16409 C  CA  . SER D  1 495 ? -64.059 31.197  40.445  0.91 130.62 ? 495  SER D CA  1 
ATOM   16410 C  C   . SER D  1 495 ? -64.246 31.018  41.937  0.91 133.07 ? 495  SER D C   1 
ATOM   16411 O  O   . SER D  1 495 ? -63.294 31.139  42.722  0.91 131.12 ? 495  SER D O   1 
ATOM   16412 C  CB  . SER D  1 495 ? -63.677 32.632  40.068  0.91 123.68 ? 495  SER D CB  1 
ATOM   16413 O  OG  . SER D  1 495 ? -62.275 32.737  39.856  0.91 120.01 ? 495  SER D OG  1 
ATOM   16414 N  N   . LYS D  1 496 ? -65.490 30.735  42.324  1.00 137.00 ? 496  LYS D N   1 
ATOM   16415 C  CA  . LYS D  1 496 ? -65.674 30.007  43.560  1.00 135.35 ? 496  LYS D CA  1 
ATOM   16416 C  C   . LYS D  1 496 ? -66.259 28.627  43.259  1.00 132.16 ? 496  LYS D C   1 
ATOM   16417 O  O   . LYS D  1 496 ? -67.447 28.442  42.990  1.00 131.40 ? 496  LYS D O   1 
ATOM   16418 C  CB  . LYS D  1 496 ? -66.496 30.792  44.593  1.00 126.34 ? 496  LYS D CB  1 
ATOM   16419 C  CG  . LYS D  1 496 ? -66.129 30.476  46.062  1.00 125.27 ? 496  LYS D CG  1 
ATOM   16420 C  CD  . LYS D  1 496 ? -64.666 30.818  46.419  1.00 123.36 ? 496  LYS D CD  1 
ATOM   16421 C  CE  . LYS D  1 496 ? -63.701 29.605  46.337  1.00 80.12  ? 496  LYS D CE  1 
ATOM   16422 N  NZ  . LYS D  1 496 ? -63.988 28.512  47.319  1.00 79.45  ? 496  LYS D NZ  1 
ATOM   16423 N  N   . SER D  1 497 ? -65.320 27.693  43.254  1.00 135.84 ? 497  SER D N   1 
ATOM   16424 C  CA  . SER D  1 497 ? -65.443 26.282  43.528  1.00 131.79 ? 497  SER D CA  1 
ATOM   16425 C  C   . SER D  1 497 ? -64.014 26.198  44.050  1.00 129.70 ? 497  SER D C   1 
ATOM   16426 O  O   . SER D  1 497 ? -63.231 27.102  43.754  1.00 132.92 ? 497  SER D O   1 
ATOM   16427 C  CB  . SER D  1 497 ? -65.626 25.495  42.237  1.00 105.94 ? 497  SER D CB  1 
ATOM   16428 O  OG  . SER D  1 497 ? -65.901 24.130  42.508  1.00 103.67 ? 497  SER D OG  1 
ATOM   16429 N  N   . PRO D  1 498 ? -63.656 25.183  44.855  1.00 109.59 ? 498  PRO D N   1 
ATOM   16430 C  CA  . PRO D  1 498 ? -62.264 25.258  45.334  1.00 101.86 ? 498  PRO D CA  1 
ATOM   16431 C  C   . PRO D  1 498 ? -61.225 25.227  44.193  1.00 94.21  ? 498  PRO D C   1 
ATOM   16432 O  O   . PRO D  1 498 ? -61.281 24.377  43.300  1.00 91.47  ? 498  PRO D O   1 
ATOM   16433 C  CB  . PRO D  1 498 ? -62.135 24.036  46.250  1.00 93.82  ? 498  PRO D CB  1 
ATOM   16434 C  CG  . PRO D  1 498 ? -63.197 23.093  45.774  1.00 96.57  ? 498  PRO D CG  1 
ATOM   16435 C  CD  . PRO D  1 498 ? -64.336 23.951  45.288  1.00 100.95 ? 498  PRO D CD  1 
ATOM   16436 N  N   . GLN D  1 499 ? -60.300 26.184  44.226  1.00 91.73  ? 499  GLN D N   1 
ATOM   16437 C  CA  . GLN D  1 499 ? -59.301 26.347  43.171  1.00 85.51  ? 499  GLN D CA  1 
ATOM   16438 C  C   . GLN D  1 499 ? -58.158 25.344  43.338  1.00 78.80  ? 499  GLN D C   1 
ATOM   16439 O  O   . GLN D  1 499 ? -57.764 25.007  44.451  1.00 79.16  ? 499  GLN D O   1 
ATOM   16440 C  CB  . GLN D  1 499 ? -58.757 27.789  43.160  1.00 81.13  ? 499  GLN D CB  1 
ATOM   16441 C  CG  . GLN D  1 499 ? -58.815 28.513  41.807  1.00 84.12  ? 499  GLN D CG  1 
ATOM   16442 C  CD  . GLN D  1 499 ? -60.238 28.871  41.371  1.00 90.93  ? 499  GLN D CD  1 
ATOM   16443 O  OE1 . GLN D  1 499 ? -61.207 28.518  42.038  1.00 95.59  ? 499  GLN D OE1 1 
ATOM   16444 N  NE2 . GLN D  1 499 ? -60.363 29.578  40.248  1.00 91.24  ? 499  GLN D NE2 1 
ATOM   16445 N  N   . TRP D  1 500 ? -57.632 24.868  42.218  1.00 67.59  ? 500  TRP D N   1 
ATOM   16446 C  CA  . TRP D  1 500 ? -56.490 23.969  42.217  1.00 57.94  ? 500  TRP D CA  1 
ATOM   16447 C  C   . TRP D  1 500 ? -55.246 24.845  42.103  1.00 53.35  ? 500  TRP D C   1 
ATOM   16448 O  O   . TRP D  1 500 ? -54.978 25.439  41.061  1.00 55.26  ? 500  TRP D O   1 
ATOM   16449 C  CB  . TRP D  1 500 ? -56.624 23.033  41.018  1.00 55.98  ? 500  TRP D CB  1 
ATOM   16450 C  CG  . TRP D  1 500 ? -55.640 21.912  40.901  1.00 53.48  ? 500  TRP D CG  1 
ATOM   16451 C  CD1 . TRP D  1 500 ? -54.360 21.878  41.366  1.00 54.65  ? 500  TRP D CD1 1 
ATOM   16452 C  CD2 . TRP D  1 500 ? -55.865 20.655  40.250  1.00 49.70  ? 500  TRP D CD2 1 
ATOM   16453 N  NE1 . TRP D  1 500 ? -53.775 20.672  41.048  1.00 53.98  ? 500  TRP D NE1 1 
ATOM   16454 C  CE2 . TRP D  1 500 ? -54.684 19.906  40.364  1.00 51.05  ? 500  TRP D CE2 1 
ATOM   16455 C  CE3 . TRP D  1 500 ? -56.958 20.090  39.589  1.00 47.15  ? 500  TRP D CE3 1 
ATOM   16456 C  CZ2 . TRP D  1 500 ? -54.569 18.625  39.846  1.00 48.14  ? 500  TRP D CZ2 1 
ATOM   16457 C  CZ3 . TRP D  1 500 ? -56.842 18.828  39.080  1.00 45.23  ? 500  TRP D CZ3 1 
ATOM   16458 C  CH2 . TRP D  1 500 ? -55.661 18.105  39.208  1.00 45.16  ? 500  TRP D CH2 1 
ATOM   16459 N  N   . PRO D  1 501 ? -54.487 24.949  43.191  1.00 39.71  ? 501  PRO D N   1 
ATOM   16460 C  CA  . PRO D  1 501 ? -53.307 25.814  43.212  1.00 39.49  ? 501  PRO D CA  1 
ATOM   16461 C  C   . PRO D  1 501 ? -52.213 25.230  42.347  1.00 45.36  ? 501  PRO D C   1 
ATOM   16462 O  O   . PRO D  1 501 ? -52.128 24.009  42.237  1.00 47.15  ? 501  PRO D O   1 
ATOM   16463 C  CB  . PRO D  1 501 ? -52.849 25.745  44.671  1.00 43.97  ? 501  PRO D CB  1 
ATOM   16464 C  CG  . PRO D  1 501 ? -54.009 25.151  45.434  1.00 44.84  ? 501  PRO D CG  1 
ATOM   16465 C  CD  . PRO D  1 501 ? -54.693 24.254  44.468  1.00 44.26  ? 501  PRO D CD  1 
ATOM   16466 N  N   . PRO D  1 502 ? -51.370 26.077  41.748  1.00 65.03  ? 502  PRO D N   1 
ATOM   16467 C  CA  . PRO D  1 502 ? -50.173 25.509  41.130  1.00 65.05  ? 502  PRO D CA  1 
ATOM   16468 C  C   . PRO D  1 502 ? -49.304 24.873  42.211  1.00 63.30  ? 502  PRO D C   1 
ATOM   16469 O  O   . PRO D  1 502 ? -49.459 25.187  43.391  1.00 69.06  ? 502  PRO D O   1 
ATOM   16470 C  CB  . PRO D  1 502 ? -49.473 26.735  40.542  1.00 68.61  ? 502  PRO D CB  1 
ATOM   16471 C  CG  . PRO D  1 502 ? -49.925 27.863  41.401  1.00 71.88  ? 502  PRO D CG  1 
ATOM   16472 C  CD  . PRO D  1 502 ? -51.362 27.547  41.714  1.00 72.12  ? 502  PRO D CD  1 
ATOM   16473 N  N   . TYR D  1 503 ? -48.419 23.971  41.816  1.00 37.79  ? 503  TYR D N   1 
ATOM   16474 C  CA  . TYR D  1 503 ? -47.456 23.406  42.743  1.00 34.70  ? 503  TYR D CA  1 
ATOM   16475 C  C   . TYR D  1 503 ? -46.141 24.171  42.568  1.00 37.71  ? 503  TYR D C   1 
ATOM   16476 O  O   . TYR D  1 503 ? -45.614 24.252  41.458  1.00 38.66  ? 503  TYR D O   1 
ATOM   16477 C  CB  . TYR D  1 503 ? -47.279 21.912  42.457  1.00 39.74  ? 503  TYR D CB  1 
ATOM   16478 C  CG  . TYR D  1 503 ? -46.172 21.221  43.228  1.00 41.21  ? 503  TYR D CG  1 
ATOM   16479 C  CD1 . TYR D  1 503 ? -44.837 21.336  42.832  1.00 42.32  ? 503  TYR D CD1 1 
ATOM   16480 C  CD2 . TYR D  1 503 ? -46.460 20.427  44.327  1.00 44.38  ? 503  TYR D CD2 1 
ATOM   16481 C  CE1 . TYR D  1 503 ? -43.814 20.701  43.533  1.00 44.03  ? 503  TYR D CE1 1 
ATOM   16482 C  CE2 . TYR D  1 503 ? -45.443 19.779  45.032  1.00 47.66  ? 503  TYR D CE2 1 
ATOM   16483 C  CZ  . TYR D  1 503 ? -44.121 19.920  44.630  1.00 46.75  ? 503  TYR D CZ  1 
ATOM   16484 O  OH  . TYR D  1 503 ? -43.110 19.284  45.330  1.00 46.46  ? 503  TYR D OH  1 
ATOM   16485 N  N   . THR D  1 504 ? -45.619 24.737  43.657  1.00 46.66  ? 504  THR D N   1 
ATOM   16486 C  CA  . THR D  1 504 ? -44.352 25.479  43.630  1.00 47.41  ? 504  THR D CA  1 
ATOM   16487 C  C   . THR D  1 504 ? -43.384 24.960  44.680  1.00 45.05  ? 504  THR D C   1 
ATOM   16488 O  O   . THR D  1 504 ? -43.792 24.299  45.629  1.00 45.02  ? 504  THR D O   1 
ATOM   16489 C  CB  . THR D  1 504 ? -44.587 26.943  43.928  1.00 61.51  ? 504  THR D CB  1 
ATOM   16490 O  OG1 . THR D  1 504 ? -45.341 27.054  45.144  1.00 62.44  ? 504  THR D OG1 1 
ATOM   16491 C  CG2 . THR D  1 504 ? -45.360 27.587  42.785  1.00 65.21  ? 504  THR D CG2 1 
ATOM   16492 N  N   . THR D  1 505 ? -42.103 25.267  44.537  1.00 49.59  ? 505  THR D N   1 
ATOM   16493 C  CA  . THR D  1 505 ? -41.132 24.707  45.469  1.00 53.44  ? 505  THR D CA  1 
ATOM   16494 C  C   . THR D  1 505 ? -41.342 25.264  46.862  1.00 58.68  ? 505  THR D C   1 
ATOM   16495 O  O   . THR D  1 505 ? -41.141 24.565  47.858  1.00 60.80  ? 505  THR D O   1 
ATOM   16496 C  CB  . THR D  1 505 ? -39.696 24.967  45.039  1.00 51.45  ? 505  THR D CB  1 
ATOM   16497 O  OG1 . THR D  1 505 ? -39.699 25.712  43.816  1.00 52.77  ? 505  THR D OG1 1 
ATOM   16498 C  CG2 . THR D  1 505 ? -38.968 23.644  44.834  1.00 49.19  ? 505  THR D CG2 1 
ATOM   16499 N  N   . ALA D  1 506 ? -41.743 26.529  46.926  1.00 56.79  ? 506  ALA D N   1 
ATOM   16500 C  CA  . ALA D  1 506 ? -42.059 27.152  48.202  1.00 55.65  ? 506  ALA D CA  1 
ATOM   16501 C  C   . ALA D  1 506 ? -43.157 26.390  48.947  1.00 53.17  ? 506  ALA D C   1 
ATOM   16502 O  O   . ALA D  1 506 ? -42.877 25.647  49.888  1.00 51.68  ? 506  ALA D O   1 
ATOM   16503 C  CB  . ALA D  1 506 ? -42.471 28.608  47.988  1.00 59.50  ? 506  ALA D CB  1 
ATOM   16504 N  N   . ALA D  1 507 ? -44.392 26.529  48.469  1.00 53.99  ? 507  ALA D N   1 
ATOM   16505 C  CA  . ALA D  1 507 ? -45.581 26.063  49.189  1.00 55.50  ? 507  ALA D CA  1 
ATOM   16506 C  C   . ALA D  1 507 ? -45.856 24.562  49.065  1.00 53.72  ? 507  ALA D C   1 
ATOM   16507 O  O   . ALA D  1 507 ? -46.373 23.940  50.003  1.00 53.15  ? 507  ALA D O   1 
ATOM   16508 C  CB  . ALA D  1 507 ? -46.797 26.859  48.740  1.00 62.93  ? 507  ALA D CB  1 
ATOM   16509 N  N   . GLN D  1 508 ? -45.518 24.010  47.896  1.00 49.39  ? 508  GLN D N   1 
ATOM   16510 C  CA  . GLN D  1 508 ? -45.682 22.591  47.563  1.00 44.41  ? 508  GLN D CA  1 
ATOM   16511 C  C   . GLN D  1 508 ? -47.097 22.080  47.730  1.00 41.25  ? 508  GLN D C   1 
ATOM   16512 O  O   . GLN D  1 508 ? -47.324 21.094  48.427  1.00 41.14  ? 508  GLN D O   1 
ATOM   16513 C  CB  . GLN D  1 508 ? -44.753 21.715  48.390  1.00 53.81  ? 508  GLN D CB  1 
ATOM   16514 C  CG  . GLN D  1 508 ? -43.339 22.200  48.495  1.00 59.42  ? 508  GLN D CG  1 
ATOM   16515 C  CD  . GLN D  1 508 ? -42.511 21.231  49.293  1.00 65.88  ? 508  GLN D CD  1 
ATOM   16516 O  OE1 . GLN D  1 508 ? -42.798 20.030  49.302  1.00 68.71  ? 508  GLN D OE1 1 
ATOM   16517 N  NE2 . GLN D  1 508 ? -41.490 21.737  49.986  1.00 67.08  ? 508  GLN D NE2 1 
ATOM   16518 N  N   . GLN D  1 509 ? -48.056 22.735  47.097  1.00 41.41  ? 509  GLN D N   1 
ATOM   16519 C  CA  . GLN D  1 509 ? -49.429 22.292  47.251  1.00 42.14  ? 509  GLN D CA  1 
ATOM   16520 C  C   . GLN D  1 509 ? -49.975 21.487  46.066  1.00 41.50  ? 509  GLN D C   1 
ATOM   16521 O  O   . GLN D  1 509 ? -49.807 21.852  44.900  1.00 42.15  ? 509  GLN D O   1 
ATOM   16522 C  CB  . GLN D  1 509 ? -50.332 23.467  47.600  1.00 48.06  ? 509  GLN D CB  1 
ATOM   16523 C  CG  . GLN D  1 509 ? -49.823 24.795  47.109  1.00 50.83  ? 509  GLN D CG  1 
ATOM   16524 C  CD  . GLN D  1 509 ? -50.582 25.956  47.721  1.00 57.36  ? 509  GLN D CD  1 
ATOM   16525 O  OE1 . GLN D  1 509 ? -51.536 25.761  48.483  1.00 59.36  ? 509  GLN D OE1 1 
ATOM   16526 N  NE2 . GLN D  1 509 ? -50.162 27.176  47.396  1.00 59.67  ? 509  GLN D NE2 1 
ATOM   16527 N  N   . TYR D  1 510 ? -50.637 20.386  46.399  1.00 40.38  ? 510  TYR D N   1 
ATOM   16528 C  CA  . TYR D  1 510 ? -51.273 19.504  45.430  1.00 37.85  ? 510  TYR D CA  1 
ATOM   16529 C  C   . TYR D  1 510 ? -52.690 19.263  45.926  1.00 39.54  ? 510  TYR D C   1 
ATOM   16530 O  O   . TYR D  1 510 ? -53.002 19.612  47.048  1.00 37.04  ? 510  TYR D O   1 
ATOM   16531 C  CB  . TYR D  1 510 ? -50.518 18.179  45.360  1.00 37.68  ? 510  TYR D CB  1 
ATOM   16532 C  CG  . TYR D  1 510 ? -50.536 17.383  46.651  1.00 37.53  ? 510  TYR D CG  1 
ATOM   16533 C  CD1 . TYR D  1 510 ? -49.668 17.684  47.692  1.00 35.59  ? 510  TYR D CD1 1 
ATOM   16534 C  CD2 . TYR D  1 510 ? -51.410 16.320  46.819  1.00 38.94  ? 510  TYR D CD2 1 
ATOM   16535 C  CE1 . TYR D  1 510 ? -49.687 16.951  48.875  1.00 37.15  ? 510  TYR D CE1 1 
ATOM   16536 C  CE2 . TYR D  1 510 ? -51.429 15.579  47.993  1.00 40.21  ? 510  TYR D CE2 1 
ATOM   16537 C  CZ  . TYR D  1 510 ? -50.570 15.897  49.022  1.00 38.55  ? 510  TYR D CZ  1 
ATOM   16538 O  OH  . TYR D  1 510 ? -50.602 15.156  50.192  1.00 37.59  ? 510  TYR D OH  1 
ATOM   16539 N  N   . VAL D  1 511 ? -53.560 18.682  45.114  1.00 37.24  ? 511  VAL D N   1 
ATOM   16540 C  CA  . VAL D  1 511 ? -54.937 18.478  45.559  1.00 37.36  ? 511  VAL D CA  1 
ATOM   16541 C  C   . VAL D  1 511 ? -55.340 17.008  45.592  1.00 37.19  ? 511  VAL D C   1 
ATOM   16542 O  O   . VAL D  1 511 ? -54.794 16.184  44.855  1.00 35.78  ? 511  VAL D O   1 
ATOM   16543 C  CB  . VAL D  1 511 ? -55.927 19.222  44.654  1.00 44.97  ? 511  VAL D CB  1 
ATOM   16544 C  CG1 . VAL D  1 511 ? -55.616 20.706  44.633  1.00 47.58  ? 511  VAL D CG1 1 
ATOM   16545 C  CG2 . VAL D  1 511 ? -55.895 18.646  43.240  1.00 40.19  ? 511  VAL D CG2 1 
ATOM   16546 N  N   . SER D  1 512 ? -56.307 16.679  46.441  1.00 41.35  ? 512  SER D N   1 
ATOM   16547 C  CA  . SER D  1 512 ? -56.884 15.338  46.413  1.00 43.77  ? 512  SER D CA  1 
ATOM   16548 C  C   . SER D  1 512 ? -58.038 15.257  45.406  1.00 44.63  ? 512  SER D C   1 
ATOM   16549 O  O   . SER D  1 512 ? -58.841 16.186  45.273  1.00 46.54  ? 512  SER D O   1 
ATOM   16550 C  CB  . SER D  1 512 ? -57.339 14.885  47.811  1.00 53.99  ? 512  SER D CB  1 
ATOM   16551 O  OG  . SER D  1 512 ? -58.628 15.375  48.152  1.00 59.23  ? 512  SER D OG  1 
ATOM   16552 N  N   . LEU D  1 513 ? -58.089 14.152  44.670  1.00 41.54  ? 513  LEU D N   1 
ATOM   16553 C  CA  . LEU D  1 513 ? -59.243 13.843  43.846  1.00 41.99  ? 513  LEU D CA  1 
ATOM   16554 C  C   . LEU D  1 513 ? -59.881 12.614  44.462  1.00 44.93  ? 513  LEU D C   1 
ATOM   16555 O  O   . LEU D  1 513 ? -59.357 11.507  44.346  1.00 43.61  ? 513  LEU D O   1 
ATOM   16556 C  CB  . LEU D  1 513 ? -58.831 13.555  42.399  1.00 37.73  ? 513  LEU D CB  1 
ATOM   16557 C  CG  . LEU D  1 513 ? -57.922 14.587  41.720  1.00 40.88  ? 513  LEU D CG  1 
ATOM   16558 C  CD1 . LEU D  1 513 ? -57.368 14.046  40.410  1.00 37.56  ? 513  LEU D CD1 1 
ATOM   16559 C  CD2 . LEU D  1 513 ? -58.631 15.923  41.500  1.00 37.63  ? 513  LEU D CD2 1 
ATOM   16560 N  N   . ASN D  1 514 ? -61.016 12.829  45.118  1.00 59.96  ? 514  ASN D N   1 
ATOM   16561 C  CA  . ASN D  1 514 ? -61.831 11.775  45.714  1.00 64.58  ? 514  ASN D CA  1 
ATOM   16562 C  C   . ASN D  1 514 ? -63.248 12.169  45.399  1.00 67.51  ? 514  ASN D C   1 
ATOM   16563 O  O   . ASN D  1 514 ? -63.468 13.049  44.567  1.00 68.81  ? 514  ASN D O   1 
ATOM   16564 C  CB  . ASN D  1 514 ? -61.619 11.635  47.231  1.00 63.57  ? 514  ASN D CB  1 
ATOM   16565 C  CG  . ASN D  1 514 ? -61.392 12.970  47.928  1.00 67.14  ? 514  ASN D CG  1 
ATOM   16566 O  OD1 . ASN D  1 514 ? -61.796 14.021  47.435  1.00 68.94  ? 514  ASN D OD1 1 
ATOM   16567 N  ND2 . ASN D  1 514 ? -60.731 12.931  49.085  1.00 68.60  ? 514  ASN D ND2 1 
ATOM   16568 N  N   . LEU D  1 515 ? -64.217 11.510  46.014  1.00 64.46  ? 515  LEU D N   1 
ATOM   16569 C  CA  . LEU D  1 515 ? -65.595 11.897  45.765  1.00 65.51  ? 515  LEU D CA  1 
ATOM   16570 C  C   . LEU D  1 515 ? -65.880 13.336  46.211  1.00 67.27  ? 515  LEU D C   1 
ATOM   16571 O  O   . LEU D  1 515 ? -66.289 14.168  45.397  1.00 69.31  ? 515  LEU D O   1 
ATOM   16572 C  CB  . LEU D  1 515 ? -66.559 10.905  46.400  1.00 56.86  ? 515  LEU D CB  1 
ATOM   16573 C  CG  . LEU D  1 515 ? -67.242 9.981   45.391  1.00 57.33  ? 515  LEU D CG  1 
ATOM   16574 C  CD1 . LEU D  1 515 ? -66.245 9.401   44.397  1.00 48.62  ? 515  LEU D CD1 1 
ATOM   16575 C  CD2 . LEU D  1 515 ? -68.001 8.880   46.128  1.00 59.14  ? 515  LEU D CD2 1 
ATOM   16576 N  N   . LYS D  1 516 ? -65.619 13.638  47.482  1.00 59.24  ? 516  LYS D N   1 
ATOM   16577 C  CA  . LYS D  1 516 ? -65.879 14.968  48.038  1.00 61.49  ? 516  LYS D CA  1 
ATOM   16578 C  C   . LYS D  1 516 ? -65.010 16.006  47.322  1.00 60.01  ? 516  LYS D C   1 
ATOM   16579 O  O   . LYS D  1 516 ? -64.065 15.630  46.642  1.00 59.39  ? 516  LYS D O   1 
ATOM   16580 C  CB  . LYS D  1 516 ? -65.631 14.957  49.550  1.00 75.27  ? 516  LYS D CB  1 
ATOM   16581 C  CG  . LYS D  1 516 ? -64.255 14.487  49.953  1.00 77.82  ? 516  LYS D CG  1 
ATOM   16582 C  CD  . LYS D  1 516 ? -64.194 14.141  51.438  1.00 82.79  ? 516  LYS D CD  1 
ATOM   16583 C  CE  . LYS D  1 516 ? -64.722 12.732  51.709  1.00 85.57  ? 516  LYS D CE  1 
ATOM   16584 N  NZ  . LYS D  1 516 ? -64.497 12.285  53.121  1.00 87.41  ? 516  LYS D NZ  1 
ATOM   16585 N  N   . PRO D  1 517 ? -65.332 17.310  47.445  1.00 64.89  ? 517  PRO D N   1 
ATOM   16586 C  CA  . PRO D  1 517 ? -64.651 18.316  46.609  1.00 64.22  ? 517  PRO D CA  1 
ATOM   16587 C  C   . PRO D  1 517 ? -63.130 18.430  46.775  1.00 62.44  ? 517  PRO D C   1 
ATOM   16588 O  O   . PRO D  1 517 ? -62.502 17.741  47.597  1.00 61.43  ? 517  PRO D O   1 
ATOM   16589 C  CB  . PRO D  1 517 ? -65.292 19.632  47.057  1.00 72.29  ? 517  PRO D CB  1 
ATOM   16590 C  CG  . PRO D  1 517 ? -66.618 19.245  47.570  1.00 75.51  ? 517  PRO D CG  1 
ATOM   16591 C  CD  . PRO D  1 517 ? -66.450 17.898  48.202  1.00 73.96  ? 517  PRO D CD  1 
ATOM   16592 N  N   . LEU D  1 518 ? -62.544 19.319  45.977  1.00 59.40  ? 518  LEU D N   1 
ATOM   16593 C  CA  . LEU D  1 518 ? -61.105 19.518  46.000  1.00 58.46  ? 518  LEU D CA  1 
ATOM   16594 C  C   . LEU D  1 518 ? -60.642 19.929  47.376  1.00 64.16  ? 518  LEU D C   1 
ATOM   16595 O  O   . LEU D  1 518 ? -61.263 20.761  48.032  1.00 66.53  ? 518  LEU D O   1 
ATOM   16596 C  CB  . LEU D  1 518 ? -60.682 20.586  45.003  1.00 55.23  ? 518  LEU D CB  1 
ATOM   16597 C  CG  . LEU D  1 518 ? -60.492 20.146  43.563  1.00 50.62  ? 518  LEU D CG  1 
ATOM   16598 C  CD1 . LEU D  1 518 ? -59.593 21.152  42.858  1.00 47.11  ? 518  LEU D CD1 1 
ATOM   16599 C  CD2 . LEU D  1 518 ? -59.917 18.737  43.518  1.00 49.17  ? 518  LEU D CD2 1 
ATOM   16600 N  N   . GLU D  1 519 ? -59.536 19.339  47.800  1.00 80.58  ? 519  GLU D N   1 
ATOM   16601 C  CA  . GLU D  1 519 ? -58.951 19.628  49.098  1.00 83.50  ? 519  GLU D CA  1 
ATOM   16602 C  C   . GLU D  1 519 ? -57.465 19.859  48.876  1.00 71.99  ? 519  GLU D C   1 
ATOM   16603 O  O   . GLU D  1 519 ? -56.766 18.974  48.390  1.00 69.83  ? 519  GLU D O   1 
ATOM   16604 C  CB  . GLU D  1 519 ? -59.186 18.434  50.030  1.00 99.25  ? 519  GLU D CB  1 
ATOM   16605 C  CG  . GLU D  1 519 ? -58.555 18.523  51.410  1.00 104.39 ? 519  GLU D CG  1 
ATOM   16606 C  CD  . GLU D  1 519 ? -58.658 17.207  52.170  1.00 108.42 ? 519  GLU D CD  1 
ATOM   16607 O  OE1 . GLU D  1 519 ? -59.543 16.382  51.843  1.00 111.03 ? 519  GLU D OE1 1 
ATOM   16608 O  OE2 . GLU D  1 519 ? -57.841 16.990  53.088  1.00 108.64 ? 519  GLU D OE2 1 
ATOM   16609 N  N   . VAL D  1 520 ? -56.975 21.048  49.199  1.00 45.00  ? 520  VAL D N   1 
ATOM   16610 C  CA  . VAL D  1 520 ? -55.566 21.327  48.953  1.00 42.11  ? 520  VAL D CA  1 
ATOM   16611 C  C   . VAL D  1 520 ? -54.683 20.841  50.101  1.00 41.83  ? 520  VAL D C   1 
ATOM   16612 O  O   . VAL D  1 520 ? -54.943 21.150  51.260  1.00 43.29  ? 520  VAL D O   1 
ATOM   16613 C  CB  . VAL D  1 520 ? -55.321 22.816  48.688  1.00 42.53  ? 520  VAL D CB  1 
ATOM   16614 C  CG1 . VAL D  1 520 ? -53.870 23.063  48.306  1.00 40.84  ? 520  VAL D CG1 1 
ATOM   16615 C  CG2 . VAL D  1 520 ? -56.249 23.298  47.600  1.00 43.02  ? 520  VAL D CG2 1 
ATOM   16616 N  N   . ARG D  1 521 ? -53.652 20.065  49.772  1.00 40.06  ? 521  ARG D N   1 
ATOM   16617 C  CA  . ARG D  1 521 ? -52.719 19.553  50.759  1.00 39.70  ? 521  ARG D CA  1 
ATOM   16618 C  C   . ARG D  1 521 ? -51.341 20.066  50.437  1.00 38.36  ? 521  ARG D C   1 
ATOM   16619 O  O   . ARG D  1 521 ? -51.071 20.458  49.299  1.00 37.38  ? 521  ARG D O   1 
ATOM   16620 C  CB  . ARG D  1 521 ? -52.701 18.037  50.764  1.00 50.98  ? 521  ARG D CB  1 
ATOM   16621 C  CG  . ARG D  1 521 ? -54.075 17.430  50.806  1.00 57.57  ? 521  ARG D CG  1 
ATOM   16622 C  CD  . ARG D  1 521 ? -54.129 16.207  51.704  1.00 59.95  ? 521  ARG D CD  1 
ATOM   16623 N  NE  . ARG D  1 521 ? -55.407 15.520  51.565  1.00 59.36  ? 521  ARG D NE  1 
ATOM   16624 C  CZ  . ARG D  1 521 ? -55.556 14.355  50.950  1.00 58.89  ? 521  ARG D CZ  1 
ATOM   16625 N  NH1 . ARG D  1 521 ? -54.495 13.734  50.438  1.00 54.88  ? 521  ARG D NH1 1 
ATOM   16626 N  NH2 . ARG D  1 521 ? -56.763 13.809  50.863  1.00 62.63  ? 521  ARG D NH2 1 
ATOM   16627 N  N   . ARG D  1 522 ? -50.472 20.069  51.448  1.00 56.16  ? 522  ARG D N   1 
ATOM   16628 C  CA  . ARG D  1 522 ? -49.132 20.633  51.321  1.00 58.48  ? 522  ARG D CA  1 
ATOM   16629 C  C   . ARG D  1 522 ? -48.037 19.614  51.615  1.00 55.09  ? 522  ARG D C   1 
ATOM   16630 O  O   . ARG D  1 522 ? -47.996 18.998  52.677  1.00 54.23  ? 522  ARG D O   1 
ATOM   16631 C  CB  . ARG D  1 522 ? -48.981 21.867  52.207  1.00 76.25  ? 522  ARG D CB  1 
ATOM   16632 C  CG  . ARG D  1 522 ? -49.223 23.184  51.482  1.00 82.63  ? 522  ARG D CG  1 
ATOM   16633 C  CD  . ARG D  1 522 ? -49.683 24.285  52.435  1.00 89.69  ? 522  ARG D CD  1 
ATOM   16634 N  NE  . ARG D  1 522 ? -49.257 24.045  53.815  1.00 95.12  ? 522  ARG D NE  1 
ATOM   16635 C  CZ  . ARG D  1 522 ? -48.036 24.295  54.287  1.00 96.66  ? 522  ARG D CZ  1 
ATOM   16636 N  NH1 . ARG D  1 522 ? -47.097 24.783  53.480  1.00 96.55  ? 522  ARG D NH1 1 
ATOM   16637 N  NH2 . ARG D  1 522 ? -47.749 24.042  55.564  1.00 95.95  ? 522  ARG D NH2 1 
ATOM   16638 N  N   . GLY D  1 523 ? -47.188 19.421  50.616  1.00 59.74  ? 523  GLY D N   1 
ATOM   16639 C  CA  . GLY D  1 523 ? -46.014 18.568  50.663  1.00 61.23  ? 523  GLY D CA  1 
ATOM   16640 C  C   . GLY D  1 523 ? -46.379 17.171  50.209  1.00 61.96  ? 523  GLY D C   1 
ATOM   16641 O  O   . GLY D  1 523 ? -47.352 16.593  50.701  1.00 62.15  ? 523  GLY D O   1 
ATOM   16642 N  N   . LEU D  1 524 ? -45.539 16.581  49.361  1.00 57.57  ? 524  LEU D N   1 
ATOM   16643 C  CA  . LEU D  1 524 ? -45.893 15.313  48.746  1.00 54.76  ? 524  LEU D CA  1 
ATOM   16644 C  C   . LEU D  1 524 ? -44.930 14.247  49.208  1.00 56.13  ? 524  LEU D C   1 
ATOM   16645 O  O   . LEU D  1 524 ? -43.823 14.147  48.674  1.00 54.12  ? 524  LEU D O   1 
ATOM   16646 C  CB  . LEU D  1 524 ? -45.789 15.446  47.228  1.00 43.08  ? 524  LEU D CB  1 
ATOM   16647 C  CG  . LEU D  1 524 ? -47.015 15.183  46.348  1.00 39.63  ? 524  LEU D CG  1 
ATOM   16648 C  CD1 . LEU D  1 524 ? -46.632 15.320  44.885  1.00 36.49  ? 524  LEU D CD1 1 
ATOM   16649 C  CD2 . LEU D  1 524 ? -47.627 13.812  46.605  1.00 38.58  ? 524  LEU D CD2 1 
ATOM   16650 N  N   . ARG D  1 525 ? -45.384 13.421  50.151  1.00 61.52  ? 525  ARG D N   1 
ATOM   16651 C  CA  . ARG D  1 525 ? -44.541 12.408  50.779  1.00 63.93  ? 525  ARG D CA  1 
ATOM   16652 C  C   . ARG D  1 525 ? -43.149 12.997  51.061  1.00 62.99  ? 525  ARG D C   1 
ATOM   16653 O  O   . ARG D  1 525 ? -42.125 12.392  50.730  1.00 61.63  ? 525  ARG D O   1 
ATOM   16654 C  CB  . ARG D  1 525 ? -44.483 11.137  49.933  1.00 66.97  ? 525  ARG D CB  1 
ATOM   16655 C  CG  . ARG D  1 525 ? -45.857 10.508  49.658  1.00 69.41  ? 525  ARG D CG  1 
ATOM   16656 C  CD  . ARG D  1 525 ? -46.465 9.847   50.884  1.00 74.26  ? 525  ARG D CD  1 
ATOM   16657 N  NE  . ARG D  1 525 ? -45.789 8.604   51.260  1.00 79.86  ? 525  ARG D NE  1 
ATOM   16658 C  CZ  . ARG D  1 525 ? -45.410 8.300   52.506  1.00 85.68  ? 525  ARG D CZ  1 
ATOM   16659 N  NH1 . ARG D  1 525 ? -45.643 9.150   53.506  1.00 87.80  ? 525  ARG D NH1 1 
ATOM   16660 N  NH2 . ARG D  1 525 ? -44.803 7.143   52.762  1.00 85.89  ? 525  ARG D NH2 1 
ATOM   16661 N  N   . ALA D  1 526 ? -43.148 14.185  51.675  1.00 61.47  ? 526  ALA D N   1 
ATOM   16662 C  CA  . ALA D  1 526 ? -42.000 15.103  51.707  1.00 53.71  ? 526  ALA D CA  1 
ATOM   16663 C  C   . ALA D  1 526 ? -40.739 14.593  52.385  1.00 49.75  ? 526  ALA D C   1 
ATOM   16664 O  O   . ALA D  1 526 ? -39.667 14.609  51.789  1.00 48.90  ? 526  ALA D O   1 
ATOM   16665 C  CB  . ALA D  1 526 ? -42.414 16.418  52.325  1.00 42.92  ? 526  ALA D CB  1 
ATOM   16666 N  N   . GLN D  1 527 ? -40.868 14.177  53.639  1.00 43.12  ? 527  GLN D N   1 
ATOM   16667 C  CA  . GLN D  1 527 ? -39.743 13.643  54.402  1.00 42.00  ? 527  GLN D CA  1 
ATOM   16668 C  C   . GLN D  1 527 ? -39.202 12.376  53.757  1.00 37.57  ? 527  GLN D C   1 
ATOM   16669 O  O   . GLN D  1 527 ? -37.983 12.186  53.625  1.00 36.57  ? 527  GLN D O   1 
ATOM   16670 C  CB  . GLN D  1 527 ? -40.202 13.324  55.820  1.00 49.06  ? 527  GLN D CB  1 
ATOM   16671 C  CG  . GLN D  1 527 ? -40.924 14.470  56.472  1.00 54.77  ? 527  GLN D CG  1 
ATOM   16672 C  CD  . GLN D  1 527 ? -40.004 15.637  56.743  1.00 59.59  ? 527  GLN D CD  1 
ATOM   16673 O  OE1 . GLN D  1 527 ? -40.312 16.784  56.398  1.00 61.03  ? 527  GLN D OE1 1 
ATOM   16674 N  NE2 . GLN D  1 527 ? -38.862 15.352  57.369  1.00 60.69  ? 527  GLN D NE2 1 
ATOM   16675 N  N   . THR D  1 528 ? -40.131 11.512  53.362  1.00 37.04  ? 528  THR D N   1 
ATOM   16676 C  CA  . THR D  1 528 ? -39.806 10.248  52.727  1.00 36.15  ? 528  THR D CA  1 
ATOM   16677 C  C   . THR D  1 528 ? -39.101 10.503  51.399  1.00 33.55  ? 528  THR D C   1 
ATOM   16678 O  O   . THR D  1 528 ? -38.095 9.866   51.072  1.00 30.95  ? 528  THR D O   1 
ATOM   16679 C  CB  . THR D  1 528 ? -41.073 9.397   52.489  1.00 37.67  ? 528  THR D CB  1 
ATOM   16680 O  OG1 . THR D  1 528 ? -41.736 9.158   53.737  1.00 38.24  ? 528  THR D OG1 1 
ATOM   16681 C  CG2 . THR D  1 528 ? -40.706 8.064   51.863  1.00 37.81  ? 528  THR D CG2 1 
ATOM   16682 N  N   . CYS D  1 529 ? -39.621 11.446  50.629  1.00 30.58  ? 529  CYS D N   1 
ATOM   16683 C  CA  . CYS D  1 529 ? -39.001 11.724  49.351  1.00 30.87  ? 529  CYS D CA  1 
ATOM   16684 C  C   . CYS D  1 529 ? -37.649 12.379  49.538  1.00 27.03  ? 529  CYS D C   1 
ATOM   16685 O  O   . CYS D  1 529 ? -36.788 12.254  48.689  1.00 28.79  ? 529  CYS D O   1 
ATOM   16686 C  CB  . CYS D  1 529 ? -39.931 12.516  48.444  1.00 27.02  ? 529  CYS D CB  1 
ATOM   16687 S  SG  . CYS D  1 529 ? -41.181 11.406  47.765  1.00 62.23  ? 529  CYS D SG  1 
ATOM   16688 N  N   . ALA D  1 530 ? -37.454 13.052  50.667  1.00 31.06  ? 530  ALA D N   1 
ATOM   16689 C  CA  . ALA D  1 530 ? -36.144 13.607  50.990  1.00 30.01  ? 530  ALA D CA  1 
ATOM   16690 C  C   . ALA D  1 530 ? -35.186 12.470  51.274  1.00 27.74  ? 530  ALA D C   1 
ATOM   16691 O  O   . ALA D  1 530 ? -34.000 12.566  50.997  1.00 27.37  ? 530  ALA D O   1 
ATOM   16692 C  CB  . ALA D  1 530 ? -36.230 14.540  52.181  1.00 41.51  ? 530  ALA D CB  1 
ATOM   16693 N  N   . PHE D  1 531 ? -35.704 11.390  51.842  1.00 30.11  ? 531  PHE D N   1 
ATOM   16694 C  CA  . PHE D  1 531 ? -34.893 10.189  52.000  1.00 30.73  ? 531  PHE D CA  1 
ATOM   16695 C  C   . PHE D  1 531 ? -34.493 9.647   50.634  1.00 30.75  ? 531  PHE D C   1 
ATOM   16696 O  O   . PHE D  1 531 ? -33.303 9.536   50.316  1.00 28.14  ? 531  PHE D O   1 
ATOM   16697 C  CB  . PHE D  1 531 ? -35.665 9.137   52.789  1.00 28.86  ? 531  PHE D CB  1 
ATOM   16698 C  CG  . PHE D  1 531 ? -35.075 7.774   52.728  1.00 28.79  ? 531  PHE D CG  1 
ATOM   16699 C  CD1 . PHE D  1 531 ? -33.927 7.475   53.403  1.00 29.19  ? 531  PHE D CD1 1 
ATOM   16700 C  CD2 . PHE D  1 531 ? -35.692 6.782   52.024  1.00 45.73  ? 531  PHE D CD2 1 
ATOM   16701 C  CE1 . PHE D  1 531 ? -33.401 6.216   53.359  1.00 29.28  ? 531  PHE D CE1 1 
ATOM   16702 C  CE2 . PHE D  1 531 ? -35.164 5.527   51.978  1.00 28.55  ? 531  PHE D CE2 1 
ATOM   16703 C  CZ  . PHE D  1 531 ? -34.022 5.245   52.646  1.00 28.97  ? 531  PHE D CZ  1 
ATOM   16704 N  N   . TRP D  1 532 ? -35.501 9.357   49.814  1.00 38.25  ? 532  TRP D N   1 
ATOM   16705 C  CA  . TRP D  1 532 ? -35.303 8.677   48.534  1.00 36.49  ? 532  TRP D CA  1 
ATOM   16706 C  C   . TRP D  1 532 ? -34.489 9.476   47.517  1.00 37.36  ? 532  TRP D C   1 
ATOM   16707 O  O   . TRP D  1 532 ? -33.576 8.941   46.910  1.00 38.50  ? 532  TRP D O   1 
ATOM   16708 C  CB  . TRP D  1 532 ? -36.651 8.267   47.926  1.00 25.55  ? 532  TRP D CB  1 
ATOM   16709 C  CG  . TRP D  1 532 ? -37.278 7.024   48.536  1.00 26.21  ? 532  TRP D CG  1 
ATOM   16710 C  CD1 . TRP D  1 532 ? -38.434 6.958   49.279  1.00 28.02  ? 532  TRP D CD1 1 
ATOM   16711 C  CD2 . TRP D  1 532 ? -36.788 5.678   48.445  1.00 28.01  ? 532  TRP D CD2 1 
ATOM   16712 N  NE1 . TRP D  1 532 ? -38.682 5.658   49.659  1.00 27.59  ? 532  TRP D NE1 1 
ATOM   16713 C  CE2 . TRP D  1 532 ? -37.689 4.850   49.157  1.00 27.10  ? 532  TRP D CE2 1 
ATOM   16714 C  CE3 . TRP D  1 532 ? -35.669 5.087   47.835  1.00 34.09  ? 532  TRP D CE3 1 
ATOM   16715 C  CZ2 . TRP D  1 532 ? -37.513 3.476   49.269  1.00 27.47  ? 532  TRP D CZ2 1 
ATOM   16716 C  CZ3 . TRP D  1 532 ? -35.494 3.721   47.950  1.00 26.09  ? 532  TRP D CZ3 1 
ATOM   16717 C  CH2 . TRP D  1 532 ? -36.411 2.931   48.657  1.00 27.70  ? 532  TRP D CH2 1 
ATOM   16718 N  N   . ASN D  1 533 ? -34.829 10.744  47.315  1.00 36.46  ? 533  ASN D N   1 
ATOM   16719 C  CA  . ASN D  1 533 ? -34.185 11.552  46.284  1.00 36.25  ? 533  ASN D CA  1 
ATOM   16720 C  C   . ASN D  1 533 ? -32.921 12.227  46.721  1.00 39.32  ? 533  ASN D C   1 
ATOM   16721 O  O   . ASN D  1 533 ? -32.171 12.703  45.876  1.00 43.04  ? 533  ASN D O   1 
ATOM   16722 C  CB  . ASN D  1 533 ? -35.105 12.657  45.790  1.00 30.02  ? 533  ASN D CB  1 
ATOM   16723 C  CG  . ASN D  1 533 ? -36.449 12.152  45.382  1.00 30.84  ? 533  ASN D CG  1 
ATOM   16724 O  OD1 . ASN D  1 533 ? -36.582 11.074  44.802  1.00 30.89  ? 533  ASN D OD1 1 
ATOM   16725 N  ND2 . ASN D  1 533 ? -37.473 12.936  45.678  1.00 33.39  ? 533  ASN D ND2 1 
ATOM   16726 N  N   . ARG D  1 534 ? -32.695 12.311  48.026  1.00 35.51  ? 534  ARG D N   1 
ATOM   16727 C  CA  . ARG D  1 534 ? -31.562 13.088  48.518  1.00 40.06  ? 534  ARG D CA  1 
ATOM   16728 C  C   . ARG D  1 534 ? -30.499 12.242  49.205  1.00 40.73  ? 534  ARG D C   1 
ATOM   16729 O  O   . ARG D  1 534 ? -29.374 12.135  48.717  1.00 44.34  ? 534  ARG D O   1 
ATOM   16730 C  CB  . ARG D  1 534 ? -32.018 14.218  49.443  1.00 51.26  ? 534  ARG D CB  1 
ATOM   16731 C  CG  . ARG D  1 534 ? -32.739 15.352  48.748  1.00 56.51  ? 534  ARG D CG  1 
ATOM   16732 C  CD  . ARG D  1 534 ? -33.417 16.265  49.760  1.00 62.77  ? 534  ARG D CD  1 
ATOM   16733 N  NE  . ARG D  1 534 ? -33.320 17.663  49.364  1.00 67.75  ? 534  ARG D NE  1 
ATOM   16734 C  CZ  . ARG D  1 534 ? -32.237 18.410  49.555  1.00 73.21  ? 534  ARG D CZ  1 
ATOM   16735 N  NH1 . ARG D  1 534 ? -31.161 17.891  50.138  1.00 74.17  ? 534  ARG D NH1 1 
ATOM   16736 N  NH2 . ARG D  1 534 ? -32.226 19.676  49.163  1.00 75.76  ? 534  ARG D NH2 1 
ATOM   16737 N  N   . PHE D  1 535 ? -30.849 11.653  50.341  1.00 31.94  ? 535  PHE D N   1 
ATOM   16738 C  CA  . PHE D  1 535 ? -29.871 10.916  51.121  1.00 28.95  ? 535  PHE D CA  1 
ATOM   16739 C  C   . PHE D  1 535 ? -29.507 9.593   50.482  1.00 27.39  ? 535  PHE D C   1 
ATOM   16740 O  O   . PHE D  1 535 ? -28.328 9.280   50.299  1.00 27.66  ? 535  PHE D O   1 
ATOM   16741 C  CB  . PHE D  1 535 ? -30.385 10.640  52.525  1.00 28.19  ? 535  PHE D CB  1 
ATOM   16742 C  CG  . PHE D  1 535 ? -29.462 9.791   53.333  1.00 28.85  ? 535  PHE D CG  1 
ATOM   16743 C  CD1 . PHE D  1 535 ? -28.261 10.314  53.812  1.00 29.32  ? 535  PHE D CD1 1 
ATOM   16744 C  CD2 . PHE D  1 535 ? -29.771 8.469   53.598  1.00 29.10  ? 535  PHE D CD2 1 
ATOM   16745 C  CE1 . PHE D  1 535 ? -27.386 9.542   54.551  1.00 30.03  ? 535  PHE D CE1 1 
ATOM   16746 C  CE2 . PHE D  1 535 ? -28.900 7.685   54.337  1.00 39.29  ? 535  PHE D CE2 1 
ATOM   16747 C  CZ  . PHE D  1 535 ? -27.701 8.226   54.814  1.00 39.45  ? 535  PHE D CZ  1 
ATOM   16748 N  N   . LEU D  1 536 ? -30.530 8.812   50.158  1.00 29.39  ? 536  LEU D N   1 
ATOM   16749 C  CA  . LEU D  1 536 ? -30.335 7.464   49.633  1.00 30.91  ? 536  LEU D CA  1 
ATOM   16750 C  C   . LEU D  1 536 ? -29.305 7.349   48.481  1.00 36.77  ? 536  LEU D C   1 
ATOM   16751 O  O   . LEU D  1 536 ? -28.496 6.424   48.484  1.00 37.89  ? 536  LEU D O   1 
ATOM   16752 C  CB  . LEU D  1 536 ? -31.689 6.843   49.274  1.00 29.24  ? 536  LEU D CB  1 
ATOM   16753 C  CG  . LEU D  1 536 ? -31.802 5.347   48.992  1.00 29.43  ? 536  LEU D CG  1 
ATOM   16754 C  CD1 . LEU D  1 536 ? -31.583 5.069   47.507  1.00 25.29  ? 536  LEU D CD1 1 
ATOM   16755 C  CD2 . LEU D  1 536 ? -30.828 4.569   49.865  1.00 26.97  ? 536  LEU D CD2 1 
ATOM   16756 N  N   . PRO D  1 537 ? -29.325 8.281   47.503  1.00 48.03  ? 537  PRO D N   1 
ATOM   16757 C  CA  . PRO D  1 537 ? -28.264 8.264   46.489  1.00 48.42  ? 537  PRO D CA  1 
ATOM   16758 C  C   . PRO D  1 537 ? -26.878 8.483   47.071  1.00 48.93  ? 537  PRO D C   1 
ATOM   16759 O  O   . PRO D  1 537 ? -25.953 7.775   46.681  1.00 50.99  ? 537  PRO D O   1 
ATOM   16760 C  CB  . PRO D  1 537 ? -28.622 9.453   45.604  1.00 43.58  ? 537  PRO D CB  1 
ATOM   16761 C  CG  . PRO D  1 537 ? -30.081 9.574   45.732  1.00 42.84  ? 537  PRO D CG  1 
ATOM   16762 C  CD  . PRO D  1 537 ? -30.365 9.269   47.162  1.00 43.34  ? 537  PRO D CD  1 
ATOM   16763 N  N   . LYS D  1 538 ? -26.743 9.459   47.965  1.00 40.32  ? 538  LYS D N   1 
ATOM   16764 C  CA  . LYS D  1 538 ? -25.477 9.730   48.637  1.00 43.37  ? 538  LYS D CA  1 
ATOM   16765 C  C   . LYS D  1 538 ? -24.964 8.437   49.256  1.00 45.85  ? 538  LYS D C   1 
ATOM   16766 O  O   . LYS D  1 538 ? -23.775 8.085   49.150  1.00 45.64  ? 538  LYS D O   1 
ATOM   16767 C  CB  . LYS D  1 538 ? -25.662 10.781  49.739  1.00 48.45  ? 538  LYS D CB  1 
ATOM   16768 C  CG  . LYS D  1 538 ? -25.193 12.186  49.403  1.00 51.72  ? 538  LYS D CG  1 
ATOM   16769 C  CD  . LYS D  1 538 ? -26.313 13.058  48.838  1.00 55.78  ? 538  LYS D CD  1 
ATOM   16770 C  CE  . LYS D  1 538 ? -25.864 14.523  48.689  1.00 59.65  ? 538  LYS D CE  1 
ATOM   16771 N  NZ  . LYS D  1 538 ? -26.900 15.418  48.089  1.00 60.13  ? 538  LYS D NZ  1 
ATOM   16772 N  N   . LEU D  1 539 ? -25.884 7.724   49.894  1.00 54.81  ? 539  LEU D N   1 
ATOM   16773 C  CA  . LEU D  1 539 ? -25.546 6.507   50.618  1.00 57.83  ? 539  LEU D CA  1 
ATOM   16774 C  C   . LEU D  1 539 ? -25.078 5.438   49.647  1.00 58.03  ? 539  LEU D C   1 
ATOM   16775 O  O   . LEU D  1 539 ? -23.971 4.913   49.753  1.00 53.96  ? 539  LEU D O   1 
ATOM   16776 C  CB  . LEU D  1 539 ? -26.773 6.014   51.398  1.00 46.75  ? 539  LEU D CB  1 
ATOM   16777 C  CG  . LEU D  1 539 ? -26.636 4.732   52.219  1.00 41.78  ? 539  LEU D CG  1 
ATOM   16778 C  CD1 . LEU D  1 539 ? -25.413 4.809   53.097  1.00 40.62  ? 539  LEU D CD1 1 
ATOM   16779 C  CD2 . LEU D  1 539 ? -27.875 4.523   53.053  1.00 40.91  ? 539  LEU D CD2 1 
ATOM   16780 N  N   . LEU D  1 540 ? -25.952 5.162   48.690  1.00 64.14  ? 540  LEU D N   1 
ATOM   16781 C  CA  . LEU D  1 540 ? -25.782 4.148   47.665  1.00 65.96  ? 540  LEU D CA  1 
ATOM   16782 C  C   . LEU D  1 540 ? -24.460 4.336   46.903  1.00 70.64  ? 540  LEU D C   1 
ATOM   16783 O  O   . LEU D  1 540 ? -23.852 3.361   46.451  1.00 68.57  ? 540  LEU D O   1 
ATOM   16784 C  CB  . LEU D  1 540 ? -26.993 4.236   46.720  1.00 48.73  ? 540  LEU D CB  1 
ATOM   16785 C  CG  . LEU D  1 540 ? -27.715 3.024   46.124  1.00 41.48  ? 540  LEU D CG  1 
ATOM   16786 C  CD1 . LEU D  1 540 ? -27.752 1.850   47.078  1.00 41.29  ? 540  LEU D CD1 1 
ATOM   16787 C  CD2 . LEU D  1 540 ? -29.118 3.433   45.728  1.00 36.43  ? 540  LEU D CD2 1 
ATOM   16788 N  N   . SER D  1 541 ? -24.030 5.591   46.764  1.00 72.58  ? 541  SER D N   1 
ATOM   16789 C  CA  . SER D  1 541 ? -22.749 5.925   46.125  1.00 80.50  ? 541  SER D CA  1 
ATOM   16790 C  C   . SER D  1 541 ? -21.513 5.753   47.036  1.00 87.39  ? 541  SER D C   1 
ATOM   16791 O  O   . SER D  1 541 ? -20.499 5.169   46.623  1.00 86.13  ? 541  SER D O   1 
ATOM   16792 C  CB  . SER D  1 541 ? -22.783 7.346   45.540  1.00 81.51  ? 541  SER D CB  1 
ATOM   16793 O  OG  . SER D  1 541 ? -22.209 8.295   46.429  1.00 82.35  ? 541  SER D OG  1 
ATOM   16794 N  N   . ALA D  1 542 ? -21.600 6.265   48.267  1.00 95.84  ? 542  ALA D N   1 
ATOM   16795 C  CA  . ALA D  1 542 ? -20.479 6.175   49.209  1.00 98.36  ? 542  ALA D CA  1 
ATOM   16796 C  C   . ALA D  1 542 ? -20.225 4.743   49.714  1.00 101.77 ? 542  ALA D C   1 
ATOM   16797 O  O   . ALA D  1 542 ? -19.199 4.472   50.341  1.00 99.72  ? 542  ALA D O   1 
ATOM   16798 C  CB  . ALA D  1 542 ? -20.673 7.142   50.371  1.00 88.13  ? 542  ALA D CB  1 
ATOM   16799 N  N   . THR D  1 543 ? -21.168 3.841   49.441  1.00 118.33 ? 543  THR D N   1 
ATOM   16800 C  CA  . THR D  1 543 ? -20.983 2.403   49.672  1.00 123.74 ? 543  THR D CA  1 
ATOM   16801 C  C   . THR D  1 543 ? -21.030 1.618   48.350  1.00 125.75 ? 543  THR D C   1 
ATOM   16802 O  O   . THR D  1 543 ? -20.836 2.185   47.269  1.00 124.47 ? 543  THR D O   1 
ATOM   16803 C  CB  . THR D  1 543 ? -22.010 1.809   50.695  1.00 103.83 ? 543  THR D CB  1 
ATOM   16804 O  OG1 . THR D  1 543 ? -21.724 0.421   50.914  1.00 105.74 ? 543  THR D OG1 1 
ATOM   16805 C  CG2 . THR D  1 543 ? -23.444 1.935   50.196  1.00 101.22 ? 543  THR D CG2 1 
ATOM   16806 O  OXT . THR D  1 543 ? -21.251 0.403   48.322  1.00 116.48 ? 543  THR D OXT 1 
HETATM 16807 C  C1  . 4OJ E  2 .   ? -7.369  -25.176 19.497  1.00 82.14  ? 600  4OJ A C1  1 
HETATM 16808 C  C2  . 4OJ E  2 .   ? -8.637  -24.601 19.345  1.00 84.53  ? 600  4OJ A C2  1 
HETATM 16809 C  C3  . 4OJ E  2 .   ? -9.329  -24.116 20.453  1.00 83.81  ? 600  4OJ A C3  1 
HETATM 16810 C  C4  . 4OJ E  2 .   ? -8.730  -24.218 21.711  1.00 81.82  ? 600  4OJ A C4  1 
HETATM 16811 C  C5  . 4OJ E  2 .   ? -7.463  -24.794 21.870  1.00 78.51  ? 600  4OJ A C5  1 
HETATM 16812 C  C6  . 4OJ E  2 .   ? -6.776  -25.266 20.754  1.00 78.01  ? 600  4OJ A C6  1 
HETATM 16813 O  O12 . 4OJ E  2 .   ? -6.896  -24.872 23.127  1.00 75.66  ? 600  4OJ A O12 1 
HETATM 16814 P  P13 . 4OJ E  2 .   ? -7.542  -24.403 24.528  1.00 35.32  ? 600  4OJ A P13 1 
HETATM 16815 O  O1P . 4OJ E  2 .   ? -8.384  -25.431 25.086  1.00 35.31  ? 600  4OJ A O1P 1 
HETATM 16816 O  O2P . 4OJ E  2 .   ? -8.260  -23.108 24.505  1.00 36.76  ? 600  4OJ A O2P 1 
HETATM 16817 C  C7  . 4OJ E  2 .   ? -5.401  -25.892 20.904  1.00 74.41  ? 600  4OJ A C7  1 
HETATM 16818 C  C1  . NAG F  3 .   ? -38.193 -36.244 42.338  1.00 111.33 ? 701  NAG A C1  1 
HETATM 16819 C  C2  . NAG F  3 .   ? -38.273 -37.577 43.095  1.00 111.62 ? 701  NAG A C2  1 
HETATM 16820 C  C3  . NAG F  3 .   ? -38.740 -38.700 42.171  1.00 113.20 ? 701  NAG A C3  1 
HETATM 16821 C  C4  . NAG F  3 .   ? -40.064 -38.296 41.520  1.00 115.26 ? 701  NAG A C4  1 
HETATM 16822 C  C5  . NAG F  3 .   ? -39.943 -36.910 40.883  1.00 114.45 ? 701  NAG A C5  1 
HETATM 16823 C  C6  . NAG F  3 .   ? -41.262 -36.441 40.275  1.00 115.29 ? 701  NAG A C6  1 
HETATM 16824 C  C7  . NAG F  3 .   ? -36.589 -37.217 44.777  1.00 104.27 ? 701  NAG A C7  1 
HETATM 16825 C  C8  . NAG F  3 .   ? -35.155 -36.761 44.750  1.00 102.73 ? 701  NAG A C8  1 
HETATM 16826 N  N2  . NAG F  3 .   ? -37.005 -37.904 43.716  1.00 107.40 ? 701  NAG A N2  1 
HETATM 16827 O  O3  . NAG F  3 .   ? -38.866 -39.914 42.887  1.00 113.21 ? 701  NAG A O3  1 
HETATM 16828 O  O4  . NAG F  3 .   ? -40.424 -39.235 40.530  1.00 115.76 ? 701  NAG A O4  1 
HETATM 16829 O  O5  . NAG F  3 .   ? -39.487 -35.957 41.829  1.00 114.44 ? 701  NAG A O5  1 
HETATM 16830 O  O6  . NAG F  3 .   ? -41.012 -35.351 39.413  1.00 113.09 ? 701  NAG A O6  1 
HETATM 16831 O  O7  . NAG F  3 .   ? -37.325 -36.950 45.729  1.00 102.24 ? 701  NAG A O7  1 
HETATM 16832 S  S   . SO4 G  4 .   ? 7.154   -7.348  32.600  1.00 84.17  ? 1544 SO4 A S   1 
HETATM 16833 O  O1  . SO4 G  4 .   ? 6.406   -6.469  31.696  1.00 84.58  ? 1544 SO4 A O1  1 
HETATM 16834 O  O2  . SO4 G  4 .   ? 6.261   -7.812  33.661  1.00 83.71  ? 1544 SO4 A O2  1 
HETATM 16835 O  O3  . SO4 G  4 .   ? 8.274   -6.627  33.202  1.00 82.65  ? 1544 SO4 A O3  1 
HETATM 16836 O  O4  . SO4 G  4 .   ? 7.692   -8.483  31.848  1.00 84.50  ? 1544 SO4 A O4  1 
HETATM 16837 S  S   . SO4 H  4 .   ? 0.886   -15.820 43.813  1.00 115.27 ? 1545 SO4 A S   1 
HETATM 16838 O  O1  . SO4 H  4 .   ? 1.091   -15.709 42.370  1.00 113.67 ? 1545 SO4 A O1  1 
HETATM 16839 O  O2  . SO4 H  4 .   ? 0.241   -14.594 44.272  1.00 115.67 ? 1545 SO4 A O2  1 
HETATM 16840 O  O3  . SO4 H  4 .   ? 2.173   -15.962 44.490  1.00 117.10 ? 1545 SO4 A O3  1 
HETATM 16841 O  O4  . SO4 H  4 .   ? 0.055   -16.981 44.143  1.00 113.70 ? 1545 SO4 A O4  1 
HETATM 16842 S  S   . SO4 I  4 .   ? -8.760  6.865   27.828  1.00 112.81 ? 1546 SO4 A S   1 
HETATM 16843 O  O1  . SO4 I  4 .   ? -9.095  7.266   29.192  1.00 112.62 ? 1546 SO4 A O1  1 
HETATM 16844 O  O2  . SO4 I  4 .   ? -9.991  6.712   27.057  1.00 114.15 ? 1546 SO4 A O2  1 
HETATM 16845 O  O3  . SO4 I  4 .   ? -8.070  5.578   27.846  1.00 112.32 ? 1546 SO4 A O3  1 
HETATM 16846 O  O4  . SO4 I  4 .   ? -7.910  7.886   27.214  1.00 112.09 ? 1546 SO4 A O4  1 
HETATM 16847 S  S   . SO4 J  4 .   ? -0.602  -0.492  37.802  1.00 102.35 ? 1547 SO4 A S   1 
HETATM 16848 O  O1  . SO4 J  4 .   ? -0.053  0.626   37.033  1.00 101.34 ? 1547 SO4 A O1  1 
HETATM 16849 O  O2  . SO4 J  4 .   ? -0.258  -0.276  39.207  1.00 100.82 ? 1547 SO4 A O2  1 
HETATM 16850 O  O3  . SO4 J  4 .   ? -0.017  -1.738  37.306  1.00 102.82 ? 1547 SO4 A O3  1 
HETATM 16851 O  O4  . SO4 J  4 .   ? -2.061  -0.585  37.669  1.00 101.64 ? 1547 SO4 A O4  1 
HETATM 16852 S  S   . SO4 K  4 .   ? -0.659  -43.923 7.277   1.00 122.30 ? 1548 SO4 A S   1 
HETATM 16853 O  O1  . SO4 K  4 .   ? -0.965  -43.090 6.115   1.00 121.15 ? 1548 SO4 A O1  1 
HETATM 16854 O  O2  . SO4 K  4 .   ? 0.714   -44.442 7.177   1.00 120.50 ? 1548 SO4 A O2  1 
HETATM 16855 O  O3  . SO4 K  4 .   ? -1.603  -45.038 7.346   1.00 122.78 ? 1548 SO4 A O3  1 
HETATM 16856 O  O4  . SO4 K  4 .   ? -0.826  -43.110 8.480   1.00 123.03 ? 1548 SO4 A O4  1 
HETATM 16857 C  C1  . 4OJ L  2 .   ? 13.954  24.064  51.182  1.00 80.36  ? 600  4OJ B C1  1 
HETATM 16858 C  C2  . 4OJ L  2 .   ? 13.545  23.515  52.401  1.00 82.76  ? 600  4OJ B C2  1 
HETATM 16859 C  C3  . 4OJ L  2 .   ? 12.236  23.075  52.583  1.00 82.82  ? 600  4OJ B C3  1 
HETATM 16860 C  C4  . 4OJ L  2 .   ? 11.342  23.194  51.519  1.00 84.53  ? 600  4OJ B C4  1 
HETATM 16861 C  C5  . 4OJ L  2 .   ? 11.739  23.748  50.293  1.00 84.07  ? 600  4OJ B C5  1 
HETATM 16862 C  C6  . 4OJ L  2 .   ? 13.057  24.177  50.129  1.00 78.06  ? 600  4OJ B C6  1 
HETATM 16863 O  O12 . 4OJ L  2 .   ? 10.824  23.847  49.253  1.00 86.62  ? 600  4OJ B O12 1 
HETATM 16864 P  P13 . 4OJ L  2 .   ? 9.246   23.423  49.246  1.00 38.13  ? 600  4OJ B P13 1 
HETATM 16865 O  O1P . 4OJ L  2 .   ? 8.441   24.510  49.747  1.00 35.83  ? 600  4OJ B O1P 1 
HETATM 16866 O  O2P . 4OJ L  2 .   ? 8.937   22.085  49.927  1.00 36.35  ? 600  4OJ B O2P 1 
HETATM 16867 C  C7  . 4OJ L  2 .   ? 13.513  24.778  48.818  1.00 74.35  ? 600  4OJ B C7  1 
HETATM 16868 C  C1  . NAG M  3 .   ? -18.857 37.250  70.070  1.00 92.06  ? 701  NAG B C1  1 
HETATM 16869 C  C2  . NAG M  3 .   ? -19.904 38.237  69.573  1.00 91.95  ? 701  NAG B C2  1 
HETATM 16870 C  C3  . NAG M  3 .   ? -19.136 39.470  69.119  1.00 93.63  ? 701  NAG B C3  1 
HETATM 16871 C  C4  . NAG M  3 .   ? -18.660 40.144  70.407  1.00 95.48  ? 701  NAG B C4  1 
HETATM 16872 C  C5  . NAG M  3 .   ? -17.811 39.164  71.244  1.00 93.84  ? 701  NAG B C5  1 
HETATM 16873 C  C6  . NAG M  3 .   ? -17.583 39.684  72.677  1.00 88.95  ? 701  NAG B C6  1 
HETATM 16874 C  C7  . NAG M  3 .   ? -20.587 36.924  67.562  1.00 90.92  ? 701  NAG B C7  1 
HETATM 16875 C  C8  . NAG M  3 .   ? -21.411 35.660  67.490  1.00 87.17  ? 701  NAG B C8  1 
HETATM 16876 N  N2  . NAG M  3 .   ? -20.850 37.722  68.595  1.00 91.93  ? 701  NAG B N2  1 
HETATM 16877 O  O3  . NAG M  3 .   ? -19.930 40.320  68.326  1.00 94.54  ? 701  NAG B O3  1 
HETATM 16878 O  O4  . NAG M  3 .   ? -17.947 41.339  70.132  1.00 97.40  ? 701  NAG B O4  1 
HETATM 16879 O  O5  . NAG M  3 .   ? -18.335 37.820  71.275  1.00 94.65  ? 701  NAG B O5  1 
HETATM 16880 O  O6  . NAG M  3 .   ? -16.527 40.624  72.729  1.00 85.90  ? 701  NAG B O6  1 
HETATM 16881 O  O7  . NAG M  3 .   ? -19.750 37.207  66.699  1.00 91.57  ? 701  NAG B O7  1 
HETATM 16882 C  C1  . NAG N  3 .   ? 20.762  4.573   59.090  1.00 97.77  ? 702  NAG B C1  1 
HETATM 16883 C  C2  . NAG N  3 .   ? 20.123  3.431   59.889  1.00 98.45  ? 702  NAG B C2  1 
HETATM 16884 C  C3  . NAG N  3 .   ? 18.733  3.845   60.377  1.00 97.34  ? 702  NAG B C3  1 
HETATM 16885 C  C4  . NAG N  3 .   ? 18.793  5.129   61.199  1.00 98.08  ? 702  NAG B C4  1 
HETATM 16886 C  C5  . NAG N  3 .   ? 19.732  6.208   60.597  1.00 106.04 ? 702  NAG B C5  1 
HETATM 16887 C  C6  . NAG N  3 .   ? 20.123  7.330   61.601  1.00 62.70  ? 702  NAG B C6  1 
HETATM 16888 C  C7  . NAG N  3 .   ? 20.394  1.005   59.584  1.00 99.11  ? 702  NAG B C7  1 
HETATM 16889 C  C8  . NAG N  3 .   ? 19.269  0.012   59.743  1.00 96.03  ? 702  NAG B C8  1 
HETATM 16890 N  N2  . NAG N  3 .   ? 20.065  2.208   59.101  1.00 100.05 ? 702  NAG B N2  1 
HETATM 16891 O  O3  . NAG N  3 .   ? 18.118  2.836   61.160  1.00 95.81  ? 702  NAG B O3  1 
HETATM 16892 O  O4  . NAG N  3 .   ? 17.454  5.588   61.315  1.00 95.62  ? 702  NAG B O4  1 
HETATM 16893 O  O5  . NAG N  3 .   ? 20.909  5.679   59.972  1.00 104.33 ? 702  NAG B O5  1 
HETATM 16894 O  O6  . NAG N  3 .   ? 21.296  7.094   62.379  1.00 61.71  ? 702  NAG B O6  1 
HETATM 16895 O  O7  . NAG N  3 .   ? 21.554  0.704   59.882  1.00 99.02  ? 702  NAG B O7  1 
HETATM 16896 S  S   . SO4 O  4 .   ? 7.913   6.036   33.124  1.00 84.52  ? 1544 SO4 B S   1 
HETATM 16897 O  O1  . SO4 O  4 .   ? 6.779   5.582   32.322  1.00 79.87  ? 1544 SO4 B O1  1 
HETATM 16898 O  O2  . SO4 O  4 .   ? 7.483   6.506   34.438  1.00 84.60  ? 1544 SO4 B O2  1 
HETATM 16899 O  O3  . SO4 O  4 .   ? 8.569   7.131   32.406  1.00 85.99  ? 1544 SO4 B O3  1 
HETATM 16900 O  O4  . SO4 O  4 .   ? 8.854   4.938   33.348  1.00 85.95  ? 1544 SO4 B O4  1 
HETATM 16901 S  S   . SO4 P  4 .   ? -5.478  14.932  33.515  1.00 128.33 ? 1545 SO4 B S   1 
HETATM 16902 O  O1  . SO4 P  4 .   ? -6.251  15.823  34.383  1.00 127.93 ? 1545 SO4 B O1  1 
HETATM 16903 O  O2  . SO4 P  4 .   ? -6.070  13.594  33.493  1.00 127.38 ? 1545 SO4 B O2  1 
HETATM 16904 O  O3  . SO4 P  4 .   ? -4.104  14.836  34.006  1.00 127.76 ? 1545 SO4 B O3  1 
HETATM 16905 O  O4  . SO4 P  4 .   ? -5.485  15.480  32.160  1.00 129.22 ? 1545 SO4 B O4  1 
HETATM 16906 S  S   . SO4 Q  4 .   ? 5.083   -7.739  49.811  1.00 127.81 ? 1546 SO4 B S   1 
HETATM 16907 O  O1  . SO4 Q  4 .   ? 4.625   -6.518  49.147  1.00 126.72 ? 1546 SO4 B O1  1 
HETATM 16908 O  O2  . SO4 Q  4 .   ? 6.433   -8.061  49.353  1.00 127.61 ? 1546 SO4 B O2  1 
HETATM 16909 O  O3  . SO4 Q  4 .   ? 4.184   -8.838  49.462  1.00 128.23 ? 1546 SO4 B O3  1 
HETATM 16910 O  O4  . SO4 Q  4 .   ? 5.092   -7.554  51.264  1.00 127.07 ? 1546 SO4 B O4  1 
HETATM 16911 C  C1  . 4OJ R  2 .   ? -24.866 20.521  85.438  1.00 61.07  ? 600  4OJ C C1  1 
HETATM 16912 C  C2  . 4OJ R  2 .   ? -23.856 21.130  84.688  1.00 61.28  ? 600  4OJ C C2  1 
HETATM 16913 C  C3  . 4OJ R  2 .   ? -23.119 20.379  83.778  1.00 59.70  ? 600  4OJ C C3  1 
HETATM 16914 C  C4  . 4OJ R  2 .   ? -23.412 19.023  83.623  1.00 58.44  ? 600  4OJ C C4  1 
HETATM 16915 C  C5  . 4OJ R  2 .   ? -24.420 18.409  84.372  1.00 57.30  ? 600  4OJ C C5  1 
HETATM 16916 C  C6  . 4OJ R  2 .   ? -25.159 19.168  85.281  1.00 57.11  ? 600  4OJ C C6  1 
HETATM 16917 O  O12 . 4OJ R  2 .   ? -24.684 17.063  84.197  1.00 55.91  ? 600  4OJ C O12 1 
HETATM 16918 P  P13 . 4OJ R  2 .   ? -23.927 16.038  83.240  1.00 25.61  ? 600  4OJ C P13 1 
HETATM 16919 O  O1P . 4OJ R  2 .   ? -22.777 15.478  83.914  1.00 23.24  ? 600  4OJ C O1P 1 
HETATM 16920 O  O2P . 4OJ R  2 .   ? -23.574 16.593  81.905  1.00 28.18  ? 600  4OJ C O2P 1 
HETATM 16921 C  C7  . 4OJ R  2 .   ? -26.258 18.532  86.115  1.00 52.67  ? 600  4OJ C C7  1 
HETATM 16922 C  C1  . NAG S  3 .   ? 11.674  4.922   84.611  0.81 102.96 ? 701  NAG C C1  1 
HETATM 16923 C  C2  . NAG S  3 .   ? 11.985  3.491   85.054  0.81 105.39 ? 701  NAG C C2  1 
HETATM 16924 C  C3  . NAG S  3 .   ? 12.353  3.504   86.540  0.81 104.34 ? 701  NAG C C3  1 
HETATM 16925 C  C4  . NAG S  3 .   ? 13.592  4.381   86.711  0.81 105.83 ? 701  NAG C C4  1 
HETATM 16926 C  C5  . NAG S  3 .   ? 13.396  5.772   86.090  0.81 104.48 ? 701  NAG C C5  1 
HETATM 16927 C  C6  . NAG S  3 .   ? 14.710  6.559   86.067  0.81 103.05 ? 701  NAG C C6  1 
HETATM 16928 C  C7  . NAG S  3 .   ? 10.963  1.734   83.672  0.81 105.28 ? 701  NAG C C7  1 
HETATM 16929 C  C8  . NAG S  3 .   ? 12.237  1.696   82.872  0.81 105.61 ? 701  NAG C C8  1 
HETATM 16930 N  N2  . NAG S  3 .   ? 10.898  2.578   84.715  0.81 105.71 ? 701  NAG C N2  1 
HETATM 16931 O  O3  . NAG S  3 .   ? 12.610  2.204   87.031  0.81 102.52 ? 701  NAG C O3  1 
HETATM 16932 O  O4  . NAG S  3 .   ? 13.908  4.501   88.083  0.81 106.32 ? 701  NAG C O4  1 
HETATM 16933 O  O5  . NAG S  3 .   ? 12.840  5.723   84.777  0.81 104.65 ? 701  NAG C O5  1 
HETATM 16934 O  O6  . NAG S  3 .   ? 15.722  5.812   85.428  0.81 102.18 ? 701  NAG C O6  1 
HETATM 16935 O  O7  . NAG S  3 .   ? 10.030  0.997   83.349  0.81 103.93 ? 701  NAG C O7  1 
HETATM 16936 CL CL  . CL  T  5 .   ? -29.578 21.394  53.020  1.00 42.61  ? 1544 CL  C CL  1 
HETATM 16937 CL CL  . CL  U  5 .   ? -30.556 -1.074  70.658  1.00 51.07  ? 1545 CL  C CL  1 
HETATM 16938 S  S   . SO4 V  4 .   ? -40.176 9.184   67.426  1.00 66.37  ? 1546 SO4 C S   1 
HETATM 16939 O  O1  . SO4 V  4 .   ? -40.497 10.427  68.139  1.00 63.20  ? 1546 SO4 C O1  1 
HETATM 16940 O  O2  . SO4 V  4 .   ? -38.844 8.693   67.772  1.00 69.51  ? 1546 SO4 C O2  1 
HETATM 16941 O  O3  . SO4 V  4 .   ? -40.164 9.465   65.995  1.00 65.13  ? 1546 SO4 C O3  1 
HETATM 16942 O  O4  . SO4 V  4 .   ? -41.146 8.135   67.758  1.00 66.46  ? 1546 SO4 C O4  1 
HETATM 16943 S  S   . SO4 W  4 .   ? -33.466 8.002   58.000  1.00 104.78 ? 1547 SO4 C S   1 
HETATM 16944 O  O1  . SO4 W  4 .   ? -34.263 9.073   57.407  1.00 105.71 ? 1547 SO4 C O1  1 
HETATM 16945 O  O2  . SO4 W  4 .   ? -33.757 7.976   59.429  1.00 106.71 ? 1547 SO4 C O2  1 
HETATM 16946 O  O3  . SO4 W  4 .   ? -32.028 8.212   57.789  1.00 100.74 ? 1547 SO4 C O3  1 
HETATM 16947 O  O4  . SO4 W  4 .   ? -33.886 6.739   57.401  1.00 104.67 ? 1547 SO4 C O4  1 
HETATM 16948 CL CL  . CL  X  5 .   ? -12.186 6.464   120.791 1.00 44.19  ? 3000 CL  C CL  1 
HETATM 16949 CL CL  . CL  Y  5 .   ? -29.928 25.763  107.397 1.00 57.36  ? 3001 CL  C CL  1 
HETATM 16950 CL CL  . CL  Z  5 .   ? -16.448 -0.036  116.088 1.00 57.08  ? 3002 CL  C CL  1 
HETATM 16951 C  C1  . 4OJ AA 2 .   ? -50.518 -1.946  33.600  1.00 67.27  ? 600  4OJ D C1  1 
HETATM 16952 C  C2  . 4OJ AA 2 .   ? -49.709 -3.090  33.687  1.00 71.68  ? 600  4OJ D C2  1 
HETATM 16953 C  C3  . 4OJ AA 2 .   ? -48.328 -2.967  33.843  1.00 73.41  ? 600  4OJ D C3  1 
HETATM 16954 C  C4  . 4OJ AA 2 .   ? -47.776 -1.685  33.916  1.00 73.04  ? 600  4OJ D C4  1 
HETATM 16955 C  C5  . 4OJ AA 2 .   ? -48.581 -0.538  33.827  1.00 68.92  ? 600  4OJ D C5  1 
HETATM 16956 C  C6  . 4OJ AA 2 .   ? -49.964 -0.671  33.672  1.00 61.04  ? 600  4OJ D C6  1 
HETATM 16957 O  O12 . 4OJ AA 2 .   ? -47.991 0.712   33.909  1.00 69.45  ? 600  4OJ D O12 1 
HETATM 16958 P  P13 . 4OJ AA 2 .   ? -46.391 1.075   34.080  1.00 33.58  ? 600  4OJ D P13 1 
HETATM 16959 O  O1P . 4OJ AA 2 .   ? -45.770 1.112   32.789  1.00 33.66  ? 600  4OJ D O1P 1 
HETATM 16960 O  O2P . 4OJ AA 2 .   ? -45.623 0.202   35.064  1.00 32.16  ? 600  4OJ D O2P 1 
HETATM 16961 C  C7  . 4OJ AA 2 .   ? -50.857 0.548   33.572  1.00 49.92  ? 600  4OJ D C7  1 
HETATM 16962 C  C1  . NAG BA 3 .   ? -19.712 -6.640  9.298   1.00 100.49 ? 701  NAG D C1  1 
HETATM 16963 C  C2  . NAG BA 3 .   ? -18.338 -6.275  8.741   1.00 101.98 ? 701  NAG D C2  1 
HETATM 16964 C  C3  . NAG BA 3 .   ? -18.446 -5.685  7.329   1.00 105.53 ? 701  NAG D C3  1 
HETATM 16965 C  C4  . NAG BA 3 .   ? -19.218 -6.610  6.369   1.00 104.67 ? 701  NAG D C4  1 
HETATM 16966 C  C5  . NAG BA 3 .   ? -20.333 -7.405  7.081   1.00 100.82 ? 701  NAG D C5  1 
HETATM 16967 C  C6  . NAG BA 3 .   ? -20.029 -8.907  7.274   1.00 95.49  ? 701  NAG D C6  1 
HETATM 16968 C  C7  . NAG BA 3 .   ? -16.879 -5.839  10.659  1.00 94.94  ? 701  NAG D C7  1 
HETATM 16969 C  C8  . NAG BA 3 .   ? -16.499 -7.294  10.632  1.00 95.44  ? 701  NAG D C8  1 
HETATM 16970 N  N2  . NAG BA 3 .   ? -17.656 -5.386  9.670   1.00 97.85  ? 701  NAG D N2  1 
HETATM 16971 O  O3  . NAG BA 3 .   ? -17.142 -5.458  6.823   1.00 108.66 ? 701  NAG D O3  1 
HETATM 16972 O  O4  . NAG BA 3 .   ? -19.742 -5.864  5.273   1.00 102.65 ? 701  NAG D O4  1 
HETATM 16973 O  O5  . NAG BA 3 .   ? -20.711 -6.768  8.302   1.00 100.19 ? 701  NAG D O5  1 
HETATM 16974 O  O6  . NAG BA 3 .   ? -20.337 -9.653  6.113   1.00 91.74  ? 701  NAG D O6  1 
HETATM 16975 O  O7  . NAG BA 3 .   ? -16.474 -5.116  11.573  1.00 92.01  ? 701  NAG D O7  1 
HETATM 16976 C  C1  . NAG CA 3 .   ? -51.190 -16.144 50.898  1.00 90.03  ? 702  NAG D C1  1 
HETATM 16977 C  C2  . NAG CA 3 .   ? -50.562 -16.638 49.557  1.00 92.66  ? 702  NAG D C2  1 
HETATM 16978 C  C3  . NAG CA 3 .   ? -49.147 -17.245 49.731  1.00 92.22  ? 702  NAG D C3  1 
HETATM 16979 C  C4  . NAG CA 3 .   ? -48.414 -16.805 51.008  1.00 93.24  ? 702  NAG D C4  1 
HETATM 16980 C  C5  . NAG CA 3 .   ? -49.308 -16.868 52.259  1.00 96.39  ? 702  NAG D C5  1 
HETATM 16981 C  C6  . NAG CA 3 .   ? -49.084 -15.664 53.190  1.00 95.42  ? 702  NAG D C6  1 
HETATM 16982 C  C7  . NAG CA 3 .   ? -51.233 -18.341 47.752  1.00 87.61  ? 702  NAG D C7  1 
HETATM 16983 C  C8  . NAG CA 3 .   ? -50.767 -17.653 46.501  1.00 84.40  ? 702  NAG D C8  1 
HETATM 16984 N  N2  . NAG CA 3 .   ? -51.463 -17.579 48.852  1.00 92.65  ? 702  NAG D N2  1 
HETATM 16985 O  O3  . NAG CA 3 .   ? -48.318 -16.935 48.623  1.00 88.01  ? 702  NAG D O3  1 
HETATM 16986 O  O4  . NAG CA 3 .   ? -47.242 -17.589 51.195  1.00 90.87  ? 702  NAG D O4  1 
HETATM 16987 O  O5  . NAG CA 3 .   ? -50.689 -17.012 51.915  1.00 95.40  ? 702  NAG D O5  1 
HETATM 16988 O  O6  . NAG CA 3 .   ? -47.764 -15.641 53.703  1.00 92.81  ? 702  NAG D O6  1 
HETATM 16989 O  O7  . NAG CA 3 .   ? -51.417 -19.565 47.710  1.00 85.23  ? 702  NAG D O7  1 
HETATM 16990 C  C1  . NAG DA 3 .   ? -73.546 -4.984  35.331  1.00 123.48 ? 703  NAG D C1  1 
HETATM 16991 C  C2  . NAG DA 3 .   ? -72.678 -6.251  35.242  1.00 124.83 ? 703  NAG D C2  1 
HETATM 16992 C  C3  . NAG DA 3 .   ? -73.523 -7.523  35.416  1.00 128.08 ? 703  NAG D C3  1 
HETATM 16993 C  C4  . NAG DA 3 .   ? -74.749 -7.247  36.286  1.00 131.28 ? 703  NAG D C4  1 
HETATM 16994 C  C5  . NAG DA 3 .   ? -75.643 -6.186  35.631  1.00 129.88 ? 703  NAG D C5  1 
HETATM 16995 C  C6  . NAG DA 3 .   ? -76.526 -5.469  36.659  1.00 128.25 ? 703  NAG D C6  1 
HETATM 16996 C  C7  . NAG DA 3 .   ? -70.618 -5.970  33.924  1.00 118.30 ? 703  NAG D C7  1 
HETATM 16997 C  C8  . NAG DA 3 .   ? -70.195 -5.031  32.828  1.00 115.28 ? 703  NAG D C8  1 
HETATM 16998 N  N2  . NAG DA 3 .   ? -71.922 -6.268  33.991  1.00 122.18 ? 703  NAG D N2  1 
HETATM 16999 O  O3  . NAG DA 3 .   ? -72.767 -8.549  36.025  1.00 127.10 ? 703  NAG D O3  1 
HETATM 17000 O  O4  . NAG DA 3 .   ? -75.466 -8.447  36.509  1.00 133.88 ? 703  NAG D O4  1 
HETATM 17001 O  O5  . NAG DA 3 .   ? -74.878 -5.235  34.886  1.00 127.33 ? 703  NAG D O5  1 
HETATM 17002 O  O6  . NAG DA 3 .   ? -77.402 -6.382  37.282  1.00 128.28 ? 703  NAG D O6  1 
HETATM 17003 O  O7  . NAG DA 3 .   ? -69.775 -6.423  34.702  1.00 117.08 ? 703  NAG D O7  1 
HETATM 17004 S  S   . SO4 EA 4 .   ? -44.143 12.198  54.948  1.00 65.34  ? 1544 SO4 D S   1 
HETATM 17005 O  O1  . SO4 EA 4 .   ? -44.371 13.564  54.464  1.00 63.70  ? 1544 SO4 D O1  1 
HETATM 17006 O  O2  . SO4 EA 4 .   ? -44.122 12.172  56.406  1.00 69.40  ? 1544 SO4 D O2  1 
HETATM 17007 O  O3  . SO4 EA 4 .   ? -42.842 11.725  54.487  1.00 64.42  ? 1544 SO4 D O3  1 
HETATM 17008 O  O4  . SO4 EA 4 .   ? -45.217 11.311  54.488  1.00 64.25  ? 1544 SO4 D O4  1 
HETATM 17009 S  S   . SO4 FA 4 .   ? -34.804 -6.188  62.261  1.00 120.34 ? 1545 SO4 D S   1 
HETATM 17010 O  O1  . SO4 FA 4 .   ? -34.324 -7.338  61.499  1.00 120.21 ? 1545 SO4 D O1  1 
HETATM 17011 O  O2  . SO4 FA 4 .   ? -35.059 -5.056  61.366  1.00 118.69 ? 1545 SO4 D O2  1 
HETATM 17012 O  O3  . SO4 FA 4 .   ? -36.039 -6.568  62.945  1.00 121.70 ? 1545 SO4 D O3  1 
HETATM 17013 O  O4  . SO4 FA 4 .   ? -33.794 -5.814  63.249  1.00 120.54 ? 1545 SO4 D O4  1 
HETATM 17014 S  S   . SO4 GA 4 .   ? -33.764 17.094  44.058  1.00 120.78 ? 1546 SO4 D S   1 
HETATM 17015 O  O1  . SO4 GA 4 .   ? -32.920 17.550  45.165  1.00 120.51 ? 1546 SO4 D O1  1 
HETATM 17016 O  O2  . SO4 GA 4 .   ? -33.256 17.629  42.791  1.00 119.35 ? 1546 SO4 D O2  1 
HETATM 17017 O  O3  . SO4 GA 4 .   ? -35.138 17.550  44.257  1.00 121.22 ? 1546 SO4 D O3  1 
HETATM 17018 O  O4  . SO4 GA 4 .   ? -33.764 15.632  44.033  1.00 120.80 ? 1546 SO4 D O4  1 
HETATM 17019 CL CL  . CL  HA 5 .   ? -45.871 3.479   55.786  1.00 61.84  ? 3000 CL  D CL  1 
HETATM 17020 CL CL  . CL  IA 5 .   ? -69.881 -0.087  20.297  1.00 54.43  ? 3001 CL  D CL  1 
HETATM 17021 CL CL  . CL  JA 5 .   ? -63.750 -3.815  21.031  1.00 66.95  ? 3002 CL  D CL  1 
HETATM 17022 O  O   . HOH KA 6 .   ? -2.130  -60.461 33.168  1.00 1.03   ? 2001 HOH A O   1 
HETATM 17023 O  O   . HOH KA 6 .   ? 2.874   -61.908 20.364  1.00 8.33   ? 2002 HOH A O   1 
HETATM 17024 O  O   . HOH KA 6 .   ? -5.386  -61.425 33.214  1.00 7.54   ? 2003 HOH A O   1 
HETATM 17025 O  O   . HOH KA 6 .   ? -1.344  -57.108 31.297  1.00 13.90  ? 2004 HOH A O   1 
HETATM 17026 O  O   . HOH KA 6 .   ? -8.469  -53.610 30.093  1.00 24.79  ? 2005 HOH A O   1 
HETATM 17027 O  O   . HOH KA 6 .   ? -1.946  -30.125 10.553  1.00 7.69   ? 2006 HOH A O   1 
HETATM 17028 O  O   . HOH KA 6 .   ? -9.413  -52.609 27.737  1.00 18.90  ? 2007 HOH A O   1 
HETATM 17029 O  O   . HOH KA 6 .   ? -16.292 -48.044 24.091  1.00 33.03  ? 2008 HOH A O   1 
HETATM 17030 O  O   . HOH KA 6 .   ? -22.158 -39.228 26.734  1.00 1.34   ? 2009 HOH A O   1 
HETATM 17031 O  O   . HOH KA 6 .   ? -27.286 -46.709 36.524  1.00 24.28  ? 2010 HOH A O   1 
HETATM 17032 O  O   . HOH KA 6 .   ? -21.925 -38.354 29.389  1.00 0.96   ? 2011 HOH A O   1 
HETATM 17033 O  O   . HOH KA 6 .   ? -22.174 -34.520 34.935  1.00 17.26  ? 2012 HOH A O   1 
HETATM 17034 O  O   . HOH KA 6 .   ? -16.251 -54.748 22.066  1.00 20.78  ? 2013 HOH A O   1 
HETATM 17035 O  O   . HOH KA 6 .   ? -21.402 -58.162 27.670  1.00 29.71  ? 2014 HOH A O   1 
HETATM 17036 O  O   . HOH KA 6 .   ? -11.479 -44.455 10.334  1.00 27.73  ? 2015 HOH A O   1 
HETATM 17037 O  O   . HOH KA 6 .   ? -6.735  -44.748 10.726  1.00 32.21  ? 2016 HOH A O   1 
HETATM 17038 O  O   . HOH KA 6 .   ? -9.076  -43.583 18.310  1.00 28.84  ? 2017 HOH A O   1 
HETATM 17039 O  O   . HOH KA 6 .   ? -11.123 -40.147 18.241  1.00 16.85  ? 2018 HOH A O   1 
HETATM 17040 O  O   . HOH KA 6 .   ? -14.278 -43.211 36.775  1.00 16.86  ? 2019 HOH A O   1 
HETATM 17041 O  O   . HOH KA 6 .   ? -13.415 -36.464 20.902  1.00 12.94  ? 2020 HOH A O   1 
HETATM 17042 O  O   . HOH KA 6 .   ? -18.618 -35.299 23.999  1.00 15.62  ? 2021 HOH A O   1 
HETATM 17043 O  O   . HOH KA 6 .   ? -19.624 -31.150 23.011  1.00 28.65  ? 2022 HOH A O   1 
HETATM 17044 O  O   . HOH KA 6 .   ? -19.777 -29.161 21.599  1.00 21.61  ? 2023 HOH A O   1 
HETATM 17045 O  O   . HOH KA 6 .   ? -13.857 -22.817 10.912  1.00 21.46  ? 2024 HOH A O   1 
HETATM 17046 O  O   . HOH KA 6 .   ? -0.541  -25.387 11.071  1.00 35.07  ? 2025 HOH A O   1 
HETATM 17047 O  O   . HOH KA 6 .   ? -7.712  -32.823 11.671  1.00 34.26  ? 2026 HOH A O   1 
HETATM 17048 O  O   . HOH KA 6 .   ? -4.657  -31.181 12.838  1.00 42.39  ? 2027 HOH A O   1 
HETATM 17049 O  O   . HOH KA 6 .   ? -9.294  -28.997 18.310  1.00 20.77  ? 2028 HOH A O   1 
HETATM 17050 O  O   . HOH KA 6 .   ? -7.157  -39.938 8.213   1.00 22.91  ? 2029 HOH A O   1 
HETATM 17051 O  O   . HOH KA 6 .   ? -15.547 -42.207 10.957  1.00 14.98  ? 2030 HOH A O   1 
HETATM 17052 O  O   . HOH KA 6 .   ? -20.539 -38.302 23.996  1.00 59.78  ? 2031 HOH A O   1 
HETATM 17053 O  O   . HOH KA 6 .   ? -16.977 -45.401 24.305  1.00 21.68  ? 2032 HOH A O   1 
HETATM 17054 O  O   . HOH KA 6 .   ? -8.880  -41.174 19.383  1.00 35.36  ? 2033 HOH A O   1 
HETATM 17055 O  O   . HOH KA 6 .   ? 6.890   -56.265 23.637  1.00 29.57  ? 2034 HOH A O   1 
HETATM 17056 O  O   . HOH KA 6 .   ? 14.542  -51.667 23.066  1.00 8.79   ? 2035 HOH A O   1 
HETATM 17057 O  O   . HOH KA 6 .   ? 7.357   -40.691 31.560  1.00 3.57   ? 2036 HOH A O   1 
HETATM 17058 O  O   . HOH KA 6 .   ? -5.752  -37.376 24.604  1.00 40.99  ? 2037 HOH A O   1 
HETATM 17059 O  O   . HOH KA 6 .   ? -4.901  -29.529 21.950  1.00 42.54  ? 2038 HOH A O   1 
HETATM 17060 O  O   . HOH KA 6 .   ? -10.614 -30.111 25.694  1.00 27.64  ? 2039 HOH A O   1 
HETATM 17061 O  O   . HOH KA 6 .   ? -8.479  -30.870 20.362  1.00 2.03   ? 2040 HOH A O   1 
HETATM 17062 O  O   . HOH KA 6 .   ? -16.702 -26.043 27.003  1.00 8.70   ? 2041 HOH A O   1 
HETATM 17063 O  O   . HOH KA 6 .   ? -11.224 -26.191 19.183  1.00 14.35  ? 2042 HOH A O   1 
HETATM 17064 O  O   . HOH KA 6 .   ? -3.419  -38.419 15.977  1.00 32.29  ? 2043 HOH A O   1 
HETATM 17065 O  O   . HOH KA 6 .   ? -3.648  -38.808 19.474  1.00 26.46  ? 2044 HOH A O   1 
HETATM 17066 O  O   . HOH KA 6 .   ? 4.585   -38.132 16.936  1.00 28.81  ? 2045 HOH A O   1 
HETATM 17067 O  O   . HOH KA 6 .   ? -1.804  -42.312 11.990  1.00 24.71  ? 2046 HOH A O   1 
HETATM 17068 O  O   . HOH KA 6 .   ? 14.885  -36.394 17.877  1.00 45.33  ? 2047 HOH A O   1 
HETATM 17069 O  O   . HOH KA 6 .   ? -22.298 -30.207 24.050  1.00 19.90  ? 2048 HOH A O   1 
HETATM 17070 O  O   . HOH KA 6 .   ? -18.763 -34.184 34.020  1.00 97.84  ? 2049 HOH A O   1 
HETATM 17071 O  O   . HOH KA 6 .   ? -17.949 -31.003 35.226  1.00 28.95  ? 2050 HOH A O   1 
HETATM 17072 O  O   . HOH KA 6 .   ? -19.810 -27.578 34.043  1.00 14.05  ? 2051 HOH A O   1 
HETATM 17073 O  O   . HOH KA 6 .   ? -23.312 -27.861 33.886  1.00 20.52  ? 2052 HOH A O   1 
HETATM 17074 O  O   . HOH KA 6 .   ? -29.534 -37.385 40.654  1.00 17.52  ? 2053 HOH A O   1 
HETATM 17075 O  O   . HOH KA 6 .   ? 14.735  -45.012 28.186  1.00 19.48  ? 2054 HOH A O   1 
HETATM 17076 O  O   . HOH KA 6 .   ? -11.978 -42.254 39.435  1.00 17.12  ? 2055 HOH A O   1 
HETATM 17077 O  O   . HOH KA 6 .   ? -0.707  -44.936 34.451  1.00 37.87  ? 2056 HOH A O   1 
HETATM 17078 O  O   . HOH KA 6 .   ? 1.304   -46.656 36.644  1.00 19.37  ? 2057 HOH A O   1 
HETATM 17079 O  O   . HOH KA 6 .   ? 1.313   -53.856 32.835  1.00 35.14  ? 2058 HOH A O   1 
HETATM 17080 O  O   . HOH KA 6 .   ? 12.297  -43.258 33.425  1.00 39.78  ? 2059 HOH A O   1 
HETATM 17081 O  O   . HOH KA 6 .   ? -0.083  -23.875 23.114  1.00 12.94  ? 2060 HOH A O   1 
HETATM 17082 O  O   . HOH KA 6 .   ? -8.866  -35.814 46.375  1.00 22.29  ? 2061 HOH A O   1 
HETATM 17083 O  O   . HOH KA 6 .   ? 0.907   -34.153 44.225  1.00 28.61  ? 2062 HOH A O   1 
HETATM 17084 O  O   . HOH KA 6 .   ? 3.127   -24.300 24.866  1.00 50.86  ? 2063 HOH A O   1 
HETATM 17085 O  O   . HOH KA 6 .   ? -4.107  -21.080 31.656  1.00 33.00  ? 2064 HOH A O   1 
HETATM 17086 O  O   . HOH KA 6 .   ? -7.670  -20.728 33.423  1.00 21.47  ? 2065 HOH A O   1 
HETATM 17087 O  O   . HOH KA 6 .   ? -27.499 -22.360 40.488  1.00 33.94  ? 2066 HOH A O   1 
HETATM 17088 O  O   . HOH KA 6 .   ? -17.997 -16.450 32.106  1.00 11.48  ? 2067 HOH A O   1 
HETATM 17089 O  O   . HOH KA 6 .   ? -37.266 -21.596 25.670  1.00 18.63  ? 2068 HOH A O   1 
HETATM 17090 O  O   . HOH KA 6 .   ? -35.795 -26.889 33.772  1.00 46.90  ? 2069 HOH A O   1 
HETATM 17091 O  O   . HOH KA 6 .   ? -32.634 -42.180 31.836  1.00 22.81  ? 2070 HOH A O   1 
HETATM 17092 O  O   . HOH KA 6 .   ? -28.954 -38.835 19.299  1.00 10.92  ? 2071 HOH A O   1 
HETATM 17093 O  O   . HOH KA 6 .   ? -19.199 -24.189 25.535  1.00 31.89  ? 2072 HOH A O   1 
HETATM 17094 O  O   . HOH KA 6 .   ? -24.841 -20.626 18.517  1.00 23.17  ? 2073 HOH A O   1 
HETATM 17095 O  O   . HOH KA 6 .   ? -19.217 -15.392 29.744  1.00 25.89  ? 2074 HOH A O   1 
HETATM 17096 O  O   . HOH KA 6 .   ? -20.002 -14.322 24.179  1.00 21.07  ? 2075 HOH A O   1 
HETATM 17097 O  O   . HOH KA 6 .   ? -16.828 -17.143 25.463  1.00 65.49  ? 2076 HOH A O   1 
HETATM 17098 O  O   . HOH KA 6 .   ? -10.317 -13.756 27.833  1.00 41.80  ? 2077 HOH A O   1 
HETATM 17099 O  O   . HOH KA 6 .   ? -19.208 -26.085 27.191  1.00 41.05  ? 2078 HOH A O   1 
HETATM 17100 O  O   . HOH KA 6 .   ? -18.692 -22.002 25.721  1.00 87.64  ? 2079 HOH A O   1 
HETATM 17101 O  O   . HOH KA 6 .   ? -21.015 -25.540 33.344  1.00 1.27   ? 2080 HOH A O   1 
HETATM 17102 O  O   . HOH KA 6 .   ? -17.979 -27.746 47.087  1.00 10.19  ? 2081 HOH A O   1 
HETATM 17103 O  O   . HOH KA 6 .   ? -15.245 -26.587 48.000  1.00 9.65   ? 2082 HOH A O   1 
HETATM 17104 O  O   . HOH KA 6 .   ? -3.641  -30.096 46.678  1.00 32.43  ? 2083 HOH A O   1 
HETATM 17105 O  O   . HOH KA 6 .   ? -0.294  -32.254 47.663  1.00 32.87  ? 2084 HOH A O   1 
HETATM 17106 O  O   . HOH KA 6 .   ? -2.884  -16.557 20.041  1.00 45.36  ? 2085 HOH A O   1 
HETATM 17107 O  O   . HOH KA 6 .   ? 5.543   -12.295 18.183  1.00 21.51  ? 2086 HOH A O   1 
HETATM 17108 O  O   . HOH KA 6 .   ? 3.761   -9.144  17.575  1.00 0.00   ? 2087 HOH A O   1 
HETATM 17109 O  O   . HOH KA 6 .   ? -2.984  -19.062 24.739  1.00 100.31 ? 2088 HOH A O   1 
HETATM 17110 O  O   . HOH KA 6 .   ? -17.759 -11.352 21.532  1.00 42.31  ? 2089 HOH A O   1 
HETATM 17111 O  O   . HOH KA 6 .   ? -16.087 -6.059  31.677  1.00 4.35   ? 2090 HOH A O   1 
HETATM 17112 O  O   . HOH KA 6 .   ? -15.458 -6.850  38.612  1.00 70.27  ? 2091 HOH A O   1 
HETATM 17113 O  O   . HOH KA 6 .   ? -18.259 -1.507  38.387  1.00 25.80  ? 2092 HOH A O   1 
HETATM 17114 O  O   . HOH KA 6 .   ? -6.621  4.662   33.853  1.00 20.92  ? 2093 HOH A O   1 
HETATM 17115 O  O   . HOH KA 6 .   ? -1.132  2.585   23.257  1.00 44.18  ? 2094 HOH A O   1 
HETATM 17116 O  O   . HOH KA 6 .   ? -5.307  -13.894 35.631  1.00 32.19  ? 2095 HOH A O   1 
HETATM 17117 O  O   . HOH KA 6 .   ? 15.212  -34.007 42.774  1.00 18.56  ? 2096 HOH A O   1 
HETATM 17118 O  O   . HOH KA 6 .   ? 13.164  -23.299 33.196  1.00 40.24  ? 2097 HOH A O   1 
HETATM 17119 O  O   . HOH KA 6 .   ? 4.431   -21.828 15.056  1.00 45.25  ? 2098 HOH A O   1 
HETATM 17120 O  O   . HOH KA 6 .   ? 13.257  -18.578 15.230  1.00 35.96  ? 2099 HOH A O   1 
HETATM 17121 O  O   . HOH KA 6 .   ? 1.550   -24.886 10.378  1.00 21.01  ? 2100 HOH A O   1 
HETATM 17122 O  O   . HOH KA 6 .   ? -5.826  -22.334 20.467  1.00 58.72  ? 2101 HOH A O   1 
HETATM 17123 O  O   . HOH KA 6 .   ? 0.749   -26.750 15.636  1.00 41.75  ? 2102 HOH A O   1 
HETATM 17124 O  O   . HOH KA 6 .   ? 14.970  -25.219 3.981   1.00 20.35  ? 2103 HOH A O   1 
HETATM 17125 O  O   . HOH KA 6 .   ? 16.426  -32.457 5.540   1.00 38.80  ? 2104 HOH A O   1 
HETATM 17126 O  O   . HOH KA 6 .   ? 15.609  -22.255 21.886  1.00 43.11  ? 2105 HOH A O   1 
HETATM 17127 O  O   . HOH KA 6 .   ? 13.428  -41.502 26.377  1.00 17.41  ? 2106 HOH A O   1 
HETATM 17128 O  O   . HOH KA 6 .   ? 23.186  -35.997 26.320  1.00 55.99  ? 2107 HOH A O   1 
HETATM 17129 O  O   . HOH KA 6 .   ? 15.601  -19.982 38.133  1.00 38.91  ? 2108 HOH A O   1 
HETATM 17130 O  O   . HOH KA 6 .   ? 17.701  -19.665 43.499  1.00 21.63  ? 2109 HOH A O   1 
HETATM 17131 O  O   . HOH KA 6 .   ? 3.404   -4.670  29.545  1.00 21.08  ? 2110 HOH A O   1 
HETATM 17132 O  O   . HOH KA 6 .   ? 10.166  -9.554  34.070  1.00 32.33  ? 2111 HOH A O   1 
HETATM 17133 O  O   . HOH KA 6 .   ? -3.967  -15.244 37.512  1.00 20.27  ? 2112 HOH A O   1 
HETATM 17134 O  O   . HOH KA 6 .   ? 2.947   -14.551 40.789  1.00 49.91  ? 2113 HOH A O   1 
HETATM 17135 O  O   . HOH KA 6 .   ? 0.226   -5.971  45.640  1.00 14.92  ? 2114 HOH A O   1 
HETATM 17136 O  O   . HOH KA 6 .   ? 4.405   -17.654 43.314  1.00 36.03  ? 2115 HOH A O   1 
HETATM 17137 O  O   . HOH KA 6 .   ? -6.288  10.886  27.421  1.00 29.80  ? 2116 HOH A O   1 
HETATM 17138 O  O   . HOH KA 6 .   ? -3.599  -44.072 10.305  1.00 10.82  ? 2117 HOH A O   1 
HETATM 17139 O  O   . HOH LA 6 .   ? 20.282  52.409  39.993  1.00 49.32  ? 2001 HOH B O   1 
HETATM 17140 O  O   . HOH LA 6 .   ? 14.948  42.570  53.113  1.00 50.89  ? 2002 HOH B O   1 
HETATM 17141 O  O   . HOH LA 6 .   ? 1.819   38.673  62.102  1.00 21.02  ? 2003 HOH B O   1 
HETATM 17142 O  O   . HOH LA 6 .   ? 0.408   39.858  66.966  1.00 14.49  ? 2004 HOH B O   1 
HETATM 17143 O  O   . HOH LA 6 .   ? -0.496  37.376  60.614  1.00 18.64  ? 2005 HOH B O   1 
HETATM 17144 O  O   . HOH LA 6 .   ? -6.259  34.491  57.975  1.00 39.48  ? 2006 HOH B O   1 
HETATM 17145 O  O   . HOH LA 6 .   ? 29.811  41.092  50.336  1.00 28.68  ? 2007 HOH B O   1 
HETATM 17146 O  O   . HOH LA 6 .   ? 7.853   49.270  60.054  1.00 19.31  ? 2008 HOH B O   1 
HETATM 17147 O  O   . HOH LA 6 .   ? 10.932  35.619  55.917  1.00 51.17  ? 2009 HOH B O   1 
HETATM 17148 O  O   . HOH LA 6 .   ? 5.551   34.391  59.554  1.00 34.72  ? 2010 HOH B O   1 
HETATM 17149 O  O   . HOH LA 6 .   ? 6.633   28.386  61.079  1.00 40.07  ? 2011 HOH B O   1 
HETATM 17150 O  O   . HOH LA 6 .   ? 18.946  10.350  60.571  1.00 23.47  ? 2012 HOH B O   1 
HETATM 17151 O  O   . HOH LA 6 .   ? 25.350  22.482  50.245  1.00 24.14  ? 2013 HOH B O   1 
HETATM 17152 O  O   . HOH LA 6 .   ? 21.653  29.658  51.054  1.00 44.23  ? 2014 HOH B O   1 
HETATM 17153 O  O   . HOH LA 6 .   ? 6.261   44.690  58.178  1.00 50.51  ? 2015 HOH B O   1 
HETATM 17154 O  O   . HOH LA 6 .   ? 22.566  40.410  46.358  1.00 20.08  ? 2016 HOH B O   1 
HETATM 17155 O  O   . HOH LA 6 .   ? 18.076  48.487  29.531  1.00 43.01  ? 2017 HOH B O   1 
HETATM 17156 O  O   . HOH LA 6 .   ? 10.165  36.635  47.530  1.00 26.48  ? 2018 HOH B O   1 
HETATM 17157 O  O   . HOH LA 6 .   ? 12.401  27.991  46.963  1.00 52.14  ? 2019 HOH B O   1 
HETATM 17158 O  O   . HOH LA 6 .   ? 7.180   28.676  52.000  1.00 49.80  ? 2020 HOH B O   1 
HETATM 17159 O  O   . HOH LA 6 .   ? 13.005  25.224  54.989  1.00 16.38  ? 2021 HOH B O   1 
HETATM 17160 O  O   . HOH LA 6 .   ? 16.225  37.377  47.202  1.00 38.15  ? 2022 HOH B O   1 
HETATM 17161 O  O   . HOH LA 6 .   ? 14.117  40.077  53.323  1.00 81.30  ? 2023 HOH B O   1 
HETATM 17162 O  O   . HOH LA 6 .   ? 28.956  43.064  48.003  1.00 55.40  ? 2024 HOH B O   1 
HETATM 17163 O  O   . HOH LA 6 .   ? 3.860   29.279  62.040  1.00 19.43  ? 2025 HOH B O   1 
HETATM 17164 O  O   . HOH LA 6 .   ? -6.171  27.230  59.161  1.00 9.48   ? 2026 HOH B O   1 
HETATM 17165 O  O   . HOH LA 6 .   ? -14.531 28.818  59.740  1.00 23.51  ? 2027 HOH B O   1 
HETATM 17166 O  O   . HOH LA 6 .   ? -12.789 33.332  54.834  1.00 32.73  ? 2028 HOH B O   1 
HETATM 17167 O  O   . HOH LA 6 .   ? -14.775 36.900  62.136  1.00 49.39  ? 2029 HOH B O   1 
HETATM 17168 O  O   . HOH LA 6 .   ? -9.847  35.233  52.133  1.00 10.24  ? 2030 HOH B O   1 
HETATM 17169 O  O   . HOH LA 6 .   ? 3.802   43.485  38.655  1.00 51.28  ? 2031 HOH B O   1 
HETATM 17170 O  O   . HOH LA 6 .   ? 6.708   50.574  38.883  1.00 48.54  ? 2032 HOH B O   1 
HETATM 17171 O  O   . HOH LA 6 .   ? -0.495  49.420  46.668  1.00 14.45  ? 2033 HOH B O   1 
HETATM 17172 O  O   . HOH LA 6 .   ? 14.065  22.053  43.010  1.00 38.41  ? 2034 HOH B O   1 
HETATM 17173 O  O   . HOH LA 6 .   ? -9.532  31.624  40.982  1.00 27.90  ? 2035 HOH B O   1 
HETATM 17174 O  O   . HOH LA 6 .   ? 13.118  23.203  39.610  1.00 42.86  ? 2036 HOH B O   1 
HETATM 17175 O  O   . HOH LA 6 .   ? -3.755  21.799  45.627  1.00 24.76  ? 2037 HOH B O   1 
HETATM 17176 O  O   . HOH LA 6 .   ? 0.319   19.552  45.964  1.00 21.49  ? 2038 HOH B O   1 
HETATM 17177 O  O   . HOH LA 6 .   ? -6.063  18.531  47.324  1.00 19.42  ? 2039 HOH B O   1 
HETATM 17178 O  O   . HOH LA 6 .   ? -7.695  21.338  46.984  1.00 34.91  ? 2040 HOH B O   1 
HETATM 17179 O  O   . HOH LA 6 .   ? -6.405  15.381  56.050  1.00 41.56  ? 2041 HOH B O   1 
HETATM 17180 O  O   . HOH LA 6 .   ? -9.877  25.345  75.611  1.00 36.46  ? 2042 HOH B O   1 
HETATM 17181 O  O   . HOH LA 6 .   ? -15.238 29.148  78.882  1.00 44.56  ? 2043 HOH B O   1 
HETATM 17182 O  O   . HOH LA 6 .   ? -15.729 32.357  70.375  1.00 50.76  ? 2044 HOH B O   1 
HETATM 17183 O  O   . HOH LA 6 .   ? -17.906 35.204  64.102  1.00 30.17  ? 2045 HOH B O   1 
HETATM 17184 O  O   . HOH LA 6 .   ? -7.685  41.220  68.315  1.00 13.54  ? 2046 HOH B O   1 
HETATM 17185 O  O   . HOH LA 6 .   ? -0.936  34.684  76.275  1.00 48.51  ? 2047 HOH B O   1 
HETATM 17186 O  O   . HOH LA 6 .   ? -5.958  32.867  78.317  1.00 28.29  ? 2048 HOH B O   1 
HETATM 17187 O  O   . HOH LA 6 .   ? 4.069   25.815  74.067  1.00 13.92  ? 2049 HOH B O   1 
HETATM 17188 O  O   . HOH LA 6 .   ? 3.394   23.124  58.860  1.00 25.63  ? 2050 HOH B O   1 
HETATM 17189 O  O   . HOH LA 6 .   ? 2.567   25.356  56.937  1.00 37.16  ? 2051 HOH B O   1 
HETATM 17190 O  O   . HOH LA 6 .   ? 0.553   15.866  63.487  1.00 45.28  ? 2052 HOH B O   1 
HETATM 17191 O  O   . HOH LA 6 .   ? 0.542   13.582  63.102  1.00 8.94   ? 2053 HOH B O   1 
HETATM 17192 O  O   . HOH LA 6 .   ? 5.956   16.968  57.095  1.00 9.98   ? 2054 HOH B O   1 
HETATM 17193 O  O   . HOH LA 6 .   ? -1.629  11.121  50.108  1.00 21.16  ? 2055 HOH B O   1 
HETATM 17194 O  O   . HOH LA 6 .   ? -4.407  25.037  57.648  1.00 18.37  ? 2056 HOH B O   1 
HETATM 17195 O  O   . HOH LA 6 .   ? -6.833  20.938  44.101  1.00 29.08  ? 2057 HOH B O   1 
HETATM 17196 O  O   . HOH LA 6 .   ? 20.186  8.784   41.495  1.00 16.02  ? 2058 HOH B O   1 
HETATM 17197 O  O   . HOH LA 6 .   ? 13.801  21.052  50.238  1.00 39.99  ? 2059 HOH B O   1 
HETATM 17198 O  O   . HOH LA 6 .   ? 4.756   3.528   58.393  1.00 13.00  ? 2060 HOH B O   1 
HETATM 17199 O  O   . HOH LA 6 .   ? -1.106  5.179   53.991  1.00 9.64   ? 2061 HOH B O   1 
HETATM 17200 O  O   . HOH LA 6 .   ? -8.650  1.160   53.557  1.00 22.36  ? 2062 HOH B O   1 
HETATM 17201 O  O   . HOH LA 6 .   ? -7.915  2.467   55.405  1.00 27.27  ? 2063 HOH B O   1 
HETATM 17202 O  O   . HOH LA 6 .   ? 21.076  6.496   42.697  1.00 23.35  ? 2064 HOH B O   1 
HETATM 17203 O  O   . HOH LA 6 .   ? -0.363  13.487  42.360  1.00 15.72  ? 2065 HOH B O   1 
HETATM 17204 O  O   . HOH LA 6 .   ? 8.787   21.688  26.285  1.00 53.84  ? 2066 HOH B O   1 
HETATM 17205 O  O   . HOH LA 6 .   ? 26.473  14.712  53.817  1.00 48.88  ? 2067 HOH B O   1 
HETATM 17206 O  O   . HOH LA 6 .   ? 22.376  8.776   43.435  1.00 23.62  ? 2068 HOH B O   1 
HETATM 17207 O  O   . HOH LA 6 .   ? 19.889  25.885  45.024  1.00 32.74  ? 2069 HOH B O   1 
HETATM 17208 O  O   . HOH LA 6 .   ? 25.095  23.986  48.124  1.00 19.93  ? 2070 HOH B O   1 
HETATM 17209 O  O   . HOH LA 6 .   ? 36.524  28.249  49.742  1.00 33.17  ? 2071 HOH B O   1 
HETATM 17210 O  O   . HOH LA 6 .   ? 36.314  30.002  36.390  1.00 35.86  ? 2072 HOH B O   1 
HETATM 17211 O  O   . HOH LA 6 .   ? 22.363  28.274  27.177  1.00 57.46  ? 2073 HOH B O   1 
HETATM 17212 O  O   . HOH LA 6 .   ? 6.291   19.065  22.842  1.00 54.46  ? 2074 HOH B O   1 
HETATM 17213 O  O   . HOH LA 6 .   ? 4.708   14.128  30.173  1.00 52.12  ? 2075 HOH B O   1 
HETATM 17214 O  O   . HOH LA 6 .   ? 0.540   19.073  19.303  1.00 30.01  ? 2076 HOH B O   1 
HETATM 17215 O  O   . HOH LA 6 .   ? 21.604  19.762  28.743  1.00 60.64  ? 2077 HOH B O   1 
HETATM 17216 O  O   . HOH LA 6 .   ? 23.899  20.024  21.754  1.00 30.64  ? 2078 HOH B O   1 
HETATM 17217 O  O   . HOH LA 6 .   ? 13.471  10.547  25.439  1.00 47.55  ? 2079 HOH B O   1 
HETATM 17218 O  O   . HOH LA 6 .   ? 8.941   4.351   37.007  1.00 34.73  ? 2080 HOH B O   1 
HETATM 17219 O  O   . HOH LA 6 .   ? 0.239   10.932  32.261  1.00 24.57  ? 2081 HOH B O   1 
HETATM 17220 O  O   . HOH LA 6 .   ? -1.817  13.419  33.255  1.00 21.73  ? 2082 HOH B O   1 
HETATM 17221 O  O   . HOH MA 6 .   ? -28.628 20.617  119.613 1.00 22.73  ? 2001 HOH C O   1 
HETATM 17222 O  O   . HOH MA 6 .   ? -32.949 13.498  120.594 1.00 40.74  ? 2002 HOH C O   1 
HETATM 17223 O  O   . HOH MA 6 .   ? -22.529 6.832   120.354 1.00 15.41  ? 2003 HOH C O   1 
HETATM 17224 O  O   . HOH MA 6 .   ? -10.225 1.341   109.961 1.00 7.82   ? 2004 HOH C O   1 
HETATM 17225 O  O   . HOH MA 6 .   ? -14.125 8.755   120.943 1.00 39.82  ? 2005 HOH C O   1 
HETATM 17226 O  O   . HOH MA 6 .   ? -8.578  16.861  93.699  1.00 16.74  ? 2006 HOH C O   1 
HETATM 17227 O  O   . HOH MA 6 .   ? -19.258 17.242  103.171 1.00 1.08   ? 2007 HOH C O   1 
HETATM 17228 O  O   . HOH MA 6 .   ? -5.243  14.786  94.221  1.00 15.38  ? 2008 HOH C O   1 
HETATM 17229 O  O   . HOH MA 6 .   ? -1.448  16.875  95.450  1.00 15.70  ? 2009 HOH C O   1 
HETATM 17230 O  O   . HOH MA 6 .   ? 3.336   12.846  100.415 1.00 0.00   ? 2010 HOH C O   1 
HETATM 17231 O  O   . HOH MA 6 .   ? 1.680   20.153  94.730  1.00 0.00   ? 2011 HOH C O   1 
HETATM 17232 O  O   . HOH MA 6 .   ? -6.058  12.456  92.788  1.00 0.82   ? 2012 HOH C O   1 
HETATM 17233 O  O   . HOH MA 6 .   ? -6.178  7.790   87.736  1.00 32.08  ? 2013 HOH C O   1 
HETATM 17234 O  O   . HOH MA 6 .   ? -12.359 3.621   109.023 1.00 11.57  ? 2014 HOH C O   1 
HETATM 17235 O  O   . HOH MA 6 .   ? -9.597  13.933  110.067 1.00 13.48  ? 2015 HOH C O   1 
HETATM 17236 O  O   . HOH MA 6 .   ? -1.924  4.777   112.065 1.00 14.00  ? 2016 HOH C O   1 
HETATM 17237 O  O   . HOH MA 6 .   ? -6.467  11.838  114.907 1.00 8.24   ? 2017 HOH C O   1 
HETATM 17238 O  O   . HOH MA 6 .   ? -9.734  8.590   121.053 1.00 22.95  ? 2018 HOH C O   1 
HETATM 17239 O  O   . HOH MA 6 .   ? -18.314 19.168  99.519  1.00 26.61  ? 2019 HOH C O   1 
HETATM 17240 O  O   . HOH MA 6 .   ? -13.592 -0.050  104.563 1.00 4.60   ? 2020 HOH C O   1 
HETATM 17241 O  O   . HOH MA 6 .   ? -16.658 17.558  94.991  1.00 25.22  ? 2021 HOH C O   1 
HETATM 17242 O  O   . HOH MA 6 .   ? -11.291 16.788  92.147  1.00 0.00   ? 2022 HOH C O   1 
HETATM 17243 O  O   . HOH MA 6 .   ? -19.463 21.900  92.110  1.00 52.87  ? 2023 HOH C O   1 
HETATM 17244 O  O   . HOH MA 6 .   ? -18.402 23.811  88.505  1.00 8.46   ? 2024 HOH C O   1 
HETATM 17245 O  O   . HOH MA 6 .   ? -12.055 19.910  86.910  1.00 19.31  ? 2025 HOH C O   1 
HETATM 17246 O  O   . HOH MA 6 .   ? -17.263 28.034  81.602  1.00 40.69  ? 2026 HOH C O   1 
HETATM 17247 O  O   . HOH MA 6 .   ? -21.137 30.843  84.148  1.00 42.22  ? 2027 HOH C O   1 
HETATM 17248 O  O   . HOH MA 6 .   ? -17.951 32.508  78.478  1.00 40.19  ? 2028 HOH C O   1 
HETATM 17249 O  O   . HOH MA 6 .   ? -32.856 28.071  89.033  1.00 16.71  ? 2029 HOH C O   1 
HETATM 17250 O  O   . HOH MA 6 .   ? -22.256 28.892  94.077  1.00 23.26  ? 2030 HOH C O   1 
HETATM 17251 O  O   . HOH MA 6 .   ? -21.772 21.492  88.970  1.00 8.31   ? 2031 HOH C O   1 
HETATM 17252 O  O   . HOH MA 6 .   ? -17.812 29.476  97.429  1.00 23.01  ? 2032 HOH C O   1 
HETATM 17253 O  O   . HOH MA 6 .   ? -23.965 26.619  102.261 1.00 17.43  ? 2033 HOH C O   1 
HETATM 17254 O  O   . HOH MA 6 .   ? -25.806 23.228  106.445 1.00 4.77   ? 2034 HOH C O   1 
HETATM 17255 O  O   . HOH MA 6 .   ? -15.425 26.645  102.844 1.00 25.53  ? 2035 HOH C O   1 
HETATM 17256 O  O   . HOH MA 6 .   ? -7.881  14.859  95.037  1.00 13.03  ? 2036 HOH C O   1 
HETATM 17257 O  O   . HOH MA 6 .   ? -9.860  13.742  101.868 1.00 42.82  ? 2037 HOH C O   1 
HETATM 17258 O  O   . HOH MA 6 .   ? -9.550  13.707  105.491 1.00 25.25  ? 2038 HOH C O   1 
HETATM 17259 O  O   . HOH MA 6 .   ? -19.797 17.286  100.445 1.00 11.61  ? 2039 HOH C O   1 
HETATM 17260 O  O   . HOH MA 6 .   ? -30.602 4.495   116.171 1.00 22.99  ? 2040 HOH C O   1 
HETATM 17261 O  O   . HOH MA 6 .   ? -38.507 4.829   113.513 1.00 24.52  ? 2041 HOH C O   1 
HETATM 17262 O  O   . HOH MA 6 .   ? -33.245 1.662   99.522  1.00 42.58  ? 2042 HOH C O   1 
HETATM 17263 O  O   . HOH MA 6 .   ? -22.377 12.628  95.706  1.00 38.64  ? 2043 HOH C O   1 
HETATM 17264 O  O   . HOH MA 6 .   ? -25.677 16.402  89.172  1.00 22.85  ? 2044 HOH C O   1 
HETATM 17265 O  O   . HOH MA 6 .   ? -22.526 18.725  90.491  1.00 0.00   ? 2045 HOH C O   1 
HETATM 17266 O  O   . HOH MA 6 .   ? -18.991 15.081  87.523  1.00 6.39   ? 2046 HOH C O   1 
HETATM 17267 O  O   . HOH MA 6 .   ? -39.696 23.859  73.669  1.00 4.09   ? 2047 HOH C O   1 
HETATM 17268 O  O   . HOH MA 6 .   ? -21.217 21.252  86.070  1.00 3.71   ? 2048 HOH C O   1 
HETATM 17269 O  O   . HOH MA 6 .   ? -26.738 19.483  99.940  1.00 44.66  ? 2049 HOH C O   1 
HETATM 17270 O  O   . HOH MA 6 .   ? -25.479 15.844  99.006  1.00 10.50  ? 2050 HOH C O   1 
HETATM 17271 O  O   . HOH MA 6 .   ? -34.171 16.489  100.364 1.00 57.70  ? 2051 HOH C O   1 
HETATM 17272 O  O   . HOH MA 6 .   ? -43.548 6.510   100.692 1.00 50.95  ? 2052 HOH C O   1 
HETATM 17273 O  O   . HOH MA 6 .   ? -9.194  18.563  87.220  1.00 14.46  ? 2053 HOH C O   1 
HETATM 17274 O  O   . HOH MA 6 .   ? -10.186 9.403   80.993  1.00 9.77   ? 2054 HOH C O   1 
HETATM 17275 O  O   . HOH MA 6 .   ? -10.547 7.480   83.915  1.00 42.48  ? 2055 HOH C O   1 
HETATM 17276 O  O   . HOH MA 6 .   ? -7.398  9.913   80.688  1.00 5.81   ? 2056 HOH C O   1 
HETATM 17277 O  O   . HOH MA 6 .   ? 3.505   3.373   86.492  1.00 22.18  ? 2057 HOH C O   1 
HETATM 17278 O  O   . HOH MA 6 .   ? -23.520 0.416   100.447 1.00 16.58  ? 2058 HOH C O   1 
HETATM 17279 O  O   . HOH MA 6 .   ? -17.848 -2.637  103.232 1.00 12.78  ? 2059 HOH C O   1 
HETATM 17280 O  O   . HOH MA 6 .   ? -15.256 1.678   104.497 1.00 41.49  ? 2060 HOH C O   1 
HETATM 17281 O  O   . HOH MA 6 .   ? -14.580 6.102   108.621 1.00 28.06  ? 2061 HOH C O   1 
HETATM 17282 O  O   . HOH MA 6 .   ? -24.196 -3.051  109.288 1.00 16.97  ? 2062 HOH C O   1 
HETATM 17283 O  O   . HOH MA 6 .   ? -14.919 1.504   107.491 1.00 26.98  ? 2063 HOH C O   1 
HETATM 17284 O  O   . HOH MA 6 .   ? -31.576 15.999  84.773  1.00 23.93  ? 2064 HOH C O   1 
HETATM 17285 O  O   . HOH MA 6 .   ? -26.628 -4.914  92.245  1.00 6.45   ? 2065 HOH C O   1 
HETATM 17286 O  O   . HOH MA 6 .   ? -27.110 -7.593  100.616 1.00 33.32  ? 2066 HOH C O   1 
HETATM 17287 O  O   . HOH MA 6 .   ? -33.194 -3.587  97.796  1.00 40.86  ? 2067 HOH C O   1 
HETATM 17288 O  O   . HOH MA 6 .   ? -19.229 4.686   77.353  1.00 42.47  ? 2068 HOH C O   1 
HETATM 17289 O  O   . HOH MA 6 .   ? -22.711 8.638   77.052  1.00 25.58  ? 2069 HOH C O   1 
HETATM 17290 O  O   . HOH MA 6 .   ? 7.551   13.520  82.443  1.00 64.94  ? 2070 HOH C O   1 
HETATM 17291 O  O   . HOH MA 6 .   ? 6.114   11.793  77.377  1.00 49.92  ? 2071 HOH C O   1 
HETATM 17292 O  O   . HOH MA 6 .   ? -1.242  22.623  94.137  1.00 22.97  ? 2072 HOH C O   1 
HETATM 17293 O  O   . HOH MA 6 .   ? -5.404  30.280  86.284  1.00 68.43  ? 2073 HOH C O   1 
HETATM 17294 O  O   . HOH MA 6 .   ? -0.621  27.104  78.763  1.00 11.70  ? 2074 HOH C O   1 
HETATM 17295 O  O   . HOH MA 6 .   ? -3.538  28.482  79.414  1.00 4.27   ? 2075 HOH C O   1 
HETATM 17296 O  O   . HOH MA 6 .   ? -12.057 17.216  82.789  1.00 28.53  ? 2076 HOH C O   1 
HETATM 17297 O  O   . HOH MA 6 .   ? -12.298 21.782  82.763  1.00 27.86  ? 2077 HOH C O   1 
HETATM 17298 O  O   . HOH MA 6 .   ? -14.705 15.245  71.250  1.00 21.37  ? 2078 HOH C O   1 
HETATM 17299 O  O   . HOH MA 6 .   ? -22.633 16.175  72.001  1.00 64.75  ? 2079 HOH C O   1 
HETATM 17300 O  O   . HOH MA 6 .   ? -16.989 12.219  69.691  1.00 20.54  ? 2080 HOH C O   1 
HETATM 17301 O  O   . HOH MA 6 .   ? -13.754 15.668  82.335  1.00 4.40   ? 2081 HOH C O   1 
HETATM 17302 O  O   . HOH MA 6 .   ? -12.844 18.178  80.717  1.00 3.51   ? 2082 HOH C O   1 
HETATM 17303 O  O   . HOH MA 6 .   ? -8.833  11.009  78.791  1.00 26.43  ? 2083 HOH C O   1 
HETATM 17304 O  O   . HOH MA 6 .   ? -20.590 2.287   75.049  1.00 31.61  ? 2084 HOH C O   1 
HETATM 17305 O  O   . HOH MA 6 .   ? -34.914 15.627  75.051  1.00 40.14  ? 2085 HOH C O   1 
HETATM 17306 O  O   . HOH MA 6 .   ? -30.904 21.041  78.047  1.00 25.40  ? 2086 HOH C O   1 
HETATM 17307 O  O   . HOH MA 6 .   ? -40.178 22.438  76.028  1.00 28.51  ? 2087 HOH C O   1 
HETATM 17308 O  O   . HOH MA 6 .   ? -33.213 18.113  73.604  1.00 37.33  ? 2088 HOH C O   1 
HETATM 17309 O  O   . HOH MA 6 .   ? -22.101 30.328  72.517  1.00 22.90  ? 2089 HOH C O   1 
HETATM 17310 O  O   . HOH MA 6 .   ? -23.582 27.306  63.938  1.00 20.83  ? 2090 HOH C O   1 
HETATM 17311 O  O   . HOH MA 6 .   ? -22.673 20.876  57.741  1.00 26.37  ? 2091 HOH C O   1 
HETATM 17312 O  O   . HOH MA 6 .   ? -15.668 12.000  56.128  1.00 21.85  ? 2092 HOH C O   1 
HETATM 17313 O  O   . HOH MA 6 .   ? -38.633 26.979  55.248  1.00 48.83  ? 2093 HOH C O   1 
HETATM 17314 O  O   . HOH MA 6 .   ? -36.350 23.029  59.138  1.00 23.39  ? 2094 HOH C O   1 
HETATM 17315 O  O   . HOH MA 6 .   ? -26.132 7.692   70.181  1.00 15.78  ? 2095 HOH C O   1 
HETATM 17316 O  O   . HOH MA 6 .   ? -40.086 -4.788  92.002  1.00 44.78  ? 2096 HOH C O   1 
HETATM 17317 O  O   . HOH MA 6 .   ? -42.018 2.607   82.895  1.00 57.37  ? 2097 HOH C O   1 
HETATM 17318 O  O   . HOH MA 6 .   ? -37.859 21.949  86.027  1.00 40.27  ? 2098 HOH C O   1 
HETATM 17319 O  O   . HOH MA 6 .   ? -45.016 22.543  83.552  1.00 25.91  ? 2099 HOH C O   1 
HETATM 17320 O  O   . HOH MA 6 .   ? -27.405 20.214  83.675  1.00 28.09  ? 2100 HOH C O   1 
HETATM 17321 O  O   . HOH MA 6 .   ? -32.996 20.638  89.676  1.00 22.81  ? 2101 HOH C O   1 
HETATM 17322 O  O   . HOH MA 6 .   ? -34.341 26.250  89.644  1.00 0.09   ? 2102 HOH C O   1 
HETATM 17323 O  O   . HOH MA 6 .   ? -44.751 26.063  99.553  1.00 15.93  ? 2103 HOH C O   1 
HETATM 17324 O  O   . HOH MA 6 .   ? -42.260 27.590  97.697  1.00 55.23  ? 2104 HOH C O   1 
HETATM 17325 O  O   . HOH MA 6 .   ? -48.089 25.730  99.722  1.00 12.88  ? 2105 HOH C O   1 
HETATM 17326 O  O   . HOH MA 6 .   ? -47.259 9.103   94.318  1.00 19.85  ? 2106 HOH C O   1 
HETATM 17327 O  O   . HOH MA 6 .   ? -47.312 13.426  86.547  1.00 62.43  ? 2107 HOH C O   1 
HETATM 17328 O  O   . HOH MA 6 .   ? -44.902 0.069   96.710  1.00 66.23  ? 2108 HOH C O   1 
HETATM 17329 O  O   . HOH MA 6 .   ? -44.609 -1.788  78.730  1.00 33.25  ? 2109 HOH C O   1 
HETATM 17330 O  O   . HOH MA 6 .   ? -44.865 -6.609  77.296  1.00 29.45  ? 2110 HOH C O   1 
HETATM 17331 O  O   . HOH MA 6 .   ? -51.239 3.009   71.240  1.00 27.22  ? 2111 HOH C O   1 
HETATM 17332 O  O   . HOH MA 6 .   ? -48.319 7.861   73.397  1.00 26.22  ? 2112 HOH C O   1 
HETATM 17333 O  O   . HOH MA 6 .   ? -38.040 13.843  64.784  1.00 24.81  ? 2113 HOH C O   1 
HETATM 17334 O  O   . HOH MA 6 .   ? -26.704 5.193   71.889  1.00 36.36  ? 2114 HOH C O   1 
HETATM 17335 O  O   . HOH MA 6 .   ? -32.242 -3.249  63.764  1.00 30.67  ? 2115 HOH C O   1 
HETATM 17336 O  O   . HOH NA 6 .   ? -64.677 15.289  9.180   1.00 35.68  ? 2001 HOH D O   1 
HETATM 17337 O  O   . HOH NA 6 .   ? -66.076 14.010  11.576  1.00 29.34  ? 2002 HOH D O   1 
HETATM 17338 O  O   . HOH NA 6 .   ? -50.225 -0.118  6.432   1.00 34.84  ? 2003 HOH D O   1 
HETATM 17339 O  O   . HOH NA 6 .   ? -56.870 7.943   -1.023  1.00 52.07  ? 2004 HOH D O   1 
HETATM 17340 O  O   . HOH NA 6 .   ? -64.667 0.810   4.568   1.00 5.66   ? 2005 HOH D O   1 
HETATM 17341 O  O   . HOH NA 6 .   ? -55.205 6.669   -6.543  1.00 17.37  ? 2006 HOH D O   1 
HETATM 17342 O  O   . HOH NA 6 .   ? -71.616 2.369   19.188  1.00 35.78  ? 2007 HOH D O   1 
HETATM 17343 O  O   . HOH NA 6 .   ? -63.289 -6.810  22.107  1.00 29.24  ? 2008 HOH D O   1 
HETATM 17344 O  O   . HOH NA 6 .   ? -48.228 0.727   9.905   1.00 58.53  ? 2009 HOH D O   1 
HETATM 17345 O  O   . HOH NA 6 .   ? -49.258 -0.100  8.291   1.00 68.28  ? 2010 HOH D O   1 
HETATM 17346 O  O   . HOH NA 6 .   ? -41.810 1.293   2.283   1.00 31.55  ? 2011 HOH D O   1 
HETATM 17347 O  O   . HOH NA 6 .   ? -40.791 -4.794  14.775  1.00 39.43  ? 2012 HOH D O   1 
HETATM 17348 O  O   . HOH NA 6 .   ? -38.580 -8.765  11.234  1.00 31.24  ? 2013 HOH D O   1 
HETATM 17349 O  O   . HOH NA 6 .   ? -38.779 -2.927  15.670  1.00 27.14  ? 2014 HOH D O   1 
HETATM 17350 O  O   . HOH NA 6 .   ? -33.824 -0.467  18.672  1.00 19.18  ? 2015 HOH D O   1 
HETATM 17351 O  O   . HOH NA 6 .   ? -65.357 -0.625  19.090  1.00 17.75  ? 2016 HOH D O   1 
HETATM 17352 O  O   . HOH NA 6 .   ? -57.486 0.225   -4.917  1.00 0.00   ? 2017 HOH D O   1 
HETATM 17353 O  O   . HOH NA 6 .   ? -58.244 7.160   -5.803  1.00 10.36  ? 2018 HOH D O   1 
HETATM 17354 O  O   . HOH NA 6 .   ? -61.022 -3.883  15.789  1.00 21.17  ? 2019 HOH D O   1 
HETATM 17355 O  O   . HOH NA 6 .   ? -51.141 -5.527  11.404  1.00 12.94  ? 2020 HOH D O   1 
HETATM 17356 O  O   . HOH NA 6 .   ? -49.542 -1.963  20.876  1.00 25.26  ? 2021 HOH D O   1 
HETATM 17357 O  O   . HOH NA 6 .   ? -44.016 -5.382  18.027  1.00 32.27  ? 2022 HOH D O   1 
HETATM 17358 O  O   . HOH NA 6 .   ? -43.898 -4.418  20.364  1.00 43.83  ? 2023 HOH D O   1 
HETATM 17359 O  O   . HOH NA 6 .   ? -44.089 -15.612 16.318  1.00 7.24   ? 2024 HOH D O   1 
HETATM 17360 O  O   . HOH NA 6 .   ? -47.264 -14.300 15.010  1.00 12.48  ? 2025 HOH D O   1 
HETATM 17361 O  O   . HOH NA 6 .   ? -43.240 -8.090  25.451  1.00 20.56  ? 2026 HOH D O   1 
HETATM 17362 O  O   . HOH NA 6 .   ? -61.305 -3.550  37.568  1.00 29.12  ? 2027 HOH D O   1 
HETATM 17363 O  O   . HOH NA 6 .   ? -59.729 -2.719  28.878  1.00 33.46  ? 2028 HOH D O   1 
HETATM 17364 O  O   . HOH NA 6 .   ? -50.156 -3.938  30.644  1.00 17.89  ? 2029 HOH D O   1 
HETATM 17365 O  O   . HOH NA 6 .   ? -23.964 1.029   34.350  1.00 2.56   ? 2030 HOH D O   1 
HETATM 17366 O  O   . HOH NA 6 .   ? -59.556 -4.718  26.638  1.00 11.56  ? 2031 HOH D O   1 
HETATM 17367 O  O   . HOH NA 6 .   ? -62.552 -5.473  24.257  1.00 38.65  ? 2032 HOH D O   1 
HETATM 17368 O  O   . HOH NA 6 .   ? -43.636 -4.040  15.494  1.00 36.90  ? 2033 HOH D O   1 
HETATM 17369 O  O   . HOH NA 6 .   ? -47.272 -1.419  11.098  1.00 50.60  ? 2034 HOH D O   1 
HETATM 17370 O  O   . HOH NA 6 .   ? -67.798 23.877  17.511  1.00 18.36  ? 2035 HOH D O   1 
HETATM 17371 O  O   . HOH NA 6 .   ? -51.414 5.799   22.824  1.00 32.53  ? 2036 HOH D O   1 
HETATM 17372 O  O   . HOH NA 6 .   ? -51.734 3.103   30.263  1.00 27.48  ? 2037 HOH D O   1 
HETATM 17373 O  O   . HOH NA 6 .   ? -51.496 -0.442  28.433  1.00 21.85  ? 2038 HOH D O   1 
HETATM 17374 O  O   . HOH NA 6 .   ? -45.504 0.288   27.716  1.00 40.85  ? 2039 HOH D O   1 
HETATM 17375 O  O   . HOH NA 6 .   ? -39.724 -2.566  28.502  1.00 31.14  ? 2040 HOH D O   1 
HETATM 17376 O  O   . HOH NA 6 .   ? -56.936 4.456   22.632  1.00 14.07  ? 2041 HOH D O   1 
HETATM 17377 O  O   . HOH NA 6 .   ? -62.145 -0.215  22.808  1.00 40.22  ? 2042 HOH D O   1 
HETATM 17378 O  O   . HOH NA 6 .   ? -63.577 9.437   26.134  1.00 39.75  ? 2043 HOH D O   1 
HETATM 17379 O  O   . HOH NA 6 .   ? -64.489 2.466   20.608  1.00 20.11  ? 2044 HOH D O   1 
HETATM 17380 O  O   . HOH NA 6 .   ? -41.127 -7.688  23.232  1.00 20.46  ? 2045 HOH D O   1 
HETATM 17381 O  O   . HOH NA 6 .   ? -33.402 -0.729  26.288  1.00 38.20  ? 2046 HOH D O   1 
HETATM 17382 O  O   . HOH NA 6 .   ? -33.569 1.867   23.763  1.00 34.30  ? 2047 HOH D O   1 
HETATM 17383 O  O   . HOH NA 6 .   ? -31.386 -2.711  24.848  1.00 0.00   ? 2048 HOH D O   1 
HETATM 17384 O  O   . HOH NA 6 .   ? -23.163 -1.230  22.526  1.00 20.81  ? 2049 HOH D O   1 
HETATM 17385 O  O   . HOH NA 6 .   ? -48.621 17.792  17.380  1.00 28.74  ? 2050 HOH D O   1 
HETATM 17386 O  O   . HOH NA 6 .   ? -53.203 19.147  11.153  1.00 36.63  ? 2051 HOH D O   1 
HETATM 17387 O  O   . HOH NA 6 .   ? -46.494 11.832  9.111   1.00 16.70  ? 2052 HOH D O   1 
HETATM 17388 O  O   . HOH NA 6 .   ? -43.986 12.756  8.283   1.00 18.45  ? 2053 HOH D O   1 
HETATM 17389 O  O   . HOH NA 6 .   ? -51.635 5.123   37.679  1.00 42.96  ? 2054 HOH D O   1 
HETATM 17390 O  O   . HOH NA 6 .   ? -39.059 20.920  18.889  1.00 38.11  ? 2055 HOH D O   1 
HETATM 17391 O  O   . HOH NA 6 .   ? -34.583 6.664   34.270  1.00 59.65  ? 2056 HOH D O   1 
HETATM 17392 O  O   . HOH NA 6 .   ? -38.116 5.329   36.810  1.00 14.43  ? 2057 HOH D O   1 
HETATM 17393 O  O   . HOH NA 6 .   ? -31.290 5.042   36.217  1.00 5.93   ? 2058 HOH D O   1 
HETATM 17394 O  O   . HOH NA 6 .   ? -22.712 2.111   32.048  1.00 0.00   ? 2059 HOH D O   1 
HETATM 17395 O  O   . HOH NA 6 .   ? -26.092 6.063   29.148  1.00 23.02  ? 2060 HOH D O   1 
HETATM 17396 O  O   . HOH NA 6 .   ? -22.806 3.796   29.686  1.00 6.07   ? 2061 HOH D O   1 
HETATM 17397 O  O   . HOH NA 6 .   ? -26.025 -13.791 20.458  1.00 27.99  ? 2062 HOH D O   1 
HETATM 17398 O  O   . HOH NA 6 .   ? -34.799 -18.838 18.886  1.00 20.71  ? 2063 HOH D O   1 
HETATM 17399 O  O   . HOH NA 6 .   ? -21.756 -16.221 13.867  1.00 47.55  ? 2064 HOH D O   1 
HETATM 17400 O  O   . HOH NA 6 .   ? -24.322 -1.383  12.863  1.00 50.50  ? 2065 HOH D O   1 
HETATM 17401 O  O   . HOH NA 6 .   ? -36.362 -11.051 32.584  1.00 6.10   ? 2066 HOH D O   1 
HETATM 17402 O  O   . HOH NA 6 .   ? -33.416 -11.950 37.201  1.00 21.11  ? 2067 HOH D O   1 
HETATM 17403 O  O   . HOH NA 6 .   ? -33.403 -3.874  37.866  1.00 28.03  ? 2068 HOH D O   1 
HETATM 17404 O  O   . HOH NA 6 .   ? -35.556 -13.949 39.538  1.00 23.58  ? 2069 HOH D O   1 
HETATM 17405 O  O   . HOH NA 6 .   ? -39.883 -7.618  36.672  1.00 20.52  ? 2070 HOH D O   1 
HETATM 17406 O  O   . HOH NA 6 .   ? -42.204 -8.069  38.593  1.00 30.47  ? 2071 HOH D O   1 
HETATM 17407 O  O   . HOH NA 6 .   ? -32.011 -2.550  27.581  1.00 18.07  ? 2072 HOH D O   1 
HETATM 17408 O  O   . HOH NA 6 .   ? -34.778 23.036  28.091  1.00 15.82  ? 2073 HOH D O   1 
HETATM 17409 O  O   . HOH NA 6 .   ? -47.034 27.103  29.115  1.00 41.74  ? 2074 HOH D O   1 
HETATM 17410 O  O   . HOH NA 6 .   ? -50.803 -0.197  42.845  1.00 63.67  ? 2075 HOH D O   1 
HETATM 17411 O  O   . HOH NA 6 .   ? -41.067 -12.151 51.390  1.00 28.72  ? 2076 HOH D O   1 
HETATM 17412 O  O   . HOH NA 6 .   ? -59.666 -15.189 39.777  1.00 24.91  ? 2077 HOH D O   1 
HETATM 17413 O  O   . HOH NA 6 .   ? -34.793 -11.471 49.729  1.00 27.56  ? 2078 HOH D O   1 
HETATM 17414 O  O   . HOH NA 6 .   ? -31.125 -5.871  47.518  1.00 8.53   ? 2079 HOH D O   1 
HETATM 17415 O  O   . HOH NA 6 .   ? -23.540 -4.729  49.534  1.00 6.33   ? 2080 HOH D O   1 
HETATM 17416 O  O   . HOH NA 6 .   ? -32.108 -0.671  60.973  1.00 18.93  ? 2081 HOH D O   1 
HETATM 17417 O  O   . HOH NA 6 .   ? -48.218 0.278   71.983  1.00 48.18  ? 2082 HOH D O   1 
HETATM 17418 O  O   . HOH NA 6 .   ? -54.814 0.678   52.444  1.00 2.83   ? 2083 HOH D O   1 
HETATM 17419 O  O   . HOH NA 6 .   ? -45.845 26.288  39.043  1.00 38.15  ? 2084 HOH D O   1 
HETATM 17420 O  O   . HOH NA 6 .   ? -51.550 21.357  42.387  1.00 41.17  ? 2085 HOH D O   1 
HETATM 17421 O  O   . HOH NA 6 .   ? -60.149 3.212   41.203  1.00 29.03  ? 2086 HOH D O   1 
HETATM 17422 O  O   . HOH NA 6 .   ? -64.729 8.449   47.417  1.00 20.94  ? 2087 HOH D O   1 
HETATM 17423 O  O   . HOH NA 6 .   ? -50.619 -1.253  36.428  1.00 32.50  ? 2088 HOH D O   1 
HETATM 17424 O  O   . HOH NA 6 .   ? -58.135 2.913   35.142  1.00 32.48  ? 2089 HOH D O   1 
HETATM 17425 O  O   . HOH NA 6 .   ? -62.341 -1.326  36.730  1.00 15.77  ? 2090 HOH D O   1 
HETATM 17426 O  O   . HOH NA 6 .   ? -63.179 10.719  37.795  1.00 90.70  ? 2091 HOH D O   1 
HETATM 17427 O  O   . HOH NA 6 .   ? -67.466 15.238  42.119  1.00 30.18  ? 2092 HOH D O   1 
HETATM 17428 O  O   . HOH NA 6 .   ? -61.743 15.430  44.922  1.00 49.58  ? 2093 HOH D O   1 
HETATM 17429 O  O   . HOH NA 6 .   ? -47.065 25.379  45.643  1.00 50.55  ? 2094 HOH D O   1 
HETATM 17430 O  O   . HOH NA 6 .   ? -45.090 29.693  46.472  1.00 15.08  ? 2095 HOH D O   1 
HETATM 17431 O  O   . HOH NA 6 .   ? -51.771 18.873  54.468  1.00 18.98  ? 2096 HOH D O   1 
HETATM 17432 O  O   . HOH NA 6 .   ? -24.092 1.204   47.049  1.00 74.25  ? 2097 HOH D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . GLY A  2   ? 0.9918 0.5706 1.0155 0.0440  0.0178  -0.1597 2   GLY A N   
2     C CA  . GLY A  2   ? 1.0402 0.6400 1.0576 0.0515  0.0249  -0.1559 2   GLY A CA  
3     C C   . GLY A  2   ? 1.1136 0.7324 1.1219 0.0438  0.0164  -0.1539 2   GLY A C   
4     O O   . GLY A  2   ? 1.1310 0.7595 1.1506 0.0340  0.0059  -0.1480 2   GLY A O   
5     N N   . ARG A  3   ? 1.4675 1.0920 1.4563 0.0488  0.0219  -0.1580 3   ARG A N   
6     C CA  . ARG A  3   ? 1.4882 1.1270 1.4627 0.0434  0.0147  -0.1573 3   ARG A CA  
7     C C   . ARG A  3   ? 1.3794 1.0480 1.3727 0.0420  0.0132  -0.1422 3   ARG A C   
8     O O   . ARG A  3   ? 1.4096 1.0916 1.3919 0.0410  0.0114  -0.1400 3   ARG A O   
9     C CB  . ARG A  3   ? 1.4488 1.0756 1.4114 0.0322  -0.0005 -0.1660 3   ARG A CB  
10    C CG  . ARG A  3   ? 1.4808 1.1168 1.4226 0.0282  -0.0088 -0.1683 3   ARG A CG  
11    C CD  . ARG A  3   ? 1.5339 1.1567 1.4420 0.0350  -0.0013 -0.1787 3   ARG A CD  
12    N NE  . ARG A  3   ? 1.5805 1.1739 1.4702 0.0349  -0.0020 -0.1942 3   ARG A NE  
13    C CZ  . ARG A  3   ? 1.5874 1.1643 1.4439 0.0392  0.0023  -0.2059 3   ARG A CZ  
14    N NH1 . ARG A  3   ? 1.5949 1.1814 1.4327 0.0437  0.0080  -0.2032 3   ARG A NH1 
15    N NH2 . ARG A  3   ? 1.5816 1.1309 1.4224 0.0388  0.0014  -0.2204 3   ARG A NH2 
16    N N   . GLU A  4   ? 0.8578 0.5352 0.8777 0.0426  0.0146  -0.1318 4   GLU A N   
17    C CA  . GLU A  4   ? 0.7353 0.4393 0.7725 0.0411  0.0129  -0.1181 4   GLU A CA  
18    C C   . GLU A  4   ? 0.6334 0.3509 0.6782 0.0512  0.0251  -0.1116 4   GLU A C   
19    O O   . GLU A  4   ? 0.6501 0.3639 0.7088 0.0577  0.0315  -0.1089 4   GLU A O   
20    C CB  . GLU A  4   ? 0.9860 0.6930 1.0469 0.0351  0.0069  -0.1097 4   GLU A CB  
21    C CG  . GLU A  4   ? 1.0349 0.7482 1.0988 0.0232  -0.0062 -0.1086 4   GLU A CG  
22    C CD  . GLU A  4   ? 1.0465 0.7858 1.1134 0.0214  -0.0094 -0.1002 4   GLU A CD  
23    O OE1 . GLU A  4   ? 1.0577 0.8087 1.1211 0.0287  -0.0017 -0.0963 4   GLU A OE1 
24    O OE2 . GLU A  4   ? 1.0210 0.7687 1.0948 0.0125  -0.0194 -0.0979 4   GLU A OE2 
25    N N   . ASP A  5   ? 0.6110 0.3444 0.6478 0.0527  0.0278  -0.1090 5   ASP A N   
26    C CA  . ASP A  5   ? 0.5414 0.2909 0.5885 0.0608  0.0385  -0.1023 5   ASP A CA  
27    C C   . ASP A  5   ? 0.4813 0.2472 0.5547 0.0599  0.0356  -0.0897 5   ASP A C   
28    O O   . ASP A  5   ? 0.4410 0.2198 0.5196 0.0531  0.0275  -0.0831 5   ASP A O   
29    C CB  . ASP A  5   ? 0.6225 0.3847 0.6554 0.0601  0.0405  -0.1014 5   ASP A CB  
30    C CG  . ASP A  5   ? 0.5996 0.3766 0.6408 0.0679  0.0529  -0.0969 5   ASP A CG  
31    O OD1 . ASP A  5   ? 0.5691 0.3495 0.6291 0.0741  0.0588  -0.0939 5   ASP A OD1 
32    O OD2 . ASP A  5   ? 0.5976 0.3828 0.6267 0.0675  0.0565  -0.0963 5   ASP A OD2 
33    N N   . PRO A  6   ? 0.5353 0.3005 0.6248 0.0675  0.0420  -0.0864 6   PRO A N   
34    C CA  . PRO A  6   ? 0.5078 0.2857 0.6199 0.0679  0.0393  -0.0745 6   PRO A CA  
35    C C   . PRO A  6   ? 0.4601 0.2638 0.5797 0.0682  0.0405  -0.0661 6   PRO A C   
36    O O   . PRO A  6   ? 0.4143 0.2309 0.5492 0.0670  0.0369  -0.0562 6   PRO A O   
37    C CB  . PRO A  6   ? 0.4335 0.2031 0.5564 0.0781  0.0468  -0.0750 6   PRO A CB  
38    C CG  . PRO A  6   ? 0.4661 0.2301 0.5765 0.0846  0.0565  -0.0848 6   PRO A CG  
39    C CD  . PRO A  6   ? 0.4894 0.2419 0.5758 0.0771  0.0524  -0.0938 6   PRO A CD  
40    N N   . GLN A  7   ? 0.3956 0.2055 0.5034 0.0699  0.0459  -0.0702 7   GLN A N   
41    C CA  . GLN A  7   ? 0.4663 0.2985 0.5796 0.0693  0.0471  -0.0631 7   GLN A CA  
42    C C   . GLN A  7   ? 0.4590 0.2979 0.5668 0.0602  0.0374  -0.0595 7   GLN A C   
43    O O   . GLN A  7   ? 0.4699 0.3265 0.5876 0.0584  0.0352  -0.0513 7   GLN A O   
44    C CB  . GLN A  7   ? 0.3770 0.2128 0.4807 0.0742  0.0576  -0.0681 7   GLN A CB  
45    C CG  . GLN A  7   ? 0.3860 0.2397 0.5085 0.0806  0.0649  -0.0626 7   GLN A CG  
46    C CD  . GLN A  7   ? 0.4280 0.2799 0.5694 0.0867  0.0645  -0.0596 7   GLN A CD  
47    O OE1 . GLN A  7   ? 0.4282 0.2932 0.5863 0.0870  0.0602  -0.0507 7   GLN A OE1 
48    N NE2 . GLN A  7   ? 0.4693 0.3034 0.6068 0.0919  0.0689  -0.0669 7   GLN A NE2 
49    N N   . LEU A  8   ? 0.4049 0.2299 0.4972 0.0546  0.0313  -0.0660 8   LEU A N   
50    C CA  . LEU A  8   ? 0.4031 0.2354 0.4916 0.0466  0.0216  -0.0631 8   LEU A CA  
51    C C   . LEU A  8   ? 0.3756 0.2073 0.4773 0.0400  0.0125  -0.0590 8   LEU A C   
52    O O   . LEU A  8   ? 0.3598 0.2013 0.4640 0.0339  0.0050  -0.0552 8   LEU A O   
53    C CB  . LEU A  8   ? 0.4876 0.3089 0.5513 0.0440  0.0188  -0.0719 8   LEU A CB  
54    C CG  . LEU A  8   ? 0.3980 0.2183 0.4456 0.0496  0.0289  -0.0758 8   LEU A CG  
55    C CD1 . LEU A  8   ? 0.4170 0.2282 0.4382 0.0462  0.0239  -0.0821 8   LEU A CD1 
56    C CD2 . LEU A  8   ? 0.3734 0.2139 0.4328 0.0524  0.0350  -0.0672 8   LEU A CD2 
57    N N   . LEU A  9   ? 0.3832 0.2031 0.4938 0.0416  0.0138  -0.0595 9   LEU A N   
58    C CA  . LEU A  9   ? 0.3691 0.1870 0.4934 0.0357  0.0074  -0.0546 9   LEU A CA  
59    C C   . LEU A  9   ? 0.3459 0.1798 0.4878 0.0383  0.0097  -0.0427 9   LEU A C   
60    O O   . LEU A  9   ? 0.3426 0.1787 0.4901 0.0463  0.0165  -0.0401 9   LEU A O   
61    C CB  . LEU A  9   ? 0.3926 0.1879 0.5171 0.0366  0.0086  -0.0600 9   LEU A CB  
62    C CG  . LEU A  9   ? 0.4830 0.2648 0.6073 0.0270  0.0002  -0.0644 9   LEU A CG  
63    C CD1 . LEU A  9   ? 0.4811 0.2442 0.6142 0.0277  0.0021  -0.0640 9   LEU A CD1 
64    C CD2 . LEU A  9   ? 0.4734 0.2717 0.6074 0.0186  -0.0073 -0.0576 9   LEU A CD2 
65    N N   . VAL A  10  ? 0.3309 0.1764 0.4816 0.0319  0.0041  -0.0359 10  VAL A N   
66    C CA  . VAL A  10  ? 0.3119 0.1710 0.4771 0.0339  0.0059  -0.0248 10  VAL A CA  
67    C C   . VAL A  10  ? 0.3270 0.1851 0.5023 0.0261  0.0008  -0.0195 10  VAL A C   
68    O O   . VAL A  10  ? 0.3126 0.1716 0.4862 0.0183  -0.0052 -0.0225 10  VAL A O   
69    C CB  . VAL A  10  ? 0.2901 0.1702 0.4553 0.0350  0.0065  -0.0206 10  VAL A CB  
70    C CG1 . VAL A  10  ? 0.2724 0.1659 0.4510 0.0363  0.0073  -0.0099 10  VAL A CG1 
71    C CG2 . VAL A  10  ? 0.4982 0.3801 0.6554 0.0421  0.0129  -0.0250 10  VAL A CG2 
72    N N   . ARG A  11  ? 0.3492 0.2048 0.5348 0.0283  0.0033  -0.0117 11  ARG A N   
73    C CA  . ARG A  11  ? 0.3501 0.2072 0.5457 0.0209  0.0004  -0.0046 11  ARG A CA  
74    C C   . ARG A  11  ? 0.3644 0.2409 0.5667 0.0225  0.0016  0.0055  11  ARG A C   
75    O O   . ARG A  11  ? 0.3821 0.2612 0.5870 0.0297  0.0053  0.0114  11  ARG A O   
76    C CB  . ARG A  11  ? 0.3259 0.1636 0.5265 0.0206  0.0021  -0.0019 11  ARG A CB  
77    C CG  . ARG A  11  ? 0.3246 0.1636 0.5356 0.0125  0.0008  0.0064  11  ARG A CG  
78    C CD  . ARG A  11  ? 0.3445 0.1629 0.5595 0.0126  0.0036  0.0109  11  ARG A CD  
79    N NE  . ARG A  11  ? 0.3438 0.1610 0.5586 0.0231  0.0078  0.0185  11  ARG A NE  
80    C CZ  . ARG A  11  ? 0.3321 0.1610 0.5507 0.0252  0.0094  0.0295  11  ARG A CZ  
81    N NH1 . ARG A  11  ? 0.3198 0.1623 0.5428 0.0175  0.0083  0.0339  11  ARG A NH1 
82    N NH2 . ARG A  11  ? 0.3339 0.1612 0.5517 0.0353  0.0118  0.0357  11  ARG A NH2 
83    N N   . VAL A  12  ? 0.2735 0.1637 0.4786 0.0162  -0.0018 0.0069  12  VAL A N   
84    C CA  . VAL A  12  ? 0.2556 0.1627 0.4665 0.0170  -0.0004 0.0159  12  VAL A CA  
85    C C   . VAL A  12  ? 0.2596 0.1643 0.4799 0.0104  -0.0003 0.0228  12  VAL A C   
86    O O   . VAL A  12  ? 0.2749 0.1660 0.4982 0.0044  -0.0018 0.0201  12  VAL A O   
87    C CB  . VAL A  12  ? 0.2428 0.1671 0.4515 0.0151  -0.0030 0.0140  12  VAL A CB  
88    C CG1 . VAL A  12  ? 0.2382 0.1634 0.4364 0.0208  -0.0021 0.0074  12  VAL A CG1 
89    C CG2 . VAL A  12  ? 0.2428 0.1680 0.4553 0.0061  -0.0084 0.0106  12  VAL A CG2 
90    N N   . ARG A  13  ? 0.2896 0.2071 0.5140 0.0110  0.0018  0.0314  13  ARG A N   
91    C CA  . ARG A  13  ? 0.3432 0.2588 0.5751 0.0058  0.0040  0.0396  13  ARG A CA  
92    C C   . ARG A  13  ? 0.2761 0.1892 0.5160 -0.0048 0.0012  0.0359  13  ARG A C   
93    O O   . ARG A  13  ? 0.2727 0.1735 0.5183 -0.0102 0.0029  0.0389  13  ARG A O   
94    C CB  . ARG A  13  ? 0.6563 0.5891 0.8894 0.0075  0.0062  0.0473  13  ARG A CB  
95    C CG  . ARG A  13  ? 0.7792 0.7082 1.0153 0.0059  0.0106  0.0579  13  ARG A CG  
96    C CD  . ARG A  13  ? 0.8754 0.7918 1.1053 0.0139  0.0126  0.0630  13  ARG A CD  
97    N NE  . ARG A  13  ? 0.9063 0.8332 1.1304 0.0231  0.0117  0.0632  13  ARG A NE  
98    C CZ  . ARG A  13  ? 0.8919 0.8303 1.1131 0.0263  0.0129  0.0698  13  ARG A CZ  
99    N NH1 . ARG A  13  ? 0.8778 0.8185 1.1000 0.0214  0.0160  0.0770  13  ARG A NH1 
100   N NH2 . ARG A  13  ? 0.8715 0.8191 1.0888 0.0340  0.0114  0.0687  13  ARG A NH2 
101   N N   . GLY A  14  ? 0.2494 0.1733 0.4898 -0.0078 -0.0034 0.0293  14  GLY A N   
102   C CA  . GLY A  14  ? 0.2539 0.1794 0.5041 -0.0178 -0.0074 0.0257  14  GLY A CA  
103   C C   . GLY A  14  ? 0.2714 0.1812 0.5198 -0.0220 -0.0123 0.0161  14  GLY A C   
104   O O   . GLY A  14  ? 0.2777 0.1879 0.5358 -0.0311 -0.0164 0.0125  14  GLY A O   
105   N N   . GLY A  15  ? 0.3826 0.2789 0.6190 -0.0157 -0.0119 0.0112  15  GLY A N   
106   C CA  . GLY A  15  ? 0.4033 0.2834 0.6347 -0.0188 -0.0164 0.0008  15  GLY A CA  
107   C C   . GLY A  15  ? 0.4052 0.2782 0.6208 -0.0105 -0.0164 -0.0064 15  GLY A C   
108   O O   . GLY A  15  ? 0.3857 0.2656 0.5958 -0.0020 -0.0122 -0.0030 15  GLY A O   
109   N N   . GLN A  16  ? 0.3336 0.1927 0.5419 -0.0131 -0.0208 -0.0169 16  GLN A N   
110   C CA  . GLN A  16  ? 0.3288 0.1793 0.5209 -0.0056 -0.0195 -0.0244 16  GLN A CA  
111   C C   . GLN A  16  ? 0.3426 0.2015 0.5238 -0.0062 -0.0252 -0.0313 16  GLN A C   
112   O O   . GLN A  16  ? 0.3663 0.2276 0.5499 -0.0137 -0.0330 -0.0357 16  GLN A O   
113   C CB  . GLN A  16  ? 0.3547 0.1807 0.5418 -0.0062 -0.0192 -0.0318 16  GLN A CB  
114   C CG  . GLN A  16  ? 0.3593 0.1748 0.5471 0.0018  -0.0114 -0.0272 16  GLN A CG  
115   C CD  . GLN A  16  ? 0.3865 0.1762 0.5713 0.0008  -0.0108 -0.0338 16  GLN A CD  
116   O OE1 . GLN A  16  ? 0.3955 0.1744 0.5898 -0.0028 -0.0095 -0.0289 16  GLN A OE1 
117   N NE2 . GLN A  16  ? 0.4021 0.1800 0.5723 0.0040  -0.0114 -0.0452 16  GLN A NE2 
118   N N   . LEU A  17  ? 0.3195 0.1829 0.4892 0.0018  -0.0214 -0.0321 17  LEU A N   
119   C CA  . LEU A  17  ? 0.3205 0.1887 0.4764 0.0022  -0.0258 -0.0382 17  LEU A CA  
120   C C   . LEU A  17  ? 0.3665 0.2223 0.5049 0.0093  -0.0207 -0.0451 17  LEU A C   
121   O O   . LEU A  17  ? 0.3625 0.2137 0.5026 0.0157  -0.0127 -0.0429 17  LEU A O   
122   C CB  . LEU A  17  ? 0.2973 0.1866 0.4568 0.0038  -0.0255 -0.0311 17  LEU A CB  
123   C CG  . LEU A  17  ? 0.2808 0.1789 0.4453 0.0106  -0.0171 -0.0230 17  LEU A CG  
124   C CD1 . LEU A  17  ? 0.2815 0.1790 0.4321 0.0179  -0.0118 -0.0262 17  LEU A CD1 
125   C CD2 . LEU A  17  ? 0.2598 0.1768 0.4359 0.0087  -0.0180 -0.0146 17  LEU A CD2 
126   N N   . ARG A  18  ? 0.3677 0.2180 0.4890 0.0085  -0.0252 -0.0534 18  ARG A N   
127   C CA  . ARG A  18  ? 0.4152 0.2546 0.5176 0.0152  -0.0194 -0.0600 18  ARG A CA  
128   C C   . ARG A  18  ? 0.3877 0.2382 0.4779 0.0177  -0.0194 -0.0589 18  ARG A C   
129   O O   . ARG A  18  ? 0.3822 0.2386 0.4687 0.0133  -0.0282 -0.0595 18  ARG A O   
130   C CB  . ARG A  18  ? 0.6703 0.4889 0.7583 0.0124  -0.0239 -0.0718 18  ARG A CB  
131   C CG  . ARG A  18  ? 0.7579 0.5683 0.8200 0.0166  -0.0223 -0.0798 18  ARG A CG  
132   C CD  . ARG A  18  ? 0.8484 0.6408 0.8947 0.0119  -0.0308 -0.0916 18  ARG A CD  
133   N NE  . ARG A  18  ? 0.8907 0.6890 0.9480 0.0027  -0.0437 -0.0915 18  ARG A NE  
134   C CZ  . ARG A  18  ? 0.9134 0.7038 0.9846 -0.0039 -0.0482 -0.0939 18  ARG A CZ  
135   N NH1 . ARG A  18  ? 0.8834 0.6579 0.9573 -0.0017 -0.0412 -0.0964 18  ARG A NH1 
136   N NH2 . ARG A  18  ? 0.9188 0.7171 1.0019 -0.0126 -0.0595 -0.0938 18  ARG A NH2 
137   N N   . GLY A  19  ? 0.4156 0.2692 0.5009 0.0248  -0.0095 -0.0569 19  GLY A N   
138   C CA  . GLY A  19  ? 0.3439 0.2055 0.4166 0.0274  -0.0074 -0.0556 19  GLY A CA  
139   C C   . GLY A  19  ? 0.3788 0.2256 0.4259 0.0304  -0.0042 -0.0645 19  GLY A C   
140   O O   . GLY A  19  ? 0.3920 0.2220 0.4281 0.0291  -0.0070 -0.0731 19  GLY A O   
141   N N   . ILE A  20  ? 0.4580 0.3098 0.4944 0.0342  0.0023  -0.0624 20  ILE A N   
142   C CA  . ILE A  20  ? 0.5029 0.3412 0.5120 0.0368  0.0058  -0.0697 20  ILE A CA  
143   C C   . ILE A  20  ? 0.4873 0.3287 0.4932 0.0428  0.0204  -0.0679 20  ILE A C   
144   O O   . ILE A  20  ? 0.4444 0.3016 0.4658 0.0438  0.0246  -0.0601 20  ILE A O   
145   C CB  . ILE A  20  ? 0.3982 0.2370 0.3904 0.0336  -0.0041 -0.0696 20  ILE A CB  
146   C CG1 . ILE A  20  ? 0.4418 0.2626 0.4020 0.0359  -0.0023 -0.0780 20  ILE A CG1 
147   C CG2 . ILE A  20  ? 0.3772 0.2322 0.3751 0.0344  -0.0022 -0.0603 20  ILE A CG2 
148   C CD1 . ILE A  20  ? 0.4788 0.3010 0.4199 0.0359  -0.0068 -0.0753 20  ILE A CD1 
149   N N   . ARG A  21  ? 0.5064 0.3329 0.4931 0.0465  0.0284  -0.0756 21  ARG A N   
150   C CA  . ARG A  21  ? 0.5421 0.3717 0.5260 0.0517  0.0433  -0.0747 21  ARG A CA  
151   C C   . ARG A  21  ? 0.5765 0.4044 0.5374 0.0512  0.0453  -0.0733 21  ARG A C   
152   O O   . ARG A  21  ? 0.6460 0.4588 0.5800 0.0505  0.0414  -0.0791 21  ARG A O   
153   C CB  . ARG A  21  ? 0.6085 0.4234 0.5847 0.0567  0.0533  -0.0835 21  ARG A CB  
154   C CG  . ARG A  21  ? 0.6011 0.4248 0.5895 0.0625  0.0689  -0.0816 21  ARG A CG  
155   C CD  . ARG A  21  ? 0.6515 0.4604 0.6321 0.0682  0.0793  -0.0910 21  ARG A CD  
156   N NE  . ARG A  21  ? 0.7591 0.5575 0.7121 0.0700  0.0894  -0.0962 21  ARG A NE  
157   C CZ  . ARG A  21  ? 0.8743 0.6683 0.8246 0.0760  0.1050  -0.1013 21  ARG A CZ  
158   N NH1 . ARG A  21  ? 0.8965 0.6961 0.8712 0.0812  0.1112  -0.1023 21  ARG A NH1 
159   N NH2 . ARG A  21  ? 0.9345 0.7182 0.8574 0.0771  0.1148  -0.1054 21  ARG A NH2 
160   N N   . LEU A  22  ? 0.5292 0.3718 0.5000 0.0516  0.0510  -0.0655 22  LEU A N   
161   C CA  . LEU A  22  ? 0.5175 0.3586 0.4686 0.0511  0.0540  -0.0626 22  LEU A CA  
162   C C   . LEU A  22  ? 0.5978 0.4378 0.5443 0.0548  0.0716  -0.0637 22  LEU A C   
163   O O   . LEU A  22  ? 0.5610 0.4100 0.5293 0.0574  0.0800  -0.0636 22  LEU A O   
164   C CB  . LEU A  22  ? 0.3868 0.2443 0.3524 0.0483  0.0482  -0.0532 22  LEU A CB  
165   C CG  . LEU A  22  ? 0.3844 0.2459 0.3569 0.0444  0.0317  -0.0511 22  LEU A CG  
166   C CD1 . LEU A  22  ? 0.3891 0.2629 0.3672 0.0426  0.0273  -0.0427 22  LEU A CD1 
167   C CD2 . LEU A  22  ? 0.4038 0.2488 0.3526 0.0433  0.0222  -0.0582 22  LEU A CD2 
168   N N   . LYS A  23  ? 0.7462 0.5749 0.6644 0.0552  0.0772  -0.0647 23  LYS A N   
169   C CA  . LYS A  23  ? 0.7980 0.6270 0.7126 0.0577  0.0953  -0.0644 23  LYS A CA  
170   C C   . LYS A  23  ? 0.7631 0.6049 0.6860 0.0552  0.0981  -0.0552 23  LYS A C   
171   O O   . LYS A  23  ? 0.7781 0.6145 0.6827 0.0531  0.0924  -0.0511 23  LYS A O   
172   C CB  . LYS A  23  ? 0.9492 0.7568 0.8269 0.0598  0.1031  -0.0709 23  LYS A CB  
173   C CG  . LYS A  23  ? 1.0301 0.8259 0.9028 0.0638  0.1088  -0.0813 23  LYS A CG  
174   C CD  . LYS A  23  ? 1.0495 0.8544 0.9430 0.0678  0.1267  -0.0829 23  LYS A CD  
175   C CE  . LYS A  23  ? 1.1411 0.9377 1.0397 0.0725  0.1296  -0.0925 23  LYS A CE  
176   N NZ  . LYS A  23  ? 1.1414 0.9137 1.0054 0.0752  0.1348  -0.1027 23  LYS A NZ  
177   N N   . ALA A  24  ? 0.7225 0.5813 0.6744 0.0555  0.1058  -0.0521 24  ALA A N   
178   C CA  . ALA A  24  ? 0.6747 0.5446 0.6357 0.0532  0.1128  -0.0452 24  ALA A CA  
179   C C   . ALA A  24  ? 0.6808 0.5437 0.6290 0.0547  0.1314  -0.0480 24  ALA A C   
180   O O   . ALA A  24  ? 0.7366 0.5902 0.6762 0.0582  0.1387  -0.0552 24  ALA A O   
181   C CB  . ALA A  24  ? 0.5721 0.4634 0.5697 0.0529  0.1119  -0.0419 24  ALA A CB  
182   N N   . PRO A  25  ? 0.5553 0.4215 0.5016 0.0518  0.1400  -0.0425 25  PRO A N   
183   C CA  . PRO A  25  ? 0.5928 0.4514 0.5257 0.0526  0.1591  -0.0448 25  PRO A CA  
184   C C   . PRO A  25  ? 0.5901 0.4595 0.5473 0.0559  0.1714  -0.0504 25  PRO A C   
185   O O   . PRO A  25  ? 0.5901 0.4481 0.5324 0.0593  0.1823  -0.0569 25  PRO A O   
186   C CB  . PRO A  25  ? 0.5784 0.4430 0.5153 0.0479  0.1650  -0.0370 25  PRO A CB  
187   C CG  . PRO A  25  ? 0.5538 0.4169 0.4844 0.0459  0.1474  -0.0315 25  PRO A CG  
188   C CD  . PRO A  25  ? 0.5199 0.3922 0.4695 0.0478  0.1331  -0.0344 25  PRO A CD  
189   N N   . GLY A  26  ? 0.6045 0.4951 0.5979 0.0555  0.1689  -0.0482 26  GLY A N   
190   C CA  . GLY A  26  ? 0.5956 0.4991 0.6156 0.0592  0.1798  -0.0527 26  GLY A CA  
191   C C   . GLY A  26  ? 0.5905 0.4878 0.6113 0.0653  0.1768  -0.0601 26  GLY A C   
192   O O   . GLY A  26  ? 0.5819 0.4779 0.6059 0.0696  0.1902  -0.0660 26  GLY A O   
193   N N   . GLY A  27  ? 0.7092 0.6020 0.7272 0.0655  0.1599  -0.0597 27  GLY A N   
194   C CA  . GLY A  27  ? 0.7411 0.6289 0.7645 0.0705  0.1549  -0.0657 27  GLY A CA  
195   C C   . GLY A  27  ? 0.7555 0.6321 0.7639 0.0684  0.1373  -0.0652 27  GLY A C   
196   O O   . GLY A  27  ? 0.8021 0.6720 0.7906 0.0642  0.1310  -0.0618 27  GLY A O   
197   N N   . PRO A  28  ? 0.6197 0.4926 0.6364 0.0714  0.1298  -0.0690 28  PRO A N   
198   C CA  . PRO A  28  ? 0.5666 0.4326 0.5739 0.0677  0.1128  -0.0674 28  PRO A CA  
199   C C   . PRO A  28  ? 0.5094 0.3931 0.5443 0.0657  0.1027  -0.0600 28  PRO A C   
200   O O   . PRO A  28  ? 0.4664 0.3656 0.5264 0.0681  0.1082  -0.0574 28  PRO A O   
201   C CB  . PRO A  28  ? 0.4275 0.2776 0.4271 0.0711  0.1106  -0.0758 28  PRO A CB  
202   C CG  . PRO A  28  ? 0.4271 0.2828 0.4458 0.0777  0.1239  -0.0794 28  PRO A CG  
203   C CD  . PRO A  28  ? 0.4463 0.3201 0.4802 0.0776  0.1348  -0.0743 28  PRO A CD  
204   N N   . VAL A  29  ? 0.3612 0.2426 0.3917 0.0617  0.0881  -0.0572 29  VAL A N   
205   C CA  . VAL A  29  ? 0.3337 0.2298 0.3872 0.0595  0.0783  -0.0504 29  VAL A CA  
206   C C   . VAL A  29  ? 0.3369 0.2242 0.3864 0.0571  0.0652  -0.0517 29  VAL A C   
207   O O   . VAL A  29  ? 0.3584 0.2300 0.3863 0.0559  0.0617  -0.0573 29  VAL A O   
208   C CB  . VAL A  29  ? 0.3173 0.2249 0.3725 0.0554  0.0749  -0.0429 29  VAL A CB  
209   C CG1 . VAL A  29  ? 0.3103 0.2291 0.3746 0.0563  0.0868  -0.0405 29  VAL A CG1 
210   C CG2 . VAL A  29  ? 0.3325 0.2283 0.3614 0.0521  0.0689  -0.0434 29  VAL A CG2 
211   N N   . SER A  30  ? 0.4608 0.3586 0.5315 0.0561  0.0580  -0.0467 30  SER A N   
212   C CA  . SER A  30  ? 0.4502 0.3421 0.5224 0.0529  0.0463  -0.0469 30  SER A CA  
213   C C   . SER A  30  ? 0.4209 0.3232 0.4960 0.0479  0.0373  -0.0403 30  SER A C   
214   O O   . SER A  30  ? 0.4376 0.3549 0.5269 0.0479  0.0385  -0.0339 30  SER A O   
215   C CB  . SER A  30  ? 0.5042 0.3994 0.5978 0.0555  0.0458  -0.0451 30  SER A CB  
216   O OG  . SER A  30  ? 0.5579 0.4478 0.6540 0.0617  0.0556  -0.0499 30  SER A OG  
217   N N   . ALA A  31  ? 0.3107 0.2051 0.3724 0.0440  0.0281  -0.0425 31  ALA A N   
218   C CA  . ALA A  31  ? 0.2972 0.2012 0.3624 0.0399  0.0192  -0.0369 31  ALA A CA  
219   C C   . ALA A  31  ? 0.2965 0.1988 0.3699 0.0357  0.0086  -0.0373 31  ALA A C   
220   O O   . ALA A  31  ? 0.3173 0.2061 0.3806 0.0342  0.0043  -0.0439 31  ALA A O   
221   C CB  . ALA A  31  ? 0.3104 0.2087 0.3532 0.0391  0.0172  -0.0383 31  ALA A CB  
222   N N   . PHE A  32  ? 0.3060 0.2216 0.3978 0.0335  0.0047  -0.0306 32  PHE A N   
223   C CA  . PHE A  32  ? 0.3299 0.2455 0.4315 0.0287  -0.0043 -0.0300 32  PHE A CA  
224   C C   . PHE A  32  ? 0.3394 0.2666 0.4441 0.0256  -0.0113 -0.0255 32  PHE A C   
225   O O   . PHE A  32  ? 0.3488 0.2892 0.4645 0.0264  -0.0089 -0.0190 32  PHE A O   
226   C CB  . PHE A  32  ? 0.2626 0.1826 0.3836 0.0293  -0.0015 -0.0256 32  PHE A CB  
227   C CG  . PHE A  32  ? 0.2884 0.1977 0.4084 0.0338  0.0056  -0.0294 32  PHE A CG  
228   C CD1 . PHE A  32  ? 0.2674 0.1820 0.3897 0.0395  0.0146  -0.0279 32  PHE A CD1 
229   C CD2 . PHE A  32  ? 0.2910 0.1849 0.4086 0.0324  0.0033  -0.0350 32  PHE A CD2 
230   C CE1 . PHE A  32  ? 0.2776 0.1838 0.4011 0.0445  0.0212  -0.0316 32  PHE A CE1 
231   C CE2 . PHE A  32  ? 0.3023 0.1858 0.4192 0.0375  0.0102  -0.0387 32  PHE A CE2 
232   C CZ  . PHE A  32  ? 0.2952 0.1854 0.4155 0.0440  0.0192  -0.0369 32  PHE A CZ  
233   N N   . LEU A  33  ? 0.2747 0.1973 0.3700 0.0225  -0.0203 -0.0294 33  LEU A N   
234   C CA  . LEU A  33  ? 0.2671 0.2000 0.3627 0.0212  -0.0268 -0.0258 33  LEU A CA  
235   C C   . LEU A  33  ? 0.2649 0.2036 0.3733 0.0158  -0.0372 -0.0258 33  LEU A C   
236   O O   . LEU A  33  ? 0.2805 0.2101 0.3856 0.0124  -0.0437 -0.0320 33  LEU A O   
237   C CB  . LEU A  33  ? 0.2849 0.2089 0.3564 0.0233  -0.0291 -0.0297 33  LEU A CB  
238   C CG  . LEU A  33  ? 0.3422 0.2577 0.3977 0.0279  -0.0182 -0.0312 33  LEU A CG  
239   C CD1 . LEU A  33  ? 0.3943 0.2987 0.4233 0.0293  -0.0216 -0.0350 33  LEU A CD1 
240   C CD2 . LEU A  33  ? 0.3043 0.2316 0.3692 0.0303  -0.0099 -0.0243 33  LEU A CD2 
241   N N   . GLY A  34  ? 0.2700 0.2240 0.3934 0.0148  -0.0389 -0.0195 34  GLY A N   
242   C CA  . GLY A  34  ? 0.2969 0.2586 0.4337 0.0098  -0.0483 -0.0195 34  GLY A CA  
243   C C   . GLY A  34  ? 0.2951 0.2586 0.4508 0.0052  -0.0467 -0.0179 34  GLY A C   
244   O O   . GLY A  34  ? 0.2831 0.2471 0.4486 -0.0005 -0.0538 -0.0207 34  GLY A O   
245   N N   . ILE A  35  ? 0.2294 0.1936 0.3901 0.0076  -0.0374 -0.0134 35  ILE A N   
246   C CA  . ILE A  35  ? 0.2241 0.1895 0.4010 0.0044  -0.0343 -0.0098 35  ILE A CA  
247   C C   . ILE A  35  ? 0.2800 0.2617 0.4731 0.0018  -0.0358 -0.0038 35  ILE A C   
248   O O   . ILE A  35  ? 0.1958 0.1877 0.3894 0.0054  -0.0324 0.0010  35  ILE A O   
249   C CB  . ILE A  35  ? 0.2182 0.1810 0.3937 0.0094  -0.0249 -0.0062 35  ILE A CB  
250   C CG1 . ILE A  35  ? 0.2311 0.1813 0.3894 0.0136  -0.0221 -0.0122 35  ILE A CG1 
251   C CG2 . ILE A  35  ? 0.2184 0.1778 0.4066 0.0070  -0.0219 -0.0026 35  ILE A CG2 
252   C CD1 . ILE A  35  ? 0.2293 0.1755 0.3883 0.0185  -0.0137 -0.0105 35  ILE A CD1 
253   N N   . PRO A  36  ? 0.2126 0.1969 0.4193 -0.0047 -0.0407 -0.0045 36  PRO A N   
254   C CA  . PRO A  36  ? 0.3002 0.3011 0.5235 -0.0071 -0.0409 0.0011  36  PRO A CA  
255   C C   . PRO A  36  ? 0.2810 0.2861 0.5118 -0.0058 -0.0317 0.0091  36  PRO A C   
256   O O   . PRO A  36  ? 0.2874 0.2836 0.5212 -0.0077 -0.0279 0.0106  36  PRO A O   
257   C CB  . PRO A  36  ? 0.2792 0.2802 0.5164 -0.0152 -0.0472 -0.0021 36  PRO A CB  
258   C CG  . PRO A  36  ? 0.3287 0.3110 0.5590 -0.0172 -0.0464 -0.0066 36  PRO A CG  
259   C CD  . PRO A  36  ? 0.2292 0.2015 0.4380 -0.0104 -0.0450 -0.0102 36  PRO A CD  
260   N N   . PHE A  37  ? 0.3112 0.3287 0.5441 -0.0023 -0.0284 0.0140  37  PHE A N   
261   C CA  . PHE A  37  ? 0.2793 0.3011 0.5177 -0.0011 -0.0206 0.0212  37  PHE A CA  
262   C C   . PHE A  37  ? 0.2623 0.2961 0.5172 -0.0055 -0.0195 0.0255  37  PHE A C   
263   O O   . PHE A  37  ? 0.2691 0.3063 0.5284 -0.0053 -0.0129 0.0318  37  PHE A O   
264   C CB  . PHE A  37  ? 0.2233 0.2492 0.4522 0.0057  -0.0164 0.0236  37  PHE A CB  
265   C CG  . PHE A  37  ? 0.2066 0.2441 0.4360 0.0076  -0.0184 0.0237  37  PHE A CG  
266   C CD1 . PHE A  37  ? 0.1917 0.2269 0.4113 0.0098  -0.0234 0.0190  37  PHE A CD1 
267   C CD2 . PHE A  37  ? 0.2009 0.2504 0.4391 0.0079  -0.0149 0.0287  37  PHE A CD2 
268   C CE1 . PHE A  37  ? 0.1787 0.2228 0.3982 0.0122  -0.0253 0.0196  37  PHE A CE1 
269   C CE2 . PHE A  37  ? 0.1862 0.2453 0.4251 0.0104  -0.0165 0.0286  37  PHE A CE2 
270   C CZ  . PHE A  37  ? 0.1744 0.2306 0.4044 0.0126  -0.0220 0.0242  37  PHE A CZ  
271   N N   . ALA A  38  ? 0.1928 0.2336 0.4569 -0.0093 -0.0259 0.0220  38  ALA A N   
272   C CA  . ALA A  38  ? 0.2052 0.2597 0.4875 -0.0134 -0.0242 0.0256  38  ALA A CA  
273   C C   . ALA A  38  ? 0.2651 0.3238 0.5614 -0.0200 -0.0320 0.0207  38  ALA A C   
274   O O   . ALA A  38  ? 0.3353 0.3900 0.6251 -0.0196 -0.0408 0.0142  38  ALA A O   
275   C CB  . ALA A  38  ? 0.1630 0.2309 0.4455 -0.0083 -0.0222 0.0283  38  ALA A CB  
276   N N   . GLU A  39  ? 0.2111 0.2777 0.5264 -0.0263 -0.0287 0.0238  39  GLU A N   
277   C CA  . GLU A  39  ? 0.2243 0.2990 0.5575 -0.0330 -0.0361 0.0192  39  GLU A CA  
278   C C   . GLU A  39  ? 0.2027 0.2923 0.5388 -0.0280 -0.0422 0.0171  39  GLU A C   
279   O O   . GLU A  39  ? 0.1914 0.2901 0.5270 -0.0228 -0.0364 0.0218  39  GLU A O   
280   C CB  . GLU A  39  ? 0.3575 0.4391 0.7120 -0.0408 -0.0290 0.0239  39  GLU A CB  
281   C CG  . GLU A  39  ? 0.4525 0.5173 0.8069 -0.0475 -0.0263 0.0242  39  GLU A CG  
282   C CD  . GLU A  39  ? 0.5591 0.6203 0.9237 -0.0554 -0.0363 0.0160  39  GLU A CD  
283   O OE1 . GLU A  39  ? 0.6044 0.6816 0.9890 -0.0599 -0.0416 0.0130  39  GLU A OE1 
284   O OE2 . GLU A  39  ? 0.5691 0.6117 0.9223 -0.0569 -0.0392 0.0119  39  GLU A OE2 
285   N N   . PRO A  40  ? 0.2040 0.2948 0.5414 -0.0291 -0.0543 0.0100  40  PRO A N   
286   C CA  . PRO A  40  ? 0.2089 0.3113 0.5470 -0.0236 -0.0623 0.0076  40  PRO A CA  
287   C C   . PRO A  40  ? 0.1980 0.3214 0.5586 -0.0233 -0.0589 0.0114  40  PRO A C   
288   O O   . PRO A  40  ? 0.1559 0.2899 0.5403 -0.0305 -0.0583 0.0113  40  PRO A O   
289   C CB  . PRO A  40  ? 0.1789 0.2794 0.5203 -0.0279 -0.0761 -0.0006 40  PRO A CB  
290   C CG  . PRO A  40  ? 0.1972 0.2904 0.5485 -0.0375 -0.0740 -0.0022 40  PRO A CG  
291   C CD  . PRO A  40  ? 0.1841 0.2637 0.5215 -0.0357 -0.0618 0.0033  40  PRO A CD  
292   N N   . PRO A  41  ? 0.2681 0.3973 0.6215 -0.0150 -0.0565 0.0143  41  PRO A N   
293   C CA  . PRO A  41  ? 0.2511 0.3981 0.6217 -0.0128 -0.0511 0.0180  41  PRO A CA  
294   C C   . PRO A  41  ? 0.2478 0.4055 0.6269 -0.0116 -0.0608 0.0135  41  PRO A C   
295   O O   . PRO A  41  ? 0.2890 0.4513 0.6616 -0.0039 -0.0621 0.0141  41  PRO A O   
296   C CB  . PRO A  41  ? 0.1861 0.3293 0.5388 -0.0038 -0.0459 0.0214  41  PRO A CB  
297   C CG  . PRO A  41  ? 0.1790 0.3070 0.5082 -0.0002 -0.0534 0.0178  41  PRO A CG  
298   C CD  . PRO A  41  ? 0.1946 0.3115 0.5213 -0.0072 -0.0571 0.0142  41  PRO A CD  
299   N N   . VAL A  42  ? 0.1524 0.3136 0.5456 -0.0189 -0.0677 0.0092  42  VAL A N   
300   C CA  . VAL A  42  ? 0.1854 0.3573 0.5869 -0.0174 -0.0786 0.0045  42  VAL A CA  
301   C C   . VAL A  42  ? 0.2277 0.4136 0.6503 -0.0230 -0.0741 0.0044  42  VAL A C   
302   O O   . VAL A  42  ? 0.2182 0.4032 0.6496 -0.0302 -0.0644 0.0070  42  VAL A O   
303   C CB  . VAL A  42  ? 0.1712 0.3366 0.5697 -0.0199 -0.0946 -0.0025 42  VAL A CB  
304   C CG1 . VAL A  42  ? 0.1691 0.3179 0.5466 -0.0170 -0.0961 -0.0025 42  VAL A CG1 
305   C CG2 . VAL A  42  ? 0.1806 0.3463 0.5946 -0.0311 -0.0965 -0.0064 42  VAL A CG2 
306   N N   . GLY A  43  ? 0.3589 0.5577 0.7896 -0.0193 -0.0811 0.0017  43  GLY A N   
307   C CA  . GLY A  43  ? 0.4076 0.6222 0.8599 -0.0236 -0.0768 0.0014  43  GLY A CA  
308   C C   . GLY A  43  ? 0.4223 0.6412 0.8759 -0.0218 -0.0602 0.0076  43  GLY A C   
309   O O   . GLY A  43  ? 0.4510 0.6700 0.8933 -0.0132 -0.0564 0.0103  43  GLY A O   
310   N N   . SER A  44  ? 0.3639 0.5853 0.8302 -0.0300 -0.0504 0.0097  44  SER A N   
311   C CA  . SER A  44  ? 0.3518 0.5768 0.8189 -0.0292 -0.0344 0.0154  44  SER A CA  
312   C C   . SER A  44  ? 0.3211 0.5319 0.7670 -0.0252 -0.0264 0.0205  44  SER A C   
313   O O   . SER A  44  ? 0.3220 0.5344 0.7644 -0.0230 -0.0141 0.0251  44  SER A O   
314   C CB  . SER A  44  ? 0.4155 0.6452 0.9005 -0.0395 -0.0261 0.0167  44  SER A CB  
315   O OG  . SER A  44  ? 0.4551 0.6745 0.9422 -0.0479 -0.0318 0.0144  44  SER A OG  
316   N N   . ARG A  45  ? 0.3293 0.5267 0.7614 -0.0242 -0.0334 0.0195  45  ARG A N   
317   C CA  . ARG A  45  ? 0.3756 0.5610 0.7889 -0.0201 -0.0267 0.0239  45  ARG A CA  
318   C C   . ARG A  45  ? 0.3529 0.5372 0.7506 -0.0098 -0.0299 0.0236  45  ARG A C   
319   O O   . ARG A  45  ? 0.3828 0.5574 0.7644 -0.0059 -0.0254 0.0266  45  ARG A O   
320   C CB  . ARG A  45  ? 0.4843 0.6550 0.8913 -0.0248 -0.0298 0.0238  45  ARG A CB  
321   C CG  . ARG A  45  ? 0.5606 0.7271 0.9773 -0.0342 -0.0220 0.0267  45  ARG A CG  
322   C CD  . ARG A  45  ? 0.6159 0.7878 1.0348 -0.0342 -0.0073 0.0329  45  ARG A CD  
323   N NE  . ARG A  45  ? 0.6481 0.8111 1.0503 -0.0297 0.0011  0.0386  45  ARG A NE  
324   C CZ  . ARG A  45  ? 0.6538 0.8187 1.0536 -0.0290 0.0137  0.0443  45  ARG A CZ  
325   N NH1 . ARG A  45  ? 0.7028 0.8780 1.1160 -0.0327 0.0201  0.0450  45  ARG A NH1 
326   N NH2 . ARG A  45  ? 0.5919 0.7488 0.9760 -0.0247 0.0197  0.0490  45  ARG A NH2 
327   N N   . ARG A  46  ? 0.1959 0.3898 0.5988 -0.0053 -0.0376 0.0201  46  ARG A N   
328   C CA  . ARG A  46  ? 0.1376 0.3293 0.5261 0.0045  -0.0412 0.0199  46  ARG A CA  
329   C C   . ARG A  46  ? 0.1332 0.3280 0.5168 0.0093  -0.0291 0.0234  46  ARG A C   
330   O O   . ARG A  46  ? 0.1357 0.3413 0.5323 0.0072  -0.0219 0.0243  46  ARG A O   
331   C CB  . ARG A  46  ? 0.1447 0.3451 0.5402 0.0083  -0.0536 0.0156  46  ARG A CB  
332   C CG  . ARG A  46  ? 0.1443 0.3405 0.5245 0.0185  -0.0581 0.0159  46  ARG A CG  
333   C CD  . ARG A  46  ? 0.2400 0.4480 0.6301 0.0234  -0.0672 0.0131  46  ARG A CD  
334   N NE  . ARG A  46  ? 0.2481 0.4532 0.6361 0.0237  -0.0831 0.0093  46  ARG A NE  
335   C CZ  . ARG A  46  ? 0.2391 0.4546 0.6371 0.0263  -0.0938 0.0063  46  ARG A CZ  
336   N NH1 . ARG A  46  ? 0.2164 0.4471 0.6297 0.0289  -0.0900 0.0066  46  ARG A NH1 
337   N NH2 . ARG A  46  ? 0.2340 0.4446 0.6264 0.0267  -0.1089 0.0028  46  ARG A NH2 
338   N N   . PHE A  47  ? 0.2237 0.4087 0.5885 0.0154  -0.0271 0.0251  47  PHE A N   
339   C CA  . PHE A  47  ? 0.2036 0.3881 0.5596 0.0199  -0.0163 0.0278  47  PHE A CA  
340   C C   . PHE A  47  ? 0.1766 0.3563 0.5290 0.0154  -0.0052 0.0318  47  PHE A C   
341   O O   . PHE A  47  ? 0.1609 0.3401 0.5060 0.0185  0.0037  0.0339  47  PHE A O   
342   C CB  . PHE A  47  ? 0.1762 0.3740 0.5432 0.0237  -0.0132 0.0267  47  PHE A CB  
343   C CG  . PHE A  47  ? 0.1823 0.3857 0.5539 0.0291  -0.0241 0.0235  47  PHE A CG  
344   C CD1 . PHE A  47  ? 0.2023 0.3975 0.5589 0.0367  -0.0293 0.0231  47  PHE A CD1 
345   C CD2 . PHE A  47  ? 0.1714 0.3885 0.5627 0.0267  -0.0291 0.0210  47  PHE A CD2 
346   C CE1 . PHE A  47  ? 0.2154 0.4150 0.5755 0.0423  -0.0396 0.0209  47  PHE A CE1 
347   C CE2 . PHE A  47  ? 0.1456 0.3685 0.5411 0.0324  -0.0399 0.0184  47  PHE A CE2 
348   C CZ  . PHE A  47  ? 0.2029 0.4166 0.5822 0.0404  -0.0452 0.0186  47  PHE A CZ  
349   N N   . MET A  48  ? 0.1958 0.3717 0.5534 0.0082  -0.0059 0.0329  48  MET A N   
350   C CA  . MET A  48  ? 0.2172 0.3895 0.5741 0.0037  0.0046  0.0375  48  MET A CA  
351   C C   . MET A  48  ? 0.2968 0.4558 0.6401 0.0036  0.0042  0.0396  48  MET A C   
352   O O   . MET A  48  ? 0.3474 0.5004 0.6872 0.0038  -0.0047 0.0370  48  MET A O   
353   C CB  . MET A  48  ? 0.1279 0.3057 0.5032 -0.0049 0.0060  0.0380  48  MET A CB  
354   C CG  . MET A  48  ? 0.1332 0.3261 0.5256 -0.0056 0.0057  0.0354  48  MET A CG  
355   S SD  . MET A  48  ? 0.6285 0.8293 1.0325 -0.0106 0.0208  0.0397  48  MET A SD  
356   C CE  . MET A  48  ? 0.1359 0.3251 0.5186 -0.0070 0.0312  0.0455  48  MET A CE  
357   N N   . PRO A  49  ? 0.2685 0.4232 0.6043 0.0035  0.0137  0.0444  49  PRO A N   
358   C CA  . PRO A  49  ? 0.2295 0.3729 0.5538 0.0037  0.0142  0.0470  49  PRO A CA  
359   C C   . PRO A  49  ? 0.2188 0.3567 0.5513 -0.0023 0.0088  0.0465  49  PRO A C   
360   O O   . PRO A  49  ? 0.2204 0.3622 0.5676 -0.0088 0.0088  0.0464  49  PRO A O   
361   C CB  . PRO A  49  ? 0.1152 0.2584 0.4362 0.0032  0.0257  0.0529  49  PRO A CB  
362   C CG  . PRO A  49  ? 0.1210 0.2745 0.4540 0.0006  0.0317  0.0535  49  PRO A CG  
363   C CD  . PRO A  49  ? 0.1400 0.3010 0.4776 0.0039  0.0247  0.0477  49  PRO A CD  
364   N N   . PRO A  50  ? 0.2464 0.3736 0.5669 -0.0003 0.0043  0.0454  50  PRO A N   
365   C CA  . PRO A  50  ? 0.3158 0.4332 0.6363 -0.0053 -0.0017 0.0428  50  PRO A CA  
366   C C   . PRO A  50  ? 0.3957 0.5068 0.7198 -0.0114 0.0047  0.0473  50  PRO A C   
367   O O   . PRO A  50  ? 0.4214 0.5270 0.7349 -0.0092 0.0118  0.0522  50  PRO A O   
368   C CB  . PRO A  50  ? 0.2578 0.3626 0.5573 -0.0004 -0.0054 0.0406  50  PRO A CB  
369   C CG  . PRO A  50  ? 0.1134 0.2192 0.4027 0.0049  0.0013  0.0440  50  PRO A CG  
370   C CD  . PRO A  50  ? 0.1091 0.2291 0.4099 0.0062  0.0052  0.0456  50  PRO A CD  
371   N N   . GLU A  51  ? 0.3440 0.4551 0.6826 -0.0188 0.0019  0.0456  51  GLU A N   
372   C CA  . GLU A  51  ? 0.3825 0.4822 0.7217 -0.0248 0.0063  0.0491  51  GLU A CA  
373   C C   . GLU A  51  ? 0.3737 0.4563 0.6968 -0.0230 0.0006  0.0457  51  GLU A C   
374   O O   . GLU A  51  ? 0.3924 0.4736 0.7120 -0.0216 -0.0083 0.0392  51  GLU A O   
375   C CB  . GLU A  51  ? 0.6303 0.7359 0.9923 -0.0342 0.0055  0.0478  51  GLU A CB  
376   C CG  . GLU A  51  ? 0.7383 0.8619 1.1196 -0.0367 0.0126  0.0510  51  GLU A CG  
377   C CD  . GLU A  51  ? 0.8403 0.9683 1.2399 -0.0455 0.0107  0.0480  51  GLU A CD  
378   O OE1 . GLU A  51  ? 0.8622 0.9962 1.2693 -0.0463 0.0000  0.0407  51  GLU A OE1 
379   O OE2 . GLU A  51  ? 0.8690 0.9940 1.2742 -0.0515 0.0199  0.0529  51  GLU A OE2 
380   N N   . PRO A  52  ? 0.4423 0.5114 0.7548 -0.0226 0.0057  0.0502  52  PRO A N   
381   C CA  . PRO A  52  ? 0.4270 0.4803 0.7252 -0.0200 0.0016  0.0471  52  PRO A CA  
382   C C   . PRO A  52  ? 0.4977 0.5419 0.8027 -0.0266 -0.0042 0.0418  52  PRO A C   
383   O O   . PRO A  52  ? 0.5403 0.5875 0.8614 -0.0344 -0.0031 0.0426  52  PRO A O   
384   C CB  . PRO A  52  ? 0.1658 0.2095 0.4553 -0.0179 0.0092  0.0544  52  PRO A CB  
385   C CG  . PRO A  52  ? 0.1711 0.2196 0.4734 -0.0241 0.0161  0.0603  52  PRO A CG  
386   C CD  . PRO A  52  ? 0.1610 0.2282 0.4757 -0.0250 0.0157  0.0584  52  PRO A CD  
387   N N   . LYS A  53  ? 0.4696 0.5028 0.7625 -0.0238 -0.0101 0.0360  53  LYS A N   
388   C CA  . LYS A  53  ? 0.4015 0.4260 0.6979 -0.0292 -0.0173 0.0288  53  LYS A CA  
389   C C   . LYS A  53  ? 0.3508 0.3634 0.6551 -0.0363 -0.0139 0.0310  53  LYS A C   
390   O O   . LYS A  53  ? 0.3477 0.3480 0.6439 -0.0339 -0.0082 0.0357  53  LYS A O   
391   C CB  . LYS A  53  ? 0.2909 0.3038 0.5694 -0.0238 -0.0221 0.0226  53  LYS A CB  
392   C CG  . LYS A  53  ? 0.2921 0.2935 0.5703 -0.0289 -0.0295 0.0143  53  LYS A CG  
393   C CD  . LYS A  53  ? 0.2719 0.2846 0.5634 -0.0347 -0.0378 0.0096  53  LYS A CD  
394   C CE  . LYS A  53  ? 0.2893 0.2899 0.5753 -0.0382 -0.0470 -0.0002 53  LYS A CE  
395   N NZ  . LYS A  53  ? 0.3055 0.3108 0.6114 -0.0482 -0.0528 -0.0037 53  LYS A NZ  
396   N N   . ARG A  54  ? 0.2467 0.2630 0.5675 -0.0451 -0.0176 0.0278  54  ARG A N   
397   C CA  . ARG A  54  ? 0.3295 0.3328 0.6588 -0.0531 -0.0147 0.0291  54  ARG A CA  
398   C C   . ARG A  54  ? 0.3178 0.3009 0.6339 -0.0521 -0.0198 0.0222  54  ARG A C   
399   O O   . ARG A  54  ? 0.3213 0.3043 0.6303 -0.0502 -0.0285 0.0137  54  ARG A O   
400   C CB  . ARG A  54  ? 0.6004 0.6147 0.9535 -0.0637 -0.0174 0.0266  54  ARG A CB  
401   C CG  . ARG A  54  ? 0.6874 0.7093 1.0562 -0.0691 -0.0068 0.0357  54  ARG A CG  
402   C CD  . ARG A  54  ? 0.7819 0.8242 1.1761 -0.0766 -0.0098 0.0328  54  ARG A CD  
403   N NE  . ARG A  54  ? 0.8910 0.9314 1.2930 -0.0825 -0.0220 0.0222  54  ARG A NE  
404   C CZ  . ARG A  54  ? 0.9461 1.0047 1.3642 -0.0850 -0.0307 0.0162  54  ARG A CZ  
405   N NH1 . ARG A  54  ? 0.9321 1.0120 1.3599 -0.0816 -0.0276 0.0197  54  ARG A NH1 
406   N NH2 . ARG A  54  ? 0.9645 1.0192 1.3869 -0.0902 -0.0428 0.0062  54  ARG A NH2 
407   N N   . PRO A  55  ? 0.2604 0.2251 0.5720 -0.0528 -0.0142 0.0259  55  PRO A N   
408   C CA  . PRO A  55  ? 0.2706 0.2145 0.5683 -0.0497 -0.0168 0.0204  55  PRO A CA  
409   C C   . PRO A  55  ? 0.2970 0.2328 0.5997 -0.0575 -0.0253 0.0099  55  PRO A C   
410   O O   . PRO A  55  ? 0.2822 0.2245 0.6028 -0.0672 -0.0275 0.0087  55  PRO A O   
411   C CB  . PRO A  55  ? 0.2747 0.2032 0.5713 -0.0497 -0.0082 0.0287  55  PRO A CB  
412   C CG  . PRO A  55  ? 0.2755 0.2122 0.5899 -0.0586 -0.0035 0.0349  55  PRO A CG  
413   C CD  . PRO A  55  ? 0.2553 0.2170 0.5757 -0.0571 -0.0047 0.0357  55  PRO A CD  
414   N N   . TRP A  56  ? 0.4594 0.3813 0.7464 -0.0531 -0.0297 0.0020  56  TRP A N   
415   C CA  . TRP A  56  ? 0.5147 0.4283 0.8009 -0.0587 -0.0391 -0.0096 56  TRP A CA  
416   C C   . TRP A  56  ? 0.6141 0.5012 0.8899 -0.0582 -0.0379 -0.0144 56  TRP A C   
417   O O   . TRP A  56  ? 0.6655 0.5426 0.9285 -0.0495 -0.0319 -0.0113 56  TRP A O   
418   C CB  . TRP A  56  ? 0.3443 0.2666 0.6175 -0.0529 -0.0467 -0.0164 56  TRP A CB  
419   C CG  . TRP A  56  ? 0.3187 0.2331 0.5709 -0.0418 -0.0424 -0.0162 56  TRP A CG  
420   C CD1 . TRP A  56  ? 0.3406 0.2364 0.5765 -0.0381 -0.0432 -0.0235 56  TRP A CD1 
421   C CD2 . TRP A  56  ? 0.2747 0.2003 0.5215 -0.0333 -0.0363 -0.0087 56  TRP A CD2 
422   N NE1 . TRP A  56  ? 0.3007 0.1968 0.5232 -0.0279 -0.0376 -0.0208 56  TRP A NE1 
423   C CE2 . TRP A  56  ? 0.2795 0.1937 0.5085 -0.0251 -0.0338 -0.0119 56  TRP A CE2 
424   C CE3 . TRP A  56  ? 0.2556 0.1997 0.5110 -0.0319 -0.0326 -0.0003 56  TRP A CE3 
425   C CZ2 . TRP A  56  ? 0.6201 0.5416 0.8415 -0.0164 -0.0282 -0.0068 56  TRP A CZ2 
426   C CZ3 . TRP A  56  ? 0.2424 0.1921 0.4882 -0.0231 -0.0275 0.0044  56  TRP A CZ3 
427   C CH2 . TRP A  56  ? 0.2469 0.1859 0.4768 -0.0158 -0.0256 0.0012  56  TRP A CH2 
428   N N   . SER A  57  ? 0.6015 0.4776 0.8836 -0.0674 -0.0439 -0.0226 57  SER A N   
429   C CA  . SER A  57  ? 0.6028 0.4523 0.8744 -0.0673 -0.0438 -0.0293 57  SER A CA  
430   C C   . SER A  57  ? 0.5339 0.3787 0.7879 -0.0636 -0.0523 -0.0416 57  SER A C   
431   O O   . SER A  57  ? 0.5163 0.3778 0.7682 -0.0628 -0.0591 -0.0445 57  SER A O   
432   C CB  . SER A  57  ? 0.8000 0.6383 1.0878 -0.0802 -0.0458 -0.0322 57  SER A CB  
433   O OG  . SER A  57  ? 0.8648 0.7171 1.1639 -0.0887 -0.0563 -0.0396 57  SER A OG  
434   N N   . GLY A  58  ? 0.4780 0.2991 0.7188 -0.0616 -0.0519 -0.0490 58  GLY A N   
435   C CA  . GLY A  58  ? 0.4828 0.2971 0.7020 -0.0559 -0.0572 -0.0598 58  GLY A CA  
436   C C   . GLY A  58  ? 0.4533 0.2759 0.6580 -0.0434 -0.0513 -0.0552 58  GLY A C   
437   O O   . GLY A  58  ? 0.3941 0.2285 0.6059 -0.0390 -0.0440 -0.0439 58  GLY A O   
438   N N   . VAL A  59  ? 0.4984 0.3146 0.6823 -0.0379 -0.0542 -0.0641 59  VAL A N   
439   C CA  . VAL A  59  ? 0.5181 0.3427 0.6884 -0.0272 -0.0489 -0.0609 59  VAL A CA  
440   C C   . VAL A  59  ? 0.5373 0.3801 0.7021 -0.0269 -0.0557 -0.0616 59  VAL A C   
441   O O   . VAL A  59  ? 0.5356 0.3738 0.6878 -0.0289 -0.0642 -0.0710 59  VAL A O   
442   C CB  . VAL A  59  ? 0.4042 0.2100 0.5541 -0.0197 -0.0446 -0.0687 59  VAL A CB  
443   C CG1 . VAL A  59  ? 0.4202 0.2360 0.5557 -0.0108 -0.0406 -0.0673 59  VAL A CG1 
444   C CG2 . VAL A  59  ? 0.4091 0.2015 0.5651 -0.0160 -0.0356 -0.0646 59  VAL A CG2 
445   N N   . LEU A  60  ? 0.6873 0.5496 0.8607 -0.0239 -0.0521 -0.0516 60  LEU A N   
446   C CA  . LEU A  60  ? 0.6931 0.5732 0.8638 -0.0230 -0.0576 -0.0504 60  LEU A CA  
447   C C   . LEU A  60  ? 0.7673 0.6427 0.9139 -0.0151 -0.0563 -0.0548 60  LEU A C   
448   O O   . LEU A  60  ? 0.8307 0.6978 0.9682 -0.0085 -0.0473 -0.0542 60  LEU A O   
449   C CB  . LEU A  60  ? 0.4688 0.3679 0.6544 -0.0213 -0.0521 -0.0386 60  LEU A CB  
450   C CG  . LEU A  60  ? 0.4251 0.3434 0.6115 -0.0199 -0.0564 -0.0356 60  LEU A CG  
451   C CD1 . LEU A  60  ? 0.4061 0.3410 0.6161 -0.0256 -0.0571 -0.0286 60  LEU A CD1 
452   C CD2 . LEU A  60  ? 0.4168 0.3398 0.5920 -0.0109 -0.0488 -0.0310 60  LEU A CD2 
453   N N   . ASP A  61  ? 0.6454 0.5260 0.7816 -0.0156 -0.0649 -0.0590 61  ASP A N   
454   C CA  . ASP A  61  ? 0.6366 0.5097 0.7470 -0.0088 -0.0633 -0.0634 61  ASP A CA  
455   C C   . ASP A  61  ? 0.5870 0.4747 0.6949 -0.0027 -0.0580 -0.0554 61  ASP A C   
456   O O   . ASP A  61  ? 0.6301 0.5308 0.7405 -0.0035 -0.0643 -0.0526 61  ASP A O   
457   C CB  . ASP A  61  ? 0.7293 0.5961 0.8243 -0.0117 -0.0757 -0.0729 61  ASP A CB  
458   C CG  . ASP A  61  ? 0.7870 0.6429 0.8520 -0.0049 -0.0732 -0.0776 61  ASP A CG  
459   O OD1 . ASP A  61  ? 0.7832 0.6488 0.8403 -0.0007 -0.0732 -0.0729 61  ASP A OD1 
460   O OD2 . ASP A  61  ? 0.8438 0.6806 0.8927 -0.0036 -0.0706 -0.0858 61  ASP A OD2 
461   N N   . ALA A  62  ? 0.3821 0.2668 0.4852 0.0035  -0.0466 -0.0524 62  ALA A N   
462   C CA  . ALA A  62  ? 0.3257 0.2228 0.4277 0.0088  -0.0404 -0.0452 62  ALA A CA  
463   C C   . ALA A  62  ? 0.3912 0.2815 0.4685 0.0140  -0.0377 -0.0488 62  ALA A C   
464   O O   . ALA A  62  ? 0.4184 0.3154 0.4934 0.0186  -0.0300 -0.0439 62  ALA A O   
465   C CB  . ALA A  62  ? 0.3676 0.2692 0.4825 0.0120  -0.0302 -0.0388 62  ALA A CB  
466   N N   . THR A  63  ? 0.4801 0.3557 0.5384 0.0131  -0.0430 -0.0578 63  THR A N   
467   C CA  . THR A  63  ? 0.5199 0.3857 0.5510 0.0180  -0.0394 -0.0617 63  THR A CA  
468   C C   . THR A  63  ? 0.5422 0.4158 0.5627 0.0196  -0.0438 -0.0577 63  THR A C   
469   O O   . THR A  63  ? 0.5370 0.4023 0.5343 0.0236  -0.0396 -0.0595 63  THR A O   
470   C CB  . THR A  63  ? 0.6971 0.5435 0.7073 0.0168  -0.0448 -0.0729 63  THR A CB  
471   O OG1 . THR A  63  ? 0.6973 0.5459 0.7118 0.0107  -0.0598 -0.0760 63  THR A OG1 
472   C CG2 . THR A  63  ? 0.7610 0.5946 0.7752 0.0172  -0.0379 -0.0780 63  THR A CG2 
473   N N   . THR A  64  ? 0.7795 0.6682 0.8160 0.0167  -0.0517 -0.0524 64  THR A N   
474   C CA  . THR A  64  ? 0.7815 0.6754 0.8067 0.0189  -0.0569 -0.0492 64  THR A CA  
475   C C   . THR A  64  ? 0.7487 0.6620 0.7951 0.0181  -0.0594 -0.0408 64  THR A C   
476   O O   . THR A  64  ? 0.7547 0.6781 0.8249 0.0141  -0.0615 -0.0387 64  THR A O   
477   C CB  . THR A  64  ? 0.7379 0.6232 0.7465 0.0171  -0.0706 -0.0563 64  THR A CB  
478   O OG1 . THR A  64  ? 0.8123 0.7007 0.8072 0.0207  -0.0752 -0.0525 64  THR A OG1 
479   C CG2 . THR A  64  ? 0.6612 0.5546 0.6921 0.0105  -0.0822 -0.0587 64  THR A CG2 
480   N N   . PHE A  65  ? 0.6109 0.5279 0.6474 0.0220  -0.0588 -0.0361 65  PHE A N   
481   C CA  . PHE A  65  ? 0.5297 0.4636 0.5832 0.0226  -0.0601 -0.0284 65  PHE A CA  
482   C C   . PHE A  65  ? 0.5329 0.4773 0.6024 0.0189  -0.0731 -0.0291 65  PHE A C   
483   O O   . PHE A  65  ? 0.5854 0.5236 0.6464 0.0170  -0.0839 -0.0352 65  PHE A O   
484   C CB  . PHE A  65  ? 0.3948 0.3270 0.4315 0.0276  -0.0581 -0.0241 65  PHE A CB  
485   C CG  . PHE A  65  ? 0.3872 0.3174 0.4198 0.0304  -0.0436 -0.0204 65  PHE A CG  
486   C CD1 . PHE A  65  ? 0.3564 0.2996 0.4095 0.0301  -0.0369 -0.0148 65  PHE A CD1 
487   C CD2 . PHE A  65  ? 0.4331 0.3485 0.4413 0.0330  -0.0364 -0.0230 65  PHE A CD2 
488   C CE1 . PHE A  65  ? 0.3679 0.3104 0.4190 0.0322  -0.0246 -0.0122 65  PHE A CE1 
489   C CE2 . PHE A  65  ? 0.4218 0.3369 0.4291 0.0349  -0.0227 -0.0200 65  PHE A CE2 
490   C CZ  . PHE A  65  ? 0.3930 0.3222 0.4226 0.0344  -0.0175 -0.0148 65  PHE A CZ  
491   N N   . GLN A  66  ? 0.4362 0.3969 0.5292 0.0178  -0.0718 -0.0231 66  GLN A N   
492   C CA  . GLN A  66  ? 0.3837 0.3574 0.4965 0.0142  -0.0822 -0.0231 66  GLN A CA  
493   C C   . GLN A  66  ? 0.4139 0.3977 0.5279 0.0182  -0.0881 -0.0189 66  GLN A C   
494   O O   . GLN A  66  ? 0.4718 0.4505 0.5692 0.0236  -0.0844 -0.0158 66  GLN A O   
495   C CB  . GLN A  66  ? 0.2505 0.2351 0.3895 0.0099  -0.0765 -0.0196 66  GLN A CB  
496   C CG  . GLN A  66  ? 0.2779 0.2554 0.4232 0.0040  -0.0781 -0.0249 66  GLN A CG  
497   C CD  . GLN A  66  ? 0.3333 0.3168 0.4913 -0.0016 -0.0910 -0.0294 66  GLN A CD  
498   O OE1 . GLN A  66  ? 0.3291 0.3203 0.4869 0.0001  -0.1004 -0.0297 66  GLN A OE1 
499   N NE2 . GLN A  66  ? 0.3698 0.3498 0.5400 -0.0082 -0.0915 -0.0328 66  GLN A NE2 
500   N N   . ASN A  67  ? 0.2957 0.2936 0.4303 0.0155  -0.0969 -0.0188 67  ASN A N   
501   C CA  . ASN A  67  ? 0.2863 0.2946 0.4247 0.0199  -0.1037 -0.0154 67  ASN A CA  
502   C C   . ASN A  67  ? 0.2706 0.2854 0.4133 0.0242  -0.0936 -0.0079 67  ASN A C   
503   O O   . ASN A  67  ? 0.2244 0.2432 0.3782 0.0222  -0.0829 -0.0049 67  ASN A O   
504   C CB  . ASN A  67  ? 0.4187 0.4437 0.5840 0.0158  -0.1134 -0.0168 67  ASN A CB  
505   C CG  . ASN A  67  ? 0.5340 0.5536 0.6987 0.0102  -0.1236 -0.0248 67  ASN A CG  
506   O OD1 . ASN A  67  ? 0.6073 0.6126 0.7476 0.0121  -0.1301 -0.0297 67  ASN A OD1 
507   N ND2 . ASN A  67  ? 0.5657 0.5955 0.7562 0.0029  -0.1246 -0.0265 67  ASN A ND2 
508   N N   . VAL A  68  ? 0.3077 0.3225 0.4407 0.0303  -0.0976 -0.0051 68  VAL A N   
509   C CA  . VAL A  68  ? 0.2888 0.3089 0.4252 0.0347  -0.0898 0.0013  68  VAL A CA  
510   C C   . VAL A  68  ? 0.2749 0.3145 0.4385 0.0348  -0.0934 0.0038  68  VAL A C   
511   O O   . VAL A  68  ? 0.3201 0.3676 0.4935 0.0346  -0.1051 0.0013  68  VAL A O   
512   C CB  . VAL A  68  ? 0.4406 0.4490 0.5525 0.0413  -0.0921 0.0033  68  VAL A CB  
513   C CG1 . VAL A  68  ? 0.4614 0.4751 0.5785 0.0458  -0.0857 0.0095  68  VAL A CG1 
514   C CG2 . VAL A  68  ? 0.4598 0.4495 0.5454 0.0410  -0.0855 0.0014  68  VAL A CG2 
515   N N   . CYS A  69  ? 0.2816 0.3294 0.4579 0.0351  -0.0832 0.0082  69  CYS A N   
516   C CA  . CYS A  69  ? 0.2631 0.3290 0.4645 0.0356  -0.0841 0.0106  69  CYS A CA  
517   C C   . CYS A  69  ? 0.2853 0.3547 0.4854 0.0424  -0.0928 0.0118  69  CYS A C   
518   O O   . CYS A  69  ? 0.3497 0.4068 0.5284 0.0478  -0.0931 0.0135  69  CYS A O   
519   C CB  . CYS A  69  ? 0.1706 0.2413 0.3795 0.0357  -0.0711 0.0149  69  CYS A CB  
520   S SG  . CYS A  69  ? 0.6360 0.7051 0.8507 0.0284  -0.0621 0.0144  69  CYS A SG  
521   N N   . TYR A  70  ? 0.1976 0.2837 0.4211 0.0423  -0.0998 0.0111  70  TYR A N   
522   C CA  . TYR A  70  ? 0.2012 0.2924 0.4267 0.0493  -0.1106 0.0116  70  TYR A CA  
523   C C   . TYR A  70  ? 0.1994 0.2867 0.4166 0.0571  -0.1047 0.0167  70  TYR A C   
524   O O   . TYR A  70  ? 0.3095 0.4038 0.5384 0.0572  -0.0942 0.0194  70  TYR A O   
525   C CB  . TYR A  70  ? 0.2293 0.3425 0.4871 0.0474  -0.1164 0.0101  70  TYR A CB  
526   C CG  . TYR A  70  ? 0.2101 0.3264 0.4692 0.0489  -0.1335 0.0060  70  TYR A CG  
527   C CD1 . TYR A  70  ? 0.3129 0.4312 0.5690 0.0582  -0.1428 0.0078  70  TYR A CD1 
528   C CD2 . TYR A  70  ? 0.3264 0.4421 0.5880 0.0415  -0.1410 0.0003  70  TYR A CD2 
529   C CE1 . TYR A  70  ? 0.3839 0.5050 0.6400 0.0603  -0.1600 0.0041  70  TYR A CE1 
530   C CE2 . TYR A  70  ? 0.3761 0.4944 0.6378 0.0427  -0.1580 -0.0042 70  TYR A CE2 
531   C CZ  . TYR A  70  ? 0.4520 0.5736 0.7108 0.0523  -0.1680 -0.0022 70  TYR A CZ  
532   O OH  . TYR A  70  ? 0.5494 0.6742 0.8079 0.0542  -0.1867 -0.0067 70  TYR A OH  
533   N N   . GLN A  71  ? 0.2167 0.2914 0.4125 0.0637  -0.1113 0.0179  71  GLN A N   
534   C CA  . GLN A  71  ? 0.2705 0.3374 0.4555 0.0706  -0.1048 0.0228  71  GLN A CA  
535   C C   . GLN A  71  ? 0.3162 0.3742 0.4859 0.0796  -0.1150 0.0251  71  GLN A C   
536   O O   . GLN A  71  ? 0.3590 0.4131 0.5190 0.0810  -0.1278 0.0229  71  GLN A O   
537   C CB  . GLN A  71  ? 0.2827 0.3340 0.4480 0.0676  -0.0919 0.0242  71  GLN A CB  
538   C CG  . GLN A  71  ? 0.2687 0.2999 0.4036 0.0678  -0.0941 0.0236  71  GLN A CG  
539   C CD  . GLN A  71  ? 0.2561 0.2796 0.3826 0.0613  -0.0833 0.0220  71  GLN A CD  
540   O OE1 . GLN A  71  ? 0.2862 0.2947 0.3921 0.0620  -0.0762 0.0236  71  GLN A OE1 
541   N NE2 . GLN A  71  ? 0.2152 0.2492 0.3587 0.0551  -0.0816 0.0191  71  GLN A NE2 
542   N N   . TYR A  72  ? 0.3749 0.4288 0.5418 0.0860  -0.1094 0.0295  72  TYR A N   
543   C CA  . TYR A  72  ? 0.4588 0.4997 0.6073 0.0950  -0.1168 0.0330  72  TYR A CA  
544   C C   . TYR A  72  ? 0.4769 0.4943 0.5907 0.0935  -0.1151 0.0338  72  TYR A C   
545   O O   . TYR A  72  ? 0.4527 0.4616 0.5571 0.0882  -0.1024 0.0340  72  TYR A O   
546   C CB  . TYR A  72  ? 0.6749 0.7148 0.8284 0.1013  -0.1092 0.0372  72  TYR A CB  
547   C CG  . TYR A  72  ? 0.7727 0.7952 0.9047 0.1108  -0.1145 0.0419  72  TYR A CG  
548   C CD1 . TYR A  72  ? 0.8072 0.8351 0.9447 0.1195  -0.1292 0.0430  72  TYR A CD1 
549   C CD2 . TYR A  72  ? 0.8172 0.8179 0.9241 0.1111  -0.1049 0.0456  72  TYR A CD2 
550   C CE1 . TYR A  72  ? 0.8517 0.8617 0.9678 0.1289  -0.1343 0.0482  72  TYR A CE1 
551   C CE2 . TYR A  72  ? 0.8528 0.8353 0.9387 0.1194  -0.1088 0.0507  72  TYR A CE2 
552   C CZ  . TYR A  72  ? 0.8685 0.8548 0.9579 0.1287  -0.1236 0.0523  72  TYR A CZ  
553   O OH  . TYR A  72  ? 0.8898 0.8559 0.9563 0.1377  -0.1276 0.0582  72  TYR A OH  
554   N N   . VAL A  73  ? 0.5587 0.5665 0.6541 0.0980  -0.1279 0.0340  73  VAL A N   
555   C CA  . VAL A  73  ? 0.5706 0.5544 0.6300 0.0979  -0.1261 0.0354  73  VAL A CA  
556   C C   . VAL A  73  ? 0.6179 0.5845 0.6571 0.1067  -0.1256 0.0422  73  VAL A C   
557   O O   . VAL A  73  ? 0.6123 0.5800 0.6515 0.1151  -0.1382 0.0445  73  VAL A O   
558   C CB  . VAL A  73  ? 0.4821 0.4621 0.5275 0.0972  -0.1401 0.0313  73  VAL A CB  
559   C CG1 . VAL A  73  ? 0.4666 0.4204 0.4723 0.0977  -0.1367 0.0330  73  VAL A CG1 
560   C CG2 . VAL A  73  ? 0.4681 0.4627 0.5330 0.0881  -0.1407 0.0244  73  VAL A CG2 
561   N N   . ASP A  74  ? 0.6238 0.5745 0.6465 0.1046  -0.1113 0.0454  74  ASP A N   
562   C CA  . ASP A  74  ? 0.6944 0.6292 0.7026 0.1116  -0.1076 0.0520  74  ASP A CA  
563   C C   . ASP A  74  ? 0.7681 0.6823 0.7440 0.1187  -0.1173 0.0562  74  ASP A C   
564   O O   . ASP A  74  ? 0.7784 0.6776 0.7277 0.1157  -0.1162 0.0557  74  ASP A O   
565   C CB  . ASP A  74  ? 0.7989 0.7230 0.8003 0.1062  -0.0894 0.0537  74  ASP A CB  
566   C CG  . ASP A  74  ? 0.8789 0.7825 0.8618 0.1121  -0.0848 0.0605  74  ASP A CG  
567   O OD1 . ASP A  74  ? 0.8719 0.7798 0.8684 0.1183  -0.0865 0.0629  74  ASP A OD1 
568   O OD2 . ASP A  74  ? 0.9425 0.8248 0.8969 0.1107  -0.0788 0.0635  74  ASP A OD2 
569   N N   . THR A  75  ? 1.0188 0.9323 0.9971 0.1287  -0.1270 0.0604  75  THR A N   
570   C CA  . THR A  75  ? 1.0731 0.9680 1.0222 0.1375  -0.1386 0.0653  75  THR A CA  
571   C C   . THR A  75  ? 1.0799 0.9484 1.0037 0.1430  -0.1307 0.0738  75  THR A C   
572   O O   . THR A  75  ? 1.1473 0.9995 1.0470 0.1517  -0.1408 0.0791  75  THR A O   
573   C CB  . THR A  75  ? 1.0347 0.9454 1.0006 0.1462  -0.1586 0.0644  75  THR A CB  
574   O OG1 . THR A  75  ? 0.9971 0.9372 1.0036 0.1422  -0.1591 0.0586  75  THR A OG1 
575   C CG2 . THR A  75  ? 1.0691 0.9745 1.0137 0.1473  -0.1741 0.0620  75  THR A CG2 
576   N N   . LEU A  76  ? 0.9394 0.8037 0.8690 0.1382  -0.1136 0.0751  76  LEU A N   
577   C CA  . LEU A  76  ? 0.9310 0.7705 0.8404 0.1428  -0.1054 0.0828  76  LEU A CA  
578   C C   . LEU A  76  ? 1.0096 0.8202 0.8764 0.1446  -0.1052 0.0886  76  LEU A C   
579   O O   . LEU A  76  ? 1.0866 0.8812 0.9342 0.1547  -0.1144 0.0951  76  LEU A O   
580   C CB  . LEU A  76  ? 0.6480 0.4865 0.5683 0.1352  -0.0865 0.0821  76  LEU A CB  
581   C CG  . LEU A  76  ? 0.5894 0.3995 0.4867 0.1380  -0.0768 0.0898  76  LEU A CG  
582   C CD1 . LEU A  76  ? 0.5762 0.3781 0.4725 0.1510  -0.0866 0.0958  76  LEU A CD1 
583   C CD2 . LEU A  76  ? 0.5228 0.3321 0.4311 0.1293  -0.0588 0.0881  76  LEU A CD2 
584   N N   . TYR A  77  ? 0.8975 0.7005 0.7489 0.1355  -0.0944 0.0864  77  TYR A N   
585   C CA  . TYR A  77  ? 0.9643 0.7396 0.7741 0.1365  -0.0921 0.0915  77  TYR A CA  
586   C C   . TYR A  77  ? 0.9718 0.7522 0.7705 0.1327  -0.0988 0.0855  77  TYR A C   
587   O O   . TYR A  77  ? 1.0124 0.7942 0.8100 0.1234  -0.0869 0.0811  77  TYR A O   
588   C CB  . TYR A  77  ? 1.0721 0.8306 0.8698 0.1288  -0.0707 0.0942  77  TYR A CB  
589   C CG  . TYR A  77  ? 1.0871 0.8331 0.8880 0.1311  -0.0616 0.1005  77  TYR A CG  
590   C CD1 . TYR A  77  ? 1.1202 0.8437 0.8989 0.1411  -0.0672 0.1093  77  TYR A CD1 
591   C CD2 . TYR A  77  ? 1.0806 0.8353 0.9046 0.1231  -0.0470 0.0974  77  TYR A CD2 
592   C CE1 . TYR A  77  ? 1.1508 0.8606 0.9318 0.1428  -0.0580 0.1147  77  TYR A CE1 
593   C CE2 . TYR A  77  ? 1.0956 0.8377 0.9220 0.1244  -0.0385 0.1021  77  TYR A CE2 
594   C CZ  . TYR A  77  ? 1.1232 0.8425 0.9285 0.1341  -0.0436 0.1107  77  TYR A CZ  
595   O OH  . TYR A  77  ? 1.1071 0.8121 0.9150 0.1351  -0.0346 0.1150  77  TYR A OH  
596   N N   . PRO A  78  ? 0.9627 0.7460 0.7538 0.1400  -0.1183 0.0848  78  PRO A N   
597   C CA  . PRO A  78  ? 0.9446 0.7340 0.7279 0.1360  -0.1260 0.0776  78  PRO A CA  
598   C C   . PRO A  78  ? 0.9650 0.7298 0.7085 0.1320  -0.1156 0.0788  78  PRO A C   
599   O O   . PRO A  78  ? 0.9878 0.7270 0.7007 0.1358  -0.1093 0.0869  78  PRO A O   
600   C CB  . PRO A  78  ? 0.8412 0.6345 0.6204 0.1460  -0.1497 0.0780  78  PRO A CB  
601   C CG  . PRO A  78  ? 0.8237 0.6246 0.6252 0.1539  -0.1539 0.0830  78  PRO A CG  
602   C CD  . PRO A  78  ? 0.8451 0.6274 0.6366 0.1523  -0.1348 0.0898  78  PRO A CD  
603   N N   . GLY A  79  ? 0.9200 0.6922 0.6645 0.1243  -0.1130 0.0707  79  GLY A N   
604   C CA  . GLY A  79  ? 0.9425 0.6941 0.6520 0.1203  -0.1026 0.0702  79  GLY A CA  
605   C C   . GLY A  79  ? 0.9444 0.6816 0.6458 0.1155  -0.0797 0.0753  79  GLY A C   
606   O O   . GLY A  79  ? 1.0010 0.7135 0.6661 0.1158  -0.0710 0.0796  79  GLY A O   
607   N N   . PHE A  80  ? 0.9784 0.7313 0.7138 0.1108  -0.0700 0.0745  80  PHE A N   
608   C CA  . PHE A  80  ? 0.9704 0.7128 0.7044 0.1057  -0.0494 0.0788  80  PHE A CA  
609   C C   . PHE A  80  ? 1.0177 0.7794 0.7808 0.0959  -0.0374 0.0715  80  PHE A C   
610   O O   . PHE A  80  ? 1.0477 0.8325 0.8453 0.0944  -0.0419 0.0675  80  PHE A O   
611   C CB  . PHE A  80  ? 0.7403 0.4800 0.4853 0.1106  -0.0498 0.0858  80  PHE A CB  
612   C CG  . PHE A  80  ? 0.7210 0.4562 0.4755 0.1041  -0.0303 0.0882  80  PHE A CG  
613   C CD1 . PHE A  80  ? 0.7653 0.4793 0.4944 0.0994  -0.0140 0.0917  80  PHE A CD1 
614   C CD2 . PHE A  80  ? 0.7227 0.4746 0.5113 0.1024  -0.0281 0.0867  80  PHE A CD2 
615   C CE1 . PHE A  80  ? 0.7732 0.4842 0.5133 0.0926  0.0036  0.0934  80  PHE A CE1 
616   C CE2 . PHE A  80  ? 0.7538 0.5016 0.5512 0.0960  -0.0113 0.0881  80  PHE A CE2 
617   C CZ  . PHE A  80  ? 0.7635 0.4914 0.5379 0.0908  0.0044  0.0913  80  PHE A CZ  
618   N N   . GLU A  81  ? 0.9234 0.6756 0.6724 0.0896  -0.0220 0.0700  81  GLU A N   
619   C CA  . GLU A  81  ? 0.9037 0.6731 0.6773 0.0812  -0.0115 0.0628  81  GLU A CA  
620   C C   . GLU A  81  ? 0.8728 0.6613 0.6842 0.0779  -0.0073 0.0621  81  GLU A C   
621   O O   . GLU A  81  ? 0.8305 0.6405 0.6695 0.0744  -0.0097 0.0559  81  GLU A O   
622   C CB  . GLU A  81  ? 0.9482 0.7030 0.7024 0.0757  0.0073  0.0628  81  GLU A CB  
623   C CG  . GLU A  81  ? 1.5848 1.3571 1.3642 0.0679  0.0182  0.0554  81  GLU A CG  
624   C CD  . GLU A  81  ? 1.5751 1.3416 1.3564 0.0616  0.0393  0.0573  81  GLU A CD  
625   O OE1 . GLU A  81  ? 1.5420 1.3172 1.3467 0.0587  0.0444  0.0591  81  GLU A OE1 
626   O OE2 . GLU A  81  ? 1.5886 1.3425 1.3489 0.0593  0.0509  0.0566  81  GLU A OE2 
627   N N   . GLY A  82  ? 0.9627 0.7421 0.7737 0.0790  -0.0014 0.0685  82  GLY A N   
628   C CA  . GLY A  82  ? 0.9237 0.7180 0.7664 0.0759  0.0034  0.0677  82  GLY A CA  
629   C C   . GLY A  82  ? 0.8740 0.6913 0.7453 0.0786  -0.0099 0.0639  82  GLY A C   
630   O O   . GLY A  82  ? 0.8684 0.7044 0.7674 0.0739  -0.0062 0.0594  82  GLY A O   
631   N N   . THR A  83  ? 0.6929 0.5088 0.5577 0.0865  -0.0252 0.0661  83  THR A N   
632   C CA  . THR A  83  ? 0.6689 0.5070 0.5611 0.0892  -0.0378 0.0626  83  THR A CA  
633   C C   . THR A  83  ? 0.6660 0.5184 0.5659 0.0864  -0.0453 0.0558  83  THR A C   
634   O O   . THR A  83  ? 0.6757 0.5494 0.6041 0.0842  -0.0486 0.0514  83  THR A O   
635   C CB  . THR A  83  ? 0.8538 0.6874 0.7406 0.0991  -0.0519 0.0673  83  THR A CB  
636   O OG1 . THR A  83  ? 0.9161 0.7257 0.7664 0.1036  -0.0549 0.0723  83  THR A OG1 
637   C CG2 . THR A  83  ? 0.8736 0.7066 0.7738 0.1020  -0.0475 0.0713  83  THR A CG2 
638   N N   . GLU A  84  ? 0.6323 0.4719 0.5059 0.0866  -0.0477 0.0548  84  GLU A N   
639   C CA  . GLU A  84  ? 0.6769 0.5270 0.5544 0.0853  -0.0581 0.0481  84  GLU A CA  
640   C C   . GLU A  84  ? 0.6581 0.5153 0.5442 0.0772  -0.0482 0.0418  84  GLU A C   
641   O O   . GLU A  84  ? 0.6168 0.4838 0.5107 0.0752  -0.0557 0.0357  84  GLU A O   
642   C CB  . GLU A  84  ? 1.0137 0.8478 0.8593 0.0908  -0.0699 0.0492  84  GLU A CB  
643   C CG  . GLU A  84  ? 1.1135 0.9438 0.9550 0.0999  -0.0825 0.0551  84  GLU A CG  
644   C CD  . GLU A  84  ? 1.2309 1.0500 1.0452 0.1060  -0.0984 0.0552  84  GLU A CD  
645   O OE1 . GLU A  84  ? 1.2835 1.0906 1.0729 0.1035  -0.0968 0.0520  84  GLU A OE1 
646   O OE2 . GLU A  84  ? 1.2553 1.0777 1.0733 0.1139  -0.1130 0.0582  84  GLU A OE2 
647   N N   . MET A  85  ? 0.8872 0.7399 0.7736 0.0728  -0.0318 0.0430  85  MET A N   
648   C CA  . MET A  85  ? 0.8725 0.7345 0.7723 0.0661  -0.0224 0.0374  85  MET A CA  
649   C C   . MET A  85  ? 0.8537 0.7392 0.7880 0.0642  -0.0277 0.0342  85  MET A C   
650   O O   . MET A  85  ? 0.8761 0.7715 0.8224 0.0604  -0.0280 0.0288  85  MET A O   
651   C CB  . MET A  85  ? 0.7331 0.5884 0.6309 0.0619  -0.0044 0.0395  85  MET A CB  
652   C CG  . MET A  85  ? 0.6817 0.5451 0.6005 0.0608  0.0009  0.0427  85  MET A CG  
653   S SD  . MET A  85  ? 0.9234 0.7735 0.8334 0.0563  0.0201  0.0462  85  MET A SD  
654   C CE  . MET A  85  ? 0.7025 0.5551 0.6116 0.0508  0.0309  0.0402  85  MET A CE  
655   N N   . TRP A  86  ? 0.6859 0.5787 0.6345 0.0672  -0.0319 0.0378  86  TRP A N   
656   C CA  . TRP A  86  ? 0.6132 0.5272 0.5935 0.0656  -0.0345 0.0358  86  TRP A CA  
657   C C   . TRP A  86  ? 0.5908 0.5167 0.5820 0.0673  -0.0492 0.0328  86  TRP A C   
658   O O   . TRP A  86  ? 0.5972 0.5403 0.6133 0.0645  -0.0506 0.0301  86  TRP A O   
659   C CB  . TRP A  86  ? 0.6336 0.5496 0.6241 0.0682  -0.0315 0.0403  86  TRP A CB  
660   C CG  . TRP A  86  ? 0.6872 0.5909 0.6679 0.0657  -0.0174 0.0431  86  TRP A CG  
661   C CD1 . TRP A  86  ? 0.7348 0.6205 0.6964 0.0688  -0.0141 0.0484  86  TRP A CD1 
662   C CD2 . TRP A  86  ? 0.6777 0.5862 0.6681 0.0593  -0.0051 0.0406  86  TRP A CD2 
663   N NE1 . TRP A  86  ? 0.7146 0.5939 0.6745 0.0639  0.0001  0.0491  86  TRP A NE1 
664   C CE2 . TRP A  86  ? 0.6969 0.5910 0.6751 0.0582  0.0054  0.0441  86  TRP A CE2 
665   C CE3 . TRP A  86  ? 0.6812 0.6045 0.6899 0.0546  -0.0022 0.0359  86  TRP A CE3 
666   C CZ2 . TRP A  86  ? 0.7208 0.6169 0.7065 0.0522  0.0181  0.0424  86  TRP A CZ2 
667   C CZ3 . TRP A  86  ? 0.7004 0.6252 0.7152 0.0497  0.0098  0.0346  86  TRP A CZ3 
668   C CH2 . TRP A  86  ? 0.7153 0.6275 0.7196 0.0483  0.0196  0.0375  86  TRP A CH2 
669   N N   . ASN A  87  ? 0.5598 0.4761 0.5321 0.0717  -0.0601 0.0333  87  ASN A N   
670   C CA  . ASN A  87  ? 0.5658 0.4939 0.5497 0.0738  -0.0758 0.0305  87  ASN A CA  
671   C C   . ASN A  87  ? 0.5169 0.4512 0.5066 0.0682  -0.0787 0.0236  87  ASN A C   
672   O O   . ASN A  87  ? 0.5168 0.4399 0.4899 0.0651  -0.0718 0.0210  87  ASN A O   
673   C CB  . ASN A  87  ? 0.7184 0.6344 0.6801 0.0811  -0.0883 0.0332  87  ASN A CB  
674   C CG  . ASN A  87  ? 0.7515 0.6673 0.7177 0.0880  -0.0904 0.0396  87  ASN A CG  
675   O OD1 . ASN A  87  ? 0.7606 0.6900 0.7517 0.0876  -0.0861 0.0405  87  ASN A OD1 
676   N ND2 . ASN A  87  ? 0.7610 0.6601 0.7015 0.0949  -0.0971 0.0439  87  ASN A ND2 
677   N N   . PRO A  88  ? 0.5635 0.5152 0.5770 0.0669  -0.0886 0.0204  88  PRO A N   
678   C CA  . PRO A  88  ? 0.5289 0.4874 0.5525 0.0609  -0.0913 0.0139  88  PRO A CA  
679   C C   . PRO A  88  ? 0.5582 0.5007 0.5547 0.0602  -0.0957 0.0094  88  PRO A C   
680   O O   . PRO A  88  ? 0.6373 0.5719 0.6162 0.0647  -0.1071 0.0094  88  PRO A O   
681   C CB  . PRO A  88  ? 0.4208 0.3968 0.4681 0.0615  -0.1047 0.0124  88  PRO A CB  
682   C CG  . PRO A  88  ? 0.4266 0.4108 0.4867 0.0664  -0.1031 0.0180  88  PRO A CG  
683   C CD  . PRO A  88  ? 0.4568 0.4229 0.4911 0.0711  -0.0966 0.0230  88  PRO A CD  
684   N N   . ASN A  89  ? 0.4492 0.3864 0.4415 0.0553  -0.0871 0.0055  89  ASN A N   
685   C CA  . ASN A  89  ? 0.5232 0.4447 0.4896 0.0546  -0.0901 0.0001  89  ASN A CA  
686   C C   . ASN A  89  ? 0.5492 0.4757 0.5253 0.0498  -0.0990 -0.0077 89  ASN A C   
687   O O   . ASN A  89  ? 0.6083 0.5211 0.5634 0.0488  -0.1007 -0.0134 89  ASN A O   
688   C CB  . ASN A  89  ? 0.6773 0.5847 0.6255 0.0536  -0.0741 0.0004  89  ASN A CB  
689   C CG  . ASN A  89  ? 0.6626 0.5796 0.6328 0.0487  -0.0629 -0.0010 89  ASN A CG  
690   O OD1 . ASN A  89  ? 0.5928 0.5248 0.5890 0.0457  -0.0668 -0.0024 89  ASN A OD1 
691   N ND2 . ASN A  89  ? 0.7097 0.6181 0.6698 0.0481  -0.0486 -0.0005 89  ASN A ND2 
692   N N   . ARG A  90  ? 0.5310 0.4760 0.5386 0.0465  -0.1033 -0.0083 90  ARG A N   
693   C CA  . ARG A  90  ? 0.4913 0.4416 0.5106 0.0416  -0.1133 -0.0154 90  ARG A CA  
694   C C   . ARG A  90  ? 0.5188 0.4864 0.5604 0.0425  -0.1262 -0.0141 90  ARG A C   
695   O O   . ARG A  90  ? 0.5129 0.4867 0.5591 0.0475  -0.1261 -0.0080 90  ARG A O   
696   C CB  . ARG A  90  ? 0.3988 0.3545 0.4373 0.0353  -0.1036 -0.0175 90  ARG A CB  
697   C CG  . ARG A  90  ? 0.3973 0.3374 0.4171 0.0346  -0.0917 -0.0200 90  ARG A CG  
698   C CD  . ARG A  90  ? 0.4773 0.4012 0.4721 0.0343  -0.0989 -0.0276 90  ARG A CD  
699   N NE  . ARG A  90  ? 0.5681 0.4780 0.5484 0.0334  -0.0870 -0.0311 90  ARG A NE  
700   C CZ  . ARG A  90  ? 0.6487 0.5463 0.6061 0.0371  -0.0763 -0.0290 90  ARG A CZ  
701   N NH1 . ARG A  90  ? 0.6520 0.5478 0.5972 0.0416  -0.0761 -0.0229 90  ARG A NH1 
702   N NH2 . ARG A  90  ? 0.6746 0.5612 0.6220 0.0364  -0.0653 -0.0329 90  ARG A NH2 
703   N N   . GLU A  91  ? 0.5760 0.5516 0.6329 0.0376  -0.1370 -0.0201 91  GLU A N   
704   C CA  . GLU A  91  ? 0.6105 0.6038 0.6897 0.0384  -0.1503 -0.0199 91  GLU A CA  
705   C C   . GLU A  91  ? 0.4993 0.5125 0.6122 0.0369  -0.1431 -0.0149 91  GLU A C   
706   O O   . GLU A  91  ? 0.4838 0.5000 0.6096 0.0318  -0.1317 -0.0144 91  GLU A O   
707   C CB  . GLU A  91  ? 0.9418 0.9376 1.0274 0.0330  -0.1647 -0.0286 91  GLU A CB  
708   C CG  . GLU A  91  ? 1.0983 1.0981 1.1794 0.0377  -0.1837 -0.0304 91  GLU A CG  
709   C CD  . GLU A  91  ? 1.2358 1.2399 1.3263 0.0313  -0.1987 -0.0398 91  GLU A CD  
710   O OE1 . GLU A  91  ? 1.2711 1.2662 1.3582 0.0244  -0.1944 -0.0457 91  GLU A OE1 
711   O OE2 . GLU A  91  ? 1.2828 1.2994 1.3852 0.0333  -0.2150 -0.0416 91  GLU A OE2 
712   N N   . LEU A  92  ? 0.3912 0.4172 0.5169 0.0419  -0.1497 -0.0112 92  LEU A N   
713   C CA  . LEU A  92  ? 0.3469 0.3919 0.5030 0.0416  -0.1433 -0.0067 92  LEU A CA  
714   C C   . LEU A  92  ? 0.3605 0.4220 0.5478 0.0336  -0.1464 -0.0107 92  LEU A C   
715   O O   . LEU A  92  ? 0.4097 0.4779 0.6058 0.0317  -0.1607 -0.0157 92  LEU A O   
716   C CB  . LEU A  92  ? 0.2744 0.3279 0.4356 0.0499  -0.1509 -0.0027 92  LEU A CB  
717   C CG  . LEU A  92  ? 0.2758 0.3193 0.4192 0.0578  -0.1433 0.0041  92  LEU A CG  
718   C CD1 . LEU A  92  ? 0.4446 0.5058 0.6137 0.0618  -0.1416 0.0082  92  LEU A CD1 
719   C CD2 . LEU A  92  ? 0.2686 0.2989 0.3968 0.0553  -0.1269 0.0062  92  LEU A CD2 
720   N N   . SER A  93  ? 0.3245 0.3926 0.5289 0.0288  -0.1336 -0.0083 93  SER A N   
721   C CA  . SER A  93  ? 0.3371 0.4217 0.5731 0.0214  -0.1346 -0.0104 93  SER A CA  
722   C C   . SER A  93  ? 0.3106 0.4081 0.5680 0.0204  -0.1215 -0.0048 93  SER A C   
723   O O   . SER A  93  ? 0.2918 0.3831 0.5383 0.0237  -0.1100 -0.0001 93  SER A O   
724   C CB  . SER A  93  ? 0.4992 0.5740 0.7321 0.0129  -0.1341 -0.0159 93  SER A CB  
725   O OG  . SER A  93  ? 0.5166 0.6058 0.7800 0.0053  -0.1313 -0.0162 93  SER A OG  
726   N N   . GLU A  94  ? 0.3685 0.4839 0.6564 0.0153  -0.1230 -0.0055 94  GLU A N   
727   C CA  . GLU A  94  ? 0.3358 0.4630 0.6433 0.0136  -0.1100 -0.0005 94  GLU A CA  
728   C C   . GLU A  94  ? 0.2908 0.4084 0.5951 0.0066  -0.0997 0.0000  94  GLU A C   
729   O O   . GLU A  94  ? 0.2765 0.3972 0.5867 0.0060  -0.0872 0.0049  94  GLU A O   
730   C CB  . GLU A  94  ? 0.3181 0.4684 0.6600 0.0109  -0.1139 -0.0010 94  GLU A CB  
731   C CG  . GLU A  94  ? 0.3150 0.4749 0.6636 0.0151  -0.1012 0.0046  94  GLU A CG  
732   C CD  . GLU A  94  ? 0.3509 0.5268 0.7159 0.0154  -0.1030 0.0035  94  GLU A CD  
733   O OE1 . GLU A  94  ? 0.3836 0.5646 0.7554 0.0139  -0.1158 -0.0012 94  GLU A OE1 
734   O OE2 . GLU A  94  ? 0.3521 0.5357 0.7229 0.0175  -0.0917 0.0071  94  GLU A OE2 
735   N N   . ASP A  95  ? 0.2611 0.3657 0.5539 0.0021  -0.1052 -0.0052 95  ASP A N   
736   C CA  . ASP A  95  ? 0.2325 0.3255 0.5204 -0.0036 -0.0965 -0.0052 95  ASP A CA  
737   C C   . ASP A  95  ? 0.2399 0.3146 0.4970 0.0019  -0.0929 -0.0049 95  ASP A C   
738   O O   . ASP A  95  ? 0.2240 0.2850 0.4628 0.0018  -0.0991 -0.0101 95  ASP A O   
739   C CB  . ASP A  95  ? 0.3089 0.3984 0.6033 -0.0113 -0.1061 -0.0123 95  ASP A CB  
740   C CG  . ASP A  95  ? 0.3652 0.4380 0.6502 -0.0165 -0.1002 -0.0141 95  ASP A CG  
741   O OD1 . ASP A  95  ? 0.4205 0.4827 0.6899 -0.0131 -0.0902 -0.0106 95  ASP A OD1 
742   O OD2 . ASP A  95  ? 0.3697 0.4401 0.6641 -0.0242 -0.1063 -0.0196 95  ASP A OD2 
743   N N   . CYS A  96  ? 0.2082 0.2833 0.4603 0.0064  -0.0822 0.0009  96  CYS A N   
744   C CA  . CYS A  96  ? 0.1841 0.2443 0.4110 0.0111  -0.0769 0.0017  96  CYS A CA  
745   C C   . CYS A  96  ? 0.1761 0.2297 0.3990 0.0100  -0.0647 0.0046  96  CYS A C   
746   O O   . CYS A  96  ? 0.1789 0.2214 0.3830 0.0136  -0.0602 0.0047  96  CYS A O   
747   C CB  . CYS A  96  ? 0.3394 0.4017 0.5569 0.0186  -0.0775 0.0046  96  CYS A CB  
748   S SG  . CYS A  96  ? 0.4644 0.5452 0.7033 0.0211  -0.0721 0.0103  96  CYS A SG  
749   N N   . LEU A  97  ? 0.1675 0.2275 0.4075 0.0055  -0.0591 0.0072  97  LEU A N   
750   C CA  . LEU A  97  ? 0.1594 0.2150 0.3950 0.0065  -0.0481 0.0113  97  LEU A CA  
751   C C   . LEU A  97  ? 0.1785 0.2193 0.4050 0.0039  -0.0470 0.0081  97  LEU A C   
752   O O   . LEU A  97  ? 0.1731 0.2120 0.4099 -0.0017 -0.0471 0.0073  97  LEU A O   
753   C CB  . LEU A  97  ? 0.1482 0.2153 0.4022 0.0039  -0.0414 0.0165  97  LEU A CB  
754   C CG  . LEU A  97  ? 0.1394 0.2222 0.4056 0.0063  -0.0413 0.0193  97  LEU A CG  
755   C CD1 . LEU A  97  ? 0.1315 0.2234 0.4130 0.0034  -0.0332 0.0243  97  LEU A CD1 
756   C CD2 . LEU A  97  ? 0.1349 0.2166 0.3879 0.0133  -0.0392 0.0207  97  LEU A CD2 
757   N N   . TYR A  98  ? 0.2745 0.3048 0.4819 0.0083  -0.0447 0.0066  98  TYR A N   
758   C CA  . TYR A  98  ? 0.2576 0.2727 0.4523 0.0081  -0.0431 0.0026  98  TYR A CA  
759   C C   . TYR A  98  ? 0.2148 0.2264 0.3973 0.0134  -0.0355 0.0048  98  TYR A C   
760   O O   . TYR A  98  ? 0.1974 0.2153 0.3771 0.0168  -0.0344 0.0074  98  TYR A O   
761   C CB  . TYR A  98  ? 0.2020 0.2077 0.3835 0.0076  -0.0518 -0.0043 98  TYR A CB  
762   C CG  . TYR A  98  ? 0.2304 0.2405 0.4249 0.0019  -0.0611 -0.0075 98  TYR A CG  
763   C CD1 . TYR A  98  ? 0.2391 0.2423 0.4405 -0.0039 -0.0619 -0.0107 98  TYR A CD1 
764   C CD2 . TYR A  98  ? 0.2403 0.2618 0.4419 0.0021  -0.0692 -0.0075 98  TYR A CD2 
765   C CE1 . TYR A  98  ? 0.2727 0.2805 0.4883 -0.0103 -0.0704 -0.0142 98  TYR A CE1 
766   C CE2 . TYR A  98  ? 0.2585 0.2865 0.4756 -0.0036 -0.0783 -0.0109 98  TYR A CE2 
767   C CZ  . TYR A  98  ? 0.2749 0.2962 0.4992 -0.0103 -0.0788 -0.0144 98  TYR A CZ  
768   O OH  . TYR A  98  ? 0.2889 0.3168 0.5302 -0.0170 -0.0877 -0.0184 98  TYR A OH  
769   N N   . LEU A  99  ? 0.1838 0.1857 0.3603 0.0142  -0.0301 0.0035  99  LEU A N   
770   C CA  . LEU A  99  ? 0.1803 0.1797 0.3473 0.0189  -0.0228 0.0046  99  LEU A CA  
771   C C   . LEU A  99  ? 0.1945 0.1798 0.3470 0.0206  -0.0205 -0.0007 99  LEU A C   
772   O O   . LEU A  99  ? 0.2074 0.1830 0.3571 0.0183  -0.0239 -0.0053 99  LEU A O   
773   C CB  . LEU A  99  ? 0.1671 0.1735 0.3449 0.0199  -0.0163 0.0100  99  LEU A CB  
774   C CG  . LEU A  99  ? 0.1678 0.1723 0.3565 0.0171  -0.0153 0.0118  99  LEU A CG  
775   C CD1 . LEU A  99  ? 0.1777 0.1700 0.3600 0.0189  -0.0125 0.0084  99  LEU A CD1 
776   C CD2 . LEU A  99  ? 0.1555 0.1693 0.3537 0.0181  -0.0108 0.0182  99  LEU A CD2 
777   N N   . ASN A  100 ? 0.2474 0.2313 0.3909 0.0245  -0.0143 -0.0003 100 ASN A N   
778   C CA  . ASN A  100 ? 0.2718 0.2438 0.4015 0.0269  -0.0098 -0.0051 100 ASN A CA  
779   C C   . ASN A  100 ? 0.2837 0.2576 0.4189 0.0299  -0.0008 -0.0035 100 ASN A C   
780   O O   . ASN A  100 ? 0.1858 0.1701 0.3289 0.0311  0.0025  0.0010  100 ASN A O   
781   C CB  . ASN A  100 ? 0.2988 0.2663 0.4109 0.0286  -0.0100 -0.0066 100 ASN A CB  
782   C CG  . ASN A  100 ? 0.3045 0.2732 0.4131 0.0268  -0.0199 -0.0068 100 ASN A CG  
783   O OD1 . ASN A  100 ? 0.3292 0.2929 0.4364 0.0242  -0.0272 -0.0108 100 ASN A OD1 
784   N ND2 . ASN A  100 ? 0.2802 0.2558 0.3883 0.0282  -0.0208 -0.0028 100 ASN A ND2 
785   N N   . VAL A  101 ? 0.2107 0.1748 0.3423 0.0314  0.0026  -0.0077 101 VAL A N   
786   C CA  . VAL A  101 ? 0.2066 0.1725 0.3445 0.0351  0.0105  -0.0071 101 VAL A CA  
787   C C   . VAL A  101 ? 0.2217 0.1775 0.3465 0.0380  0.0169  -0.0129 101 VAL A C   
788   O O   . VAL A  101 ? 0.2382 0.1812 0.3535 0.0378  0.0155  -0.0183 101 VAL A O   
789   C CB  . VAL A  101 ? 0.2067 0.1700 0.3560 0.0354  0.0097  -0.0062 101 VAL A CB  
790   C CG1 . VAL A  101 ? 0.2009 0.1689 0.3591 0.0403  0.0164  -0.0046 101 VAL A CG1 
791   C CG2 . VAL A  101 ? 0.1968 0.1671 0.3570 0.0317  0.0038  -0.0011 101 VAL A CG2 
792   N N   . TRP A  102 ? 0.2177 0.1786 0.3419 0.0405  0.0243  -0.0121 102 TRP A N   
793   C CA  . TRP A  102 ? 0.2319 0.1847 0.3464 0.0435  0.0328  -0.0173 102 TRP A CA  
794   C C   . TRP A  102 ? 0.2340 0.1934 0.3644 0.0474  0.0393  -0.0169 102 TRP A C   
795   O O   . TRP A  102 ? 0.2089 0.1816 0.3533 0.0478  0.0396  -0.0123 102 TRP A O   
796   C CB  . TRP A  102 ? 0.3191 0.2727 0.4222 0.0431  0.0382  -0.0169 102 TRP A CB  
797   C CG  . TRP A  102 ? 0.3286 0.2730 0.4118 0.0409  0.0332  -0.0179 102 TRP A CG  
798   C CD1 . TRP A  102 ? 0.3567 0.2864 0.4183 0.0416  0.0352  -0.0230 102 TRP A CD1 
799   C CD2 . TRP A  102 ? 0.3363 0.2854 0.4186 0.0384  0.0252  -0.0137 102 TRP A CD2 
800   N NE1 . TRP A  102 ? 0.3763 0.3014 0.4232 0.0397  0.0278  -0.0219 102 TRP A NE1 
801   C CE2 . TRP A  102 ? 0.3722 0.3095 0.4328 0.0379  0.0216  -0.0162 102 TRP A CE2 
802   C CE3 . TRP A  102 ? 0.3585 0.3205 0.4557 0.0369  0.0207  -0.0082 102 TRP A CE3 
803   C CZ2 . TRP A  102 ? 0.4225 0.3614 0.4779 0.0364  0.0131  -0.0132 102 TRP A CZ2 
804   C CZ3 . TRP A  102 ? 0.3846 0.3479 0.4769 0.0353  0.0135  -0.0056 102 TRP A CZ3 
805   C CH2 . TRP A  102 ? 0.4098 0.3622 0.4824 0.0353  0.0094  -0.0080 102 TRP A CH2 
806   N N   . THR A  103 ? 0.3901 0.3401 0.5181 0.0508  0.0439  -0.0221 103 THR A N   
807   C CA  . THR A  103 ? 0.4159 0.3720 0.5592 0.0558  0.0504  -0.0225 103 THR A CA  
808   C C   . THR A  103 ? 0.4601 0.4076 0.5942 0.0592  0.0605  -0.0293 103 THR A C   
809   O O   . THR A  103 ? 0.5253 0.4596 0.6394 0.0576  0.0612  -0.0337 103 THR A O   
810   C CB  . THR A  103 ? 0.2632 0.2164 0.4181 0.0582  0.0459  -0.0213 103 THR A CB  
811   O OG1 . THR A  103 ? 0.2544 0.1903 0.3984 0.0591  0.0461  -0.0275 103 THR A OG1 
812   C CG2 . THR A  103 ? 0.2745 0.2329 0.4350 0.0542  0.0366  -0.0151 103 THR A CG2 
813   N N   . PRO A  104 ? 0.2501 0.2055 0.3986 0.0641  0.0683  -0.0302 104 PRO A N   
814   C CA  . PRO A  104 ? 0.2678 0.2157 0.4101 0.0680  0.0793  -0.0370 104 PRO A CA  
815   C C   . PRO A  104 ? 0.2872 0.2172 0.4198 0.0707  0.0784  -0.0429 104 PRO A C   
816   O O   . PRO A  104 ? 0.2849 0.2103 0.4213 0.0701  0.0696  -0.0412 104 PRO A O   
817   C CB  . PRO A  104 ? 0.3858 0.3493 0.5522 0.0730  0.0853  -0.0360 104 PRO A CB  
818   C CG  . PRO A  104 ? 0.3755 0.3550 0.5532 0.0694  0.0797  -0.0291 104 PRO A CG  
819   C CD  . PRO A  104 ? 0.3423 0.3160 0.5123 0.0655  0.0680  -0.0252 104 PRO A CD  
820   N N   . TYR A  105 ? 0.4827 0.4017 0.6016 0.0732  0.0878  -0.0499 105 TYR A N   
821   C CA  . TYR A  105 ? 0.5247 0.4260 0.6349 0.0768  0.0888  -0.0570 105 TYR A CA  
822   C C   . TYR A  105 ? 0.5656 0.4686 0.6872 0.0846  0.1011  -0.0618 105 TYR A C   
823   O O   . TYR A  105 ? 0.6168 0.5240 0.7354 0.0859  0.1126  -0.0642 105 TYR A O   
824   C CB  . TYR A  105 ? 0.3516 0.2351 0.4319 0.0733  0.0882  -0.0627 105 TYR A CB  
825   C CG  . TYR A  105 ? 0.3744 0.2378 0.4433 0.0752  0.0860  -0.0704 105 TYR A CG  
826   C CD1 . TYR A  105 ? 0.3953 0.2483 0.4591 0.0814  0.0972  -0.0783 105 TYR A CD1 
827   C CD2 . TYR A  105 ? 0.4127 0.2669 0.4759 0.0705  0.0731  -0.0704 105 TYR A CD2 
828   C CE1 . TYR A  105 ? 0.4183 0.2512 0.4706 0.0830  0.0952  -0.0862 105 TYR A CE1 
829   C CE2 . TYR A  105 ? 0.3993 0.2339 0.4520 0.0713  0.0708  -0.0781 105 TYR A CE2 
830   C CZ  . TYR A  105 ? 0.4204 0.2436 0.4669 0.0777  0.0817  -0.0861 105 TYR A CZ  
831   O OH  . TYR A  105 ? 0.4446 0.2469 0.4802 0.0786  0.0795  -0.0945 105 TYR A OH  
832   N N   . PRO A  106 ? 0.4437 0.3435 0.5794 0.0901  0.0992  -0.0627 106 PRO A N   
833   C CA  . PRO A  106 ? 0.4801 0.3735 0.6202 0.0887  0.0871  -0.0595 106 PRO A CA  
834   C C   . PRO A  106 ? 0.5292 0.4407 0.6876 0.0867  0.0798  -0.0498 106 PRO A C   
835   O O   . PRO A  106 ? 0.5463 0.4754 0.7182 0.0884  0.0843  -0.0468 106 PRO A O   
836   C CB  . PRO A  106 ? 0.3990 0.2843 0.5501 0.0972  0.0913  -0.0635 106 PRO A CB  
837   C CG  . PRO A  106 ? 0.3974 0.2973 0.5631 0.1034  0.1025  -0.0645 106 PRO A CG  
838   C CD  . PRO A  106 ? 0.3903 0.2933 0.5405 0.0989  0.1100  -0.0669 106 PRO A CD  
839   N N   . ARG A  107 ? 0.4692 0.3760 0.6282 0.0831  0.0690  -0.0455 107 ARG A N   
840   C CA  . ARG A  107 ? 0.4319 0.3530 0.6044 0.0806  0.0614  -0.0364 107 ARG A CA  
841   C C   . ARG A  107 ? 0.4046 0.3405 0.5985 0.0878  0.0651  -0.0333 107 ARG A C   
842   O O   . ARG A  107 ? 0.4612 0.3916 0.6623 0.0951  0.0698  -0.0368 107 ARG A O   
843   C CB  . ARG A  107 ? 0.5632 0.4730 0.7355 0.0780  0.0523  -0.0336 107 ARG A CB  
844   C CG  . ARG A  107 ? 0.6148 0.5321 0.7869 0.0707  0.0437  -0.0267 107 ARG A CG  
845   C CD  . ARG A  107 ? 0.6292 0.5334 0.7868 0.0634  0.0375  -0.0296 107 ARG A CD  
846   N NE  . ARG A  107 ? 0.6438 0.5294 0.7994 0.0640  0.0357  -0.0334 107 ARG A NE  
847   C CZ  . ARG A  107 ? 0.6131 0.4946 0.7799 0.0649  0.0325  -0.0285 107 ARG A CZ  
848   N NH1 . ARG A  107 ? 0.5856 0.4807 0.7654 0.0660  0.0305  -0.0196 107 ARG A NH1 
849   N NH2 . ARG A  107 ? 0.6207 0.4830 0.7843 0.0648  0.0314  -0.0327 107 ARG A NH2 
850   N N   . PRO A  108 ? 0.3682 0.3229 0.5724 0.0860  0.0631  -0.0275 108 PRO A N   
851   C CA  . PRO A  108 ? 0.3534 0.3250 0.5783 0.0921  0.0660  -0.0254 108 PRO A CA  
852   C C   . PRO A  108 ? 0.3809 0.3517 0.6159 0.0983  0.0612  -0.0221 108 PRO A C   
853   O O   . PRO A  108 ? 0.3467 0.3088 0.5803 0.0977  0.0539  -0.0175 108 PRO A O   
854   C CB  . PRO A  108 ? 0.3260 0.3138 0.5550 0.0868  0.0610  -0.0193 108 PRO A CB  
855   C CG  . PRO A  108 ? 0.2213 0.2001 0.4351 0.0796  0.0542  -0.0166 108 PRO A CG  
856   C CD  . PRO A  108 ? 0.3517 0.3128 0.5486 0.0782  0.0577  -0.0232 108 PRO A CD  
857   N N   . ALA A  109 ? 0.5016 0.4812 0.7446 0.1035  0.0650  -0.0242 109 ALA A N   
858   C CA  . ALA A  109 ? 0.5341 0.5141 0.7846 0.1099  0.0599  -0.0210 109 ALA A CA  
859   C C   . ALA A  109 ? 0.5746 0.5670 0.8314 0.1087  0.0502  -0.0125 109 ALA A C   
860   O O   . ALA A  109 ? 0.5569 0.5405 0.8114 0.1098  0.0435  -0.0072 109 ALA A O   
861   C CB  . ALA A  109 ? 0.3543 0.3430 0.6134 0.1160  0.0660  -0.0255 109 ALA A CB  
862   N N   . SER A  110 ? 0.6566 0.6682 0.9203 0.1062  0.0499  -0.0115 110 SER A N   
863   C CA  . SER A  110 ? 0.6301 0.6540 0.8978 0.1046  0.0411  -0.0048 110 SER A CA  
864   C C   . SER A  110 ? 0.5470 0.5706 0.8076 0.0970  0.0385  -0.0015 110 SER A C   
865   O O   . SER A  110 ? 0.5662 0.5862 0.8217 0.0926  0.0438  -0.0050 110 SER A O   
866   C CB  . SER A  110 ? 0.6042 0.6485 0.8833 0.1058  0.0413  -0.0061 110 SER A CB  
867   O OG  . SER A  110 ? 0.6276 0.6769 0.9091 0.1031  0.0508  -0.0123 110 SER A OG  
868   N N   . PRO A  111 ? 0.3260 0.3533 0.5858 0.0959  0.0303  0.0052  111 PRO A N   
869   C CA  . PRO A  111 ? 0.2974 0.3238 0.5507 0.0893  0.0277  0.0087  111 PRO A CA  
870   C C   . PRO A  111 ? 0.2733 0.3133 0.5279 0.0841  0.0299  0.0066  111 PRO A C   
871   O O   . PRO A  111 ? 0.2683 0.3208 0.5256 0.0830  0.0253  0.0091  111 PRO A O   
872   C CB  . PRO A  111 ? 0.3858 0.4134 0.6381 0.0908  0.0194  0.0163  111 PRO A CB  
873   C CG  . PRO A  111 ? 0.4181 0.4384 0.6731 0.0982  0.0182  0.0170  111 PRO A CG  
874   C CD  . PRO A  111 ? 0.4261 0.4537 0.6887 0.1017  0.0235  0.0102  111 PRO A CD  
875   N N   . THR A  112 ? 0.3331 0.3696 0.5851 0.0813  0.0370  0.0016  112 THR A N   
876   C CA  . THR A  112 ? 0.3762 0.4224 0.6280 0.0761  0.0401  -0.0001 112 THR A CA  
877   C C   . THR A  112 ? 0.2914 0.3406 0.5385 0.0711  0.0344  0.0048  112 THR A C   
878   O O   . THR A  112 ? 0.2568 0.2969 0.4988 0.0704  0.0310  0.0081  112 THR A O   
879   C CB  . THR A  112 ? 0.5741 0.6119 0.8209 0.0748  0.0493  -0.0055 112 THR A CB  
880   O OG1 . THR A  112 ? 0.6012 0.6238 0.8346 0.0725  0.0465  -0.0046 112 THR A OG1 
881   C CG2 . THR A  112 ? 0.5954 0.6304 0.8456 0.0796  0.0566  -0.0110 112 THR A CG2 
882   N N   . PRO A  113 ? 0.1835 0.2452 0.4329 0.0676  0.0337  0.0048  113 PRO A N   
883   C CA  . PRO A  113 ? 0.1560 0.2208 0.4005 0.0630  0.0294  0.0084  113 PRO A CA  
884   C C   . PRO A  113 ? 0.1622 0.2186 0.3985 0.0593  0.0326  0.0078  113 PRO A C   
885   O O   . PRO A  113 ? 0.1420 0.1918 0.3727 0.0584  0.0388  0.0036  113 PRO A O   
886   C CB  . PRO A  113 ? 0.1310 0.2092 0.3804 0.0605  0.0295  0.0066  113 PRO A CB  
887   C CG  . PRO A  113 ? 0.1363 0.2170 0.3924 0.0616  0.0367  0.0015  113 PRO A CG  
888   C CD  . PRO A  113 ? 0.1457 0.2192 0.4034 0.0675  0.0371  0.0012  113 PRO A CD  
889   N N   . VAL A  114 ? 0.1302 0.1854 0.3593 0.0559  0.0276  0.0117  114 VAL A N   
890   C CA  . VAL A  114 ? 0.2635 0.3089 0.4794 0.0516  0.0274  0.0117  114 VAL A CA  
891   C C   . VAL A  114 ? 0.2594 0.3096 0.4707 0.0473  0.0276  0.0120  114 VAL A C   
892   O O   . VAL A  114 ? 0.2703 0.3301 0.4872 0.0470  0.0254  0.0139  114 VAL A O   
893   C CB  . VAL A  114 ? 0.1341 0.1737 0.3470 0.0511  0.0218  0.0160  114 VAL A CB  
894   C CG1 . VAL A  114 ? 0.1791 0.2086 0.3812 0.0474  0.0212  0.0147  114 VAL A CG1 
895   C CG2 . VAL A  114 ? 0.2112 0.2458 0.4296 0.0558  0.0211  0.0168  114 VAL A CG2 
896   N N   . LEU A  115 ? 0.2695 0.3119 0.4697 0.0445  0.0300  0.0100  115 LEU A N   
897   C CA  . LEU A  115 ? 0.2270 0.2711 0.4213 0.0410  0.0301  0.0107  115 LEU A CA  
898   C C   . LEU A  115 ? 0.2557 0.2930 0.4406 0.0391  0.0256  0.0125  115 LEU A C   
899   O O   . LEU A  115 ? 0.3153 0.3427 0.4912 0.0388  0.0258  0.0105  115 LEU A O   
900   C CB  . LEU A  115 ? 0.1700 0.2100 0.3583 0.0397  0.0371  0.0072  115 LEU A CB  
901   C CG  . LEU A  115 ? 0.1482 0.1970 0.3473 0.0399  0.0429  0.0050  115 LEU A CG  
902   C CD1 . LEU A  115 ? 0.1470 0.1889 0.3381 0.0383  0.0513  0.0020  115 LEU A CD1 
903   C CD2 . LEU A  115 ? 0.1229 0.1810 0.3281 0.0378  0.0404  0.0067  115 LEU A CD2 
904   N N   . ILE A  116 ? 0.1716 0.2143 0.3587 0.0379  0.0214  0.0159  116 ILE A N   
905   C CA  . ILE A  116 ? 0.1234 0.1620 0.3044 0.0361  0.0172  0.0174  116 ILE A CA  
906   C C   . ILE A  116 ? 0.1626 0.2007 0.3368 0.0348  0.0179  0.0173  116 ILE A C   
907   O O   . ILE A  116 ? 0.1289 0.1733 0.3065 0.0345  0.0191  0.0182  116 ILE A O   
908   C CB  . ILE A  116 ? 0.1173 0.1614 0.3049 0.0359  0.0132  0.0214  116 ILE A CB  
909   C CG1 . ILE A  116 ? 0.1203 0.1619 0.3130 0.0372  0.0125  0.0224  116 ILE A CG1 
910   C CG2 . ILE A  116 ? 0.2874 0.3295 0.4720 0.0338  0.0094  0.0225  116 ILE A CG2 
911   C CD1 . ILE A  116 ? 0.1165 0.1627 0.3145 0.0370  0.0100  0.0271  116 ILE A CD1 
912   N N   . TRP A  117 ? 0.1322 0.1618 0.2961 0.0341  0.0167  0.0160  117 TRP A N   
913   C CA  . TRP A  117 ? 0.1357 0.1622 0.2912 0.0337  0.0169  0.0164  117 TRP A CA  
914   C C   . TRP A  117 ? 0.1340 0.1622 0.2896 0.0336  0.0106  0.0186  117 TRP A C   
915   O O   . TRP A  117 ? 0.1383 0.1636 0.2925 0.0332  0.0059  0.0181  117 TRP A O   
916   C CB  . TRP A  117 ? 0.1498 0.1649 0.2913 0.0338  0.0200  0.0139  117 TRP A CB  
917   C CG  . TRP A  117 ? 0.1575 0.1663 0.2874 0.0340  0.0187  0.0152  117 TRP A CG  
918   C CD1 . TRP A  117 ? 0.1651 0.1687 0.2867 0.0348  0.0121  0.0157  117 TRP A CD1 
919   C CD2 . TRP A  117 ? 0.1738 0.1805 0.2996 0.0336  0.0235  0.0162  117 TRP A CD2 
920   N NE1 . TRP A  117 ? 0.1854 0.1834 0.2971 0.0358  0.0123  0.0175  117 TRP A NE1 
921   C CE2 . TRP A  117 ? 0.2048 0.2036 0.3185 0.0348  0.0198  0.0180  117 TRP A CE2 
922   C CE3 . TRP A  117 ? 0.1713 0.1819 0.3033 0.0321  0.0303  0.0157  117 TRP A CE3 
923   C CZ2 . TRP A  117 ? 0.2351 0.2280 0.3415 0.0349  0.0232  0.0198  117 TRP A CZ2 
924   C CZ3 . TRP A  117 ? 0.1916 0.1970 0.3174 0.0311  0.0340  0.0169  117 TRP A CZ3 
925   C CH2 . TRP A  117 ? 0.2329 0.2286 0.3454 0.0327  0.0307  0.0192  117 TRP A CH2 
926   N N   . ILE A  118 ? 0.1284 0.1616 0.2868 0.0340  0.0106  0.0205  118 ILE A N   
927   C CA  . ILE A  118 ? 0.1277 0.1632 0.2872 0.0347  0.0056  0.0223  118 ILE A CA  
928   C C   . ILE A  118 ? 0.1649 0.1925 0.3130 0.0361  0.0056  0.0223  118 ILE A C   
929   O O   . ILE A  118 ? 0.1632 0.1890 0.3087 0.0361  0.0102  0.0224  118 ILE A O   
930   C CB  . ILE A  118 ? 0.1173 0.1629 0.2870 0.0350  0.0060  0.0243  118 ILE A CB  
931   C CG1 . ILE A  118 ? 0.1109 0.1623 0.2890 0.0340  0.0069  0.0251  118 ILE A CG1 
932   C CG2 . ILE A  118 ? 0.1166 0.1662 0.2904 0.0360  0.0015  0.0259  118 ILE A CG2 
933   C CD1 . ILE A  118 ? 0.1038 0.1640 0.2889 0.0344  0.0075  0.0273  118 ILE A CD1 
934   N N   . TYR A  119 ? 0.1532 0.1757 0.2945 0.0372  0.0000  0.0223  119 TYR A N   
935   C CA  . TYR A  119 ? 0.1611 0.1743 0.2893 0.0395  -0.0010 0.0232  119 TYR A CA  
936   C C   . TYR A  119 ? 0.1891 0.2059 0.3215 0.0420  -0.0022 0.0255  119 TYR A C   
937   O O   . TYR A  119 ? 0.1441 0.1717 0.2897 0.0422  -0.0036 0.0262  119 TYR A O   
938   C CB  . TYR A  119 ? 0.1718 0.1774 0.2890 0.0406  -0.0078 0.0222  119 TYR A CB  
939   C CG  . TYR A  119 ? 0.2131 0.2269 0.3408 0.0408  -0.0166 0.0220  119 TYR A CG  
940   C CD1 . TYR A  119 ? 0.1680 0.1866 0.3006 0.0438  -0.0219 0.0240  119 TYR A CD1 
941   C CD2 . TYR A  119 ? 0.2344 0.2506 0.3676 0.0381  -0.0193 0.0196  119 TYR A CD2 
942   C CE1 . TYR A  119 ? 0.1649 0.1928 0.3098 0.0435  -0.0294 0.0235  119 TYR A CE1 
943   C CE2 . TYR A  119 ? 0.2225 0.2463 0.3669 0.0372  -0.0267 0.0192  119 TYR A CE2 
944   C CZ  . TYR A  119 ? 0.2169 0.2475 0.3679 0.0397  -0.0317 0.0211  119 TYR A CZ  
945   O OH  . TYR A  119 ? 0.1607 0.2006 0.3256 0.0382  -0.0387 0.0203  119 TYR A OH  
946   N N   . GLY A  120 ? 0.1666 0.1731 0.2867 0.0440  -0.0008 0.0268  120 GLY A N   
947   C CA  . GLY A  120 ? 0.2038 0.2102 0.3253 0.0474  -0.0025 0.0289  120 GLY A CA  
948   C C   . GLY A  120 ? 0.2115 0.2145 0.3275 0.0517  -0.0111 0.0305  120 GLY A C   
949   O O   . GLY A  120 ? 0.1810 0.1868 0.2979 0.0514  -0.0176 0.0293  120 GLY A O   
950   N N   . GLY A  121 ? 0.3715 0.3674 0.4813 0.0558  -0.0118 0.0329  121 GLY A N   
951   C CA  . GLY A  121 ? 0.3903 0.3856 0.4985 0.0612  -0.0211 0.0346  121 GLY A CA  
952   C C   . GLY A  121 ? 0.3594 0.3659 0.4839 0.0652  -0.0240 0.0353  121 GLY A C   
953   O O   . GLY A  121 ? 0.3653 0.3773 0.4954 0.0691  -0.0326 0.0358  121 GLY A O   
954   N N   . GLY A  122 ? 0.2447 0.2558 0.3777 0.0641  -0.0169 0.0347  122 GLY A N   
955   C CA  . GLY A  122 ? 0.2067 0.2248 0.3515 0.0687  -0.0173 0.0352  122 GLY A CA  
956   C C   . GLY A  122 ? 0.1636 0.1999 0.3283 0.0691  -0.0207 0.0341  122 GLY A C   
957   O O   . GLY A  122 ? 0.1632 0.2059 0.3381 0.0740  -0.0219 0.0345  122 GLY A O   
958   N N   . PHE A  123 ? 0.1611 0.2050 0.3314 0.0640  -0.0213 0.0328  123 PHE A N   
959   C CA  . PHE A  123 ? 0.1845 0.2444 0.3729 0.0629  -0.0243 0.0321  123 PHE A CA  
960   C C   . PHE A  123 ? 0.2522 0.3168 0.4470 0.0672  -0.0342 0.0325  123 PHE A C   
961   O O   . PHE A  123 ? 0.2596 0.3388 0.4726 0.0668  -0.0368 0.0319  123 PHE A O   
962   C CB  . PHE A  123 ? 0.1353 0.2055 0.3367 0.0637  -0.0179 0.0319  123 PHE A CB  
963   C CG  . PHE A  123 ? 0.1295 0.1964 0.3254 0.0603  -0.0094 0.0311  123 PHE A CG  
964   C CD1 . PHE A  123 ? 0.1357 0.2056 0.3326 0.0547  -0.0070 0.0307  123 PHE A CD1 
965   C CD2 . PHE A  123 ? 0.1408 0.2019 0.3315 0.0628  -0.0044 0.0306  123 PHE A CD2 
966   C CE1 . PHE A  123 ? 0.1174 0.1854 0.3100 0.0520  -0.0005 0.0299  123 PHE A CE1 
967   C CE2 . PHE A  123 ? 0.1420 0.2012 0.3287 0.0593  0.0021  0.0292  123 PHE A CE2 
968   C CZ  . PHE A  123 ? 0.1203 0.1837 0.3081 0.0541  0.0037  0.0289  123 PHE A CZ  
969   N N   . TYR A  124 ? 0.4126 0.4651 0.5929 0.0712  -0.0399 0.0336  124 TYR A N   
970   C CA  . TYR A  124 ? 0.4582 0.5150 0.6430 0.0752  -0.0515 0.0337  124 TYR A CA  
971   C C   . TYR A  124 ? 0.4267 0.4756 0.5980 0.0720  -0.0581 0.0324  124 TYR A C   
972   O O   . TYR A  124 ? 0.4337 0.4857 0.6070 0.0742  -0.0691 0.0316  124 TYR A O   
973   C CB  . TYR A  124 ? 0.5048 0.5559 0.6855 0.0842  -0.0557 0.0362  124 TYR A CB  
974   C CG  . TYR A  124 ? 0.4662 0.4956 0.6211 0.0864  -0.0539 0.0387  124 TYR A CG  
975   C CD1 . TYR A  124 ? 0.4592 0.4793 0.6066 0.0849  -0.0432 0.0394  124 TYR A CD1 
976   C CD2 . TYR A  124 ? 0.4660 0.4837 0.6036 0.0895  -0.0628 0.0401  124 TYR A CD2 
977   C CE1 . TYR A  124 ? 0.5295 0.5298 0.6547 0.0858  -0.0403 0.0417  124 TYR A CE1 
978   C CE2 . TYR A  124 ? 0.5331 0.5297 0.6457 0.0910  -0.0597 0.0430  124 TYR A CE2 
979   C CZ  . TYR A  124 ? 0.5813 0.5693 0.6886 0.0888  -0.0478 0.0439  124 TYR A CZ  
980   O OH  . TYR A  124 ? 0.6283 0.5951 0.7123 0.0893  -0.0431 0.0469  124 TYR A OH  
981   N N   . SER A  125 ? 0.2158 0.2548 0.3735 0.0670  -0.0516 0.0317  125 SER A N   
982   C CA  . SER A  125 ? 0.2117 0.2382 0.3503 0.0657  -0.0562 0.0306  125 SER A CA  
983   C C   . SER A  125 ? 0.2085 0.2286 0.3387 0.0596  -0.0488 0.0288  125 SER A C   
984   O O   . SER A  125 ? 0.2138 0.2385 0.3518 0.0564  -0.0400 0.0287  125 SER A O   
985   C CB  . SER A  125 ? 0.2649 0.2744 0.3817 0.0712  -0.0572 0.0336  125 SER A CB  
986   O OG  . SER A  125 ? 0.2188 0.2172 0.3237 0.0687  -0.0460 0.0347  125 SER A OG  
987   N N   . GLY A  126 ? 0.2111 0.2199 0.3238 0.0587  -0.0525 0.0272  126 GLY A N   
988   C CA  . GLY A  126 ? 0.2856 0.2860 0.3874 0.0542  -0.0452 0.0252  126 GLY A CA  
989   C C   . GLY A  126 ? 0.2470 0.2531 0.3571 0.0492  -0.0476 0.0213  126 GLY A C   
990   O O   . GLY A  126 ? 0.2008 0.2185 0.3271 0.0482  -0.0546 0.0200  126 GLY A O   
991   N N   . ALA A  127 ? 0.2092 0.2072 0.3096 0.0461  -0.0411 0.0192  127 ALA A N   
992   C CA  . ALA A  127 ? 0.2076 0.2070 0.3127 0.0418  -0.0423 0.0152  127 ALA A CA  
993   C C   . ALA A  127 ? 0.2108 0.2007 0.3050 0.0400  -0.0331 0.0135  127 ALA A C   
994   O O   . ALA A  127 ? 0.2210 0.2002 0.2986 0.0417  -0.0277 0.0144  127 ALA A O   
995   C CB  . ALA A  127 ? 0.2238 0.2190 0.3212 0.0421  -0.0540 0.0118  127 ALA A CB  
996   N N   . ALA A  128 ? 0.2544 0.2472 0.3576 0.0365  -0.0314 0.0108  128 ALA A N   
997   C CA  . ALA A  128 ? 0.2062 0.1922 0.3031 0.0353  -0.0227 0.0088  128 ALA A CA  
998   C C   . ALA A  128 ? 0.2438 0.2146 0.3189 0.0360  -0.0240 0.0048  128 ALA A C   
999   O O   . ALA A  128 ? 0.2803 0.2437 0.3467 0.0360  -0.0158 0.0030  128 ALA A O   
1000  C CB  . ALA A  128 ? 0.2158 0.2086 0.3290 0.0324  -0.0210 0.0077  128 ALA A CB  
1001  N N   . SER A  129 ? 0.2419 0.2087 0.3081 0.0369  -0.0343 0.0032  129 SER A N   
1002  C CA  . SER A  129 ? 0.2662 0.2177 0.3091 0.0376  -0.0371 -0.0012 129 SER A CA  
1003  C C   . SER A  129 ? 0.2819 0.2208 0.3013 0.0409  -0.0309 0.0010  129 SER A C   
1004  O O   . SER A  129 ? 0.4549 0.3800 0.4538 0.0414  -0.0275 -0.0023 129 SER A O   
1005  C CB  . SER A  129 ? 0.6041 0.5556 0.6444 0.0376  -0.0517 -0.0039 129 SER A CB  
1006  O OG  . SER A  129 ? 0.6634 0.6294 0.7289 0.0344  -0.0575 -0.0042 129 SER A OG  
1007  N N   . LEU A  130 ? 0.3393 0.2820 0.3615 0.0429  -0.0285 0.0065  130 LEU A N   
1008  C CA  . LEU A  130 ? 0.3374 0.2672 0.3380 0.0457  -0.0229 0.0097  130 LEU A CA  
1009  C C   . LEU A  130 ? 0.3767 0.2966 0.3651 0.0444  -0.0097 0.0080  130 LEU A C   
1010  O O   . LEU A  130 ? 0.3610 0.2881 0.3642 0.0419  -0.0019 0.0063  130 LEU A O   
1011  C CB  . LEU A  130 ? 0.2787 0.2151 0.2896 0.0471  -0.0201 0.0155  130 LEU A CB  
1012  C CG  . LEU A  130 ? 0.2747 0.2190 0.2946 0.0499  -0.0320 0.0178  130 LEU A CG  
1013  C CD1 . LEU A  130 ? 0.2628 0.2127 0.2931 0.0515  -0.0279 0.0226  130 LEU A CD1 
1014  C CD2 . LEU A  130 ? 0.4563 0.3876 0.4526 0.0537  -0.0410 0.0180  130 LEU A CD2 
1015  N N   . ASP A  131 ? 0.5428 0.4462 0.5038 0.0465  -0.0070 0.0086  131 ASP A N   
1016  C CA  . ASP A  131 ? 0.6047 0.4973 0.5513 0.0455  0.0059  0.0064  131 ASP A CA  
1017  C C   . ASP A  131 ? 0.5352 0.4342 0.4961 0.0432  0.0199  0.0087  131 ASP A C   
1018  O O   . ASP A  131 ? 0.5076 0.4077 0.4730 0.0416  0.0295  0.0053  131 ASP A O   
1019  C CB  . ASP A  131 ? 0.6963 0.5687 0.6083 0.0483  0.0062  0.0077  131 ASP A CB  
1020  C CG  . ASP A  131 ? 0.7364 0.6021 0.6327 0.0507  -0.0089 0.0044  131 ASP A CG  
1021  O OD1 . ASP A  131 ? 0.7573 0.6345 0.6713 0.0496  -0.0195 0.0012  131 ASP A OD1 
1022  O OD2 . ASP A  131 ? 0.7452 0.5937 0.6108 0.0535  -0.0102 0.0052  131 ASP A OD2 
1023  N N   . VAL A  132 ? 0.5629 0.4667 0.5322 0.0432  0.0208  0.0139  132 VAL A N   
1024  C CA  . VAL A  132 ? 0.5577 0.4680 0.5411 0.0405  0.0328  0.0154  132 VAL A CA  
1025  C C   . VAL A  132 ? 0.5674 0.4949 0.5783 0.0384  0.0339  0.0124  132 VAL A C   
1026  O O   . VAL A  132 ? 0.6019 0.5347 0.6236 0.0362  0.0439  0.0118  132 VAL A O   
1027  C CB  . VAL A  132 ? 0.4447 0.3552 0.4310 0.0408  0.0328  0.0210  132 VAL A CB  
1028  C CG1 . VAL A  132 ? 0.4733 0.3647 0.4316 0.0431  0.0343  0.0248  132 VAL A CG1 
1029  C CG2 . VAL A  132 ? 0.4233 0.3450 0.4242 0.0427  0.0205  0.0222  132 VAL A CG2 
1030  N N   . TYR A  133 ? 0.4016 0.3378 0.4240 0.0389  0.0236  0.0108  133 TYR A N   
1031  C CA  . TYR A  133 ? 0.3209 0.2716 0.3673 0.0372  0.0244  0.0091  133 TYR A CA  
1032  C C   . TYR A  133 ? 0.2883 0.2367 0.3344 0.0371  0.0267  0.0040  133 TYR A C   
1033  O O   . TYR A  133 ? 0.2615 0.2197 0.3254 0.0364  0.0261  0.0026  133 TYR A O   
1034  C CB  . TYR A  133 ? 0.2247 0.1868 0.2865 0.0374  0.0141  0.0107  133 TYR A CB  
1035  C CG  . TYR A  133 ? 0.2232 0.1875 0.2858 0.0386  0.0103  0.0150  133 TYR A CG  
1036  C CD1 . TYR A  133 ? 0.2212 0.1838 0.2825 0.0383  0.0175  0.0177  133 TYR A CD1 
1037  C CD2 . TYR A  133 ? 0.2497 0.2182 0.3161 0.0400  -0.0005 0.0160  133 TYR A CD2 
1038  C CE1 . TYR A  133 ? 0.3503 0.3133 0.4121 0.0399  0.0139  0.0214  133 TYR A CE1 
1039  C CE2 . TYR A  133 ? 0.2170 0.1878 0.2853 0.0421  -0.0040 0.0197  133 TYR A CE2 
1040  C CZ  . TYR A  133 ? 0.3633 0.3306 0.4286 0.0424  0.0032  0.0224  133 TYR A CZ  
1041  O OH  . TYR A  133 ? 0.2174 0.1854 0.2842 0.0450  -0.0001 0.0257  133 TYR A OH  
1042  N N   . ASP A  134 ? 0.2675 0.2018 0.2924 0.0381  0.0293  0.0011  134 ASP A N   
1043  C CA  . ASP A  134 ? 0.2791 0.2089 0.3016 0.0385  0.0317  -0.0045 134 ASP A CA  
1044  C C   . ASP A  134 ? 0.2625 0.2011 0.3028 0.0381  0.0417  -0.0057 134 ASP A C   
1045  O O   . ASP A  134 ? 0.2643 0.2033 0.3044 0.0377  0.0520  -0.0048 134 ASP A O   
1046  C CB  . ASP A  134 ? 0.5737 0.4857 0.5675 0.0398  0.0355  -0.0073 134 ASP A CB  
1047  C CG  . ASP A  134 ? 0.6765 0.5815 0.6650 0.0407  0.0377  -0.0141 134 ASP A CG  
1048  O OD1 . ASP A  134 ? 0.6961 0.6026 0.6907 0.0403  0.0283  -0.0171 134 ASP A OD1 
1049  O OD2 . ASP A  134 ? 0.7361 0.6337 0.7144 0.0416  0.0493  -0.0167 134 ASP A OD2 
1050  N N   . GLY A  135 ? 0.3016 0.2472 0.3577 0.0383  0.0384  -0.0079 135 GLY A N   
1051  C CA  . GLY A  135 ? 0.3056 0.2616 0.3815 0.0389  0.0452  -0.0083 135 GLY A CA  
1052  C C   . GLY A  135 ? 0.3098 0.2593 0.3811 0.0409  0.0551  -0.0133 135 GLY A C   
1053  O O   . GLY A  135 ? 0.2674 0.2256 0.3551 0.0422  0.0613  -0.0141 135 GLY A O   
1054  N N   . ARG A  136 ? 0.3202 0.2545 0.3686 0.0416  0.0563  -0.0168 136 ARG A N   
1055  C CA  . ARG A  136 ? 0.3368 0.2624 0.3775 0.0440  0.0655  -0.0227 136 ARG A CA  
1056  C C   . ARG A  136 ? 0.3371 0.2693 0.3875 0.0448  0.0797  -0.0228 136 ARG A C   
1057  O O   . ARG A  136 ? 0.2884 0.2234 0.3496 0.0475  0.0859  -0.0267 136 ARG A O   
1058  C CB  . ARG A  136 ? 0.3819 0.2889 0.3919 0.0444  0.0647  -0.0260 136 ARG A CB  
1059  C CG  . ARG A  136 ? 0.3736 0.2713 0.3669 0.0456  0.0788  -0.0282 136 ARG A CG  
1060  C CD  . ARG A  136 ? 0.4319 0.3124 0.3921 0.0453  0.0761  -0.0280 136 ARG A CD  
1061  N NE  . ARG A  136 ? 0.4511 0.3174 0.3920 0.0468  0.0691  -0.0342 136 ARG A NE  
1062  C CZ  . ARG A  136 ? 0.4406 0.3049 0.3778 0.0458  0.0536  -0.0346 136 ARG A CZ  
1063  N NH1 . ARG A  136 ? 0.4238 0.2996 0.3753 0.0438  0.0440  -0.0288 136 ARG A NH1 
1064  N NH2 . ARG A  136 ? 0.4627 0.3136 0.3825 0.0466  0.0478  -0.0413 136 ARG A NH2 
1065  N N   . PHE A  137 ? 0.4373 0.3727 0.4860 0.0424  0.0844  -0.0187 137 PHE A N   
1066  C CA  . PHE A  137 ? 0.4419 0.3834 0.4996 0.0419  0.0986  -0.0190 137 PHE A CA  
1067  C C   . PHE A  137 ? 0.3863 0.3472 0.4752 0.0420  0.0991  -0.0181 137 PHE A C   
1068  O O   . PHE A  137 ? 0.3654 0.3330 0.4673 0.0434  0.1091  -0.0210 137 PHE A O   
1069  C CB  . PHE A  137 ? 0.4180 0.3542 0.4624 0.0386  0.1041  -0.0149 137 PHE A CB  
1070  C CG  . PHE A  137 ? 0.4438 0.3606 0.4556 0.0390  0.1021  -0.0146 137 PHE A CG  
1071  C CD1 . PHE A  137 ? 0.4486 0.3515 0.4395 0.0404  0.1127  -0.0183 137 PHE A CD1 
1072  C CD2 . PHE A  137 ? 0.4671 0.3797 0.4689 0.0384  0.0893  -0.0109 137 PHE A CD2 
1073  C CE1 . PHE A  137 ? 0.5078 0.3920 0.4662 0.0411  0.1098  -0.0180 137 PHE A CE1 
1074  C CE2 . PHE A  137 ? 0.5052 0.4005 0.4771 0.0394  0.0858  -0.0106 137 PHE A CE2 
1075  C CZ  . PHE A  137 ? 0.5395 0.4200 0.4884 0.0408  0.0956  -0.0141 137 PHE A CZ  
1076  N N   . LEU A  138 ? 0.3302 0.3004 0.4309 0.0407  0.0885  -0.0141 138 LEU A N   
1077  C CA  . LEU A  138 ? 0.3049 0.2926 0.4327 0.0413  0.0871  -0.0132 138 LEU A CA  
1078  C C   . LEU A  138 ? 0.2935 0.2827 0.4310 0.0458  0.0859  -0.0168 138 LEU A C   
1079  O O   . LEU A  138 ? 0.3267 0.3267 0.4832 0.0482  0.0908  -0.0185 138 LEU A O   
1080  C CB  . LEU A  138 ? 0.2057 0.2008 0.3403 0.0393  0.0762  -0.0085 138 LEU A CB  
1081  C CG  . LEU A  138 ? 0.2037 0.2005 0.3359 0.0354  0.0788  -0.0054 138 LEU A CG  
1082  C CD1 . LEU A  138 ? 0.1925 0.1918 0.3248 0.0342  0.0681  -0.0014 138 LEU A CD1 
1083  C CD2 . LEU A  138 ? 0.1949 0.2053 0.3471 0.0339  0.0857  -0.0062 138 LEU A CD2 
1084  N N   . ALA A  139 ? 0.2304 0.2081 0.3550 0.0470  0.0793  -0.0181 139 ALA A N   
1085  C CA  . ALA A  139 ? 0.2543 0.2293 0.3851 0.0512  0.0782  -0.0216 139 ALA A CA  
1086  C C   . ALA A  139 ? 0.2836 0.2564 0.4153 0.0545  0.0910  -0.0268 139 ALA A C   
1087  O O   . ALA A  139 ? 0.2895 0.2718 0.4408 0.0583  0.0941  -0.0282 139 ALA A O   
1088  C CB  . ALA A  139 ? 0.3938 0.3541 0.5074 0.0507  0.0703  -0.0233 139 ALA A CB  
1089  N N   . GLN A  140 ? 0.3652 0.3255 0.4757 0.0535  0.0985  -0.0297 140 GLN A N   
1090  C CA  . GLN A  140 ? 0.3625 0.3186 0.4712 0.0569  0.1117  -0.0353 140 GLN A CA  
1091  C C   . GLN A  140 ? 0.3580 0.3307 0.4886 0.0570  0.1219  -0.0347 140 GLN A C   
1092  O O   . GLN A  140 ? 0.3889 0.3699 0.5383 0.0615  0.1267  -0.0378 140 GLN A O   
1093  C CB  . GLN A  140 ? 0.3943 0.3320 0.4719 0.0557  0.1177  -0.0382 140 GLN A CB  
1094  C CG  . GLN A  140 ? 0.4823 0.4105 0.5522 0.0601  0.1294  -0.0454 140 GLN A CG  
1095  C CD  . GLN A  140 ? 0.5699 0.5093 0.6553 0.0611  0.1454  -0.0466 140 GLN A CD  
1096  O OE1 . GLN A  140 ? 0.5942 0.5389 0.6796 0.0569  0.1513  -0.0429 140 GLN A OE1 
1097  N NE2 . GLN A  140 ? 0.5762 0.5196 0.6765 0.0668  0.1524  -0.0518 140 GLN A NE2 
1098  N N   . VAL A  141 ? 0.2855 0.2631 0.4150 0.0520  0.1247  -0.0308 141 VAL A N   
1099  C CA  . VAL A  141 ? 0.2928 0.2848 0.4415 0.0504  0.1356  -0.0309 141 VAL A CA  
1100  C C   . VAL A  141 ? 0.2616 0.2743 0.4416 0.0515  0.1295  -0.0293 141 VAL A C   
1101  O O   . VAL A  141 ? 0.2365 0.2622 0.4384 0.0542  0.1366  -0.0322 141 VAL A O   
1102  C CB  . VAL A  141 ? 0.4324 0.4216 0.5702 0.0440  0.1396  -0.0269 141 VAL A CB  
1103  C CG1 . VAL A  141 ? 0.4159 0.4192 0.5743 0.0413  0.1520  -0.0277 141 VAL A CG1 
1104  C CG2 . VAL A  141 ? 0.4908 0.4586 0.5949 0.0432  0.1443  -0.0274 141 VAL A CG2 
1105  N N   . GLU A  142 ? 0.2240 0.2403 0.4060 0.0496  0.1165  -0.0248 142 GLU A N   
1106  C CA  . GLU A  142 ? 0.2061 0.2406 0.4138 0.0506  0.1097  -0.0229 142 GLU A CA  
1107  C C   . GLU A  142 ? 0.1986 0.2337 0.4133 0.0562  0.1005  -0.0228 142 GLU A C   
1108  O O   . GLU A  142 ? 0.1897 0.2373 0.4215 0.0576  0.0928  -0.0204 142 GLU A O   
1109  C CB  . GLU A  142 ? 0.3195 0.3589 0.5270 0.0452  0.1025  -0.0182 142 GLU A CB  
1110  C CG  . GLU A  142 ? 0.4042 0.4488 0.6161 0.0399  0.1117  -0.0183 142 GLU A CG  
1111  C CD  . GLU A  142 ? 0.4952 0.5558 0.7325 0.0412  0.1200  -0.0221 142 GLU A CD  
1112  O OE1 . GLU A  142 ? 0.5458 0.6183 0.8002 0.0451  0.1124  -0.0226 142 GLU A OE1 
1113  O OE2 . GLU A  142 ? 0.5039 0.5641 0.7415 0.0380  0.1329  -0.0240 142 GLU A OE2 
1114  N N   . GLY A  143 ? 0.3288 0.3488 0.5285 0.0591  0.1011  -0.0254 143 GLY A N   
1115  C CA  . GLY A  143 ? 0.3555 0.3726 0.5607 0.0645  0.0944  -0.0259 143 GLY A CA  
1116  C C   . GLY A  143 ? 0.3603 0.3807 0.5686 0.0632  0.0812  -0.0204 143 GLY A C   
1117  O O   . GLY A  143 ? 0.3653 0.3900 0.5863 0.0675  0.0756  -0.0190 143 GLY A O   
1118  N N   . ALA A  144 ? 0.3157 0.3337 0.5123 0.0577  0.0766  -0.0171 144 ALA A N   
1119  C CA  . ALA A  144 ? 0.2758 0.2992 0.4768 0.0561  0.0657  -0.0118 144 ALA A CA  
1120  C C   . ALA A  144 ? 0.2688 0.2793 0.4567 0.0555  0.0586  -0.0108 144 ALA A C   
1121  O O   . ALA A  144 ? 0.2904 0.2874 0.4643 0.0557  0.0611  -0.0146 144 ALA A O   
1122  C CB  . ALA A  144 ? 0.1869 0.2163 0.3855 0.0510  0.0648  -0.0090 144 ALA A CB  
1123  N N   . VAL A  145 ? 0.2011 0.2159 0.3937 0.0544  0.0498  -0.0061 145 VAL A N   
1124  C CA  . VAL A  145 ? 0.1766 0.1817 0.3601 0.0525  0.0427  -0.0045 145 VAL A CA  
1125  C C   . VAL A  145 ? 0.1677 0.1769 0.3465 0.0480  0.0380  -0.0008 145 VAL A C   
1126  O O   . VAL A  145 ? 0.3773 0.3977 0.5654 0.0475  0.0357  0.0029  145 VAL A O   
1127  C CB  . VAL A  145 ? 0.2177 0.2236 0.4115 0.0552  0.0375  -0.0014 145 VAL A CB  
1128  C CG1 . VAL A  145 ? 0.1727 0.1731 0.3608 0.0514  0.0301  0.0017  145 VAL A CG1 
1129  C CG2 . VAL A  145 ? 0.2395 0.2364 0.4350 0.0600  0.0411  -0.0055 145 VAL A CG2 
1130  N N   . LEU A  146 ? 0.2791 0.2791 0.4430 0.0451  0.0363  -0.0021 146 LEU A N   
1131  C CA  . LEU A  146 ? 0.2891 0.2922 0.4477 0.0417  0.0328  0.0008  146 LEU A CA  
1132  C C   . LEU A  146 ? 0.3073 0.3061 0.4617 0.0394  0.0246  0.0023  146 LEU A C   
1133  O O   . LEU A  146 ? 0.3252 0.3133 0.4708 0.0389  0.0226  -0.0009 146 LEU A O   
1134  C CB  . LEU A  146 ? 0.1821 0.1788 0.3264 0.0406  0.0380  -0.0016 146 LEU A CB  
1135  C CG  . LEU A  146 ? 0.1738 0.1744 0.3146 0.0381  0.0361  0.0017  146 LEU A CG  
1136  C CD1 . LEU A  146 ? 0.1764 0.1784 0.3158 0.0377  0.0447  0.0009  146 LEU A CD1 
1137  C CD2 . LEU A  146 ? 0.3375 0.3283 0.4626 0.0368  0.0306  0.0016  146 LEU A CD2 
1138  N N   . VAL A  147 ? 0.2000 0.2074 0.3611 0.0377  0.0202  0.0068  147 VAL A N   
1139  C CA  . VAL A  147 ? 0.2074 0.2133 0.3678 0.0352  0.0131  0.0084  147 VAL A CA  
1140  C C   . VAL A  147 ? 0.2247 0.2339 0.3802 0.0337  0.0104  0.0101  147 VAL A C   
1141  O O   . VAL A  147 ? 0.2349 0.2505 0.3923 0.0342  0.0133  0.0119  147 VAL A O   
1142  C CB  . VAL A  147 ? 0.1496 0.1620 0.3228 0.0348  0.0105  0.0125  147 VAL A CB  
1143  C CG1 . VAL A  147 ? 0.1543 0.1623 0.3280 0.0317  0.0047  0.0127  147 VAL A CG1 
1144  C CG2 . VAL A  147 ? 0.1506 0.1624 0.3304 0.0379  0.0138  0.0124  147 VAL A CG2 
1145  N N   . SER A  148 ? 0.2429 0.2474 0.3925 0.0319  0.0045  0.0091  148 SER A N   
1146  C CA  . SER A  148 ? 0.2259 0.2342 0.3731 0.0313  0.0005  0.0111  148 SER A CA  
1147  C C   . SER A  148 ? 0.2499 0.2607 0.4030 0.0290  -0.0072 0.0117  148 SER A C   
1148  O O   . SER A  148 ? 0.3186 0.3222 0.4676 0.0275  -0.0114 0.0083  148 SER A O   
1149  C CB  . SER A  148 ? 0.1715 0.1712 0.3020 0.0324  0.0013  0.0091  148 SER A CB  
1150  O OG  . SER A  148 ? 0.1873 0.1757 0.3061 0.0322  -0.0010 0.0048  148 SER A OG  
1151  N N   . MET A  149 ? 0.1489 0.1699 0.3119 0.0285  -0.0089 0.0154  149 MET A N   
1152  C CA  . MET A  149 ? 0.1483 0.1739 0.3204 0.0259  -0.0152 0.0160  149 MET A CA  
1153  C C   . MET A  149 ? 0.1497 0.1789 0.3198 0.0271  -0.0202 0.0164  149 MET A C   
1154  O O   . MET A  149 ? 0.1479 0.1775 0.3120 0.0299  -0.0177 0.0178  149 MET A O   
1155  C CB  . MET A  149 ? 0.1373 0.1723 0.3243 0.0245  -0.0128 0.0200  149 MET A CB  
1156  C CG  . MET A  149 ? 0.1272 0.1726 0.3198 0.0260  -0.0110 0.0236  149 MET A CG  
1157  S SD  . MET A  149 ? 0.1243 0.1683 0.3072 0.0296  -0.0059 0.0236  149 MET A SD  
1158  C CE  . MET A  149 ? 0.1194 0.1643 0.3061 0.0298  -0.0004 0.0249  149 MET A CE  
1159  N N   . ASN A  150 ? 0.1544 0.1856 0.3298 0.0250  -0.0275 0.0149  150 ASN A N   
1160  C CA  . ASN A  150 ? 0.1901 0.2282 0.3693 0.0265  -0.0333 0.0159  150 ASN A CA  
1161  C C   . ASN A  150 ? 0.1410 0.1928 0.3376 0.0259  -0.0307 0.0197  150 ASN A C   
1162  O O   . ASN A  150 ? 0.1357 0.1915 0.3431 0.0227  -0.0279 0.0210  150 ASN A O   
1163  C CB  . ASN A  150 ? 0.1655 0.2019 0.3454 0.0243  -0.0431 0.0121  150 ASN A CB  
1164  C CG  . ASN A  150 ? 0.2078 0.2313 0.3667 0.0267  -0.0472 0.0087  150 ASN A CG  
1165  O OD1 . ASN A  150 ? 0.2153 0.2307 0.3598 0.0294  -0.0413 0.0094  150 ASN A OD1 
1166  N ND2 . ASN A  150 ? 0.2088 0.2302 0.3655 0.0254  -0.0572 0.0050  150 ASN A ND2 
1167  N N   . TYR A  151 ? 0.1374 0.1952 0.3358 0.0294  -0.0311 0.0217  151 TYR A N   
1168  C CA  . TYR A  151 ? 0.1874 0.2584 0.4024 0.0291  -0.0289 0.0245  151 TYR A CA  
1169  C C   . TYR A  151 ? 0.1694 0.2473 0.3907 0.0319  -0.0356 0.0242  151 TYR A C   
1170  O O   . TYR A  151 ? 0.1409 0.2122 0.3502 0.0357  -0.0398 0.0232  151 TYR A O   
1171  C CB  . TYR A  151 ? 0.1189 0.1920 0.3324 0.0312  -0.0206 0.0273  151 TYR A CB  
1172  C CG  . TYR A  151 ? 0.1216 0.1887 0.3225 0.0355  -0.0194 0.0272  151 TYR A CG  
1173  C CD1 . TYR A  151 ? 0.1273 0.1830 0.3134 0.0357  -0.0177 0.0257  151 TYR A CD1 
1174  C CD2 . TYR A  151 ? 0.1198 0.1920 0.3240 0.0392  -0.0190 0.0285  151 TYR A CD2 
1175  C CE1 . TYR A  151 ? 0.1314 0.1807 0.3063 0.0387  -0.0155 0.0259  151 TYR A CE1 
1176  C CE2 . TYR A  151 ? 0.1384 0.2030 0.3307 0.0428  -0.0175 0.0285  151 TYR A CE2 
1177  C CZ  . TYR A  151 ? 0.1486 0.2015 0.3262 0.0421  -0.0157 0.0274  151 TYR A CZ  
1178  O OH  . TYR A  151 ? 0.1674 0.2116 0.3331 0.0446  -0.0131 0.0278  151 TYR A OH  
1179  N N   . ARG A  152 ? 0.1254 0.2163 0.3656 0.0301  -0.0364 0.0251  152 ARG A N   
1180  C CA  . ARG A  152 ? 0.1390 0.2390 0.3889 0.0336  -0.0425 0.0248  152 ARG A CA  
1181  C C   . ARG A  152 ? 0.1265 0.2251 0.3691 0.0403  -0.0398 0.0266  152 ARG A C   
1182  O O   . ARG A  152 ? 0.1192 0.2197 0.3622 0.0414  -0.0314 0.0287  152 ARG A O   
1183  C CB  . ARG A  152 ? 0.1212 0.2372 0.3955 0.0303  -0.0415 0.0256  152 ARG A CB  
1184  C CG  . ARG A  152 ? 0.1262 0.2442 0.4103 0.0241  -0.0479 0.0229  152 ARG A CG  
1185  C CD  . ARG A  152 ? 0.1202 0.2522 0.4277 0.0192  -0.0434 0.0245  152 ARG A CD  
1186  N NE  . ARG A  152 ? 0.1137 0.2433 0.4187 0.0173  -0.0319 0.0283  152 ARG A NE  
1187  C CZ  . ARG A  152 ? 0.1969 0.3336 0.5126 0.0133  -0.0244 0.0307  152 ARG A CZ  
1188  N NH1 . ARG A  152 ? 0.1999 0.3469 0.5303 0.0104  -0.0263 0.0293  152 ARG A NH1 
1189  N NH2 . ARG A  152 ? 0.1088 0.2419 0.4194 0.0123  -0.0150 0.0345  152 ARG A NH2 
1190  N N   . VAL A  153 ? 0.1763 0.2701 0.4106 0.0449  -0.0473 0.0258  153 VAL A N   
1191  C CA  . VAL A  153 ? 0.1388 0.2295 0.3665 0.0516  -0.0458 0.0276  153 VAL A CA  
1192  C C   . VAL A  153 ? 0.1522 0.2558 0.3969 0.0560  -0.0517 0.0277  153 VAL A C   
1193  O O   . VAL A  153 ? 0.1387 0.2538 0.4000 0.0532  -0.0572 0.0262  153 VAL A O   
1194  C CB  . VAL A  153 ? 0.2127 0.2870 0.4174 0.0544  -0.0498 0.0273  153 VAL A CB  
1195  C CG1 . VAL A  153 ? 0.2143 0.2771 0.4041 0.0510  -0.0420 0.0272  153 VAL A CG1 
1196  C CG2 . VAL A  153 ? 0.2020 0.2746 0.4039 0.0536  -0.0614 0.0248  153 VAL A CG2 
1197  N N   . GLY A  154 ? 0.1887 0.2902 0.4301 0.0629  -0.0507 0.0294  154 GLY A N   
1198  C CA  . GLY A  154 ? 0.2395 0.3501 0.4907 0.0679  -0.0560 0.0289  154 GLY A CA  
1199  C C   . GLY A  154 ? 0.2474 0.3734 0.5144 0.0646  -0.0497 0.0275  154 GLY A C   
1200  O O   . GLY A  154 ? 0.1346 0.2618 0.4019 0.0612  -0.0393 0.0280  154 GLY A O   
1201  N N   . THR A  155 ? 0.2243 0.3616 0.5039 0.0658  -0.0560 0.0260  155 THR A N   
1202  C CA  . THR A  155 ? 0.2094 0.3615 0.5053 0.0628  -0.0496 0.0248  155 THR A CA  
1203  C C   . THR A  155 ? 0.2674 0.4236 0.5712 0.0534  -0.0458 0.0244  155 THR A C   
1204  O O   . THR A  155 ? 0.3086 0.4703 0.6182 0.0500  -0.0359 0.0250  155 THR A O   
1205  C CB  . THR A  155 ? 0.1529 0.3176 0.4628 0.0662  -0.0573 0.0232  155 THR A CB  
1206  O OG1 . THR A  155 ? 0.1605 0.3227 0.4689 0.0662  -0.0708 0.0221  155 THR A OG1 
1207  C CG2 . THR A  155 ? 0.1597 0.3235 0.4659 0.0758  -0.0565 0.0240  155 THR A CG2 
1208  N N   . PHE A  156 ? 0.3348 0.4870 0.6379 0.0496  -0.0538 0.0234  156 PHE A N   
1209  C CA  . PHE A  156 ? 0.3355 0.4901 0.6468 0.0408  -0.0515 0.0229  156 PHE A CA  
1210  C C   . PHE A  156 ? 0.3492 0.4964 0.6515 0.0384  -0.0406 0.0255  156 PHE A C   
1211  O O   . PHE A  156 ? 0.4104 0.5613 0.7200 0.0325  -0.0338 0.0265  156 PHE A O   
1212  C CB  . PHE A  156 ? 0.2726 0.4216 0.5823 0.0383  -0.0630 0.0207  156 PHE A CB  
1213  C CG  . PHE A  156 ? 0.2980 0.4503 0.6097 0.0425  -0.0762 0.0183  156 PHE A CG  
1214  C CD1 . PHE A  156 ? 0.3246 0.4896 0.6538 0.0389  -0.0820 0.0154  156 PHE A CD1 
1215  C CD2 . PHE A  156 ? 0.3196 0.4618 0.6154 0.0503  -0.0828 0.0192  156 PHE A CD2 
1216  C CE1 . PHE A  156 ? 0.3639 0.5324 0.6943 0.0432  -0.0950 0.0131  156 PHE A CE1 
1217  C CE2 . PHE A  156 ? 0.3460 0.4900 0.6412 0.0549  -0.0957 0.0174  156 PHE A CE2 
1218  C CZ  . PHE A  156 ? 0.3719 0.5296 0.6844 0.0515  -0.1022 0.0142  156 PHE A CZ  
1219  N N   . GLY A  157 ? 0.2562 0.3923 0.5425 0.0428  -0.0393 0.0267  157 GLY A N   
1220  C CA  . GLY A  157 ? 0.2725 0.4022 0.5497 0.0412  -0.0295 0.0287  157 GLY A CA  
1221  C C   . GLY A  157 ? 0.2655 0.3987 0.5411 0.0434  -0.0199 0.0297  157 GLY A C   
1222  O O   . GLY A  157 ? 0.2886 0.4223 0.5635 0.0401  -0.0119 0.0312  157 GLY A O   
1223  N N   . PHE A  158 ? 0.1866 0.3201 0.4595 0.0498  -0.0212 0.0290  158 PHE A N   
1224  C CA  . PHE A  158 ? 0.1957 0.3306 0.4658 0.0529  -0.0127 0.0292  158 PHE A CA  
1225  C C   . PHE A  158 ? 0.1813 0.3275 0.4627 0.0559  -0.0101 0.0281  158 PHE A C   
1226  O O   . PHE A  158 ? 0.1805 0.3266 0.4585 0.0590  -0.0030 0.0278  158 PHE A O   
1227  C CB  . PHE A  158 ? 0.2167 0.3395 0.4716 0.0572  -0.0112 0.0295  158 PHE A CB  
1228  C CG  . PHE A  158 ? 0.2062 0.3200 0.4519 0.0537  -0.0105 0.0305  158 PHE A CG  
1229  C CD1 . PHE A  158 ? 0.1796 0.2928 0.4218 0.0501  -0.0032 0.0313  158 PHE A CD1 
1230  C CD2 . PHE A  158 ? 0.1985 0.3050 0.4395 0.0542  -0.0176 0.0308  158 PHE A CD2 
1231  C CE1 . PHE A  158 ? 0.1746 0.2807 0.4096 0.0474  -0.0029 0.0320  158 PHE A CE1 
1232  C CE2 . PHE A  158 ? 0.1678 0.2669 0.4020 0.0514  -0.0164 0.0315  158 PHE A CE2 
1233  C CZ  . PHE A  158 ? 0.1795 0.2789 0.4112 0.0480  -0.0090 0.0319  158 PHE A CZ  
1234  N N   . LEU A  159 ? 0.1967 0.3529 0.4919 0.0554  -0.0160 0.0270  159 LEU A N   
1235  C CA  . LEU A  159 ? 0.1772 0.3454 0.4847 0.0587  -0.0131 0.0258  159 LEU A CA  
1236  C C   . LEU A  159 ? 0.1890 0.3629 0.5016 0.0542  -0.0020 0.0267  159 LEU A C   
1237  O O   . LEU A  159 ? 0.2004 0.3748 0.5160 0.0472  -0.0002 0.0281  159 LEU A O   
1238  C CB  . LEU A  159 ? 0.1355 0.3149 0.4588 0.0585  -0.0218 0.0243  159 LEU A CB  
1239  C CG  . LEU A  159 ? 0.1412 0.3346 0.4792 0.0628  -0.0195 0.0229  159 LEU A CG  
1240  C CD1 . LEU A  159 ? 0.1492 0.3487 0.4954 0.0674  -0.0314 0.0215  159 LEU A CD1 
1241  C CD2 . LEU A  159 ? 0.1393 0.3451 0.4930 0.0563  -0.0116 0.0229  159 LEU A CD2 
1242  N N   . ALA A  160 ? 0.1296 0.3068 0.4424 0.0585  0.0056  0.0260  160 ALA A N   
1243  C CA  . ALA A  160 ? 0.1282 0.3090 0.4426 0.0550  0.0167  0.0272  160 ALA A CA  
1244  C C   . ALA A  160 ? 0.1607 0.3527 0.4860 0.0590  0.0230  0.0256  160 ALA A C   
1245  O O   . ALA A  160 ? 0.1389 0.3302 0.4623 0.0665  0.0218  0.0235  160 ALA A O   
1246  C CB  . ALA A  160 ? 0.2095 0.3784 0.5065 0.0557  0.0217  0.0282  160 ALA A CB  
1247  N N   . LEU A  161 ? 0.3415 0.5432 0.6782 0.0541  0.0303  0.0268  161 LEU A N   
1248  C CA  . LEU A  161 ? 0.2986 0.5110 0.6450 0.0570  0.0394  0.0256  161 LEU A CA  
1249  C C   . LEU A  161 ? 0.2628 0.4722 0.6020 0.0534  0.0510  0.0282  161 LEU A C   
1250  O O   . LEU A  161 ? 0.2520 0.4681 0.6006 0.0473  0.0567  0.0306  161 LEU A O   
1251  C CB  . LEU A  161 ? 0.2072 0.4354 0.5759 0.0540  0.0381  0.0250  161 LEU A CB  
1252  C CG  . LEU A  161 ? 0.1483 0.3815 0.5251 0.0592  0.0267  0.0224  161 LEU A CG  
1253  C CD1 . LEU A  161 ? 0.1526 0.4028 0.5528 0.0560  0.0256  0.0215  161 LEU A CD1 
1254  C CD2 . LEU A  161 ? 0.1534 0.3853 0.5253 0.0691  0.0285  0.0201  161 LEU A CD2 
1255  N N   . PRO A  162 ? 0.2526 0.4518 0.5750 0.0572  0.0546  0.0279  162 PRO A N   
1256  C CA  . PRO A  162 ? 0.3087 0.5015 0.6189 0.0545  0.0629  0.0308  162 PRO A CA  
1257  C C   . PRO A  162 ? 0.3618 0.5634 0.6792 0.0519  0.0753  0.0329  162 PRO A C   
1258  O O   . PRO A  162 ? 0.3402 0.5502 0.6651 0.0557  0.0815  0.0304  162 PRO A O   
1259  C CB  . PRO A  162 ? 0.2410 0.4251 0.5366 0.0614  0.0644  0.0280  162 PRO A CB  
1260  C CG  . PRO A  162 ? 0.2144 0.3956 0.5113 0.0659  0.0542  0.0251  162 PRO A CG  
1261  C CD  . PRO A  162 ? 0.1876 0.3814 0.5028 0.0654  0.0512  0.0244  162 PRO A CD  
1262  N N   . GLY A  163 ? 0.4527 0.6518 0.7673 0.0455  0.0794  0.0377  163 GLY A N   
1263  C CA  . GLY A  163 ? 0.5004 0.7063 0.8206 0.0421  0.0918  0.0409  163 GLY A CA  
1264  C C   . GLY A  163 ? 0.4610 0.6772 0.8013 0.0358  0.0913  0.0421  163 GLY A C   
1265  O O   . GLY A  163 ? 0.4703 0.6935 0.8180 0.0327  0.1020  0.0443  163 GLY A O   
1266  N N   . SER A  164 ? 0.3579 0.5749 0.7068 0.0338  0.0792  0.0404  164 SER A N   
1267  C CA  . SER A  164 ? 0.3339 0.5602 0.7024 0.0273  0.0772  0.0410  164 SER A CA  
1268  C C   . SER A  164 ? 0.3400 0.5579 0.7062 0.0203  0.0720  0.0445  164 SER A C   
1269  O O   . SER A  164 ? 0.3750 0.5819 0.7279 0.0218  0.0650  0.0446  164 SER A O   
1270  C CB  . SER A  164 ? 0.2374 0.4726 0.6192 0.0306  0.0669  0.0360  164 SER A CB  
1271  O OG  . SER A  164 ? 0.2251 0.4547 0.6067 0.0276  0.0546  0.0356  164 SER A OG  
1272  N N   . ARG A  165 ? 0.2301 0.4527 0.6097 0.0125  0.0759  0.0472  165 ARG A N   
1273  C CA  . ARG A  165 ? 0.2374 0.4516 0.6166 0.0056  0.0717  0.0503  165 ARG A CA  
1274  C C   . ARG A  165 ? 0.1861 0.4006 0.5718 0.0053  0.0569  0.0459  165 ARG A C   
1275  O O   . ARG A  165 ? 0.1684 0.3732 0.5485 0.0025  0.0504  0.0469  165 ARG A O   
1276  C CB  . ARG A  165 ? 0.5082 0.7261 0.8999 -0.0030 0.0808  0.0545  165 ARG A CB  
1277  C CG  . ARG A  165 ? 0.6192 0.8438 1.0316 -0.0100 0.0735  0.0520  165 ARG A CG  
1278  C CD  . ARG A  165 ? 0.7267 0.9411 1.1397 -0.0186 0.0738  0.0563  165 ARG A CD  
1279  N NE  . ARG A  165 ? 0.8302 1.0492 1.2612 -0.0250 0.0648  0.0527  165 ARG A NE  
1280  C CZ  . ARG A  165 ? 0.9163 1.1259 1.3495 -0.0322 0.0612  0.0543  165 ARG A CZ  
1281  N NH1 . ARG A  165 ? 0.9312 1.1263 1.3500 -0.0335 0.0660  0.0601  165 ARG A NH1 
1282  N NH2 . ARG A  165 ? 0.9382 1.1528 1.3881 -0.0378 0.0526  0.0500  165 ARG A NH2 
1283  N N   . GLU A  166 ? 0.2866 0.5122 0.6837 0.0088  0.0518  0.0412  166 GLU A N   
1284  C CA  . GLU A  166 ? 0.3308 0.5589 0.7366 0.0079  0.0381  0.0373  166 GLU A CA  
1285  C C   . GLU A  166 ? 0.2219 0.4404 0.6122 0.0141  0.0276  0.0350  166 GLU A C   
1286  O O   . GLU A  166 ? 0.1776 0.3921 0.5686 0.0121  0.0171  0.0333  166 GLU A O   
1287  C CB  . GLU A  166 ? 0.6502 0.8954 1.0768 0.0088  0.0364  0.0337  166 GLU A CB  
1288  C CG  . GLU A  166 ? 0.7871 1.0392 1.2328 0.0008  0.0302  0.0322  166 GLU A CG  
1289  C CD  . GLU A  166 ? 0.9024 1.1499 1.3518 -0.0088 0.0385  0.0363  166 GLU A CD  
1290  O OE1 . GLU A  166 ? 0.9511 1.2035 1.4049 -0.0107 0.0515  0.0393  166 GLU A OE1 
1291  O OE2 . GLU A  166 ? 0.9264 1.1647 1.3739 -0.0142 0.0324  0.0367  166 GLU A OE2 
1292  N N   . ALA A  167 ? 0.1345 0.3494 0.5113 0.0216  0.0308  0.0347  167 ALA A N   
1293  C CA  . ALA A  167 ? 0.1294 0.3346 0.4909 0.0275  0.0225  0.0329  167 ALA A CA  
1294  C C   . ALA A  167 ? 0.1358 0.3319 0.4792 0.0314  0.0299  0.0347  167 ALA A C   
1295  O O   . ALA A  167 ? 0.1284 0.3247 0.4659 0.0382  0.0318  0.0328  167 ALA A O   
1296  C CB  . ALA A  167 ? 0.1874 0.4000 0.5552 0.0339  0.0154  0.0291  167 ALA A CB  
1297  N N   . PRO A  168 ? 0.1246 0.3126 0.4598 0.0271  0.0339  0.0383  168 PRO A N   
1298  C CA  . PRO A  168 ? 0.1524 0.3343 0.4733 0.0296  0.0422  0.0406  168 PRO A CA  
1299  C C   . PRO A  168 ? 0.1972 0.3694 0.5017 0.0354  0.0375  0.0385  168 PRO A C   
1300  O O   . PRO A  168 ? 0.2375 0.4067 0.5318 0.0392  0.0436  0.0385  168 PRO A O   
1301  C CB  . PRO A  168 ? 0.2268 0.4029 0.5455 0.0233  0.0452  0.0454  168 PRO A CB  
1302  C CG  . PRO A  168 ? 0.2471 0.4275 0.5816 0.0170  0.0403  0.0452  168 PRO A CG  
1303  C CD  . PRO A  168 ? 0.1228 0.3066 0.4617 0.0202  0.0300  0.0402  168 PRO A CD  
1304  N N   . GLY A  169 ? 0.3303 0.4973 0.6322 0.0358  0.0273  0.0366  169 GLY A N   
1305  C CA  . GLY A  169 ? 0.3104 0.4674 0.5974 0.0404  0.0232  0.0350  169 GLY A CA  
1306  C C   . GLY A  169 ? 0.2914 0.4381 0.5665 0.0380  0.0227  0.0371  169 GLY A C   
1307  O O   . GLY A  169 ? 0.3246 0.4711 0.5996 0.0344  0.0280  0.0403  169 GLY A O   
1308  N N   . ASN A  170 ? 0.2287 0.3670 0.4940 0.0406  0.0166  0.0353  170 ASN A N   
1309  C CA  . ASN A  170 ? 0.1896 0.3185 0.4449 0.0388  0.0147  0.0364  170 ASN A CA  
1310  C C   . ASN A  170 ? 0.1773 0.3055 0.4387 0.0334  0.0115  0.0381  170 ASN A C   
1311  O O   . ASN A  170 ? 0.1334 0.2554 0.3890 0.0316  0.0119  0.0396  170 ASN A O   
1312  C CB  . ASN A  170 ? 0.1233 0.2494 0.3696 0.0394  0.0215  0.0379  170 ASN A CB  
1313  C CG  . ASN A  170 ? 0.1055 0.2324 0.3472 0.0444  0.0256  0.0359  170 ASN A CG  
1314  O OD1 . ASN A  170 ? 0.1072 0.2321 0.3476 0.0482  0.0224  0.0332  170 ASN A OD1 
1315  N ND2 . ASN A  170 ? 0.1125 0.2421 0.3518 0.0449  0.0330  0.0374  170 ASN A ND2 
1316  N N   . VAL A  171 ? 0.2510 0.3856 0.5252 0.0309  0.0078  0.0374  171 VAL A N   
1317  C CA  . VAL A  171 ? 0.2466 0.3801 0.5283 0.0255  0.0045  0.0385  171 VAL A CA  
1318  C C   . VAL A  171 ? 0.2326 0.3565 0.5058 0.0265  -0.0020 0.0370  171 VAL A C   
1319  O O   . VAL A  171 ? 0.2728 0.3922 0.5469 0.0232  -0.0026 0.0382  171 VAL A O   
1320  C CB  . VAL A  171 ? 0.2212 0.3642 0.5204 0.0218  0.0014  0.0374  171 VAL A CB  
1321  C CG1 . VAL A  171 ? 0.1097 0.2623 0.4165 0.0219  0.0094  0.0387  171 VAL A CG1 
1322  C CG2 . VAL A  171 ? 0.1092 0.2539 0.4107 0.0248  -0.0083 0.0337  171 VAL A CG2 
1323  N N   . GLY A  172 ? 0.1701 0.2905 0.4351 0.0314  -0.0060 0.0349  172 GLY A N   
1324  C CA  . GLY A  172 ? 0.1779 0.2889 0.4340 0.0328  -0.0105 0.0339  172 GLY A CA  
1325  C C   . GLY A  172 ? 0.1900 0.2935 0.4349 0.0323  -0.0051 0.0351  172 GLY A C   
1326  O O   . GLY A  172 ? 0.1995 0.2946 0.4369 0.0300  -0.0067 0.0343  172 GLY A O   
1327  N N   . LEU A  173 ? 0.0987 0.2039 0.3391 0.0342  0.0011  0.0362  173 LEU A N   
1328  C CA  . LEU A  173 ? 0.0951 0.1960 0.3272 0.0342  0.0055  0.0373  173 LEU A CA  
1329  C C   . LEU A  173 ? 0.0990 0.2001 0.3352 0.0302  0.0075  0.0400  173 LEU A C   
1330  O O   . LEU A  173 ? 0.0961 0.1909 0.3248 0.0295  0.0082  0.0405  173 LEU A O   
1331  C CB  . LEU A  173 ? 0.1027 0.2060 0.3297 0.0368  0.0108  0.0372  173 LEU A CB  
1332  C CG  . LEU A  173 ? 0.0966 0.1960 0.3165 0.0409  0.0103  0.0346  173 LEU A CG  
1333  C CD1 . LEU A  173 ? 0.0980 0.2008 0.3158 0.0433  0.0157  0.0341  173 LEU A CD1 
1334  C CD2 . LEU A  173 ? 0.0960 0.1871 0.3071 0.0409  0.0093  0.0334  173 LEU A CD2 
1335  N N   . LEU A  174 ? 0.1230 0.2313 0.3719 0.0276  0.0085  0.0419  174 LEU A N   
1336  C CA  . LEU A  174 ? 0.1508 0.2576 0.4037 0.0232  0.0106  0.0449  174 LEU A CA  
1337  C C   . LEU A  174 ? 0.1590 0.2575 0.4107 0.0203  0.0050  0.0430  174 LEU A C   
1338  O O   . LEU A  174 ? 0.1724 0.2641 0.4207 0.0184  0.0063  0.0447  174 LEU A O   
1339  C CB  . LEU A  174 ? 0.1803 0.2972 0.4487 0.0202  0.0141  0.0473  174 LEU A CB  
1340  C CG  . LEU A  174 ? 0.1010 0.2239 0.3673 0.0227  0.0215  0.0492  174 LEU A CG  
1341  C CD1 . LEU A  174 ? 0.1050 0.2363 0.3848 0.0190  0.0261  0.0513  174 LEU A CD1 
1342  C CD2 . LEU A  174 ? 0.1029 0.2202 0.3567 0.0241  0.0259  0.0523  174 LEU A CD2 
1343  N N   . ASP A  175 ? 0.1302 0.2286 0.3838 0.0206  -0.0014 0.0392  175 ASP A N   
1344  C CA  . ASP A  175 ? 0.1452 0.2345 0.3948 0.0184  -0.0071 0.0363  175 ASP A CA  
1345  C C   . ASP A  175 ? 0.1721 0.2517 0.4077 0.0206  -0.0053 0.0357  175 ASP A C   
1346  O O   . ASP A  175 ? 0.1705 0.2424 0.4035 0.0187  -0.0051 0.0357  175 ASP A O   
1347  C CB  . ASP A  175 ? 0.1338 0.2235 0.3824 0.0200  -0.0145 0.0323  175 ASP A CB  
1348  C CG  . ASP A  175 ? 0.1385 0.2390 0.4038 0.0179  -0.0182 0.0319  175 ASP A CG  
1349  O OD1 . ASP A  175 ? 0.1108 0.2170 0.3890 0.0135  -0.0149 0.0342  175 ASP A OD1 
1350  O OD2 . ASP A  175 ? 0.1267 0.2300 0.3925 0.0206  -0.0245 0.0295  175 ASP A OD2 
1351  N N   . GLN A  176 ? 0.2646 0.3445 0.4921 0.0247  -0.0038 0.0351  176 GLN A N   
1352  C CA  . GLN A  176 ? 0.2300 0.3032 0.4466 0.0267  -0.0015 0.0344  176 GLN A CA  
1353  C C   . GLN A  176 ? 0.2621 0.3347 0.4798 0.0260  0.0024  0.0375  176 GLN A C   
1354  O O   . GLN A  176 ? 0.3181 0.3836 0.5322 0.0257  0.0021  0.0367  176 GLN A O   
1355  C CB  . GLN A  176 ? 0.1051 0.1807 0.3163 0.0302  0.0007  0.0339  176 GLN A CB  
1356  C CG  . GLN A  176 ? 0.1044 0.1766 0.3101 0.0320  -0.0028 0.0313  176 GLN A CG  
1357  C CD  . GLN A  176 ? 0.1024 0.1758 0.3039 0.0351  -0.0001 0.0312  176 GLN A CD  
1358  O OE1 . GLN A  176 ? 0.0985 0.1756 0.3008 0.0356  0.0040  0.0322  176 GLN A OE1 
1359  N NE2 . GLN A  176 ? 0.1071 0.1763 0.3032 0.0372  -0.0027 0.0298  176 GLN A NE2 
1360  N N   . ARG A  177 ? 0.1195 0.1989 0.3413 0.0261  0.0060  0.0410  177 ARG A N   
1361  C CA  . ARG A  177 ? 0.1043 0.1821 0.3246 0.0261  0.0093  0.0448  177 ARG A CA  
1362  C C   . ARG A  177 ? 0.1104 0.1817 0.3346 0.0230  0.0083  0.0463  177 ARG A C   
1363  O O   . ARG A  177 ? 0.1141 0.1794 0.3345 0.0241  0.0090  0.0478  177 ARG A O   
1364  C CB  . ARG A  177 ? 0.3074 0.3924 0.5298 0.0263  0.0138  0.0486  177 ARG A CB  
1365  C CG  . ARG A  177 ? 0.1104 0.1923 0.3295 0.0263  0.0168  0.0536  177 ARG A CG  
1366  C CD  . ARG A  177 ? 0.1501 0.2380 0.3687 0.0264  0.0221  0.0575  177 ARG A CD  
1367  N NE  . ARG A  177 ? 0.1723 0.2647 0.3841 0.0300  0.0230  0.0551  177 ARG A NE  
1368  C CZ  . ARG A  177 ? 0.1925 0.2911 0.4041 0.0309  0.0275  0.0559  177 ARG A CZ  
1369  N NH1 . ARG A  177 ? 0.1852 0.2876 0.4040 0.0283  0.0322  0.0595  177 ARG A NH1 
1370  N NH2 . ARG A  177 ? 0.1831 0.2840 0.3876 0.0341  0.0277  0.0528  177 ARG A NH2 
1371  N N   . LEU A  178 ? 0.2421 0.3146 0.4748 0.0192  0.0065  0.0457  178 LEU A N   
1372  C CA  . LEU A  178 ? 0.2533 0.3187 0.4908 0.0152  0.0055  0.0465  178 LEU A CA  
1373  C C   . LEU A  178 ? 0.1237 0.1786 0.3538 0.0166  0.0025  0.0428  178 LEU A C   
1374  O O   . LEU A  178 ? 0.1298 0.1767 0.3582 0.0167  0.0038  0.0446  178 LEU A O   
1375  C CB  . LEU A  178 ? 0.1215 0.1912 0.3708 0.0103  0.0025  0.0448  178 LEU A CB  
1376  C CG  . LEU A  178 ? 0.1308 0.1931 0.3868 0.0049  0.0023  0.0458  178 LEU A CG  
1377  C CD1 . LEU A  178 ? 0.2324 0.2948 0.4912 0.0034  0.0091  0.0528  178 LEU A CD1 
1378  C CD2 . LEU A  178 ? 0.2354 0.3024 0.5039 -0.0002 -0.0022 0.0426  178 LEU A CD2 
1379  N N   . ALA A  179 ? 0.1215 0.1759 0.3466 0.0183  -0.0008 0.0379  179 ALA A N   
1380  C CA  . ALA A  179 ? 0.1261 0.1710 0.3430 0.0201  -0.0022 0.0340  179 ALA A CA  
1381  C C   . ALA A  179 ? 0.1242 0.1676 0.3362 0.0241  0.0015  0.0356  179 ALA A C   
1382  O O   . ALA A  179 ? 0.1297 0.1652 0.3387 0.0256  0.0018  0.0339  179 ALA A O   
1383  C CB  . ALA A  179 ? 0.1260 0.1706 0.3363 0.0212  -0.0054 0.0294  179 ALA A CB  
1384  N N   . LEU A  180 ? 0.1357 0.1871 0.3476 0.0262  0.0039  0.0384  180 LEU A N   
1385  C CA  . LEU A  180 ? 0.1164 0.1683 0.3254 0.0298  0.0060  0.0400  180 LEU A CA  
1386  C C   . LEU A  180 ? 0.1466 0.1933 0.3579 0.0300  0.0068  0.0443  180 LEU A C   
1387  O O   . LEU A  180 ? 0.1718 0.2135 0.3817 0.0330  0.0069  0.0438  180 LEU A O   
1388  C CB  . LEU A  180 ? 0.1102 0.1710 0.3178 0.0315  0.0076  0.0417  180 LEU A CB  
1389  C CG  . LEU A  180 ? 0.1053 0.1689 0.3089 0.0332  0.0078  0.0376  180 LEU A CG  
1390  C CD1 . LEU A  180 ? 0.1053 0.1666 0.3073 0.0315  0.0062  0.0344  180 LEU A CD1 
1391  C CD2 . LEU A  180 ? 0.1014 0.1723 0.3035 0.0344  0.0091  0.0389  180 LEU A CD2 
1392  N N   . GLN A  181 ? 0.1357 0.1833 0.3510 0.0270  0.0079  0.0486  181 GLN A N   
1393  C CA  . GLN A  181 ? 0.1858 0.2260 0.4027 0.0263  0.0092  0.0534  181 GLN A CA  
1394  C C   . GLN A  181 ? 0.1697 0.1985 0.3876 0.0255  0.0073  0.0501  181 GLN A C   
1395  O O   . GLN A  181 ? 0.1771 0.1981 0.3934 0.0285  0.0077  0.0518  181 GLN A O   
1396  C CB  . GLN A  181 ? 0.3690 0.4112 0.5913 0.0216  0.0117  0.0579  181 GLN A CB  
1397  C CG  . GLN A  181 ? 0.4655 0.5173 0.6858 0.0225  0.0149  0.0615  181 GLN A CG  
1398  C CD  . GLN A  181 ? 0.5885 0.6442 0.8167 0.0173  0.0183  0.0645  181 GLN A CD  
1399  O OE1 . GLN A  181 ? 0.6771 0.7261 0.9111 0.0130  0.0193  0.0668  181 GLN A OE1 
1400  N NE2 . GLN A  181 ? 0.5792 0.6455 0.8089 0.0175  0.0205  0.0642  181 GLN A NE2 
1401  N N   . TRP A  182 ? 0.1424 0.1701 0.3624 0.0221  0.0049  0.0451  182 TRP A N   
1402  C CA  . TRP A  182 ? 0.1515 0.1676 0.3708 0.0209  0.0029  0.0408  182 TRP A CA  
1403  C C   . TRP A  182 ? 0.1533 0.1644 0.3669 0.0265  0.0037  0.0381  182 TRP A C   
1404  O O   . TRP A  182 ? 0.1633 0.1636 0.3768 0.0279  0.0041  0.0376  182 TRP A O   
1405  C CB  . TRP A  182 ? 0.1514 0.1680 0.3707 0.0173  -0.0009 0.0349  182 TRP A CB  
1406  C CG  . TRP A  182 ? 0.1638 0.1673 0.3815 0.0152  -0.0034 0.0300  182 TRP A CG  
1407  C CD1 . TRP A  182 ? 0.1728 0.1703 0.3968 0.0094  -0.0057 0.0293  182 TRP A CD1 
1408  C CD2 . TRP A  182 ? 0.1704 0.1645 0.3796 0.0187  -0.0033 0.0246  182 TRP A CD2 
1409  N NE1 . TRP A  182 ? 0.1851 0.1693 0.4039 0.0092  -0.0077 0.0234  182 TRP A NE1 
1410  C CE2 . TRP A  182 ? 0.1840 0.1658 0.3933 0.0152  -0.0059 0.0205  182 TRP A CE2 
1411  C CE3 . TRP A  182 ? 0.1670 0.1623 0.3693 0.0242  -0.0008 0.0225  182 TRP A CE3 
1412  C CZ2 . TRP A  182 ? 0.1949 0.1649 0.3958 0.0176  -0.0059 0.0143  182 TRP A CZ2 
1413  C CZ3 . TRP A  182 ? 0.2169 0.2016 0.4124 0.0263  -0.0001 0.0168  182 TRP A CZ3 
1414  C CH2 . TRP A  182 ? 0.1913 0.1630 0.3852 0.0234  -0.0025 0.0127  182 TRP A CH2 
1415  N N   . VAL A  183 ? 0.1447 0.1635 0.3546 0.0297  0.0044  0.0361  183 VAL A N   
1416  C CA  . VAL A  183 ? 0.1455 0.1626 0.3529 0.0349  0.0060  0.0337  183 VAL A CA  
1417  C C   . VAL A  183 ? 0.1533 0.1694 0.3638 0.0388  0.0069  0.0388  183 VAL A C   
1418  O O   . VAL A  183 ? 0.1827 0.1913 0.3940 0.0424  0.0075  0.0375  183 VAL A O   
1419  C CB  . VAL A  183 ? 0.1362 0.1625 0.3408 0.0365  0.0071  0.0312  183 VAL A CB  
1420  C CG1 . VAL A  183 ? 0.1365 0.1639 0.3422 0.0415  0.0093  0.0296  183 VAL A CG1 
1421  C CG2 . VAL A  183 ? 0.1375 0.1609 0.3365 0.0340  0.0062  0.0262  183 VAL A CG2 
1422  N N   . GLN A  184 ? 0.1454 0.1680 0.3568 0.0386  0.0069  0.0446  184 GLN A N   
1423  C CA  . GLN A  184 ? 0.1518 0.1721 0.3636 0.0428  0.0068  0.0502  184 GLN A CA  
1424  C C   . GLN A  184 ? 0.2001 0.2061 0.4133 0.0427  0.0071  0.0523  184 GLN A C   
1425  O O   . GLN A  184 ? 0.2144 0.2146 0.4285 0.0481  0.0068  0.0524  184 GLN A O   
1426  C CB  . GLN A  184 ? 0.2312 0.2583 0.4408 0.0420  0.0072  0.0564  184 GLN A CB  
1427  C CG  . GLN A  184 ? 0.3077 0.3324 0.5147 0.0472  0.0063  0.0624  184 GLN A CG  
1428  C CD  . GLN A  184 ? 0.3616 0.3928 0.5629 0.0472  0.0068  0.0680  184 GLN A CD  
1429  O OE1 . GLN A  184 ? 0.3577 0.3855 0.5571 0.0434  0.0096  0.0730  184 GLN A OE1 
1430  N NE2 . GLN A  184 ? 0.3668 0.4072 0.5654 0.0513  0.0045  0.0669  184 GLN A NE2 
1431  N N   . GLU A  185 ? 0.2611 0.2612 0.4756 0.0366  0.0076  0.0535  185 GLU A N   
1432  C CA  . GLU A  185 ? 0.3310 0.3160 0.5472 0.0349  0.0081  0.0553  185 GLU A CA  
1433  C C   . GLU A  185 ? 0.3304 0.3046 0.5465 0.0368  0.0074  0.0486  185 GLU A C   
1434  O O   . GLU A  185 ? 0.4108 0.3732 0.6273 0.0404  0.0079  0.0502  185 GLU A O   
1435  C CB  . GLU A  185 ? 0.6254 0.6086 0.8455 0.0267  0.0087  0.0567  185 GLU A CB  
1436  C CG  . GLU A  185 ? 0.7877 0.7780 1.0082 0.0246  0.0113  0.0643  185 GLU A CG  
1437  C CD  . GLU A  185 ? 0.9504 0.9386 1.1780 0.0161  0.0129  0.0658  185 GLU A CD  
1438  O OE1 . GLU A  185 ? 0.9895 0.9659 1.2209 0.0122  0.0120  0.0632  185 GLU A OE1 
1439  O OE2 . GLU A  185 ? 1.0068 1.0053 1.2368 0.0132  0.0154  0.0691  185 GLU A OE2 
1440  N N   . ASN A  186 ? 0.2447 0.2215 0.4595 0.0344  0.0064  0.0412  186 ASN A N   
1441  C CA  . ASN A  186 ? 0.2128 0.1783 0.4251 0.0357  0.0063  0.0341  186 ASN A CA  
1442  C C   . ASN A  186 ? 0.2155 0.1840 0.4246 0.0414  0.0080  0.0284  186 ASN A C   
1443  O O   . ASN A  186 ? 0.2434 0.2016 0.4491 0.0424  0.0088  0.0222  186 ASN A O   
1444  C CB  . ASN A  186 ? 0.2051 0.1661 0.4161 0.0286  0.0038  0.0289  186 ASN A CB  
1445  C CG  . ASN A  186 ? 0.2598 0.2212 0.4768 0.0218  0.0026  0.0336  186 ASN A CG  
1446  O OD1 . ASN A  186 ? 0.3418 0.2908 0.5618 0.0187  0.0027  0.0345  186 ASN A OD1 
1447  N ND2 . ASN A  186 ? 0.1892 0.1646 0.4087 0.0194  0.0023  0.0367  186 ASN A ND2 
1448  N N   . ILE A  187 ? 0.1810 0.1629 0.3907 0.0447  0.0089  0.0295  187 ILE A N   
1449  C CA  . ILE A  187 ? 0.2396 0.2242 0.4467 0.0478  0.0114  0.0231  187 ILE A CA  
1450  C C   . ILE A  187 ? 0.2602 0.2383 0.4704 0.0546  0.0142  0.0210  187 ILE A C   
1451  O O   . ILE A  187 ? 0.2638 0.2385 0.4711 0.0566  0.0174  0.0145  187 ILE A O   
1452  C CB  . ILE A  187 ? 0.1648 0.1646 0.3722 0.0484  0.0123  0.0235  187 ILE A CB  
1453  C CG1 . ILE A  187 ? 0.1650 0.1646 0.3661 0.0476  0.0150  0.0168  187 ILE A CG1 
1454  C CG2 . ILE A  187 ? 0.1611 0.1689 0.3755 0.0544  0.0132  0.0260  187 ILE A CG2 
1455  C CD1 . ILE A  187 ? 0.1712 0.1626 0.3639 0.0426  0.0128  0.0134  187 ILE A CD1 
1456  N N   . ALA A  188 ? 0.2499 0.2257 0.4656 0.0586  0.0131  0.0265  188 ALA A N   
1457  C CA  . ALA A  188 ? 0.2909 0.2616 0.5116 0.0663  0.0151  0.0250  188 ALA A CA  
1458  C C   . ALA A  188 ? 0.3164 0.2695 0.5330 0.0658  0.0170  0.0194  188 ALA A C   
1459  O O   . ALA A  188 ? 0.3439 0.2925 0.5623 0.0715  0.0205  0.0144  188 ALA A O   
1460  C CB  . ALA A  188 ? 0.4834 0.4538 0.7092 0.0711  0.0125  0.0329  188 ALA A CB  
1461  N N   . ALA A  189 ? 0.2229 0.1663 0.4343 0.0589  0.0148  0.0195  189 ALA A N   
1462  C CA  . ALA A  189 ? 0.2392 0.1654 0.4455 0.0572  0.0156  0.0130  189 ALA A CA  
1463  C C   . ALA A  189 ? 0.2406 0.1673 0.4401 0.0583  0.0189  0.0041  189 ALA A C   
1464  O O   . ALA A  189 ? 0.2607 0.1741 0.4562 0.0609  0.0216  -0.0023 189 ALA A O   
1465  C CB  . ALA A  189 ? 0.3988 0.3180 0.6023 0.0482  0.0119  0.0137  189 ALA A CB  
1466  N N   . PHE A  190 ? 0.2847 0.2255 0.4817 0.0563  0.0193  0.0037  190 PHE A N   
1467  C CA  . PHE A  190 ? 0.2898 0.2308 0.4784 0.0570  0.0233  -0.0037 190 PHE A CA  
1468  C C   . PHE A  190 ? 0.2933 0.2433 0.4883 0.0640  0.0294  -0.0049 190 PHE A C   
1469  O O   . PHE A  190 ? 0.2855 0.2365 0.4743 0.0646  0.0344  -0.0104 190 PHE A O   
1470  C CB  . PHE A  190 ? 0.2192 0.1687 0.4010 0.0511  0.0208  -0.0035 190 PHE A CB  
1471  C CG  . PHE A  190 ? 0.2411 0.1843 0.4183 0.0442  0.0147  -0.0035 190 PHE A CG  
1472  C CD1 . PHE A  190 ? 0.2144 0.1634 0.3995 0.0406  0.0106  0.0033  190 PHE A CD1 
1473  C CD2 . PHE A  190 ? 0.2861 0.2182 0.4513 0.0411  0.0130  -0.0105 190 PHE A CD2 
1474  C CE1 . PHE A  190 ? 0.2180 0.1631 0.4020 0.0339  0.0054  0.0030  190 PHE A CE1 
1475  C CE2 . PHE A  190 ? 0.2406 0.1686 0.4038 0.0345  0.0063  -0.0111 190 PHE A CE2 
1476  C CZ  . PHE A  190 ? 0.2377 0.1729 0.4119 0.0308  0.0027  -0.0044 190 PHE A CZ  
1477  N N   . GLY A  191 ? 0.2198 0.1769 0.4272 0.0691  0.0289  0.0003  191 GLY A N   
1478  C CA  . GLY A  191 ? 0.2148 0.1835 0.4318 0.0755  0.0335  -0.0008 191 GLY A CA  
1479  C C   . GLY A  191 ? 0.1969 0.1843 0.4199 0.0739  0.0318  0.0035  191 GLY A C   
1480  O O   . GLY A  191 ? 0.1913 0.1908 0.4234 0.0777  0.0352  0.0022  191 GLY A O   
1481  N N   . GLY A  192 ? 0.3489 0.3388 0.5675 0.0683  0.0267  0.0083  192 GLY A N   
1482  C CA  . GLY A  192 ? 0.3371 0.3426 0.5594 0.0664  0.0247  0.0120  192 GLY A CA  
1483  C C   . GLY A  192 ? 0.2993 0.3127 0.5318 0.0712  0.0211  0.0177  192 GLY A C   
1484  O O   . GLY A  192 ? 0.2999 0.3060 0.5365 0.0762  0.0200  0.0195  192 GLY A O   
1485  N N   . ASP A  193 ? 0.1583 0.1856 0.3939 0.0699  0.0189  0.0204  193 ASP A N   
1486  C CA  . ASP A  193 ? 0.1578 0.1928 0.3961 0.0728  0.0140  0.0251  193 ASP A CA  
1487  C C   . ASP A  193 ? 0.1499 0.1900 0.3844 0.0690  0.0102  0.0304  193 ASP A C   
1488  O O   . ASP A  193 ? 0.1409 0.1914 0.3745 0.0661  0.0101  0.0289  193 ASP A O   
1489  C CB  . ASP A  193 ? 0.2949 0.3430 0.5383 0.0747  0.0149  0.0212  193 ASP A CB  
1490  C CG  . ASP A  193 ? 0.3170 0.3729 0.5624 0.0785  0.0086  0.0251  193 ASP A CG  
1491  O OD1 . ASP A  193 ? 0.3725 0.4213 0.6147 0.0810  0.0047  0.0310  193 ASP A OD1 
1492  O OD2 . ASP A  193 ? 0.2638 0.3325 0.5142 0.0791  0.0076  0.0222  193 ASP A OD2 
1493  N N   . PRO A  194 ? 0.1866 0.2187 0.4186 0.0689  0.0076  0.0365  194 PRO A N   
1494  C CA  . PRO A  194 ? 0.1793 0.2162 0.4056 0.0647  0.0053  0.0410  194 PRO A CA  
1495  C C   . PRO A  194 ? 0.2247 0.2747 0.4523 0.0671  0.0021  0.0422  194 PRO A C   
1496  O O   . PRO A  194 ? 0.2485 0.3052 0.4732 0.0640  0.0014  0.0435  194 PRO A O   
1497  C CB  . PRO A  194 ? 0.2074 0.2329 0.4297 0.0646  0.0039  0.0476  194 PRO A CB  
1498  C CG  . PRO A  194 ? 0.2392 0.2515 0.4628 0.0651  0.0061  0.0446  194 PRO A CG  
1499  C CD  . PRO A  194 ? 0.2595 0.2764 0.4900 0.0708  0.0075  0.0391  194 PRO A CD  
1500  N N   . MET A  195 ? 0.1497 0.2031 0.3801 0.0721  0.0000  0.0409  195 MET A N   
1501  C CA  . MET A  195 ? 0.1474 0.2131 0.3782 0.0738  -0.0042 0.0407  195 MET A CA  
1502  C C   . MET A  195 ? 0.1997 0.2760 0.4326 0.0695  -0.0021 0.0342  195 MET A C   
1503  O O   . MET A  195 ? 0.1336 0.2201 0.3669 0.0692  -0.0054 0.0335  195 MET A O   
1504  C CB  . MET A  195 ? 0.1677 0.2350 0.4025 0.0808  -0.0079 0.0409  195 MET A CB  
1505  C CG  . MET A  195 ? 0.1880 0.2441 0.4188 0.0857  -0.0109 0.0487  195 MET A CG  
1506  S SD  . MET A  195 ? 0.6012 0.6566 0.8365 0.0951  -0.0151 0.0487  195 MET A SD  
1507  C CE  . MET A  195 ? 0.1789 0.2551 0.4203 0.0965  -0.0200 0.0435  195 MET A CE  
1508  N N   . SER A  196 ? 0.1330 0.2064 0.3673 0.0663  0.0034  0.0295  196 SER A N   
1509  C CA  . SER A  196 ? 0.1249 0.2061 0.3602 0.0619  0.0061  0.0247  196 SER A CA  
1510  C C   . SER A  196 ? 0.1200 0.1950 0.3509 0.0573  0.0104  0.0238  196 SER A C   
1511  O O   . SER A  196 ? 0.1224 0.1905 0.3541 0.0573  0.0145  0.0215  196 SER A O   
1512  C CB  . SER A  196 ? 0.1268 0.2140 0.3700 0.0634  0.0088  0.0192  196 SER A CB  
1513  O OG  . SER A  196 ? 0.1206 0.2149 0.3660 0.0590  0.0118  0.0150  196 SER A OG  
1514  N N   . VAL A  197 ? 0.1526 0.2306 0.3792 0.0539  0.0093  0.0253  197 VAL A N   
1515  C CA  . VAL A  197 ? 0.1689 0.2419 0.3917 0.0503  0.0121  0.0249  197 VAL A CA  
1516  C C   . VAL A  197 ? 0.1735 0.2524 0.3946 0.0469  0.0133  0.0226  197 VAL A C   
1517  O O   . VAL A  197 ? 0.1505 0.2353 0.3702 0.0464  0.0104  0.0238  197 VAL A O   
1518  C CB  . VAL A  197 ? 0.1119 0.1791 0.3287 0.0490  0.0098  0.0299  197 VAL A CB  
1519  C CG1 . VAL A  197 ? 0.1103 0.1729 0.3208 0.0447  0.0114  0.0284  197 VAL A CG1 
1520  C CG2 . VAL A  197 ? 0.1197 0.1786 0.3376 0.0514  0.0090  0.0323  197 VAL A CG2 
1521  N N   . THR A  198 ? 0.2502 0.3262 0.4700 0.0446  0.0178  0.0190  198 THR A N   
1522  C CA  . THR A  198 ? 0.2992 0.3778 0.5163 0.0412  0.0196  0.0171  198 THR A CA  
1523  C C   . THR A  198 ? 0.3620 0.4322 0.5685 0.0388  0.0201  0.0181  198 THR A C   
1524  O O   . THR A  198 ? 0.4389 0.5010 0.6403 0.0385  0.0221  0.0171  198 THR A O   
1525  C CB  . THR A  198 ? 0.1030 0.1839 0.3253 0.0402  0.0249  0.0127  198 THR A CB  
1526  O OG1 . THR A  198 ? 0.2753 0.3655 0.5074 0.0420  0.0230  0.0113  198 THR A OG1 
1527  C CG2 . THR A  198 ? 0.1023 0.1827 0.3205 0.0361  0.0274  0.0112  198 THR A CG2 
1528  N N   . LEU A  199 ? 0.1789 0.2511 0.3822 0.0374  0.0178  0.0199  199 LEU A N   
1529  C CA  . LEU A  199 ? 0.1302 0.1963 0.3255 0.0357  0.0179  0.0206  199 LEU A CA  
1530  C C   . LEU A  199 ? 0.1568 0.2201 0.3482 0.0338  0.0216  0.0179  199 LEU A C   
1531  O O   . LEU A  199 ? 0.1887 0.2571 0.3840 0.0328  0.0229  0.0163  199 LEU A O   
1532  C CB  . LEU A  199 ? 0.1916 0.2615 0.3862 0.0357  0.0150  0.0234  199 LEU A CB  
1533  C CG  . LEU A  199 ? 0.2210 0.2927 0.4177 0.0367  0.0123  0.0273  199 LEU A CG  
1534  C CD1 . LEU A  199 ? 0.0951 0.1703 0.2903 0.0363  0.0116  0.0292  199 LEU A CD1 
1535  C CD2 . LEU A  199 ? 0.1005 0.1657 0.2966 0.0362  0.0114  0.0281  199 LEU A CD2 
1536  N N   . PHE A  200 ? 0.1501 0.2046 0.3333 0.0331  0.0234  0.0173  200 PHE A N   
1537  C CA  . PHE A  200 ? 0.1477 0.1971 0.3249 0.0313  0.0271  0.0160  200 PHE A CA  
1538  C C   . PHE A  200 ? 0.1777 0.2183 0.3438 0.0317  0.0254  0.0175  200 PHE A C   
1539  O O   . PHE A  200 ? 0.1259 0.1616 0.2870 0.0325  0.0230  0.0178  200 PHE A O   
1540  C CB  . PHE A  200 ? 0.1202 0.1678 0.2985 0.0300  0.0335  0.0132  200 PHE A CB  
1541  C CG  . PHE A  200 ? 0.1296 0.1681 0.2995 0.0307  0.0363  0.0123  200 PHE A CG  
1542  C CD1 . PHE A  200 ? 0.1298 0.1671 0.2997 0.0327  0.0330  0.0125  200 PHE A CD1 
1543  C CD2 . PHE A  200 ? 0.1404 0.1706 0.3016 0.0291  0.0428  0.0111  200 PHE A CD2 
1544  C CE1 . PHE A  200 ? 0.1406 0.1686 0.3015 0.0333  0.0355  0.0106  200 PHE A CE1 
1545  C CE2 . PHE A  200 ? 0.1517 0.1727 0.3028 0.0299  0.0458  0.0098  200 PHE A CE2 
1546  C CZ  . PHE A  200 ? 0.1518 0.1717 0.3025 0.0322  0.0418  0.0092  200 PHE A CZ  
1547  N N   . GLY A  201 ? 0.3084 0.3467 0.4710 0.0312  0.0260  0.0180  201 GLY A N   
1548  C CA  . GLY A  201 ? 0.2762 0.3074 0.4298 0.0326  0.0230  0.0199  201 GLY A CA  
1549  C C   . GLY A  201 ? 0.3005 0.3238 0.4468 0.0321  0.0263  0.0202  201 GLY A C   
1550  O O   . GLY A  201 ? 0.3518 0.3763 0.5018 0.0298  0.0308  0.0186  201 GLY A O   
1551  N N   . GLU A  202 ? 0.2686 0.2833 0.4048 0.0343  0.0237  0.0222  202 GLU A N   
1552  C CA  . GLU A  202 ? 0.3223 0.3265 0.4495 0.0344  0.0267  0.0233  202 GLU A CA  
1553  C C   . GLU A  202 ? 0.3437 0.3458 0.4685 0.0384  0.0214  0.0255  202 GLU A C   
1554  O O   . GLU A  202 ? 0.3826 0.3871 0.5072 0.0410  0.0151  0.0267  202 GLU A O   
1555  C CB  . GLU A  202 ? 0.3785 0.3699 0.4913 0.0337  0.0306  0.0239  202 GLU A CB  
1556  C CG  . GLU A  202 ? 0.4557 0.4346 0.5589 0.0325  0.0365  0.0253  202 GLU A CG  
1557  C CD  . GLU A  202 ? 0.5536 0.5208 0.6435 0.0367  0.0320  0.0289  202 GLU A CD  
1558  O OE1 . GLU A  202 ? 0.5655 0.5365 0.6557 0.0406  0.0238  0.0298  202 GLU A OE1 
1559  O OE2 . GLU A  202 ? 0.5999 0.5541 0.6796 0.0363  0.0367  0.0309  202 GLU A OE2 
1560  N N   . SER A  203 ? 0.2718 0.2694 0.3957 0.0388  0.0238  0.0259  203 SER A N   
1561  C CA  . SER A  203 ? 0.2860 0.2818 0.4094 0.0434  0.0196  0.0277  203 SER A CA  
1562  C C   . SER A  203 ? 0.2591 0.2695 0.3957 0.0453  0.0151  0.0270  203 SER A C   
1563  O O   . SER A  203 ? 0.2068 0.2260 0.3522 0.0433  0.0173  0.0249  203 SER A O   
1564  C CB  . SER A  203 ? 0.3393 0.3238 0.4494 0.0472  0.0154  0.0309  203 SER A CB  
1565  O OG  . SER A  203 ? 0.3614 0.3403 0.4692 0.0521  0.0128  0.0329  203 SER A OG  
1566  N N   . ALA A  204 ? 0.3996 0.4123 0.5372 0.0492  0.0089  0.0288  204 ALA A N   
1567  C CA  . ALA A  204 ? 0.3705 0.3972 0.5213 0.0504  0.0056  0.0286  204 ALA A CA  
1568  C C   . ALA A  204 ? 0.3336 0.3682 0.4902 0.0462  0.0069  0.0274  204 ALA A C   
1569  O O   . ALA A  204 ? 0.3125 0.3572 0.4786 0.0454  0.0080  0.0268  204 ALA A O   
1570  C CB  . ALA A  204 ? 0.1483 0.1767 0.3005 0.0541  -0.0016 0.0303  204 ALA A CB  
1571  N N   . GLY A  205 ? 0.2209 0.2500 0.3708 0.0439  0.0071  0.0270  205 GLY A N   
1572  C CA  . GLY A  205 ? 0.2055 0.2403 0.3604 0.0407  0.0083  0.0258  205 GLY A CA  
1573  C C   . GLY A  205 ? 0.2316 0.2710 0.3914 0.0385  0.0133  0.0243  205 GLY A C   
1574  O O   . GLY A  205 ? 0.2710 0.3191 0.4388 0.0376  0.0130  0.0243  205 GLY A O   
1575  N N   . ALA A  206 ? 0.2165 0.2496 0.3713 0.0376  0.0175  0.0232  206 ALA A N   
1576  C CA  . ALA A  206 ? 0.2131 0.2512 0.3735 0.0353  0.0210  0.0210  206 ALA A CA  
1577  C C   . ALA A  206 ? 0.2119 0.2578 0.3782 0.0369  0.0195  0.0209  206 ALA A C   
1578  O O   . ALA A  206 ? 0.1810 0.2348 0.3529 0.0358  0.0197  0.0198  206 ALA A O   
1579  C CB  . ALA A  206 ? 0.1897 0.2190 0.3447 0.0333  0.0258  0.0195  206 ALA A CB  
1580  N N   . ALA A  207 ? 0.2210 0.2646 0.3857 0.0401  0.0178  0.0222  207 ALA A N   
1581  C CA  . ALA A  207 ? 0.2091 0.2598 0.3791 0.0422  0.0175  0.0220  207 ALA A CA  
1582  C C   . ALA A  207 ? 0.2043 0.2652 0.3813 0.0419  0.0156  0.0236  207 ALA A C   
1583  O O   . ALA A  207 ? 0.1285 0.1962 0.3087 0.0420  0.0169  0.0233  207 ALA A O   
1584  C CB  . ALA A  207 ? 0.1230 0.1700 0.2918 0.0463  0.0162  0.0231  207 ALA A CB  
1585  N N   . SER A  208 ? 0.1084 0.1690 0.2863 0.0415  0.0128  0.0254  208 SER A N   
1586  C CA  . SER A  208 ? 0.3112 0.3794 0.4959 0.0405  0.0113  0.0272  208 SER A CA  
1587  C C   . SER A  208 ? 0.0993 0.1702 0.2845 0.0385  0.0132  0.0267  208 SER A C   
1588  O O   . SER A  208 ? 0.1220 0.1993 0.3107 0.0386  0.0139  0.0280  208 SER A O   
1589  C CB  . SER A  208 ? 0.1046 0.1701 0.2894 0.0398  0.0076  0.0281  208 SER A CB  
1590  O OG  . SER A  208 ? 0.1082 0.1735 0.2943 0.0422  0.0043  0.0288  208 SER A OG  
1591  N N   . VAL A  209 ? 0.1009 0.1670 0.2824 0.0371  0.0142  0.0248  209 VAL A N   
1592  C CA  . VAL A  209 ? 0.1393 0.2090 0.3231 0.0358  0.0152  0.0239  209 VAL A CA  
1593  C C   . VAL A  209 ? 0.0973 0.1723 0.2817 0.0363  0.0159  0.0231  209 VAL A C   
1594  O O   . VAL A  209 ? 0.0957 0.1762 0.2821 0.0368  0.0150  0.0245  209 VAL A O   
1595  C CB  . VAL A  209 ? 0.1395 0.2044 0.3211 0.0341  0.0174  0.0213  209 VAL A CB  
1596  C CG1 . VAL A  209 ? 0.0983 0.1691 0.2849 0.0333  0.0179  0.0197  209 VAL A CG1 
1597  C CG2 . VAL A  209 ? 0.1428 0.2018 0.3216 0.0339  0.0171  0.0218  209 VAL A CG2 
1598  N N   . GLY A  210 ? 0.1372 0.2093 0.3185 0.0365  0.0174  0.0208  210 GLY A N   
1599  C CA  . GLY A  210 ? 0.1465 0.2222 0.3266 0.0370  0.0181  0.0189  210 GLY A CA  
1600  C C   . GLY A  210 ? 0.1327 0.2140 0.3135 0.0391  0.0179  0.0216  210 GLY A C   
1601  O O   . GLY A  210 ? 0.1261 0.2120 0.3052 0.0394  0.0176  0.0216  210 GLY A O   
1602  N N   . MET A  211 ? 0.1006 0.1817 0.2837 0.0405  0.0182  0.0240  211 MET A N   
1603  C CA  . MET A  211 ? 0.1003 0.1874 0.2862 0.0418  0.0194  0.0268  211 MET A CA  
1604  C C   . MET A  211 ? 0.0989 0.1896 0.2860 0.0406  0.0187  0.0300  211 MET A C   
1605  O O   . MET A  211 ? 0.1020 0.1966 0.2872 0.0413  0.0206  0.0319  211 MET A O   
1606  C CB  . MET A  211 ? 0.0993 0.1871 0.2909 0.0431  0.0190  0.0284  211 MET A CB  
1607  C CG  . MET A  211 ? 0.1055 0.1956 0.2980 0.0462  0.0218  0.0274  211 MET A CG  
1608  S SD  . MET A  211 ? 0.2030 0.2895 0.3991 0.0490  0.0196  0.0269  211 MET A SD  
1609  C CE  . MET A  211 ? 0.1117 0.1899 0.2996 0.0512  0.0219  0.0228  211 MET A CE  
1610  N N   . HIS A  212 ? 0.1354 0.2237 0.3246 0.0390  0.0163  0.0308  212 HIS A N   
1611  C CA  . HIS A  212 ? 0.1312 0.2210 0.3212 0.0385  0.0154  0.0338  212 HIS A CA  
1612  C C   . HIS A  212 ? 0.0994 0.1911 0.2847 0.0394  0.0146  0.0327  212 HIS A C   
1613  O O   . HIS A  212 ? 0.1559 0.2493 0.3394 0.0402  0.0142  0.0359  212 HIS A O   
1614  C CB  . HIS A  212 ? 0.0947 0.1804 0.2876 0.0373  0.0134  0.0339  212 HIS A CB  
1615  C CG  . HIS A  212 ? 0.0941 0.1780 0.2912 0.0361  0.0127  0.0353  212 HIS A CG  
1616  N ND1 . HIS A  212 ? 0.0953 0.1815 0.2970 0.0350  0.0132  0.0389  212 HIS A ND1 
1617  C CD2 . HIS A  212 ? 0.0941 0.1740 0.2913 0.0356  0.0110  0.0334  212 HIS A CD2 
1618  C CE1 . HIS A  212 ? 0.1224 0.2072 0.3286 0.0336  0.0114  0.0386  212 HIS A CE1 
1619  N NE2 . HIS A  212 ? 0.1007 0.1816 0.3033 0.0343  0.0096  0.0353  212 HIS A NE2 
1620  N N   . ILE A  213 ? 0.1158 0.2068 0.2993 0.0391  0.0141  0.0282  213 ILE A N   
1621  C CA  . ILE A  213 ? 0.1067 0.2009 0.2868 0.0397  0.0122  0.0261  213 ILE A CA  
1622  C C   . ILE A  213 ? 0.1093 0.2056 0.2824 0.0413  0.0135  0.0270  213 ILE A C   
1623  O O   . ILE A  213 ? 0.1157 0.2144 0.2838 0.0427  0.0117  0.0286  213 ILE A O   
1624  C CB  . ILE A  213 ? 0.1071 0.2002 0.2880 0.0381  0.0119  0.0203  213 ILE A CB  
1625  C CG1 . ILE A  213 ? 0.0990 0.1905 0.2862 0.0365  0.0117  0.0193  213 ILE A CG1 
1626  C CG2 . ILE A  213 ? 0.1086 0.2059 0.2860 0.0384  0.0091  0.0171  213 ILE A CG2 
1627  C CD1 . ILE A  213 ? 0.0999 0.1879 0.2879 0.0340  0.0137  0.0149  213 ILE A CD1 
1628  N N   . LEU A  214 ? 0.1656 0.2606 0.3378 0.0416  0.0169  0.0261  214 LEU A N   
1629  C CA  . LEU A  214 ? 0.2085 0.3050 0.3735 0.0434  0.0196  0.0258  214 LEU A CA  
1630  C C   . LEU A  214 ? 0.2815 0.3805 0.4456 0.0444  0.0227  0.0315  214 LEU A C   
1631  O O   . LEU A  214 ? 0.3396 0.4398 0.4960 0.0460  0.0258  0.0318  214 LEU A O   
1632  C CB  . LEU A  214 ? 0.1181 0.2120 0.2834 0.0441  0.0225  0.0220  214 LEU A CB  
1633  C CG  . LEU A  214 ? 0.1190 0.2089 0.2831 0.0427  0.0204  0.0163  214 LEU A CG  
1634  C CD1 . LEU A  214 ? 0.1212 0.2060 0.2855 0.0437  0.0232  0.0133  214 LEU A CD1 
1635  C CD2 . LEU A  214 ? 0.1268 0.2184 0.2832 0.0426  0.0182  0.0129  214 LEU A CD2 
1636  N N   . SER A  215 ? 0.2310 0.3301 0.4024 0.0431  0.0225  0.0359  215 SER A N   
1637  C CA  . SER A  215 ? 0.2366 0.3374 0.4092 0.0428  0.0261  0.0416  215 SER A CA  
1638  C C   . SER A  215 ? 0.2688 0.3675 0.4380 0.0427  0.0238  0.0461  215 SER A C   
1639  O O   . SER A  215 ? 0.3181 0.4145 0.4924 0.0417  0.0203  0.0466  215 SER A O   
1640  C CB  . SER A  215 ? 0.2141 0.3162 0.3984 0.0410  0.0273  0.0430  215 SER A CB  
1641  O OG  . SER A  215 ? 0.2111 0.3157 0.3990 0.0399  0.0316  0.0480  215 SER A OG  
1642  N N   . LEU A  216 ? 0.1367 0.2353 0.2965 0.0440  0.0262  0.0496  216 LEU A N   
1643  C CA  . LEU A  216 ? 0.1419 0.2372 0.2954 0.0451  0.0235  0.0544  216 LEU A CA  
1644  C C   . LEU A  216 ? 0.1435 0.2349 0.3050 0.0433  0.0230  0.0593  216 LEU A C   
1645  O O   . LEU A  216 ? 0.1413 0.2295 0.3021 0.0448  0.0184  0.0606  216 LEU A O   
1646  C CB  . LEU A  216 ? 0.4496 0.5440 0.5893 0.0469  0.0276  0.0582  216 LEU A CB  
1647  C CG  . LEU A  216 ? 0.1705 0.2617 0.2962 0.0501  0.0233  0.0610  216 LEU A CG  
1648  C CD1 . LEU A  216 ? 0.1796 0.2651 0.3031 0.0498  0.0259  0.0698  216 LEU A CD1 
1649  C CD2 . LEU A  216 ? 0.1645 0.2571 0.2936 0.0515  0.0146  0.0566  216 LEU A CD2 
1650  N N   . PRO A  217 ? 0.2459 0.3377 0.4161 0.0403  0.0274  0.0616  217 PRO A N   
1651  C CA  . PRO A  217 ? 0.2473 0.3341 0.4251 0.0380  0.0264  0.0651  217 PRO A CA  
1652  C C   . PRO A  217 ? 0.2980 0.3832 0.4825 0.0378  0.0211  0.0607  217 PRO A C   
1653  O O   . PRO A  217 ? 0.3493 0.4287 0.5365 0.0374  0.0191  0.0627  217 PRO A O   
1654  C CB  . PRO A  217 ? 0.1345 0.2242 0.3220 0.0342  0.0316  0.0666  217 PRO A CB  
1655  C CG  . PRO A  217 ? 0.1401 0.2347 0.3217 0.0354  0.0373  0.0673  217 PRO A CG  
1656  C CD  . PRO A  217 ? 0.1378 0.2341 0.3108 0.0390  0.0339  0.0619  217 PRO A CD  
1657  N N   . SER A  218 ? 0.2651 0.3539 0.4515 0.0382  0.0195  0.0548  218 SER A N   
1658  C CA  . SER A  218 ? 0.2488 0.3355 0.4395 0.0380  0.0157  0.0506  218 SER A CA  
1659  C C   . SER A  218 ? 0.2437 0.3300 0.4306 0.0408  0.0122  0.0491  218 SER A C   
1660  O O   . SER A  218 ? 0.2471 0.3305 0.4380 0.0411  0.0100  0.0475  218 SER A O   
1661  C CB  . SER A  218 ? 0.1768 0.2661 0.3703 0.0373  0.0159  0.0457  218 SER A CB  
1662  O OG  . SER A  218 ? 0.1029 0.1931 0.3030 0.0351  0.0174  0.0467  218 SER A OG  
1663  N N   . ARG A  219 ? 0.2078 0.2972 0.3873 0.0430  0.0116  0.0492  219 ARG A N   
1664  C CA  . ARG A  219 ? 0.2834 0.3747 0.4611 0.0456  0.0071  0.0471  219 ARG A CA  
1665  C C   . ARG A  219 ? 0.3799 0.4675 0.5596 0.0480  0.0043  0.0508  219 ARG A C   
1666  O O   . ARG A  219 ? 0.3913 0.4811 0.5752 0.0500  0.0007  0.0481  219 ARG A O   
1667  C CB  . ARG A  219 ? 0.3436 0.4384 0.5114 0.0476  0.0058  0.0466  219 ARG A CB  
1668  C CG  . ARG A  219 ? 0.3828 0.4813 0.5492 0.0464  0.0062  0.0402  219 ARG A CG  
1669  C CD  . ARG A  219 ? 0.4303 0.5304 0.6051 0.0451  0.0041  0.0346  219 ARG A CD  
1670  N NE  . ARG A  219 ? 0.5059 0.6073 0.6864 0.0467  0.0003  0.0350  219 ARG A NE  
1671  C CZ  . ARG A  219 ? 0.5959 0.7026 0.7778 0.0482  -0.0045 0.0319  219 ARG A CZ  
1672  N NH1 . ARG A  219 ? 0.6145 0.7246 0.7910 0.0477  -0.0063 0.0280  219 ARG A NH1 
1673  N NH2 . ARG A  219 ? 0.6233 0.7320 0.8129 0.0503  -0.0076 0.0323  219 ARG A NH2 
1674  N N   . SER A  220 ? 0.4916 0.5737 0.6693 0.0478  0.0063  0.0570  220 SER A N   
1675  C CA  . SER A  220 ? 0.4398 0.5161 0.6181 0.0505  0.0040  0.0614  220 SER A CA  
1676  C C   . SER A  220 ? 0.4075 0.4796 0.5954 0.0496  0.0039  0.0590  220 SER A C   
1677  O O   . SER A  220 ? 0.4276 0.4945 0.6176 0.0525  0.0019  0.0612  220 SER A O   
1678  C CB  . SER A  220 ? 0.2946 0.3642 0.4668 0.0499  0.0072  0.0693  220 SER A CB  
1679  O OG  . SER A  220 ? 0.2983 0.3714 0.4620 0.0491  0.0104  0.0707  220 SER A OG  
1680  N N   . LEU A  221 ? 0.2900 0.3633 0.4826 0.0459  0.0060  0.0546  221 LEU A N   
1681  C CA  . LEU A  221 ? 0.2411 0.3093 0.4400 0.0447  0.0062  0.0517  221 LEU A CA  
1682  C C   . LEU A  221 ? 0.2635 0.3344 0.4664 0.0460  0.0052  0.0457  221 LEU A C   
1683  O O   . LEU A  221 ? 0.2982 0.3639 0.5047 0.0461  0.0057  0.0435  221 LEU A O   
1684  C CB  . LEU A  221 ? 0.1174 0.1840 0.3182 0.0401  0.0085  0.0508  221 LEU A CB  
1685  C CG  . LEU A  221 ? 0.1235 0.1882 0.3234 0.0380  0.0107  0.0567  221 LEU A CG  
1686  C CD1 . LEU A  221 ? 0.1564 0.2210 0.3616 0.0334  0.0122  0.0556  221 LEU A CD1 
1687  C CD2 . LEU A  221 ? 0.1335 0.1898 0.3331 0.0395  0.0102  0.0612  221 LEU A CD2 
1688  N N   . PHE A  222 ? 0.1113 0.1897 0.3136 0.0469  0.0042  0.0427  222 PHE A N   
1689  C CA  . PHE A  222 ? 0.1067 0.1880 0.3139 0.0470  0.0046  0.0371  222 PHE A CA  
1690  C C   . PHE A  222 ? 0.1961 0.2861 0.4052 0.0490  0.0019  0.0352  222 PHE A C   
1691  O O   . PHE A  222 ? 0.2196 0.3130 0.4233 0.0496  -0.0002 0.0371  222 PHE A O   
1692  C CB  . PHE A  222 ? 0.1015 0.1817 0.3070 0.0433  0.0074  0.0336  222 PHE A CB  
1693  C CG  . PHE A  222 ? 0.1724 0.2571 0.3739 0.0419  0.0076  0.0329  222 PHE A CG  
1694  C CD1 . PHE A  222 ? 0.1739 0.2582 0.3714 0.0410  0.0081  0.0362  222 PHE A CD1 
1695  C CD2 . PHE A  222 ? 0.0966 0.1859 0.2992 0.0412  0.0078  0.0287  222 PHE A CD2 
1696  C CE1 . PHE A  222 ? 0.0991 0.1869 0.2928 0.0404  0.0089  0.0351  222 PHE A CE1 
1697  C CE2 . PHE A  222 ? 0.0962 0.1878 0.2945 0.0400  0.0081  0.0275  222 PHE A CE2 
1698  C CZ  . PHE A  222 ? 0.1690 0.2598 0.3624 0.0401  0.0086  0.0306  222 PHE A CZ  
1699  N N   . HIS A  223 ? 0.1046 0.1982 0.3212 0.0501  0.0019  0.0311  223 HIS A N   
1700  C CA  . HIS A  223 ? 0.1051 0.2079 0.3255 0.0514  -0.0015 0.0284  223 HIS A CA  
1701  C C   . HIS A  223 ? 0.1778 0.2857 0.4014 0.0476  0.0006  0.0225  223 HIS A C   
1702  O O   . HIS A  223 ? 0.1885 0.3049 0.4168 0.0480  -0.0028 0.0199  223 HIS A O   
1703  C CB  . HIS A  223 ? 0.2612 0.3650 0.4868 0.0553  -0.0036 0.0279  223 HIS A CB  
1704  C CG  . HIS A  223 ? 0.2013 0.2969 0.4243 0.0587  -0.0043 0.0336  223 HIS A CG  
1705  N ND1 . HIS A  223 ? 0.1626 0.2487 0.3847 0.0573  -0.0003 0.0341  223 HIS A ND1 
1706  C CD2 . HIS A  223 ? 0.1898 0.2844 0.4113 0.0634  -0.0087 0.0395  223 HIS A CD2 
1707  C CE1 . HIS A  223 ? 0.1571 0.2366 0.3784 0.0605  -0.0018 0.0396  223 HIS A CE1 
1708  N NE2 . HIS A  223 ? 0.1700 0.2539 0.3902 0.0643  -0.0066 0.0434  223 HIS A NE2 
1709  N N   . ARG A  224 ? 0.0971 0.1996 0.3187 0.0441  0.0056  0.0206  224 ARG A N   
1710  C CA  . ARG A  224 ? 0.0947 0.2001 0.3205 0.0406  0.0087  0.0156  224 ARG A CA  
1711  C C   . ARG A  224 ? 0.0995 0.1968 0.3179 0.0375  0.0130  0.0155  224 ARG A C   
1712  O O   . ARG A  224 ? 0.0944 0.1846 0.3079 0.0379  0.0143  0.0179  224 ARG A O   
1713  C CB  . ARG A  224 ? 0.2395 0.3459 0.4719 0.0405  0.0116  0.0124  224 ARG A CB  
1714  C CG  . ARG A  224 ? 0.2754 0.3918 0.5171 0.0393  0.0102  0.0080  224 ARG A CG  
1715  C CD  . ARG A  224 ? 0.3037 0.4234 0.5523 0.0417  0.0107  0.0065  224 ARG A CD  
1716  N NE  . ARG A  224 ? 0.3233 0.4392 0.5679 0.0467  0.0072  0.0107  224 ARG A NE  
1717  C CZ  . ARG A  224 ? 0.3949 0.5147 0.6453 0.0508  0.0047  0.0104  224 ARG A CZ  
1718  N NH1 . ARG A  224 ? 0.4112 0.5404 0.6721 0.0503  0.0051  0.0060  224 ARG A NH1 
1719  N NH2 . ARG A  224 ? 0.4425 0.5570 0.6892 0.0555  0.0020  0.0147  224 ARG A NH2 
1720  N N   . ALA A  225 ? 0.0940 0.1915 0.3114 0.0342  0.0149  0.0123  225 ALA A N   
1721  C CA  . ALA A  225 ? 0.1184 0.2070 0.3272 0.0322  0.0181  0.0129  225 ALA A CA  
1722  C C   . ALA A  225 ? 0.1356 0.2199 0.3445 0.0287  0.0233  0.0097  225 ALA A C   
1723  O O   . ALA A  225 ? 0.1290 0.2185 0.3449 0.0264  0.0243  0.0061  225 ALA A O   
1724  C CB  . ALA A  225 ? 0.2020 0.2904 0.4045 0.0325  0.0158  0.0143  225 ALA A CB  
1725  N N   . VAL A  226 ? 0.2803 0.3549 0.4813 0.0282  0.0265  0.0110  226 VAL A N   
1726  C CA  . VAL A  226 ? 0.2601 0.3274 0.4571 0.0251  0.0319  0.0092  226 VAL A CA  
1727  C C   . VAL A  226 ? 0.2477 0.3057 0.4336 0.0256  0.0314  0.0115  226 VAL A C   
1728  O O   . VAL A  226 ? 0.2681 0.3208 0.4473 0.0277  0.0299  0.0140  226 VAL A O   
1729  C CB  . VAL A  226 ? 0.1136 0.1760 0.3095 0.0245  0.0373  0.0086  226 VAL A CB  
1730  C CG1 . VAL A  226 ? 0.1223 0.1771 0.3140 0.0208  0.0439  0.0073  226 VAL A CG1 
1731  C CG2 . VAL A  226 ? 0.1962 0.2682 0.4045 0.0253  0.0378  0.0066  226 VAL A CG2 
1732  N N   . LEU A  227 ? 0.1200 0.1762 0.3048 0.0239  0.0321  0.0100  227 LEU A N   
1733  C CA  . LEU A  227 ? 0.1205 0.1675 0.2960 0.0249  0.0321  0.0117  227 LEU A CA  
1734  C C   . LEU A  227 ? 0.2120 0.2473 0.3810 0.0222  0.0379  0.0113  227 LEU A C   
1735  O O   . LEU A  227 ? 0.2494 0.2838 0.4223 0.0183  0.0416  0.0084  227 LEU A O   
1736  C CB  . LEU A  227 ? 0.1185 0.1692 0.2956 0.0255  0.0295  0.0104  227 LEU A CB  
1737  C CG  . LEU A  227 ? 0.1107 0.1713 0.2915 0.0282  0.0249  0.0114  227 LEU A CG  
1738  C CD1 . LEU A  227 ? 0.2031 0.2730 0.3915 0.0267  0.0234  0.0088  227 LEU A CD1 
1739  C CD2 . LEU A  227 ? 0.3951 0.4548 0.5724 0.0303  0.0236  0.0115  227 LEU A CD2 
1740  N N   . GLN A  228 ? 0.1826 0.2083 0.3414 0.0239  0.0387  0.0142  228 GLN A N   
1741  C CA  . GLN A  228 ? 0.1661 0.1785 0.3153 0.0219  0.0445  0.0150  228 GLN A CA  
1742  C C   . GLN A  228 ? 0.1639 0.1657 0.3029 0.0248  0.0423  0.0178  228 GLN A C   
1743  O O   . GLN A  228 ? 0.1702 0.1690 0.3023 0.0288  0.0378  0.0205  228 GLN A O   
1744  C CB  . GLN A  228 ? 0.2677 0.2749 0.4094 0.0223  0.0470  0.0164  228 GLN A CB  
1745  C CG  . GLN A  228 ? 0.3089 0.3266 0.4609 0.0213  0.0484  0.0139  228 GLN A CG  
1746  C CD  . GLN A  228 ? 0.3719 0.3823 0.5146 0.0219  0.0521  0.0144  228 GLN A CD  
1747  O OE1 . GLN A  228 ? 0.3764 0.3921 0.5261 0.0209  0.0561  0.0121  228 GLN A OE1 
1748  N NE2 . GLN A  228 ? 0.4149 0.4130 0.5415 0.0241  0.0506  0.0172  228 GLN A NE2 
1749  N N   . SER A  229 ? 0.1760 0.1719 0.3147 0.0228  0.0452  0.0167  229 SER A N   
1750  C CA  . SER A  229 ? 0.2127 0.1957 0.3414 0.0258  0.0444  0.0193  229 SER A CA  
1751  C C   . SER A  229 ? 0.2149 0.2032 0.3452 0.0315  0.0373  0.0205  229 SER A C   
1752  O O   . SER A  229 ? 0.1804 0.1607 0.3022 0.0361  0.0344  0.0238  229 SER A O   
1753  C CB  . SER A  229 ? 0.3011 0.2685 0.4140 0.0268  0.0472  0.0234  229 SER A CB  
1754  O OG  . SER A  229 ? 0.3297 0.2888 0.4398 0.0213  0.0559  0.0228  229 SER A OG  
1755  N N   . GLY A  230 ? 0.1589 0.1609 0.3001 0.0315  0.0347  0.0178  230 GLY A N   
1756  C CA  . GLY A  230 ? 0.1532 0.1615 0.2977 0.0362  0.0298  0.0185  230 GLY A CA  
1757  C C   . GLY A  230 ? 0.1527 0.1740 0.3068 0.0348  0.0290  0.0153  230 GLY A C   
1758  O O   . GLY A  230 ? 0.1559 0.1833 0.3148 0.0311  0.0301  0.0134  230 GLY A O   
1759  N N   . THR A  231 ? 0.2060 0.2316 0.3626 0.0382  0.0271  0.0149  231 THR A N   
1760  C CA  . THR A  231 ? 0.2308 0.2666 0.3929 0.0374  0.0267  0.0120  231 THR A CA  
1761  C C   . THR A  231 ? 0.1896 0.2322 0.3544 0.0421  0.0246  0.0137  231 THR A C   
1762  O O   . THR A  231 ? 0.1504 0.1892 0.3141 0.0459  0.0238  0.0158  231 THR A O   
1763  C CB  . THR A  231 ? 0.4376 0.4677 0.5979 0.0354  0.0293  0.0074  231 THR A CB  
1764  O OG1 . THR A  231 ? 0.4979 0.5151 0.6524 0.0379  0.0310  0.0082  231 THR A OG1 
1765  C CG2 . THR A  231 ? 0.4551 0.4840 0.6175 0.0294  0.0313  0.0047  231 THR A CG2 
1766  N N   . PRO A  232 ? 0.1235 0.1765 0.2920 0.0419  0.0240  0.0130  232 PRO A N   
1767  C CA  . PRO A  232 ? 0.1229 0.1819 0.2940 0.0459  0.0240  0.0145  232 PRO A CA  
1768  C C   . PRO A  232 ? 0.1303 0.1854 0.2986 0.0488  0.0266  0.0114  232 PRO A C   
1769  O O   . PRO A  232 ? 0.1319 0.1889 0.3031 0.0532  0.0275  0.0125  232 PRO A O   
1770  C CB  . PRO A  232 ? 0.1164 0.1853 0.2897 0.0444  0.0234  0.0153  232 PRO A CB  
1771  C CG  . PRO A  232 ? 0.1779 0.2463 0.3500 0.0405  0.0223  0.0132  232 PRO A CG  
1772  C CD  . PRO A  232 ? 0.1202 0.1791 0.2900 0.0386  0.0235  0.0108  232 PRO A CD  
1773  N N   . ASN A  233 ? 0.2537 0.3033 0.4174 0.0465  0.0280  0.0068  233 ASN A N   
1774  C CA  . ASN A  233 ? 0.2672 0.3101 0.4271 0.0491  0.0306  0.0030  233 ASN A CA  
1775  C C   . ASN A  233 ? 0.2988 0.3296 0.4570 0.0509  0.0312  0.0042  233 ASN A C   
1776  O O   . ASN A  233 ? 0.3262 0.3544 0.4848 0.0498  0.0295  0.0078  233 ASN A O   
1777  C CB  . ASN A  233 ? 0.2994 0.3395 0.4547 0.0453  0.0312  -0.0030 233 ASN A CB  
1778  C CG  . ASN A  233 ? 0.2819 0.3184 0.4384 0.0395  0.0301  -0.0040 233 ASN A CG  
1779  O OD1 . ASN A  233 ? 0.2736 0.3162 0.4340 0.0374  0.0282  -0.0009 233 ASN A OD1 
1780  N ND2 . ASN A  233 ? 0.2506 0.2768 0.4043 0.0366  0.0318  -0.0086 233 ASN A ND2 
1781  N N   . GLY A  234 ? 0.3696 0.3913 0.5244 0.0540  0.0336  0.0012  234 GLY A N   
1782  C CA  . GLY A  234 ? 0.3890 0.3974 0.5410 0.0566  0.0340  0.0032  234 GLY A CA  
1783  C C   . GLY A  234 ? 0.3625 0.3735 0.5188 0.0642  0.0326  0.0068  234 GLY A C   
1784  O O   . GLY A  234 ? 0.3411 0.3658 0.5043 0.0660  0.0313  0.0087  234 GLY A O   
1785  N N   . PRO A  235 ? 0.3255 0.3232 0.4782 0.0686  0.0327  0.0081  235 PRO A N   
1786  C CA  . PRO A  235 ? 0.2857 0.2837 0.4430 0.0773  0.0314  0.0103  235 PRO A CA  
1787  C C   . PRO A  235 ? 0.2542 0.2633 0.4189 0.0800  0.0262  0.0154  235 PRO A C   
1788  O O   . PRO A  235 ? 0.2533 0.2718 0.4274 0.0858  0.0255  0.0159  235 PRO A O   
1789  C CB  . PRO A  235 ? 0.2640 0.2417 0.4129 0.0800  0.0319  0.0112  235 PRO A CB  
1790  C CG  . PRO A  235 ? 0.2669 0.2357 0.4075 0.0719  0.0327  0.0119  235 PRO A CG  
1791  C CD  . PRO A  235 ? 0.2746 0.2551 0.4186 0.0650  0.0343  0.0078  235 PRO A CD  
1792  N N   . TRP A  236 ? 0.1793 0.1868 0.3401 0.0759  0.0229  0.0187  236 TRP A N   
1793  C CA  . TRP A  236 ? 0.1751 0.1897 0.3409 0.0787  0.0169  0.0229  236 TRP A CA  
1794  C C   . TRP A  236 ? 0.2077 0.2396 0.3829 0.0753  0.0150  0.0235  236 TRP A C   
1795  O O   . TRP A  236 ? 0.1999 0.2401 0.3831 0.0782  0.0102  0.0259  236 TRP A O   
1796  C CB  . TRP A  236 ? 0.2399 0.2407 0.3940 0.0777  0.0138  0.0264  236 TRP A CB  
1797  C CG  . TRP A  236 ? 0.2310 0.2278 0.3779 0.0696  0.0168  0.0255  236 TRP A CG  
1798  C CD1 . TRP A  236 ? 0.2555 0.2399 0.3944 0.0656  0.0218  0.0236  236 TRP A CD1 
1799  C CD2 . TRP A  236 ? 0.2371 0.2427 0.3859 0.0646  0.0151  0.0261  236 TRP A CD2 
1800  N NE1 . TRP A  236 ? 0.2774 0.2640 0.4144 0.0586  0.0235  0.0229  236 TRP A NE1 
1801  C CE2 . TRP A  236 ? 0.2794 0.2784 0.4217 0.0583  0.0195  0.0245  236 TRP A CE2 
1802  C CE3 . TRP A  236 ? 0.2233 0.2414 0.3794 0.0647  0.0106  0.0275  236 TRP A CE3 
1803  C CZ2 . TRP A  236 ? 0.3098 0.3146 0.4528 0.0532  0.0195  0.0244  236 TRP A CZ2 
1804  C CZ3 . TRP A  236 ? 0.2538 0.2757 0.4091 0.0593  0.0106  0.0274  236 TRP A CZ3 
1805  C CH2 . TRP A  236 ? 0.3034 0.3187 0.4520 0.0541  0.0151  0.0259  236 TRP A CH2 
1806  N N   . ALA A  237 ? 0.1583 0.1956 0.3334 0.0696  0.0184  0.0214  237 ALA A N   
1807  C CA  . ALA A  237 ? 0.2703 0.3196 0.4514 0.0657  0.0165  0.0229  237 ALA A CA  
1808  C C   . ALA A  237 ? 0.3393 0.4036 0.5320 0.0668  0.0181  0.0228  237 ALA A C   
1809  O O   . ALA A  237 ? 0.3929 0.4662 0.5914 0.0639  0.0164  0.0247  237 ALA A O   
1810  C CB  . ALA A  237 ? 0.1352 0.1822 0.3103 0.0592  0.0182  0.0217  237 ALA A CB  
1811  N N   . THR A  238 ? 0.3327 0.3989 0.5283 0.0709  0.0221  0.0207  238 THR A N   
1812  C CA  . THR A  238 ? 0.2724 0.3523 0.4780 0.0720  0.0255  0.0207  238 THR A CA  
1813  C C   . THR A  238 ? 0.2140 0.2961 0.4255 0.0786  0.0270  0.0196  238 THR A C   
1814  O O   . THR A  238 ? 0.2096 0.2816 0.4182 0.0836  0.0265  0.0185  238 THR A O   
1815  C CB  . THR A  238 ? 0.3331 0.4143 0.5323 0.0690  0.0310  0.0181  238 THR A CB  
1816  O OG1 . THR A  238 ? 0.3566 0.4269 0.5442 0.0656  0.0304  0.0158  238 THR A OG1 
1817  C CG2 . THR A  238 ? 0.3014 0.3928 0.5048 0.0647  0.0314  0.0209  238 THR A CG2 
1818  N N   . VAL A  239 ? 0.1371 0.2313 0.3558 0.0784  0.0289  0.0197  239 VAL A N   
1819  C CA  . VAL A  239 ? 0.1494 0.2474 0.3737 0.0843  0.0312  0.0177  239 VAL A CA  
1820  C C   . VAL A  239 ? 0.1928 0.3007 0.4209 0.0841  0.0393  0.0162  239 VAL A C   
1821  O O   . VAL A  239 ? 0.1395 0.2546 0.3691 0.0789  0.0413  0.0181  239 VAL A O   
1822  C CB  . VAL A  239 ? 0.1468 0.2507 0.3796 0.0865  0.0245  0.0193  239 VAL A CB  
1823  C CG1 . VAL A  239 ? 0.1533 0.2453 0.3811 0.0909  0.0181  0.0202  239 VAL A CG1 
1824  C CG2 . VAL A  239 ? 0.1382 0.2512 0.3767 0.0800  0.0209  0.0218  239 VAL A CG2 
1825  N N   . SER A  240 ? 0.2315 0.3384 0.4607 0.0903  0.0441  0.0129  240 SER A N   
1826  C CA  . SER A  240 ? 0.2454 0.3619 0.4792 0.0919  0.0525  0.0111  240 SER A CA  
1827  C C   . SER A  240 ? 0.1932 0.3239 0.4388 0.0882  0.0512  0.0140  240 SER A C   
1828  O O   . SER A  240 ? 0.1979 0.3314 0.4504 0.0879  0.0436  0.0156  240 SER A O   
1829  C CB  . SER A  240 ? 0.5496 0.6629 0.7851 0.1001  0.0555  0.0071  240 SER A CB  
1830  O OG  . SER A  240 ? 0.6318 0.7554 0.8730 0.1022  0.0640  0.0052  240 SER A OG  
1831  N N   . ALA A  241 ? 0.2055 0.3446 0.4534 0.0854  0.0589  0.0148  241 ALA A N   
1832  C CA  . ALA A  241 ? 0.2122 0.3642 0.4727 0.0813  0.0589  0.0175  241 ALA A CA  
1833  C C   . ALA A  241 ? 0.2037 0.3638 0.4772 0.0864  0.0578  0.0154  241 ALA A C   
1834  O O   . ALA A  241 ? 0.2019 0.3697 0.4869 0.0846  0.0517  0.0168  241 ALA A O   
1835  C CB  . ALA A  241 ? 0.2907 0.4486 0.5503 0.0781  0.0691  0.0191  241 ALA A CB  
1836  N N   . GLY A  242 ? 0.1675 0.3256 0.4391 0.0933  0.0635  0.0116  242 GLY A N   
1837  C CA  . GLY A  242 ? 0.1751 0.3401 0.4584 0.0997  0.0626  0.0092  242 GLY A CA  
1838  C C   . GLY A  242 ? 0.1866 0.3465 0.4715 0.1032  0.0511  0.0097  242 GLY A C   
1839  O O   . GLY A  242 ? 0.2255 0.3953 0.5237 0.1056  0.0466  0.0098  242 GLY A O   
1840  N N   . GLU A  243 ? 0.1878 0.3326 0.4594 0.1037  0.0466  0.0100  243 GLU A N   
1841  C CA  . GLU A  243 ? 0.2360 0.3742 0.5067 0.1068  0.0360  0.0113  243 GLU A CA  
1842  C C   . GLU A  243 ? 0.2571 0.4036 0.5354 0.1013  0.0282  0.0146  243 GLU A C   
1843  O O   . GLU A  243 ? 0.2313 0.3845 0.5194 0.1048  0.0216  0.0150  243 GLU A O   
1844  C CB  . GLU A  243 ? 0.2859 0.4057 0.5410 0.1072  0.0339  0.0116  243 GLU A CB  
1845  C CG  . GLU A  243 ? 0.3741 0.4857 0.6264 0.1096  0.0235  0.0141  243 GLU A CG  
1846  C CD  . GLU A  243 ? 0.5127 0.6231 0.7698 0.1194  0.0198  0.0132  243 GLU A CD  
1847  O OE1 . GLU A  243 ? 0.5760 0.6909 0.8387 0.1247  0.0257  0.0099  243 GLU A OE1 
1848  O OE2 . GLU A  243 ? 0.5422 0.6463 0.7966 0.1223  0.0110  0.0158  243 GLU A OE2 
1849  N N   . ALA A  244 ? 0.3781 0.5241 0.6521 0.0932  0.0288  0.0167  244 ALA A N   
1850  C CA  . ALA A  244 ? 0.3386 0.4913 0.6193 0.0872  0.0223  0.0193  244 ALA A CA  
1851  C C   . ALA A  244 ? 0.3079 0.4771 0.6068 0.0876  0.0222  0.0187  244 ALA A C   
1852  O O   . ALA A  244 ? 0.3087 0.4830 0.6156 0.0876  0.0136  0.0194  244 ALA A O   
1853  C CB  . ALA A  244 ? 0.1967 0.3478 0.4719 0.0790  0.0256  0.0213  244 ALA A CB  
1854  N N   . ARG A  245 ? 0.1555 0.3333 0.4611 0.0882  0.0319  0.0173  245 ARG A N   
1855  C CA  . ARG A  245 ? 0.1592 0.3540 0.4839 0.0884  0.0338  0.0166  245 ARG A CA  
1856  C C   . ARG A  245 ? 0.1672 0.3670 0.5012 0.0968  0.0275  0.0147  245 ARG A C   
1857  O O   . ARG A  245 ? 0.1684 0.3804 0.5175 0.0963  0.0216  0.0150  245 ARG A O   
1858  C CB  . ARG A  245 ? 0.2819 0.4829 0.6096 0.0883  0.0470  0.0154  245 ARG A CB  
1859  C CG  . ARG A  245 ? 0.3078 0.5255 0.6548 0.0911  0.0507  0.0137  245 ARG A CG  
1860  C CD  . ARG A  245 ? 0.3410 0.5645 0.6897 0.0888  0.0647  0.0134  245 ARG A CD  
1861  N NE  . ARG A  245 ? 0.3303 0.5536 0.6768 0.0792  0.0679  0.0172  245 ARG A NE  
1862  C CZ  . ARG A  245 ? 0.3253 0.5598 0.6868 0.0726  0.0675  0.0193  245 ARG A CZ  
1863  N NH1 . ARG A  245 ? 0.2686 0.5169 0.6494 0.0744  0.0637  0.0177  245 ARG A NH1 
1864  N NH2 . ARG A  245 ? 0.3598 0.5916 0.7177 0.0644  0.0708  0.0230  245 ARG A NH2 
1865  N N   . ARG A  246 ? 0.2535 0.4435 0.5782 0.1047  0.0286  0.0129  246 ARG A N   
1866  C CA  . ARG A  246 ? 0.3129 0.5031 0.6421 0.1142  0.0225  0.0117  246 ARG A CA  
1867  C C   . ARG A  246 ? 0.3088 0.4971 0.6381 0.1139  0.0093  0.0142  246 ARG A C   
1868  O O   . ARG A  246 ? 0.3358 0.5356 0.6789 0.1175  0.0028  0.0143  246 ARG A O   
1869  C CB  . ARG A  246 ? 0.4728 0.6464 0.7872 0.1212  0.0254  0.0100  246 ARG A CB  
1870  C CG  . ARG A  246 ? 0.5390 0.7106 0.8569 0.1325  0.0209  0.0087  246 ARG A CG  
1871  C CD  . ARG A  246 ? 0.5758 0.7262 0.8765 0.1381  0.0216  0.0078  246 ARG A CD  
1872  N NE  . ARG A  246 ? 0.5684 0.7042 0.8564 0.1369  0.0127  0.0112  246 ARG A NE  
1873  C CZ  . ARG A  246 ? 0.5342 0.6698 0.8240 0.1409  0.0020  0.0140  246 ARG A CZ  
1874  N NH1 . ARG A  246 ? 0.5285 0.6787 0.8335 0.1464  -0.0020 0.0138  246 ARG A NH1 
1875  N NH2 . ARG A  246 ? 0.4984 0.6194 0.7747 0.1396  -0.0046 0.0172  246 ARG A NH2 
1876  N N   . ARG A  247 ? 0.2928 0.4671 0.6069 0.1097  0.0054  0.0163  247 ARG A N   
1877  C CA  . ARG A  247 ? 0.2876 0.4570 0.5979 0.1099  -0.0065 0.0187  247 ARG A CA  
1878  C C   . ARG A  247 ? 0.2732 0.4576 0.5984 0.1038  -0.0117 0.0192  247 ARG A C   
1879  O O   . ARG A  247 ? 0.2550 0.4432 0.5855 0.1065  -0.0220 0.0200  247 ARG A O   
1880  C CB  . ARG A  247 ? 0.1723 0.3240 0.4639 0.1063  -0.0079 0.0205  247 ARG A CB  
1881  C CG  . ARG A  247 ? 0.1797 0.3144 0.4570 0.1127  -0.0057 0.0203  247 ARG A CG  
1882  C CD  . ARG A  247 ? 0.1739 0.2935 0.4355 0.1076  -0.0052 0.0220  247 ARG A CD  
1883  N NE  . ARG A  247 ? 0.1814 0.2837 0.4300 0.1123  -0.0022 0.0218  247 ARG A NE  
1884  C CZ  . ARG A  247 ? 0.1790 0.2672 0.4147 0.1089  -0.0014 0.0232  247 ARG A CZ  
1885  N NH1 . ARG A  247 ? 0.1690 0.2586 0.4026 0.1015  -0.0035 0.0249  247 ARG A NH1 
1886  N NH2 . ARG A  247 ? 0.1875 0.2598 0.4132 0.1129  0.0019  0.0227  247 ARG A NH2 
1887  N N   . ALA A  248 ? 0.2509 0.4433 0.5827 0.0957  -0.0043 0.0188  248 ALA A N   
1888  C CA  . ALA A  248 ? 0.1925 0.3974 0.5385 0.0885  -0.0079 0.0192  248 ALA A CA  
1889  C C   . ALA A  248 ? 0.1681 0.3904 0.5345 0.0924  -0.0102 0.0176  248 ALA A C   
1890  O O   . ALA A  248 ? 0.1712 0.4002 0.5467 0.0920  -0.0204 0.0177  248 ALA A O   
1891  C CB  . ALA A  248 ? 0.1531 0.3606 0.5005 0.0797  0.0015  0.0198  248 ALA A CB  
1892  N N   . THR A  249 ? 0.2580 0.4879 0.6320 0.0962  -0.0010 0.0160  249 THR A N   
1893  C CA  . THR A  249 ? 0.3002 0.5489 0.6962 0.0999  -0.0018 0.0144  249 THR A CA  
1894  C C   . THR A  249 ? 0.3308 0.5787 0.7274 0.1100  -0.0126 0.0143  249 THR A C   
1895  O O   . THR A  249 ? 0.3755 0.6385 0.7900 0.1122  -0.0188 0.0137  249 THR A O   
1896  C CB  . THR A  249 ? 0.2062 0.4629 0.6097 0.1028  0.0112  0.0124  249 THR A CB  
1897  O OG1 . THR A  249 ? 0.2366 0.4795 0.6242 0.1105  0.0148  0.0115  249 THR A OG1 
1898  C CG2 . THR A  249 ? 0.1770 0.4363 0.5816 0.0931  0.0222  0.0132  249 THR A CG2 
1899  N N   . LEU A  250 ? 0.2038 0.4341 0.5812 0.1163  -0.0148 0.0153  250 LEU A N   
1900  C CA  . LEU A  250 ? 0.2155 0.4413 0.5898 0.1259  -0.0257 0.0165  250 LEU A CA  
1901  C C   . LEU A  250 ? 0.2034 0.4292 0.5773 0.1225  -0.0390 0.0184  250 LEU A C   
1902  O O   . LEU A  250 ? 0.2129 0.4479 0.5975 0.1276  -0.0485 0.0188  250 LEU A O   
1903  C CB  . LEU A  250 ? 0.2083 0.4131 0.5615 0.1328  -0.0243 0.0174  250 LEU A CB  
1904  C CG  . LEU A  250 ? 0.2209 0.4157 0.5655 0.1416  -0.0360 0.0203  250 LEU A CG  
1905  C CD1 . LEU A  250 ? 0.2339 0.4424 0.5947 0.1513  -0.0406 0.0201  250 LEU A CD1 
1906  C CD2 . LEU A  250 ? 0.5685 0.7404 0.8917 0.1469  -0.0333 0.0214  250 LEU A CD2 
1907  N N   . LEU A  251 ? 0.1943 0.4097 0.5559 0.1143  -0.0401 0.0195  251 LEU A N   
1908  C CA  . LEU A  251 ? 0.1953 0.4100 0.5560 0.1105  -0.0523 0.0205  251 LEU A CA  
1909  C C   . LEU A  251 ? 0.1954 0.4310 0.5799 0.1057  -0.0559 0.0186  251 LEU A C   
1910  O O   . LEU A  251 ? 0.2796 0.5207 0.6704 0.1074  -0.0681 0.0185  251 LEU A O   
1911  C CB  . LEU A  251 ? 0.2005 0.4022 0.5466 0.1020  -0.0512 0.0214  251 LEU A CB  
1912  C CG  . LEU A  251 ? 0.2502 0.4490 0.5931 0.0988  -0.0641 0.0219  251 LEU A CG  
1913  C CD1 . LEU A  251 ? 0.2478 0.4260 0.5677 0.0985  -0.0652 0.0241  251 LEU A CD1 
1914  C CD2 . LEU A  251 ? 0.1962 0.4065 0.5535 0.0881  -0.0646 0.0199  251 LEU A CD2 
1915  N N   . ALA A  252 ? 0.2656 0.5119 0.6627 0.0994  -0.0452 0.0170  252 ALA A N   
1916  C CA  . ALA A  252 ? 0.2730 0.5398 0.6950 0.0945  -0.0459 0.0151  252 ALA A CA  
1917  C C   . ALA A  252 ? 0.2794 0.5600 0.7167 0.1037  -0.0529 0.0143  252 ALA A C   
1918  O O   . ALA A  252 ? 0.2716 0.5629 0.7222 0.1022  -0.0636 0.0133  252 ALA A O   
1919  C CB  . ALA A  252 ? 0.3475 0.6218 0.7783 0.0890  -0.0309 0.0143  252 ALA A CB  
1920  N N   . ARG A  253 ? 0.2133 0.4930 0.6486 0.1135  -0.0472 0.0145  253 ARG A N   
1921  C CA  . ARG A  253 ? 0.2552 0.5461 0.7034 0.1241  -0.0535 0.0143  253 ARG A CA  
1922  C C   . ARG A  253 ? 0.2390 0.5232 0.6792 0.1288  -0.0699 0.0164  253 ARG A C   
1923  O O   . ARG A  253 ? 0.2405 0.5390 0.6971 0.1317  -0.0797 0.0159  253 ARG A O   
1924  C CB  . ARG A  253 ? 0.6505 0.9361 1.0929 0.1347  -0.0450 0.0143  253 ARG A CB  
1925  C CG  . ARG A  253 ? 0.7753 1.0794 1.2390 0.1361  -0.0340 0.0117  253 ARG A CG  
1926  C CD  . ARG A  253 ? 0.8976 1.2059 1.3674 0.1505  -0.0349 0.0115  253 ARG A CD  
1927  N NE  . ARG A  253 ? 0.9985 1.3207 1.4848 0.1558  -0.0479 0.0124  253 ARG A NE  
1928  C CZ  . ARG A  253 ? 1.0458 1.3588 1.5225 0.1652  -0.0597 0.0154  253 ARG A CZ  
1929  N NH1 . ARG A  253 ? 1.0638 1.3530 1.5145 0.1702  -0.0596 0.0178  253 ARG A NH1 
1930  N NH2 . ARG A  253 ? 1.0372 1.3647 1.5304 0.1694  -0.0717 0.0162  253 ARG A NH2 
1931  N N   . LEU A  254 ? 0.4615 0.7240 0.8766 0.1292  -0.0730 0.0187  254 LEU A N   
1932  C CA  . LEU A  254 ? 0.4921 0.7447 0.8951 0.1344  -0.0877 0.0212  254 LEU A CA  
1933  C C   . LEU A  254 ? 0.5111 0.7720 0.9225 0.1274  -0.1001 0.0198  254 LEU A C   
1934  O O   . LEU A  254 ? 0.5726 0.8350 0.9843 0.1329  -0.1136 0.0209  254 LEU A O   
1935  C CB  . LEU A  254 ? 0.3973 0.6241 0.7712 0.1355  -0.0867 0.0241  254 LEU A CB  
1936  C CG  . LEU A  254 ? 0.2438 0.4597 0.6077 0.1452  -0.0786 0.0257  254 LEU A CG  
1937  C CD1 . LEU A  254 ? 0.2479 0.4387 0.5850 0.1478  -0.0805 0.0290  254 LEU A CD1 
1938  C CD2 . LEU A  254 ? 0.5890 0.8149 0.9653 0.1566  -0.0837 0.0267  254 LEU A CD2 
1939  N N   . VAL A  255 ? 0.2329 0.4982 0.6503 0.1153  -0.0960 0.0173  255 VAL A N   
1940  C CA  . VAL A  255 ? 0.2316 0.5033 0.6567 0.1076  -0.1074 0.0151  255 VAL A CA  
1941  C C   . VAL A  255 ? 0.3017 0.5983 0.7573 0.1050  -0.1086 0.0121  255 VAL A C   
1942  O O   . VAL A  255 ? 0.3273 0.6324 0.7945 0.0968  -0.1159 0.0093  255 VAL A O   
1943  C CB  . VAL A  255 ? 0.3551 0.6177 0.7719 0.0960  -0.1035 0.0141  255 VAL A CB  
1944  C CG1 . VAL A  255 ? 0.3641 0.6031 0.7523 0.0984  -0.1028 0.0169  255 VAL A CG1 
1945  C CG2 . VAL A  255 ? 0.3889 0.6600 0.8182 0.0889  -0.0880 0.0131  255 VAL A CG2 
1946  N N   . GLY A  256 ? 0.4882 0.7965 0.9571 0.1116  -0.1008 0.0124  256 GLY A N   
1947  C CA  . GLY A  256 ? 0.5390 0.8723 1.0383 0.1108  -0.1017 0.0099  256 GLY A CA  
1948  C C   . GLY A  256 ? 0.5621 0.9050 1.0760 0.0987  -0.0901 0.0076  256 GLY A C   
1949  O O   . GLY A  256 ? 0.5355 0.8954 1.0722 0.0920  -0.0934 0.0049  256 GLY A O   
1950  N N   . CYS A  257 ? 0.6991 1.0305 1.1996 0.0960  -0.0763 0.0089  257 CYS A N   
1951  C CA  . CYS A  257 ? 0.7349 1.0719 1.2452 0.0848  -0.0645 0.0078  257 CYS A CA  
1952  C C   . CYS A  257 ? 0.8131 1.1544 1.3270 0.0880  -0.0483 0.0083  257 CYS A C   
1953  O O   . CYS A  257 ? 0.8068 1.1371 1.3076 0.0837  -0.0370 0.0095  257 CYS A O   
1954  C CB  . CYS A  257 ? 0.5827 0.9005 1.0722 0.0767  -0.0631 0.0090  257 CYS A CB  
1955  S SG  . CYS A  257 ? 1.0935 1.4178 1.5975 0.0616  -0.0655 0.0069  257 CYS A SG  
1956  N N   . PRO A  258 ? 0.7930 1.1501 1.3241 0.0962  -0.0471 0.0073  258 PRO A N   
1957  C CA  . PRO A  258 ? 0.8387 1.2060 1.3820 0.0936  -0.0309 0.0065  258 PRO A CA  
1958  C C   . PRO A  258 ? 0.8679 1.2502 1.4334 0.0811  -0.0277 0.0053  258 PRO A C   
1959  O O   . PRO A  258 ? 0.8271 1.2051 1.3887 0.0735  -0.0152 0.0062  258 PRO A O   
1960  C CB  . PRO A  258 ? 1.0145 1.3945 1.5707 0.1061  -0.0299 0.0056  258 PRO A CB  
1961  C CG  . PRO A  258 ? 1.0046 1.3717 1.5441 0.1165  -0.0424 0.0071  258 PRO A CG  
1962  C CD  . PRO A  258 ? 0.9819 1.3422 1.5146 0.1096  -0.0558 0.0077  258 PRO A CD  
1963  N N   . PRO A  259 ? 1.1649 1.5630 1.7518 0.0788  -0.0392 0.0033  259 PRO A N   
1964  C CA  . PRO A  259 ? 1.2096 1.6181 1.8074 0.0873  -0.0543 0.0022  259 PRO A CA  
1965  C C   . PRO A  259 ? 1.2969 1.7254 1.9166 0.0969  -0.0501 0.0012  259 PRO A C   
1966  O O   . PRO A  259 ? 1.3118 1.7563 1.9522 0.0924  -0.0387 -0.0001 259 PRO A O   
1967  C CB  . PRO A  259 ? 0.7743 1.1930 1.3890 0.0771  -0.0649 -0.0002 259 PRO A CB  
1968  C CG  . PRO A  259 ? 0.7490 1.1740 1.3760 0.0652  -0.0513 -0.0006 259 PRO A CG  
1969  C CD  . PRO A  259 ? 0.7604 1.1671 1.3636 0.0650  -0.0371 0.0022  259 PRO A CD  
1970  N N   . GLY A  260 ? 1.1659 1.5935 1.7815 0.1100  -0.0590 0.0019  260 GLY A N   
1971  C CA  . GLY A  260 ? 1.2096 1.6570 1.8477 0.1201  -0.0579 0.0010  260 GLY A CA  
1972  C C   . GLY A  260 ? 1.2292 1.6746 1.8629 0.1301  -0.0442 0.0014  260 GLY A C   
1973  O O   . GLY A  260 ? 1.2001 1.6634 1.8548 0.1385  -0.0425 0.0003  260 GLY A O   
1974  N N   . GLY A  261 ? 1.3648 1.7886 1.9717 0.1299  -0.0353 0.0027  261 GLY A N   
1975  C CA  . GLY A  261 ? 1.3762 1.7957 1.9765 0.1378  -0.0214 0.0022  261 GLY A CA  
1976  C C   . GLY A  261 ? 1.3691 1.7875 1.9675 0.1292  -0.0036 0.0012  261 GLY A C   
1977  O O   . GLY A  261 ? 1.3669 1.7819 1.9597 0.1351  0.0084  0.0001  261 GLY A O   
1978  N N   . ALA A  262 ? 1.3098 1.7303 1.9122 0.1154  -0.0022 0.0016  262 ALA A N   
1979  C CA  . ALA A  262 ? 1.2930 1.7092 1.8903 0.1054  0.0131  0.0019  262 ALA A CA  
1980  C C   . ALA A  262 ? 1.3133 1.7030 1.8780 0.1022  0.0140  0.0040  262 ALA A C   
1981  O O   . ALA A  262 ? 1.3226 1.6971 1.8681 0.1102  0.0072  0.0046  262 ALA A O   
1982  C CB  . ALA A  262 ? 1.1118 1.5429 1.7305 0.0925  0.0143  0.0017  262 ALA A CB  
1983  N N   . GLY A  263 ? 1.3224 1.7063 1.8811 0.0910  0.0227  0.0053  263 GLY A N   
1984  C CA  . GLY A  263 ? 1.2802 1.6409 1.8103 0.0876  0.0244  0.0073  263 GLY A CA  
1985  C C   . GLY A  263 ? 1.2507 1.6020 1.7665 0.0860  0.0402  0.0081  263 GLY A C   
1986  O O   . GLY A  263 ? 1.2299 1.5619 1.7214 0.0859  0.0405  0.0094  263 GLY A O   
1987  N N   . GLY A  264 ? 1.2986 1.6635 1.8293 0.0847  0.0533  0.0073  264 GLY A N   
1988  C CA  . GLY A  264 ? 1.2550 1.6126 1.7736 0.0813  0.0690  0.0084  264 GLY A CA  
1989  C C   . GLY A  264 ? 1.1881 1.5368 1.6979 0.0690  0.0728  0.0121  264 GLY A C   
1990  O O   . GLY A  264 ? 1.1755 1.5074 1.6626 0.0678  0.0775  0.0139  264 GLY A O   
1991  N N   . ASN A  265 ? 1.0154 1.3752 1.5436 0.0600  0.0709  0.0132  265 ASN A N   
1992  C CA  . ASN A  265 ? 0.9315 1.2829 1.4535 0.0483  0.0740  0.0168  265 ASN A CA  
1993  C C   . ASN A  265 ? 0.8378 1.1719 1.3415 0.0468  0.0614  0.0179  265 ASN A C   
1994  O O   . ASN A  265 ? 0.8496 1.1861 1.3591 0.0483  0.0474  0.0162  265 ASN A O   
1995  C CB  . ASN A  265 ? 0.8097 1.1778 1.3585 0.0393  0.0745  0.0170  265 ASN A CB  
1996  C CG  . ASN A  265 ? 0.8481 1.2084 1.3929 0.0271  0.0810  0.0211  265 ASN A CG  
1997  O OD1 . ASN A  265 ? 0.8154 1.1642 1.3515 0.0220  0.0722  0.0225  265 ASN A OD1 
1998  N ND2 . ASN A  265 ? 0.9349 1.3011 1.4861 0.0227  0.0970  0.0233  265 ASN A ND2 
1999  N N   . ASP A  266 ? 0.5504 0.8674 1.0319 0.0441  0.0664  0.0208  266 ASP A N   
2000  C CA  . ASP A  266 ? 0.4076 0.7082 0.8717 0.0422  0.0560  0.0221  266 ASP A CA  
2001  C C   . ASP A  266 ? 0.2990 0.6019 0.7743 0.0333  0.0474  0.0228  266 ASP A C   
2002  O O   . ASP A  266 ? 0.2525 0.5562 0.7309 0.0353  0.0338  0.0206  266 ASP A O   
2003  C CB  . ASP A  266 ? 0.4930 0.7770 0.9341 0.0404  0.0640  0.0254  266 ASP A CB  
2004  C CG  . ASP A  266 ? 0.4786 0.7516 0.9002 0.0496  0.0631  0.0239  266 ASP A CG  
2005  O OD1 . ASP A  266 ? 0.4873 0.7669 0.9139 0.0579  0.0628  0.0207  266 ASP A OD1 
2006  O OD2 . ASP A  266 ? 0.4477 0.7055 0.8497 0.0486  0.0628  0.0259  266 ASP A OD2 
2007  N N   . THR A  267 ? 0.3812 0.6846 0.8620 0.0237  0.0554  0.0257  267 THR A N   
2008  C CA  . THR A  267 ? 0.3488 0.6513 0.8384 0.0143  0.0487  0.0264  267 THR A CA  
2009  C C   . THR A  267 ? 0.3517 0.6679 0.8613 0.0148  0.0363  0.0223  267 THR A C   
2010  O O   . THR A  267 ? 0.3377 0.6489 0.8466 0.0117  0.0242  0.0211  267 THR A O   
2011  C CB  . THR A  267 ? 0.2871 0.5941 0.7883 0.0043  0.0607  0.0297  267 THR A CB  
2012  O OG1 . THR A  267 ? 0.3148 0.6246 0.8125 0.0070  0.0760  0.0317  267 THR A OG1 
2013  C CG2 . THR A  267 ? 0.2596 0.5506 0.7490 -0.0035 0.0604  0.0335  267 THR A CG2 
2014  N N   . GLU A  268 ? 0.3339 0.6674 0.8610 0.0191  0.0394  0.0201  268 GLU A N   
2015  C CA  . GLU A  268 ? 0.3953 0.7445 0.9430 0.0213  0.0281  0.0162  268 GLU A CA  
2016  C C   . GLU A  268 ? 0.3249 0.6669 0.8602 0.0298  0.0131  0.0142  268 GLU A C   
2017  O O   . GLU A  268 ? 0.2824 0.6286 0.8263 0.0286  -0.0006 0.0118  268 GLU A O   
2018  C CB  . GLU A  268 ? 0.9607 1.3289 1.5272 0.0260  0.0367  0.0147  268 GLU A CB  
2019  C CG  . GLU A  268 ? 1.1099 1.4917 1.6899 0.0349  0.0256  0.0111  268 GLU A CG  
2020  C CD  . GLU A  268 ? 1.2173 1.6173 1.8256 0.0289  0.0180  0.0087  268 GLU A CD  
2021  O OE1 . GLU A  268 ? 1.2406 1.6367 1.8521 0.0182  0.0153  0.0091  268 GLU A OE1 
2022  O OE2 . GLU A  268 ? 1.2516 1.6698 1.8794 0.0350  0.0148  0.0061  268 GLU A OE2 
2023  N N   . LEU A  269 ? 0.3373 0.6677 0.8518 0.0382  0.0159  0.0151  269 LEU A N   
2024  C CA  . LEU A  269 ? 0.3041 0.6257 0.8044 0.0470  0.0037  0.0139  269 LEU A CA  
2025  C C   . LEU A  269 ? 0.2641 0.5692 0.7478 0.0428  -0.0053 0.0149  269 LEU A C   
2026  O O   . LEU A  269 ? 0.1713 0.4747 0.6534 0.0455  -0.0190 0.0134  269 LEU A O   
2027  C CB  . LEU A  269 ? 0.1974 0.5110 0.6814 0.0567  0.0104  0.0144  269 LEU A CB  
2028  C CG  . LEU A  269 ? 0.1739 0.4748 0.6399 0.0655  0.0001  0.0141  269 LEU A CG  
2029  C CD1 . LEU A  269 ? 0.3655 0.6703 0.8320 0.0769  0.0029  0.0127  269 LEU A CD1 
2030  C CD2 . LEU A  269 ? 0.1657 0.4460 0.6063 0.0634  0.0024  0.0162  269 LEU A CD2 
2031  N N   . ILE A  270 ? 0.2767 0.5695 0.7473 0.0367  0.0023  0.0176  270 ILE A N   
2032  C CA  . ILE A  270 ? 0.2475 0.5255 0.7043 0.0322  -0.0051 0.0184  270 ILE A CA  
2033  C C   . ILE A  270 ? 0.2318 0.5176 0.7058 0.0246  -0.0139 0.0164  270 ILE A C   
2034  O O   . ILE A  270 ? 0.2244 0.5053 0.6942 0.0252  -0.0269 0.0146  270 ILE A O   
2035  C CB  . ILE A  270 ? 0.2603 0.5254 0.7027 0.0270  0.0054  0.0220  270 ILE A CB  
2036  C CG1 . ILE A  270 ? 0.2457 0.5029 0.6706 0.0344  0.0130  0.0233  270 ILE A CG1 
2037  C CG2 . ILE A  270 ? 0.2521 0.5033 0.6832 0.0220  -0.0021 0.0228  270 ILE A CG2 
2038  C CD1 . ILE A  270 ? 0.2594 0.5204 0.6867 0.0322  0.0284  0.0255  270 ILE A CD1 
2039  N N   . ALA A  271 ? 0.2531 0.5508 0.7465 0.0175  -0.0069 0.0165  271 ALA A N   
2040  C CA  . ALA A  271 ? 0.3178 0.6229 0.8290 0.0093  -0.0149 0.0141  271 ALA A CA  
2041  C C   . ALA A  271 ? 0.3269 0.6427 0.8488 0.0144  -0.0299 0.0100  271 ALA A C   
2042  O O   . ALA A  271 ? 0.3373 0.6521 0.8634 0.0098  -0.0419 0.0073  271 ALA A O   
2043  C CB  . ALA A  271 ? 0.4732 0.7904 1.0049 0.0010  -0.0039 0.0150  271 ALA A CB  
2044  N N   . CYS A  272 ? 0.3905 0.7156 0.9158 0.0241  -0.0300 0.0094  272 CYS A N   
2045  C CA  . CYS A  272 ? 0.4470 0.7790 0.9777 0.0305  -0.0454 0.0064  272 CYS A CA  
2046  C C   . CYS A  272 ? 0.4561 0.7695 0.9617 0.0351  -0.0561 0.0068  272 CYS A C   
2047  O O   . CYS A  272 ? 0.4680 0.7801 0.9740 0.0339  -0.0703 0.0043  272 CYS A O   
2048  C CB  . CYS A  272 ? 0.4449 0.7917 0.9870 0.0405  -0.0432 0.0059  272 CYS A CB  
2049  S SG  . CYS A  272 ? 0.9307 1.2830 1.4746 0.0513  -0.0623 0.0037  272 CYS A SG  
2050  N N   . LEU A  273 ? 0.3899 0.6889 0.8736 0.0403  -0.0493 0.0096  273 LEU A N   
2051  C CA  . LEU A  273 ? 0.3805 0.6614 0.8401 0.0445  -0.0572 0.0105  273 LEU A CA  
2052  C C   . LEU A  273 ? 0.3768 0.6486 0.8318 0.0360  -0.0648 0.0093  273 LEU A C   
2053  O O   . LEU A  273 ? 0.3703 0.6328 0.8130 0.0387  -0.0768 0.0083  273 LEU A O   
2054  C CB  . LEU A  273 ? 0.2493 0.5162 0.6885 0.0478  -0.0460 0.0136  273 LEU A CB  
2055  C CG  . LEU A  273 ? 0.2257 0.4836 0.6480 0.0589  -0.0472 0.0148  273 LEU A CG  
2056  C CD1 . LEU A  273 ? 0.1599 0.4089 0.5693 0.0597  -0.0334 0.0169  273 LEU A CD1 
2057  C CD2 . LEU A  273 ? 0.1967 0.4403 0.6017 0.0614  -0.0593 0.0150  273 LEU A CD2 
2058  N N   . ARG A  274 ? 0.3938 0.6676 0.8583 0.0260  -0.0574 0.0095  274 ARG A N   
2059  C CA  . ARG A  274 ? 0.3703 0.6343 0.8308 0.0175  -0.0626 0.0084  274 ARG A CA  
2060  C C   . ARG A  274 ? 0.3266 0.5980 0.7998 0.0146  -0.0777 0.0037  274 ARG A C   
2061  O O   . ARG A  274 ? 0.3370 0.5991 0.8048 0.0092  -0.0855 0.0016  274 ARG A O   
2062  C CB  . ARG A  274 ? 0.3865 0.6498 0.8542 0.0079  -0.0501 0.0104  274 ARG A CB  
2063  C CG  . ARG A  274 ? 0.4067 0.6534 0.8537 0.0079  -0.0414 0.0144  274 ARG A CG  
2064  C CD  . ARG A  274 ? 0.4514 0.6934 0.9031 -0.0023 -0.0343 0.0161  274 ARG A CD  
2065  N NE  . ARG A  274 ? 0.4750 0.7282 0.9420 -0.0063 -0.0221 0.0181  274 ARG A NE  
2066  C CZ  . ARG A  274 ? 0.4936 0.7427 0.9535 -0.0064 -0.0083 0.0226  274 ARG A CZ  
2067  N NH1 . ARG A  274 ? 0.4500 0.6846 0.8884 -0.0029 -0.0052 0.0254  274 ARG A NH1 
2068  N NH2 . ARG A  274 ? 0.5417 0.8014 1.0159 -0.0101 0.0024  0.0242  274 ARG A NH2 
2069  N N   . THR A  275 ? 0.2291 0.5175 0.7194 0.0182  -0.0820 0.0018  275 THR A N   
2070  C CA  . THR A  275 ? 0.2258 0.5225 0.7279 0.0166  -0.0978 -0.0029 275 THR A CA  
2071  C C   . THR A  275 ? 0.2325 0.5208 0.7171 0.0256  -0.1126 -0.0039 275 THR A C   
2072  O O   . THR A  275 ? 0.2440 0.5287 0.7261 0.0229  -0.1265 -0.0077 275 THR A O   
2073  C CB  . THR A  275 ? 0.2754 0.5954 0.8059 0.0160  -0.0975 -0.0048 275 THR A CB  
2074  O OG1 . THR A  275 ? 0.2984 0.6256 0.8281 0.0280  -0.0996 -0.0036 275 THR A OG1 
2075  C CG2 . THR A  275 ? 0.2506 0.5780 0.7956 0.0090  -0.0804 -0.0027 275 THR A CG2 
2076  N N   . ARG A  276 ? 0.2628 0.5470 0.7344 0.0363  -0.1096 -0.0005 276 ARG A N   
2077  C CA  . ARG A  276 ? 0.2798 0.5549 0.7337 0.0453  -0.1229 -0.0005 276 ARG A CA  
2078  C C   . ARG A  276 ? 0.2790 0.5344 0.7111 0.0420  -0.1292 -0.0013 276 ARG A C   
2079  O O   . ARG A  276 ? 0.2683 0.5131 0.6915 0.0375  -0.1191 0.0006  276 ARG A O   
2080  C CB  . ARG A  276 ? 0.2668 0.5381 0.7093 0.0567  -0.1169 0.0036  276 ARG A CB  
2081  C CG  . ARG A  276 ? 0.3327 0.6226 0.7952 0.0617  -0.1114 0.0040  276 ARG A CG  
2082  C CD  . ARG A  276 ? 0.4513 0.7547 0.9272 0.0668  -0.1261 0.0017  276 ARG A CD  
2083  N NE  . ARG A  276 ? 0.5569 0.8802 1.0555 0.0711  -0.1201 0.0019  276 ARG A NE  
2084  C CZ  . ARG A  276 ? 0.6309 0.9740 1.1572 0.0645  -0.1180 -0.0009 276 ARG A CZ  
2085  N NH1 . ARG A  276 ? 0.6493 0.9946 1.1844 0.0530  -0.1218 -0.0042 276 ARG A NH1 
2086  N NH2 . ARG A  276 ? 0.6477 1.0083 1.1936 0.0694  -0.1120 -0.0007 276 ARG A NH2 
2087  N N   . PRO A  277 ? 0.2867 0.5370 0.7097 0.0447  -0.1459 -0.0040 277 PRO A N   
2088  C CA  . PRO A  277 ? 0.3021 0.5336 0.7028 0.0431  -0.1541 -0.0054 277 PRO A CA  
2089  C C   . PRO A  277 ? 0.3680 0.5827 0.7451 0.0492  -0.1466 -0.0005 277 PRO A C   
2090  O O   . PRO A  277 ? 0.4232 0.6381 0.7950 0.0584  -0.1435 0.0031  277 PRO A O   
2091  C CB  . PRO A  277 ? 0.2488 0.4798 0.6421 0.0489  -0.1729 -0.0081 277 PRO A CB  
2092  C CG  . PRO A  277 ? 0.2549 0.5075 0.6730 0.0505  -0.1755 -0.0093 277 PRO A CG  
2093  C CD  . PRO A  277 ? 0.2401 0.5022 0.6714 0.0516  -0.1582 -0.0054 277 PRO A CD  
2094  N N   . ALA A  278 ? 0.3738 0.5741 0.7376 0.0444  -0.1440 -0.0007 278 ALA A N   
2095  C CA  . ALA A  278 ? 0.3228 0.5084 0.6672 0.0487  -0.1350 0.0039  278 ALA A CA  
2096  C C   . ALA A  278 ? 0.3299 0.5061 0.6551 0.0602  -0.1407 0.0069  278 ALA A C   
2097  O O   . ALA A  278 ? 0.3531 0.5263 0.6726 0.0661  -0.1310 0.0111  278 ALA A O   
2098  C CB  . ALA A  278 ? 0.2126 0.3842 0.5452 0.0430  -0.1360 0.0024  278 ALA A CB  
2099  N N   . GLN A  279 ? 0.2628 0.4335 0.5770 0.0635  -0.1567 0.0045  279 GLN A N   
2100  C CA  . GLN A  279 ? 0.2921 0.4510 0.5849 0.0744  -0.1631 0.0080  279 GLN A CA  
2101  C C   . GLN A  279 ? 0.3155 0.4839 0.6169 0.0826  -0.1590 0.0115  279 GLN A C   
2102  O O   . GLN A  279 ? 0.3590 0.5154 0.6431 0.0913  -0.1581 0.0159  279 GLN A O   
2103  C CB  . GLN A  279 ? 0.3721 0.5228 0.6493 0.0764  -0.1818 0.0047  279 GLN A CB  
2104  C CG  . GLN A  279 ? 0.4348 0.5672 0.6825 0.0872  -0.1881 0.0090  279 GLN A CG  
2105  C CD  . GLN A  279 ? 0.5133 0.6253 0.7381 0.0882  -0.1807 0.0123  279 GLN A CD  
2106  O OE1 . GLN A  279 ? 0.5272 0.6328 0.7473 0.0817  -0.1803 0.0094  279 GLN A OE1 
2107  N NE2 . GLN A  279 ? 0.5535 0.6547 0.7643 0.0965  -0.1745 0.0183  279 GLN A NE2 
2108  N N   . ASP A  280 ? 0.2916 0.4805 0.6193 0.0801  -0.1560 0.0097  280 ASP A N   
2109  C CA  . ASP A  280 ? 0.3441 0.5429 0.6814 0.0882  -0.1513 0.0126  280 ASP A CA  
2110  C C   . ASP A  280 ? 0.2525 0.4457 0.5853 0.0903  -0.1345 0.0163  280 ASP A C   
2111  O O   . ASP A  280 ? 0.2360 0.4234 0.5601 0.0995  -0.1316 0.0199  280 ASP A O   
2112  C CB  . ASP A  280 ? 0.7026 0.9252 1.0699 0.0848  -0.1516 0.0094  280 ASP A CB  
2113  C CG  . ASP A  280 ? 0.8943 1.1244 1.2670 0.0867  -0.1692 0.0064  280 ASP A CG  
2114  O OD1 . ASP A  280 ? 0.9752 1.1917 1.3264 0.0931  -0.1809 0.0077  280 ASP A OD1 
2115  O OD2 . ASP A  280 ? 0.9450 1.1942 1.3428 0.0817  -0.1714 0.0028  280 ASP A OD2 
2116  N N   . LEU A  281 ? 0.2149 0.4091 0.5530 0.0814  -0.1237 0.0152  281 LEU A N   
2117  C CA  . LEU A  281 ? 0.2020 0.3895 0.5336 0.0817  -0.1086 0.0180  281 LEU A CA  
2118  C C   . LEU A  281 ? 0.2060 0.3724 0.5116 0.0872  -0.1096 0.0212  281 LEU A C   
2119  O O   . LEU A  281 ? 0.2049 0.3645 0.5023 0.0931  -0.1018 0.0240  281 LEU A O   
2120  C CB  . LEU A  281 ? 0.1876 0.3775 0.5263 0.0709  -0.0996 0.0165  281 LEU A CB  
2121  C CG  . LEU A  281 ? 0.1803 0.3866 0.5399 0.0670  -0.0891 0.0157  281 LEU A CG  
2122  C CD1 . LEU A  281 ? 0.1892 0.4129 0.5695 0.0669  -0.0973 0.0130  281 LEU A CD1 
2123  C CD2 . LEU A  281 ? 0.2379 0.4426 0.6005 0.0567  -0.0812 0.0153  281 LEU A CD2 
2124  N N   . VAL A  282 ? 0.2613 0.4165 0.5535 0.0851  -0.1193 0.0204  282 VAL A N   
2125  C CA  . VAL A  282 ? 0.2709 0.4050 0.5375 0.0902  -0.1204 0.0237  282 VAL A CA  
2126  C C   . VAL A  282 ? 0.2911 0.4181 0.5464 0.1014  -0.1258 0.0271  282 VAL A C   
2127  O O   . VAL A  282 ? 0.3128 0.4259 0.5536 0.1066  -0.1195 0.0308  282 VAL A O   
2128  C CB  . VAL A  282 ? 0.2255 0.3482 0.4782 0.0867  -0.1306 0.0219  282 VAL A CB  
2129  C CG1 . VAL A  282 ? 0.2537 0.3539 0.4782 0.0936  -0.1335 0.0257  282 VAL A CG1 
2130  C CG2 . VAL A  282 ? 0.2090 0.3335 0.4689 0.0769  -0.1228 0.0199  282 VAL A CG2 
2131  N N   . ASP A  283 ? 0.2639 0.4005 0.5267 0.1049  -0.1373 0.0258  283 ASP A N   
2132  C CA  . ASP A  283 ? 0.3064 0.4377 0.5605 0.1159  -0.1434 0.0294  283 ASP A CA  
2133  C C   . ASP A  283 ? 0.2826 0.4184 0.5453 0.1213  -0.1314 0.0318  283 ASP A C   
2134  O O   . ASP A  283 ? 0.3087 0.4326 0.5584 0.1304  -0.1316 0.0360  283 ASP A O   
2135  C CB  . ASP A  283 ? 0.4652 0.6097 0.7301 0.1181  -0.1578 0.0271  283 ASP A CB  
2136  C CG  . ASP A  283 ? 0.5396 0.6778 0.7928 0.1139  -0.1719 0.0240  283 ASP A CG  
2137  O OD1 . ASP A  283 ? 0.5596 0.6782 0.7888 0.1130  -0.1727 0.0251  283 ASP A OD1 
2138  O OD2 . ASP A  283 ? 0.5425 0.6953 0.8103 0.1116  -0.1823 0.0200  283 ASP A OD2 
2139  N N   . HIS A  284 ? 0.2438 0.3957 0.5273 0.1159  -0.1209 0.0291  284 HIS A N   
2140  C CA  . HIS A  284 ? 0.2403 0.3960 0.5305 0.1214  -0.1099 0.0305  284 HIS A CA  
2141  C C   . HIS A  284 ? 0.2280 0.3732 0.5094 0.1195  -0.0955 0.0313  284 HIS A C   
2142  O O   . HIS A  284 ? 0.2279 0.3740 0.5123 0.1247  -0.0873 0.0318  284 HIS A O   
2143  C CB  . HIS A  284 ? 0.3738 0.5535 0.6912 0.1198  -0.1075 0.0273  284 HIS A CB  
2144  C CG  . HIS A  284 ? 0.4353 0.6256 0.7625 0.1252  -0.1207 0.0271  284 HIS A CG  
2145  N ND1 . HIS A  284 ? 0.4631 0.6502 0.7837 0.1235  -0.1353 0.0265  284 HIS A ND1 
2146  C CD2 . HIS A  284 ? 0.5010 0.7044 0.8433 0.1328  -0.1221 0.0275  284 HIS A CD2 
2147  C CE1 . HIS A  284 ? 0.5344 0.7328 0.8659 0.1295  -0.1456 0.0264  284 HIS A CE1 
2148  N NE2 . HIS A  284 ? 0.5560 0.7648 0.9016 0.1353  -0.1377 0.0272  284 HIS A NE2 
2149  N N   . GLU A  285 ? 0.3277 0.4630 0.5985 0.1125  -0.0927 0.0311  285 GLU A N   
2150  C CA  . GLU A  285 ? 0.3529 0.4828 0.6201 0.1090  -0.0788 0.0310  285 GLU A CA  
2151  C C   . GLU A  285 ? 0.3320 0.4455 0.5842 0.1167  -0.0738 0.0338  285 GLU A C   
2152  O O   . GLU A  285 ? 0.3121 0.4234 0.5639 0.1156  -0.0626 0.0330  285 GLU A O   
2153  C CB  . GLU A  285 ? 0.4653 0.5898 0.7268 0.0999  -0.0766 0.0304  285 GLU A CB  
2154  C CG  . GLU A  285 ? 0.5489 0.6543 0.7899 0.1013  -0.0825 0.0329  285 GLU A CG  
2155  C CD  . GLU A  285 ? 0.6586 0.7603 0.8967 0.0928  -0.0779 0.0321  285 GLU A CD  
2156  O OE1 . GLU A  285 ? 0.6712 0.7860 0.9237 0.0855  -0.0738 0.0296  285 GLU A OE1 
2157  O OE2 . GLU A  285 ? 0.7301 0.8152 0.9518 0.0935  -0.0778 0.0343  285 GLU A OE2 
2158  N N   . TRP A  286 ? 0.2551 0.3564 0.4944 0.1245  -0.0824 0.0371  286 TRP A N   
2159  C CA  . TRP A  286 ? 0.3517 0.4343 0.5754 0.1316  -0.0781 0.0404  286 TRP A CA  
2160  C C   . TRP A  286 ? 0.3601 0.4469 0.5912 0.1403  -0.0748 0.0404  286 TRP A C   
2161  O O   . TRP A  286 ? 0.2554 0.3275 0.4764 0.1451  -0.0684 0.0418  286 TRP A O   
2162  C CB  . TRP A  286 ? 0.8060 0.8694 1.0086 0.1357  -0.0879 0.0448  286 TRP A CB  
2163  C CG  . TRP A  286 ? 0.9235 0.9774 1.1150 0.1283  -0.0879 0.0448  286 TRP A CG  
2164  C CD1 . TRP A  286 ? 0.9418 1.0022 1.1355 0.1223  -0.0954 0.0428  286 TRP A CD1 
2165  C CD2 . TRP A  286 ? 0.9800 1.0162 1.1577 0.1259  -0.0796 0.0465  286 TRP A CD2 
2166  N NE1 . TRP A  286 ? 0.9497 0.9971 1.1310 0.1172  -0.0923 0.0434  286 TRP A NE1 
2167  C CE2 . TRP A  286 ? 0.9929 1.0261 1.1636 0.1185  -0.0816 0.0457  286 TRP A CE2 
2168  C CE3 . TRP A  286 ? 1.0190 1.0413 1.1893 0.1287  -0.0701 0.0483  286 TRP A CE3 
2169  C CZ2 . TRP A  286 ? 1.0515 1.0696 1.2034 0.1119  -0.0714 0.0460  286 TRP A CZ2 
2170  C CZ3 . TRP A  286 ? 1.0650 1.0724 1.2199 0.1224  -0.0617 0.0489  286 TRP A CZ3 
2171  C CH2 . TRP A  286 ? 1.0853 1.0917 1.2305 0.1137  -0.0617 0.0477  286 TRP A CH2 
2172  N N   . HIS A  287 ? 0.5076 0.6142 0.7572 0.1422  -0.0788 0.0386  287 HIS A N   
2173  C CA  . HIS A  287 ? 0.4520 0.5644 0.7105 0.1517  -0.0772 0.0388  287 HIS A CA  
2174  C C   . HIS A  287 ? 0.4383 0.5581 0.7069 0.1501  -0.0642 0.0347  287 HIS A C   
2175  O O   . HIS A  287 ? 0.4885 0.6089 0.7613 0.1582  -0.0604 0.0342  287 HIS A O   
2176  C CB  . HIS A  287 ? 0.4078 0.5402 0.6845 0.1541  -0.0865 0.0381  287 HIS A CB  
2177  C CG  . HIS A  287 ? 0.4421 0.5709 0.7113 0.1538  -0.1008 0.0406  287 HIS A CG  
2178  N ND1 . HIS A  287 ? 0.4320 0.5789 0.7174 0.1536  -0.1111 0.0391  287 HIS A ND1 
2179  C CD2 . HIS A  287 ? 0.4840 0.5930 0.7307 0.1536  -0.1069 0.0440  287 HIS A CD2 
2180  C CE1 . HIS A  287 ? 0.4670 0.6049 0.7390 0.1533  -0.1236 0.0410  287 HIS A CE1 
2181  N NE2 . HIS A  287 ? 0.4982 0.6128 0.7459 0.1535  -0.1211 0.0441  287 HIS A NE2 
2182  N N   . VAL A  288 ? 0.4104 0.5351 0.6821 0.1399  -0.0573 0.0319  288 VAL A N   
2183  C CA  . VAL A  288 ? 0.4125 0.5442 0.6925 0.1376  -0.0451 0.0282  288 VAL A CA  
2184  C C   . VAL A  288 ? 0.4540 0.5673 0.7193 0.1397  -0.0366 0.0279  288 VAL A C   
2185  O O   . VAL A  288 ? 0.5329 0.6502 0.8038 0.1408  -0.0275 0.0247  288 VAL A O   
2186  C CB  . VAL A  288 ? 0.2746 0.4189 0.5640 0.1260  -0.0407 0.0260  288 VAL A CB  
2187  C CG1 . VAL A  288 ? 0.2042 0.3658 0.5095 0.1235  -0.0489 0.0257  288 VAL A CG1 
2188  C CG2 . VAL A  288 ? 0.2456 0.3764 0.5200 0.1188  -0.0398 0.0274  288 VAL A CG2 
2189  N N   . LEU A  289 ? 0.3578 0.4509 0.6049 0.1403  -0.0394 0.0309  289 LEU A N   
2190  C CA  . LEU A  289 ? 0.3090 0.3829 0.5424 0.1416  -0.0319 0.0307  289 LEU A CA  
2191  C C   . LEU A  289 ? 0.3500 0.4187 0.5843 0.1512  -0.0282 0.0291  289 LEU A C   
2192  O O   . LEU A  289 ? 0.3898 0.4595 0.6265 0.1604  -0.0346 0.0309  289 LEU A O   
2193  C CB  . LEU A  289 ? 0.2857 0.3381 0.5004 0.1421  -0.0366 0.0351  289 LEU A CB  
2194  C CG  . LEU A  289 ? 0.2711 0.3196 0.4796 0.1320  -0.0342 0.0357  289 LEU A CG  
2195  C CD1 . LEU A  289 ? 0.3257 0.3533 0.5161 0.1335  -0.0396 0.0407  289 LEU A CD1 
2196  C CD2 . LEU A  289 ? 0.2293 0.2753 0.4376 0.1271  -0.0226 0.0326  289 LEU A CD2 
2197  N N   . PRO A  290 ? 0.2438 0.3069 0.4761 0.1495  -0.0180 0.0256  290 PRO A N   
2198  C CA  . PRO A  290 ? 0.2563 0.3133 0.4892 0.1575  -0.0126 0.0226  290 PRO A CA  
2199  C C   . PRO A  290 ? 0.2977 0.3321 0.5169 0.1661  -0.0167 0.0254  290 PRO A C   
2200  O O   . PRO A  290 ? 0.2915 0.3265 0.5149 0.1761  -0.0188 0.0249  290 PRO A O   
2201  C CB  . PRO A  290 ? 0.2479 0.2998 0.4768 0.1509  -0.0018 0.0191  290 PRO A CB  
2202  C CG  . PRO A  290 ? 0.2919 0.3577 0.5259 0.1408  -0.0007 0.0193  290 PRO A CG  
2203  C CD  . PRO A  290 ? 0.2277 0.2922 0.4582 0.1391  -0.0107 0.0239  290 PRO A CD  
2204  N N   . GLN A  291 ? 0.5695 0.5840 0.7726 0.1624  -0.0175 0.0286  291 GLN A N   
2205  C CA  . GLN A  291 ? 0.6205 0.6088 0.8078 0.1690  -0.0197 0.0316  291 GLN A CA  
2206  C C   . GLN A  291 ? 0.6477 0.6217 0.8201 0.1687  -0.0276 0.0383  291 GLN A C   
2207  O O   . GLN A  291 ? 0.6460 0.6271 0.8183 0.1614  -0.0300 0.0402  291 GLN A O   
2208  C CB  . GLN A  291 ? 0.6146 0.5852 0.7936 0.1651  -0.0097 0.0288  291 GLN A CB  
2209  C CG  . GLN A  291 ? 0.6249 0.6033 0.8135 0.1666  -0.0012 0.0222  291 GLN A CG  
2210  C CD  . GLN A  291 ? 0.6113 0.6024 0.8054 0.1566  0.0065  0.0188  291 GLN A CD  
2211  O OE1 . GLN A  291 ? 0.6159 0.6066 0.8057 0.1485  0.0063  0.0212  291 GLN A OE1 
2212  N NE2 . GLN A  291 ? 0.6122 0.6142 0.8153 0.1577  0.0135  0.0132  291 GLN A NE2 
2213  N N   . GLU A  292 ? 0.5554 0.5071 0.7141 0.1766  -0.0314 0.0417  292 GLU A N   
2214  C CA  . GLU A  292 ? 0.5431 0.4741 0.6831 0.1762  -0.0371 0.0483  292 GLU A CA  
2215  C C   . GLU A  292 ? 0.4968 0.4161 0.6301 0.1654  -0.0271 0.0479  292 GLU A C   
2216  O O   . GLU A  292 ? 0.4781 0.3855 0.6091 0.1641  -0.0184 0.0451  292 GLU A O   
2217  C CB  . GLU A  292 ? 0.8065 0.7147 0.9371 0.1843  -0.0423 0.0507  292 GLU A CB  
2218  C CG  . GLU A  292 ? 0.8865 0.7695 1.0042 0.1805  -0.0449 0.0603  292 GLU A CG  
2219  C CD  . GLU A  292 ? 0.9874 0.8522 1.1026 0.1880  -0.0462 0.0661  292 GLU A CD  
2220  O OE1 . GLU A  292 ? 0.9752 0.8433 1.1027 0.1931  -0.0448 0.0606  292 GLU A OE1 
2221  O OE2 . GLU A  292 ? 1.0674 0.9138 1.1626 0.1891  -0.0488 0.0746  292 GLU A OE2 
2222  N N   . SER A  293 ? 0.4683 0.3913 0.5980 0.1580  -0.0278 0.0507  293 SER A N   
2223  C CA  . SER A  293 ? 0.4014 0.3196 0.5280 0.1477  -0.0175 0.0498  293 SER A CA  
2224  C C   . SER A  293 ? 0.3451 0.2606 0.4599 0.1409  -0.0202 0.0537  293 SER A C   
2225  O O   . SER A  293 ? 0.3149 0.2377 0.4299 0.1439  -0.0301 0.0566  293 SER A O   
2226  C CB  . SER A  293 ? 0.3976 0.3394 0.5427 0.1424  -0.0123 0.0430  293 SER A CB  
2227  O OG  . SER A  293 ? 0.3971 0.3606 0.5527 0.1404  -0.0191 0.0430  293 SER A OG  
2228  N N   . ILE A  294 ? 0.3113 0.2173 0.4150 0.1305  -0.0117 0.0522  294 ILE A N   
2229  C CA  . ILE A  294 ? 0.3047 0.2124 0.3988 0.1215  -0.0120 0.0532  294 ILE A CA  
2230  C C   . ILE A  294 ? 0.2825 0.2030 0.3854 0.1109  -0.0043 0.0475  294 ILE A C   
2231  O O   . ILE A  294 ? 0.2778 0.1987 0.3871 0.1090  0.0028  0.0433  294 ILE A O   
2232  C CB  . ILE A  294 ? 0.3277 0.2089 0.3968 0.1193  -0.0092 0.0582  294 ILE A CB  
2233  C CG1 . ILE A  294 ? 0.3379 0.2014 0.4016 0.1163  0.0012  0.0568  294 ILE A CG1 
2234  C CG2 . ILE A  294 ? 0.3513 0.2197 0.4080 0.1296  -0.0185 0.0648  294 ILE A CG2 
2235  C CD1 . ILE A  294 ? 0.4260 0.2660 0.4676 0.1107  0.0068  0.0610  294 ILE A CD1 
2236  N N   . PHE A  295 ? 0.5764 0.5067 0.6785 0.1045  -0.0062 0.0472  295 PHE A N   
2237  C CA  . PHE A  295 ? 0.5627 0.5050 0.6720 0.0950  -0.0002 0.0427  295 PHE A CA  
2238  C C   . PHE A  295 ? 0.5571 0.5193 0.6865 0.0967  0.0000  0.0386  295 PHE A C   
2239  O O   . PHE A  295 ? 0.5405 0.5089 0.6757 0.0914  0.0063  0.0344  295 PHE A O   
2240  C CB  . PHE A  295 ? 0.2570 0.1850 0.3570 0.0882  0.0092  0.0411  295 PHE A CB  
2241  C CG  . PHE A  295 ? 0.2443 0.1788 0.3442 0.0784  0.0134  0.0387  295 PHE A CG  
2242  C CD1 . PHE A  295 ? 0.2247 0.1789 0.3362 0.0757  0.0109  0.0364  295 PHE A CD1 
2243  C CD2 . PHE A  295 ? 0.2533 0.1738 0.3424 0.0719  0.0204  0.0388  295 PHE A CD2 
2244  C CE1 . PHE A  295 ? 0.8025 0.7619 0.9142 0.0676  0.0146  0.0344  295 PHE A CE1 
2245  C CE2 . PHE A  295 ? 0.2420 0.1697 0.3331 0.0635  0.0244  0.0364  295 PHE A CE2 
2246  C CZ  . PHE A  295 ? 0.2228 0.1695 0.3249 0.0618  0.0212  0.0342  295 PHE A CZ  
2247  N N   . ARG A  296 ? 0.4425 0.4147 0.5822 0.1042  -0.0070 0.0399  296 ARG A N   
2248  C CA  . ARG A  296 ? 0.4306 0.4236 0.5906 0.1060  -0.0069 0.0367  296 ARG A CA  
2249  C C   . ARG A  296 ? 0.4524 0.4607 0.6222 0.1071  -0.0157 0.0383  296 ARG A C   
2250  O O   . ARG A  296 ? 0.4488 0.4530 0.6155 0.1132  -0.0242 0.0415  296 ARG A O   
2251  C CB  . ARG A  296 ? 0.2727 0.2640 0.4403 0.1152  -0.0056 0.0359  296 ARG A CB  
2252  C CG  . ARG A  296 ? 0.2355 0.2118 0.3949 0.1142  0.0029  0.0332  296 ARG A CG  
2253  C CD  . ARG A  296 ? 0.2208 0.2065 0.3845 0.1065  0.0100  0.0283  296 ARG A CD  
2254  N NE  . ARG A  296 ? 0.3159 0.2875 0.4724 0.1055  0.0171  0.0247  296 ARG A NE  
2255  C CZ  . ARG A  296 ? 0.2948 0.2522 0.4386 0.0984  0.0208  0.0240  296 ARG A CZ  
2256  N NH1 . ARG A  296 ? 0.2776 0.2335 0.4144 0.0924  0.0188  0.0269  296 ARG A NH1 
2257  N NH2 . ARG A  296 ? 0.2913 0.2361 0.4300 0.0971  0.0268  0.0199  296 ARG A NH2 
2258  N N   . PHE A  297 ? 0.4939 0.5192 0.6754 0.1012  -0.0141 0.0359  297 PHE A N   
2259  C CA  . PHE A  297 ? 0.4615 0.5006 0.6527 0.1001  -0.0218 0.0366  297 PHE A CA  
2260  C C   . PHE A  297 ? 0.3595 0.4187 0.5678 0.1003  -0.0211 0.0336  297 PHE A C   
2261  O O   . PHE A  297 ? 0.3250 0.3891 0.5375 0.0987  -0.0131 0.0309  297 PHE A O   
2262  C CB  . PHE A  297 ? 0.4907 0.5297 0.6747 0.0909  -0.0205 0.0361  297 PHE A CB  
2263  C CG  . PHE A  297 ? 0.5362 0.5558 0.6990 0.0878  -0.0174 0.0371  297 PHE A CG  
2264  C CD1 . PHE A  297 ? 0.5863 0.5926 0.7337 0.0899  -0.0231 0.0401  297 PHE A CD1 
2265  C CD2 . PHE A  297 ? 0.5469 0.5619 0.7052 0.0827  -0.0085 0.0351  297 PHE A CD2 
2266  C CE1 . PHE A  297 ? 0.6134 0.6020 0.7417 0.0866  -0.0185 0.0413  297 PHE A CE1 
2267  C CE2 . PHE A  297 ? 0.5768 0.5757 0.7186 0.0791  -0.0048 0.0359  297 PHE A CE2 
2268  C CZ  . PHE A  297 ? 0.6070 0.5926 0.7340 0.0809  -0.0090 0.0391  297 PHE A CZ  
2269  N N   . SER A  298 ? 0.1799 0.2495 0.3958 0.1016  -0.0293 0.0338  298 SER A N   
2270  C CA  . SER A  298 ? 0.1767 0.2640 0.4077 0.1023  -0.0287 0.0311  298 SER A CA  
2271  C C   . SER A  298 ? 0.1624 0.2627 0.4025 0.0940  -0.0224 0.0290  298 SER A C   
2272  O O   . SER A  298 ? 0.1833 0.2905 0.4293 0.0939  -0.0148 0.0269  298 SER A O   
2273  C CB  . SER A  298 ? 0.3045 0.4000 0.5426 0.1057  -0.0395 0.0318  298 SER A CB  
2274  O OG  . SER A  298 ? 0.3793 0.4685 0.6138 0.1155  -0.0439 0.0332  298 SER A OG  
2275  N N   . PHE A  299 ? 0.1553 0.2578 0.3958 0.0875  -0.0254 0.0297  299 PHE A N   
2276  C CA  . PHE A  299 ? 0.1439 0.2561 0.3913 0.0797  -0.0196 0.0285  299 PHE A CA  
2277  C C   . PHE A  299 ? 0.1411 0.2447 0.3787 0.0744  -0.0153 0.0294  299 PHE A C   
2278  O O   . PHE A  299 ? 0.1361 0.2335 0.3686 0.0724  -0.0200 0.0306  299 PHE A O   
2279  C CB  . PHE A  299 ? 0.1424 0.2666 0.4022 0.0762  -0.0257 0.0281  299 PHE A CB  
2280  C CG  . PHE A  299 ? 0.1495 0.2844 0.4211 0.0812  -0.0294 0.0270  299 PHE A CG  
2281  C CD1 . PHE A  299 ? 0.1602 0.2921 0.4301 0.0875  -0.0396 0.0277  299 PHE A CD1 
2282  C CD2 . PHE A  299 ? 0.3579 0.5058 0.6423 0.0802  -0.0228 0.0254  299 PHE A CD2 
2283  C CE1 . PHE A  299 ? 0.1679 0.3110 0.4499 0.0929  -0.0437 0.0267  299 PHE A CE1 
2284  C CE2 . PHE A  299 ? 0.3367 0.4962 0.6343 0.0852  -0.0260 0.0242  299 PHE A CE2 
2285  C CZ  . PHE A  299 ? 0.1645 0.3219 0.4612 0.0917  -0.0367 0.0248  299 PHE A CZ  
2286  N N   . VAL A  300 ? 0.1324 0.2358 0.3676 0.0729  -0.0064 0.0285  300 VAL A N   
2287  C CA  . VAL A  300 ? 0.1268 0.2230 0.3533 0.0688  -0.0022 0.0289  300 VAL A CA  
2288  C C   . VAL A  300 ? 0.1204 0.2250 0.3508 0.0643  0.0048  0.0283  300 VAL A C   
2289  O O   . VAL A  300 ? 0.1213 0.2359 0.3607 0.0647  0.0069  0.0277  300 VAL A O   
2290  C CB  . VAL A  300 ? 0.2691 0.3528 0.4859 0.0729  0.0011  0.0286  300 VAL A CB  
2291  C CG1 . VAL A  300 ? 0.3029 0.3763 0.5149 0.0784  -0.0051 0.0303  300 VAL A CG1 
2292  C CG2 . VAL A  300 ? 0.2536 0.3398 0.4720 0.0758  0.0076  0.0264  300 VAL A CG2 
2293  N N   . PRO A  301 ? 0.3943 0.4949 0.6181 0.0604  0.0084  0.0287  301 PRO A N   
2294  C CA  . PRO A  301 ? 0.3363 0.4434 0.5620 0.0571  0.0146  0.0290  301 PRO A CA  
2295  C C   . PRO A  301 ? 0.3534 0.4645 0.5811 0.0610  0.0204  0.0273  301 PRO A C   
2296  O O   . PRO A  301 ? 0.4090 0.5138 0.6322 0.0655  0.0215  0.0255  301 PRO A O   
2297  C CB  . PRO A  301 ? 0.1292 0.2295 0.3461 0.0550  0.0166  0.0290  301 PRO A CB  
2298  C CG  . PRO A  301 ? 0.1443 0.2379 0.3584 0.0541  0.0110  0.0297  301 PRO A CG  
2299  C CD  . PRO A  301 ? 0.1851 0.2764 0.4011 0.0586  0.0066  0.0294  301 PRO A CD  
2300  N N   . VAL A  302 ? 0.2004 0.3212 0.4356 0.0594  0.0247  0.0280  302 VAL A N   
2301  C CA  . VAL A  302 ? 0.1926 0.3184 0.4306 0.0632  0.0315  0.0264  302 VAL A CA  
2302  C C   . VAL A  302 ? 0.2054 0.3311 0.4373 0.0620  0.0388  0.0269  302 VAL A C   
2303  O O   . VAL A  302 ? 0.1891 0.3149 0.4189 0.0575  0.0387  0.0296  302 VAL A O   
2304  C CB  . VAL A  302 ? 0.1231 0.2607 0.3744 0.0626  0.0328  0.0270  302 VAL A CB  
2305  C CG1 . VAL A  302 ? 0.1195 0.2626 0.3752 0.0562  0.0355  0.0302  302 VAL A CG1 
2306  C CG2 . VAL A  302 ? 0.1303 0.2730 0.3852 0.0678  0.0399  0.0246  302 VAL A CG2 
2307  N N   . VAL A  303 ? 0.2596 0.3846 0.4881 0.0666  0.0450  0.0243  303 VAL A N   
2308  C CA  . VAL A  303 ? 0.3010 0.4272 0.5238 0.0662  0.0521  0.0250  303 VAL A CA  
2309  C C   . VAL A  303 ? 0.3928 0.5292 0.6222 0.0657  0.0598  0.0269  303 VAL A C   
2310  O O   . VAL A  303 ? 0.4379 0.5777 0.6695 0.0700  0.0659  0.0243  303 VAL A O   
2311  C CB  . VAL A  303 ? 0.1530 0.2712 0.3651 0.0705  0.0551  0.0201  303 VAL A CB  
2312  C CG1 . VAL A  303 ? 0.1618 0.2778 0.3592 0.0686  0.0597  0.0192  303 VAL A CG1 
2313  C CG2 . VAL A  303 ? 0.1342 0.2411 0.3396 0.0698  0.0480  0.0181  303 VAL A CG2 
2314  N N   . ASP A  304 ? 0.2949 0.4353 0.5271 0.0605  0.0602  0.0315  304 ASP A N   
2315  C CA  . ASP A  304 ? 0.3337 0.4834 0.5745 0.0581  0.0669  0.0345  304 ASP A CA  
2316  C C   . ASP A  304 ? 0.3626 0.5144 0.5964 0.0584  0.0773  0.0379  304 ASP A C   
2317  O O   . ASP A  304 ? 0.3387 0.4971 0.5778 0.0562  0.0849  0.0413  304 ASP A O   
2318  C CB  . ASP A  304 ? 0.4683 0.6204 0.7186 0.0520  0.0610  0.0377  304 ASP A CB  
2319  C CG  . ASP A  304 ? 0.5412 0.6863 0.7851 0.0485  0.0554  0.0405  304 ASP A CG  
2320  O OD1 . ASP A  304 ? 0.5059 0.6447 0.7391 0.0508  0.0540  0.0394  304 ASP A OD1 
2321  O OD2 . ASP A  304 ? 0.5332 0.6793 0.7839 0.0434  0.0523  0.0433  304 ASP A OD2 
2322  N N   . GLY A  305 ? 0.6455 0.7872 0.8596 0.0592  0.0752  0.0358  305 GLY A N   
2323  C CA  . GLY A  305 ? 0.7101 0.8479 0.9072 0.0578  0.0801  0.0382  305 GLY A CA  
2324  C C   . GLY A  305 ? 0.7384 0.8758 0.9362 0.0523  0.0782  0.0448  305 GLY A C   
2325  O O   . GLY A  305 ? 0.8160 0.9504 1.0011 0.0511  0.0828  0.0485  305 GLY A O   
2326  N N   . ASP A  306 ? 0.5694 0.7085 0.7808 0.0492  0.0715  0.0463  306 ASP A N   
2327  C CA  . ASP A  306 ? 0.5398 0.6771 0.7532 0.0441  0.0695  0.0520  306 ASP A CA  
2328  C C   . ASP A  306 ? 0.5147 0.6442 0.7226 0.0428  0.0594  0.0510  306 ASP A C   
2329  O O   . ASP A  306 ? 0.5519 0.6747 0.7457 0.0426  0.0575  0.0525  306 ASP A O   
2330  C CB  . ASP A  306 ? 0.5159 0.6623 0.7514 0.0406  0.0715  0.0547  306 ASP A CB  
2331  C CG  . ASP A  306 ? 0.5063 0.6496 0.7444 0.0347  0.0707  0.0605  306 ASP A CG  
2332  O OD1 . ASP A  306 ? 0.5238 0.6585 0.7461 0.0340  0.0707  0.0638  306 ASP A OD1 
2333  O OD2 . ASP A  306 ? 0.4893 0.6383 0.7455 0.0308  0.0697  0.0617  306 ASP A OD2 
2334  N N   . PHE A  307 ? 0.3617 0.4920 0.5805 0.0424  0.0529  0.0484  307 PHE A N   
2335  C CA  . PHE A  307 ? 0.2738 0.3967 0.4874 0.0415  0.0446  0.0470  307 PHE A CA  
2336  C C   . PHE A  307 ? 0.2426 0.3605 0.4429 0.0447  0.0431  0.0426  307 PHE A C   
2337  O O   . PHE A  307 ? 0.2146 0.3273 0.4043 0.0443  0.0402  0.0426  307 PHE A O   
2338  C CB  . PHE A  307 ? 0.2564 0.3803 0.4818 0.0407  0.0386  0.0451  307 PHE A CB  
2339  C CG  . PHE A  307 ? 0.2586 0.3748 0.4790 0.0390  0.0318  0.0443  307 PHE A CG  
2340  C CD1 . PHE A  307 ? 0.2276 0.3378 0.4375 0.0409  0.0291  0.0410  307 PHE A CD1 
2341  C CD2 . PHE A  307 ? 0.2640 0.3788 0.4910 0.0354  0.0286  0.0464  307 PHE A CD2 
2342  C CE1 . PHE A  307 ? 0.2083 0.3125 0.4150 0.0395  0.0242  0.0401  307 PHE A CE1 
2343  C CE2 . PHE A  307 ? 0.2412 0.3487 0.4633 0.0344  0.0233  0.0453  307 PHE A CE2 
2344  C CZ  . PHE A  307 ? 0.2121 0.3149 0.4244 0.0366  0.0215  0.0422  307 PHE A CZ  
2345  N N   . LEU A  308 ? 0.3286 0.4481 0.5307 0.0480  0.0446  0.0386  308 LEU A N   
2346  C CA  . LEU A  308 ? 0.3516 0.4661 0.5416 0.0507  0.0447  0.0339  308 LEU A CA  
2347  C C   . LEU A  308 ? 0.4217 0.5393 0.6055 0.0528  0.0525  0.0341  308 LEU A C   
2348  O O   . LEU A  308 ? 0.4120 0.5356 0.6045 0.0548  0.0581  0.0343  308 LEU A O   
2349  C CB  . LEU A  308 ? 0.2379 0.3499 0.4320 0.0534  0.0426  0.0295  308 LEU A CB  
2350  C CG  . LEU A  308 ? 0.1132 0.2205 0.3101 0.0514  0.0356  0.0294  308 LEU A CG  
2351  C CD1 . LEU A  308 ? 0.1136 0.2165 0.3123 0.0544  0.0337  0.0261  308 LEU A CD1 
2352  C CD2 . LEU A  308 ? 0.1131 0.2151 0.3003 0.0490  0.0324  0.0285  308 LEU A CD2 
2353  N N   . SER A  309 ? 0.5465 0.6603 0.7153 0.0526  0.0528  0.0342  309 SER A N   
2354  C CA  . SER A  309 ? 0.5427 0.6579 0.7015 0.0545  0.0604  0.0350  309 SER A CA  
2355  C C   . SER A  309 ? 0.5720 0.6852 0.7248 0.0585  0.0637  0.0283  309 SER A C   
2356  O O   . SER A  309 ? 0.5795 0.6960 0.7315 0.0612  0.0721  0.0279  309 SER A O   
2357  C CB  . SER A  309 ? 0.2849 0.3955 0.4274 0.0535  0.0581  0.0372  309 SER A CB  
2358  O OG  . SER A  309 ? 0.2712 0.3769 0.4010 0.0553  0.0544  0.0310  309 SER A OG  
2359  N N   . ASP A  310 ? 0.4683 0.5755 0.6171 0.0589  0.0577  0.0228  310 ASP A N   
2360  C CA  . ASP A  310 ? 0.4564 0.5597 0.6025 0.0625  0.0598  0.0160  310 ASP A CA  
2361  C C   . ASP A  310 ? 0.4336 0.5331 0.5892 0.0620  0.0541  0.0139  310 ASP A C   
2362  O O   . ASP A  310 ? 0.4669 0.5681 0.6309 0.0592  0.0494  0.0176  310 ASP A O   
2363  C CB  . ASP A  310 ? 0.5170 0.6136 0.6443 0.0630  0.0588  0.0106  310 ASP A CB  
2364  C CG  . ASP A  310 ? 0.5842 0.6767 0.7059 0.0673  0.0644  0.0040  310 ASP A CG  
2365  O OD1 . ASP A  310 ? 0.6199 0.7143 0.7537 0.0703  0.0682  0.0035  310 ASP A OD1 
2366  O OD2 . ASP A  310 ? 0.5996 0.6867 0.7046 0.0680  0.0647  -0.0010 310 ASP A OD2 
2367  N N   . THR A  311 ? 0.3031 0.3963 0.4564 0.0648  0.0547  0.0081  311 THR A N   
2368  C CA  . THR A  311 ? 0.2733 0.3603 0.4321 0.0642  0.0496  0.0064  311 THR A CA  
2369  C C   . THR A  311 ? 0.2422 0.3248 0.3952 0.0593  0.0433  0.0054  311 THR A C   
2370  O O   . THR A  311 ? 0.1913 0.2730 0.3337 0.0577  0.0424  0.0028  311 THR A O   
2371  C CB  . THR A  311 ? 0.3590 0.4377 0.5150 0.0682  0.0522  0.0005  311 THR A CB  
2372  O OG1 . THR A  311 ? 0.3588 0.4303 0.5008 0.0668  0.0518  -0.0057 311 THR A OG1 
2373  C CG2 . THR A  311 ? 0.3963 0.4804 0.5576 0.0739  0.0594  0.0005  311 THR A CG2 
2374  N N   . PRO A  312 ? 0.4231 0.5034 0.5830 0.0572  0.0390  0.0073  312 PRO A N   
2375  C CA  . PRO A  312 ? 0.4627 0.5398 0.6199 0.0527  0.0340  0.0063  312 PRO A CA  
2376  C C   . PRO A  312 ? 0.5657 0.6360 0.7143 0.0514  0.0335  -0.0005 312 PRO A C   
2377  O O   . PRO A  312 ? 0.6227 0.6944 0.7680 0.0480  0.0299  -0.0021 312 PRO A O   
2378  C CB  . PRO A  312 ? 0.1344 0.2074 0.2987 0.0520  0.0319  0.0083  312 PRO A CB  
2379  C CG  . PRO A  312 ? 0.1302 0.2088 0.3024 0.0550  0.0332  0.0126  312 PRO A CG  
2380  C CD  . PRO A  312 ? 0.1399 0.2212 0.3105 0.0590  0.0384  0.0107  312 PRO A CD  
2381  N N   . GLU A  313 ? 0.4851 0.5484 0.6311 0.0541  0.0366  -0.0046 313 GLU A N   
2382  C CA  . GLU A  313 ? 0.5443 0.6001 0.6815 0.0529  0.0365  -0.0121 313 GLU A CA  
2383  C C   . GLU A  313 ? 0.4811 0.5424 0.6091 0.0521  0.0353  -0.0141 313 GLU A C   
2384  O O   . GLU A  313 ? 0.4920 0.5538 0.6169 0.0481  0.0305  -0.0170 313 GLU A O   
2385  C CB  . GLU A  313 ? 1.0457 1.0937 1.1804 0.0577  0.0414  -0.0158 313 GLU A CB  
2386  C CG  . GLU A  313 ? 1.1546 1.1971 1.2974 0.0602  0.0422  -0.0128 313 GLU A CG  
2387  C CD  . GLU A  313 ? 1.2351 1.2678 1.3782 0.0558  0.0393  -0.0140 313 GLU A CD  
2388  O OE1 . GLU A  313 ? 1.2660 1.2943 1.4039 0.0513  0.0380  -0.0195 313 GLU A OE1 
2389  O OE2 . GLU A  313 ? 1.2481 1.2776 1.3964 0.0565  0.0384  -0.0096 313 GLU A OE2 
2390  N N   . ALA A  314 ? 0.5564 0.6220 0.6800 0.0561  0.0398  -0.0125 314 ALA A N   
2391  C CA  . ALA A  314 ? 0.5401 0.6094 0.6516 0.0564  0.0397  -0.0136 314 ALA A CA  
2392  C C   . ALA A  314 ? 0.5441 0.6197 0.6566 0.0529  0.0336  -0.0094 314 ALA A C   
2393  O O   . ALA A  314 ? 0.6080 0.6839 0.7112 0.0514  0.0290  -0.0125 314 ALA A O   
2394  C CB  . ALA A  314 ? 0.4143 0.4883 0.5237 0.0609  0.0471  -0.0100 314 ALA A CB  
2395  N N   . LEU A  315 ? 0.4446 0.5248 0.5684 0.0521  0.0332  -0.0027 315 LEU A N   
2396  C CA  . LEU A  315 ? 0.3454 0.4312 0.4708 0.0501  0.0288  0.0022  315 LEU A CA  
2397  C C   . LEU A  315 ? 0.3446 0.4296 0.4719 0.0465  0.0220  -0.0013 315 LEU A C   
2398  O O   . LEU A  315 ? 0.4138 0.5025 0.5361 0.0459  0.0173  -0.0010 315 LEU A O   
2399  C CB  . LEU A  315 ? 0.2142 0.3038 0.3513 0.0500  0.0303  0.0092  315 LEU A CB  
2400  C CG  . LEU A  315 ? 0.2229 0.3161 0.3586 0.0528  0.0367  0.0133  315 LEU A CG  
2401  C CD1 . LEU A  315 ? 0.2308 0.3282 0.3794 0.0522  0.0379  0.0195  315 LEU A CD1 
2402  C CD2 . LEU A  315 ? 0.2354 0.3303 0.3585 0.0534  0.0367  0.0152  315 LEU A CD2 
2403  N N   . ILE A  316 ? 0.1932 0.2737 0.3279 0.0442  0.0216  -0.0044 316 ILE A N   
2404  C CA  . ILE A  316 ? 0.1749 0.2553 0.3138 0.0401  0.0166  -0.0081 316 ILE A CA  
2405  C C   . ILE A  316 ? 0.1910 0.2690 0.3214 0.0389  0.0140  -0.0160 316 ILE A C   
2406  O O   . ILE A  316 ? 0.1989 0.2798 0.3319 0.0356  0.0085  -0.0197 316 ILE A O   
2407  C CB  . ILE A  316 ? 0.2286 0.3035 0.3768 0.0373  0.0180  -0.0088 316 ILE A CB  
2408  C CG1 . ILE A  316 ? 0.2881 0.3532 0.4328 0.0378  0.0217  -0.0136 316 ILE A CG1 
2409  C CG2 . ILE A  316 ? 0.1972 0.2735 0.3523 0.0385  0.0198  -0.0020 316 ILE A CG2 
2410  C CD1 . ILE A  316 ? 0.3080 0.3653 0.4591 0.0356  0.0235  -0.0132 316 ILE A CD1 
2411  N N   . ASN A  317 ? 0.3088 0.3819 0.4296 0.0416  0.0177  -0.0191 317 ASN A N   
2412  C CA  . ASN A  317 ? 0.4291 0.4986 0.5399 0.0404  0.0148  -0.0275 317 ASN A CA  
2413  C C   . ASN A  317 ? 0.4826 0.5587 0.5833 0.0414  0.0095  -0.0272 317 ASN A C   
2414  O O   . ASN A  317 ? 0.5052 0.5828 0.6032 0.0387  0.0026  -0.0331 317 ASN A O   
2415  C CB  . ASN A  317 ? 0.6086 0.6692 0.7111 0.0433  0.0208  -0.0320 317 ASN A CB  
2416  C CG  . ASN A  317 ? 0.6977 0.7486 0.8016 0.0397  0.0201  -0.0403 317 ASN A CG  
2417  O OD1 . ASN A  317 ? 0.7017 0.7462 0.8143 0.0386  0.0231  -0.0394 317 ASN A OD1 
2418  N ND2 . ASN A  317 ? 0.7561 0.8050 0.8509 0.0375  0.0156  -0.0485 317 ASN A ND2 
2419  N N   . THR A  318 ? 0.6029 0.6827 0.6982 0.0454  0.0124  -0.0202 318 THR A N   
2420  C CA  . THR A  318 ? 0.6315 0.7150 0.7133 0.0475  0.0086  -0.0186 318 THR A CA  
2421  C C   . THR A  318 ? 0.6916 0.7825 0.7786 0.0475  0.0033  -0.0115 318 THR A C   
2422  O O   . THR A  318 ? 0.7871 0.8800 0.8618 0.0499  -0.0004 -0.0093 318 THR A O   
2423  C CB  . THR A  318 ? 0.5127 0.5941 0.5824 0.0519  0.0165  -0.0150 318 THR A CB  
2424  O OG1 . THR A  318 ? 0.5090 0.5939 0.5897 0.0528  0.0217  -0.0063 318 THR A OG1 
2425  C CG2 . THR A  318 ? 0.5134 0.5873 0.5783 0.0531  0.0225  -0.0220 318 THR A CG2 
2426  N N   . GLY A  319 ? 0.4693 0.5631 0.5729 0.0454  0.0031  -0.0080 319 GLY A N   
2427  C CA  . GLY A  319 ? 0.4403 0.5395 0.5493 0.0464  0.0000  -0.0006 319 GLY A CA  
2428  C C   . GLY A  319 ? 0.4252 0.5301 0.5350 0.0461  -0.0096 -0.0023 319 GLY A C   
2429  O O   . GLY A  319 ? 0.3705 0.4763 0.4781 0.0442  -0.0149 -0.0100 319 GLY A O   
2430  N N   . ASP A  320 ? 0.7089 0.8174 0.8222 0.0481  -0.0124 0.0045  320 ASP A N   
2431  C CA  . ASP A  320 ? 0.8031 0.9184 0.9225 0.0484  -0.0218 0.0030  320 ASP A CA  
2432  C C   . ASP A  320 ? 0.8337 0.9526 0.9715 0.0472  -0.0215 0.0060  320 ASP A C   
2433  O O   . ASP A  320 ? 0.8784 0.9959 1.0178 0.0494  -0.0192 0.0134  320 ASP A O   
2434  C CB  . ASP A  320 ? 0.8486 0.9648 0.9542 0.0532  -0.0274 0.0079  320 ASP A CB  
2435  C CG  . ASP A  320 ? 0.8936 1.0179 1.0081 0.0546  -0.0378 0.0069  320 ASP A CG  
2436  O OD1 . ASP A  320 ? 0.8977 1.0277 1.0209 0.0515  -0.0431 -0.0014 320 ASP A OD1 
2437  O OD2 . ASP A  320 ? 0.9155 1.0404 1.0296 0.0586  -0.0404 0.0143  320 ASP A OD2 
2438  N N   . PHE A  321 ? 0.7238 0.8466 0.8750 0.0434  -0.0233 -0.0003 321 PHE A N   
2439  C CA  . PHE A  321 ? 0.6472 0.7721 0.8152 0.0416  -0.0210 0.0011  321 PHE A CA  
2440  C C   . PHE A  321 ? 0.7637 0.8977 0.9452 0.0426  -0.0273 0.0005  321 PHE A C   
2441  O O   . PHE A  321 ? 0.8044 0.9402 1.0000 0.0406  -0.0242 0.0000  321 PHE A O   
2442  C CB  . PHE A  321 ? 0.4724 0.5925 0.6462 0.0369  -0.0146 -0.0031 321 PHE A CB  
2443  C CG  . PHE A  321 ? 0.4094 0.5211 0.5727 0.0374  -0.0081 -0.0011 321 PHE A CG  
2444  C CD1 . PHE A  321 ? 0.3886 0.4976 0.5477 0.0403  -0.0045 0.0062  321 PHE A CD1 
2445  C CD2 . PHE A  321 ? 0.3685 0.4750 0.5271 0.0351  -0.0056 -0.0068 321 PHE A CD2 
2446  C CE1 . PHE A  321 ? 0.3569 0.4604 0.5094 0.0410  0.0015  0.0077  321 PHE A CE1 
2447  C CE2 . PHE A  321 ? 0.3368 0.4366 0.4877 0.0366  0.0004  -0.0051 321 PHE A CE2 
2448  C CZ  . PHE A  321 ? 0.3222 0.4216 0.4709 0.0396  0.0038  0.0021  321 PHE A CZ  
2449  N N   . GLN A  322 ? 0.4091 0.5491 0.5865 0.0460  -0.0361 0.0001  322 GLN A N   
2450  C CA  . GLN A  322 ? 0.4698 0.6201 0.6617 0.0480  -0.0431 -0.0007 322 GLN A CA  
2451  C C   . GLN A  322 ? 0.5062 0.6562 0.7074 0.0513  -0.0405 0.0058  322 GLN A C   
2452  O O   . GLN A  322 ? 0.4605 0.6187 0.6786 0.0520  -0.0429 0.0039  322 GLN A O   
2453  C CB  . GLN A  322 ? 0.9008 1.0564 1.0837 0.0525  -0.0542 -0.0010 322 GLN A CB  
2454  C CG  . GLN A  322 ? 1.0119 1.1697 1.1883 0.0492  -0.0592 -0.0095 322 GLN A CG  
2455  C CD  . GLN A  322 ? 1.1193 1.2728 1.2719 0.0537  -0.0647 -0.0071 322 GLN A CD  
2456  O OE1 . GLN A  322 ? 1.1390 1.2912 1.2834 0.0599  -0.0680 0.0005  322 GLN A OE1 
2457  N NE2 . GLN A  322 ? 1.1614 1.3111 1.3015 0.0509  -0.0650 -0.0135 322 GLN A NE2 
2458  N N   . ASP A  323 ? 0.9660 1.1068 1.1569 0.0533  -0.0352 0.0130  323 ASP A N   
2459  C CA  . ASP A  323 ? 1.0189 1.1565 1.2163 0.0559  -0.0321 0.0189  323 ASP A CA  
2460  C C   . ASP A  323 ? 0.8803 1.0192 1.0930 0.0520  -0.0263 0.0152  323 ASP A C   
2461  O O   . ASP A  323 ? 0.8701 1.0096 1.0928 0.0540  -0.0250 0.0170  323 ASP A O   
2462  C CB  . ASP A  323 ? 1.3371 1.4640 1.5212 0.0563  -0.0262 0.0258  323 ASP A CB  
2463  C CG  . ASP A  323 ? 1.4444 1.5663 1.6299 0.0602  -0.0255 0.0331  323 ASP A CG  
2464  O OD1 . ASP A  323 ? 1.4805 1.6003 1.6763 0.0590  -0.0214 0.0331  323 ASP A OD1 
2465  O OD2 . ASP A  323 ? 1.4631 1.5816 1.6378 0.0643  -0.0286 0.0391  323 ASP A OD2 
2466  N N   . LEU A  324 ? 0.6904 0.8287 0.9038 0.0466  -0.0227 0.0097  324 LEU A N   
2467  C CA  . LEU A  324 ? 0.5020 0.6348 0.7198 0.0427  -0.0145 0.0087  324 LEU A CA  
2468  C C   . LEU A  324 ? 0.4345 0.5717 0.6651 0.0380  -0.0120 0.0022  324 LEU A C   
2469  O O   . LEU A  324 ? 0.4605 0.6029 0.6939 0.0353  -0.0153 -0.0034 324 LEU A O   
2470  C CB  . LEU A  324 ? 0.1621 0.2864 0.3669 0.0408  -0.0103 0.0099  324 LEU A CB  
2471  C CG  . LEU A  324 ? 0.1055 0.2225 0.3115 0.0380  -0.0031 0.0103  324 LEU A CG  
2472  C CD1 . LEU A  324 ? 0.1026 0.2155 0.3083 0.0405  -0.0013 0.0162  324 LEU A CD1 
2473  C CD2 . LEU A  324 ? 0.1074 0.2186 0.3042 0.0361  -0.0001 0.0092  324 LEU A CD2 
2474  N N   . GLN A  325 ? 0.2175 0.3517 0.4552 0.0368  -0.0059 0.0027  325 GLN A N   
2475  C CA  . GLN A  325 ? 0.1563 0.2911 0.4032 0.0317  -0.0005 -0.0022 325 GLN A CA  
2476  C C   . GLN A  325 ? 0.1054 0.2280 0.3442 0.0293  0.0072  -0.0003 325 GLN A C   
2477  O O   . GLN A  325 ? 0.0954 0.2123 0.3300 0.0318  0.0095  0.0040  325 GLN A O   
2478  C CB  . GLN A  325 ? 0.2454 0.3884 0.5086 0.0326  0.0006  -0.0040 325 GLN A CB  
2479  C CG  . GLN A  325 ? 0.3205 0.4730 0.5882 0.0372  -0.0076 -0.0037 325 GLN A CG  
2480  C CD  . GLN A  325 ? 0.4037 0.5509 0.6655 0.0425  -0.0075 0.0017  325 GLN A CD  
2481  O OE1 . GLN A  325 ? 0.4402 0.5804 0.6921 0.0453  -0.0084 0.0069  325 GLN A OE1 
2482  N NE2 . GLN A  325 ? 0.4275 0.5778 0.6965 0.0437  -0.0059 0.0002  325 GLN A NE2 
2483  N N   . VAL A  326 ? 0.1063 0.2245 0.3428 0.0246  0.0107  -0.0036 326 VAL A N   
2484  C CA  . VAL A  326 ? 0.1126 0.2188 0.3408 0.0228  0.0171  -0.0018 326 VAL A CA  
2485  C C   . VAL A  326 ? 0.1037 0.2072 0.3381 0.0177  0.0237  -0.0053 326 VAL A C   
2486  O O   . VAL A  326 ? 0.1821 0.2914 0.4257 0.0139  0.0235  -0.0101 326 VAL A O   
2487  C CB  . VAL A  326 ? 0.1252 0.2243 0.3415 0.0227  0.0164  -0.0012 326 VAL A CB  
2488  C CG1 . VAL A  326 ? 0.1016 0.2021 0.3109 0.0272  0.0121  0.0030  326 VAL A CG1 
2489  C CG2 . VAL A  326 ? 0.1182 0.2200 0.3369 0.0193  0.0146  -0.0067 326 VAL A CG2 
2490  N N   . LEU A  327 ? 0.1652 0.2595 0.3940 0.0176  0.0296  -0.0027 327 LEU A N   
2491  C CA  . LEU A  327 ? 0.1626 0.2500 0.3919 0.0129  0.0374  -0.0045 327 LEU A CA  
2492  C C   . LEU A  327 ? 0.2024 0.2751 0.4162 0.0127  0.0395  -0.0018 327 LEU A C   
2493  O O   . LEU A  327 ? 0.1982 0.2648 0.4023 0.0163  0.0386  0.0022  327 LEU A O   
2494  C CB  . LEU A  327 ? 0.1123 0.2000 0.3457 0.0137  0.0427  -0.0038 327 LEU A CB  
2495  C CG  . LEU A  327 ? 0.1216 0.1991 0.3505 0.0099  0.0524  -0.0038 327 LEU A CG  
2496  C CD1 . LEU A  327 ? 0.1254 0.2079 0.3669 0.0038  0.0570  -0.0083 327 LEU A CD1 
2497  C CD2 . LEU A  327 ? 0.1236 0.1993 0.3513 0.0125  0.0569  -0.0026 327 LEU A CD2 
2498  N N   . VAL A  328 ? 0.1737 0.2410 0.3862 0.0087  0.0417  -0.0042 328 VAL A N   
2499  C CA  . VAL A  328 ? 0.1631 0.2164 0.3621 0.0093  0.0432  -0.0019 328 VAL A CA  
2500  C C   . VAL A  328 ? 0.1535 0.1952 0.3497 0.0044  0.0509  -0.0026 328 VAL A C   
2501  O O   . VAL A  328 ? 0.1461 0.1913 0.3525 -0.0012 0.0543  -0.0066 328 VAL A O   
2502  C CB  . VAL A  328 ? 0.1303 0.1847 0.3269 0.0106  0.0381  -0.0035 328 VAL A CB  
2503  C CG1 . VAL A  328 ? 0.1211 0.1854 0.3185 0.0153  0.0316  -0.0020 328 VAL A CG1 
2504  C CG2 . VAL A  328 ? 0.1343 0.1922 0.3392 0.0054  0.0382  -0.0095 328 VAL A CG2 
2505  N N   . GLY A  329 ? 0.1785 0.2058 0.3607 0.0063  0.0535  0.0016  329 GLY A N   
2506  C CA  . GLY A  329 ? 0.1955 0.2091 0.3724 0.0019  0.0613  0.0020  329 GLY A CA  
2507  C C   . GLY A  329 ? 0.2771 0.2735 0.4366 0.0053  0.0622  0.0069  329 GLY A C   
2508  O O   . GLY A  329 ? 0.3482 0.3447 0.5010 0.0111  0.0564  0.0097  329 GLY A O   
2509  N N   . VAL A  330 ? 0.2592 0.2406 0.4116 0.0017  0.0692  0.0081  330 VAL A N   
2510  C CA  . VAL A  330 ? 0.2570 0.2203 0.3916 0.0055  0.0696  0.0132  330 VAL A CA  
2511  C C   . VAL A  330 ? 0.2726 0.2221 0.3965 0.0026  0.0786  0.0166  330 VAL A C   
2512  O O   . VAL A  330 ? 0.2247 0.1790 0.3572 -0.0032 0.0855  0.0142  330 VAL A O   
2513  C CB  . VAL A  330 ? 0.2155 0.1692 0.3485 0.0052  0.0690  0.0121  330 VAL A CB  
2514  C CG1 . VAL A  330 ? 0.2011 0.1679 0.3427 0.0083  0.0611  0.0085  330 VAL A CG1 
2515  C CG2 . VAL A  330 ? 0.2249 0.1737 0.3647 -0.0032 0.0767  0.0086  330 VAL A CG2 
2516  N N   . VAL A  331 ? 0.3521 0.2849 0.4571 0.0068  0.0786  0.0222  331 VAL A N   
2517  C CA  . VAL A  331 ? 0.3704 0.2865 0.4616 0.0038  0.0882  0.0259  331 VAL A CA  
2518  C C   . VAL A  331 ? 0.4083 0.3059 0.4930 0.0009  0.0934  0.0278  331 VAL A C   
2519  O O   . VAL A  331 ? 0.4225 0.3199 0.5123 0.0022  0.0888  0.0260  331 VAL A O   
2520  C CB  . VAL A  331 ? 0.2996 0.2060 0.3706 0.0099  0.0857  0.0312  331 VAL A CB  
2521  C CG1 . VAL A  331 ? 0.2553 0.1778 0.3329 0.0117  0.0818  0.0288  331 VAL A CG1 
2522  C CG2 . VAL A  331 ? 0.2766 0.1741 0.3363 0.0175  0.0767  0.0351  331 VAL A CG2 
2523  N N   . LYS A  332 ? 0.4001 0.2812 0.4725 -0.0029 0.1036  0.0315  332 LYS A N   
2524  C CA  . LYS A  332 ? 0.4710 0.3352 0.5410 -0.0083 0.1111  0.0326  332 LYS A CA  
2525  C C   . LYS A  332 ? 0.4789 0.3256 0.5345 -0.0017 0.1056  0.0369  332 LYS A C   
2526  O O   . LYS A  332 ? 0.4920 0.3328 0.5537 -0.0041 0.1061  0.0346  332 LYS A O   
2527  C CB  . LYS A  332 ? 0.6781 0.5278 0.7382 -0.0147 0.1251  0.0361  332 LYS A CB  
2528  C CG  . LYS A  332 ? 0.7107 0.5465 0.7749 -0.0232 0.1348  0.0356  332 LYS A CG  
2529  C CD  . LYS A  332 ? 0.7419 0.5582 0.7902 -0.0281 0.1491  0.0414  332 LYS A CD  
2530  C CE  . LYS A  332 ? 0.7631 0.5745 0.8254 -0.0401 0.1612  0.0386  332 LYS A CE  
2531  N NZ  . LYS A  332 ? 0.7765 0.5788 0.8438 -0.0416 0.1572  0.0366  332 LYS A NZ  
2532  N N   . ASP A  333 ? 0.5644 0.4024 0.6012 0.0067  0.1001  0.0428  333 ASP A N   
2533  C CA  . ASP A  333 ? 0.6222 0.4479 0.6490 0.0147  0.0927  0.0464  333 ASP A CA  
2534  C C   . ASP A  333 ? 0.6018 0.4420 0.6308 0.0235  0.0799  0.0460  333 ASP A C   
2535  O O   . ASP A  333 ? 0.6149 0.4527 0.6304 0.0285  0.0759  0.0500  333 ASP A O   
2536  C CB  . ASP A  333 ? 0.6757 0.4736 0.6766 0.0172  0.0973  0.0548  333 ASP A CB  
2537  C CG  . ASP A  333 ? 0.7185 0.5039 0.7150 0.0076  0.1121  0.0562  333 ASP A CG  
2538  O OD1 . ASP A  333 ? 0.7413 0.5332 0.7359 0.0043  0.1172  0.0559  333 ASP A OD1 
2539  O OD2 . ASP A  333 ? 0.7360 0.5051 0.7318 0.0030  0.1189  0.0572  333 ASP A OD2 
2540  N N   . GLU A  334 ? 0.4683 0.3220 0.5132 0.0254  0.0738  0.0413  334 GLU A N   
2541  C CA  . GLU A  334 ? 0.3932 0.2631 0.4442 0.0324  0.0630  0.0403  334 GLU A CA  
2542  C C   . GLU A  334 ? 0.4253 0.2839 0.4650 0.0419  0.0560  0.0452  334 GLU A C   
2543  O O   . GLU A  334 ? 0.4684 0.3339 0.5054 0.0482  0.0477  0.0471  334 GLU A O   
2544  C CB  . GLU A  334 ? 0.3859 0.2745 0.4573 0.0306  0.0603  0.0335  334 GLU A CB  
2545  C CG  . GLU A  334 ? 0.4291 0.3315 0.5136 0.0222  0.0651  0.0285  334 GLU A CG  
2546  C CD  . GLU A  334 ? 0.4679 0.3875 0.5576 0.0235  0.0608  0.0278  334 GLU A CD  
2547  O OE1 . GLU A  334 ? 0.5113 0.4365 0.5993 0.0301  0.0529  0.0295  334 GLU A OE1 
2548  O OE2 . GLU A  334 ? 0.4480 0.3756 0.5444 0.0179  0.0654  0.0254  334 GLU A OE2 
2549  N N   . GLY A  335 ? 0.4353 0.2760 0.4690 0.0431  0.0592  0.0471  335 GLY A N   
2550  C CA  . GLY A  335 ? 0.4636 0.2945 0.4901 0.0531  0.0523  0.0510  335 GLY A CA  
2551  C C   . GLY A  335 ? 0.4984 0.3150 0.5040 0.0595  0.0483  0.0587  335 GLY A C   
2552  O O   . GLY A  335 ? 0.4862 0.3074 0.4908 0.0685  0.0382  0.0608  335 GLY A O   
2553  N N   . SER A  336 ? 0.5509 0.3507 0.5399 0.0547  0.0562  0.0627  336 SER A N   
2554  C CA  . SER A  336 ? 0.5406 0.3194 0.5040 0.0606  0.0541  0.0709  336 SER A CA  
2555  C C   . SER A  336 ? 0.4722 0.2605 0.4301 0.0686  0.0418  0.0727  336 SER A C   
2556  O O   . SER A  336 ? 0.4717 0.2466 0.4142 0.0775  0.0347  0.0786  336 SER A O   
2557  C CB  . SER A  336 ? 0.5070 0.2683 0.4533 0.0529  0.0663  0.0745  336 SER A CB  
2558  O OG  . SER A  336 ? 0.4104 0.1882 0.3670 0.0445  0.0720  0.0693  336 SER A OG  
2559  N N   . TYR A  337 ? 0.4071 0.2180 0.3778 0.0658  0.0386  0.0676  337 TYR A N   
2560  C CA  . TYR A  337 ? 0.4878 0.3082 0.4550 0.0720  0.0269  0.0684  337 TYR A CA  
2561  C C   . TYR A  337 ? 0.5640 0.3897 0.5392 0.0821  0.0152  0.0694  337 TYR A C   
2562  O O   . TYR A  337 ? 0.5498 0.3687 0.5120 0.0901  0.0057  0.0738  337 TYR A O   
2563  C CB  . TYR A  337 ? 0.7051 0.5486 0.6873 0.0666  0.0263  0.0622  337 TYR A CB  
2564  C CG  . TYR A  337 ? 0.8350 0.6865 0.8122 0.0712  0.0152  0.0623  337 TYR A CG  
2565  C CD1 . TYR A  337 ? 0.8793 0.7410 0.8658 0.0788  0.0029  0.0623  337 TYR A CD1 
2566  C CD2 . TYR A  337 ? 0.8985 0.7475 0.8628 0.0678  0.0172  0.0618  337 TYR A CD2 
2567  C CE1 . TYR A  337 ? 0.9186 0.7880 0.9023 0.0822  -0.0079 0.0618  337 TYR A CE1 
2568  C CE2 . TYR A  337 ? 0.9520 0.8072 0.9113 0.0716  0.0065  0.0610  337 TYR A CE2 
2569  C CZ  . TYR A  337 ? 0.9682 0.8338 0.9378 0.0785  -0.0065 0.0610  337 TYR A CZ  
2570  O OH  . TYR A  337 ? 0.9901 0.8628 0.9570 0.0815  -0.0179 0.0595  337 TYR A OH  
2571  N N   . PHE A  338 ? 0.6715 0.5094 0.6679 0.0821  0.0158  0.0652  338 PHE A N   
2572  C CA  . PHE A  338 ? 0.6296 0.4778 0.6385 0.0911  0.0059  0.0648  338 PHE A CA  
2573  C C   . PHE A  338 ? 0.6583 0.4860 0.6559 0.0996  0.0039  0.0702  338 PHE A C   
2574  O O   . PHE A  338 ? 0.6876 0.5212 0.6934 0.1088  -0.0048 0.0709  338 PHE A O   
2575  C CB  . PHE A  338 ? 0.5003 0.3679 0.5339 0.0882  0.0084  0.0582  338 PHE A CB  
2576  C CG  . PHE A  338 ? 0.4863 0.3719 0.5305 0.0799  0.0111  0.0533  338 PHE A CG  
2577  C CD1 . PHE A  338 ? 0.4809 0.3628 0.5233 0.0707  0.0211  0.0511  338 PHE A CD1 
2578  C CD2 . PHE A  338 ? 0.4761 0.3821 0.5328 0.0813  0.0036  0.0511  338 PHE A CD2 
2579  C CE1 . PHE A  338 ? 0.4676 0.3657 0.5199 0.0641  0.0231  0.0469  338 PHE A CE1 
2580  C CE2 . PHE A  338 ? 0.4829 0.4034 0.5483 0.0741  0.0062  0.0471  338 PHE A CE2 
2581  C CZ  . PHE A  338 ? 0.4654 0.3820 0.5284 0.0661  0.0156  0.0451  338 PHE A CZ  
2582  N N   . LEU A  339 ? 0.5938 0.3973 0.5735 0.0965  0.0125  0.0742  339 LEU A N   
2583  C CA  . LEU A  339 ? 0.5986 0.3789 0.5659 0.1044  0.0118  0.0800  339 LEU A CA  
2584  C C   . LEU A  339 ? 0.6676 0.4398 0.6186 0.1150  -0.0001 0.0867  339 LEU A C   
2585  O O   . LEU A  339 ? 0.7012 0.4705 0.6553 0.1257  -0.0079 0.0891  339 LEU A O   
2586  C CB  . LEU A  339 ? 0.5200 0.2751 0.4712 0.0974  0.0246  0.0831  339 LEU A CB  
2587  C CG  . LEU A  339 ? 0.4857 0.2457 0.4540 0.0887  0.0346  0.0765  339 LEU A CG  
2588  C CD1 . LEU A  339 ? 0.5165 0.2501 0.4696 0.0820  0.0467  0.0800  339 LEU A CD1 
2589  C CD2 . LEU A  339 ? 0.4607 0.2269 0.4453 0.0957  0.0304  0.0730  339 LEU A CD2 
2590  N N   . VAL A  340 ? 0.7308 0.5000 0.6646 0.1125  -0.0020 0.0892  340 VAL A N   
2591  C CA  . VAL A  340 ? 0.7413 0.5018 0.6562 0.1221  -0.0141 0.0952  340 VAL A CA  
2592  C C   . VAL A  340 ? 0.6796 0.4649 0.6148 0.1297  -0.0290 0.0918  340 VAL A C   
2593  O O   . VAL A  340 ? 0.6790 0.4613 0.6052 0.1395  -0.0419 0.0957  340 VAL A O   
2594  C CB  . VAL A  340 ? 0.6833 0.4354 0.5744 0.1167  -0.0117 0.0972  340 VAL A CB  
2595  C CG1 . VAL A  340 ? 0.6791 0.4075 0.5523 0.1088  0.0044  0.1008  340 VAL A CG1 
2596  C CG2 . VAL A  340 ? 0.6594 0.4372 0.5670 0.1093  -0.0122 0.0896  340 VAL A CG2 
2597  N N   . TYR A  341 ? 0.4868 0.2962 0.4501 0.1252  -0.0266 0.0844  341 TYR A N   
2598  C CA  . TYR A  341 ? 0.4944 0.3303 0.4819 0.1297  -0.0371 0.0801  341 TYR A CA  
2599  C C   . TYR A  341 ? 0.5293 0.3686 0.5328 0.1397  -0.0412 0.0804  341 TYR A C   
2600  O O   . TYR A  341 ? 0.4949 0.3580 0.5236 0.1419  -0.0457 0.0757  341 TYR A O   
2601  C CB  . TYR A  341 ? 0.6858 0.5455 0.6927 0.1200  -0.0329 0.0728  341 TYR A CB  
2602  C CG  . TYR A  341 ? 0.7575 0.6231 0.7558 0.1163  -0.0384 0.0719  341 TYR A CG  
2603  C CD1 . TYR A  341 ? 0.8123 0.6597 0.7850 0.1117  -0.0333 0.0748  341 TYR A CD1 
2604  C CD2 . TYR A  341 ? 0.7662 0.6546 0.7816 0.1172  -0.0483 0.0680  341 TYR A CD2 
2605  C CE1 . TYR A  341 ? 0.8399 0.6912 0.8033 0.1087  -0.0378 0.0733  341 TYR A CE1 
2606  C CE2 . TYR A  341 ? 0.7902 0.6822 0.7971 0.1137  -0.0535 0.0666  341 TYR A CE2 
2607  C CZ  . TYR A  341 ? 0.8495 0.7224 0.8295 0.1098  -0.0484 0.0691  341 TYR A CZ  
2608  O OH  . TYR A  341 ? 0.9118 0.7866 0.8814 0.1066  -0.0529 0.0670  341 TYR A OH  
2609  N N   . GLY A  342 ? 0.7621 0.5768 0.7505 0.1458  -0.0388 0.0860  342 GLY A N   
2610  C CA  . GLY A  342 ? 0.7573 0.5711 0.7582 0.1564  -0.0420 0.0867  342 GLY A CA  
2611  C C   . GLY A  342 ? 0.7075 0.5075 0.7110 0.1552  -0.0315 0.0856  342 GLY A C   
2612  O O   . GLY A  342 ? 0.7180 0.5254 0.7379 0.1609  -0.0343 0.0831  342 GLY A O   
2613  N N   . VAL A  343 ? 0.5541 0.3344 0.5424 0.1473  -0.0193 0.0869  343 VAL A N   
2614  C CA  . VAL A  343 ? 0.5390 0.2964 0.5193 0.1468  -0.0118 0.0884  343 VAL A CA  
2615  C C   . VAL A  343 ? 0.5668 0.3005 0.5209 0.1500  -0.0158 0.0970  343 VAL A C   
2616  O O   . VAL A  343 ? 0.5890 0.3115 0.5220 0.1457  -0.0137 0.1015  343 VAL A O   
2617  C CB  . VAL A  343 ? 0.5659 0.3137 0.5449 0.1355  0.0036  0.0852  343 VAL A CB  
2618  C CG1 . VAL A  343 ? 0.4932 0.2140 0.4602 0.1334  0.0111  0.0873  343 VAL A CG1 
2619  C CG2 . VAL A  343 ? 0.5405 0.3141 0.5462 0.1311  0.0063  0.0756  343 VAL A CG2 
2620  N N   . PRO A  344 ? 0.6146 0.3409 0.5699 0.1579  -0.0212 0.0994  344 PRO A N   
2621  C CA  . PRO A  344 ? 0.6481 0.3524 0.5796 0.1621  -0.0251 0.1081  344 PRO A CA  
2622  C C   . PRO A  344 ? 0.7051 0.3805 0.6133 0.1537  -0.0123 0.1121  344 PRO A C   
2623  O O   . PRO A  344 ? 0.6950 0.3641 0.6097 0.1468  -0.0010 0.1079  344 PRO A O   
2624  C CB  . PRO A  344 ? 0.5727 0.2774 0.5174 0.1717  -0.0310 0.1083  344 PRO A CB  
2625  C CG  . PRO A  344 ? 0.5409 0.2749 0.5161 0.1746  -0.0350 0.1005  344 PRO A CG  
2626  C CD  . PRO A  344 ? 0.5153 0.2564 0.4958 0.1646  -0.0249 0.0943  344 PRO A CD  
2627  N N   . GLY A  345 ? 0.8551 0.5135 0.7365 0.1540  -0.0139 0.1199  345 GLY A N   
2628  C CA  . GLY A  345 ? 0.9137 0.5456 0.7722 0.1455  -0.0012 0.1243  345 GLY A CA  
2629  C C   . GLY A  345 ? 0.9275 0.5610 0.7745 0.1364  0.0056  0.1241  345 GLY A C   
2630  O O   . GLY A  345 ? 1.0066 0.6202 0.8313 0.1297  0.0152  0.1287  345 GLY A O   
2631  N N   . PHE A  346 ? 0.5961 0.2536 0.4588 0.1363  0.0011  0.1186  346 PHE A N   
2632  C CA  . PHE A  346 ? 0.5971 0.2576 0.4531 0.1276  0.0086  0.1172  346 PHE A CA  
2633  C C   . PHE A  346 ? 0.6606 0.3275 0.5020 0.1318  -0.0017 0.1197  346 PHE A C   
2634  O O   . PHE A  346 ? 0.6304 0.3193 0.4870 0.1378  -0.0138 0.1162  346 PHE A O   
2635  C CB  . PHE A  346 ? 0.7501 0.4304 0.6332 0.1222  0.0143  0.1089  346 PHE A CB  
2636  C CG  . PHE A  346 ? 0.7611 0.4322 0.6532 0.1138  0.0278  0.1056  346 PHE A CG  
2637  C CD1 . PHE A  346 ? 0.7480 0.4198 0.6549 0.1179  0.0260  0.1025  346 PHE A CD1 
2638  C CD2 . PHE A  346 ? 0.7488 0.4125 0.6360 0.1010  0.0420  0.1046  346 PHE A CD2 
2639  C CE1 . PHE A  346 ? 0.7226 0.3852 0.6367 0.1099  0.0375  0.0986  346 PHE A CE1 
2640  C CE2 . PHE A  346 ? 0.7173 0.3726 0.6139 0.0928  0.0536  0.1011  346 PHE A CE2 
2641  C CZ  . PHE A  346 ? 0.7103 0.3649 0.6196 0.0971  0.0509  0.0978  346 PHE A CZ  
2642  N N   . SER A  347 ? 1.0634 0.7113 0.8758 0.1280  0.0037  0.1253  347 SER A N   
2643  C CA  . SER A  347 ? 1.0828 0.7329 0.8763 0.1305  -0.0041 0.1272  347 SER A CA  
2644  C C   . SER A  347 ? 1.0614 0.7042 0.8415 0.1199  0.0099  0.1268  347 SER A C   
2645  O O   . SER A  347 ? 1.0919 0.7253 0.8741 0.1105  0.0259  0.1265  347 SER A O   
2646  C CB  . SER A  347 ? 0.9891 0.6220 0.7554 0.1376  -0.0122 0.1346  347 SER A CB  
2647  O OG  . SER A  347 ? 0.9991 0.6273 0.7401 0.1374  -0.0155 0.1364  347 SER A OG  
2648  N N   . LYS A  348 ? 0.7832 0.4369 0.5551 0.1193  0.0038  0.1243  348 LYS A N   
2649  C CA  . LYS A  348 ? 0.7760 0.4269 0.5361 0.1084  0.0168  0.1225  348 LYS A CA  
2650  C C   . LYS A  348 ? 0.8304 0.4476 0.5478 0.1105  0.0222  0.1323  348 LYS A C   
2651  O O   . LYS A  348 ? 0.7881 0.3958 0.4913 0.1017  0.0367  0.1328  348 LYS A O   
2652  C CB  . LYS A  348 ? 0.8086 0.4848 0.5782 0.1064  0.0090  0.1148  348 LYS A CB  
2653  C CG  . LYS A  348 ? 0.8226 0.4921 0.5662 0.1154  -0.0061 0.1180  348 LYS A CG  
2654  C CD  . LYS A  348 ? 0.7516 0.4410 0.5003 0.1112  -0.0105 0.1101  348 LYS A CD  
2655  C CE  . LYS A  348 ? 0.7265 0.4076 0.4470 0.1192  -0.0253 0.1124  348 LYS A CE  
2656  N NZ  . LYS A  348 ? 0.7378 0.3872 0.4149 0.1198  -0.0175 0.1200  348 LYS A NZ  
2657  N N   . ASP A  349 ? 1.1092 0.7154 0.8118 0.1204  0.0104  0.1379  349 ASP A N   
2658  C CA  . ASP A  349 ? 1.1640 0.7483 0.8299 0.1225  0.0107  0.1445  349 ASP A CA  
2659  C C   . ASP A  349 ? 1.2351 0.7969 0.8900 0.1183  0.0241  0.1503  349 ASP A C   
2660  O O   . ASP A  349 ? 1.3300 0.8712 0.9539 0.1191  0.0273  0.1563  349 ASP A O   
2661  C CB  . ASP A  349 ? 0.9736 0.5623 0.6314 0.1349  -0.0109 0.1461  349 ASP A CB  
2662  C CG  . ASP A  349 ? 0.9330 0.5444 0.6019 0.1384  -0.0251 0.1398  349 ASP A CG  
2663  O OD1 . ASP A  349 ? 0.9155 0.5267 0.5725 0.1333  -0.0201 0.1372  349 ASP A OD1 
2664  O OD2 . ASP A  349 ? 0.9250 0.5551 0.6159 0.1459  -0.0408 0.1370  349 ASP A OD2 
2665  N N   . ASN A  350 ? 0.8956 0.4608 0.5756 0.1138  0.0319  0.1483  350 ASN A N   
2666  C CA  . ASN A  350 ? 0.8929 0.4380 0.5671 0.1089  0.0445  0.1527  350 ASN A CA  
2667  C C   . ASN A  350 ? 0.8426 0.3951 0.5453 0.0988  0.0576  0.1472  350 ASN A C   
2668  O O   . ASN A  350 ? 0.7682 0.3418 0.4966 0.0977  0.0547  0.1405  350 ASN A O   
2669  C CB  . ASN A  350 ? 1.0542 0.5894 0.7236 0.1193  0.0331  0.1579  350 ASN A CB  
2670  C CG  . ASN A  350 ? 1.0984 0.6541 0.7981 0.1270  0.0194  0.1534  350 ASN A CG  
2671  O OD1 . ASN A  350 ? 1.1084 0.6712 0.8335 0.1229  0.0252  0.1489  350 ASN A OD1 
2672  N ND2 . ASN A  350 ? 1.1277 0.6936 0.8255 0.1380  0.0013  0.1540  350 ASN A ND2 
2673  N N   . GLU A  351 ? 1.0802 0.6154 0.7782 0.0912  0.0718  0.1499  351 GLU A N   
2674  C CA  . GLU A  351 ? 1.0885 0.6290 0.8106 0.0795  0.0859  0.1444  351 GLU A CA  
2675  C C   . GLU A  351 ? 1.0130 0.5685 0.7660 0.0823  0.0788  0.1384  351 GLU A C   
2676  O O   . GLU A  351 ? 1.0009 0.5653 0.7766 0.0733  0.0878  0.1322  351 GLU A O   
2677  C CB  . GLU A  351 ? 1.2649 0.7826 0.9754 0.0721  0.0999  0.1487  351 GLU A CB  
2678  C CG  . GLU A  351 ? 1.3200 0.8378 1.0332 0.0578  0.1188  0.1460  351 GLU A CG  
2679  C CD  . GLU A  351 ? 1.4079 0.9082 1.1209 0.0495  0.1320  0.1480  351 GLU A CD  
2680  O OE1 . GLU A  351 ? 1.4356 0.9146 1.1281 0.0550  0.1297  0.1553  351 GLU A OE1 
2681  O OE2 . GLU A  351 ? 1.4430 0.9515 1.1774 0.0375  0.1440  0.1419  351 GLU A OE2 
2682  N N   . SER A  352 ? 0.8768 0.4357 0.6311 0.0949  0.0627  0.1400  352 SER A N   
2683  C CA  . SER A  352 ? 0.8256 0.3997 0.6083 0.0992  0.0553  0.1343  352 SER A CA  
2684  C C   . SER A  352 ? 0.8589 0.4242 0.6549 0.0919  0.0660  0.1315  352 SER A C   
2685  O O   . SER A  352 ? 0.8041 0.3822 0.6226 0.0846  0.0722  0.1240  352 SER A O   
2686  C CB  . SER A  352 ? 0.7868 0.3871 0.5911 0.0979  0.0523  0.1269  352 SER A CB  
2687  O OG  . SER A  352 ? 0.7829 0.3927 0.5777 0.1059  0.0397  0.1286  352 SER A OG  
2688  N N   . LEU A  353 ? 1.1889 0.7318 0.9704 0.0937  0.0681  0.1373  353 LEU A N   
2689  C CA  . LEU A  353 ? 1.1641 0.6975 0.9582 0.0891  0.0750  0.1345  353 LEU A CA  
2690  C C   . LEU A  353 ? 1.1552 0.6937 0.9611 0.1017  0.0614  0.1334  353 LEU A C   
2691  O O   . LEU A  353 ? 1.2159 0.7548 1.0117 0.1132  0.0489  0.1384  353 LEU A O   
2692  C CB  . LEU A  353 ? 0.8183 0.3239 0.5908 0.0840  0.0854  0.1415  353 LEU A CB  
2693  C CG  . LEU A  353 ? 0.7962 0.2979 0.5553 0.0728  0.0988  0.1431  353 LEU A CG  
2694  C CD1 . LEU A  353 ? 0.8397 0.3140 0.5722 0.0706  0.1071  0.1518  353 LEU A CD1 
2695  C CD2 . LEU A  353 ? 0.7464 0.2598 0.5286 0.0588  0.1113  0.1346  353 LEU A CD2 
2696  N N   . ILE A  354 ? 0.9155 0.4598 0.7439 0.0997  0.0633  0.1262  354 ILE A N   
2697  C CA  . ILE A  354 ? 0.8646 0.4173 0.7074 0.1116  0.0513  0.1237  354 ILE A CA  
2698  C C   . ILE A  354 ? 0.8826 0.4207 0.7329 0.1111  0.0555  0.1211  354 ILE A C   
2699  O O   . ILE A  354 ? 0.8814 0.4101 0.7347 0.0996  0.0676  0.1176  354 ILE A O   
2700  C CB  . ILE A  354 ? 0.6987 0.2811 0.5655 0.1137  0.0454  0.1154  354 ILE A CB  
2701  C CG1 . ILE A  354 ? 0.6547 0.2437 0.5390 0.1020  0.0566  0.1065  354 ILE A CG1 
2702  C CG2 . ILE A  354 ? 0.6490 0.2453 0.5087 0.1149  0.0402  0.1177  354 ILE A CG2 
2703  C CD1 . ILE A  354 ? 0.5989 0.2136 0.5079 0.1055  0.0512  0.0981  354 ILE A CD1 
2704  N N   . SER A  355 ? 0.8614 0.3980 0.7160 0.1235  0.0452  0.1225  355 SER A N   
2705  C CA  . SER A  355 ? 0.8827 0.4046 0.7440 0.1243  0.0484  0.1199  355 SER A CA  
2706  C C   . SER A  355 ? 0.8536 0.3915 0.7396 0.1205  0.0513  0.1081  355 SER A C   
2707  O O   . SER A  355 ? 0.8309 0.3919 0.7294 0.1183  0.0500  0.1028  355 SER A O   
2708  C CB  . SER A  355 ? 0.9323 0.4483 0.7920 0.1395  0.0368  0.1247  355 SER A CB  
2709  O OG  . SER A  355 ? 0.9046 0.4464 0.7807 0.1496  0.0245  0.1215  355 SER A OG  
2710  N N   . ARG A  356 ? 0.8345 0.3596 0.7270 0.1201  0.0550  0.1039  356 ARG A N   
2711  C CA  . ARG A  356 ? 0.7715 0.3097 0.6851 0.1167  0.0578  0.0923  356 ARG A CA  
2712  C C   . ARG A  356 ? 0.7486 0.3097 0.6780 0.1293  0.0466  0.0887  356 ARG A C   
2713  O O   . ARG A  356 ? 0.6995 0.2834 0.6437 0.1273  0.0462  0.0817  356 ARG A O   
2714  C CB  . ARG A  356 ? 0.7965 0.3140 0.7116 0.1136  0.0640  0.0883  356 ARG A CB  
2715  C CG  . ARG A  356 ? 0.7444 0.2738 0.6786 0.1091  0.0675  0.0755  356 ARG A CG  
2716  C CD  . ARG A  356 ? 0.7543 0.2676 0.6874 0.0946  0.0792  0.0708  356 ARG A CD  
2717  N NE  . ARG A  356 ? 0.7629 0.2893 0.7137 0.0905  0.0815  0.0581  356 ARG A NE  
2718  C CZ  . ARG A  356 ? 0.7552 0.3005 0.7163 0.0815  0.0850  0.0520  356 ARG A CZ  
2719  N NH1 . ARG A  356 ? 0.7683 0.3212 0.7246 0.0754  0.0873  0.0573  356 ARG A NH1 
2720  N NH2 . ARG A  356 ? 0.7192 0.2752 0.6951 0.0787  0.0863  0.0404  356 ARG A NH2 
2721  N N   . ALA A  357 ? 0.9216 0.4773 0.8487 0.1422  0.0375  0.0936  357 ALA A N   
2722  C CA  . ALA A  357 ? 0.9657 0.5440 0.9102 0.1546  0.0266  0.0905  357 ALA A CA  
2723  C C   . ALA A  357 ? 0.9794 0.5841 0.9297 0.1543  0.0215  0.0903  357 ALA A C   
2724  O O   . ALA A  357 ? 0.9968 0.6260 0.9665 0.1582  0.0175  0.0835  357 ALA A O   
2725  C CB  . ALA A  357 ? 0.9106 0.4794 0.8501 0.1675  0.0174  0.0981  357 ALA A CB  
2726  N N   . GLN A  358 ? 0.9417 0.5405 0.8745 0.1494  0.0224  0.0977  358 GLN A N   
2727  C CA  . GLN A  358 ? 0.8547 0.4744 0.7891 0.1477  0.0184  0.0982  358 GLN A CA  
2728  C C   . GLN A  358 ? 0.7650 0.3990 0.7116 0.1377  0.0265  0.0898  358 GLN A C   
2729  O O   . GLN A  358 ? 0.7352 0.3939 0.6951 0.1394  0.0220  0.0862  358 GLN A O   
2730  C CB  . GLN A  358 ? 0.7170 0.3227 0.6265 0.1440  0.0195  0.1075  358 GLN A CB  
2731  C CG  . GLN A  358 ? 0.6960 0.3144 0.6012 0.1529  0.0066  0.1128  358 GLN A CG  
2732  C CD  . GLN A  358 ? 0.7116 0.3083 0.5892 0.1548  0.0049  0.1233  358 GLN A CD  
2733  O OE1 . GLN A  358 ? 0.7147 0.2927 0.5736 0.1456  0.0153  0.1268  358 GLN A OE1 
2734  N NE2 . GLN A  358 ? 0.7280 0.3273 0.6032 0.1667  -0.0078 0.1284  358 GLN A NE2 
2735  N N   . PHE A  359 ? 0.6015 0.2205 0.5446 0.1268  0.0384  0.0868  359 PHE A N   
2736  C CA  . PHE A  359 ? 0.5749 0.2070 0.5314 0.1169  0.0463  0.0783  359 PHE A CA  
2737  C C   . PHE A  359 ? 0.5539 0.2045 0.5321 0.1224  0.0432  0.0690  359 PHE A C   
2738  O O   . PHE A  359 ? 0.5244 0.1978 0.5165 0.1207  0.0429  0.0639  359 PHE A O   
2739  C CB  . PHE A  359 ? 0.5889 0.2018 0.5393 0.1035  0.0591  0.0763  359 PHE A CB  
2740  C CG  . PHE A  359 ? 0.6697 0.2957 0.6369 0.0937  0.0662  0.0662  359 PHE A CG  
2741  C CD1 . PHE A  359 ? 0.5396 0.1824 0.5126 0.0868  0.0689  0.0648  359 PHE A CD1 
2742  C CD2 . PHE A  359 ? 0.5669 0.1883 0.5440 0.0917  0.0697  0.0577  359 PHE A CD2 
2743  C CE1 . PHE A  359 ? 0.5177 0.1733 0.5073 0.0781  0.0746  0.0555  359 PHE A CE1 
2744  C CE2 . PHE A  359 ? 0.5457 0.1796 0.5378 0.0829  0.0752  0.0481  359 PHE A CE2 
2745  C CZ  . PHE A  359 ? 0.5210 0.1723 0.5198 0.0761  0.0774  0.0471  359 PHE A CZ  
2746  N N   . LEU A  360 ? 0.6107 0.2512 0.5916 0.1291  0.0414  0.0669  360 LEU A N   
2747  C CA  . LEU A  360 ? 0.6203 0.2765 0.6199 0.1350  0.0394  0.0579  360 LEU A CA  
2748  C C   . LEU A  360 ? 0.6086 0.2924 0.6207 0.1442  0.0296  0.0583  360 LEU A C   
2749  O O   . LEU A  360 ? 0.5634 0.2699 0.5913 0.1434  0.0305  0.0514  360 LEU A O   
2750  C CB  . LEU A  360 ? 0.6544 0.2929 0.6528 0.1422  0.0385  0.0568  360 LEU A CB  
2751  C CG  . LEU A  360 ? 0.6712 0.2786 0.6547 0.1346  0.0463  0.0590  360 LEU A CG  
2752  C CD1 . LEU A  360 ? 0.6978 0.2890 0.6817 0.1432  0.0444  0.0578  360 LEU A CD1 
2753  C CD2 . LEU A  360 ? 0.6493 0.2541 0.6352 0.1200  0.0571  0.0515  360 LEU A CD2 
2754  N N   . ALA A  361 ? 0.5986 0.2807 0.6041 0.1524  0.0203  0.0665  361 ALA A N   
2755  C CA  . ALA A  361 ? 0.5269 0.2342 0.5446 0.1608  0.0096  0.0674  361 ALA A CA  
2756  C C   . ALA A  361 ? 0.4987 0.2250 0.5205 0.1539  0.0110  0.0660  361 ALA A C   
2757  O O   . ALA A  361 ? 0.5385 0.2907 0.5777 0.1565  0.0075  0.0613  361 ALA A O   
2758  C CB  . ALA A  361 ? 0.9610 0.6601 0.9676 0.1679  0.0002  0.0771  361 ALA A CB  
2759  N N   . GLY A  362 ? 0.5815 0.2944 0.5873 0.1447  0.0170  0.0701  362 GLY A N   
2760  C CA  . GLY A  362 ? 0.5526 0.2801 0.5610 0.1372  0.0198  0.0692  362 GLY A CA  
2761  C C   . GLY A  362 ? 0.5433 0.2883 0.5707 0.1324  0.0260  0.0599  362 GLY A C   
2762  O O   . GLY A  362 ? 0.5558 0.3258 0.5974 0.1334  0.0226  0.0573  362 GLY A O   
2763  N N   . VAL A  363 ? 0.4616 0.1936 0.4894 0.1268  0.0348  0.0546  363 VAL A N   
2764  C CA  . VAL A  363 ? 0.4405 0.1871 0.4848 0.1222  0.0404  0.0452  363 VAL A CA  
2765  C C   . VAL A  363 ? 0.4240 0.1947 0.4855 0.1315  0.0342  0.0408  363 VAL A C   
2766  O O   . VAL A  363 ? 0.3992 0.1917 0.4747 0.1282  0.0358  0.0355  363 VAL A O   
2767  C CB  . VAL A  363 ? 0.4690 0.1954 0.5098 0.1161  0.0490  0.0395  363 VAL A CB  
2768  C CG1 . VAL A  363 ? 0.4410 0.1818 0.4977 0.1153  0.0523  0.0289  363 VAL A CG1 
2769  C CG2 . VAL A  363 ? 0.4639 0.1752 0.4949 0.1030  0.0572  0.0412  363 VAL A CG2 
2770  N N   . ARG A  364 ? 0.4381 0.2064 0.4993 0.1424  0.0271  0.0430  364 ARG A N   
2771  C CA  . ARG A  364 ? 0.4227 0.2159 0.5015 0.1507  0.0213  0.0391  364 ARG A CA  
2772  C C   . ARG A  364 ? 0.4810 0.2986 0.5680 0.1505  0.0149  0.0420  364 ARG A C   
2773  O O   . ARG A  364 ? 0.3779 0.2205 0.4814 0.1511  0.0142  0.0373  364 ARG A O   
2774  C CB  . ARG A  364 ? 0.4427 0.2301 0.5224 0.1626  0.0140  0.0407  364 ARG A CB  
2775  C CG  . ARG A  364 ? 0.5848 0.3505 0.6595 0.1648  0.0193  0.0370  364 ARG A CG  
2776  C CD  . ARG A  364 ? 0.5519 0.3173 0.6299 0.1570  0.0298  0.0282  364 ARG A CD  
2777  N NE  . ARG A  364 ? 0.5039 0.2946 0.5988 0.1603  0.0306  0.0209  364 ARG A NE  
2778  C CZ  . ARG A  364 ? 0.5272 0.3184 0.6285 0.1674  0.0321  0.0147  364 ARG A CZ  
2779  N NH1 . ARG A  364 ? 0.5665 0.3342 0.6599 0.1721  0.0322  0.0149  364 ARG A NH1 
2780  N NH2 . ARG A  364 ? 0.5144 0.3290 0.6297 0.1696  0.0340  0.0085  364 ARG A NH2 
2781  N N   . ILE A  365 ? 0.6326 0.4421 0.7070 0.1494  0.0104  0.0497  365 ILE A N   
2782  C CA  . ILE A  365 ? 0.5903 0.4208 0.6710 0.1497  0.0032  0.0525  365 ILE A CA  
2783  C C   . ILE A  365 ? 0.6027 0.4479 0.6900 0.1390  0.0090  0.0493  365 ILE A C   
2784  O O   . ILE A  365 ? 0.6273 0.4981 0.7298 0.1382  0.0056  0.0464  365 ILE A O   
2785  C CB  . ILE A  365 ? 0.5198 0.3368 0.5828 0.1521  -0.0040 0.0613  365 ILE A CB  
2786  C CG1 . ILE A  365 ? 0.4290 0.2374 0.4898 0.1625  -0.0128 0.0645  365 ILE A CG1 
2787  C CG2 . ILE A  365 ? 0.3875 0.2245 0.4557 0.1507  -0.0104 0.0632  365 ILE A CG2 
2788  C CD1 . ILE A  365 ? 0.4355 0.2488 0.4921 0.1676  -0.0250 0.0710  365 ILE A CD1 
2789  N N   . GLY A  366 ? 0.4379 0.2686 0.5131 0.1286  0.0167  0.0485  366 GLY A N   
2790  C CA  . GLY A  366 ? 0.3472 0.1913 0.4258 0.1160  0.0210  0.0443  366 GLY A CA  
2791  C C   . GLY A  366 ? 0.3294 0.1891 0.4230 0.1122  0.0258  0.0357  366 GLY A C   
2792  O O   . GLY A  366 ? 0.3078 0.1870 0.4093 0.1057  0.0257  0.0327  366 GLY A O   
2793  N N   . VAL A  367 ? 0.4392 0.2892 0.5352 0.1163  0.0299  0.0317  367 VAL A N   
2794  C CA  . VAL A  367 ? 0.4277 0.2915 0.5358 0.1142  0.0341  0.0233  367 VAL A CA  
2795  C C   . VAL A  367 ? 0.4300 0.3011 0.5492 0.1269  0.0314  0.0226  367 VAL A C   
2796  O O   . VAL A  367 ? 0.4339 0.2919 0.5525 0.1326  0.0352  0.0194  367 VAL A O   
2797  C CB  . VAL A  367 ? 0.5173 0.3636 0.6190 0.1077  0.0421  0.0172  367 VAL A CB  
2798  C CG1 . VAL A  367 ? 0.3218 0.1847 0.4310 0.0995  0.0454  0.0091  367 VAL A CG1 
2799  C CG2 . VAL A  367 ? 0.3533 0.1793 0.4412 0.0999  0.0449  0.0209  367 VAL A CG2 
2800  N N   . PRO A  368 ? 0.3251 0.2170 0.4552 0.1315  0.0250  0.0254  368 PRO A N   
2801  C CA  . PRO A  368 ? 0.3912 0.2934 0.5307 0.1422  0.0195  0.0256  368 PRO A CA  
2802  C C   . PRO A  368 ? 0.4354 0.3509 0.5863 0.1446  0.0244  0.0180  368 PRO A C   
2803  O O   . PRO A  368 ? 0.4287 0.3469 0.5842 0.1533  0.0221  0.0164  368 PRO A O   
2804  C CB  . PRO A  368 ? 0.3166 0.2386 0.4632 0.1419  0.0113  0.0298  368 PRO A CB  
2805  C CG  . PRO A  368 ? 0.3213 0.2486 0.4665 0.1308  0.0146  0.0298  368 PRO A CG  
2806  C CD  . PRO A  368 ? 0.2921 0.2041 0.4269 0.1232  0.0229  0.0255  368 PRO A CD  
2807  N N   . GLN A  369 ? 0.5326 0.4563 0.6876 0.1373  0.0311  0.0133  369 GLN A N   
2808  C CA  . GLN A  369 ? 0.5388 0.4742 0.7017 0.1386  0.0368  0.0062  369 GLN A CA  
2809  C C   . GLN A  369 ? 0.5572 0.4720 0.7115 0.1385  0.0442  0.0001  369 GLN A C   
2810  O O   . GLN A  369 ? 0.5978 0.5179 0.7552 0.1392  0.0501  -0.0068 369 GLN A O   
2811  C CB  . GLN A  369 ? 0.5958 0.5511 0.7663 0.1311  0.0392  0.0045  369 GLN A CB  
2812  C CG  . GLN A  369 ? 0.6638 0.6185 0.8273 0.1212  0.0357  0.0083  369 GLN A CG  
2813  C CD  . GLN A  369 ? 0.6660 0.6012 0.8147 0.1132  0.0392  0.0057  369 GLN A CD  
2814  O OE1 . GLN A  369 ? 0.6645 0.5788 0.8042 0.1154  0.0391  0.0078  369 GLN A OE1 
2815  N NE2 . GLN A  369 ? 0.6459 0.5879 0.7925 0.1039  0.0420  0.0014  369 GLN A NE2 
2816  N N   . ALA A  370 ? 0.5291 0.4195 0.6715 0.1369  0.0444  0.0025  370 ALA A N   
2817  C CA  . ALA A  370 ? 0.5176 0.3857 0.6509 0.1353  0.0509  -0.0036 370 ALA A CA  
2818  C C   . ALA A  370 ? 0.5412 0.3977 0.6716 0.1453  0.0498  -0.0046 370 ALA A C   
2819  O O   . ALA A  370 ? 0.5197 0.3697 0.6471 0.1511  0.0435  0.0019  370 ALA A O   
2820  C CB  . ALA A  370 ? 0.3738 0.2221 0.4932 0.1258  0.0511  -0.0010 370 ALA A CB  
2821  N N   . SER A  371 ? 0.5987 0.4521 0.7293 0.1476  0.0557  -0.0131 371 SER A N   
2822  C CA  . SER A  371 ? 0.6810 0.5220 0.8091 0.1570  0.0556  -0.0154 371 SER A CA  
2823  C C   . SER A  371 ? 0.7335 0.5429 0.8474 0.1547  0.0563  -0.0141 371 SER A C   
2824  O O   . SER A  371 ? 0.7660 0.5647 0.8727 0.1453  0.0577  -0.0119 371 SER A O   
2825  C CB  . SER A  371 ? 0.7683 0.6134 0.8986 0.1590  0.0628  -0.0257 371 SER A CB  
2826  O OG  . SER A  371 ? 0.8060 0.6407 0.9288 0.1494  0.0689  -0.0322 371 SER A OG  
2827  N N   . ASP A  372 ? 0.7164 0.5108 0.8269 0.1628  0.0556  -0.0156 372 ASP A N   
2828  C CA  . ASP A  372 ? 0.7358 0.4988 0.8326 0.1596  0.0578  -0.0158 372 ASP A CA  
2829  C C   . ASP A  372 ? 0.6981 0.4537 0.7905 0.1502  0.0658  -0.0255 372 ASP A C   
2830  O O   . ASP A  372 ? 0.6940 0.4660 0.7930 0.1504  0.0694  -0.0328 372 ASP A O   
2831  C CB  . ASP A  372 ? 0.8286 0.5781 0.9243 0.1707  0.0558  -0.0169 372 ASP A CB  
2832  C CG  . ASP A  372 ? 0.8371 0.6021 0.9428 0.1820  0.0475  -0.0108 372 ASP A CG  
2833  O OD1 . ASP A  372 ? 0.8108 0.6027 0.9274 0.1824  0.0449  -0.0092 372 ASP A OD1 
2834  O OD2 . ASP A  372 ? 0.8552 0.6057 0.9588 0.1901  0.0432  -0.0078 372 ASP A OD2 
2835  N N   . LEU A  373 ? 0.7565 0.4886 0.8381 0.1412  0.0685  -0.0257 373 LEU A N   
2836  C CA  . LEU A  373 ? 0.7703 0.4939 0.8480 0.1303  0.0750  -0.0356 373 LEU A CA  
2837  C C   . LEU A  373 ? 0.6785 0.4217 0.7629 0.1215  0.0761  -0.0365 373 LEU A C   
2838  O O   . LEU A  373 ? 0.6951 0.4309 0.7769 0.1098  0.0795  -0.0417 373 LEU A O   
2839  C CB  . LEU A  373 ? 0.6491 0.3704 0.7264 0.1351  0.0789  -0.0472 373 LEU A CB  
2840  C CG  . LEU A  373 ? 0.6002 0.3177 0.6741 0.1253  0.0844  -0.0598 373 LEU A CG  
2841  C CD1 . LEU A  373 ? 0.6255 0.3220 0.6912 0.1279  0.0874  -0.0689 373 LEU A CD1 
2842  C CD2 . LEU A  373 ? 0.5424 0.2866 0.6239 0.1261  0.0861  -0.0648 373 LEU A CD2 
2843  N N   . ALA A  374 ? 0.4586 0.2267 0.5525 0.1264  0.0725  -0.0311 374 ALA A N   
2844  C CA  . ALA A  374 ? 0.4155 0.2026 0.5134 0.1167  0.0707  -0.0293 374 ALA A CA  
2845  C C   . ALA A  374 ? 0.4336 0.2067 0.5253 0.1129  0.0684  -0.0199 374 ALA A C   
2846  O O   . ALA A  374 ? 0.4513 0.2214 0.5387 0.1006  0.0691  -0.0201 374 ALA A O   
2847  C CB  . ALA A  374 ? 0.4339 0.2507 0.5432 0.1225  0.0671  -0.0260 374 ALA A CB  
2848  N N   . ALA A  375 ? 0.4323 0.1973 0.5220 0.1232  0.0650  -0.0120 375 ALA A N   
2849  C CA  . ALA A  375 ? 0.4407 0.1926 0.5215 0.1213  0.0621  -0.0020 375 ALA A CA  
2850  C C   . ALA A  375 ? 0.5405 0.2620 0.6086 0.1154  0.0663  -0.0029 375 ALA A C   
2851  O O   . ALA A  375 ? 0.4741 0.1837 0.5345 0.1075  0.0679  0.0024  375 ALA A O   
2852  C CB  . ALA A  375 ? 0.4440 0.2015 0.5253 0.1332  0.0541  0.0059  375 ALA A CB  
2853  N N   . GLU A  376 ? 0.6150 0.3239 0.6809 0.1189  0.0686  -0.0097 376 GLU A N   
2854  C CA  . GLU A  376 ? 0.6757 0.3559 0.7308 0.1121  0.0728  -0.0117 376 GLU A CA  
2855  C C   . GLU A  376 ? 0.6158 0.2947 0.6724 0.0967  0.0786  -0.0184 376 GLU A C   
2856  O O   . GLU A  376 ? 0.6449 0.3044 0.6942 0.0868  0.0822  -0.0175 376 GLU A O   
2857  C CB  . GLU A  376 ? 1.0149 0.6823 1.0681 0.1195  0.0736  -0.0184 376 GLU A CB  
2858  C CG  . GLU A  376 ? 1.1589 0.7953 1.2010 0.1134  0.0771  -0.0194 376 GLU A CG  
2859  C CD  . GLU A  376 ? 1.2726 0.8956 1.3130 0.1211  0.0777  -0.0265 376 GLU A CD  
2860  O OE1 . GLU A  376 ? 1.2947 0.9301 1.3414 0.1342  0.0743  -0.0270 376 GLU A OE1 
2861  O OE2 . GLU A  376 ? 1.3153 0.9160 1.3491 0.1139  0.0818  -0.0318 376 GLU A OE2 
2862  N N   . ALA A  377 ? 0.5185 0.2190 0.5855 0.0944  0.0794  -0.0252 377 ALA A N   
2863  C CA  . ALA A  377 ? 0.4867 0.1942 0.5564 0.0792  0.0814  -0.0316 377 ALA A CA  
2864  C C   . ALA A  377 ? 0.4757 0.1885 0.5444 0.0713  0.0803  -0.0226 377 ALA A C   
2865  O O   . ALA A  377 ? 0.5191 0.2225 0.5861 0.0588  0.0838  -0.0240 377 ALA A O   
2866  C CB  . ALA A  377 ? 0.4504 0.1862 0.5280 0.0783  0.0788  -0.0393 377 ALA A CB  
2867  N N   . VAL A  378 ? 0.4755 0.2037 0.5460 0.0786  0.0756  -0.0139 378 VAL A N   
2868  C CA  . VAL A  378 ? 0.4548 0.1879 0.5227 0.0728  0.0744  -0.0053 378 VAL A CA  
2869  C C   . VAL A  378 ? 0.4826 0.1846 0.5383 0.0702  0.0791  0.0012  378 VAL A C   
2870  O O   . VAL A  378 ? 0.4873 0.1850 0.5407 0.0585  0.0830  0.0027  378 VAL A O   
2871  C CB  . VAL A  378 ? 0.4196 0.1719 0.4902 0.0823  0.0677  0.0025  378 VAL A CB  
2872  C CG1 . VAL A  378 ? 0.4158 0.1684 0.4803 0.0772  0.0670  0.0112  378 VAL A CG1 
2873  C CG2 . VAL A  378 ? 0.3921 0.1749 0.4746 0.0826  0.0643  -0.0031 378 VAL A CG2 
2874  N N   . VAL A  379 ? 0.4886 0.1702 0.5364 0.0808  0.0787  0.0050  379 VAL A N   
2875  C CA  . VAL A  379 ? 0.5170 0.1730 0.5501 0.0783  0.0807  0.0121  379 VAL A CA  
2876  C C   . VAL A  379 ? 0.5334 0.1724 0.5650 0.0649  0.0880  0.0057  379 VAL A C   
2877  O O   . VAL A  379 ? 0.5451 0.1719 0.5696 0.0556  0.0925  0.0106  379 VAL A O   
2878  C CB  . VAL A  379 ? 0.5385 0.1821 0.5641 0.0916  0.0757  0.0162  379 VAL A CB  
2879  C CG1 . VAL A  379 ? 0.5688 0.1860 0.5785 0.0891  0.0775  0.0247  379 VAL A CG1 
2880  C CG2 . VAL A  379 ? 0.7825 0.4451 0.8121 0.1044  0.0674  0.0215  379 VAL A CG2 
2881  N N   . LEU A  380 ? 0.6668 0.3054 0.7050 0.0637  0.0892  -0.0056 380 LEU A N   
2882  C CA  . LEU A  380 ? 0.6633 0.2888 0.7025 0.0501  0.0950  -0.0138 380 LEU A CA  
2883  C C   . LEU A  380 ? 0.6479 0.2844 0.6949 0.0357  0.0988  -0.0152 380 LEU A C   
2884  O O   . LEU A  380 ? 0.6520 0.2760 0.6966 0.0237  0.1040  -0.0144 380 LEU A O   
2885  C CB  . LEU A  380 ? 0.6151 0.2436 0.6607 0.0511  0.0946  -0.0273 380 LEU A CB  
2886  C CG  . LEU A  380 ? 0.5628 0.1806 0.6109 0.0356  0.0991  -0.0369 380 LEU A CG  
2887  C CD1 . LEU A  380 ? 0.5977 0.1878 0.6357 0.0362  0.1010  -0.0368 380 LEU A CD1 
2888  C CD2 . LEU A  380 ? 0.5501 0.1818 0.6078 0.0319  0.0981  -0.0511 380 LEU A CD2 
2889  N N   . HIS A  381 ? 0.6415 0.3048 0.6985 0.0364  0.0954  -0.0171 381 HIS A N   
2890  C CA  . HIS A  381 ? 0.6799 0.3613 0.7451 0.0231  0.0963  -0.0188 381 HIS A CA  
2891  C C   . HIS A  381 ? 0.7139 0.3879 0.7724 0.0193  0.1003  -0.0073 381 HIS A C   
2892  O O   . HIS A  381 ? 0.7697 0.4398 0.8316 0.0062  0.1062  -0.0083 381 HIS A O   
2893  C CB  . HIS A  381 ? 0.6331 0.3498 0.7086 0.0249  0.0894  -0.0229 381 HIS A CB  
2894  C CG  . HIS A  381 ? 0.6725 0.4081 0.7587 0.0115  0.0895  -0.0278 381 HIS A CG  
2895  N ND1 . HIS A  381 ? 0.6721 0.4199 0.7674 0.0049  0.0872  -0.0397 381 HIS A ND1 
2896  C CD2 . HIS A  381 ? 0.6760 0.4202 0.7655 0.0039  0.0916  -0.0226 381 HIS A CD2 
2897  C CE1 . HIS A  381 ? 0.6733 0.4375 0.7784 -0.0059 0.0871  -0.0413 381 HIS A CE1 
2898  N NE2 . HIS A  381 ? 0.6699 0.4323 0.7723 -0.0066 0.0904  -0.0312 381 HIS A NE2 
2899  N N   . TYR A  382 ? 0.5976 0.2697 0.6465 0.0308  0.0972  0.0032  382 TYR A N   
2900  C CA  . TYR A  382 ? 0.5496 0.2171 0.5896 0.0284  0.1000  0.0139  382 TYR A CA  
2901  C C   . TYR A  382 ? 0.5446 0.1819 0.5680 0.0274  0.1054  0.0221  382 TYR A C   
2902  O O   . TYR A  382 ? 0.5386 0.1715 0.5538 0.0224  0.1095  0.0296  382 TYR A O   
2903  C CB  . TYR A  382 ? 0.4742 0.1606 0.5118 0.0393  0.0922  0.0207  382 TYR A CB  
2904  C CG  . TYR A  382 ? 0.4729 0.1934 0.5245 0.0351  0.0879  0.0152  382 TYR A CG  
2905  C CD1 . TYR A  382 ? 0.4323 0.1643 0.4863 0.0262  0.0904  0.0173  382 TYR A CD1 
2906  C CD2 . TYR A  382 ? 0.4215 0.1617 0.4837 0.0401  0.0820  0.0080  382 TYR A CD2 
2907  C CE1 . TYR A  382 ? 0.4200 0.1820 0.4868 0.0228  0.0864  0.0126  382 TYR A CE1 
2908  C CE2 . TYR A  382 ? 0.4534 0.2230 0.5271 0.0364  0.0782  0.0038  382 TYR A CE2 
2909  C CZ  . TYR A  382 ? 0.4167 0.1968 0.4928 0.0279  0.0800  0.0062  382 TYR A CZ  
2910  O OH  . TYR A  382 ? 0.3908 0.1985 0.4781 0.0250  0.0761  0.0024  382 TYR A OH  
2911  N N   . THR A  383 ? 0.5497 0.1695 0.5672 0.0317  0.1044  0.0203  383 THR A N   
2912  C CA  . THR A  383 ? 0.5943 0.1882 0.5960 0.0306  0.1080  0.0277  383 THR A CA  
2913  C C   . THR A  383 ? 0.6423 0.2272 0.6472 0.0138  0.1173  0.0243  383 THR A C   
2914  O O   . THR A  383 ? 0.6156 0.2076 0.6347 0.0049  0.1192  0.0132  383 THR A O   
2915  C CB  . THR A  383 ? 0.6051 0.1824 0.6011 0.0406  0.1040  0.0265  383 THR A CB  
2916  O OG1 . THR A  383 ? 0.5961 0.1848 0.5925 0.0562  0.0953  0.0288  383 THR A OG1 
2917  C CG2 . THR A  383 ? 0.6408 0.1911 0.6201 0.0405  0.1071  0.0354  383 THR A CG2 
2918  N N   . ASP A  384 ? 0.8272 0.3971 0.8191 0.0095  0.1228  0.0334  384 ASP A N   
2919  C CA  . ASP A  384 ? 0.9200 0.4777 0.9138 -0.0051 0.1320  0.0311  384 ASP A CA  
2920  C C   . ASP A  384 ? 0.9740 0.5055 0.9577 -0.0008 0.1316  0.0323  384 ASP A C   
2921  O O   . ASP A  384 ? 1.0092 0.5240 0.9758 0.0075  0.1305  0.0426  384 ASP A O   
2922  C CB  . ASP A  384 ? 1.0627 0.6169 1.0471 -0.0117 0.1395  0.0403  384 ASP A CB  
2923  C CG  . ASP A  384 ? 1.1520 0.6937 1.1390 -0.0265 0.1497  0.0386  384 ASP A CG  
2924  O OD1 . ASP A  384 ? 1.1862 0.7267 1.1861 -0.0337 0.1504  0.0285  384 ASP A OD1 
2925  O OD2 . ASP A  384 ? 1.1828 0.7159 1.1588 -0.0308 0.1570  0.0470  384 ASP A OD2 
2926  N N   . TRP A  385 ? 0.9495 0.4773 0.9437 -0.0064 0.1321  0.0215  385 TRP A N   
2927  C CA  . TRP A  385 ? 0.9187 0.4235 0.9055 -0.0003 0.1303  0.0205  385 TRP A CA  
2928  C C   . TRP A  385 ? 0.9466 0.4266 0.9244 -0.0089 0.1381  0.0256  385 TRP A C   
2929  O O   . TRP A  385 ? 0.9538 0.4108 0.9225 -0.0036 0.1374  0.0276  385 TRP A O   
2930  C CB  . TRP A  385 ? 0.7406 0.2509 0.7405 -0.0016 0.1271  0.0062  385 TRP A CB  
2931  C CG  . TRP A  385 ? 0.6825 0.2125 0.6877 0.0102  0.1193  0.0026  385 TRP A CG  
2932  C CD1 . TRP A  385 ? 0.6640 0.2202 0.6824 0.0072  0.1175  -0.0035 385 TRP A CD1 
2933  C CD2 . TRP A  385 ? 0.6713 0.1976 0.6698 0.0273  0.1125  0.0055  385 TRP A CD2 
2934  N NE1 . TRP A  385 ? 0.6178 0.1859 0.6373 0.0211  0.1106  -0.0045 385 TRP A NE1 
2935  C CE2 . TRP A  385 ? 0.6394 0.1906 0.6475 0.0336  0.1074  0.0008  385 TRP A CE2 
2936  C CE3 . TRP A  385 ? 0.6991 0.2041 0.6856 0.0380  0.1101  0.0116  385 TRP A CE3 
2937  C CZ2 . TRP A  385 ? 0.6363 0.1931 0.6432 0.0498  0.1005  0.0018  385 TRP A CZ2 
2938  C CZ3 . TRP A  385 ? 0.7150 0.2259 0.7011 0.0543  0.1026  0.0123  385 TRP A CZ3 
2939  C CH2 . TRP A  385 ? 0.6873 0.2246 0.6839 0.0599  0.0981  0.0073  385 TRP A CH2 
2940  N N   . LEU A  386 ? 0.9820 0.4674 0.9633 -0.0220 0.1460  0.0275  386 LEU A N   
2941  C CA  . LEU A  386 ? 1.0269 0.4905 0.9992 -0.0304 0.1549  0.0338  386 LEU A CA  
2942  C C   . LEU A  386 ? 1.0724 0.5221 1.0226 -0.0198 0.1546  0.0488  386 LEU A C   
2943  O O   . LEU A  386 ? 1.1297 0.5538 1.0663 -0.0192 0.1584  0.0557  386 LEU A O   
2944  C CB  . LEU A  386 ? 0.8408 0.3178 0.8261 -0.0475 0.1637  0.0304  386 LEU A CB  
2945  C CG  . LEU A  386 ? 0.8697 0.3319 0.8618 -0.0615 0.1711  0.0254  386 LEU A CG  
2946  C CD1 . LEU A  386 ? 0.8367 0.3193 0.8479 -0.0780 0.1779  0.0192  386 LEU A CD1 
2947  C CD2 . LEU A  386 ? 0.8292 0.2607 0.8016 -0.0598 0.1773  0.0369  386 LEU A CD2 
2948  N N   . HIS A  387 ? 0.8330 0.2995 0.7795 -0.0115 0.1496  0.0534  387 HIS A N   
2949  C CA  . HIS A  387 ? 0.8568 0.3136 0.7822 -0.0006 0.1473  0.0668  387 HIS A CA  
2950  C C   . HIS A  387 ? 0.7618 0.2350 0.6873 0.0142  0.1357  0.0675  387 HIS A C   
2951  O O   . HIS A  387 ? 0.7403 0.2304 0.6649 0.0154  0.1344  0.0705  387 HIS A O   
2952  C CB  . HIS A  387 ? 1.1957 0.6561 1.1142 -0.0094 0.1561  0.0734  387 HIS A CB  
2953  C CG  . HIS A  387 ? 1.2909 0.7422 1.2149 -0.0257 0.1684  0.0711  387 HIS A CG  
2954  N ND1 . HIS A  387 ? 1.2961 0.7671 1.2388 -0.0397 0.1749  0.0634  387 HIS A ND1 
2955  C CD2 . HIS A  387 ? 1.3468 0.7721 1.2615 -0.0303 0.1752  0.0752  387 HIS A CD2 
2956  C CE1 . HIS A  387 ? 1.3356 0.7943 1.2811 -0.0523 0.1850  0.0626  387 HIS A CE1 
2957  N NE2 . HIS A  387 ? 1.3628 0.7931 1.2910 -0.0471 0.1857  0.0698  387 HIS A NE2 
2958  N N   . PRO A  388 ? 0.8714 0.3401 0.7991 0.0255  0.1275  0.0643  388 PRO A N   
2959  C CA  . PRO A  388 ? 0.8320 0.3178 0.7650 0.0394  0.1165  0.0623  388 PRO A CA  
2960  C C   . PRO A  388 ? 0.8257 0.3105 0.7435 0.0524  0.1094  0.0738  388 PRO A C   
2961  O O   . PRO A  388 ? 0.7513 0.2549 0.6743 0.0622  0.1008  0.0732  388 PRO A O   
2962  C CB  . PRO A  388 ? 0.7437 0.2182 0.6814 0.0462  0.1127  0.0561  388 PRO A CB  
2963  C CG  . PRO A  388 ? 0.7709 0.2242 0.7077 0.0337  0.1217  0.0532  388 PRO A CG  
2964  C CD  . PRO A  388 ? 0.8015 0.2455 0.7259 0.0256  0.1293  0.0629  388 PRO A CD  
2965  N N   . GLU A  389 ? 0.8260 0.2885 0.7254 0.0525  0.1128  0.0839  389 GLU A N   
2966  C CA  . GLU A  389 ? 0.8472 0.3050 0.7292 0.0644  0.1058  0.0953  389 GLU A CA  
2967  C C   . GLU A  389 ? 0.8221 0.2850 0.6920 0.0587  0.1103  0.1021  389 GLU A C   
2968  O O   . GLU A  389 ? 0.8207 0.2799 0.6741 0.0676  0.1047  0.1114  389 GLU A O   
2969  C CB  . GLU A  389 ? 1.1167 0.5454 0.9836 0.0699  0.1058  0.1027  389 GLU A CB  
2970  C CG  . GLU A  389 ? 1.2003 0.6214 1.0777 0.0766  0.1016  0.0964  389 GLU A CG  
2971  C CD  . GLU A  389 ? 1.2798 0.7082 1.1583 0.0947  0.0883  0.0990  389 GLU A CD  
2972  O OE1 . GLU A  389 ? 1.3197 0.7508 1.1860 0.1023  0.0823  0.1082  389 GLU A OE1 
2973  O OE2 . GLU A  389 ? 1.2963 0.7283 1.1882 0.1013  0.0839  0.0915  389 GLU A OE2 
2974  N N   . ASP A  390 ? 0.9170 0.3885 0.7953 0.0440  0.1203  0.0971  390 ASP A N   
2975  C CA  . ASP A  390 ? 0.9397 0.4151 0.8072 0.0376  0.1266  0.1028  390 ASP A CA  
2976  C C   . ASP A  390 ? 0.9453 0.4407 0.8112 0.0465  0.1175  0.1048  390 ASP A C   
2977  O O   . ASP A  390 ? 0.9512 0.4691 0.8351 0.0462  0.1140  0.0971  390 ASP A O   
2978  C CB  . ASP A  390 ? 0.9367 0.4220 0.8190 0.0205  0.1384  0.0955  390 ASP A CB  
2979  C CG  . ASP A  390 ? 0.9724 0.4537 0.8414 0.0124  0.1485  0.1020  390 ASP A CG  
2980  O OD1 . ASP A  390 ? 0.9402 0.4348 0.8037 0.0153  0.1464  0.1049  390 ASP A OD1 
2981  O OD2 . ASP A  390 ? 1.0256 0.4900 0.8897 0.0030  0.1591  0.1040  390 ASP A OD2 
2982  N N   . PRO A  391 ? 0.8923 0.3792 0.7361 0.0542  0.1136  0.1151  391 PRO A N   
2983  C CA  . PRO A  391 ? 0.8884 0.3909 0.7271 0.0641  0.1032  0.1182  391 PRO A CA  
2984  C C   . PRO A  391 ? 0.8955 0.4177 0.7409 0.0560  0.1081  0.1145  391 PRO A C   
2985  O O   . PRO A  391 ? 0.9000 0.4431 0.7556 0.0617  0.0997  0.1112  391 PRO A O   
2986  C CB  . PRO A  391 ? 0.8799 0.3626 0.6899 0.0704  0.1014  0.1299  391 PRO A CB  
2987  C CG  . PRO A  391 ? 0.9074 0.3649 0.7113 0.0688  0.1066  0.1328  391 PRO A CG  
2988  C CD  . PRO A  391 ? 0.8824 0.3419 0.7035 0.0540  0.1188  0.1245  391 PRO A CD  
2989  N N   . THR A  392 ? 0.8667 0.3831 0.7078 0.0430  0.1216  0.1151  392 THR A N   
2990  C CA  . THR A  392 ? 0.8025 0.3378 0.6534 0.0340  0.1279  0.1108  392 THR A CA  
2991  C C   . THR A  392 ? 0.7511 0.3073 0.6314 0.0292  0.1271  0.0995  392 THR A C   
2992  O O   . THR A  392 ? 0.7285 0.3058 0.6197 0.0315  0.1222  0.0959  392 THR A O   
2993  C CB  . THR A  392 ? 0.8162 0.3423 0.6610 0.0203  0.1437  0.1123  392 THR A CB  
2994  O OG1 . THR A  392 ? 0.8397 0.3511 0.6559 0.0245  0.1453  0.1223  392 THR A OG1 
2995  C CG2 . THR A  392 ? 0.7849 0.3338 0.6489 0.0096  0.1507  0.1050  392 THR A CG2 
2996  N N   . HIS A  393 ? 0.6729 0.2223 0.5654 0.0227  0.1316  0.0940  393 HIS A N   
2997  C CA  . HIS A  393 ? 0.6602 0.2275 0.5790 0.0181  0.1307  0.0827  393 HIS A CA  
2998  C C   . HIS A  393 ? 0.6156 0.1958 0.5416 0.0310  0.1177  0.0802  393 HIS A C   
2999  O O   . HIS A  393 ? 0.5847 0.1865 0.5274 0.0299  0.1154  0.0738  393 HIS A O   
3000  C CB  . HIS A  393 ? 0.9440 0.5001 0.8726 0.0098  0.1363  0.0767  393 HIS A CB  
3001  C CG  . HIS A  393 ? 1.0353 0.6102 0.9896 0.0037  0.1356  0.0644  393 HIS A CG  
3002  N ND1 . HIS A  393 ? 1.0460 0.6315 1.0102 0.0129  0.1260  0.0590  393 HIS A ND1 
3003  C CD2 . HIS A  393 ? 1.0675 0.6543 1.0400 -0.0104 0.1430  0.0563  393 HIS A CD2 
3004  C CE1 . HIS A  393 ? 1.0368 0.6378 1.0221 0.0047  0.1277  0.0482  393 HIS A CE1 
3005  N NE2 . HIS A  393 ? 1.0554 0.6579 1.0467 -0.0096 0.1373  0.0462  393 HIS A NE2 
3006  N N   . LEU A  394 ? 0.7688 0.3366 0.6836 0.0433  0.1094  0.0850  394 LEU A N   
3007  C CA  . LEU A  394 ? 0.7380 0.3189 0.6593 0.0571  0.0967  0.0835  394 LEU A CA  
3008  C C   . LEU A  394 ? 0.6913 0.2924 0.6135 0.0614  0.0911  0.0853  394 LEU A C   
3009  O O   . LEU A  394 ? 0.6766 0.2985 0.6160 0.0646  0.0861  0.0791  394 LEU A O   
3010  C CB  . LEU A  394 ? 0.6429 0.2071 0.5497 0.0696  0.0889  0.0905  394 LEU A CB  
3011  C CG  . LEU A  394 ? 0.6597 0.2089 0.5717 0.0691  0.0911  0.0863  394 LEU A CG  
3012  C CD1 . LEU A  394 ? 0.6893 0.2206 0.5875 0.0813  0.0840  0.0937  394 LEU A CD1 
3013  C CD2 . LEU A  394 ? 0.7804 0.3477 0.7149 0.0705  0.0880  0.0752  394 LEU A CD2 
3014  N N   . ARG A  395 ? 0.6055 0.1997 0.5086 0.0616  0.0921  0.0935  395 ARG A N   
3015  C CA  . ARG A  395 ? 0.5866 0.1973 0.4879 0.0649  0.0873  0.0953  395 ARG A CA  
3016  C C   . ARG A  395 ? 0.5552 0.1859 0.4764 0.0552  0.0934  0.0876  395 ARG A C   
3017  O O   . ARG A  395 ? 0.5257 0.1808 0.4622 0.0594  0.0856  0.0827  395 ARG A O   
3018  C CB  . ARG A  395 ? 0.6466 0.2436 0.5220 0.0640  0.0903  0.1043  395 ARG A CB  
3019  C CG  . ARG A  395 ? 0.6525 0.2644 0.5244 0.0654  0.0872  0.1054  395 ARG A CG  
3020  C CD  . ARG A  395 ? 0.6547 0.2638 0.5205 0.0529  0.1009  0.1060  395 ARG A CD  
3021  N NE  . ARG A  395 ? 0.6834 0.2702 0.5216 0.0518  0.1064  0.1142  395 ARG A NE  
3022  C CZ  . ARG A  395 ? 0.6888 0.2682 0.5209 0.0402  0.1208  0.1150  395 ARG A CZ  
3023  N NH1 . ARG A  395 ? 0.6688 0.2626 0.5223 0.0287  0.1303  0.1079  395 ARG A NH1 
3024  N NH2 . ARG A  395 ? 0.7218 0.2807 0.5276 0.0402  0.1258  0.1228  395 ARG A NH2 
3025  N N   . ASP A  396 ? 0.5606 0.1859 0.4838 0.0416  0.1061  0.0857  396 ASP A N   
3026  C CA  . ASP A  396 ? 0.5843 0.2312 0.5279 0.0310  0.1116  0.0778  396 ASP A CA  
3027  C C   . ASP A  396 ? 0.5318 0.1998 0.5001 0.0317  0.1051  0.0674  396 ASP A C   
3028  O O   . ASP A  396 ? 0.4884 0.1857 0.4730 0.0304  0.1000  0.0610  396 ASP A O   
3029  C CB  . ASP A  396 ? 0.7936 0.4304 0.7383 0.0162  0.1264  0.0769  396 ASP A CB  
3030  C CG  . ASP A  396 ? 0.8752 0.5051 0.8009 0.0130  0.1334  0.0842  396 ASP A CG  
3031  O OD1 . ASP A  396 ? 0.9381 0.5740 0.8534 0.0204  0.1275  0.0883  396 ASP A OD1 
3032  O OD2 . ASP A  396 ? 0.8666 0.4864 0.7884 0.0029  0.1449  0.0851  396 ASP A OD2 
3033  N N   . ALA A  397 ? 0.5289 0.1802 0.4982 0.0343  0.1056  0.0660  397 ALA A N   
3034  C CA  . ALA A  397 ? 0.5006 0.1668 0.4887 0.0368  0.0998  0.0567  397 ALA A CA  
3035  C C   . ALA A  397 ? 0.4838 0.1740 0.4775 0.0476  0.0876  0.0561  397 ALA A C   
3036  O O   . ALA A  397 ? 0.4689 0.1864 0.4782 0.0441  0.0846  0.0495  397 ALA A O   
3037  C CB  . ALA A  397 ? 0.5635 0.2062 0.5461 0.0415  0.1002  0.0568  397 ALA A CB  
3038  N N   . MET A  398 ? 0.5391 0.2188 0.5201 0.0606  0.0806  0.0633  398 MET A N   
3039  C CA  . MET A  398 ? 0.5056 0.2070 0.4935 0.0715  0.0688  0.0628  398 MET A CA  
3040  C C   . MET A  398 ? 0.4970 0.2260 0.4928 0.0668  0.0658  0.0605  398 MET A C   
3041  O O   . MET A  398 ? 0.4657 0.2202 0.4781 0.0688  0.0598  0.0546  398 MET A O   
3042  C CB  . MET A  398 ? 0.4993 0.1845 0.4694 0.0844  0.0619  0.0726  398 MET A CB  
3043  C CG  . MET A  398 ? 0.4785 0.1857 0.4567 0.0955  0.0492  0.0726  398 MET A CG  
3044  S SD  . MET A  398 ? 0.7279 0.4416 0.7234 0.1059  0.0444  0.0670  398 MET A SD  
3045  C CE  . MET A  398 ? 0.6769 0.4257 0.6968 0.0976  0.0450  0.0557  398 MET A CE  
3046  N N   . SER A  399 ? 0.4503 0.1730 0.4338 0.0606  0.0708  0.0650  399 SER A N   
3047  C CA  . SER A  399 ? 0.4262 0.1725 0.4169 0.0551  0.0699  0.0622  399 SER A CA  
3048  C C   . SER A  399 ? 0.4414 0.2091 0.4548 0.0470  0.0722  0.0524  399 SER A C   
3049  O O   . SER A  399 ? 0.3741 0.1663 0.4007 0.0487  0.0658  0.0481  399 SER A O   
3050  C CB  . SER A  399 ? 0.4933 0.2275 0.4688 0.0478  0.0785  0.0671  399 SER A CB  
3051  O OG  . SER A  399 ? 0.4511 0.2078 0.4372 0.0409  0.0798  0.0626  399 SER A OG  
3052  N N   . ALA A  400 ? 0.5105 0.2680 0.5281 0.0381  0.0811  0.0487  400 ALA A N   
3053  C CA  . ALA A  400 ? 0.4951 0.2714 0.5330 0.0299  0.0829  0.0391  400 ALA A CA  
3054  C C   . ALA A  400 ? 0.4686 0.2590 0.5186 0.0364  0.0752  0.0332  400 ALA A C   
3055  O O   . ALA A  400 ? 0.4310 0.2435 0.4958 0.0330  0.0729  0.0265  400 ALA A O   
3056  C CB  . ALA A  400 ? 0.5189 0.2797 0.5589 0.0191  0.0931  0.0360  400 ALA A CB  
3057  N N   . VAL A  401 ? 0.4158 0.1931 0.4591 0.0463  0.0716  0.0360  401 VAL A N   
3058  C CA  . VAL A  401 ? 0.3841 0.1734 0.4383 0.0530  0.0659  0.0306  401 VAL A CA  
3059  C C   . VAL A  401 ? 0.3479 0.1631 0.4097 0.0574  0.0582  0.0309  401 VAL A C   
3060  O O   . VAL A  401 ? 0.3533 0.1890 0.4284 0.0549  0.0565  0.0245  401 VAL A O   
3061  C CB  . VAL A  401 ? 0.3943 0.1640 0.4406 0.0639  0.0639  0.0340  401 VAL A CB  
3062  C CG1 . VAL A  401 ? 0.3815 0.1658 0.4401 0.0713  0.0590  0.0281  401 VAL A CG1 
3063  C CG2 . VAL A  401 ? 0.4207 0.1628 0.4595 0.0588  0.0720  0.0335  401 VAL A CG2 
3064  N N   . VAL A  402 ? 0.3519 0.1654 0.4043 0.0636  0.0536  0.0383  402 VAL A N   
3065  C CA  . VAL A  402 ? 0.3300 0.1670 0.3901 0.0675  0.0460  0.0385  402 VAL A CA  
3066  C C   . VAL A  402 ? 0.3087 0.1642 0.3779 0.0580  0.0482  0.0342  402 VAL A C   
3067  O O   . VAL A  402 ? 0.2874 0.1641 0.3697 0.0581  0.0447  0.0298  402 VAL A O   
3068  C CB  . VAL A  402 ? 0.3399 0.1712 0.3872 0.0739  0.0404  0.0464  402 VAL A CB  
3069  C CG1 . VAL A  402 ? 0.3177 0.1724 0.3728 0.0739  0.0342  0.0456  402 VAL A CG1 
3070  C CG2 . VAL A  402 ? 0.3563 0.1762 0.3989 0.0858  0.0349  0.0504  402 VAL A CG2 
3071  N N   . GLY A  403 ? 0.3966 0.2435 0.4589 0.0500  0.0545  0.0356  403 GLY A N   
3072  C CA  . GLY A  403 ? 0.2986 0.1617 0.3696 0.0415  0.0570  0.0319  403 GLY A CA  
3073  C C   . GLY A  403 ? 0.2831 0.1605 0.3700 0.0366  0.0578  0.0238  403 GLY A C   
3074  O O   . GLY A  403 ? 0.2625 0.1605 0.3597 0.0358  0.0542  0.0208  403 GLY A O   
3075  N N   . ASP A  404 ? 0.3869 0.2521 0.4744 0.0334  0.0623  0.0202  404 ASP A N   
3076  C CA  . ASP A  404 ? 0.4621 0.3382 0.5622 0.0288  0.0625  0.0118  404 ASP A CA  
3077  C C   . ASP A  404 ? 0.4381 0.3292 0.5446 0.0360  0.0561  0.0090  404 ASP A C   
3078  O O   . ASP A  404 ? 0.4158 0.3247 0.5320 0.0333  0.0540  0.0040  404 ASP A O   
3079  C CB  . ASP A  404 ? 0.5706 0.4275 0.6683 0.0246  0.0680  0.0082  404 ASP A CB  
3080  C CG  . ASP A  404 ? 0.6054 0.4520 0.7020 0.0143  0.0758  0.0088  404 ASP A CG  
3081  O OD1 . ASP A  404 ? 0.6036 0.4628 0.7046 0.0097  0.0769  0.0097  404 ASP A OD1 
3082  O OD2 . ASP A  404 ? 0.6020 0.4279 0.6940 0.0107  0.0814  0.0081  404 ASP A OD2 
3083  N N   . HIS A  405 ? 0.3688 0.2529 0.4701 0.0456  0.0531  0.0126  405 HIS A N   
3084  C CA  . HIS A  405 ? 0.3452 0.2426 0.4536 0.0524  0.0487  0.0098  405 HIS A CA  
3085  C C   . HIS A  405 ? 0.3142 0.2335 0.4294 0.0540  0.0437  0.0116  405 HIS A C   
3086  O O   . HIS A  405 ? 0.2946 0.2296 0.4181 0.0545  0.0421  0.0076  405 HIS A O   
3087  C CB  . HIS A  405 ? 0.3803 0.2650 0.4839 0.0626  0.0473  0.0126  405 HIS A CB  
3088  C CG  . HIS A  405 ? 0.3694 0.2690 0.4817 0.0704  0.0437  0.0104  405 HIS A CG  
3089  N ND1 . HIS A  405 ? 0.3665 0.2817 0.4868 0.0677  0.0442  0.0041  405 HIS A ND1 
3090  C CD2 . HIS A  405 ? 0.3829 0.2843 0.4973 0.0807  0.0399  0.0138  405 HIS A CD2 
3091  C CE1 . HIS A  405 ? 0.3904 0.3159 0.5169 0.0758  0.0421  0.0039  405 HIS A CE1 
3092  N NE2 . HIS A  405 ? 0.3901 0.3085 0.5148 0.0837  0.0394  0.0095  405 HIS A NE2 
3093  N N   . ASN A  406 ? 0.3001 0.2194 0.4109 0.0552  0.0413  0.0176  406 ASN A N   
3094  C CA  . ASN A  406 ? 0.2805 0.2192 0.3980 0.0563  0.0365  0.0190  406 ASN A CA  
3095  C C   . ASN A  406 ? 0.2492 0.1984 0.3703 0.0485  0.0377  0.0175  406 ASN A C   
3096  O O   . ASN A  406 ? 0.1989 0.1644 0.3271 0.0487  0.0344  0.0173  406 ASN A O   
3097  C CB  . ASN A  406 ? 0.3168 0.2525 0.4289 0.0628  0.0314  0.0253  406 ASN A CB  
3098  C CG  . ASN A  406 ? 0.4349 0.3586 0.5432 0.0713  0.0298  0.0275  406 ASN A CG  
3099  O OD1 . ASN A  406 ? 0.4843 0.4166 0.6013 0.0773  0.0275  0.0257  406 ASN A OD1 
3100  N ND2 . ASN A  406 ? 0.4815 0.3845 0.5765 0.0723  0.0314  0.0315  406 ASN A ND2 
3101  N N   . VAL A  407 ? 0.3551 0.2952 0.4725 0.0417  0.0428  0.0165  407 VAL A N   
3102  C CA  . VAL A  407 ? 0.3677 0.3181 0.4897 0.0352  0.0441  0.0154  407 VAL A CA  
3103  C C   . VAL A  407 ? 0.4137 0.3662 0.5424 0.0272  0.0485  0.0097  407 VAL A C   
3104  O O   . VAL A  407 ? 0.4658 0.4338 0.6038 0.0251  0.0463  0.0059  407 VAL A O   
3105  C CB  . VAL A  407 ? 0.2183 0.1612 0.3312 0.0345  0.0456  0.0205  407 VAL A CB  
3106  C CG1 . VAL A  407 ? 0.2065 0.1608 0.3259 0.0286  0.0476  0.0186  407 VAL A CG1 
3107  C CG2 . VAL A  407 ? 0.2161 0.1612 0.3245 0.0418  0.0392  0.0249  407 VAL A CG2 
3108  N N   . VAL A  408 ? 0.3287 0.2657 0.4530 0.0227  0.0542  0.0092  408 VAL A N   
3109  C CA  . VAL A  408 ? 0.3410 0.2815 0.4740 0.0141  0.0580  0.0033  408 VAL A CA  
3110  C C   . VAL A  408 ? 0.3144 0.2640 0.4551 0.0137  0.0545  -0.0036 408 VAL A C   
3111  O O   . VAL A  408 ? 0.3231 0.2883 0.4734 0.0102  0.0522  -0.0077 408 VAL A O   
3112  C CB  . VAL A  408 ? 0.2445 0.1663 0.3728 0.0080  0.0657  0.0037  408 VAL A CB  
3113  C CG1 . VAL A  408 ? 0.2403 0.1712 0.3810 -0.0017 0.0696  -0.0012 408 VAL A CG1 
3114  C CG2 . VAL A  408 ? 0.2556 0.1643 0.3708 0.0106  0.0687  0.0114  408 VAL A CG2 
3115  N N   . CYS A  409 ? 0.4031 0.3431 0.5390 0.0179  0.0539  -0.0051 409 CYS A N   
3116  C CA  . CYS A  409 ? 0.4257 0.3732 0.5664 0.0176  0.0511  -0.0122 409 CYS A CA  
3117  C C   . CYS A  409 ? 0.3923 0.3596 0.5374 0.0215  0.0456  -0.0129 409 CYS A C   
3118  O O   . CYS A  409 ? 0.4157 0.3931 0.5657 0.0185  0.0433  -0.0186 409 CYS A O   
3119  C CB  . CYS A  409 ? 0.3930 0.3239 0.5272 0.0209  0.0529  -0.0147 409 CYS A CB  
3120  S SG  . CYS A  409 ? 0.3808 0.2899 0.5125 0.0124  0.0598  -0.0164 409 CYS A SG  
3121  N N   . PRO A  410 ? 0.2031 0.1757 0.3464 0.0280  0.0433  -0.0070 410 PRO A N   
3122  C CA  . PRO A  410 ? 0.1844 0.1752 0.3327 0.0302  0.0391  -0.0066 410 PRO A CA  
3123  C C   . PRO A  410 ? 0.1732 0.1761 0.3282 0.0250  0.0378  -0.0067 410 PRO A C   
3124  O O   . PRO A  410 ? 0.1647 0.1806 0.3237 0.0250  0.0345  -0.0088 410 PRO A O   
3125  C CB  . PRO A  410 ? 0.2221 0.2138 0.3683 0.0372  0.0374  -0.0003 410 PRO A CB  
3126  C CG  . PRO A  410 ? 0.2200 0.1945 0.3591 0.0387  0.0398  0.0030  410 PRO A CG  
3127  C CD  . PRO A  410 ? 0.2468 0.2085 0.3834 0.0349  0.0436  -0.0018 410 PRO A CD  
3128  N N   . VAL A  411 ? 0.1867 0.1849 0.3422 0.0212  0.0405  -0.0043 411 VAL A N   
3129  C CA  . VAL A  411 ? 0.2771 0.2861 0.4406 0.0164  0.0403  -0.0053 411 VAL A CA  
3130  C C   . VAL A  411 ? 0.2620 0.2761 0.4329 0.0106  0.0399  -0.0123 411 VAL A C   
3131  O O   . VAL A  411 ? 0.1713 0.1994 0.3494 0.0096  0.0361  -0.0145 411 VAL A O   
3132  C CB  . VAL A  411 ? 0.1706 0.1723 0.3326 0.0133  0.0451  -0.0019 411 VAL A CB  
3133  C CG1 . VAL A  411 ? 0.1639 0.1766 0.3364 0.0082  0.0461  -0.0043 411 VAL A CG1 
3134  C CG2 . VAL A  411 ? 0.1683 0.1675 0.3231 0.0188  0.0438  0.0042  411 VAL A CG2 
3135  N N   . ALA A  412 ? 0.2530 0.2549 0.4219 0.0070  0.0432  -0.0159 412 ALA A N   
3136  C CA  . ALA A  412 ? 0.2596 0.2649 0.4353 0.0010  0.0420  -0.0236 412 ALA A CA  
3137  C C   . ALA A  412 ? 0.2861 0.3011 0.4603 0.0045  0.0358  -0.0274 412 ALA A C   
3138  O O   . ALA A  412 ? 0.3420 0.3685 0.5231 0.0013  0.0315  -0.0324 412 ALA A O   
3139  C CB  . ALA A  412 ? 0.2032 0.1908 0.3754 -0.0029 0.0468  -0.0265 412 ALA A CB  
3140  N N   . GLN A  413 ? 0.1833 0.1941 0.3486 0.0113  0.0353  -0.0251 413 GLN A N   
3141  C CA  . GLN A  413 ? 0.2131 0.2313 0.3747 0.0148  0.0310  -0.0285 413 GLN A CA  
3142  C C   . GLN A  413 ? 0.1835 0.2182 0.3487 0.0167  0.0266  -0.0256 413 GLN A C   
3143  O O   . GLN A  413 ? 0.1697 0.2133 0.3351 0.0159  0.0221  -0.0297 413 GLN A O   
3144  C CB  . GLN A  413 ? 0.4987 0.5091 0.6516 0.0218  0.0330  -0.0267 413 GLN A CB  
3145  C CG  . GLN A  413 ? 0.6340 0.6495 0.7814 0.0250  0.0307  -0.0310 413 GLN A CG  
3146  C CD  . GLN A  413 ? 0.7751 0.7894 0.9175 0.0329  0.0329  -0.0272 413 GLN A CD  
3147  O OE1 . GLN A  413 ? 0.8082 0.8179 0.9521 0.0362  0.0350  -0.0217 413 GLN A OE1 
3148  N NE2 . GLN A  413 ? 0.8421 0.8611 0.9788 0.0363  0.0324  -0.0303 413 GLN A NE2 
3149  N N   . LEU A  414 ? 0.3540 0.3918 0.5212 0.0192  0.0275  -0.0187 414 LEU A N   
3150  C CA  . LEU A  414 ? 0.3554 0.4068 0.5262 0.0209  0.0238  -0.0155 414 LEU A CA  
3151  C C   . LEU A  414 ? 0.3523 0.4126 0.5324 0.0160  0.0211  -0.0187 414 LEU A C   
3152  O O   . LEU A  414 ? 0.3487 0.4199 0.5306 0.0172  0.0162  -0.0192 414 LEU A O   
3153  C CB  . LEU A  414 ? 0.2515 0.3029 0.4229 0.0239  0.0253  -0.0084 414 LEU A CB  
3154  C CG  . LEU A  414 ? 0.1293 0.1921 0.3048 0.0254  0.0222  -0.0049 414 LEU A CG  
3155  C CD1 . LEU A  414 ? 0.1290 0.1981 0.3002 0.0290  0.0195  -0.0043 414 LEU A CD1 
3156  C CD2 . LEU A  414 ? 0.1240 0.1843 0.2997 0.0272  0.0237  0.0007  414 LEU A CD2 
3157  N N   . ALA A  415 ? 0.2641 0.3197 0.4504 0.0107  0.0244  -0.0207 415 ALA A N   
3158  C CA  . ALA A  415 ? 0.2523 0.3176 0.4505 0.0058  0.0224  -0.0244 415 ALA A CA  
3159  C C   . ALA A  415 ? 0.3389 0.4097 0.5379 0.0039  0.0167  -0.0315 415 ALA A C   
3160  O O   . ALA A  415 ? 0.3862 0.4697 0.5897 0.0049  0.0106  -0.0327 415 ALA A O   
3161  C CB  . ALA A  415 ? 0.1508 0.2091 0.3554 -0.0002 0.0286  -0.0255 415 ALA A CB  
3162  N N   . GLY A  416 ? 0.3950 0.4553 0.5886 0.0015  0.0183  -0.0363 416 GLY A N   
3163  C CA  . GLY A  416 ? 0.4183 0.4817 0.6109 -0.0009 0.0128  -0.0444 416 GLY A CA  
3164  C C   . GLY A  416 ? 0.4046 0.4767 0.5889 0.0049  0.0064  -0.0437 416 GLY A C   
3165  O O   . GLY A  416 ? 0.4426 0.5249 0.6301 0.0037  -0.0007 -0.0482 416 GLY A O   
3166  N N   . ARG A  417 ? 0.2370 0.3053 0.4110 0.0113  0.0089  -0.0379 417 ARG A N   
3167  C CA  . ARG A  417 ? 0.2442 0.3190 0.4086 0.0167  0.0047  -0.0364 417 ARG A CA  
3168  C C   . ARG A  417 ? 0.1999 0.2876 0.3699 0.0186  0.0000  -0.0317 417 ARG A C   
3169  O O   . ARG A  417 ? 0.1649 0.2597 0.3301 0.0205  -0.0062 -0.0331 417 ARG A O   
3170  C CB  . ARG A  417 ? 0.5435 0.6114 0.6979 0.0223  0.0097  -0.0317 417 ARG A CB  
3171  C CG  . ARG A  417 ? 0.7144 0.7691 0.8632 0.0219  0.0141  -0.0363 417 ARG A CG  
3172  C CD  . ARG A  417 ? 0.8653 0.9175 1.0009 0.0263  0.0144  -0.0391 417 ARG A CD  
3173  N NE  . ARG A  417 ? 0.9608 1.0213 1.0904 0.0261  0.0080  -0.0426 417 ARG A NE  
3174  C CZ  . ARG A  417 ? 0.9985 1.0565 1.1226 0.0232  0.0040  -0.0516 417 ARG A CZ  
3175  N NH1 . ARG A  417 ? 1.0159 1.0624 1.1406 0.0197  0.0066  -0.0581 417 ARG A NH1 
3176  N NH2 . ARG A  417 ? 0.9953 1.0610 1.1123 0.0239  -0.0030 -0.0540 417 ARG A NH2 
3177  N N   . LEU A  418 ? 0.2256 0.3150 0.4043 0.0186  0.0030  -0.0260 418 LEU A N   
3178  C CA  . LEU A  418 ? 0.2108 0.3108 0.3956 0.0208  -0.0007 -0.0216 418 LEU A CA  
3179  C C   . LEU A  418 ? 0.2037 0.3136 0.3988 0.0176  -0.0070 -0.0270 418 LEU A C   
3180  O O   . LEU A  418 ? 0.1424 0.2617 0.3386 0.0206  -0.0133 -0.0256 418 LEU A O   
3181  C CB  . LEU A  418 ? 0.1515 0.2498 0.3435 0.0209  0.0042  -0.0160 418 LEU A CB  
3182  C CG  . LEU A  418 ? 0.1251 0.2175 0.3104 0.0247  0.0083  -0.0094 418 LEU A CG  
3183  C CD1 . LEU A  418 ? 0.1175 0.2086 0.3095 0.0241  0.0116  -0.0056 418 LEU A CD1 
3184  C CD2 . LEU A  418 ? 0.1248 0.2222 0.3040 0.0292  0.0050  -0.0054 418 LEU A CD2 
3185  N N   . ALA A  419 ? 0.2601 0.3681 0.4636 0.0115  -0.0054 -0.0332 419 ALA A N   
3186  C CA  . ALA A  419 ? 0.2634 0.3820 0.4797 0.0074  -0.0113 -0.0395 419 ALA A CA  
3187  C C   . ALA A  419 ? 0.3039 0.4259 0.5107 0.0088  -0.0199 -0.0445 419 ALA A C   
3188  O O   . ALA A  419 ? 0.3486 0.4822 0.5590 0.0111  -0.0282 -0.0451 419 ALA A O   
3189  C CB  . ALA A  419 ? 0.2197 0.3338 0.4468 -0.0005 -0.0064 -0.0449 419 ALA A CB  
3190  N N   . ALA A  420 ? 0.3186 0.4298 0.5121 0.0082  -0.0180 -0.0481 420 ALA A N   
3191  C CA  . ALA A  420 ? 0.3362 0.4481 0.5173 0.0094  -0.0254 -0.0540 420 ALA A CA  
3192  C C   . ALA A  420 ? 0.2753 0.3926 0.4446 0.0168  -0.0300 -0.0481 420 ALA A C   
3193  O O   . ALA A  420 ? 0.2853 0.4076 0.4467 0.0185  -0.0386 -0.0516 420 ALA A O   
3194  C CB  . ALA A  420 ? 0.4809 0.5782 0.6487 0.0085  -0.0204 -0.0581 420 ALA A CB  
3195  N N   . GLN A  421 ? 0.1955 0.3110 0.3631 0.0210  -0.0245 -0.0389 421 GLN A N   
3196  C CA  . GLN A  421 ? 0.2762 0.3948 0.4329 0.0275  -0.0272 -0.0322 421 GLN A CA  
3197  C C   . GLN A  421 ? 0.2928 0.4229 0.4616 0.0291  -0.0333 -0.0288 421 GLN A C   
3198  O O   . GLN A  421 ? 0.2605 0.3928 0.4231 0.0345  -0.0354 -0.0219 421 GLN A O   
3199  C CB  . GLN A  421 ? 0.4455 0.5566 0.5957 0.0307  -0.0184 -0.0245 421 GLN A CB  
3200  C CG  . GLN A  421 ? 0.4885 0.5929 0.6201 0.0341  -0.0156 -0.0243 421 GLN A CG  
3201  C CD  . GLN A  421 ? 0.5513 0.6495 0.6757 0.0315  -0.0159 -0.0336 421 GLN A CD  
3202  O OE1 . GLN A  421 ? 0.5539 0.6446 0.6826 0.0288  -0.0103 -0.0366 421 GLN A OE1 
3203  N NE2 . GLN A  421 ? 0.6009 0.7009 0.7131 0.0325  -0.0226 -0.0384 421 GLN A NE2 
3204  N N   . GLY A  422 ? 0.5446 0.6816 0.7314 0.0244  -0.0355 -0.0338 422 GLY A N   
3205  C CA  . GLY A  422 ? 0.5816 0.7308 0.7830 0.0261  -0.0412 -0.0321 422 GLY A CA  
3206  C C   . GLY A  422 ? 0.5614 0.7106 0.7712 0.0284  -0.0353 -0.0244 422 GLY A C   
3207  O O   . GLY A  422 ? 0.6219 0.7745 0.8302 0.0339  -0.0385 -0.0184 422 GLY A O   
3208  N N   . ALA A  423 ? 0.3725 0.5159 0.5891 0.0244  -0.0264 -0.0244 423 ALA A N   
3209  C CA  . ALA A  423 ? 0.2945 0.4382 0.5203 0.0257  -0.0212 -0.0189 423 ALA A CA  
3210  C C   . ALA A  423 ? 0.3110 0.4602 0.5561 0.0204  -0.0180 -0.0236 423 ALA A C   
3211  O O   . ALA A  423 ? 0.3412 0.4898 0.5908 0.0145  -0.0170 -0.0301 423 ALA A O   
3212  C CB  . ALA A  423 ? 0.1228 0.2546 0.3384 0.0265  -0.0132 -0.0137 423 ALA A CB  
3213  N N   . ARG A  424 ? 0.2089 0.3631 0.4654 0.0224  -0.0159 -0.0205 424 ARG A N   
3214  C CA  . ARG A  424 ? 0.1970 0.3553 0.4707 0.0176  -0.0104 -0.0241 424 ARG A CA  
3215  C C   . ARG A  424 ? 0.1793 0.3235 0.4449 0.0147  -0.0002 -0.0216 424 ARG A C   
3216  O O   . ARG A  424 ? 0.2008 0.3377 0.4572 0.0185  0.0029  -0.0156 424 ARG A O   
3217  C CB  . ARG A  424 ? 0.2926 0.4606 0.5804 0.0218  -0.0110 -0.0218 424 ARG A CB  
3218  C CG  . ARG A  424 ? 0.8778 1.0520 1.1837 0.0171  -0.0050 -0.0259 424 ARG A CG  
3219  C CD  . ARG A  424 ? 0.8635 1.0501 1.1845 0.0120  -0.0101 -0.0337 424 ARG A CD  
3220  N NE  . ARG A  424 ? 0.8757 1.0721 1.1971 0.0156  -0.0231 -0.0358 424 ARG A NE  
3221  C CZ  . ARG A  424 ? 0.8970 1.1000 1.2170 0.0228  -0.0309 -0.0325 424 ARG A CZ  
3222  N NH1 . ARG A  424 ? 0.9071 1.1079 1.2263 0.0269  -0.0266 -0.0274 424 ARG A NH1 
3223  N NH2 . ARG A  424 ? 0.8883 1.0993 1.2069 0.0261  -0.0433 -0.0346 424 ARG A NH2 
3224  N N   . VAL A  425 ? 0.1762 0.3160 0.4447 0.0081  0.0045  -0.0261 425 VAL A N   
3225  C CA  . VAL A  425 ? 0.1771 0.3021 0.4360 0.0061  0.0134  -0.0233 425 VAL A CA  
3226  C C   . VAL A  425 ? 0.1880 0.3130 0.4594 0.0002  0.0213  -0.0258 425 VAL A C   
3227  O O   . VAL A  425 ? 0.2284 0.3605 0.5129 -0.0052 0.0207  -0.0318 425 VAL A O   
3228  C CB  . VAL A  425 ? 0.1569 0.2713 0.4031 0.0039  0.0133  -0.0253 425 VAL A CB  
3229  C CG1 . VAL A  425 ? 0.1239 0.2228 0.3603 0.0030  0.0215  -0.0217 425 VAL A CG1 
3230  C CG2 . VAL A  425 ? 0.1222 0.2374 0.3563 0.0093  0.0064  -0.0235 425 VAL A CG2 
3231  N N   . TYR A  426 ? 0.1897 0.3070 0.4571 0.0011  0.0289  -0.0215 426 TYR A N   
3232  C CA  . TYR A  426 ? 0.2218 0.3345 0.4956 -0.0048 0.0387  -0.0230 426 TYR A CA  
3233  C C   . TYR A  426 ? 0.2941 0.3878 0.5507 -0.0061 0.0447  -0.0197 426 TYR A C   
3234  O O   . TYR A  426 ? 0.3175 0.4035 0.5596 -0.0011 0.0427  -0.0151 426 TYR A O   
3235  C CB  . TYR A  426 ? 0.1622 0.2809 0.4451 -0.0028 0.0435  -0.0214 426 TYR A CB  
3236  C CG  . TYR A  426 ? 0.1817 0.3195 0.4839 -0.0009 0.0374  -0.0249 426 TYR A CG  
3237  C CD1 . TYR A  426 ? 0.1852 0.3290 0.4844 0.0062  0.0286  -0.0224 426 TYR A CD1 
3238  C CD2 . TYR A  426 ? 0.2047 0.3516 0.5229 -0.0063 0.0397  -0.0301 426 TYR A CD2 
3239  C CE1 . TYR A  426 ? 0.1975 0.3534 0.5048 0.0087  0.0216  -0.0243 426 TYR A CE1 
3240  C CE2 . TYR A  426 ? 0.2293 0.3899 0.5571 -0.0038 0.0321  -0.0325 426 TYR A CE2 
3241  C CZ  . TYR A  426 ? 0.2425 0.4075 0.5646 0.0040  0.0230  -0.0295 426 TYR A CZ  
3242  O OH  . TYR A  426 ? 0.2808 0.4589 0.6123 0.0071  0.0154  -0.0313 426 TYR A OH  
3243  N N   . ALA A  427 ? 0.2981 0.3842 0.5569 -0.0129 0.0517  -0.0221 427 ALA A N   
3244  C CA  . ALA A  427 ? 0.2795 0.3462 0.5216 -0.0139 0.0568  -0.0189 427 ALA A CA  
3245  C C   . ALA A  427 ? 0.2653 0.3217 0.5059 -0.0184 0.0684  -0.0170 427 ALA A C   
3246  O O   . ALA A  427 ? 0.1608 0.2241 0.4165 -0.0242 0.0740  -0.0204 427 ALA A O   
3247  C CB  . ALA A  427 ? 0.1532 0.2149 0.3936 -0.0172 0.0538  -0.0230 427 ALA A CB  
3248  N N   . TYR A  428 ? 0.2196 0.2594 0.4416 -0.0155 0.0720  -0.0113 428 TYR A N   
3249  C CA  . TYR A  428 ? 0.2399 0.2672 0.4558 -0.0190 0.0832  -0.0086 428 TYR A CA  
3250  C C   . TYR A  428 ? 0.2873 0.2926 0.4834 -0.0185 0.0863  -0.0041 428 TYR A C   
3251  O O   . TYR A  428 ? 0.3040 0.3035 0.4880 -0.0127 0.0798  -0.0013 428 TYR A O   
3252  C CB  . TYR A  428 ? 0.2721 0.3021 0.4844 -0.0148 0.0859  -0.0055 428 TYR A CB  
3253  C CG  . TYR A  428 ? 0.2883 0.3104 0.4825 -0.0073 0.0803  -0.0005 428 TYR A CG  
3254  C CD1 . TYR A  428 ? 0.2665 0.2700 0.4409 -0.0058 0.0840  0.0044  428 TYR A CD1 
3255  C CD2 . TYR A  428 ? 0.3032 0.3365 0.5007 -0.0017 0.0712  -0.0006 428 TYR A CD2 
3256  C CE1 . TYR A  428 ? 0.2556 0.2537 0.4160 0.0007  0.0780  0.0082  428 TYR A CE1 
3257  C CE2 . TYR A  428 ? 0.2923 0.3195 0.4761 0.0041  0.0664  0.0035  428 TYR A CE2 
3258  C CZ  . TYR A  428 ? 0.2897 0.3001 0.4559 0.0053  0.0694  0.0075  428 TYR A CZ  
3259  O OH  . TYR A  428 ? 0.3323 0.3378 0.4864 0.0109  0.0637  0.0111  428 TYR A OH  
3260  N N   . ILE A  429 ? 0.3902 0.3831 0.5835 -0.0246 0.0966  -0.0032 429 ILE A N   
3261  C CA  . ILE A  429 ? 0.4045 0.3742 0.5761 -0.0230 0.1008  0.0027  429 ILE A CA  
3262  C C   . ILE A  429 ? 0.4192 0.3823 0.5814 -0.0230 0.1099  0.0068  429 ILE A C   
3263  O O   . ILE A  429 ? 0.4305 0.3988 0.6040 -0.0291 0.1190  0.0045  429 ILE A O   
3264  C CB  . ILE A  429 ? 0.2783 0.2340 0.4497 -0.0295 0.1056  0.0014  429 ILE A CB  
3265  C CG1 . ILE A  429 ? 0.3512 0.2812 0.5001 -0.0283 0.1122  0.0085  429 ILE A CG1 
3266  C CG2 . ILE A  429 ? 0.2457 0.2080 0.4355 -0.0396 0.1141  -0.0033 429 ILE A CG2 
3267  C CD1 . ILE A  429 ? 0.4152 0.3373 0.5461 -0.0186 0.1042  0.0134  429 ILE A CD1 
3268  N N   . PHE A  430 ? 0.2932 0.2461 0.4355 -0.0161 0.1071  0.0122  430 PHE A N   
3269  C CA  . PHE A  430 ? 0.2980 0.2430 0.4272 -0.0151 0.1146  0.0158  430 PHE A CA  
3270  C C   . PHE A  430 ? 0.3276 0.2476 0.4361 -0.0170 0.1230  0.0214  430 PHE A C   
3271  O O   . PHE A  430 ? 0.3121 0.2178 0.4027 -0.0117 0.1176  0.0260  430 PHE A O   
3272  C CB  . PHE A  430 ? 0.2459 0.1928 0.3637 -0.0067 0.1058  0.0180  430 PHE A CB  
3273  C CG  . PHE A  430 ? 0.3178 0.2553 0.4192 -0.0049 0.1120  0.0210  430 PHE A CG  
3274  C CD1 . PHE A  430 ? 0.2990 0.2482 0.4099 -0.0057 0.1166  0.0177  430 PHE A CD1 
3275  C CD2 . PHE A  430 ? 0.3434 0.2596 0.4187 -0.0018 0.1130  0.0269  430 PHE A CD2 
3276  C CE1 . PHE A  430 ? 0.3306 0.2700 0.4246 -0.0039 0.1230  0.0197  430 PHE A CE1 
3277  C CE2 . PHE A  430 ? 0.3462 0.2524 0.4032 0.0000  0.1185  0.0293  430 PHE A CE2 
3278  C CZ  . PHE A  430 ? 0.3454 0.2629 0.4113 -0.0012 0.1239  0.0254  430 PHE A CZ  
3279  N N   . GLU A  431 ? 0.3647 0.2796 0.4761 -0.0244 0.1364  0.0212  431 GLU A N   
3280  C CA  . GLU A  431 ? 0.3870 0.2770 0.4804 -0.0278 0.1460  0.0267  431 GLU A CA  
3281  C C   . GLU A  431 ? 0.3958 0.2687 0.4643 -0.0260 0.1550  0.0327  431 GLU A C   
3282  O O   . GLU A  431 ? 0.4071 0.2579 0.4587 -0.0287 0.1635  0.0381  431 GLU A O   
3283  C CB  . GLU A  431 ? 0.4777 0.3688 0.5891 -0.0385 0.1559  0.0233  431 GLU A CB  
3284  C CG  . GLU A  431 ? 0.5226 0.4149 0.6448 -0.0403 0.1483  0.0200  431 GLU A CG  
3285  C CD  . GLU A  431 ? 0.5966 0.4969 0.7427 -0.0514 0.1556  0.0140  431 GLU A CD  
3286  O OE1 . GLU A  431 ? 0.6125 0.5320 0.7784 -0.0555 0.1597  0.0094  431 GLU A OE1 
3287  O OE2 . GLU A  431 ? 0.6346 0.5219 0.7806 -0.0561 0.1570  0.0137  431 GLU A OE2 
3288  N N   . HIS A  432 ? 0.4781 0.3596 0.5429 -0.0216 0.1535  0.0318  432 HIS A N   
3289  C CA  . HIS A  432 ? 0.5215 0.3866 0.5614 -0.0203 0.1630  0.0365  432 HIS A CA  
3290  C C   . HIS A  432 ? 0.5036 0.3513 0.5126 -0.0114 0.1543  0.0425  432 HIS A C   
3291  O O   . HIS A  432 ? 0.4699 0.3269 0.4785 -0.0046 0.1417  0.0408  432 HIS A O   
3292  C CB  . HIS A  432 ? 0.5484 0.4284 0.5978 -0.0207 0.1689  0.0320  432 HIS A CB  
3293  C CG  . HIS A  432 ? 0.5835 0.4466 0.6045 -0.0180 0.1772  0.0360  432 HIS A CG  
3294  N ND1 . HIS A  432 ? 0.6057 0.4525 0.6139 -0.0236 0.1941  0.0397  432 HIS A ND1 
3295  C CD2 . HIS A  432 ? 0.5824 0.4411 0.5837 -0.0105 0.1708  0.0368  432 HIS A CD2 
3296  C CE1 . HIS A  432 ? 0.6347 0.4678 0.6152 -0.0191 0.1980  0.0426  432 HIS A CE1 
3297  N NE2 . HIS A  432 ? 0.6119 0.4519 0.5877 -0.0112 0.1835  0.0406  432 HIS A NE2 
3298  N N   . ARG A  433 ? 0.4865 0.3086 0.4696 -0.0117 0.1615  0.0494  433 ARG A N   
3299  C CA  . ARG A  433 ? 0.5008 0.3046 0.4522 -0.0033 0.1540  0.0556  433 ARG A CA  
3300  C C   . ARG A  433 ? 0.5531 0.3540 0.4866 -0.0007 0.1582  0.0553  433 ARG A C   
3301  O O   . ARG A  433 ? 0.5781 0.3737 0.5072 -0.0059 0.1737  0.0555  433 ARG A O   
3302  C CB  . ARG A  433 ? 0.5243 0.2999 0.4532 -0.0042 0.1600  0.0637  433 ARG A CB  
3303  C CG  . ARG A  433 ? 0.5499 0.3054 0.4450 0.0052  0.1512  0.0706  433 ARG A CG  
3304  C CD  . ARG A  433 ? 0.6117 0.3391 0.4861 0.0053  0.1558  0.0791  433 ARG A CD  
3305  N NE  . ARG A  433 ? 0.6840 0.3904 0.5224 0.0143  0.1492  0.0863  433 ARG A NE  
3306  C CZ  . ARG A  433 ? 0.7449 0.4480 0.5755 0.0237  0.1328  0.0890  433 ARG A CZ  
3307  N NH1 . ARG A  433 ? 0.7356 0.4540 0.5910 0.0253  0.1226  0.0852  433 ARG A NH1 
3308  N NH2 . ARG A  433 ? 0.8020 0.4866 0.5998 0.0316  0.1264  0.0952  433 ARG A NH2 
3309  N N   . ALA A  434 ? 0.5782 0.3826 0.5019 0.0072  0.1448  0.0545  434 ALA A N   
3310  C CA  . ALA A  434 ? 0.5862 0.3869 0.4917 0.0100  0.1475  0.0533  434 ALA A CA  
3311  C C   . ALA A  434 ? 0.6355 0.4077 0.5038 0.0109  0.1567  0.0603  434 ALA A C   
3312  O O   . ALA A  434 ? 0.6532 0.4068 0.5020 0.0141  0.1522  0.0672  434 ALA A O   
3313  C CB  . ALA A  434 ? 0.5378 0.3469 0.4407 0.0176  0.1302  0.0507  434 ALA A CB  
3314  N N   . SER A  435 ? 0.6109 0.3794 0.4689 0.0085  0.1699  0.0586  435 SER A N   
3315  C CA  . SER A  435 ? 0.6395 0.3806 0.4590 0.0096  0.1796  0.0650  435 SER A CA  
3316  C C   . SER A  435 ? 0.7027 0.4314 0.4919 0.0192  0.1637  0.0675  435 SER A C   
3317  O O   . SER A  435 ? 0.7497 0.4533 0.5051 0.0225  0.1642  0.0751  435 SER A O   
3318  C CB  . SER A  435 ? 0.6151 0.3570 0.4319 0.0052  0.1981  0.0615  435 SER A CB  
3319  O OG  . SER A  435 ? 0.5578 0.3036 0.3635 0.0107  0.1924  0.0564  435 SER A OG  
3320  N N   . THR A  436 ? 0.8103 0.5567 0.6124 0.0235  0.1489  0.0613  436 THR A N   
3321  C CA  . THR A  436 ? 0.9073 0.6458 0.6853 0.0319  0.1325  0.0619  436 THR A CA  
3322  C C   . THR A  436 ? 0.8765 0.6120 0.6547 0.0369  0.1167  0.0669  436 THR A C   
3323  O O   . THR A  436 ? 0.8860 0.6169 0.6481 0.0441  0.1010  0.0678  436 THR A O   
3324  C CB  . THR A  436 ? 1.1308 0.8898 0.9255 0.0338  0.1230  0.0530  436 THR A CB  
3325  O OG1 . THR A  436 ? 1.2022 0.9726 1.0135 0.0285  0.1376  0.0473  436 THR A OG1 
3326  C CG2 . THR A  436 ? 1.1393 0.8862 0.9027 0.0405  0.1121  0.0520  436 THR A CG2 
3327  N N   . LEU A  437 ? 0.7993 0.5379 0.5966 0.0332  0.1205  0.0697  437 LEU A N   
3328  C CA  . LEU A  437 ? 0.7402 0.4803 0.5451 0.0379  0.1063  0.0728  437 LEU A CA  
3329  C C   . LEU A  437 ? 0.8009 0.5158 0.5714 0.0453  0.0989  0.0812  437 LEU A C   
3330  O O   . LEU A  437 ? 0.8584 0.5495 0.6013 0.0443  0.1098  0.0875  437 LEU A O   
3331  C CB  . LEU A  437 ? 0.5878 0.3357 0.4201 0.0320  0.1128  0.0728  437 LEU A CB  
3332  C CG  . LEU A  437 ? 0.5493 0.3155 0.4071 0.0354  0.0979  0.0700  437 LEU A CG  
3333  C CD1 . LEU A  437 ? 0.5282 0.3158 0.4216 0.0283  0.1034  0.0640  437 LEU A CD1 
3334  C CD2 . LEU A  437 ? 0.5567 0.3074 0.4038 0.0408  0.0909  0.0769  437 LEU A CD2 
3335  N N   . THR A  438 ? 0.8335 0.5545 0.6070 0.0527  0.0803  0.0813  438 THR A N   
3336  C CA  . THR A  438 ? 0.8531 0.5548 0.5975 0.0617  0.0685  0.0882  438 THR A CA  
3337  C C   . THR A  438 ? 0.8426 0.5339 0.5898 0.0646  0.0667  0.0951  438 THR A C   
3338  O O   . THR A  438 ? 0.8720 0.5367 0.5906 0.0674  0.0709  0.1036  438 THR A O   
3339  C CB  . THR A  438 ? 0.8946 0.6101 0.6427 0.0684  0.0487  0.0840  438 THR A CB  
3340  O OG1 . THR A  438 ? 0.8893 0.6305 0.6666 0.0635  0.0489  0.0749  438 THR A OG1 
3341  C CG2 . THR A  438 ? 0.9188 0.6167 0.6286 0.0735  0.0433  0.0858  438 THR A CG2 
3342  N N   . TRP A  439 ? 0.6478 0.3592 0.4282 0.0645  0.0602  0.0913  439 TRP A N   
3343  C CA  . TRP A  439 ? 0.6048 0.3097 0.3938 0.0670  0.0585  0.0958  439 TRP A CA  
3344  C C   . TRP A  439 ? 0.6411 0.3233 0.4173 0.0613  0.0758  0.1016  439 TRP A C   
3345  O O   . TRP A  439 ? 0.6150 0.2982 0.3936 0.0524  0.0909  0.0992  439 TRP A O   
3346  C CB  . TRP A  439 ? 0.6040 0.3345 0.4323 0.0633  0.0570  0.0889  439 TRP A CB  
3347  C CG  . TRP A  439 ? 0.5775 0.3324 0.4248 0.0670  0.0428  0.0830  439 TRP A CG  
3348  C CD1 . TRP A  439 ? 0.5261 0.3026 0.3916 0.0623  0.0432  0.0755  439 TRP A CD1 
3349  C CD2 . TRP A  439 ? 0.6046 0.3655 0.4571 0.0761  0.0264  0.0840  439 TRP A CD2 
3350  N NE1 . TRP A  439 ? 0.5192 0.3137 0.3998 0.0671  0.0285  0.0720  439 TRP A NE1 
3351  C CE2 . TRP A  439 ? 0.5646 0.3510 0.4386 0.0755  0.0181  0.0769  439 TRP A CE2 
3352  C CE3 . TRP A  439 ? 0.6358 0.3830 0.4777 0.0850  0.0181  0.0903  439 TRP A CE3 
3353  C CZ2 . TRP A  439 ? 0.5531 0.3529 0.4395 0.0826  0.0025  0.0757  439 TRP A CZ2 
3354  C CZ3 . TRP A  439 ? 0.6140 0.3756 0.4691 0.0929  0.0018  0.0888  439 TRP A CZ3 
3355  C CH2 . TRP A  439 ? 0.5583 0.3464 0.4359 0.0912  -0.0054 0.0814  439 TRP A CH2 
3356  N N   . PRO A  440 ? 0.7208 0.3825 0.4848 0.0663  0.0740  0.1092  440 PRO A N   
3357  C CA  . PRO A  440 ? 0.7487 0.3826 0.4940 0.0620  0.0895  0.1166  440 PRO A CA  
3358  C C   . PRO A  440 ? 0.7060 0.3483 0.4771 0.0498  0.1053  0.1120  440 PRO A C   
3359  O O   . PRO A  440 ? 0.6509 0.3204 0.4529 0.0453  0.1041  0.1032  440 PRO A O   
3360  C CB  . PRO A  440 ? 0.9836 0.6008 0.7212 0.0710  0.0804  0.1236  440 PRO A CB  
3361  C CG  . PRO A  440 ? 0.9603 0.6044 0.7281 0.0760  0.0652  0.1169  440 PRO A CG  
3362  C CD  . PRO A  440 ? 0.9282 0.5933 0.6995 0.0763  0.0575  0.1108  440 PRO A CD  
3363  N N   . LEU A  441 ? 0.8466 0.4650 0.6048 0.0445  0.1200  0.1181  441 LEU A N   
3364  C CA  . LEU A  441 ? 0.8622 0.4880 0.6438 0.0317  0.1360  0.1134  441 LEU A CA  
3365  C C   . LEU A  441 ? 0.8391 0.4771 0.6519 0.0298  0.1319  0.1085  441 LEU A C   
3366  O O   . LEU A  441 ? 0.7947 0.4536 0.6367 0.0212  0.1374  0.1004  441 LEU A O   
3367  C CB  . LEU A  441 ? 0.9411 0.5374 0.6997 0.0251  0.1546  0.1212  441 LEU A CB  
3368  C CG  . LEU A  441 ? 0.9054 0.5120 0.6861 0.0108  0.1729  0.1157  441 LEU A CG  
3369  C CD1 . LEU A  441 ? 0.8977 0.5064 0.7033 0.0043  0.1757  0.1125  441 LEU A CD1 
3370  C CD2 . LEU A  441 ? 0.8333 0.4731 0.6392 0.0079  0.1705  0.1056  441 LEU A CD2 
3371  N N   . TRP A  442 ? 0.9618 0.5868 0.7681 0.0383  0.1222  0.1130  442 TRP A N   
3372  C CA  . TRP A  442 ? 0.9474 0.5789 0.7791 0.0371  0.1197  0.1088  442 TRP A CA  
3373  C C   . TRP A  442 ? 0.9105 0.5766 0.7738 0.0375  0.1096  0.0986  442 TRP A C   
3374  O O   . TRP A  442 ? 0.9397 0.6156 0.8269 0.0336  0.1104  0.0928  442 TRP A O   
3375  C CB  . TRP A  442 ? 0.8813 0.4902 0.6981 0.0475  0.1116  0.1160  442 TRP A CB  
3376  C CG  . TRP A  442 ? 0.8719 0.4894 0.6837 0.0612  0.0929  0.1172  442 TRP A CG  
3377  C CD1 . TRP A  442 ? 0.9136 0.5165 0.6959 0.0707  0.0849  0.1249  442 TRP A CD1 
3378  C CD2 . TRP A  442 ? 0.8237 0.4669 0.6611 0.0668  0.0795  0.1103  442 TRP A CD2 
3379  N NE1 . TRP A  442 ? 0.9055 0.5238 0.6954 0.0816  0.0671  0.1230  442 TRP A NE1 
3380  C CE2 . TRP A  442 ? 0.8431 0.4865 0.6671 0.0792  0.0642  0.1142  442 TRP A CE2 
3381  C CE3 . TRP A  442 ? 0.7671 0.4329 0.6368 0.0624  0.0791  0.1011  442 TRP A CE3 
3382  C CZ2 . TRP A  442 ? 0.7860 0.4525 0.6302 0.0868  0.0497  0.1093  442 TRP A CZ2 
3383  C CZ3 . TRP A  442 ? 0.7402 0.4272 0.6268 0.0703  0.0652  0.0968  442 TRP A CZ3 
3384  C CH2 . TRP A  442 ? 0.7468 0.4344 0.6217 0.0821  0.0513  0.1009  442 TRP A CH2 
3385  N N   . MET A  443 ? 0.7361 0.4195 0.5985 0.0421  0.1005  0.0963  443 MET A N   
3386  C CA  . MET A  443 ? 0.6464 0.3612 0.5362 0.0430  0.0907  0.0877  443 MET A CA  
3387  C C   . MET A  443 ? 0.6398 0.3754 0.5520 0.0323  0.0994  0.0798  443 MET A C   
3388  O O   . MET A  443 ? 0.6282 0.3890 0.5633 0.0322  0.0926  0.0728  443 MET A O   
3389  C CB  . MET A  443 ? 0.5223 0.2464 0.4032 0.0518  0.0771  0.0882  443 MET A CB  
3390  C CG  . MET A  443 ? 0.5145 0.2197 0.3731 0.0631  0.0671  0.0960  443 MET A CG  
3391  S SD  . MET A  443 ? 0.7382 0.4614 0.5961 0.0725  0.0485  0.0940  443 MET A SD  
3392  C CE  . MET A  443 ? 0.4551 0.2125 0.3536 0.0696  0.0440  0.0840  443 MET A CE  
3393  N N   . GLY A  444 ? 0.6323 0.3573 0.5379 0.0236  0.1144  0.0812  444 GLY A N   
3394  C CA  . GLY A  444 ? 0.5917 0.3349 0.5204 0.0131  0.1239  0.0740  444 GLY A CA  
3395  C C   . GLY A  444 ? 0.5400 0.3070 0.4788 0.0132  0.1202  0.0685  444 GLY A C   
3396  O O   . GLY A  444 ? 0.5460 0.3083 0.4665 0.0158  0.1210  0.0710  444 GLY A O   
3397  N N   . VAL A  445 ? 0.4518 0.2436 0.4190 0.0105  0.1161  0.0608  445 VAL A N   
3398  C CA  . VAL A  445 ? 0.3840 0.1988 0.3635 0.0109  0.1118  0.0554  445 VAL A CA  
3399  C C   . VAL A  445 ? 0.3847 0.2134 0.3744 0.0180  0.0966  0.0531  445 VAL A C   
3400  O O   . VAL A  445 ? 0.3414 0.1876 0.3542 0.0157  0.0936  0.0475  445 VAL A O   
3401  C CB  . VAL A  445 ? 0.4010 0.2341 0.4067 0.0019  0.1197  0.0485  445 VAL A CB  
3402  C CG1 . VAL A  445 ? 0.3931 0.2459 0.4081 0.0029  0.1170  0.0440  445 VAL A CG1 
3403  C CG2 . VAL A  445 ? 0.4231 0.2428 0.4247 -0.0065 0.1360  0.0503  445 VAL A CG2 
3404  N N   . PRO A  446 ? 0.4872 0.3081 0.4593 0.0266  0.0869  0.0574  446 PRO A N   
3405  C CA  . PRO A  446 ? 0.4766 0.3076 0.4568 0.0339  0.0731  0.0565  446 PRO A CA  
3406  C C   . PRO A  446 ? 0.4350 0.2916 0.4348 0.0339  0.0664  0.0505  446 PRO A C   
3407  O O   . PRO A  446 ? 0.4202 0.2859 0.4243 0.0300  0.0706  0.0474  446 PRO A O   
3408  C CB  . PRO A  446 ? 0.3799 0.1953 0.3351 0.0423  0.0655  0.0628  446 PRO A CB  
3409  C CG  . PRO A  446 ? 0.3972 0.2028 0.3337 0.0396  0.0729  0.0646  446 PRO A CG  
3410  C CD  . PRO A  446 ? 0.3991 0.2022 0.3427 0.0299  0.0886  0.0630  446 PRO A CD  
3411  N N   . HIS A  447 ? 0.3772 0.2444 0.3887 0.0387  0.0567  0.0490  447 HIS A N   
3412  C CA  . HIS A  447 ? 0.3295 0.2198 0.3607 0.0388  0.0505  0.0440  447 HIS A CA  
3413  C C   . HIS A  447 ? 0.3618 0.2580 0.3876 0.0401  0.0466  0.0434  447 HIS A C   
3414  O O   . HIS A  447 ? 0.4300 0.3174 0.4400 0.0453  0.0404  0.0468  447 HIS A O   
3415  C CB  . HIS A  447 ? 0.3111 0.2064 0.3489 0.0454  0.0409  0.0445  447 HIS A CB  
3416  C CG  . HIS A  447 ? 0.3401 0.2576 0.3984 0.0452  0.0359  0.0399  447 HIS A CG  
3417  N ND1 . HIS A  447 ? 0.3591 0.2883 0.4326 0.0394  0.0408  0.0353  447 HIS A ND1 
3418  C CD2 . HIS A  447 ? 0.3696 0.2993 0.4355 0.0500  0.0267  0.0394  447 HIS A CD2 
3419  C CE1 . HIS A  447 ? 0.3757 0.3220 0.4631 0.0410  0.0350  0.0327  447 HIS A CE1 
3420  N NE2 . HIS A  447 ? 0.3817 0.3287 0.4655 0.0470  0.0271  0.0351  447 HIS A NE2 
3421  N N   . GLY A  448 ? 0.3314 0.2417 0.3700 0.0356  0.0497  0.0390  448 GLY A N   
3422  C CA  . GLY A  448 ? 0.3070 0.2236 0.3429 0.0366  0.0459  0.0374  448 GLY A CA  
3423  C C   . GLY A  448 ? 0.3025 0.2102 0.3251 0.0337  0.0543  0.0372  448 GLY A C   
3424  O O   . GLY A  448 ? 0.2963 0.2088 0.3171 0.0343  0.0520  0.0349  448 GLY A O   
3425  N N   . TYR A  449 ? 0.3813 0.2758 0.3949 0.0302  0.0648  0.0394  449 TYR A N   
3426  C CA  . TYR A  449 ? 0.4483 0.3319 0.4461 0.0278  0.0742  0.0400  449 TYR A CA  
3427  C C   . TYR A  449 ? 0.4836 0.3781 0.4971 0.0216  0.0847  0.0355  449 TYR A C   
3428  O O   . TYR A  449 ? 0.5725 0.4589 0.5755 0.0191  0.0949  0.0356  449 TYR A O   
3429  C CB  . TYR A  449 ? 0.5487 0.4083 0.5220 0.0285  0.0797  0.0462  449 TYR A CB  
3430  C CG  . TYR A  449 ? 0.6412 0.4911 0.5959 0.0362  0.0676  0.0500  449 TYR A CG  
3431  C CD1 . TYR A  449 ? 0.6756 0.5300 0.6386 0.0408  0.0570  0.0513  449 TYR A CD1 
3432  C CD2 . TYR A  449 ? 0.7017 0.5401 0.6322 0.0393  0.0660  0.0515  449 TYR A CD2 
3433  C CE1 . TYR A  449 ? 0.7136 0.5622 0.6635 0.0482  0.0450  0.0543  449 TYR A CE1 
3434  C CE2 . TYR A  449 ? 0.7601 0.5916 0.6753 0.0466  0.0529  0.0544  449 TYR A CE2 
3435  C CZ  . TYR A  449 ? 0.7488 0.5863 0.6752 0.0511  0.0423  0.0559  449 TYR A CZ  
3436  O OH  . TYR A  449 ? 0.7610 0.5940 0.6756 0.0586  0.0287  0.0584  449 TYR A OH  
3437  N N   . GLU A  450 ? 0.4162 0.3292 0.4547 0.0195  0.0823  0.0315  450 GLU A N   
3438  C CA  . GLU A  450 ? 0.4104 0.3370 0.4661 0.0153  0.0892  0.0267  450 GLU A CA  
3439  C C   . GLU A  450 ? 0.4295 0.3662 0.4887 0.0188  0.0827  0.0239  450 GLU A C   
3440  O O   . GLU A  450 ? 0.4647 0.4103 0.5342 0.0171  0.0880  0.0202  450 GLU A O   
3441  C CB  . GLU A  450 ? 0.3464 0.2875 0.4263 0.0116  0.0888  0.0237  450 GLU A CB  
3442  C CG  . GLU A  450 ? 0.3293 0.2871 0.4244 0.0146  0.0777  0.0213  450 GLU A CG  
3443  C CD  . GLU A  450 ? 0.3250 0.2784 0.4121 0.0197  0.0675  0.0243  450 GLU A CD  
3444  O OE1 . GLU A  450 ? 0.3142 0.2517 0.3827 0.0220  0.0672  0.0283  450 GLU A OE1 
3445  O OE2 . GLU A  450 ? 0.3361 0.3021 0.4354 0.0216  0.0599  0.0228  450 GLU A OE2 
3446  N N   . ILE A  451 ? 0.3822 0.3175 0.4339 0.0238  0.0714  0.0254  451 ILE A N   
3447  C CA  . ILE A  451 ? 0.3497 0.2948 0.4072 0.0264  0.0645  0.0225  451 ILE A CA  
3448  C C   . ILE A  451 ? 0.3614 0.3001 0.4075 0.0264  0.0707  0.0203  451 ILE A C   
3449  O O   . ILE A  451 ? 0.3684 0.3172 0.4271 0.0258  0.0731  0.0165  451 ILE A O   
3450  C CB  . ILE A  451 ? 0.2973 0.2409 0.3481 0.0310  0.0519  0.0243  451 ILE A CB  
3451  C CG1 . ILE A  451 ? 0.2238 0.1777 0.2898 0.0317  0.0457  0.0252  451 ILE A CG1 
3452  C CG2 . ILE A  451 ? 0.2352 0.1846 0.2882 0.0327  0.0465  0.0211  451 ILE A CG2 
3453  C CD1 . ILE A  451 ? 0.2168 0.1763 0.2852 0.0356  0.0339  0.0256  451 ILE A CD1 
3454  N N   . GLU A  452 ? 0.3647 0.2857 0.3861 0.0277  0.0734  0.0229  452 GLU A N   
3455  C CA  . GLU A  452 ? 0.4053 0.3172 0.4107 0.0282  0.0795  0.0208  452 GLU A CA  
3456  C C   . GLU A  452 ? 0.3491 0.2657 0.3650 0.0242  0.0939  0.0180  452 GLU A C   
3457  O O   . GLU A  452 ? 0.3260 0.2414 0.3377 0.0250  0.0992  0.0144  452 GLU A O   
3458  C CB  . GLU A  452 ? 0.5735 0.4639 0.5478 0.0303  0.0803  0.0249  452 GLU A CB  
3459  C CG  . GLU A  452 ? 0.6699 0.5494 0.6364 0.0267  0.0930  0.0286  452 GLU A CG  
3460  C CD  . GLU A  452 ? 0.7728 0.6324 0.7126 0.0296  0.0898  0.0348  452 GLU A CD  
3461  O OE1 . GLU A  452 ? 0.7616 0.6208 0.6970 0.0342  0.0758  0.0364  452 GLU A OE1 
3462  O OE2 . GLU A  452 ? 0.8611 0.7053 0.7848 0.0273  0.1014  0.0383  452 GLU A OE2 
3463  N N   . PHE A  453 ? 0.3645 0.2867 0.3949 0.0200  0.1002  0.0191  453 PHE A N   
3464  C CA  . PHE A  453 ? 0.4059 0.3369 0.4525 0.0158  0.1127  0.0159  453 PHE A CA  
3465  C C   . PHE A  453 ? 0.3943 0.3463 0.4682 0.0163  0.1082  0.0113  453 PHE A C   
3466  O O   . PHE A  453 ? 0.3958 0.3566 0.4832 0.0150  0.1165  0.0077  453 PHE A O   
3467  C CB  . PHE A  453 ? 0.4961 0.4245 0.5482 0.0102  0.1214  0.0182  453 PHE A CB  
3468  C CG  . PHE A  453 ? 0.5506 0.4573 0.5766 0.0088  0.1309  0.0226  453 PHE A CG  
3469  C CD1 . PHE A  453 ? 0.5992 0.4896 0.6034 0.0115  0.1243  0.0281  453 PHE A CD1 
3470  C CD2 . PHE A  453 ? 0.5622 0.4647 0.5852 0.0051  0.1468  0.0216  453 PHE A CD2 
3471  C CE1 . PHE A  453 ? 0.6601 0.5286 0.6377 0.0108  0.1328  0.0330  453 PHE A CE1 
3472  C CE2 . PHE A  453 ? 0.6341 0.5148 0.6305 0.0038  0.1566  0.0264  453 PHE A CE2 
3473  C CZ  . PHE A  453 ? 0.6818 0.5446 0.6544 0.0067  0.1492  0.0324  453 PHE A CZ  
3474  N N   . ILE A  454 ? 0.4852 0.4454 0.5675 0.0186  0.0955  0.0119  454 ILE A N   
3475  C CA  . ILE A  454 ? 0.4385 0.4167 0.5438 0.0197  0.0904  0.0086  454 ILE A CA  
3476  C C   . ILE A  454 ? 0.4483 0.4257 0.5492 0.0236  0.0879  0.0060  454 ILE A C   
3477  O O   . ILE A  454 ? 0.4682 0.4558 0.5842 0.0245  0.0906  0.0025  454 ILE A O   
3478  C CB  . ILE A  454 ? 0.2762 0.2623 0.3905 0.0206  0.0789  0.0103  454 ILE A CB  
3479  C CG1 . ILE A  454 ? 0.2358 0.2252 0.3593 0.0164  0.0819  0.0111  454 ILE A CG1 
3480  C CG2 . ILE A  454 ? 0.2379 0.2390 0.3699 0.0227  0.0727  0.0079  454 ILE A CG2 
3481  C CD1 . ILE A  454 ? 0.1967 0.1993 0.3411 0.0129  0.0887  0.0074  454 ILE A CD1 
3482  N N   . PHE A  455 ? 0.3407 0.3053 0.4208 0.0262  0.0827  0.0073  455 PHE A N   
3483  C CA  . PHE A  455 ? 0.3402 0.3017 0.4141 0.0294  0.0796  0.0042  455 PHE A CA  
3484  C C   . PHE A  455 ? 0.3996 0.3516 0.4612 0.0296  0.0912  0.0013  455 PHE A C   
3485  O O   . PHE A  455 ? 0.4348 0.3820 0.4893 0.0323  0.0903  -0.0022 455 PHE A O   
3486  C CB  . PHE A  455 ? 0.3521 0.3045 0.4098 0.0317  0.0682  0.0059  455 PHE A CB  
3487  C CG  . PHE A  455 ? 0.3110 0.2746 0.3834 0.0324  0.0568  0.0072  455 PHE A CG  
3488  C CD1 . PHE A  455 ? 0.2907 0.2599 0.3706 0.0313  0.0535  0.0106  455 PHE A CD1 
3489  C CD2 . PHE A  455 ? 0.2958 0.2630 0.3739 0.0340  0.0501  0.0048  455 PHE A CD2 
3490  C CE1 . PHE A  455 ? 0.2778 0.2571 0.3703 0.0320  0.0444  0.0118  455 PHE A CE1 
3491  C CE2 . PHE A  455 ? 0.2940 0.2709 0.3852 0.0342  0.0410  0.0065  455 PHE A CE2 
3492  C CZ  . PHE A  455 ? 0.2750 0.2584 0.3732 0.0334  0.0384  0.0100  455 PHE A CZ  
3493  N N   . GLY A  456 ? 0.4970 0.4453 0.5555 0.0266  0.1027  0.0025  456 GLY A N   
3494  C CA  . GLY A  456 ? 0.5388 0.4798 0.5881 0.0264  0.1163  -0.0003 456 GLY A CA  
3495  C C   . GLY A  456 ? 0.5564 0.4772 0.5731 0.0287  0.1170  -0.0003 456 GLY A C   
3496  O O   . GLY A  456 ? 0.5868 0.5019 0.5950 0.0305  0.1247  -0.0044 456 GLY A O   
3497  N N   . LEU A  457 ? 0.3236 0.2333 0.3218 0.0292  0.1087  0.0041  457 LEU A N   
3498  C CA  . LEU A  457 ? 0.3526 0.2419 0.3171 0.0314  0.1084  0.0049  457 LEU A CA  
3499  C C   . LEU A  457 ? 0.3798 0.2551 0.3249 0.0297  0.1250  0.0058  457 LEU A C   
3500  O O   . LEU A  457 ? 0.4058 0.2652 0.3235 0.0323  0.1272  0.0042  457 LEU A O   
3501  C CB  . LEU A  457 ? 0.3557 0.2377 0.3072 0.0327  0.0959  0.0101  457 LEU A CB  
3502  C CG  . LEU A  457 ? 0.3478 0.2330 0.2998 0.0359  0.0796  0.0079  457 LEU A CG  
3503  C CD1 . LEU A  457 ? 0.3163 0.2218 0.3003 0.0350  0.0746  0.0061  457 LEU A CD1 
3504  C CD2 . LEU A  457 ? 0.3563 0.2331 0.2929 0.0380  0.0681  0.0127  457 LEU A CD2 
3505  N N   . PRO A  458 ? 0.5780 0.4576 0.5353 0.0252  0.1367  0.0085  458 PRO A N   
3506  C CA  . PRO A  458 ? 0.5916 0.4600 0.5347 0.0228  0.1551  0.0090  458 PRO A CA  
3507  C C   . PRO A  458 ? 0.6272 0.4993 0.5742 0.0243  0.1656  0.0022  458 PRO A C   
3508  O O   . PRO A  458 ? 0.6795 0.5395 0.6086 0.0234  0.1807  0.0020  458 PRO A O   
3509  C CB  . PRO A  458 ? 0.3895 0.2682 0.3559 0.0168  0.1636  0.0115  458 PRO A CB  
3510  C CG  . PRO A  458 ? 0.3730 0.2553 0.3460 0.0169  0.1494  0.0153  458 PRO A CG  
3511  C CD  . PRO A  458 ? 0.3993 0.2895 0.3770 0.0219  0.1333  0.0122  458 PRO A CD  
3512  N N   . LEU A  459 ? 0.4700 0.3579 0.4395 0.0267  0.1585  -0.0030 459 LEU A N   
3513  C CA  . LEU A  459 ? 0.4744 0.3651 0.4483 0.0294  0.1671  -0.0097 459 LEU A CA  
3514  C C   . LEU A  459 ? 0.5616 0.4328 0.5017 0.0336  0.1646  -0.0126 459 LEU A C   
3515  O O   . LEU A  459 ? 0.6161 0.4835 0.5509 0.0361  0.1743  -0.0183 459 LEU A O   
3516  C CB  . LEU A  459 ? 0.3612 0.2730 0.3688 0.0312  0.1601  -0.0137 459 LEU A CB  
3517  C CG  . LEU A  459 ? 0.3460 0.2764 0.3854 0.0278  0.1708  -0.0143 459 LEU A CG  
3518  C CD1 . LEU A  459 ? 0.3307 0.2684 0.3823 0.0228  0.1663  -0.0090 459 LEU A CD1 
3519  C CD2 . LEU A  459 ? 0.3259 0.2743 0.3945 0.0313  0.1679  -0.0194 459 LEU A CD2 
3520  N N   . ASP A  460 ? 0.6470 0.5060 0.5647 0.0348  0.1513  -0.0090 460 ASP A N   
3521  C CA  . ASP A  460 ? 0.7047 0.5431 0.5862 0.0383  0.1476  -0.0112 460 ASP A CA  
3522  C C   . ASP A  460 ? 0.8278 0.6469 0.6780 0.0371  0.1603  -0.0070 460 ASP A C   
3523  O O   . ASP A  460 ? 0.9011 0.7141 0.7423 0.0352  0.1577  0.0002  460 ASP A O   
3524  C CB  . ASP A  460 ? 0.7067 0.5421 0.5799 0.0400  0.1269  -0.0091 460 ASP A CB  
3525  C CG  . ASP A  460 ? 0.7930 0.6097 0.6324 0.0436  0.1202  -0.0128 460 ASP A CG  
3526  O OD1 . ASP A  460 ? 0.8152 0.6181 0.6320 0.0448  0.1325  -0.0161 460 ASP A OD1 
3527  O OD2 . ASP A  460 ? 0.8394 0.6554 0.6748 0.0452  0.1026  -0.0130 460 ASP A OD2 
3528  N N   . PRO A  461 ? 0.9001 0.7081 0.7319 0.0385  0.1744  -0.0115 461 PRO A N   
3529  C CA  . PRO A  461 ? 0.9213 0.7095 0.7210 0.0374  0.1899  -0.0080 461 PRO A CA  
3530  C C   . PRO A  461 ? 0.9586 0.7242 0.7176 0.0398  0.1790  -0.0032 461 PRO A C   
3531  O O   . PRO A  461 ? 1.0115 0.7634 0.7503 0.0380  0.1861  0.0042  461 PRO A O   
3532  C CB  . PRO A  461 ? 0.8642 0.6470 0.6542 0.0401  0.2033  -0.0161 461 PRO A CB  
3533  C CG  . PRO A  461 ? 0.8651 0.6555 0.6666 0.0440  0.1883  -0.0235 461 PRO A CG  
3534  C CD  . PRO A  461 ? 0.8223 0.6348 0.6618 0.0418  0.1763  -0.0206 461 PRO A CD  
3535  N N   . SER A  462 ? 0.7773 0.5391 0.5252 0.0439  0.1614  -0.0072 462 SER A N   
3536  C CA  . SER A  462 ? 0.7933 0.5358 0.5045 0.0470  0.1481  -0.0038 462 SER A CA  
3537  C C   . SER A  462 ? 0.7731 0.5173 0.4888 0.0460  0.1374  0.0054  462 SER A C   
3538  O O   . SER A  462 ? 0.7870 0.5158 0.4737 0.0491  0.1260  0.0094  462 SER A O   
3539  C CB  . SER A  462 ? 0.9721 0.7141 0.6777 0.0506  0.1303  -0.0113 462 SER A CB  
3540  O OG  . SER A  462 ? 0.9573 0.7194 0.6970 0.0497  0.1149  -0.0115 462 SER A OG  
3541  N N   . LEU A  463 ? 0.9808 0.7435 0.7324 0.0421  0.1401  0.0085  463 LEU A N   
3542  C CA  . LEU A  463 ? 0.9841 0.7496 0.7430 0.0416  0.1293  0.0161  463 LEU A CA  
3543  C C   . LEU A  463 ? 1.0282 0.7819 0.7759 0.0388  0.1414  0.0249  463 LEU A C   
3544  O O   . LEU A  463 ? 1.0489 0.8025 0.8008 0.0389  0.1329  0.0312  463 LEU A O   
3545  C CB  . LEU A  463 ? 0.7518 0.5429 0.5536 0.0397  0.1207  0.0144  463 LEU A CB  
3546  C CG  . LEU A  463 ? 0.7240 0.5220 0.5305 0.0431  0.1024  0.0090  463 LEU A CG  
3547  C CD1 . LEU A  463 ? 0.7108 0.5301 0.5531 0.0418  0.0916  0.0099  463 LEU A CD1 
3548  C CD2 . LEU A  463 ? 0.7164 0.4961 0.4878 0.0475  0.0891  0.0108  463 LEU A CD2 
3549  N N   . ASN A  464 ? 0.8714 0.6143 0.6046 0.0364  0.1615  0.0251  464 ASN A N   
3550  C CA  . ASN A  464 ? 0.8367 0.5650 0.5559 0.0329  0.1759  0.0335  464 ASN A CA  
3551  C C   . ASN A  464 ? 0.7637 0.5076 0.5190 0.0266  0.1825  0.0366  464 ASN A C   
3552  O O   . ASN A  464 ? 0.7653 0.4971 0.5116 0.0242  0.1873  0.0445  464 ASN A O   
3553  C CB  . ASN A  464 ? 1.1849 0.8890 0.8652 0.0374  0.1656  0.0415  464 ASN A CB  
3554  C CG  . ASN A  464 ? 1.2175 0.9027 0.8562 0.0431  0.1605  0.0387  464 ASN A CG  
3555  O OD1 . ASN A  464 ? 1.2565 0.9390 0.8861 0.0428  0.1721  0.0325  464 ASN A OD1 
3556  N ND2 . ASN A  464 ? 1.1915 0.8636 0.8050 0.0488  0.1428  0.0429  464 ASN A ND2 
3557  N N   . TYR A  465 ? 0.6631 0.4325 0.4583 0.0241  0.1823  0.0305  465 TYR A N   
3558  C CA  . TYR A  465 ? 0.6188 0.4030 0.4474 0.0176  0.1905  0.0321  465 TYR A CA  
3559  C C   . TYR A  465 ? 0.6251 0.4062 0.4545 0.0121  0.2145  0.0316  465 TYR A C   
3560  O O   . TYR A  465 ? 0.5954 0.3689 0.4071 0.0140  0.2243  0.0281  465 TYR A O   
3561  C CB  . TYR A  465 ? 0.6269 0.4392 0.4967 0.0171  0.1811  0.0260  465 TYR A CB  
3562  C CG  . TYR A  465 ? 0.6419 0.4596 0.5171 0.0208  0.1598  0.0274  465 TYR A CG  
3563  C CD1 . TYR A  465 ? 0.6671 0.4838 0.5311 0.0266  0.1454  0.0242  465 TYR A CD1 
3564  C CD2 . TYR A  465 ? 0.6394 0.4632 0.5314 0.0183  0.1546  0.0314  465 TYR A CD2 
3565  C CE1 . TYR A  465 ? 0.6601 0.4828 0.5309 0.0296  0.1269  0.0254  465 TYR A CE1 
3566  C CE2 . TYR A  465 ? 0.6320 0.4612 0.5293 0.0220  0.1364  0.0325  465 TYR A CE2 
3567  C CZ  . TYR A  465 ? 0.6599 0.4892 0.5473 0.0275  0.1229  0.0297  465 TYR A CZ  
3568  O OH  . TYR A  465 ? 0.6899 0.5256 0.5844 0.0308  0.1058  0.0307  465 TYR A OH  
3569  N N   . THR A  466 ? 0.7327 0.5192 0.5822 0.0052  0.2244  0.0348  466 THR A N   
3570  C CA  . THR A  466 ? 0.7610 0.5494 0.6201 -0.0013 0.2476  0.0339  466 THR A CA  
3571  C C   . THR A  466 ? 0.7596 0.5769 0.6600 -0.0031 0.2510  0.0253  466 THR A C   
3572  O O   . THR A  466 ? 0.7298 0.5666 0.6584 -0.0022 0.2370  0.0222  466 THR A O   
3573  C CB  . THR A  466 ? 0.7225 0.5049 0.5884 -0.0091 0.2569  0.0404  466 THR A CB  
3574  O OG1 . THR A  466 ? 0.6756 0.4814 0.5822 -0.0127 0.2488  0.0375  466 THR A OG1 
3575  C CG2 . THR A  466 ? 0.7746 0.5306 0.6051 -0.0063 0.2491  0.0495  466 THR A CG2 
3576  N N   . THR A  467 ? 0.7502 0.5699 0.6540 -0.0053 0.2701  0.0217  467 THR A N   
3577  C CA  . THR A  467 ? 0.7802 0.6268 0.7230 -0.0061 0.2750  0.0135  467 THR A CA  
3578  C C   . THR A  467 ? 0.7744 0.6444 0.7602 -0.0119 0.2707  0.0126  467 THR A C   
3579  O O   . THR A  467 ? 0.7793 0.6731 0.7972 -0.0101 0.2636  0.0065  467 THR A O   
3580  C CB  . THR A  467 ? 0.9184 0.7627 0.8584 -0.0082 0.2972  0.0106  467 THR A CB  
3581  O OG1 . THR A  467 ? 0.9776 0.8074 0.9059 -0.0149 0.3068  0.0168  467 THR A OG1 
3582  C CG2 . THR A  467 ? 0.9350 0.7616 0.8380 -0.0008 0.3001  0.0083  467 THR A CG2 
3583  N N   . GLU A  468 ? 0.7450 0.6071 0.7300 -0.0186 0.2742  0.0186  468 GLU A N   
3584  C CA  . GLU A  468 ? 0.7268 0.6082 0.7488 -0.0245 0.2689  0.0175  468 GLU A CA  
3585  C C   . GLU A  468 ? 0.6186 0.5087 0.6475 -0.0191 0.2451  0.0166  468 GLU A C   
3586  O O   . GLU A  468 ? 0.5627 0.4762 0.6251 -0.0198 0.2371  0.0119  468 GLU A O   
3587  C CB  . GLU A  468 ? 1.0766 0.9439 1.0927 -0.0326 0.2766  0.0238  468 GLU A CB  
3588  C CG  . GLU A  468 ? 1.2313 1.0929 1.2455 -0.0377 0.2913  0.0232  468 GLU A CG  
3589  C CD  . GLU A  468 ? 1.3787 1.2124 1.3482 -0.0342 0.3010  0.0282  468 GLU A CD  
3590  O OE1 . GLU A  468 ? 1.4468 1.2583 1.3827 -0.0307 0.2962  0.0352  468 GLU A OE1 
3591  O OE2 . GLU A  468 ? 1.3951 1.2290 1.3625 -0.0346 0.3126  0.0251  468 GLU A OE2 
3592  N N   . GLU A  469 ? 0.6568 0.5280 0.6533 -0.0137 0.2340  0.0212  469 GLU A N   
3593  C CA  . GLU A  469 ? 0.6056 0.4832 0.6055 -0.0082 0.2124  0.0207  469 GLU A CA  
3594  C C   . GLU A  469 ? 0.5973 0.4913 0.6107 -0.0026 0.2053  0.0139  469 GLU A C   
3595  O O   . GLU A  469 ? 0.5861 0.4951 0.6182 -0.0002 0.1908  0.0116  469 GLU A O   
3596  C CB  . GLU A  469 ? 0.5424 0.3962 0.5046 -0.0033 0.2032  0.0269  469 GLU A CB  
3597  C CG  . GLU A  469 ? 0.5491 0.3862 0.4988 -0.0073 0.2059  0.0343  469 GLU A CG  
3598  C CD  . GLU A  469 ? 0.5607 0.3734 0.4715 -0.0014 0.1975  0.0406  469 GLU A CD  
3599  O OE1 . GLU A  469 ? 0.5743 0.3712 0.4557 0.0015  0.2037  0.0418  469 GLU A OE1 
3600  O OE2 . GLU A  469 ? 0.5595 0.3688 0.4691 0.0007  0.1846  0.0442  469 GLU A OE2 
3601  N N   . ARG A  470 ? 0.5218 0.4115 0.5244 -0.0004 0.2161  0.0108  470 ARG A N   
3602  C CA  . ARG A  470 ? 0.4876 0.3897 0.5009 0.0053  0.2104  0.0043  470 ARG A CA  
3603  C C   . ARG A  470 ? 0.4390 0.3681 0.4950 0.0029  0.2117  -0.0005 470 ARG A C   
3604  O O   . ARG A  470 ? 0.4629 0.4066 0.5370 0.0064  0.1979  -0.0032 470 ARG A O   
3605  C CB  . ARG A  470 ? 0.7075 0.5972 0.6986 0.0083  0.2232  0.0015  470 ARG A CB  
3606  C CG  . ARG A  470 ? 0.7884 0.6833 0.7806 0.0152  0.2153  -0.0048 470 ARG A CG  
3607  C CD  . ARG A  470 ? 0.8656 0.7785 0.8866 0.0157  0.2267  -0.0114 470 ARG A CD  
3608  N NE  . ARG A  470 ? 0.9593 0.8647 0.9712 0.0130  0.2489  -0.0120 470 ARG A NE  
3609  C CZ  . ARG A  470 ? 1.0304 0.9514 1.0682 0.0123  0.2630  -0.0171 470 ARG A CZ  
3610  N NH1 . ARG A  470 ? 1.0098 0.9542 1.0833 0.0148  0.2561  -0.0219 470 ARG A NH1 
3611  N NH2 . ARG A  470 ? 1.1062 1.0192 1.1339 0.0092  0.2801  -0.0170 470 ARG A NH2 
3612  N N   . ILE A  471 ? 0.4578 0.3936 0.5301 -0.0032 0.2281  -0.0013 471 ILE A N   
3613  C CA  . ILE A  471 ? 0.4306 0.3932 0.5451 -0.0059 0.2293  -0.0060 471 ILE A CA  
3614  C C   . ILE A  471 ? 0.4092 0.3824 0.5402 -0.0074 0.2126  -0.0046 471 ILE A C   
3615  O O   . ILE A  471 ? 0.4063 0.3990 0.5623 -0.0046 0.2024  -0.0083 471 ILE A O   
3616  C CB  . ILE A  471 ? 0.4732 0.4398 0.6016 -0.0140 0.2465  -0.0063 471 ILE A CB  
3617  C CG1 . ILE A  471 ? 0.4966 0.4528 0.6081 -0.0124 0.2605  -0.0080 471 ILE A CG1 
3618  C CG2 . ILE A  471 ? 0.4370 0.4303 0.6058 -0.0166 0.2387  -0.0113 471 ILE A CG2 
3619  C CD1 . ILE A  471 ? 0.5227 0.4741 0.6355 -0.0204 0.2732  -0.0064 471 ILE A CD1 
3620  N N   . PHE A  472 ? 0.4041 0.3633 0.5197 -0.0114 0.2103  0.0010  472 PHE A N   
3621  C CA  . PHE A  472 ? 0.3952 0.3610 0.5223 -0.0130 0.1962  0.0025  472 PHE A CA  
3622  C C   . PHE A  472 ? 0.3779 0.3500 0.5050 -0.0056 0.1782  0.0014  472 PHE A C   
3623  O O   . PHE A  472 ? 0.3639 0.3539 0.5150 -0.0053 0.1684  -0.0012 472 PHE A O   
3624  C CB  . PHE A  472 ? 0.4505 0.3942 0.5528 -0.0162 0.1970  0.0093  472 PHE A CB  
3625  C CG  . PHE A  472 ? 0.4398 0.3867 0.5495 -0.0171 0.1830  0.0109  472 PHE A CG  
3626  C CD1 . PHE A  472 ? 0.4164 0.3820 0.5571 -0.0217 0.1805  0.0072  472 PHE A CD1 
3627  C CD2 . PHE A  472 ? 0.4578 0.3882 0.5426 -0.0131 0.1728  0.0160  472 PHE A CD2 
3628  C CE1 . PHE A  472 ? 0.4111 0.3778 0.5558 -0.0223 0.1686  0.0083  472 PHE A CE1 
3629  C CE2 . PHE A  472 ? 0.4391 0.3718 0.5303 -0.0133 0.1613  0.0172  472 PHE A CE2 
3630  C CZ  . PHE A  472 ? 0.4222 0.3723 0.5423 -0.0180 0.1596  0.0133  472 PHE A CZ  
3631  N N   . ALA A  473 ? 0.3265 0.2835 0.4260 0.0000  0.1743  0.0032  473 ALA A N   
3632  C CA  . ALA A  473 ? 0.2979 0.2575 0.3938 0.0064  0.1582  0.0025  473 ALA A CA  
3633  C C   . ALA A  473 ? 0.3166 0.2959 0.4379 0.0095  0.1555  -0.0030 473 ALA A C   
3634  O O   . ALA A  473 ? 0.2745 0.2651 0.4094 0.0117  0.1426  -0.0035 473 ALA A O   
3635  C CB  . ALA A  473 ? 0.3109 0.2510 0.3739 0.0109  0.1566  0.0042  473 ALA A CB  
3636  N N   . GLN A  474 ? 0.5712 0.5538 0.6985 0.0099  0.1681  -0.0068 474 GLN A N   
3637  C CA  . GLN A  474 ? 0.5566 0.5589 0.7116 0.0131  0.1673  -0.0121 474 GLN A CA  
3638  C C   . GLN A  474 ? 0.4925 0.5152 0.6781 0.0101  0.1612  -0.0128 474 GLN A C   
3639  O O   . GLN A  474 ? 0.4718 0.5071 0.6726 0.0140  0.1499  -0.0143 474 GLN A O   
3640  C CB  . GLN A  474 ? 0.4911 0.4959 0.6524 0.0128  0.1847  -0.0161 474 GLN A CB  
3641  C CG  . GLN A  474 ? 0.5620 0.5487 0.6950 0.0171  0.1907  -0.0171 474 GLN A CG  
3642  C CD  . GLN A  474 ? 0.6149 0.6051 0.7555 0.0174  0.2089  -0.0216 474 GLN A CD  
3643  O OE1 . GLN A  474 ? 0.6349 0.6262 0.7806 0.0115  0.2231  -0.0207 474 GLN A OE1 
3644  N NE2 . GLN A  474 ? 0.6268 0.6186 0.7691 0.0242  0.2093  -0.0265 474 GLN A NE2 
3645  N N   . ARG A  475 ? 0.2949 0.3196 0.4883 0.0029  0.1687  -0.0118 475 ARG A N   
3646  C CA  . ARG A  475 ? 0.2517 0.2948 0.4732 -0.0009 0.1634  -0.0134 475 ARG A CA  
3647  C C   . ARG A  475 ? 0.2423 0.2867 0.4614 0.0010  0.1462  -0.0111 475 ARG A C   
3648  O O   . ARG A  475 ? 0.2541 0.3156 0.4945 0.0025  0.1370  -0.0134 475 ARG A O   
3649  C CB  . ARG A  475 ? 0.3507 0.3918 0.5777 -0.0100 0.1748  -0.0127 475 ARG A CB  
3650  C CG  . ARG A  475 ? 0.3794 0.4385 0.6331 -0.0145 0.1672  -0.0158 475 ARG A CG  
3651  C CD  . ARG A  475 ? 0.4464 0.5024 0.7044 -0.0234 0.1775  -0.0164 475 ARG A CD  
3652  N NE  . ARG A  475 ? 0.4854 0.5389 0.7464 -0.0296 0.1734  -0.0152 475 ARG A NE  
3653  C CZ  . ARG A  475 ? 0.5007 0.5357 0.7455 -0.0351 0.1822  -0.0108 475 ARG A CZ  
3654  N NH1 . ARG A  475 ? 0.5046 0.5215 0.7267 -0.0349 0.1955  -0.0068 475 ARG A NH1 
3655  N NH2 . ARG A  475 ? 0.4804 0.5134 0.7297 -0.0404 0.1776  -0.0105 475 ARG A NH2 
3656  N N   . LEU A  476 ? 0.2685 0.2950 0.4616 0.0014  0.1418  -0.0065 476 LEU A N   
3657  C CA  . LEU A  476 ? 0.2180 0.2451 0.4076 0.0040  0.1265  -0.0043 476 LEU A CA  
3658  C C   . LEU A  476 ? 0.2122 0.2473 0.4069 0.0108  0.1171  -0.0058 476 LEU A C   
3659  O O   . LEU A  476 ? 0.2058 0.2539 0.4157 0.0122  0.1075  -0.0066 476 LEU A O   
3660  C CB  . LEU A  476 ? 0.2177 0.2245 0.3794 0.0041  0.1239  0.0007  476 LEU A CB  
3661  C CG  . LEU A  476 ? 0.2287 0.2264 0.3858 -0.0022 0.1305  0.0031  476 LEU A CG  
3662  C CD1 . LEU A  476 ? 0.2421 0.2195 0.3714 -0.0005 0.1269  0.0084  476 LEU A CD1 
3663  C CD2 . LEU A  476 ? 0.2131 0.2248 0.3922 -0.0058 0.1251  0.0009  476 LEU A CD2 
3664  N N   . MET A  477 ? 0.2036 0.2298 0.3847 0.0149  0.1203  -0.0063 477 MET A N   
3665  C CA  . MET A  477 ? 0.1951 0.2262 0.3801 0.0210  0.1123  -0.0078 477 MET A CA  
3666  C C   . MET A  477 ? 0.2787 0.3298 0.4922 0.0225  0.1103  -0.0109 477 MET A C   
3667  O O   . MET A  477 ? 0.1672 0.2257 0.3882 0.0257  0.0993  -0.0102 477 MET A O   
3668  C CB  . MET A  477 ? 0.2113 0.2305 0.3804 0.0245  0.1185  -0.0096 477 MET A CB  
3669  C CG  . MET A  477 ? 0.2248 0.2247 0.3644 0.0250  0.1150  -0.0066 477 MET A CG  
3670  S SD  . MET A  477 ? 0.4048 0.3881 0.5215 0.0275  0.1253  -0.0095 477 MET A SD  
3671  C CE  . MET A  477 ? 0.4211 0.4104 0.5480 0.0337  0.1185  -0.0136 477 MET A CE  
3672  N N   . LYS A  478 ? 0.3061 0.3663 0.5356 0.0203  0.1210  -0.0142 478 LYS A N   
3673  C CA  . LYS A  478 ? 0.3290 0.4102 0.5881 0.0217  0.1185  -0.0174 478 LYS A CA  
3674  C C   . LYS A  478 ? 0.3075 0.3984 0.5759 0.0189  0.1068  -0.0161 478 LYS A C   
3675  O O   . LYS A  478 ? 0.2887 0.3892 0.5653 0.0221  0.0957  -0.0165 478 LYS A O   
3676  C CB  . LYS A  478 ? 0.5419 0.6289 0.8108 0.0182  0.1285  -0.0208 478 LYS A CB  
3677  C CG  . LYS A  478 ? 0.6350 0.7217 0.9045 0.0238  0.1335  -0.0237 478 LYS A CG  
3678  C CD  . LYS A  478 ? 0.6911 0.7918 0.9792 0.0223  0.1360  -0.0272 478 LYS A CD  
3679  C CE  . LYS A  478 ? 0.7117 0.8222 1.0108 0.0296  0.1272  -0.0289 478 LYS A CE  
3680  N NZ  . LYS A  478 ? 0.7211 0.8208 1.0090 0.0363  0.1316  -0.0299 478 LYS A NZ  
3681  N N   . TYR A  479 ? 0.4007 0.4862 0.6632 0.0130  0.1086  -0.0144 479 TYR A N   
3682  C CA  . TYR A  479 ? 0.3580 0.4512 0.6280 0.0108  0.0983  -0.0139 479 TYR A CA  
3683  C C   . TYR A  479 ? 0.3234 0.4146 0.5844 0.0162  0.0856  -0.0110 479 TYR A C   
3684  O O   . TYR A  479 ? 0.3452 0.4478 0.6171 0.0183  0.0761  -0.0116 479 TYR A O   
3685  C CB  . TYR A  479 ? 0.2729 0.3553 0.5316 0.0042  0.1012  -0.0121 479 TYR A CB  
3686  C CG  . TYR A  479 ? 0.2670 0.3530 0.5381 -0.0031 0.1124  -0.0149 479 TYR A CG  
3687  C CD1 . TYR A  479 ? 0.2615 0.3629 0.5523 -0.0049 0.1103  -0.0193 479 TYR A CD1 
3688  C CD2 . TYR A  479 ? 0.2916 0.3610 0.5468 -0.0082 0.1218  -0.0124 479 TYR A CD2 
3689  C CE1 . TYR A  479 ? 0.2839 0.3867 0.5831 -0.0122 0.1189  -0.0219 479 TYR A CE1 
3690  C CE2 . TYR A  479 ? 0.3018 0.3732 0.5686 -0.0159 0.1333  -0.0146 479 TYR A CE2 
3691  C CZ  . TYR A  479 ? 0.2754 0.3635 0.5640 -0.0180 0.1312  -0.0196 479 TYR A CZ  
3692  O OH  . TYR A  479 ? 0.2350 0.3231 0.5312 -0.0256 0.1399  -0.0218 479 TYR A OH  
3693  N N   . TRP A  480 ? 0.1473 0.2226 0.3861 0.0181  0.0850  -0.0077 480 TRP A N   
3694  C CA  . TRP A  480 ? 0.1374 0.2093 0.3668 0.0219  0.0741  -0.0045 480 TRP A CA  
3695  C C   . TRP A  480 ? 0.1417 0.2209 0.3798 0.0276  0.0688  -0.0050 480 TRP A C   
3696  O O   . TRP A  480 ? 0.1222 0.2077 0.3650 0.0298  0.0597  -0.0034 480 TRP A O   
3697  C CB  . TRP A  480 ? 0.1469 0.2013 0.3526 0.0223  0.0745  -0.0015 480 TRP A CB  
3698  C CG  . TRP A  480 ? 0.1520 0.2002 0.3478 0.0199  0.0704  0.0013  480 TRP A CG  
3699  C CD1 . TRP A  480 ? 0.1429 0.1865 0.3289 0.0222  0.0621  0.0042  480 TRP A CD1 
3700  C CD2 . TRP A  480 ? 0.1866 0.2321 0.3821 0.0149  0.0747  0.0012  480 TRP A CD2 
3701  N NE1 . TRP A  480 ? 0.1752 0.2139 0.3551 0.0198  0.0609  0.0059  480 TRP A NE1 
3702  C CE2 . TRP A  480 ? 0.1875 0.2263 0.3722 0.0153  0.0685  0.0042  480 TRP A CE2 
3703  C CE3 . TRP A  480 ? 0.2282 0.2762 0.4326 0.0099  0.0838  -0.0012 480 TRP A CE3 
3704  C CZ2 . TRP A  480 ? 0.1899 0.2228 0.3711 0.0115  0.0707  0.0048  480 TRP A CZ2 
3705  C CZ3 . TRP A  480 ? 0.1618 0.2037 0.3627 0.0051  0.0861  -0.0005 480 TRP A CZ3 
3706  C CH2 . TRP A  480 ? 0.1710 0.2047 0.3598 0.0062  0.0794  0.0025  480 TRP A CH2 
3707  N N   . THR A  481 ? 0.3626 0.4396 0.6019 0.0304  0.0751  -0.0070 481 THR A N   
3708  C CA  . THR A  481 ? 0.3646 0.4468 0.6125 0.0364  0.0707  -0.0075 481 THR A CA  
3709  C C   . THR A  481 ? 0.3479 0.4454 0.6126 0.0368  0.0661  -0.0092 481 THR A C   
3710  O O   . THR A  481 ? 0.3699 0.4707 0.6364 0.0410  0.0578  -0.0079 481 THR A O   
3711  C CB  . THR A  481 ? 0.2231 0.2970 0.4654 0.0394  0.0784  -0.0099 481 THR A CB  
3712  O OG1 . THR A  481 ? 0.2041 0.2846 0.4582 0.0379  0.0894  -0.0137 481 THR A OG1 
3713  C CG2 . THR A  481 ? 0.1568 0.2125 0.3740 0.0378  0.0798  -0.0084 481 THR A CG2 
3714  N N   . ASN A  482 ? 0.1313 0.2360 0.4043 0.0321  0.0704  -0.0118 482 ASN A N   
3715  C CA  . ASN A  482 ? 0.1282 0.2465 0.4133 0.0315  0.0632  -0.0134 482 ASN A CA  
3716  C C   . ASN A  482 ? 0.1200 0.2409 0.4017 0.0315  0.0522  -0.0108 482 ASN A C   
3717  O O   . ASN A  482 ? 0.1181 0.2460 0.4033 0.0351  0.0435  -0.0101 482 ASN A O   
3718  C CB  . ASN A  482 ? 0.2085 0.3340 0.5044 0.0256  0.0697  -0.0170 482 ASN A CB  
3719  C CG  . ASN A  482 ? 0.2555 0.3839 0.5593 0.0267  0.0783  -0.0200 482 ASN A CG  
3720  O OD1 . ASN A  482 ? 0.2883 0.4168 0.5926 0.0327  0.0770  -0.0201 482 ASN A OD1 
3721  N ND2 . ASN A  482 ? 0.2731 0.4032 0.5829 0.0208  0.0879  -0.0226 482 ASN A ND2 
3722  N N   . PHE A  483 ? 0.1885 0.3035 0.4630 0.0279  0.0531  -0.0093 483 PHE A N   
3723  C CA  . PHE A  483 ? 0.2070 0.3241 0.4778 0.0281  0.0437  -0.0072 483 PHE A CA  
3724  C C   . PHE A  483 ? 0.2526 0.3658 0.5154 0.0337  0.0371  -0.0033 483 PHE A C   
3725  O O   . PHE A  483 ? 0.3029 0.4213 0.5658 0.0360  0.0287  -0.0019 483 PHE A O   
3726  C CB  . PHE A  483 ? 0.1500 0.2602 0.4144 0.0242  0.0466  -0.0060 483 PHE A CB  
3727  C CG  . PHE A  483 ? 0.1502 0.2617 0.4099 0.0250  0.0380  -0.0040 483 PHE A CG  
3728  C CD1 . PHE A  483 ? 0.1619 0.2832 0.4287 0.0235  0.0321  -0.0065 483 PHE A CD1 
3729  C CD2 . PHE A  483 ? 0.1703 0.2724 0.4162 0.0271  0.0355  0.0001  483 PHE A CD2 
3730  C CE1 . PHE A  483 ? 0.1979 0.3202 0.4599 0.0247  0.0252  -0.0049 483 PHE A CE1 
3731  C CE2 . PHE A  483 ? 0.2104 0.3133 0.4509 0.0278  0.0289  0.0020  483 PHE A CE2 
3732  C CZ  . PHE A  483 ? 0.2176 0.3304 0.4659 0.0268  0.0242  -0.0005 483 PHE A CZ  
3733  N N   . ALA A  484 ? 0.1552 0.2587 0.4115 0.0359  0.0414  -0.0017 484 ALA A N   
3734  C CA  . ALA A  484 ? 0.1425 0.2403 0.3920 0.0404  0.0365  0.0018  484 ALA A CA  
3735  C C   . ALA A  484 ? 0.1598 0.2636 0.4150 0.0447  0.0313  0.0019  484 ALA A C   
3736  O O   . ALA A  484 ? 0.1570 0.2610 0.4088 0.0473  0.0241  0.0052  484 ALA A O   
3737  C CB  . ALA A  484 ? 0.1143 0.2017 0.3590 0.0419  0.0429  0.0018  484 ALA A CB  
3738  N N   . ARG A  485 ? 0.2027 0.3109 0.4667 0.0457  0.0358  -0.0016 485 ARG A N   
3739  C CA  . ARG A  485 ? 0.2310 0.3449 0.5020 0.0509  0.0318  -0.0019 485 ARG A CA  
3740  C C   . ARG A  485 ? 0.1517 0.2781 0.4295 0.0513  0.0239  -0.0020 485 ARG A C   
3741  O O   . ARG A  485 ? 0.1246 0.2523 0.4008 0.0558  0.0165  0.0010  485 ARG A O   
3742  C CB  . ARG A  485 ? 0.5479 0.6633 0.8270 0.0519  0.0400  -0.0060 485 ARG A CB  
3743  C CG  . ARG A  485 ? 0.6683 0.7863 0.9538 0.0585  0.0377  -0.0063 485 ARG A CG  
3744  C CD  . ARG A  485 ? 0.7642 0.8838 1.0577 0.0594  0.0473  -0.0109 485 ARG A CD  
3745  N NE  . ARG A  485 ? 0.8339 0.9666 1.1395 0.0555  0.0498  -0.0143 485 ARG A NE  
3746  C CZ  . ARG A  485 ? 0.8540 0.9863 1.1608 0.0497  0.0591  -0.0170 485 ARG A CZ  
3747  N NH1 . ARG A  485 ? 0.8534 0.9731 1.1490 0.0478  0.0667  -0.0166 485 ARG A NH1 
3748  N NH2 . ARG A  485 ? 0.8450 0.9894 1.1644 0.0459  0.0608  -0.0199 485 ARG A NH2 
3749  N N   . THR A  486 ? 0.2091 0.3443 0.4949 0.0468  0.0258  -0.0056 486 THR A N   
3750  C CA  . THR A  486 ? 0.2178 0.3663 0.5125 0.0469  0.0185  -0.0071 486 THR A CA  
3751  C C   . THR A  486 ? 0.2005 0.3515 0.4915 0.0431  0.0134  -0.0068 486 THR A C   
3752  O O   . THR A  486 ? 0.1874 0.3494 0.4856 0.0435  0.0065  -0.0084 486 THR A O   
3753  C CB  . THR A  486 ? 0.2773 0.4366 0.5874 0.0446  0.0229  -0.0122 486 THR A CB  
3754  O OG1 . THR A  486 ? 0.2630 0.4229 0.5755 0.0369  0.0280  -0.0150 486 THR A OG1 
3755  C CG2 . THR A  486 ? 0.3367 0.4916 0.6494 0.0471  0.0313  -0.0132 486 THR A CG2 
3756  N N   . GLY A  487 ? 0.2251 0.3665 0.5059 0.0398  0.0166  -0.0051 487 GLY A N   
3757  C CA  . GLY A  487 ? 0.2427 0.3860 0.5214 0.0359  0.0136  -0.0058 487 GLY A CA  
3758  C C   . GLY A  487 ? 0.2926 0.4414 0.5813 0.0294  0.0179  -0.0110 487 GLY A C   
3759  O O   . GLY A  487 ? 0.3351 0.4859 0.6244 0.0259  0.0154  -0.0127 487 GLY A O   
3760  N N   . ASP A  488 ? 0.2552 0.4060 0.5524 0.0275  0.0248  -0.0137 488 ASP A N   
3761  C CA  . ASP A  488 ? 0.3105 0.4657 0.6182 0.0206  0.0304  -0.0184 488 ASP A CA  
3762  C C   . ASP A  488 ? 0.3669 0.5131 0.6724 0.0183  0.0426  -0.0183 488 ASP A C   
3763  O O   . ASP A  488 ? 0.4456 0.5898 0.7502 0.0223  0.0459  -0.0173 488 ASP A O   
3764  C CB  . ASP A  488 ? 0.4204 0.5906 0.7440 0.0211  0.0262  -0.0222 488 ASP A CB  
3765  C CG  . ASP A  488 ? 0.4862 0.6625 0.8233 0.0134  0.0315  -0.0275 488 ASP A CG  
3766  O OD1 . ASP A  488 ? 0.5315 0.6991 0.8661 0.0082  0.0417  -0.0279 488 ASP A OD1 
3767  O OD2 . ASP A  488 ? 0.4776 0.6674 0.8283 0.0124  0.0255  -0.0313 488 ASP A OD2 
3768  N N   . PRO A  489 ? 0.3795 0.5197 0.6841 0.0119  0.0500  -0.0195 489 PRO A N   
3769  C CA  . PRO A  489 ? 0.3632 0.4937 0.6636 0.0100  0.0624  -0.0188 489 PRO A CA  
3770  C C   . PRO A  489 ? 0.3870 0.5244 0.6996 0.0083  0.0691  -0.0222 489 PRO A C   
3771  O O   . PRO A  489 ? 0.4272 0.5575 0.7359 0.0083  0.0795  -0.0217 489 PRO A O   
3772  C CB  . PRO A  489 ? 0.3411 0.4638 0.6382 0.0035  0.0682  -0.0188 489 PRO A CB  
3773  C CG  . PRO A  489 ? 0.3496 0.4757 0.6460 0.0035  0.0580  -0.0189 489 PRO A CG  
3774  C CD  . PRO A  489 ? 0.3517 0.4916 0.6570 0.0067  0.0480  -0.0211 489 PRO A CD  
3775  N N   . ASN A  490 ? 0.2639 0.4151 0.5910 0.0069  0.0636  -0.0258 490 ASN A N   
3776  C CA  . ASN A  490 ? 0.3022 0.4617 0.6440 0.0040  0.0701  -0.0295 490 ASN A CA  
3777  C C   . ASN A  490 ? 0.3669 0.5293 0.7115 0.0102  0.0728  -0.0293 490 ASN A C   
3778  O O   . ASN A  490 ? 0.3778 0.5410 0.7179 0.0174  0.0652  -0.0271 490 ASN A O   
3779  C CB  . ASN A  490 ? 0.3605 0.5353 0.7187 0.0012  0.0622  -0.0337 490 ASN A CB  
3780  C CG  . ASN A  490 ? 0.3499 0.5224 0.7114 -0.0079 0.0653  -0.0364 490 ASN A CG  
3781  O OD1 . ASN A  490 ? 0.3593 0.5235 0.7195 -0.0134 0.0773  -0.0365 490 ASN A OD1 
3782  N ND2 . ASN A  490 ? 0.3323 0.5108 0.6972 -0.0094 0.0550  -0.0384 490 ASN A ND2 
3783  N N   . ASP A  491 ? 0.2770 0.4401 0.6287 0.0074  0.0843  -0.0315 491 ASP A N   
3784  C CA  . ASP A  491 ? 0.3486 0.5165 0.7067 0.0128  0.0880  -0.0326 491 ASP A CA  
3785  C C   . ASP A  491 ? 0.3336 0.5194 0.7091 0.0158  0.0778  -0.0350 491 ASP A C   
3786  O O   . ASP A  491 ? 0.2787 0.4751 0.6683 0.0105  0.0766  -0.0382 491 ASP A O   
3787  C CB  . ASP A  491 ? 0.8355 0.9998 1.1966 0.0085  0.1038  -0.0345 491 ASP A CB  
3788  C CG  . ASP A  491 ? 0.9453 1.0911 1.2864 0.0089  0.1139  -0.0317 491 ASP A CG  
3789  O OD1 . ASP A  491 ? 0.9829 1.1239 1.3171 0.0156  0.1151  -0.0309 491 ASP A OD1 
3790  O OD2 . ASP A  491 ? 0.9720 1.1074 1.3040 0.0027  0.1207  -0.0303 491 ASP A OD2 
3791  N N   . PRO A  492 ? 0.5562 0.7447 0.9301 0.0244  0.0699  -0.0332 492 PRO A N   
3792  C CA  . PRO A  492 ? 0.6374 0.8411 1.0238 0.0288  0.0578  -0.0341 492 PRO A CA  
3793  C C   . PRO A  492 ? 0.7415 0.9614 1.1501 0.0290  0.0604  -0.0382 492 PRO A C   
3794  O O   . PRO A  492 ? 0.6963 0.9304 1.1193 0.0268  0.0534  -0.0408 492 PRO A O   
3795  C CB  . PRO A  492 ? 0.6919 0.8896 1.0678 0.0380  0.0518  -0.0302 492 PRO A CB  
3796  C CG  . PRO A  492 ? 0.6756 0.8601 1.0420 0.0391  0.0633  -0.0296 492 PRO A CG  
3797  C CD  . PRO A  492 ? 0.6567 0.8332 1.0174 0.0306  0.0732  -0.0305 492 PRO A CD  
3798  N N   . ARG A  493 ? 1.1950 1.4129 1.6067 0.0316  0.0707  -0.0392 493 ARG A N   
3799  C CA  . ARG A  493 ? 1.3222 1.5554 1.7556 0.0324  0.0747  -0.0430 493 ARG A CA  
3800  C C   . ARG A  493 ? 1.3919 1.6306 1.8364 0.0220  0.0815  -0.0465 493 ARG A C   
3801  O O   . ARG A  493 ? 1.4199 1.6747 1.8831 0.0195  0.0761  -0.0496 493 ARG A O   
3802  C CB  . ARG A  493 ? 1.2164 1.4442 1.6485 0.0374  0.0858  -0.0435 493 ARG A CB  
3803  C CG  . ARG A  493 ? 1.2191 1.4410 1.6421 0.0478  0.0798  -0.0407 493 ARG A CG  
3804  C CD  . ARG A  493 ? 1.2508 1.4627 1.6680 0.0515  0.0922  -0.0416 493 ARG A CD  
3805  N NE  . ARG A  493 ? 1.2926 1.4871 1.6912 0.0461  0.1017  -0.0406 493 ARG A NE  
3806  C CZ  . ARG A  493 ? 1.3279 1.5095 1.7152 0.0486  0.1122  -0.0410 493 ARG A CZ  
3807  N NH1 . ARG A  493 ? 1.3432 1.5270 1.7363 0.0563  0.1148  -0.0429 493 ARG A NH1 
3808  N NH2 . ARG A  493 ? 1.3282 1.4943 1.6979 0.0437  0.1200  -0.0398 493 ARG A NH2 
3809  N N   . ASP A  494 ? 1.1908 1.4151 1.6229 0.0160  0.0930  -0.0457 494 ASP A N   
3810  C CA  . ASP A  494 ? 1.2163 1.4413 1.6560 0.0060  0.1024  -0.0483 494 ASP A CA  
3811  C C   . ASP A  494 ? 1.1790 1.4107 1.6254 -0.0003 0.0931  -0.0499 494 ASP A C   
3812  O O   . ASP A  494 ? 1.1481 1.3767 1.5846 0.0017  0.0818  -0.0479 494 ASP A O   
3813  C CB  . ASP A  494 ? 1.3991 1.6038 1.8187 0.0018  0.1150  -0.0458 494 ASP A CB  
3814  C CG  . ASP A  494 ? 1.4552 1.6587 1.8818 -0.0062 0.1302  -0.0480 494 ASP A CG  
3815  O OD1 . ASP A  494 ? 1.4651 1.6834 1.9128 -0.0106 0.1300  -0.0517 494 ASP A OD1 
3816  O OD2 . ASP A  494 ? 1.4846 1.6719 1.8949 -0.0081 0.1425  -0.0459 494 ASP A OD2 
3817  N N   . SER A  495 ? 1.2421 1.4835 1.7063 -0.0078 0.0979  -0.0540 495 SER A N   
3818  C CA  . SER A  495 ? 1.2198 1.4622 1.6878 -0.0164 0.0936  -0.0561 495 SER A CA  
3819  C C   . SER A  495 ? 1.2108 1.4438 1.6786 -0.0262 0.1093  -0.0570 495 SER A C   
3820  O O   . SER A  495 ? 1.1971 1.4394 1.6822 -0.0298 0.1176  -0.0600 495 SER A O   
3821  C CB  . SER A  495 ? 1.1287 1.3928 1.6203 -0.0168 0.0825  -0.0606 495 SER A CB  
3822  O OG  . SER A  495 ? 1.1096 1.3815 1.6002 -0.0071 0.0688  -0.0591 495 SER A OG  
3823  N N   . LYS A  496 ? 1.2282 1.4428 1.6765 -0.0302 0.1133  -0.0541 496 LYS A N   
3824  C CA  . LYS A  496 ? 1.2200 1.4212 1.6626 -0.0387 0.1289  -0.0535 496 LYS A CA  
3825  C C   . LYS A  496 ? 1.2752 1.4552 1.6943 -0.0416 0.1317  -0.0494 496 LYS A C   
3826  O O   . LYS A  496 ? 1.2727 1.4478 1.6793 -0.0370 0.1221  -0.0470 496 LYS A O   
3827  C CB  . LYS A  496 ? 0.9402 1.1382 1.3818 -0.0368 0.1437  -0.0524 496 LYS A CB  
3828  C CG  . LYS A  496 ? 0.8714 1.0548 1.2900 -0.0295 0.1471  -0.0478 496 LYS A CG  
3829  C CD  . LYS A  496 ? 0.8148 0.9772 1.2140 -0.0341 0.1629  -0.0445 496 LYS A CD  
3830  C CE  . LYS A  496 ? 0.7513 0.8989 1.1267 -0.0269 0.1647  -0.0402 496 LYS A CE  
3831  N NZ  . LYS A  496 ? 0.6872 0.8332 1.0539 -0.0220 0.1503  -0.0382 496 LYS A NZ  
3832  N N   . SER A  497 ? 1.4437 1.6112 1.8576 -0.0492 0.1458  -0.0484 497 SER A N   
3833  C CA  . SER A  497 ? 1.4581 1.6030 1.8500 -0.0533 0.1535  -0.0441 497 SER A CA  
3834  C C   . SER A  497 ? 1.4711 1.6067 1.8547 -0.0572 0.1466  -0.0433 497 SER A C   
3835  O O   . SER A  497 ? 1.4883 1.6069 1.8509 -0.0556 0.1494  -0.0385 497 SER A O   
3836  C CB  . SER A  497 ? 1.2308 1.3632 1.6009 -0.0456 0.1570  -0.0390 497 SER A CB  
3837  O OG  . SER A  497 ? 1.1893 1.3243 1.5536 -0.0389 0.1429  -0.0379 497 SER A OG  
3838  N N   . PRO A  498 ? 1.5710 1.7174 1.9706 -0.0621 0.1378  -0.0482 498 PRO A N   
3839  C CA  . PRO A  498 ? 1.5177 1.6852 1.9340 -0.0577 0.1229  -0.0524 498 PRO A CA  
3840  C C   . PRO A  498 ? 1.4222 1.5862 1.8235 -0.0494 0.1120  -0.0492 498 PRO A C   
3841  O O   . PRO A  498 ? 1.4337 1.5806 1.8157 -0.0488 0.1161  -0.0447 498 PRO A O   
3842  C CB  . PRO A  498 ? 1.1607 1.3344 1.5914 -0.0662 0.1176  -0.0579 498 PRO A CB  
3843  C CG  . PRO A  498 ? 1.1858 1.3471 1.6159 -0.0756 0.1331  -0.0574 498 PRO A CG  
3844  C CD  . PRO A  498 ? 1.2087 1.3485 1.6134 -0.0728 0.1435  -0.0504 498 PRO A CD  
3845  N N   . GLN A  499 ? 0.8322 1.0112 1.2412 -0.0428 0.0987  -0.0509 499 GLN A N   
3846  C CA  . GLN A  499 ? 0.6753 0.8506 1.0697 -0.0347 0.0895  -0.0472 499 GLN A CA  
3847  C C   . GLN A  499 ? 0.4839 0.6489 0.8670 -0.0375 0.0847  -0.0465 499 GLN A C   
3848  O O   . GLN A  499 ? 0.4261 0.5895 0.8151 -0.0454 0.0852  -0.0500 499 GLN A O   
3849  C CB  . GLN A  499 ? 0.9403 1.1328 1.3445 -0.0273 0.0763  -0.0487 499 GLN A CB  
3850  C CG  . GLN A  499 ? 0.9877 1.1942 1.4071 -0.0307 0.0652  -0.0541 499 GLN A CG  
3851  C CD  . GLN A  499 ? 1.0257 1.2418 1.4437 -0.0224 0.0500  -0.0534 499 GLN A CD  
3852  O OE1 . GLN A  499 ? 1.0564 1.2786 1.4756 -0.0147 0.0475  -0.0512 499 GLN A OE1 
3853  N NE2 . GLN A  499 ? 1.0097 1.2261 1.4241 -0.0239 0.0400  -0.0552 499 GLN A NE2 
3854  N N   . TRP A  500 ? 0.5913 0.7486 0.9584 -0.0309 0.0807  -0.0420 500 TRP A N   
3855  C CA  . TRP A  500 ? 0.4646 0.6110 0.8191 -0.0316 0.0777  -0.0401 500 TRP A CA  
3856  C C   . TRP A  500 ? 0.4037 0.5609 0.7622 -0.0286 0.0624  -0.0427 500 TRP A C   
3857  O O   . TRP A  500 ? 0.3977 0.5616 0.7534 -0.0207 0.0541  -0.0408 500 TRP A O   
3858  C CB  . TRP A  500 ? 0.2923 0.4269 0.6292 -0.0253 0.0816  -0.0337 500 TRP A CB  
3859  C CG  . TRP A  500 ? 0.2337 0.3574 0.5566 -0.0235 0.0791  -0.0302 500 TRP A CG  
3860  C CD1 . TRP A  500 ? 0.2334 0.3575 0.5568 -0.0253 0.0718  -0.0321 500 TRP A CD1 
3861  C CD2 . TRP A  500 ? 0.2091 0.3202 0.5158 -0.0190 0.0840  -0.0244 500 TRP A CD2 
3862  N NE1 . TRP A  500 ? 0.2242 0.3326 0.5244 -0.0211 0.0701  -0.0268 500 TRP A NE1 
3863  C CE2 . TRP A  500 ? 0.2213 0.3215 0.5107 -0.0174 0.0766  -0.0220 500 TRP A CE2 
3864  C CE3 . TRP A  500 ? 0.1841 0.2885 0.4823 -0.0156 0.0919  -0.0211 500 TRP A CE3 
3865  C CZ2 . TRP A  500 ? 0.2045 0.2892 0.4709 -0.0126 0.0766  -0.0163 500 TRP A CZ2 
3866  C CZ3 . TRP A  500 ? 0.1484 0.2362 0.4219 -0.0112 0.0911  -0.0157 500 TRP A CZ3 
3867  C CH2 . TRP A  500 ? 0.1826 0.2616 0.4416 -0.0098 0.0832  -0.0132 500 TRP A CH2 
3868  N N   . PRO A  501 ? 0.2157 0.3735 0.5801 -0.0352 0.0591  -0.0474 501 PRO A N   
3869  C CA  . PRO A  501 ? 0.1812 0.3489 0.5502 -0.0343 0.0453  -0.0516 501 PRO A CA  
3870  C C   . PRO A  501 ? 0.1803 0.3409 0.5352 -0.0299 0.0399  -0.0488 501 PRO A C   
3871  O O   . PRO A  501 ? 0.2116 0.3579 0.5559 -0.0309 0.0476  -0.0452 501 PRO A O   
3872  C CB  . PRO A  501 ? 0.2165 0.3832 0.5960 -0.0449 0.0475  -0.0581 501 PRO A CB  
3873  C CG  . PRO A  501 ? 0.2328 0.3813 0.6038 -0.0501 0.0621  -0.0547 501 PRO A CG  
3874  C CD  . PRO A  501 ? 0.2277 0.3735 0.5925 -0.0447 0.0701  -0.0487 501 PRO A CD  
3875  N N   . PRO A  502 ? 0.3105 0.4810 0.6655 -0.0249 0.0270  -0.0504 502 PRO A N   
3876  C CA  . PRO A  502 ? 0.3521 0.5140 0.6894 -0.0199 0.0219  -0.0472 502 PRO A CA  
3877  C C   . PRO A  502 ? 0.4002 0.5483 0.7258 -0.0255 0.0226  -0.0501 502 PRO A C   
3878  O O   . PRO A  502 ? 0.4619 0.6150 0.7994 -0.0326 0.0203  -0.0574 502 PRO A O   
3879  C CB  . PRO A  502 ? 0.3923 0.5687 0.7330 -0.0139 0.0082  -0.0487 502 PRO A CB  
3880  C CG  . PRO A  502 ? 0.4117 0.5995 0.7644 -0.0122 0.0077  -0.0487 502 PRO A CG  
3881  C CD  . PRO A  502 ? 0.4019 0.5888 0.7666 -0.0213 0.0167  -0.0529 502 PRO A CD  
3882  N N   . TYR A  503 ? 0.2482 0.3793 0.5518 -0.0222 0.0256  -0.0448 503 TYR A N   
3883  C CA  . TYR A  503 ? 0.2132 0.3307 0.5035 -0.0249 0.0249  -0.0472 503 TYR A CA  
3884  C C   . TYR A  503 ? 0.2089 0.3345 0.4959 -0.0220 0.0127  -0.0513 503 TYR A C   
3885  O O   . TYR A  503 ? 0.2230 0.3543 0.5031 -0.0144 0.0066  -0.0476 503 TYR A O   
3886  C CB  . TYR A  503 ? 0.2628 0.3628 0.5320 -0.0203 0.0299  -0.0401 503 TYR A CB  
3887  C CG  . TYR A  503 ? 0.2789 0.3638 0.5348 -0.0220 0.0302  -0.0422 503 TYR A CG  
3888  C CD1 . TYR A  503 ? 0.2759 0.3603 0.5201 -0.0172 0.0228  -0.0432 503 TYR A CD1 
3889  C CD2 . TYR A  503 ? 0.3281 0.3982 0.5824 -0.0281 0.0386  -0.0429 503 TYR A CD2 
3890  C CE1 . TYR A  503 ? 0.3266 0.3972 0.5592 -0.0180 0.0237  -0.0457 503 TYR A CE1 
3891  C CE2 . TYR A  503 ? 0.3766 0.4317 0.6191 -0.0289 0.0390  -0.0449 503 TYR A CE2 
3892  C CZ  . TYR A  503 ? 0.4012 0.4570 0.6334 -0.0237 0.0315  -0.0466 503 TYR A CZ  
3893  O OH  . TYR A  503 ? 0.4732 0.5136 0.6939 -0.0239 0.0326  -0.0492 503 TYR A OH  
3894  N N   . THR A  504 ? 0.1872 0.3124 0.4783 -0.0283 0.0095  -0.0592 504 THR A N   
3895  C CA  . THR A  504 ? 0.2249 0.3563 0.5110 -0.0262 -0.0022 -0.0645 504 THR A CA  
3896  C C   . THR A  504 ? 0.2644 0.3791 0.5360 -0.0292 -0.0006 -0.0684 504 THR A C   
3897  O O   . THR A  504 ? 0.2337 0.3343 0.5042 -0.0341 0.0086  -0.0680 504 THR A O   
3898  C CB  . THR A  504 ? 0.4113 0.5613 0.7193 -0.0312 -0.0102 -0.0727 504 THR A CB  
3899  O OG1 . THR A  504 ? 0.4392 0.5846 0.7577 -0.0417 -0.0065 -0.0803 504 THR A OG1 
3900  C CG2 . THR A  504 ? 0.4405 0.6059 0.7678 -0.0296 -0.0084 -0.0694 504 THR A CG2 
3901  N N   . THR A  505 ? 0.4462 0.5609 0.7051 -0.0258 -0.0091 -0.0720 505 THR A N   
3902  C CA  . THR A  505 ? 0.4959 0.5939 0.7399 -0.0275 -0.0074 -0.0763 505 THR A CA  
3903  C C   . THR A  505 ? 0.4505 0.5462 0.7070 -0.0381 -0.0074 -0.0861 505 THR A C   
3904  O O   . THR A  505 ? 0.4117 0.4904 0.6639 -0.0425 0.0000  -0.0877 505 THR A O   
3905  C CB  . THR A  505 ? 0.6334 0.7314 0.8589 -0.0209 -0.0153 -0.0779 505 THR A CB  
3906  O OG1 . THR A  505 ? 0.6861 0.8003 0.9137 -0.0155 -0.0234 -0.0748 505 THR A OG1 
3907  C CG2 . THR A  505 ? 0.6003 0.6834 0.8068 -0.0145 -0.0086 -0.0716 505 THR A CG2 
3908  N N   . ALA A  506 ? 0.5477 0.6605 0.8205 -0.0420 -0.0160 -0.0926 506 ALA A N   
3909  C CA  . ALA A  506 ? 0.5830 0.6977 0.8730 -0.0532 -0.0169 -0.1025 506 ALA A CA  
3910  C C   . ALA A  506 ? 0.5445 0.6514 0.8484 -0.0612 -0.0038 -0.1004 506 ALA A C   
3911  O O   . ALA A  506 ? 0.5600 0.6485 0.8586 -0.0669 0.0031  -0.1029 506 ALA A O   
3912  C CB  . ALA A  506 ? 0.5783 0.7170 0.8870 -0.0547 -0.0288 -0.1083 506 ALA A CB  
3913  N N   . ALA A  507 ? 0.3034 0.4233 0.6238 -0.0611 0.0000  -0.0955 507 ALA A N   
3914  C CA  . ALA A  507 ? 0.2808 0.3966 0.6162 -0.0691 0.0124  -0.0939 507 ALA A CA  
3915  C C   . ALA A  507 ? 0.2456 0.3414 0.5646 -0.0659 0.0249  -0.0842 507 ALA A C   
3916  O O   . ALA A  507 ? 0.2215 0.3039 0.5436 -0.0731 0.0357  -0.0836 507 ALA A O   
3917  C CB  . ALA A  507 ? 0.5290 0.6675 0.8890 -0.0698 0.0120  -0.0933 507 ALA A CB  
3918  N N   . GLN A  508 ? 0.2689 0.3627 0.5708 -0.0552 0.0232  -0.0765 508 GLN A N   
3919  C CA  . GLN A  508 ? 0.2676 0.3460 0.5542 -0.0503 0.0326  -0.0668 508 GLN A CA  
3920  C C   . GLN A  508 ? 0.2517 0.3282 0.5485 -0.0548 0.0443  -0.0625 508 GLN A C   
3921  O O   . GLN A  508 ? 0.2025 0.2609 0.4930 -0.0590 0.0539  -0.0602 508 GLN A O   
3922  C CB  . GLN A  508 ? 0.3772 0.4329 0.6449 -0.0497 0.0358  -0.0664 508 GLN A CB  
3923  C CG  . GLN A  508 ? 0.3957 0.4497 0.6564 -0.0495 0.0272  -0.0740 508 GLN A CG  
3924  C CD  . GLN A  508 ? 0.4454 0.4755 0.6928 -0.0512 0.0329  -0.0750 508 GLN A CD  
3925  O OE1 . GLN A  508 ? 0.4657 0.4818 0.7000 -0.0461 0.0392  -0.0674 508 GLN A OE1 
3926  N NE2 . GLN A  508 ? 0.4645 0.4892 0.7159 -0.0586 0.0306  -0.0847 508 GLN A NE2 
3927  N N   . GLN A  509 ? 0.2486 0.3426 0.5598 -0.0533 0.0438  -0.0611 509 GLN A N   
3928  C CA  . GLN A  509 ? 0.2936 0.3861 0.6134 -0.0571 0.0557  -0.0573 509 GLN A CA  
3929  C C   . GLN A  509 ? 0.3139 0.4005 0.6184 -0.0485 0.0594  -0.0481 509 GLN A C   
3930  O O   . GLN A  509 ? 0.3194 0.4155 0.6203 -0.0404 0.0520  -0.0457 509 GLN A O   
3931  C CB  . GLN A  509 ? 0.3516 0.4671 0.6995 -0.0615 0.0547  -0.0624 509 GLN A CB  
3932  C CG  . GLN A  509 ? 0.3850 0.5079 0.7511 -0.0711 0.0508  -0.0723 509 GLN A CG  
3933  C CD  . GLN A  509 ? 0.4527 0.5987 0.8408 -0.0718 0.0459  -0.0764 509 GLN A CD  
3934  O OE1 . GLN A  509 ? 0.4736 0.6316 0.8617 -0.0632 0.0408  -0.0730 509 GLN A OE1 
3935  N NE2 . GLN A  509 ? 0.5001 0.6492 0.9013 -0.0805 0.0469  -0.0826 509 GLN A NE2 
3936  N N   . TYR A  510 ? 0.1820 0.2519 0.4768 -0.0504 0.0708  -0.0429 510 TYR A N   
3937  C CA  . TYR A  510 ? 0.1902 0.2546 0.4719 -0.0435 0.0751  -0.0349 510 TYR A CA  
3938  C C   . TYR A  510 ? 0.1883 0.2490 0.4768 -0.0494 0.0885  -0.0332 510 TYR A C   
3939  O O   . TYR A  510 ? 0.2007 0.2611 0.5022 -0.0586 0.0943  -0.0375 510 TYR A O   
3940  C CB  . TYR A  510 ? 0.2604 0.3046 0.5171 -0.0383 0.0748  -0.0292 510 TYR A CB  
3941  C CG  . TYR A  510 ? 0.2502 0.2740 0.4991 -0.0443 0.0827  -0.0288 510 TYR A CG  
3942  C CD1 . TYR A  510 ? 0.2883 0.3072 0.5392 -0.0486 0.0793  -0.0344 510 TYR A CD1 
3943  C CD2 . TYR A  510 ? 0.2255 0.2335 0.4636 -0.0455 0.0935  -0.0228 510 TYR A CD2 
3944  C CE1 . TYR A  510 ? 0.3145 0.3130 0.5585 -0.0541 0.0867  -0.0339 510 TYR A CE1 
3945  C CE2 . TYR A  510 ? 0.2602 0.2476 0.4901 -0.0508 0.1009  -0.0216 510 TYR A CE2 
3946  C CZ  . TYR A  510 ? 0.3080 0.2905 0.5413 -0.0551 0.0975  -0.0271 510 TYR A CZ  
3947  O OH  . TYR A  510 ? 0.3607 0.3209 0.5859 -0.0603 0.1049  -0.0259 510 TYR A OH  
3948  N N   . VAL A  511 ? 0.3038 0.3612 0.5834 -0.0445 0.0939  -0.0274 511 VAL A N   
3949  C CA  . VAL A  511 ? 0.3357 0.3886 0.6193 -0.0497 0.1078  -0.0257 511 VAL A CA  
3950  C C   . VAL A  511 ? 0.3867 0.4160 0.6436 -0.0468 0.1150  -0.0179 511 VAL A C   
3951  O O   . VAL A  511 ? 0.3702 0.3904 0.6083 -0.0395 0.1082  -0.0138 511 VAL A O   
3952  C CB  . VAL A  511 ? 0.3261 0.3977 0.6255 -0.0471 0.1098  -0.0269 511 VAL A CB  
3953  C CG1 . VAL A  511 ? 0.3230 0.4185 0.6487 -0.0488 0.1014  -0.0343 511 VAL A CG1 
3954  C CG2 . VAL A  511 ? 0.3037 0.3738 0.5874 -0.0367 0.1047  -0.0220 511 VAL A CG2 
3955  N N   . SER A  512 ? 0.5859 0.6057 0.8418 -0.0527 0.1289  -0.0160 512 SER A N   
3956  C CA  . SER A  512 ? 0.6609 0.6577 0.8906 -0.0504 0.1369  -0.0084 512 SER A CA  
3957  C C   . SER A  512 ? 0.6949 0.6960 0.9199 -0.0455 0.1416  -0.0059 512 SER A C   
3958  O O   . SER A  512 ? 0.7462 0.7608 0.9892 -0.0489 0.1490  -0.0092 512 SER A O   
3959  C CB  . SER A  512 ? 0.6265 0.6080 0.8554 -0.0600 0.1507  -0.0073 512 SER A CB  
3960  O OG  . SER A  512 ? 0.6383 0.6324 0.8866 -0.0662 0.1617  -0.0103 512 SER A OG  
3961  N N   . LEU A  513 ? 0.4445 0.4342 0.6460 -0.0374 0.1373  -0.0006 513 LEU A N   
3962  C CA  . LEU A  513 ? 0.3902 0.3799 0.5828 -0.0327 0.1419  0.0017  513 LEU A CA  
3963  C C   . LEU A  513 ? 0.3724 0.3378 0.5397 -0.0339 0.1530  0.0077  513 LEU A C   
3964  O O   . LEU A  513 ? 0.3400 0.2877 0.4845 -0.0300 0.1486  0.0129  513 LEU A O   
3965  C CB  . LEU A  513 ? 0.4108 0.4049 0.5949 -0.0232 0.1291  0.0028  513 LEU A CB  
3966  C CG  . LEU A  513 ? 0.3683 0.3846 0.5740 -0.0211 0.1181  -0.0021 513 LEU A CG  
3967  C CD1 . LEU A  513 ? 0.3451 0.3643 0.5420 -0.0124 0.1079  -0.0003 513 LEU A CD1 
3968  C CD2 . LEU A  513 ? 0.3399 0.3746 0.5710 -0.0249 0.1240  -0.0073 513 LEU A CD2 
3969  N N   . ASN A  514 ? 0.4717 0.4365 0.6435 -0.0391 0.1677  0.0073  514 ASN A N   
3970  C CA  . ASN A  514 ? 0.5252 0.4663 0.6719 -0.0409 0.1804  0.0133  514 ASN A CA  
3971  C C   . ASN A  514 ? 0.5010 0.4468 0.6531 -0.0436 0.1954  0.0118  514 ASN A C   
3972  O O   . ASN A  514 ? 0.4763 0.4438 0.6507 -0.0425 0.1946  0.0062  514 ASN A O   
3973  C CB  . ASN A  514 ? 0.5469 0.4723 0.6908 -0.0485 0.1865  0.0158  514 ASN A CB  
3974  C CG  . ASN A  514 ? 0.5817 0.5225 0.7573 -0.0587 0.1934  0.0098  514 ASN A CG  
3975  O OD1 . ASN A  514 ? 0.5937 0.5462 0.7849 -0.0627 0.2043  0.0068  514 ASN A OD1 
3976  N ND2 . ASN A  514 ? 0.5975 0.5391 0.7839 -0.0628 0.1868  0.0073  514 ASN A ND2 
3977  N N   . LEU A  515 ? 0.5091 0.4343 0.6407 -0.0469 0.2096  0.0168  515 LEU A N   
3978  C CA  . LEU A  515 ? 0.5135 0.4405 0.6465 -0.0493 0.2261  0.0158  515 LEU A CA  
3979  C C   . LEU A  515 ? 0.5945 0.5419 0.7605 -0.0562 0.2304  0.0087  515 LEU A C   
3980  O O   . LEU A  515 ? 0.6168 0.5784 0.7948 -0.0542 0.2336  0.0041  515 LEU A O   
3981  C CB  . LEU A  515 ? 0.3945 0.2921 0.4933 -0.0507 0.2393  0.0235  515 LEU A CB  
3982  C CG  . LEU A  515 ? 0.4067 0.2928 0.4751 -0.0418 0.2384  0.0262  515 LEU A CG  
3983  C CD1 . LEU A  515 ? 0.3977 0.3029 0.4835 -0.0404 0.2452  0.0198  515 LEU A CD1 
3984  C CD2 . LEU A  515 ? 0.3928 0.2772 0.4487 -0.0328 0.2181  0.0273  515 LEU A CD2 
3985  N N   . LYS A  516 ? 0.6576 0.6058 0.8367 -0.0631 0.2279  0.0073  516 LYS A N   
3986  C CA  . LYS A  516 ? 0.6618 0.6305 0.8721 -0.0688 0.2271  -0.0003 516 LYS A CA  
3987  C C   . LYS A  516 ? 0.6378 0.6330 0.8721 -0.0638 0.2133  -0.0064 516 LYS A C   
3988  O O   . LYS A  516 ? 0.6334 0.6295 0.8609 -0.0575 0.2046  -0.0047 516 LYS A O   
3989  C CB  . LYS A  516 ? 0.6804 0.6434 0.8980 -0.0768 0.2252  -0.0010 516 LYS A CB  
3990  C CG  . LYS A  516 ? 0.7382 0.6748 0.9348 -0.0824 0.2377  0.0048  516 LYS A CG  
3991  C CD  . LYS A  516 ? 0.7871 0.7187 0.9922 -0.0892 0.2331  0.0033  516 LYS A CD  
3992  C CE  . LYS A  516 ? 0.8682 0.7727 1.0532 -0.0948 0.2448  0.0091  516 LYS A CE  
3993  N NZ  . LYS A  516 ? 0.9026 0.8133 1.1059 -0.1039 0.2540  0.0048  516 LYS A NZ  
3994  N N   . PRO A  517 ? 0.6165 0.6333 0.8784 -0.0664 0.2108  -0.0133 517 PRO A N   
3995  C CA  . PRO A  517 ? 0.5999 0.6404 0.8831 -0.0616 0.1958  -0.0187 517 PRO A CA  
3996  C C   . PRO A  517 ? 0.6106 0.6536 0.8998 -0.0635 0.1833  -0.0199 517 PRO A C   
3997  O O   . PRO A  517 ? 0.6530 0.6797 0.9321 -0.0689 0.1868  -0.0172 517 PRO A O   
3998  C CB  . PRO A  517 ? 0.4122 0.4715 0.7212 -0.0652 0.1975  -0.0248 517 PRO A CB  
3999  C CG  . PRO A  517 ? 0.4163 0.4628 0.7225 -0.0747 0.2101  -0.0237 517 PRO A CG  
4000  C CD  . PRO A  517 ? 0.4326 0.4530 0.7069 -0.0732 0.2213  -0.0161 517 PRO A CD  
4001  N N   . LEU A  518 ? 0.4342 0.4961 0.7387 -0.0589 0.1690  -0.0240 518 LEU A N   
4002  C CA  . LEU A  518 ? 0.4470 0.5113 0.7554 -0.0597 0.1569  -0.0255 518 LEU A CA  
4003  C C   . LEU A  518 ? 0.4820 0.5474 0.8033 -0.0691 0.1569  -0.0298 518 LEU A C   
4004  O O   . LEU A  518 ? 0.4863 0.5648 0.8259 -0.0729 0.1583  -0.0346 518 LEU A O   
4005  C CB  . LEU A  518 ? 0.4774 0.5620 0.7986 -0.0528 0.1415  -0.0290 518 LEU A CB  
4006  C CG  . LEU A  518 ? 0.4648 0.5516 0.7767 -0.0428 0.1362  -0.0260 518 LEU A CG  
4007  C CD1 . LEU A  518 ? 0.4092 0.5091 0.7289 -0.0382 0.1197  -0.0283 518 LEU A CD1 
4008  C CD2 . LEU A  518 ? 0.4848 0.5512 0.7730 -0.0409 0.1438  -0.0192 518 LEU A CD2 
4009  N N   . GLU A  519 ? 0.5904 0.6419 0.9027 -0.0727 0.1554  -0.0282 519 GLU A N   
4010  C CA  . GLU A  519 ? 0.6386 0.6923 0.9639 -0.0806 0.1516  -0.0336 519 GLU A CA  
4011  C C   . GLU A  519 ? 0.5090 0.5675 0.8357 -0.0775 0.1375  -0.0358 519 GLU A C   
4012  O O   . GLU A  519 ? 0.4946 0.5463 0.8073 -0.0713 0.1348  -0.0311 519 GLU A O   
4013  C CB  . GLU A  519 ? 1.1008 1.1310 1.4140 -0.0886 0.1636  -0.0305 519 GLU A CB  
4014  C CG  . GLU A  519 ? 1.2497 1.2541 1.5356 -0.0859 0.1679  -0.0224 519 GLU A CG  
4015  C CD  . GLU A  519 ? 1.3695 1.3485 1.6384 -0.0917 0.1820  -0.0171 519 GLU A CD  
4016  O OE1 . GLU A  519 ? 1.3940 1.3623 1.6639 -0.0984 0.1825  -0.0189 519 GLU A OE1 
4017  O OE2 . GLU A  519 ? 1.4038 1.3725 1.6568 -0.0892 0.1924  -0.0113 519 GLU A OE2 
4018  N N   . VAL A  520 ? 0.3326 0.4035 0.6762 -0.0817 0.1284  -0.0431 520 VAL A N   
4019  C CA  . VAL A  520 ? 0.2668 0.3425 0.6114 -0.0790 0.1151  -0.0461 520 VAL A CA  
4020  C C   . VAL A  520 ? 0.2539 0.3128 0.5932 -0.0860 0.1158  -0.0480 520 VAL A C   
4021  O O   . VAL A  520 ? 0.2742 0.3325 0.6233 -0.0942 0.1172  -0.0532 520 VAL A O   
4022  C CB  . VAL A  520 ? 0.2126 0.3133 0.5767 -0.0772 0.1017  -0.0533 520 VAL A CB  
4023  C CG1 . VAL A  520 ? 0.1966 0.3002 0.5597 -0.0753 0.0887  -0.0568 520 VAL A CG1 
4024  C CG2 . VAL A  520 ? 0.1956 0.3107 0.5628 -0.0688 0.0994  -0.0510 520 VAL A CG2 
4025  N N   . ARG A  521 ? 0.2897 0.3331 0.6088 -0.0809 0.1131  -0.0434 521 ARG A N   
4026  C CA  . ARG A  521 ? 0.3349 0.3592 0.6420 -0.0840 0.1113  -0.0447 521 ARG A CA  
4027  C C   . ARG A  521 ? 0.3448 0.3779 0.6518 -0.0796 0.0957  -0.0504 521 ARG A C   
4028  O O   . ARG A  521 ? 0.2956 0.3391 0.5970 -0.0702 0.0867  -0.0486 521 ARG A O   
4029  C CB  . ARG A  521 ? 0.3804 0.3781 0.6582 -0.0787 0.1174  -0.0354 521 ARG A CB  
4030  C CG  . ARG A  521 ? 0.3849 0.3767 0.6565 -0.0786 0.1300  -0.0283 521 ARG A CG  
4031  C CD  . ARG A  521 ? 0.4524 0.4141 0.7020 -0.0805 0.1402  -0.0215 521 ARG A CD  
4032  N NE  . ARG A  521 ? 0.5191 0.4747 0.7660 -0.0840 0.1549  -0.0164 521 ARG A NE  
4033  C CZ  . ARG A  521 ? 0.5563 0.4977 0.7792 -0.0772 0.1594  -0.0079 521 ARG A CZ  
4034  N NH1 . ARG A  521 ? 0.5857 0.5190 0.7881 -0.0669 0.1496  -0.0038 521 ARG A NH1 
4035  N NH2 . ARG A  521 ? 0.5471 0.4826 0.7665 -0.0808 0.1736  -0.0039 521 ARG A NH2 
4036  N N   . ARG A  522 ? 0.5227 0.5507 0.8354 -0.0868 0.0930  -0.0574 522 ARG A N   
4037  C CA  . ARG A  522 ? 0.5914 0.6269 0.9031 -0.0835 0.0789  -0.0638 522 ARG A CA  
4038  C C   . ARG A  522 ? 0.6206 0.6333 0.9078 -0.0787 0.0773  -0.0615 522 ARG A C   
4039  O O   . ARG A  522 ? 0.6950 0.6863 0.9751 -0.0838 0.0846  -0.0610 522 ARG A O   
4040  C CB  . ARG A  522 ? 0.7331 0.7806 1.0680 -0.0940 0.0748  -0.0750 522 ARG A CB  
4041  C CG  . ARG A  522 ? 0.8458 0.9178 1.2089 -0.0989 0.0763  -0.0780 522 ARG A CG  
4042  C CD  . ARG A  522 ? 0.9840 1.0666 1.3649 -0.1073 0.0694  -0.0887 522 ARG A CD  
4043  N NE  . ARG A  522 ? 1.0953 1.1738 1.4693 -0.1070 0.0580  -0.0957 522 ARG A NE  
4044  C CZ  . ARG A  522 ? 1.1492 1.2458 1.5273 -0.1024 0.0431  -0.1014 522 ARG A CZ  
4045  N NH1 . ARG A  522 ? 1.1554 1.2769 1.5503 -0.0991 0.0376  -0.1016 522 ARG A NH1 
4046  N NH2 . ARG A  522 ? 1.1621 1.2505 1.5254 -0.1004 0.0337  -0.1066 522 ARG A NH2 
4047  N N   . GLY A  523 ? 0.5475 0.5643 0.8217 -0.0682 0.0683  -0.0594 523 GLY A N   
4048  C CA  . GLY A  523 ? 0.5394 0.5389 0.7926 -0.0620 0.0657  -0.0578 523 GLY A CA  
4049  C C   . GLY A  523 ? 0.5348 0.5171 0.7710 -0.0565 0.0736  -0.0474 523 GLY A C   
4050  O O   . GLY A  523 ? 0.5220 0.4927 0.7586 -0.0618 0.0840  -0.0437 523 GLY A O   
4051  N N   . LEU A  524 ? 0.4832 0.4624 0.7036 -0.0462 0.0687  -0.0430 524 LEU A N   
4052  C CA  . LEU A  524 ? 0.4371 0.4044 0.6421 -0.0394 0.0732  -0.0333 524 LEU A CA  
4053  C C   . LEU A  524 ? 0.5084 0.4555 0.6973 -0.0346 0.0731  -0.0318 524 LEU A C   
4054  O O   . LEU A  524 ? 0.5492 0.5002 0.7323 -0.0277 0.0661  -0.0332 524 LEU A O   
4055  C CB  . LEU A  524 ? 0.2441 0.2280 0.4479 -0.0311 0.0669  -0.0297 524 LEU A CB  
4056  C CG  . LEU A  524 ? 0.2435 0.2221 0.4342 -0.0234 0.0686  -0.0206 524 LEU A CG  
4057  C CD1 . LEU A  524 ? 0.2211 0.1945 0.4122 -0.0273 0.0777  -0.0162 524 LEU A CD1 
4058  C CD2 . LEU A  524 ? 0.1967 0.1927 0.3887 -0.0163 0.0607  -0.0193 524 LEU A CD2 
4059  N N   . ARG A  525 ? 0.5596 0.4848 0.7408 -0.0378 0.0813  -0.0285 525 ARG A N   
4060  C CA  . ARG A  525 ? 0.5820 0.4851 0.7489 -0.0335 0.0820  -0.0273 525 ARG A CA  
4061  C C   . ARG A  525 ? 0.5642 0.4704 0.7339 -0.0331 0.0754  -0.0363 525 ARG A C   
4062  O O   . ARG A  525 ? 0.5748 0.4773 0.7347 -0.0244 0.0712  -0.0357 525 ARG A O   
4063  C CB  . ARG A  525 ? 0.6372 0.5340 0.7883 -0.0220 0.0803  -0.0185 525 ARG A CB  
4064  C CG  . ARG A  525 ? 0.6873 0.5785 0.8311 -0.0212 0.0860  -0.0096 525 ARG A CG  
4065  C CD  . ARG A  525 ? 0.7612 0.6261 0.8946 -0.0250 0.0953  -0.0050 525 ARG A CD  
4066  N NE  . ARG A  525 ? 0.8562 0.7009 0.9754 -0.0177 0.0938  -0.0021 525 ARG A NE  
4067  C CZ  . ARG A  525 ? 0.9565 0.7798 1.0721 -0.0213 0.0985  -0.0039 525 ARG A CZ  
4068  N NH1 . ARG A  525 ? 0.9643 0.7840 1.0900 -0.0334 0.1051  -0.0088 525 ARG A NH1 
4069  N NH2 . ARG A  525 ? 1.0031 0.8086 1.1061 -0.0130 0.0966  -0.0009 525 ARG A NH2 
4070  N N   . ALA A  526 ? 0.4146 0.3280 0.5981 -0.0426 0.0745  -0.0451 526 ALA A N   
4071  C CA  . ALA A  526 ? 0.3338 0.2550 0.5205 -0.0428 0.0667  -0.0548 526 ALA A CA  
4072  C C   . ALA A  526 ? 0.3497 0.2510 0.5238 -0.0390 0.0666  -0.0580 526 ALA A C   
4073  O O   . ALA A  526 ? 0.3319 0.2384 0.4992 -0.0314 0.0607  -0.0603 526 ALA A O   
4074  C CB  . ALA A  526 ? 0.3391 0.2710 0.5435 -0.0544 0.0653  -0.0638 526 ALA A CB  
4075  N N   . GLN A  527 ? 0.6665 0.5445 0.8374 -0.0440 0.0737  -0.0583 527 GLN A N   
4076  C CA  . GLN A  527 ? 0.7549 0.6127 0.9150 -0.0406 0.0738  -0.0625 527 GLN A CA  
4077  C C   . GLN A  527 ? 0.7553 0.6059 0.9007 -0.0270 0.0735  -0.0544 527 GLN A C   
4078  O O   . GLN A  527 ? 0.8117 0.6593 0.9497 -0.0194 0.0700  -0.0580 527 GLN A O   
4079  C CB  . GLN A  527 ? 0.6876 0.5202 0.8479 -0.0495 0.0820  -0.0639 527 GLN A CB  
4080  C CG  . GLN A  527 ? 0.6889 0.5299 0.8670 -0.0640 0.0845  -0.0690 527 GLN A CG  
4081  C CD  . GLN A  527 ? 0.6936 0.5509 0.8831 -0.0696 0.0761  -0.0820 527 GLN A CD  
4082  O OE1 . GLN A  527 ? 0.6929 0.5731 0.8980 -0.0753 0.0723  -0.0852 527 GLN A OE1 
4083  N NE2 . GLN A  527 ? 0.6984 0.5432 0.8797 -0.0677 0.0727  -0.0900 527 GLN A NE2 
4084  N N   . THR A  528 ? 0.4303 0.2790 0.5720 -0.0238 0.0772  -0.0438 528 THR A N   
4085  C CA  . THR A  528 ? 0.3518 0.1938 0.4811 -0.0114 0.0765  -0.0355 528 THR A CA  
4086  C C   . THR A  528 ? 0.3173 0.1818 0.4481 -0.0035 0.0690  -0.0361 528 THR A C   
4087  O O   . THR A  528 ? 0.3184 0.1806 0.4427 0.0061  0.0666  -0.0356 528 THR A O   
4088  C CB  . THR A  528 ? 0.3664 0.2018 0.4907 -0.0110 0.0814  -0.0247 528 THR A CB  
4089  O OG1 . THR A  528 ? 0.4455 0.2522 0.5608 -0.0130 0.0884  -0.0216 528 THR A OG1 
4090  C CG2 . THR A  528 ? 0.3285 0.1710 0.4453 0.0008  0.0771  -0.0169 528 THR A CG2 
4091  N N   . CYS A  529 ? 0.3718 0.2583 0.5123 -0.0076 0.0658  -0.0372 529 CYS A N   
4092  C CA  . CYS A  529 ? 0.3701 0.2769 0.5118 -0.0010 0.0593  -0.0373 529 CYS A CA  
4093  C C   . CYS A  529 ? 0.3455 0.2555 0.4863 0.0000  0.0554  -0.0466 529 CYS A C   
4094  O O   . CYS A  529 ? 0.3658 0.2838 0.5024 0.0079  0.0521  -0.0462 529 CYS A O   
4095  C CB  . CYS A  529 ? 0.3846 0.3121 0.5358 -0.0047 0.0569  -0.0352 529 CYS A CB  
4096  S SG  . CYS A  529 ? 0.9156 0.8407 1.0624 -0.0009 0.0603  -0.0234 529 CYS A SG  
4097  N N   . ALA A  530 ? 0.2971 0.1999 0.4411 -0.0081 0.0560  -0.0552 530 ALA A N   
4098  C CA  . ALA A  530 ? 0.3058 0.2077 0.4455 -0.0066 0.0525  -0.0647 530 ALA A CA  
4099  C C   . ALA A  530 ? 0.3181 0.2033 0.4463 0.0031  0.0556  -0.0629 530 ALA A C   
4100  O O   . ALA A  530 ? 0.3330 0.2231 0.4555 0.0100  0.0532  -0.0662 530 ALA A O   
4101  C CB  . ALA A  530 ? 0.3214 0.2156 0.4663 -0.0176 0.0525  -0.0748 530 ALA A CB  
4102  N N   . PHE A  531 ? 0.3911 0.2568 0.5158 0.0043  0.0611  -0.0572 531 PHE A N   
4103  C CA  . PHE A  531 ? 0.4159 0.2664 0.5312 0.0148  0.0635  -0.0547 531 PHE A CA  
4104  C C   . PHE A  531 ? 0.4137 0.2798 0.5281 0.0256  0.0606  -0.0481 531 PHE A C   
4105  O O   . PHE A  531 ? 0.4184 0.2884 0.5296 0.0330  0.0596  -0.0515 531 PHE A O   
4106  C CB  . PHE A  531 ? 0.3593 0.1856 0.4702 0.0144  0.0692  -0.0486 531 PHE A CB  
4107  C CG  . PHE A  531 ? 0.3666 0.1816 0.4698 0.0270  0.0703  -0.0421 531 PHE A CG  
4108  C CD1 . PHE A  531 ? 0.3825 0.1848 0.4804 0.0339  0.0714  -0.0473 531 PHE A CD1 
4109  C CD2 . PHE A  531 ? 0.4948 0.3113 0.5959 0.0322  0.0700  -0.0310 531 PHE A CD2 
4110  C CE1 . PHE A  531 ? 0.4389 0.2317 0.5318 0.0464  0.0721  -0.0412 531 PHE A CE1 
4111  C CE2 . PHE A  531 ? 0.5248 0.3319 0.6201 0.0442  0.0697  -0.0251 531 PHE A CE2 
4112  C CZ  . PHE A  531 ? 0.3819 0.1778 0.4741 0.0515  0.0707  -0.0301 531 PHE A CZ  
4113  N N   . TRP A  532 ? 0.3690 0.2442 0.4866 0.0258  0.0598  -0.0393 532 TRP A N   
4114  C CA  . TRP A  532 ? 0.3584 0.2468 0.4762 0.0351  0.0571  -0.0323 532 TRP A CA  
4115  C C   . TRP A  532 ? 0.3586 0.2686 0.4799 0.0371  0.0532  -0.0358 532 TRP A C   
4116  O O   . TRP A  532 ? 0.3707 0.2869 0.4912 0.0457  0.0526  -0.0342 532 TRP A O   
4117  C CB  . TRP A  532 ? 0.2840 0.1773 0.4038 0.0334  0.0566  -0.0234 532 TRP A CB  
4118  C CG  . TRP A  532 ? 0.4081 0.2809 0.5209 0.0355  0.0600  -0.0168 532 TRP A CG  
4119  C CD1 . TRP A  532 ? 0.3103 0.1695 0.4206 0.0279  0.0643  -0.0147 532 TRP A CD1 
4120  C CD2 . TRP A  532 ? 0.4791 0.3424 0.5862 0.0462  0.0593  -0.0110 532 TRP A CD2 
4121  N NE1 . TRP A  532 ? 0.3262 0.1663 0.4270 0.0334  0.0665  -0.0074 532 TRP A NE1 
4122  C CE2 . TRP A  532 ? 0.3246 0.1672 0.4235 0.0450  0.0626  -0.0051 532 TRP A CE2 
4123  C CE3 . TRP A  532 ? 0.3030 0.1738 0.4117 0.0569  0.0562  -0.0102 532 TRP A CE3 
4124  C CZ2 . TRP A  532 ? 0.3379 0.1665 0.4290 0.0548  0.0617  0.0017  532 TRP A CZ2 
4125  C CZ3 . TRP A  532 ? 0.5439 0.4027 0.6478 0.0662  0.0555  -0.0040 532 TRP A CZ3 
4126  C CH2 . TRP A  532 ? 0.3321 0.1697 0.4267 0.0655  0.0576  0.0020  532 TRP A CH2 
4127  N N   . ASN A  533 ? 0.3754 0.2972 0.5010 0.0292  0.0508  -0.0402 533 ASN A N   
4128  C CA  . ASN A  533 ? 0.3874 0.3290 0.5148 0.0304  0.0467  -0.0425 533 ASN A CA  
4129  C C   . ASN A  533 ? 0.4049 0.3440 0.5261 0.0318  0.0465  -0.0518 533 ASN A C   
4130  O O   . ASN A  533 ? 0.3996 0.3491 0.5178 0.0375  0.0456  -0.0522 533 ASN A O   
4131  C CB  . ASN A  533 ? 0.4396 0.3954 0.5742 0.0224  0.0432  -0.0428 533 ASN A CB  
4132  C CG  . ASN A  533 ? 0.4093 0.3676 0.5490 0.0208  0.0442  -0.0345 533 ASN A CG  
4133  O OD1 . ASN A  533 ? 0.4026 0.3589 0.5402 0.0269  0.0452  -0.0273 533 ASN A OD1 
4134  N ND2 . ASN A  533 ? 0.3569 0.3202 0.5037 0.0126  0.0437  -0.0359 533 ASN A ND2 
4135  N N   . ARG A  534 ? 0.4101 0.3347 0.5289 0.0264  0.0478  -0.0594 534 ARG A N   
4136  C CA  . ARG A  534 ? 0.4774 0.3984 0.5888 0.0267  0.0469  -0.0698 534 ARG A CA  
4137  C C   . ARG A  534 ? 0.4554 0.3583 0.5593 0.0340  0.0519  -0.0724 534 ARG A C   
4138  O O   . ARG A  534 ? 0.4505 0.3570 0.5483 0.0412  0.0530  -0.0752 534 ARG A O   
4139  C CB  . ARG A  534 ? 0.7641 0.6827 0.8778 0.0158  0.0438  -0.0788 534 ARG A CB  
4140  C CG  . ARG A  534 ? 0.8541 0.7931 0.9758 0.0099  0.0380  -0.0776 534 ARG A CG  
4141  C CD  . ARG A  534 ? 0.9527 0.8894 1.0819 -0.0016 0.0354  -0.0851 534 ARG A CD  
4142  N NE  . ARG A  534 ? 1.0056 0.9596 1.1366 -0.0050 0.0275  -0.0907 534 ARG A NE  
4143  C CZ  . ARG A  534 ? 1.0592 1.0135 1.1797 -0.0035 0.0233  -0.0994 534 ARG A CZ  
4144  N NH1 . ARG A  534 ? 1.0577 0.9962 1.1662 0.0014  0.0273  -0.1039 534 ARG A NH1 
4145  N NH2 . ARG A  534 ? 1.0776 1.0477 1.1990 -0.0062 0.0151  -0.1035 534 ARG A NH2 
4146  N N   . PHE A  535 ? 0.3914 0.2741 0.4956 0.0323  0.0555  -0.0718 535 PHE A N   
4147  C CA  . PHE A  535 ? 0.3978 0.2603 0.4950 0.0390  0.0601  -0.0754 535 PHE A CA  
4148  C C   . PHE A  535 ? 0.3502 0.2141 0.4476 0.0515  0.0626  -0.0675 535 PHE A C   
4149  O O   . PHE A  535 ? 0.3573 0.2241 0.4510 0.0595  0.0644  -0.0709 535 PHE A O   
4150  C CB  . PHE A  535 ? 0.3744 0.2126 0.4711 0.0328  0.0632  -0.0774 535 PHE A CB  
4151  C CG  . PHE A  535 ? 0.3984 0.2137 0.4877 0.0399  0.0678  -0.0812 535 PHE A CG  
4152  C CD1 . PHE A  535 ? 0.4132 0.2238 0.4954 0.0418  0.0683  -0.0925 535 PHE A CD1 
4153  C CD2 . PHE A  535 ? 0.5193 0.3168 0.6077 0.0454  0.0716  -0.0736 535 PHE A CD2 
4154  C CE1 . PHE A  535 ? 0.4367 0.2254 0.5123 0.0492  0.0731  -0.0965 535 PHE A CE1 
4155  C CE2 . PHE A  535 ? 0.4317 0.2073 0.5138 0.0530  0.0757  -0.0769 535 PHE A CE2 
4156  C CZ  . PHE A  535 ? 0.4456 0.2168 0.5220 0.0549  0.0768  -0.0886 535 PHE A CZ  
4157  N N   . LEU A  536 ? 0.3497 0.2121 0.4515 0.0533  0.0627  -0.0573 536 LEU A N   
4158  C CA  . LEU A  536 ? 0.3663 0.2294 0.4697 0.0651  0.0638  -0.0498 536 LEU A CA  
4159  C C   . LEU A  536 ? 0.3732 0.2565 0.4797 0.0727  0.0632  -0.0496 536 LEU A C   
4160  O O   . LEU A  536 ? 0.3873 0.2684 0.4953 0.0831  0.0655  -0.0481 536 LEU A O   
4161  C CB  . LEU A  536 ? 0.3373 0.2004 0.4440 0.0650  0.0620  -0.0388 536 LEU A CB  
4162  C CG  . LEU A  536 ? 0.3453 0.1906 0.4494 0.0736  0.0635  -0.0322 536 LEU A CG  
4163  C CD1 . LEU A  536 ? 0.3305 0.1867 0.4382 0.0768  0.0598  -0.0218 536 LEU A CD1 
4164  C CD2 . LEU A  536 ? 0.3576 0.1972 0.4613 0.0852  0.0657  -0.0354 536 LEU A CD2 
4165  N N   . PRO A  537 ? 0.4823 0.3854 0.5908 0.0678  0.0603  -0.0505 537 PRO A N   
4166  C CA  . PRO A  537 ? 0.5108 0.4300 0.6207 0.0748  0.0615  -0.0508 537 PRO A CA  
4167  C C   . PRO A  537 ? 0.5574 0.4669 0.6602 0.0802  0.0662  -0.0596 537 PRO A C   
4168  O O   . PRO A  537 ? 0.6169 0.5289 0.7229 0.0900  0.0697  -0.0580 537 PRO A O   
4169  C CB  . PRO A  537 ? 0.6168 0.5531 0.7261 0.0675  0.0579  -0.0519 537 PRO A CB  
4170  C CG  . PRO A  537 ? 0.6105 0.5465 0.7241 0.0596  0.0542  -0.0474 537 PRO A CG  
4171  C CD  . PRO A  537 ? 0.6118 0.5252 0.7230 0.0577  0.0563  -0.0492 537 PRO A CD  
4172  N N   . LYS A  538 ? 0.5257 0.4238 0.6199 0.0742  0.0663  -0.0691 538 LYS A N   
4173  C CA  . LYS A  538 ? 0.5427 0.4299 0.6278 0.0789  0.0708  -0.0790 538 LYS A CA  
4174  C C   . LYS A  538 ? 0.5563 0.4254 0.6428 0.0883  0.0756  -0.0786 538 LYS A C   
4175  O O   . LYS A  538 ? 0.5545 0.4167 0.6359 0.0957  0.0807  -0.0851 538 LYS A O   
4176  C CB  . LYS A  538 ? 0.5340 0.4107 0.6100 0.0694  0.0685  -0.0898 538 LYS A CB  
4177  C CG  . LYS A  538 ? 0.5734 0.4674 0.6468 0.0619  0.0632  -0.0919 538 LYS A CG  
4178  C CD  . LYS A  538 ? 0.6802 0.5641 0.7476 0.0519  0.0594  -0.1024 538 LYS A CD  
4179  C CE  . LYS A  538 ? 0.7627 0.6652 0.8311 0.0441  0.0522  -0.1024 538 LYS A CE  
4180  N NZ  . LYS A  538 ? 0.8113 0.7083 0.8838 0.0322  0.0471  -0.1078 538 LYS A NZ  
4181  N N   . LEU A  539 ? 0.6208 0.4818 0.7133 0.0885  0.0741  -0.0706 539 LEU A N   
4182  C CA  . LEU A  539 ? 0.6620 0.5033 0.7548 0.0972  0.0776  -0.0694 539 LEU A CA  
4183  C C   . LEU A  539 ? 0.7791 0.6326 0.8806 0.1099  0.0792  -0.0635 539 LEU A C   
4184  O O   . LEU A  539 ? 0.8899 0.7423 0.9907 0.1184  0.0842  -0.0689 539 LEU A O   
4185  C CB  . LEU A  539 ? 0.5409 0.3663 0.6342 0.0925  0.0755  -0.0630 539 LEU A CB  
4186  C CG  . LEU A  539 ? 0.5295 0.3257 0.6178 0.0977  0.0793  -0.0652 539 LEU A CG  
4187  C CD1 . LEU A  539 ? 0.5155 0.3004 0.5963 0.0985  0.0835  -0.0782 539 LEU A CD1 
4188  C CD2 . LEU A  539 ? 0.5508 0.3293 0.6359 0.0881  0.0784  -0.0618 539 LEU A CD2 
4189  N N   . LEU A  540 ? 0.7841 0.6507 0.8945 0.1111  0.0752  -0.0530 540 LEU A N   
4190  C CA  . LEU A  540 ? 0.8080 0.6861 0.9296 0.1231  0.0755  -0.0468 540 LEU A CA  
4191  C C   . LEU A  540 ? 1.2354 1.1343 1.3620 0.1275  0.0795  -0.0504 540 LEU A C   
4192  O O   . LEU A  540 ? 1.2038 1.1150 1.3418 0.1371  0.0810  -0.0469 540 LEU A O   
4193  C CB  . LEU A  540 ? 0.7092 0.5953 0.8379 0.1224  0.0692  -0.0355 540 LEU A CB  
4194  C CG  . LEU A  540 ? 0.6501 0.5548 0.7818 0.1136  0.0645  -0.0304 540 LEU A CG  
4195  C CD1 . LEU A  540 ? 0.5991 0.4940 0.7279 0.1090  0.0599  -0.0231 540 LEU A CD1 
4196  C CD2 . LEU A  540 ? 0.6537 0.5665 0.7799 0.1039  0.0656  -0.0367 540 LEU A CD2 
4197  N N   . SER A  541 ? 1.1917 1.0934 1.3089 0.1201  0.0812  -0.0577 541 SER A N   
4198  C CA  . SER A  541 ? 1.2300 1.1481 1.3453 0.1206  0.0852  -0.0621 541 SER A CA  
4199  C C   . SER A  541 ? 1.2870 1.1975 1.3943 0.1270  0.0931  -0.0723 541 SER A C   
4200  O O   . SER A  541 ? 1.3032 1.2200 1.4005 0.1229  0.0951  -0.0781 541 SER A O   
4201  C CB  . SER A  541 ? 1.3578 1.2866 1.4669 0.1091  0.0810  -0.0623 541 SER A CB  
4202  O OG  . SER A  541 ? 1.3709 1.3129 1.4898 0.1057  0.0756  -0.0524 541 SER A OG  
4203  N N   . ALA A  542 ? 1.2978 1.1950 1.4084 0.1373  0.0975  -0.0746 542 ALA A N   
4204  C CA  . ALA A  542 ? 1.3101 1.1842 1.4093 0.1407  0.1026  -0.0854 542 ALA A CA  
4205  C C   . ALA A  542 ? 1.3265 1.1760 1.4259 0.1423  0.1001  -0.0839 542 ALA A C   
4206  O O   . ALA A  542 ? 1.3129 1.1396 1.4027 0.1435  0.1034  -0.0925 542 ALA A O   
4207  C CB  . ALA A  542 ? 1.2921 1.1606 1.3739 0.1309  0.1023  -0.0954 542 ALA A CB  
4208  N N   . THR A  543 ? 1.5081 1.3615 1.6171 0.1418  0.0943  -0.0729 543 THR A N   
4209  C CA  . THR A  543 ? 1.5474 1.3847 1.6584 0.1468  0.0905  -0.0668 543 THR A CA  
4210  C C   . THR A  543 ? 1.6071 1.4184 1.7080 0.1505  0.0926  -0.0733 543 THR A C   
4211  O O   . THR A  543 ? 1.6336 1.4233 1.7285 0.1461  0.0902  -0.0716 543 THR A O   
4212  C CB  . THR A  543 ? 1.5280 1.3839 1.6518 0.1562  0.0863  -0.0577 543 THR A CB  
4213  O OG1 . THR A  543 ? 1.5108 1.3866 1.6437 0.1519  0.0822  -0.0497 543 THR A OG1 
4214  C CG2 . THR A  543 ? 1.5260 1.3648 1.6487 0.1622  0.0812  -0.0524 543 THR A CG2 
4215  O OXT . THR A  543 ? 1.5447 1.3557 1.6434 0.1576  0.0967  -0.0800 543 THR A OXT 
4216  N N   . ASP B  5   ? 1.3615 0.9044 0.9955 -0.5886 0.2793  -0.0144 5   ASP B N   
4217  C CA  . ASP B  5   ? 1.3654 0.9133 0.9898 -0.5852 0.2813  -0.0122 5   ASP B CA  
4218  C C   . ASP B  5   ? 1.3841 0.9066 0.9901 -0.5756 0.2739  -0.0016 5   ASP B C   
4219  O O   . ASP B  5   ? 1.3424 0.8586 0.9528 -0.5622 0.2649  0.0001  5   ASP B O   
4220  C CB  . ASP B  5   ? 1.4791 1.0578 1.1226 -0.5754 0.2808  -0.0208 5   ASP B CB  
4221  C CG  . ASP B  5   ? 1.4897 1.0843 1.1304 -0.5810 0.2888  -0.0238 5   ASP B CG  
4222  O OD1 . ASP B  5   ? 1.4970 1.0819 1.1223 -0.5769 0.2878  -0.0180 5   ASP B OD1 
4223  O OD2 . ASP B  5   ? 1.4859 1.1032 1.1404 -0.5893 0.2962  -0.0323 5   ASP B OD2 
4224  N N   . PRO B  6   ? 1.7329 1.2409 1.3180 -0.5828 0.2777  0.0054  6   PRO B N   
4225  C CA  . PRO B  6   ? 1.7728 1.2536 1.3386 -0.5762 0.2709  0.0165  6   PRO B CA  
4226  C C   . PRO B  6   ? 1.7273 1.2144 1.2950 -0.5591 0.2639  0.0170  6   PRO B C   
4227  O O   . PRO B  6   ? 1.7088 1.1793 1.2724 -0.5479 0.2549  0.0227  6   PRO B O   
4228  C CB  . PRO B  6   ? 1.9354 1.4059 1.4804 -0.5901 0.2783  0.0221  6   PRO B CB  
4229  C CG  . PRO B  6   ? 1.9230 1.4227 1.4783 -0.5979 0.2880  0.0125  6   PRO B CG  
4230  C CD  . PRO B  6   ? 1.8922 1.4112 1.4718 -0.5972 0.2885  0.0028  6   PRO B CD  
4231  N N   . GLN B  7   ? 1.6879 1.1992 1.2627 -0.5573 0.2681  0.0107  7   GLN B N   
4232  C CA  . GLN B  7   ? 1.6556 1.1729 1.2298 -0.5432 0.2631  0.0115  7   GLN B CA  
4233  C C   . GLN B  7   ? 1.6224 1.1500 1.2149 -0.5278 0.2550  0.0073  7   GLN B C   
4234  O O   . GLN B  7   ? 1.6214 1.1433 1.2113 -0.5142 0.2475  0.0108  7   GLN B O   
4235  C CB  . GLN B  7   ? 1.5866 1.1279 1.1650 -0.5472 0.2708  0.0051  7   GLN B CB  
4236  C CG  . GLN B  7   ? 1.6334 1.1686 1.1950 -0.5638 0.2801  0.0077  7   GLN B CG  
4237  C CD  . GLN B  7   ? 1.6626 1.1795 1.2010 -0.5623 0.2780  0.0169  7   GLN B CD  
4238  O OE1 . GLN B  7   ? 1.6690 1.1975 1.2033 -0.5636 0.2824  0.0148  7   GLN B OE1 
4239  N NE2 . GLN B  7   ? 1.6766 1.1649 1.2002 -0.5596 0.2712  0.0270  7   GLN B NE2 
4240  N N   . LEU B  8   ? 1.5483 1.0912 1.1593 -0.5304 0.2568  -0.0003 8   LEU B N   
4241  C CA  . LEU B  8   ? 1.4784 1.0349 1.1086 -0.5174 0.2501  -0.0055 8   LEU B CA  
4242  C C   . LEU B  8   ? 1.4850 1.0200 1.1111 -0.5078 0.2407  0.0003  8   LEU B C   
4243  O O   . LEU B  8   ? 1.4750 1.0189 1.1150 -0.4966 0.2345  -0.0031 8   LEU B O   
4244  C CB  . LEU B  8   ? 1.2253 0.8044 0.8762 -0.5235 0.2545  -0.0151 8   LEU B CB  
4245  C CG  . LEU B  8   ? 1.2223 0.8268 0.8825 -0.5324 0.2638  -0.0227 8   LEU B CG  
4246  C CD1 . LEU B  8   ? 1.1933 0.8247 0.8792 -0.5294 0.2635  -0.0324 8   LEU B CD1 
4247  C CD2 . LEU B  8   ? 1.2146 0.8266 0.8684 -0.5288 0.2661  -0.0220 8   LEU B CD2 
4248  N N   . LEU B  9   ? 1.6202 1.1274 1.2280 -0.5126 0.2394  0.0090  9   LEU B N   
4249  C CA  . LEU B  9   ? 1.6007 1.0861 1.2043 -0.5034 0.2304  0.0149  9   LEU B CA  
4250  C C   . LEU B  9   ? 1.5734 1.0380 1.1581 -0.4970 0.2255  0.0245  9   LEU B C   
4251  O O   . LEU B  9   ? 1.5988 1.0468 1.1658 -0.5064 0.2288  0.0312  9   LEU B O   
4252  C CB  . LEU B  9   ? 1.4443 0.9132 1.0466 -0.5135 0.2314  0.0164  9   LEU B CB  
4253  C CG  . LEU B  9   ? 1.4191 0.8667 1.0207 -0.5058 0.2228  0.0208  9   LEU B CG  
4254  C CD1 . LEU B  9   ? 1.4018 0.8507 1.0158 -0.5124 0.2240  0.0157  9   LEU B CD1 
4255  C CD2 . LEU B  9   ? 1.4543 0.8707 1.0350 -0.5086 0.2205  0.0321  9   LEU B CD2 
4256  N N   . VAL B  10  ? 1.2540 0.7196 0.8427 -0.4813 0.2175  0.0252  10  VAL B N   
4257  C CA  . VAL B  10  ? 1.2596 0.7090 0.8326 -0.4736 0.2124  0.0334  10  VAL B CA  
4258  C C   . VAL B  10  ? 1.2579 0.6926 0.8325 -0.4600 0.2021  0.0372  10  VAL B C   
4259  O O   . VAL B  10  ? 1.2258 0.6700 0.8162 -0.4530 0.1986  0.0318  10  VAL B O   
4260  C CB  . VAL B  10  ? 1.3062 0.7748 0.8801 -0.4683 0.2142  0.0305  10  VAL B CB  
4261  C CG1 . VAL B  10  ? 1.2862 0.7789 0.8811 -0.4570 0.2114  0.0224  10  VAL B CG1 
4262  C CG2 . VAL B  10  ? 1.2679 0.7202 0.8248 -0.4616 0.2094  0.0389  10  VAL B CG2 
4263  N N   . ARG B  11  ? 1.5825 0.9944 1.1409 -0.4566 0.1973  0.0463  11  ARG B N   
4264  C CA  . ARG B  11  ? 1.6532 1.0457 1.2113 -0.4468 0.1883  0.0510  11  ARG B CA  
4265  C C   . ARG B  11  ? 1.6245 1.0243 1.1911 -0.4294 0.1804  0.0494  11  ARG B C   
4266  O O   . ARG B  11  ? 1.6371 1.0394 1.2168 -0.4228 0.1762  0.0456  11  ARG B O   
4267  C CB  . ARG B  11  ? 1.7488 1.1104 1.2876 -0.4519 0.1860  0.0620  11  ARG B CB  
4268  C CG  . ARG B  11  ? 1.8053 1.1488 1.3451 -0.4602 0.1861  0.0639  11  ARG B CG  
4269  C CD  . ARG B  11  ? 1.8044 1.1322 1.3500 -0.4489 0.1768  0.0663  11  ARG B CD  
4270  N NE  . ARG B  11  ? 1.7880 1.1242 1.3516 -0.4479 0.1764  0.0587  11  ARG B NE  
4271  C CZ  . ARG B  11  ? 1.8080 1.1326 1.3740 -0.4575 0.1784  0.0585  11  ARG B CZ  
4272  N NH1 . ARG B  11  ? 1.8622 1.1662 1.4139 -0.4693 0.1813  0.0659  11  ARG B NH1 
4273  N NH2 . ARG B  11  ? 1.7631 1.0967 1.3457 -0.4558 0.1776  0.0511  11  ARG B NH2 
4274  N N   . VAL B  12  ? 1.3986 0.8010 0.9578 -0.4222 0.1782  0.0522  12  VAL B N   
4275  C CA  . VAL B  12  ? 1.3123 0.7254 0.8815 -0.4061 0.1715  0.0494  12  VAL B CA  
4276  C C   . VAL B  12  ? 1.2698 0.6679 0.8426 -0.3953 0.1626  0.0521  12  VAL B C   
4277  O O   . VAL B  12  ? 1.2326 0.6340 0.8182 -0.3942 0.1614  0.0476  12  VAL B O   
4278  C CB  . VAL B  12  ? 1.2282 0.6728 0.8150 -0.4021 0.1744  0.0396  12  VAL B CB  
4279  C CG1 . VAL B  12  ? 1.2242 0.6830 0.8071 -0.4106 0.1823  0.0374  12  VAL B CG1 
4280  C CG2 . VAL B  12  ? 1.1389 0.5942 0.7424 -0.4042 0.1756  0.0327  12  VAL B CG2 
4281  N N   . ARG B  13  ? 1.4077 0.7890 0.9694 -0.3882 0.1565  0.0594  13  ARG B N   
4282  C CA  . ARG B  13  ? 1.4796 0.8420 1.0423 -0.3796 0.1482  0.0635  13  ARG B CA  
4283  C C   . ARG B  13  ? 1.5933 0.9656 1.1751 -0.3720 0.1449  0.0564  13  ARG B C   
4284  O O   . ARG B  13  ? 1.6245 0.9807 1.2089 -0.3680 0.1396  0.0586  13  ARG B O   
4285  C CB  . ARG B  13  ? 1.5823 0.9373 1.1364 -0.3686 0.1416  0.0690  13  ARG B CB  
4286  C CG  . ARG B  13  ? 1.6422 0.9782 1.1976 -0.3584 0.1325  0.0734  13  ARG B CG  
4287  C CD  . ARG B  13  ? 1.6679 1.0154 1.2306 -0.3431 0.1266  0.0710  13  ARG B CD  
4288  N NE  . ARG B  13  ? 1.7316 1.0640 1.2816 -0.3368 0.1208  0.0788  13  ARG B NE  
4289  C CZ  . ARG B  13  ? 1.7639 1.0977 1.3007 -0.3392 0.1227  0.0824  13  ARG B CZ  
4290  N NH1 . ARG B  13  ? 1.7723 1.1217 1.3072 -0.3479 0.1306  0.0788  13  ARG B NH1 
4291  N NH2 . ARG B  13  ? 1.7663 1.0859 1.2920 -0.3332 0.1167  0.0894  13  ARG B NH2 
4292  N N   . GLY B  14  ? 1.4705 0.8687 1.0656 -0.3700 0.1479  0.0482  14  GLY B N   
4293  C CA  . GLY B  14  ? 1.4055 0.8139 1.0175 -0.3668 0.1466  0.0412  14  GLY B CA  
4294  C C   . GLY B  14  ? 1.3772 0.7824 0.9935 -0.3788 0.1512  0.0384  14  GLY B C   
4295  O O   . GLY B  14  ? 1.3374 0.7466 0.9662 -0.3765 0.1493  0.0334  14  GLY B O   
4296  N N   . GLY B  15  ? 1.4089 0.8064 1.0146 -0.3918 0.1572  0.0415  15  GLY B N   
4297  C CA  . GLY B  15  ? 1.4040 0.7994 1.0133 -0.4044 0.1623  0.0387  15  GLY B CA  
4298  C C   . GLY B  15  ? 1.3903 0.8071 1.0045 -0.4148 0.1709  0.0328  15  GLY B C   
4299  O O   . GLY B  15  ? 1.3859 0.8213 1.0018 -0.4121 0.1732  0.0301  15  GLY B O   
4300  N N   . GLN B  16  ? 1.3264 0.7406 0.9438 -0.4265 0.1754  0.0303  16  GLN B N   
4301  C CA  . GLN B  16  ? 1.3319 0.7606 0.9507 -0.4396 0.1844  0.0262  16  GLN B CA  
4302  C C   . GLN B  16  ? 1.2512 0.7116 0.8839 -0.4371 0.1876  0.0178  16  GLN B C   
4303  O O   . GLN B  16  ? 1.2321 0.7062 0.8788 -0.4281 0.1837  0.0125  16  GLN B O   
4304  C CB  . GLN B  16  ? 1.5882 1.0085 1.2106 -0.4512 0.1875  0.0244  16  GLN B CB  
4305  C CG  . GLN B  16  ? 1.6562 1.0832 1.2755 -0.4670 0.1968  0.0226  16  GLN B CG  
4306  C CD  . GLN B  16  ? 1.7342 1.1350 1.3409 -0.4789 0.1989  0.0291  16  GLN B CD  
4307  O OE1 . GLN B  16  ? 1.7723 1.1741 1.3833 -0.4908 0.2040  0.0259  16  GLN B OE1 
4308  N NE2 . GLN B  16  ? 1.7461 1.1233 1.3377 -0.4758 0.1948  0.0385  16  GLN B NE2 
4309  N N   . LEU B  17  ? 1.1868 0.6585 0.8159 -0.4457 0.1948  0.0166  17  LEU B N   
4310  C CA  . LEU B  17  ? 1.1613 0.6625 0.8036 -0.4441 0.1983  0.0090  17  LEU B CA  
4311  C C   . LEU B  17  ? 1.1644 0.6779 0.8102 -0.4590 0.2075  0.0044  17  LEU B C   
4312  O O   . LEU B  17  ? 1.1950 0.6964 0.8271 -0.4699 0.2127  0.0086  17  LEU B O   
4313  C CB  . LEU B  17  ? 1.1372 0.6442 0.7733 -0.4366 0.1975  0.0114  17  LEU B CB  
4314  C CG  . LEU B  17  ? 1.1061 0.6183 0.7469 -0.4202 0.1899  0.0117  17  LEU B CG  
4315  C CD1 . LEU B  17  ? 1.1010 0.6183 0.7336 -0.4175 0.1916  0.0139  17  LEU B CD1 
4316  C CD2 . LEU B  17  ? 1.0716 0.6072 0.7331 -0.4135 0.1880  0.0038  17  LEU B CD2 
4317  N N   . ARG B  18  ? 1.1421 0.6799 0.8059 -0.4595 0.2096  -0.0040 18  ARG B N   
4318  C CA  . ARG B  18  ? 1.2132 0.7666 0.8827 -0.4726 0.2184  -0.0093 18  ARG B CA  
4319  C C   . ARG B  18  ? 1.1450 0.7258 0.8258 -0.4694 0.2213  -0.0151 18  ARG B C   
4320  O O   . ARG B  18  ? 1.1036 0.7035 0.8015 -0.4620 0.2183  -0.0207 18  ARG B O   
4321  C CB  . ARG B  18  ? 1.5568 1.1155 1.2390 -0.4794 0.2196  -0.0149 18  ARG B CB  
4322  C CG  . ARG B  18  ? 1.5732 1.1519 1.2650 -0.4919 0.2282  -0.0217 18  ARG B CG  
4323  C CD  . ARG B  18  ? 1.6058 1.1833 1.3054 -0.5014 0.2299  -0.0256 18  ARG B CD  
4324  N NE  . ARG B  18  ? 1.6702 1.2186 1.3551 -0.5077 0.2294  -0.0191 18  ARG B NE  
4325  C CZ  . ARG B  18  ? 1.7206 1.2539 1.3900 -0.5190 0.2350  -0.0140 18  ARG B CZ  
4326  N NH1 . ARG B  18  ? 1.7153 1.2599 1.3810 -0.5255 0.2420  -0.0150 18  ARG B NH1 
4327  N NH2 . ARG B  18  ? 1.7516 1.2579 1.4093 -0.5239 0.2335  -0.0078 18  ARG B NH2 
4328  N N   . GLY B  19  ? 1.2514 0.8343 0.9231 -0.4757 0.2275  -0.0137 19  GLY B N   
4329  C CA  . GLY B  19  ? 1.2288 0.8365 0.9107 -0.4734 0.2309  -0.0191 19  GLY B CA  
4330  C C   . GLY B  19  ? 1.2323 0.8639 0.9317 -0.4820 0.2370  -0.0278 19  GLY B C   
4331  O O   . GLY B  19  ? 1.2259 0.8581 0.9333 -0.4867 0.2369  -0.0307 19  GLY B O   
4332  N N   . ILE B  20  ? 1.4446 1.0961 1.1508 -0.4839 0.2423  -0.0322 20  ILE B N   
4333  C CA  . ILE B  20  ? 1.4815 1.1568 1.2046 -0.4928 0.2489  -0.0407 20  ILE B CA  
4334  C C   . ILE B  20  ? 1.5148 1.2001 1.2339 -0.5004 0.2575  -0.0427 20  ILE B C   
4335  O O   . ILE B  20  ? 1.5299 1.2139 1.2418 -0.4938 0.2565  -0.0401 20  ILE B O   
4336  C CB  . ILE B  20  ? 1.1094 0.8090 0.8566 -0.4829 0.2441  -0.0471 20  ILE B CB  
4337  C CG1 . ILE B  20  ? 1.1013 0.8266 0.8671 -0.4920 0.2508  -0.0559 20  ILE B CG1 
4338  C CG2 . ILE B  20  ? 1.0941 0.8008 0.8437 -0.4692 0.2396  -0.0459 20  ILE B CG2 
4339  C CD1 . ILE B  20  ? 1.0185 0.7707 0.8079 -0.4827 0.2473  -0.0619 20  ILE B CD1 
4340  N N   . ARG B  21  ? 1.3831 1.0783 1.1069 -0.5145 0.2660  -0.0477 21  ARG B N   
4341  C CA  . ARG B  21  ? 1.3509 1.0579 1.0725 -0.5230 0.2751  -0.0509 21  ARG B CA  
4342  C C   . ARG B  21  ? 1.2505 0.9896 0.9964 -0.5187 0.2768  -0.0600 21  ARG B C   
4343  O O   . ARG B  21  ? 1.1885 0.9443 0.9544 -0.5190 0.2759  -0.0660 21  ARG B O   
4344  C CB  . ARG B  21  ? 1.4764 1.1779 1.1902 -0.5411 0.2841  -0.0517 21  ARG B CB  
4345  C CG  . ARG B  21  ? 1.5356 1.2189 1.2245 -0.5495 0.2894  -0.0455 21  ARG B CG  
4346  C CD  . ARG B  21  ? 1.5937 1.2724 1.2755 -0.5682 0.2986  -0.0464 21  ARG B CD  
4347  N NE  . ARG B  21  ? 1.5851 1.2901 1.2803 -0.5774 0.3081  -0.0557 21  ARG B NE  
4348  C CZ  . ARG B  21  ? 1.5855 1.2941 1.2708 -0.5860 0.3164  -0.0565 21  ARG B CZ  
4349  N NH1 . ARG B  21  ? 1.5969 1.2840 1.2579 -0.5867 0.3160  -0.0480 21  ARG B NH1 
4350  N NH2 . ARG B  21  ? 1.5799 1.3139 1.2796 -0.5940 0.3250  -0.0659 21  ARG B NH2 
4351  N N   . LEU B  22  ? 1.2011 0.9484 0.9455 -0.5148 0.2790  -0.0607 22  LEU B N   
4352  C CA  . LEU B  22  ? 1.1811 0.9576 0.9483 -0.5094 0.2800  -0.0687 22  LEU B CA  
4353  C C   . LEU B  22  ? 1.1830 0.9733 0.9501 -0.5183 0.2902  -0.0737 22  LEU B C   
4354  O O   . LEU B  22  ? 1.1809 0.9566 0.9270 -0.5244 0.2946  -0.0694 22  LEU B O   
4355  C CB  . LEU B  22  ? 1.1996 0.9771 0.9706 -0.4923 0.2714  -0.0660 22  LEU B CB  
4356  C CG  . LEU B  22  ? 1.1444 0.9170 0.9221 -0.4795 0.2605  -0.0631 22  LEU B CG  
4357  C CD1 . LEU B  22  ? 1.0962 0.8729 0.8766 -0.4652 0.2550  -0.0614 22  LEU B CD1 
4358  C CD2 . LEU B  22  ? 1.1077 0.9000 0.9094 -0.4801 0.2591  -0.0697 22  LEU B CD2 
4359  N N   . LYS B  23  ? 1.1620 0.9809 0.9532 -0.5186 0.2934  -0.0827 23  LYS B N   
4360  C CA  . LYS B  23  ? 1.2236 1.0593 1.0188 -0.5269 0.3034  -0.0892 23  LYS B CA  
4361  C C   . LYS B  23  ? 1.1824 1.0298 0.9833 -0.5167 0.3024  -0.0910 23  LYS B C   
4362  O O   . LYS B  23  ? 1.1203 0.9863 0.9427 -0.5068 0.2981  -0.0956 23  LYS B O   
4363  C CB  . LYS B  23  ? 1.5218 1.3829 1.3404 -0.5352 0.3091  -0.0990 23  LYS B CB  
4364  C CG  . LYS B  23  ? 1.5278 1.4083 1.3738 -0.5245 0.3016  -0.1033 23  LYS B CG  
4365  C CD  . LYS B  23  ? 1.5348 1.4471 1.4063 -0.5294 0.3081  -0.1147 23  LYS B CD  
4366  C CE  . LYS B  23  ? 1.4983 1.4298 1.3911 -0.5156 0.3022  -0.1183 23  LYS B CE  
4367  N NZ  . LYS B  23  ? 1.4682 1.3955 1.3695 -0.5031 0.2899  -0.1132 23  LYS B NZ  
4368  N N   . ALA B  24  ? 1.4485 1.2841 1.2286 -0.5205 0.3069  -0.0881 24  ALA B N   
4369  C CA  . ALA B  24  ? 1.4594 1.3083 1.2431 -0.5166 0.3101  -0.0930 24  ALA B CA  
4370  C C   . ALA B  24  ? 1.5229 1.3914 1.3133 -0.5311 0.3230  -0.1034 24  ALA B C   
4371  O O   . ALA B  24  ? 1.5832 1.4472 1.3661 -0.5449 0.3294  -0.1038 24  ALA B O   
4372  C CB  . ALA B  24  ? 1.2677 1.0944 1.0256 -0.5134 0.3082  -0.0849 24  ALA B CB  
4373  N N   . PRO B  25  ? 1.3685 1.2593 1.1741 -0.5282 0.3269  -0.1121 25  PRO B N   
4374  C CA  . PRO B  25  ? 1.3704 1.2813 1.1832 -0.5412 0.3395  -0.1230 25  PRO B CA  
4375  C C   . PRO B  25  ? 1.3907 1.2866 1.1766 -0.5568 0.3486  -0.1206 25  PRO B C   
4376  O O   . PRO B  25  ? 1.3843 1.2914 1.1739 -0.5708 0.3583  -0.1274 25  PRO B O   
4377  C CB  . PRO B  25  ? 1.2158 1.1432 1.0401 -0.5328 0.3402  -0.1293 25  PRO B CB  
4378  C CG  . PRO B  25  ? 1.1705 1.0991 1.0095 -0.5158 0.3280  -0.1255 25  PRO B CG  
4379  C CD  . PRO B  25  ? 1.1872 1.0880 1.0081 -0.5121 0.3194  -0.1131 25  PRO B CD  
4380  N N   . GLY B  26  ? 1.4791 1.3503 1.2388 -0.5544 0.3453  -0.1109 26  GLY B N   
4381  C CA  . GLY B  26  ? 1.5335 1.3899 1.2666 -0.5685 0.3532  -0.1078 26  GLY B CA  
4382  C C   . GLY B  26  ? 1.5589 1.3864 1.2690 -0.5742 0.3501  -0.0962 26  GLY B C   
4383  O O   . GLY B  26  ? 1.6073 1.4198 1.2932 -0.5853 0.3557  -0.0919 26  GLY B O   
4384  N N   . GLY B  27  ? 1.3816 1.2012 1.0992 -0.5670 0.3415  -0.0913 27  GLY B N   
4385  C CA  . GLY B  27  ? 1.4082 1.2005 1.1061 -0.5716 0.3381  -0.0807 27  GLY B CA  
4386  C C   . GLY B  27  ? 1.4029 1.1887 1.1119 -0.5614 0.3277  -0.0763 27  GLY B C   
4387  O O   . GLY B  27  ? 1.3542 1.1597 1.0882 -0.5536 0.3244  -0.0826 27  GLY B O   
4388  N N   . PRO B  28  ? 1.6383 1.3965 1.3281 -0.5635 0.3234  -0.0667 28  PRO B N   
4389  C CA  . PRO B  28  ? 1.6279 1.3762 1.3236 -0.5525 0.3128  -0.0625 28  PRO B CA  
4390  C C   . PRO B  28  ? 1.6312 1.3615 1.3144 -0.5383 0.3032  -0.0542 28  PRO B C   
4391  O O   . PRO B  28  ? 1.6518 1.3714 1.3168 -0.5389 0.3045  -0.0497 28  PRO B O   
4392  C CB  . PRO B  28  ? 1.4689 1.1977 1.1514 -0.5645 0.3147  -0.0578 28  PRO B CB  
4393  C CG  . PRO B  28  ? 1.5077 1.2249 1.1669 -0.5784 0.3233  -0.0544 28  PRO B CG  
4394  C CD  . PRO B  28  ? 1.5042 1.2390 1.1665 -0.5765 0.3280  -0.0595 28  PRO B CD  
4395  N N   . VAL B  29  ? 1.3939 1.1190 1.0851 -0.5267 0.2936  -0.0517 29  VAL B N   
4396  C CA  . VAL B  29  ? 1.3466 1.0528 1.0259 -0.5136 0.2839  -0.0435 29  VAL B CA  
4397  C C   . VAL B  29  ? 1.3097 1.0002 0.9887 -0.5089 0.2761  -0.0389 29  VAL B C   
4398  O O   . VAL B  29  ? 1.2483 0.9504 0.9448 -0.5091 0.2752  -0.0439 29  VAL B O   
4399  C CB  . VAL B  29  ? 1.3731 1.0948 1.0664 -0.4985 0.2788  -0.0464 29  VAL B CB  
4400  C CG1 . VAL B  29  ? 1.3637 1.0965 1.0537 -0.5014 0.2854  -0.0496 29  VAL B CG1 
4401  C CG2 . VAL B  29  ? 1.3478 1.0927 1.0691 -0.4927 0.2764  -0.0539 29  VAL B CG2 
4402  N N   . SER B  30  ? 1.6290 1.2932 1.2881 -0.5048 0.2704  -0.0296 30  SER B N   
4403  C CA  . SER B  30  ? 1.6746 1.3219 1.3321 -0.4983 0.2621  -0.0247 30  SER B CA  
4404  C C   . SER B  30  ? 1.6333 1.2871 1.3015 -0.4807 0.2531  -0.0249 30  SER B C   
4405  O O   . SER B  30  ? 1.6528 1.3001 1.3116 -0.4728 0.2498  -0.0209 30  SER B O   
4406  C CB  . SER B  30  ? 1.5330 1.1489 1.1647 -0.5020 0.2600  -0.0144 30  SER B CB  
4407  O OG  . SER B  30  ? 1.5713 1.1803 1.1902 -0.5186 0.2687  -0.0132 30  SER B OG  
4408  N N   . ALA B  31  ? 1.3125 0.9794 1.0005 -0.4751 0.2494  -0.0297 31  ALA B N   
4409  C CA  . ALA B  31  ? 1.1754 0.8508 0.8758 -0.4593 0.2412  -0.0306 31  ALA B CA  
4410  C C   . ALA B  31  ? 1.1824 0.8410 0.8801 -0.4530 0.2331  -0.0263 31  ALA B C   
4411  O O   . ALA B  31  ? 1.1974 0.8552 0.9005 -0.4592 0.2339  -0.0282 31  ALA B O   
4412  C CB  . ALA B  31  ? 1.0211 0.7261 0.7471 -0.4577 0.2428  -0.0395 31  ALA B CB  
4413  N N   . PHE B  32  ? 1.2888 0.9345 0.9786 -0.4411 0.2255  -0.0207 32  PHE B N   
4414  C CA  . PHE B  32  ? 1.3187 0.9499 1.0075 -0.4338 0.2176  -0.0172 32  PHE B CA  
4415  C C   . PHE B  32  ? 1.2548 0.8981 0.9574 -0.4186 0.2101  -0.0192 32  PHE B C   
4416  O O   . PHE B  32  ? 1.2711 0.9112 0.9684 -0.4093 0.2064  -0.0160 32  PHE B O   
4417  C CB  . PHE B  32  ? 1.4129 1.0150 1.0793 -0.4334 0.2146  -0.0082 32  PHE B CB  
4418  C CG  . PHE B  32  ? 1.4747 1.0637 1.1247 -0.4479 0.2217  -0.0049 32  PHE B CG  
4419  C CD1 . PHE B  32  ? 1.4880 1.0786 1.1276 -0.4522 0.2267  -0.0036 32  PHE B CD1 
4420  C CD2 . PHE B  32  ? 1.5147 1.0895 1.1596 -0.4576 0.2234  -0.0031 32  PHE B CD2 
4421  C CE1 . PHE B  32  ? 1.5448 1.1236 1.1687 -0.4661 0.2334  -0.0004 32  PHE B CE1 
4422  C CE2 . PHE B  32  ? 1.5597 1.1221 1.1894 -0.4714 0.2300  0.0004  32  PHE B CE2 
4423  C CZ  . PHE B  32  ? 1.5816 1.1460 1.2004 -0.4758 0.2350  0.0019  32  PHE B CZ  
4424  N N   . LEU B  33  ? 1.1165 0.7730 0.8364 -0.4162 0.2077  -0.0240 33  LEU B N   
4425  C CA  . LEU B  33  ? 1.0466 0.7189 0.7821 -0.4034 0.2016  -0.0267 33  LEU B CA  
4426  C C   . LEU B  33  ? 1.0438 0.7075 0.7818 -0.3950 0.1936  -0.0250 33  LEU B C   
4427  O O   . LEU B  33  ? 1.0867 0.7484 0.8290 -0.4000 0.1934  -0.0269 33  LEU B O   
4428  C CB  . LEU B  33  ? 0.9248 0.6251 0.6816 -0.4065 0.2052  -0.0345 33  LEU B CB  
4429  C CG  . LEU B  33  ? 0.9365 0.6486 0.6945 -0.4170 0.2144  -0.0381 33  LEU B CG  
4430  C CD1 . LEU B  33  ? 0.9156 0.6564 0.6976 -0.4178 0.2164  -0.0458 33  LEU B CD1 
4431  C CD2 . LEU B  33  ? 0.9385 0.6458 0.6847 -0.4140 0.2160  -0.0349 33  LEU B CD2 
4432  N N   . GLY B  34  ? 0.9144 0.5738 0.6503 -0.3822 0.1869  -0.0218 34  GLY B N   
4433  C CA  . GLY B  34  ? 0.9019 0.5565 0.6422 -0.3739 0.1796  -0.0212 34  GLY B CA  
4434  C C   . GLY B  34  ? 0.9232 0.5510 0.6471 -0.3732 0.1765  -0.0153 34  GLY B C   
4435  O O   . GLY B  34  ? 0.9231 0.5438 0.6493 -0.3708 0.1723  -0.0154 34  GLY B O   
4436  N N   . ILE B  35  ? 0.9426 0.5552 0.6499 -0.3755 0.1785  -0.0101 35  ILE B N   
4437  C CA  . ILE B  35  ? 1.0071 0.5938 0.6989 -0.3731 0.1745  -0.0034 35  ILE B CA  
4438  C C   . ILE B  35  ? 0.9499 0.5355 0.6452 -0.3585 0.1663  -0.0020 35  ILE B C   
4439  O O   . ILE B  35  ? 0.9196 0.5136 0.6165 -0.3505 0.1645  -0.0017 35  ILE B O   
4440  C CB  . ILE B  35  ? 0.9836 0.5564 0.6573 -0.3769 0.1773  0.0023  35  ILE B CB  
4441  C CG1 . ILE B  35  ? 1.0046 0.5820 0.6752 -0.3916 0.1864  0.0004  35  ILE B CG1 
4442  C CG2 . ILE B  35  ? 1.0046 0.5499 0.6631 -0.3742 0.1724  0.0097  35  ILE B CG2 
4443  C CD1 . ILE B  35  ? 1.0221 0.5915 0.6767 -0.3956 0.1900  0.0048  35  ILE B CD1 
4444  N N   . PRO B  36  ? 0.9391 0.5153 0.6366 -0.3550 0.1616  -0.0017 36  PRO B N   
4445  C CA  . PRO B  36  ? 1.1172 0.6912 0.8171 -0.3414 0.1540  -0.0002 36  PRO B CA  
4446  C C   . PRO B  36  ? 1.0882 0.6445 0.7730 -0.3359 0.1509  0.0066  36  PRO B C   
4447  O O   . PRO B  36  ? 1.1011 0.6361 0.7726 -0.3411 0.1514  0.0115  36  PRO B O   
4448  C CB  . PRO B  36  ? 1.0245 0.5891 0.7279 -0.3417 0.1508  -0.0013 36  PRO B CB  
4449  C CG  . PRO B  36  ? 1.0771 0.6302 0.7737 -0.3551 0.1561  -0.0005 36  PRO B CG  
4450  C CD  . PRO B  36  ? 0.9571 0.5256 0.6561 -0.3634 0.1630  -0.0033 36  PRO B CD  
4451  N N   . PHE B  37  ? 0.9662 0.5307 0.6530 -0.3258 0.1477  0.0071  37  PHE B N   
4452  C CA  . PHE B  37  ? 0.9463 0.4945 0.6199 -0.3193 0.1437  0.0134  37  PHE B CA  
4453  C C   . PHE B  37  ? 0.9058 0.4482 0.5824 -0.3069 0.1358  0.0147  37  PHE B C   
4454  O O   . PHE B  37  ? 0.9088 0.4364 0.5751 -0.3014 0.1318  0.0200  37  PHE B O   
4455  C CB  . PHE B  37  ? 0.9087 0.4648 0.5778 -0.3183 0.1461  0.0143  37  PHE B CB  
4456  C CG  . PHE B  37  ? 0.9158 0.4944 0.5993 -0.3101 0.1447  0.0098  37  PHE B CG  
4457  C CD1 . PHE B  37  ? 0.9039 0.5037 0.6007 -0.3147 0.1493  0.0040  37  PHE B CD1 
4458  C CD2 . PHE B  37  ? 0.8559 0.4345 0.5402 -0.2978 0.1386  0.0115  37  PHE B CD2 
4459  C CE1 . PHE B  37  ? 0.8304 0.4502 0.5409 -0.3072 0.1476  0.0004  37  PHE B CE1 
4460  C CE2 . PHE B  37  ? 0.8254 0.4240 0.5230 -0.2906 0.1373  0.0078  37  PHE B CE2 
4461  C CZ  . PHE B  37  ? 1.1068 0.7257 0.8176 -0.2953 0.1417  0.0024  37  PHE B CZ  
4462  N N   . ALA B  38  ? 1.0010 0.5553 0.6917 -0.3029 0.1336  0.0100  38  ALA B N   
4463  C CA  . ALA B  38  ? 0.9608 0.5113 0.6558 -0.2919 0.1266  0.0103  38  ALA B CA  
4464  C C   . ALA B  38  ? 0.9713 0.5280 0.6780 -0.2932 0.1258  0.0055  38  ALA B C   
4465  O O   . ALA B  38  ? 0.9723 0.5441 0.6879 -0.2994 0.1297  0.0009  38  ALA B O   
4466  C CB  . ALA B  38  ? 0.8381 0.4027 0.5390 -0.2812 0.1234  0.0096  38  ALA B CB  
4467  N N   . GLU B  39  ? 1.0063 0.5514 0.7132 -0.2875 0.1208  0.0064  39  GLU B N   
4468  C CA  . GLU B  39  ? 0.9941 0.5455 0.7123 -0.2876 0.1195  0.0014  39  GLU B CA  
4469  C C   . GLU B  39  ? 0.9954 0.5702 0.7261 -0.2809 0.1179  -0.0026 39  GLU B C   
4470  O O   . GLU B  39  ? 0.9984 0.5771 0.7287 -0.2719 0.1148  -0.0007 39  GLU B O   
4471  C CB  . GLU B  39  ? 0.8631 0.3970 0.5795 -0.2827 0.1145  0.0029  39  GLU B CB  
4472  C CG  . GLU B  39  ? 0.8976 0.4086 0.6053 -0.2908 0.1159  0.0058  39  GLU B CG  
4473  C CD  . GLU B  39  ? 1.3114 0.8254 1.0241 -0.3021 0.1203  0.0014  39  GLU B CD  
4474  O OE1 . GLU B  39  ? 1.2951 0.8284 1.0189 -0.3033 0.1217  -0.0042 39  GLU B OE1 
4475  O OE2 . GLU B  39  ? 1.3276 0.8243 1.0333 -0.3102 0.1223  0.0038  39  GLU B OE2 
4476  N N   . PRO B  40  ? 0.9977 0.5880 0.7395 -0.2856 0.1199  -0.0079 40  PRO B N   
4477  C CA  . PRO B  40  ? 0.9801 0.5936 0.7344 -0.2811 0.1189  -0.0114 40  PRO B CA  
4478  C C   . PRO B  40  ? 1.0164 0.6321 0.7743 -0.2693 0.1129  -0.0109 40  PRO B C   
4479  O O   . PRO B  40  ? 1.0482 0.6553 0.8064 -0.2669 0.1099  -0.0117 40  PRO B O   
4480  C CB  . PRO B  40  ? 0.9259 0.5495 0.6900 -0.2882 0.1206  -0.0167 40  PRO B CB  
4481  C CG  . PRO B  40  ? 0.9835 0.5939 0.7401 -0.2990 0.1251  -0.0161 40  PRO B CG  
4482  C CD  . PRO B  40  ? 1.0078 0.5945 0.7511 -0.2962 0.1233  -0.0107 40  PRO B CD  
4483  N N   . PRO B  41  ? 0.9981 0.6253 0.7591 -0.2622 0.1114  -0.0099 41  PRO B N   
4484  C CA  . PRO B  41  ? 0.9325 0.5636 0.6974 -0.2509 0.1059  -0.0093 41  PRO B CA  
4485  C C   . PRO B  41  ? 0.9257 0.5747 0.7042 -0.2497 0.1042  -0.0138 41  PRO B C   
4486  O O   . PRO B  41  ? 0.9537 0.6191 0.7406 -0.2456 0.1030  -0.0145 41  PRO B O   
4487  C CB  . PRO B  41  ? 0.7088 0.3467 0.4724 -0.2465 0.1063  -0.0069 41  PRO B CB  
4488  C CG  . PRO B  41  ? 0.7107 0.3602 0.4786 -0.2551 0.1115  -0.0090 41  PRO B CG  
4489  C CD  . PRO B  41  ? 0.7493 0.3878 0.5118 -0.2654 0.1152  -0.0098 41  PRO B CD  
4490  N N   . VAL B  42  ? 0.7074 0.3530 0.4882 -0.2536 0.1039  -0.0167 42  VAL B N   
4491  C CA  . VAL B  42  ? 0.6902 0.3515 0.4827 -0.2529 0.1018  -0.0209 42  VAL B CA  
4492  C C   . VAL B  42  ? 0.6870 0.3410 0.4790 -0.2464 0.0975  -0.0214 42  VAL B C   
4493  O O   . VAL B  42  ? 0.6988 0.3359 0.4825 -0.2430 0.0963  -0.0186 42  VAL B O   
4494  C CB  . VAL B  42  ? 0.7013 0.3667 0.4979 -0.2635 0.1051  -0.0248 42  VAL B CB  
4495  C CG1 . VAL B  42  ? 0.7102 0.3791 0.5057 -0.2709 0.1101  -0.0242 42  VAL B CG1 
4496  C CG2 . VAL B  42  ? 0.7233 0.3708 0.5135 -0.2674 0.1054  -0.0256 42  VAL B CG2 
4497  N N   . GLY B  43  ? 0.6718 0.3385 0.4728 -0.2450 0.0951  -0.0249 43  GLY B N   
4498  C CA  . GLY B  43  ? 0.6959 0.3571 0.4972 -0.2395 0.0914  -0.0261 43  GLY B CA  
4499  C C   . GLY B  43  ? 0.6611 0.3154 0.4582 -0.2293 0.0881  -0.0225 43  GLY B C   
4500  O O   . GLY B  43  ? 0.6438 0.3081 0.4436 -0.2236 0.0868  -0.0204 43  GLY B O   
4501  N N   . SER B  44  ? 0.6747 0.3120 0.4663 -0.2269 0.0867  -0.0219 44  SER B N   
4502  C CA  . SER B  44  ? 0.6913 0.3207 0.4794 -0.2175 0.0834  -0.0186 44  SER B CA  
4503  C C   . SER B  44  ? 0.6859 0.3093 0.4664 -0.2160 0.0845  -0.0136 44  SER B C   
4504  O O   . SER B  44  ? 0.6674 0.2887 0.4457 -0.2080 0.0817  -0.0107 44  SER B O   
4505  C CB  . SER B  44  ? 0.8838 0.4958 0.6692 -0.2161 0.0815  -0.0195 44  SER B CB  
4506  O OG  . SER B  44  ? 0.9366 0.5321 0.7152 -0.2228 0.0840  -0.0183 44  SER B OG  
4507  N N   . ARG B  45  ? 0.7977 0.4191 0.5743 -0.2241 0.0886  -0.0129 45  ARG B N   
4508  C CA  . ARG B  45  ? 0.8742 0.4896 0.6426 -0.2242 0.0902  -0.0085 45  ARG B CA  
4509  C C   . ARG B  45  ? 0.8450 0.4783 0.6183 -0.2225 0.0912  -0.0084 45  ARG B C   
4510  O O   . ARG B  45  ? 0.8881 0.5192 0.6557 -0.2234 0.0932  -0.0055 45  ARG B O   
4511  C CB  . ARG B  45  ? 1.1636 0.7662 0.9243 -0.2341 0.0944  -0.0076 45  ARG B CB  
4512  C CG  . ARG B  45  ? 1.2830 0.8635 1.0319 -0.2328 0.0934  -0.0027 45  ARG B CG  
4513  C CD  . ARG B  45  ? 1.3430 0.9241 1.0864 -0.2268 0.0922  0.0014  45  ARG B CD  
4514  N NE  . ARG B  45  ? 1.3718 0.9336 1.1057 -0.2225 0.0891  0.0061  45  ARG B NE  
4515  C CZ  . ARG B  45  ? 1.3683 0.9239 1.1044 -0.2144 0.0842  0.0065  45  ARG B CZ  
4516  N NH1 . ARG B  45  ? 1.3390 0.9057 1.0856 -0.2101 0.0822  0.0024  45  ARG B NH1 
4517  N NH2 . ARG B  45  ? 1.3873 0.9252 1.1152 -0.2109 0.0813  0.0109  45  ARG B NH2 
4518  N N   . ARG B  46  ? 0.7634 0.4144 0.5479 -0.2204 0.0898  -0.0114 46  ARG B N   
4519  C CA  . ARG B  46  ? 0.6952 0.3633 0.4865 -0.2183 0.0900  -0.0113 46  ARG B CA  
4520  C C   . ARG B  46  ? 0.6761 0.3437 0.4658 -0.2082 0.0866  -0.0083 46  ARG B C   
4521  O O   . ARG B  46  ? 0.7036 0.3658 0.4927 -0.2020 0.0829  -0.0080 46  ARG B O   
4522  C CB  . ARG B  46  ? 0.6183 0.3045 0.4223 -0.2193 0.0889  -0.0150 46  ARG B CB  
4523  C CG  . ARG B  46  ? 0.5966 0.3004 0.4098 -0.2157 0.0879  -0.0145 46  ARG B CG  
4524  C CD  . ARG B  46  ? 0.5780 0.2973 0.4029 -0.2138 0.0846  -0.0170 46  ARG B CD  
4525  N NE  . ARG B  46  ? 0.5783 0.3094 0.4114 -0.2218 0.0866  -0.0199 46  ARG B NE  
4526  C CZ  . ARG B  46  ? 0.5679 0.3109 0.4101 -0.2228 0.0840  -0.0223 46  ARG B CZ  
4527  N NH1 . ARG B  46  ? 0.5568 0.3011 0.4003 -0.2166 0.0799  -0.0224 46  ARG B NH1 
4528  N NH2 . ARG B  46  ? 0.5693 0.3231 0.4191 -0.2302 0.0856  -0.0248 46  ARG B NH2 
4529  N N   . PHE B  47  ? 0.6514 0.3248 0.4410 -0.2070 0.0878  -0.0065 47  PHE B N   
4530  C CA  . PHE B  47  ? 0.6292 0.3025 0.4172 -0.1981 0.0850  -0.0037 47  PHE B CA  
4531  C C   . PHE B  47  ? 0.6646 0.3187 0.4392 -0.1963 0.0846  -0.0001 47  PHE B C   
4532  O O   . PHE B  47  ? 0.6821 0.3343 0.4540 -0.1893 0.0821  0.0023  47  PHE B O   
4533  C CB  . PHE B  47  ? 0.5840 0.2657 0.3800 -0.1898 0.0801  -0.0045 47  PHE B CB  
4534  C CG  . PHE B  47  ? 0.5651 0.2659 0.3743 -0.1905 0.0795  -0.0071 47  PHE B CG  
4535  C CD1 . PHE B  47  ? 0.5551 0.2687 0.3711 -0.1920 0.0811  -0.0071 47  PHE B CD1 
4536  C CD2 . PHE B  47  ? 0.5582 0.2639 0.3732 -0.1900 0.0771  -0.0096 47  PHE B CD2 
4537  C CE1 . PHE B  47  ? 0.7755 0.5063 0.6047 -0.1926 0.0799  -0.0090 47  PHE B CE1 
4538  C CE2 . PHE B  47  ? 0.5421 0.2649 0.3689 -0.1910 0.0760  -0.0115 47  PHE B CE2 
4539  C CZ  . PHE B  47  ? 0.5323 0.2675 0.3665 -0.1921 0.0771  -0.0110 47  PHE B CZ  
4540  N N   . MET B  48  ? 0.7476 0.3873 0.5141 -0.2028 0.0867  0.0004  48  MET B N   
4541  C CA  . MET B  48  ? 0.7651 0.3849 0.5196 -0.2010 0.0853  0.0041  48  MET B CA  
4542  C C   . MET B  48  ? 0.8222 0.4334 0.5663 -0.2076 0.0892  0.0067  48  MET B C   
4543  O O   . MET B  48  ? 0.8548 0.4723 0.6005 -0.2157 0.0938  0.0050  48  MET B O   
4544  C CB  . MET B  48  ? 0.6805 0.2874 0.4335 -0.2029 0.0841  0.0033  48  MET B CB  
4545  C CG  . MET B  48  ? 0.6642 0.2785 0.4268 -0.1974 0.0806  0.0002  48  MET B CG  
4546  S SD  . MET B  48  ? 0.8878 0.4878 0.6477 -0.1883 0.0752  0.0022  48  MET B SD  
4547  C CE  . MET B  48  ? 0.6656 0.2626 0.4181 -0.1825 0.0737  0.0070  48  MET B CE  
4548  N N   . PRO B  49  ? 0.7426 0.3394 0.4759 -0.2045 0.0874  0.0110  49  PRO B N   
4549  C CA  . PRO B  49  ? 0.7487 0.3348 0.4697 -0.2110 0.0908  0.0142  49  PRO B CA  
4550  C C   . PRO B  49  ? 0.7824 0.3592 0.4997 -0.2209 0.0943  0.0138  49  PRO B C   
4551  O O   . PRO B  49  ? 0.8188 0.3882 0.5383 -0.2208 0.0924  0.0129  49  PRO B O   
4552  C CB  . PRO B  49  ? 0.7597 0.3289 0.4707 -0.2051 0.0865  0.0189  49  PRO B CB  
4553  C CG  . PRO B  49  ? 0.7289 0.3065 0.4487 -0.1943 0.0814  0.0177  49  PRO B CG  
4554  C CD  . PRO B  49  ? 0.6982 0.2880 0.4304 -0.1948 0.0818  0.0131  49  PRO B CD  
4555  N N   . PRO B  50  ? 0.8838 0.4615 0.5962 -0.2298 0.0997  0.0140  50  PRO B N   
4556  C CA  . PRO B  50  ? 0.9596 0.5296 0.6690 -0.2402 0.1036  0.0134  50  PRO B CA  
4557  C C   . PRO B  50  ? 1.0785 0.6239 0.7757 -0.2418 0.1017  0.0181  50  PRO B C   
4558  O O   . PRO B  50  ? 1.1456 0.6800 0.8322 -0.2395 0.1001  0.0227  50  PRO B O   
4559  C CB  . PRO B  50  ? 0.7804 0.3574 0.4866 -0.2484 0.1096  0.0130  50  PRO B CB  
4560  C CG  . PRO B  50  ? 0.7731 0.3513 0.4742 -0.2426 0.1083  0.0156  50  PRO B CG  
4561  C CD  . PRO B  50  ? 0.7481 0.3341 0.4580 -0.2310 0.1026  0.0146  50  PRO B CD  
4562  N N   . GLU B  51  ? 0.9757 0.5127 0.6750 -0.2455 0.1014  0.0169  51  GLU B N   
4563  C CA  . GLU B  51  ? 1.0047 0.5180 0.6933 -0.2497 0.1007  0.0212  51  GLU B CA  
4564  C C   . GLU B  51  ? 0.9892 0.4992 0.6718 -0.2626 0.1071  0.0215  51  GLU B C   
4565  O O   . GLU B  51  ? 0.9606 0.4863 0.6510 -0.2680 0.1113  0.0168  51  GLU B O   
4566  C CB  . GLU B  51  ? 1.2191 0.7244 0.9141 -0.2475 0.0974  0.0193  51  GLU B CB  
4567  C CG  . GLU B  51  ? 1.2795 0.7886 0.9818 -0.2356 0.0915  0.0182  51  GLU B CG  
4568  C CD  . GLU B  51  ? 1.3650 0.8708 1.0761 -0.2349 0.0895  0.0145  51  GLU B CD  
4569  O OE1 . GLU B  51  ? 1.3659 0.8829 1.0846 -0.2402 0.0926  0.0096  51  GLU B OE1 
4570  O OE2 . GLU B  51  ? 1.4140 0.9062 1.1250 -0.2291 0.0848  0.0162  51  GLU B OE2 
4571  N N   . PRO B  52  ? 1.1767 0.6667 0.8458 -0.2677 0.1076  0.0270  52  PRO B N   
4572  C CA  . PRO B  52  ? 1.2062 0.6942 0.8688 -0.2804 0.1142  0.0275  52  PRO B CA  
4573  C C   . PRO B  52  ? 1.2423 0.7298 0.9115 -0.2882 0.1170  0.0238  52  PRO B C   
4574  O O   . PRO B  52  ? 1.2555 0.7376 0.9310 -0.2843 0.1132  0.0223  52  PRO B O   
4575  C CB  . PRO B  52  ? 0.9878 0.4525 0.6337 -0.2831 0.1131  0.0351  52  PRO B CB  
4576  C CG  . PRO B  52  ? 0.9763 0.4351 0.6205 -0.2708 0.1060  0.0383  52  PRO B CG  
4577  C CD  . PRO B  52  ? 0.9529 0.4219 0.6120 -0.2626 0.1025  0.0332  52  PRO B CD  
4578  N N   . LYS B  53  ? 1.0784 0.5720 0.7467 -0.2993 0.1235  0.0220  53  LYS B N   
4579  C CA  . LYS B  53  ? 1.0536 0.5477 0.7281 -0.3078 0.1265  0.0182  53  LYS B CA  
4580  C C   . LYS B  53  ? 1.0992 0.5679 0.7665 -0.3101 0.1240  0.0224  53  LYS B C   
4581  O O   . LYS B  53  ? 1.1218 0.5727 0.7759 -0.3120 0.1234  0.0288  53  LYS B O   
4582  C CB  . LYS B  53  ? 1.0419 0.5441 0.7144 -0.3200 0.1342  0.0165  53  LYS B CB  
4583  C CG  . LYS B  53  ? 1.0625 0.5641 0.7403 -0.3303 0.1379  0.0129  53  LYS B CG  
4584  C CD  . LYS B  53  ? 1.0597 0.5801 0.7541 -0.3270 0.1366  0.0058  53  LYS B CD  
4585  C CE  . LYS B  53  ? 1.0686 0.5889 0.7684 -0.3375 0.1401  0.0017  53  LYS B CE  
4586  N NZ  . LYS B  53  ? 1.0238 0.5654 0.7397 -0.3357 0.1396  -0.0054 53  LYS B NZ  
4587  N N   . ARG B  54  ? 1.2025 0.6691 0.8788 -0.3097 0.1220  0.0188  54  ARG B N   
4588  C CA  . ARG B  54  ? 1.3099 0.7524 0.9813 -0.3133 0.1202  0.0221  54  ARG B CA  
4589  C C   . ARG B  54  ? 1.3654 0.8033 1.0325 -0.3276 0.1265  0.0221  54  ARG B C   
4590  O O   . ARG B  54  ? 1.3604 0.8160 1.0346 -0.3337 0.1313  0.0166  54  ARG B O   
4591  C CB  . ARG B  54  ? 1.4350 0.8763 1.1179 -0.3079 0.1159  0.0178  54  ARG B CB  
4592  C CG  . ARG B  54  ? 1.4933 0.9120 1.1727 -0.3014 0.1098  0.0224  54  ARG B CG  
4593  C CD  . ARG B  54  ? 1.5389 0.9503 1.2280 -0.3017 0.1075  0.0181  54  ARG B CD  
4594  N NE  . ARG B  54  ? 1.5181 0.9483 1.2202 -0.2947 0.1056  0.0113  54  ARG B NE  
4595  C CZ  . ARG B  54  ? 1.5282 0.9586 1.2403 -0.2956 0.1046  0.0056  54  ARG B CZ  
4596  N NH1 . ARG B  54  ? 1.5745 0.9875 1.2861 -0.3030 0.1053  0.0057  54  ARG B NH1 
4597  N NH2 . ARG B  54  ? 1.4858 0.9336 1.2084 -0.2895 0.1030  -0.0001 54  ARG B NH2 
4598  N N   . PRO B  55  ? 1.4035 0.8175 1.0591 -0.3333 0.1265  0.0283  55  PRO B N   
4599  C CA  . PRO B  55  ? 1.3897 0.7985 1.0383 -0.3475 0.1330  0.0297  55  PRO B CA  
4600  C C   . PRO B  55  ? 1.3396 0.7536 0.9987 -0.3552 0.1360  0.0234  55  PRO B C   
4601  O O   . PRO B  55  ? 1.2977 0.7135 0.9676 -0.3496 0.1323  0.0192  55  PRO B O   
4602  C CB  . PRO B  55  ? 1.3791 0.7586 1.0143 -0.3497 0.1304  0.0383  55  PRO B CB  
4603  C CG  . PRO B  55  ? 1.3745 0.7434 1.0154 -0.3385 0.1226  0.0389  55  PRO B CG  
4604  C CD  . PRO B  55  ? 1.3548 0.7452 1.0045 -0.3271 0.1202  0.0344  55  PRO B CD  
4605  N N   . TRP B  56  ? 1.3657 0.7826 1.0221 -0.3679 0.1428  0.0224  56  TRP B N   
4606  C CA  . TRP B  56  ? 1.3812 0.8032 1.0475 -0.3762 0.1459  0.0163  56  TRP B CA  
4607  C C   . TRP B  56  ? 1.4528 0.8578 1.1110 -0.3902 0.1504  0.0195  56  TRP B C   
4608  O O   . TRP B  56  ? 1.4755 0.8709 1.1205 -0.3958 0.1533  0.0255  56  TRP B O   
4609  C CB  . TRP B  56  ? 1.2643 0.7156 0.9414 -0.3780 0.1501  0.0089  56  TRP B CB  
4610  C CG  . TRP B  56  ? 1.2482 0.7085 0.9187 -0.3857 0.1565  0.0101  56  TRP B CG  
4611  C CD1 . TRP B  56  ? 1.2633 0.7290 0.9345 -0.3989 0.1635  0.0076  56  TRP B CD1 
4612  C CD2 . TRP B  56  ? 1.2262 0.6914 0.8891 -0.3810 0.1568  0.0137  56  TRP B CD2 
4613  N NE1 . TRP B  56  ? 1.2549 0.7288 0.9194 -0.4028 0.1683  0.0092  56  TRP B NE1 
4614  C CE2 . TRP B  56  ? 1.2279 0.7016 0.8872 -0.3919 0.1643  0.0129  56  TRP B CE2 
4615  C CE3 . TRP B  56  ? 1.1985 0.6622 0.8577 -0.3687 0.1515  0.0171  56  TRP B CE3 
4616  C CZ2 . TRP B  56  ? 1.1985 0.6787 0.8504 -0.3911 0.1667  0.0153  56  TRP B CZ2 
4617  C CZ3 . TRP B  56  ? 1.1923 0.6623 0.8441 -0.3679 0.1537  0.0196  56  TRP B CZ3 
4618  C CH2 . TRP B  56  ? 1.1886 0.6667 0.8368 -0.3791 0.1613  0.0186  56  TRP B CH2 
4619  N N   . SER B  57  ? 1.4002 0.8013 1.0665 -0.3960 0.1510  0.0153  57  SER B N   
4620  C CA  . SER B  57  ? 1.4413 0.8314 1.1029 -0.4107 0.1564  0.0165  57  SER B CA  
4621  C C   . SER B  57  ? 1.3953 0.8096 1.0666 -0.4188 0.1627  0.0086  57  SER B C   
4622  O O   . SER B  57  ? 1.3491 0.7837 1.0331 -0.4133 0.1614  0.0017  57  SER B O   
4623  C CB  . SER B  57  ? 1.6016 0.9689 1.2655 -0.4130 0.1530  0.0173  57  SER B CB  
4624  O OG  . SER B  57  ? 1.6418 0.9916 1.2970 -0.4263 0.1573  0.0217  57  SER B OG  
4625  N N   . GLY B  58  ? 1.4824 0.8947 1.1476 -0.4321 0.1694  0.0098  58  GLY B N   
4626  C CA  . GLY B  58  ? 1.4764 0.9113 1.1506 -0.4408 0.1758  0.0027  58  GLY B CA  
4627  C C   . GLY B  58  ? 1.4607 0.9095 1.1292 -0.4435 0.1810  0.0039  58  GLY B C   
4628  O O   . GLY B  58  ? 1.4561 0.9011 1.1157 -0.4362 0.1787  0.0090  58  GLY B O   
4629  N N   . VAL B  59  ? 1.3659 0.8305 1.0398 -0.4544 0.1879  -0.0011 59  VAL B N   
4630  C CA  . VAL B  59  ? 1.3549 0.8346 1.0254 -0.4580 0.1936  -0.0013 59  VAL B CA  
4631  C C   . VAL B  59  ? 1.2998 0.8083 0.9851 -0.4498 0.1925  -0.0081 59  VAL B C   
4632  O O   . VAL B  59  ? 1.2697 0.7960 0.9690 -0.4537 0.1946  -0.0154 59  VAL B O   
4633  C CB  . VAL B  59  ? 1.4673 0.9497 1.1367 -0.4746 0.2021  -0.0033 59  VAL B CB  
4634  C CG1 . VAL B  59  ? 1.4612 0.9607 1.1284 -0.4783 0.2083  -0.0043 59  VAL B CG1 
4635  C CG2 . VAL B  59  ? 1.5223 0.9753 1.1772 -0.4836 0.2031  0.0039  59  VAL B CG2 
4636  N N   . LEU B  60  ? 1.2731 0.7858 0.9550 -0.4389 0.1893  -0.0055 60  LEU B N   
4637  C CA  . LEU B  60  ? 1.2279 0.7640 0.9231 -0.4284 0.1864  -0.0105 60  LEU B CA  
4638  C C   . LEU B  60  ? 1.1873 0.7470 0.8898 -0.4342 0.1927  -0.0152 60  LEU B C   
4639  O O   . LEU B  60  ? 1.1925 0.7491 0.8856 -0.4424 0.1986  -0.0128 60  LEU B O   
4640  C CB  . LEU B  60  ? 1.3537 0.8837 1.0419 -0.4151 0.1807  -0.0055 60  LEU B CB  
4641  C CG  . LEU B  60  ? 1.3372 0.8875 1.0382 -0.4025 0.1761  -0.0095 60  LEU B CG  
4642  C CD1 . LEU B  60  ? 1.3569 0.9122 1.0706 -0.3992 0.1720  -0.0143 60  LEU B CD1 
4643  C CD2 . LEU B  60  ? 1.2950 0.8363 0.9875 -0.3906 0.1708  -0.0040 60  LEU B CD2 
4644  N N   . ASP B  61  ? 1.0448 0.6284 0.7642 -0.4298 0.1916  -0.0218 61  ASP B N   
4645  C CA  . ASP B  61  ? 1.1217 0.7284 0.8506 -0.4357 0.1975  -0.0269 61  ASP B CA  
4646  C C   . ASP B  61  ? 1.0942 0.7116 0.8227 -0.4272 0.1968  -0.0257 61  ASP B C   
4647  O O   . ASP B  61  ? 1.0764 0.7041 0.8132 -0.4154 0.1913  -0.0268 61  ASP B O   
4648  C CB  . ASP B  61  ? 1.2844 0.9122 1.0329 -0.4363 0.1965  -0.0346 61  ASP B CB  
4649  C CG  . ASP B  61  ? 1.3346 0.9855 1.0944 -0.4444 0.2030  -0.0403 61  ASP B CG  
4650  O OD1 . ASP B  61  ? 1.3587 1.0256 1.1243 -0.4390 0.2034  -0.0415 61  ASP B OD1 
4651  O OD2 . ASP B  61  ? 1.3567 1.0100 1.1203 -0.4563 0.2078  -0.0438 61  ASP B OD2 
4652  N N   . ALA B  62  ? 1.1816 0.7958 0.8996 -0.4338 0.2027  -0.0233 62  ALA B N   
4653  C CA  . ALA B  62  ? 1.1177 0.7424 0.8349 -0.4282 0.2036  -0.0227 62  ALA B CA  
4654  C C   . ALA B  62  ? 1.0827 0.7339 0.8145 -0.4340 0.2097  -0.0297 62  ALA B C   
4655  O O   . ALA B  62  ? 1.0574 0.7182 0.7890 -0.4326 0.2126  -0.0301 62  ALA B O   
4656  C CB  . ALA B  62  ? 1.0953 0.7002 0.7915 -0.4312 0.2058  -0.0156 62  ALA B CB  
4657  N N   . THR B  63  ? 1.0066 0.6689 0.7511 -0.4411 0.2119  -0.0352 63  THR B N   
4658  C CA  . THR B  63  ? 1.0069 0.6926 0.7650 -0.4489 0.2184  -0.0418 63  THR B CA  
4659  C C   . THR B  63  ? 0.9913 0.7032 0.7695 -0.4400 0.2155  -0.0469 63  THR B C   
4660  O O   . THR B  63  ? 0.9682 0.7010 0.7597 -0.4454 0.2205  -0.0526 63  THR B O   
4661  C CB  . THR B  63  ? 1.0884 0.7761 0.8526 -0.4609 0.2221  -0.0459 63  THR B CB  
4662  O OG1 . THR B  63  ? 1.0474 0.7477 0.8284 -0.4555 0.2166  -0.0502 63  THR B OG1 
4663  C CG2 . THR B  63  ? 1.1166 0.7760 0.8627 -0.4674 0.2226  -0.0402 63  THR B CG2 
4664  N N   . THR B  64  ? 1.2387 0.9501 1.0202 -0.4265 0.2074  -0.0449 64  THR B N   
4665  C CA  . THR B  64  ? 1.2066 0.9418 1.0068 -0.4178 0.2042  -0.0489 64  THR B CA  
4666  C C   . THR B  64  ? 1.2213 0.9531 1.0193 -0.4030 0.1970  -0.0450 64  THR B C   
4667  O O   . THR B  64  ? 1.2480 0.9593 1.0319 -0.3978 0.1928  -0.0397 64  THR B O   
4668  C CB  . THR B  64  ? 0.8978 0.6487 0.7165 -0.4189 0.2015  -0.0543 64  THR B CB  
4669  O OG1 . THR B  64  ? 0.8696 0.6455 0.7077 -0.4129 0.1995  -0.0582 64  THR B OG1 
4670  C CG2 . THR B  64  ? 0.8935 0.6312 0.7086 -0.4123 0.1940  -0.0518 64  THR B CG2 
4671  N N   . PHE B  65  ? 1.0376 0.7898 0.8505 -0.3962 0.1954  -0.0478 65  PHE B N   
4672  C CA  . PHE B  65  ? 1.0050 0.7573 0.8186 -0.3822 0.1887  -0.0448 65  PHE B CA  
4673  C C   . PHE B  65  ? 0.9930 0.7417 0.8106 -0.3740 0.1805  -0.0437 65  PHE B C   
4674  O O   . PHE B  65  ? 0.9408 0.7015 0.7722 -0.3758 0.1786  -0.0476 65  PHE B O   
4675  C CB  . PHE B  65  ? 0.8400 0.6162 0.6710 -0.3778 0.1891  -0.0484 65  PHE B CB  
4676  C CG  . PHE B  65  ? 0.8207 0.5979 0.6452 -0.3805 0.1951  -0.0481 65  PHE B CG  
4677  C CD1 . PHE B  65  ? 0.8380 0.5942 0.6411 -0.3806 0.1964  -0.0428 65  PHE B CD1 
4678  C CD2 . PHE B  65  ? 0.8106 0.6101 0.6511 -0.3831 0.1994  -0.0533 65  PHE B CD2 
4679  C CE1 . PHE B  65  ? 0.8456 0.6030 0.6421 -0.3836 0.2021  -0.0428 65  PHE B CE1 
4680  C CE2 . PHE B  65  ? 0.8176 0.6189 0.6524 -0.3859 0.2054  -0.0537 65  PHE B CE2 
4681  C CZ  . PHE B  65  ? 0.8353 0.6153 0.6475 -0.3864 0.2068  -0.0484 65  PHE B CZ  
4682  N N   . GLN B  66  ? 1.1570 0.8900 0.9628 -0.3649 0.1756  -0.0386 66  GLN B N   
4683  C CA  . GLN B  66  ? 1.1606 0.8891 0.9686 -0.3564 0.1680  -0.0375 66  GLN B CA  
4684  C C   . GLN B  66  ? 1.1444 0.8918 0.9685 -0.3462 0.1626  -0.0390 66  GLN B C   
4685  O O   . GLN B  66  ? 1.1458 0.9112 0.9820 -0.3463 0.1647  -0.0416 66  GLN B O   
4686  C CB  . GLN B  66  ? 0.9606 0.6650 0.7505 -0.3508 0.1648  -0.0315 66  GLN B CB  
4687  C CG  . GLN B  66  ? 0.9908 0.6768 0.7714 -0.3561 0.1645  -0.0303 66  GLN B CG  
4688  C CD  . GLN B  66  ? 1.0165 0.7108 0.8093 -0.3554 0.1607  -0.0342 66  GLN B CD  
4689  O OE1 . GLN B  66  ? 1.0270 0.7319 0.8291 -0.3639 0.1637  -0.0387 66  GLN B OE1 
4690  N NE2 . GLN B  66  ? 1.0277 0.7174 0.8206 -0.3455 0.1540  -0.0327 66  GLN B NE2 
4691  N N   . ASN B  67  ? 1.0238 0.7664 0.8481 -0.3376 0.1557  -0.0374 67  ASN B N   
4692  C CA  . ASN B  67  ? 0.9535 0.7115 0.7917 -0.3278 0.1498  -0.0382 67  ASN B CA  
4693  C C   . ASN B  67  ? 0.9379 0.7003 0.7765 -0.3197 0.1489  -0.0358 67  ASN B C   
4694  O O   . ASN B  67  ? 0.9612 0.7101 0.7857 -0.3188 0.1511  -0.0325 67  ASN B O   
4695  C CB  . ASN B  67  ? 0.8628 0.6114 0.6974 -0.3209 0.1433  -0.0365 67  ASN B CB  
4696  C CG  . ASN B  67  ? 0.8568 0.6066 0.6960 -0.3272 0.1428  -0.0398 67  ASN B CG  
4697  O OD1 . ASN B  67  ? 0.8285 0.5960 0.6824 -0.3316 0.1432  -0.0439 67  ASN B OD1 
4698  N ND2 . ASN B  67  ? 0.8799 0.6108 0.7072 -0.3279 0.1416  -0.0383 67  ASN B ND2 
4699  N N   . VAL B  68  ? 0.7853 0.5665 0.6405 -0.3138 0.1452  -0.0374 68  VAL B N   
4700  C CA  . VAL B  68  ? 0.7567 0.5428 0.6146 -0.3047 0.1431  -0.0352 68  VAL B CA  
4701  C C   . VAL B  68  ? 0.7211 0.5008 0.5763 -0.2935 0.1356  -0.0321 68  VAL B C   
4702  O O   . VAL B  68  ? 0.6538 0.4361 0.5143 -0.2920 0.1313  -0.0330 68  VAL B O   
4703  C CB  . VAL B  68  ? 0.6574 0.4677 0.5360 -0.3047 0.1436  -0.0385 68  VAL B CB  
4704  C CG1 . VAL B  68  ? 0.6453 0.4621 0.5303 -0.2937 0.1391  -0.0363 68  VAL B CG1 
4705  C CG2 . VAL B  68  ? 0.6715 0.4870 0.5506 -0.3141 0.1517  -0.0412 68  VAL B CG2 
4706  N N   . CYS B  69  ? 0.7700 0.5411 0.6163 -0.2862 0.1343  -0.0286 69  CYS B N   
4707  C CA  . CYS B  69  ? 0.7542 0.5202 0.5985 -0.2754 0.1276  -0.0258 69  CYS B CA  
4708  C C   . CYS B  69  ? 0.7370 0.5216 0.5995 -0.2695 0.1225  -0.0270 69  CYS B C   
4709  O O   . CYS B  69  ? 0.7611 0.5620 0.6372 -0.2700 0.1236  -0.0286 69  CYS B O   
4710  C CB  . CYS B  69  ? 0.7538 0.5105 0.5877 -0.2692 0.1276  -0.0223 69  CYS B CB  
4711  S SG  . CYS B  69  ? 1.0420 0.7733 0.8527 -0.2738 0.1310  -0.0192 69  CYS B SG  
4712  N N   . TYR B  70  ? 0.6073 0.3891 0.4700 -0.2640 0.1168  -0.0262 70  TYR B N   
4713  C CA  . TYR B  70  ? 0.5855 0.3840 0.4646 -0.2596 0.1115  -0.0271 70  TYR B CA  
4714  C C   . TYR B  70  ? 0.5659 0.3749 0.4543 -0.2522 0.1095  -0.0254 70  TYR B C   
4715  O O   . TYR B  70  ? 0.5782 0.3785 0.4582 -0.2454 0.1084  -0.0226 70  TYR B O   
4716  C CB  . TYR B  70  ? 0.6042 0.3963 0.4797 -0.2551 0.1061  -0.0264 70  TYR B CB  
4717  C CG  . TYR B  70  ? 0.6022 0.4094 0.4919 -0.2574 0.1028  -0.0289 70  TYR B CG  
4718  C CD1 . TYR B  70  ? 0.6401 0.4640 0.5454 -0.2525 0.0985  -0.0283 70  TYR B CD1 
4719  C CD2 . TYR B  70  ? 0.6135 0.4186 0.5019 -0.2649 0.1038  -0.0318 70  TYR B CD2 
4720  C CE1 . TYR B  70  ? 0.6915 0.5294 0.6100 -0.2548 0.0949  -0.0302 70  TYR B CE1 
4721  C CE2 . TYR B  70  ? 0.6762 0.4957 0.5776 -0.2674 0.1005  -0.0342 70  TYR B CE2 
4722  C CZ  . TYR B  70  ? 0.7373 0.5734 0.6537 -0.2623 0.0959  -0.0332 70  TYR B CZ  
4723  O OH  . TYR B  70  ? 0.7932 0.6439 0.7229 -0.2648 0.0918  -0.0350 70  TYR B OH  
4724  N N   . GLN B  71  ? 0.5535 0.3815 0.4599 -0.2537 0.1089  -0.0272 71  GLN B N   
4725  C CA  . GLN B  71  ? 0.5368 0.3753 0.4535 -0.2479 0.1077  -0.0260 71  GLN B CA  
4726  C C   . GLN B  71  ? 0.6208 0.4805 0.5602 -0.2474 0.1041  -0.0271 71  GLN B C   
4727  O O   . GLN B  71  ? 0.5222 0.3908 0.4704 -0.2535 0.1038  -0.0295 71  GLN B O   
4728  C CB  . GLN B  71  ? 0.5676 0.4038 0.4793 -0.2521 0.1147  -0.0269 71  GLN B CB  
4729  C CG  . GLN B  71  ? 0.5668 0.4128 0.4865 -0.2626 0.1200  -0.0308 71  GLN B CG  
4730  C CD  . GLN B  71  ? 0.5733 0.4153 0.4853 -0.2681 0.1277  -0.0321 71  GLN B CD  
4731  O OE1 . GLN B  71  ? 0.5668 0.4219 0.4904 -0.2691 0.1304  -0.0340 71  GLN B OE1 
4732  N NE2 . GLN B  71  ? 0.5943 0.4179 0.4866 -0.2721 0.1312  -0.0311 71  GLN B NE2 
4733  N N   . TYR B  72  ? 0.6426 0.5103 0.5917 -0.2402 0.1012  -0.0252 72  TYR B N   
4734  C CA  . TYR B  72  ? 0.6329 0.5206 0.6048 -0.2393 0.0976  -0.0256 72  TYR B CA  
4735  C C   . TYR B  72  ? 0.6647 0.5638 0.6468 -0.2477 0.1032  -0.0294 72  TYR B C   
4736  O O   . TYR B  72  ? 0.7011 0.5964 0.6769 -0.2504 0.1096  -0.0308 72  TYR B O   
4737  C CB  . TYR B  72  ? 0.7331 0.6248 0.7120 -0.2302 0.0942  -0.0227 72  TYR B CB  
4738  C CG  . TYR B  72  ? 0.7607 0.6725 0.7641 -0.2293 0.0909  -0.0229 72  TYR B CG  
4739  C CD1 . TYR B  72  ? 0.7575 0.6794 0.7748 -0.2267 0.0834  -0.0212 72  TYR B CD1 
4740  C CD2 . TYR B  72  ? 0.8025 0.7234 0.8155 -0.2311 0.0952  -0.0249 72  TYR B CD2 
4741  C CE1 . TYR B  72  ? 0.7672 0.7071 0.8079 -0.2259 0.0795  -0.0208 72  TYR B CE1 
4742  C CE2 . TYR B  72  ? 0.8245 0.7641 0.8614 -0.2301 0.0918  -0.0251 72  TYR B CE2 
4743  C CZ  . TYR B  72  ? 0.8125 0.7614 0.8636 -0.2274 0.0836  -0.0228 72  TYR B CZ  
4744  O OH  . TYR B  72  ? 0.8176 0.7847 0.8931 -0.2266 0.0794  -0.0225 72  TYR B OH  
4745  N N   . VAL B  73  ? 0.7370 0.6503 0.7347 -0.2522 0.1009  -0.0314 73  VAL B N   
4746  C CA  . VAL B  73  ? 0.7536 0.6809 0.7646 -0.2598 0.1056  -0.0353 73  VAL B CA  
4747  C C   . VAL B  73  ? 0.7556 0.7013 0.7898 -0.2556 0.1020  -0.0349 73  VAL B C   
4748  O O   . VAL B  73  ? 0.7588 0.7133 0.8063 -0.2511 0.0942  -0.0325 73  VAL B O   
4749  C CB  . VAL B  73  ? 0.7018 0.6351 0.7179 -0.2680 0.1052  -0.0382 73  VAL B CB  
4750  C CG1 . VAL B  73  ? 0.6974 0.6501 0.7336 -0.2743 0.1078  -0.0421 73  VAL B CG1 
4751  C CG2 . VAL B  73  ? 0.7012 0.6171 0.6959 -0.2741 0.1105  -0.0395 73  VAL B CG2 
4752  N N   . ASP B  74  ? 0.6559 0.6075 0.6951 -0.2573 0.1077  -0.0372 74  ASP B N   
4753  C CA  . ASP B  74  ? 0.6692 0.6365 0.7294 -0.2523 0.1044  -0.0367 74  ASP B CA  
4754  C C   . ASP B  74  ? 0.6688 0.6566 0.7538 -0.2556 0.1000  -0.0383 74  ASP B C   
4755  O O   . ASP B  74  ? 0.6652 0.6618 0.7567 -0.2638 0.1047  -0.0429 74  ASP B O   
4756  C CB  . ASP B  74  ? 0.8388 0.8081 0.8984 -0.2538 0.1121  -0.0397 74  ASP B CB  
4757  C CG  . ASP B  74  ? 0.8551 0.8418 0.9379 -0.2496 0.1092  -0.0403 74  ASP B CG  
4758  O OD1 . ASP B  74  ? 0.8453 0.8283 0.9277 -0.2414 0.1055  -0.0370 74  ASP B OD1 
4759  O OD2 . ASP B  74  ? 0.8698 0.8740 0.9709 -0.2552 0.1112  -0.0451 74  ASP B OD2 
4760  N N   . THR B  75  ? 0.7211 0.7165 0.8201 -0.2491 0.0908  -0.0345 75  THR B N   
4761  C CA  . THR B  75  ? 0.7548 0.7688 0.8775 -0.2512 0.0843  -0.0348 75  THR B CA  
4762  C C   . THR B  75  ? 0.7477 0.7800 0.8939 -0.2497 0.0828  -0.0364 75  THR B C   
4763  O O   . THR B  75  ? 0.7248 0.7739 0.8922 -0.2516 0.0770  -0.0369 75  THR B O   
4764  C CB  . THR B  75  ? 0.8407 0.8519 0.9637 -0.2468 0.0748  -0.0301 75  THR B CB  
4765  O OG1 . THR B  75  ? 0.8530 0.8581 0.9738 -0.2374 0.0705  -0.0254 75  THR B OG1 
4766  C CG2 . THR B  75  ? 0.8479 0.8433 0.9486 -0.2503 0.0773  -0.0308 75  THR B CG2 
4767  N N   . LEU B  76  ? 0.8403 0.8696 0.9827 -0.2467 0.0880  -0.0376 76  LEU B N   
4768  C CA  . LEU B  76  ? 0.8191 0.8630 0.9816 -0.2434 0.0861  -0.0390 76  LEU B CA  
4769  C C   . LEU B  76  ? 0.8463 0.9120 1.0318 -0.2499 0.0883  -0.0453 76  LEU B C   
4770  O O   . LEU B  76  ? 0.8225 0.9041 1.0305 -0.2480 0.0807  -0.0444 76  LEU B O   
4771  C CB  . LEU B  76  ? 0.6754 0.7105 0.8267 -0.2399 0.0930  -0.0405 76  LEU B CB  
4772  C CG  . LEU B  76  ? 0.5962 0.6453 0.7672 -0.2361 0.0920  -0.0429 76  LEU B CG  
4773  C CD1 . LEU B  76  ? 0.5526 0.6063 0.7367 -0.2292 0.0796  -0.0363 76  LEU B CD1 
4774  C CD2 . LEU B  76  ? 0.5555 0.5954 0.7142 -0.2333 0.0997  -0.0453 76  LEU B CD2 
4775  N N   . TYR B  77  ? 0.9719 1.0387 1.1519 -0.2574 0.0987  -0.0518 77  TYR B N   
4776  C CA  . TYR B  77  ? 0.9909 1.0787 1.1922 -0.2639 0.1024  -0.0591 77  TYR B CA  
4777  C C   . TYR B  77  ? 0.9987 1.0870 1.1951 -0.2731 0.1060  -0.0620 77  TYR B C   
4778  O O   . TYR B  77  ? 1.0599 1.1431 1.2441 -0.2795 0.1163  -0.0668 77  TYR B O   
4779  C CB  . TYR B  77  ? 0.9027 0.9943 1.1046 -0.2652 0.1130  -0.0662 77  TYR B CB  
4780  C CG  . TYR B  77  ? 0.9020 1.0005 1.1174 -0.2574 0.1101  -0.0663 77  TYR B CG  
4781  C CD1 . TYR B  77  ? 0.8906 1.0038 1.1298 -0.2527 0.0997  -0.0638 77  TYR B CD1 
4782  C CD2 . TYR B  77  ? 0.9090 0.9994 1.1134 -0.2550 0.1178  -0.0691 77  TYR B CD2 
4783  C CE1 . TYR B  77  ? 0.8758 0.9952 1.1277 -0.2457 0.0971  -0.0642 77  TYR B CE1 
4784  C CE2 . TYR B  77  ? 0.8870 0.9836 1.1041 -0.2480 0.1156  -0.0700 77  TYR B CE2 
4785  C CZ  . TYR B  77  ? 0.8575 0.9685 1.0985 -0.2432 0.1053  -0.0676 77  TYR B CZ  
4786  O OH  . TYR B  77  ? 0.8069 0.9237 1.0609 -0.2362 0.1030  -0.0688 77  TYR B OH  
4787  N N   . PRO B  78  ? 0.7286 0.8230 0.9343 -0.2743 0.0974  -0.0591 78  PRO B N   
4788  C CA  . PRO B  78  ? 0.6686 0.7630 0.8699 -0.2828 0.0996  -0.0614 78  PRO B CA  
4789  C C   . PRO B  78  ? 0.6827 0.7902 0.8929 -0.2915 0.1092  -0.0702 78  PRO B C   
4790  O O   . PRO B  78  ? 0.6703 0.7970 0.9032 -0.2912 0.1092  -0.0745 78  PRO B O   
4791  C CB  . PRO B  78  ? 0.4993 0.6066 0.7195 -0.2820 0.0879  -0.0584 78  PRO B CB  
4792  C CG  . PRO B  78  ? 0.4919 0.5943 0.7133 -0.2721 0.0791  -0.0514 78  PRO B CG  
4793  C CD  . PRO B  78  ? 0.5374 0.6390 0.7585 -0.2678 0.0847  -0.0533 78  PRO B CD  
4794  N N   . GLY B  79  ? 0.7800 0.8773 0.9727 -0.2991 0.1174  -0.0729 79  GLY B N   
4795  C CA  . GLY B  79  ? 0.8105 0.9189 1.0095 -0.3087 0.1271  -0.0813 79  GLY B CA  
4796  C C   . GLY B  79  ? 0.8346 0.9501 1.0384 -0.3090 0.1362  -0.0874 79  GLY B C   
4797  O O   . GLY B  79  ? 0.8691 0.9983 1.0834 -0.3165 0.1437  -0.0954 79  GLY B O   
4798  N N   . PHE B  80  ? 0.7456 0.8520 0.9419 -0.3011 0.1358  -0.0843 80  PHE B N   
4799  C CA  . PHE B  80  ? 0.7469 0.8579 0.9450 -0.3011 0.1448  -0.0904 80  PHE B CA  
4800  C C   . PHE B  80  ? 0.7635 0.8546 0.9325 -0.3057 0.1550  -0.0909 80  PHE B C   
4801  O O   . PHE B  80  ? 0.7533 0.8238 0.9007 -0.3010 0.1526  -0.0842 80  PHE B O   
4802  C CB  . PHE B  80  ? 0.7887 0.9015 0.9955 -0.2905 0.1390  -0.0874 80  PHE B CB  
4803  C CG  . PHE B  80  ? 0.8250 0.9410 1.0324 -0.2901 0.1483  -0.0938 80  PHE B CG  
4804  C CD1 . PHE B  80  ? 0.8484 0.9869 1.0802 -0.2926 0.1528  -0.1032 80  PHE B CD1 
4805  C CD2 . PHE B  80  ? 0.8508 0.9476 1.0346 -0.2872 0.1525  -0.0912 80  PHE B CD2 
4806  C CE1 . PHE B  80  ? 0.8636 1.0055 1.0962 -0.2924 0.1619  -0.1102 80  PHE B CE1 
4807  C CE2 . PHE B  80  ? 0.8658 0.9656 1.0496 -0.2873 0.1612  -0.0976 80  PHE B CE2 
4808  C CZ  . PHE B  80  ? 0.8717 0.9940 1.0797 -0.2900 0.1662  -0.1074 80  PHE B CZ  
4809  N N   . GLU B  81  ? 0.7714 0.8690 0.9401 -0.3149 0.1660  -0.0989 81  GLU B N   
4810  C CA  . GLU B  81  ? 0.8356 0.9150 0.9765 -0.3215 0.1754  -0.0993 81  GLU B CA  
4811  C C   . GLU B  81  ? 0.7842 0.8445 0.9041 -0.3151 0.1762  -0.0947 81  GLU B C   
4812  O O   . GLU B  81  ? 0.7359 0.7750 0.8298 -0.3168 0.1780  -0.0901 81  GLU B O   
4813  C CB  . GLU B  81  ? 1.2238 1.3159 1.3703 -0.3319 0.1876  -0.1095 81  GLU B CB  
4814  C CG  . GLU B  81  ? 1.3224 1.3961 1.4402 -0.3397 0.1977  -0.1100 81  GLU B CG  
4815  C CD  . GLU B  81  ? 1.3731 1.4599 1.4961 -0.3501 0.2101  -0.1205 81  GLU B CD  
4816  O OE1 . GLU B  81  ? 1.3941 1.5030 1.5414 -0.3539 0.2112  -0.1273 81  GLU B OE1 
4817  O OE2 . GLU B  81  ? 1.3743 1.4495 1.4772 -0.3546 0.2188  -0.1220 81  GLU B OE2 
4818  N N   . GLY B  82  ? 0.9894 1.0575 1.1213 -0.3076 0.1744  -0.0958 82  GLY B N   
4819  C CA  . GLY B  82  ? 1.0321 1.0850 1.1470 -0.3017 0.1756  -0.0927 82  GLY B CA  
4820  C C   . GLY B  82  ? 1.0306 1.0626 1.1275 -0.2941 0.1671  -0.0824 82  GLY B C   
4821  O O   . GLY B  82  ? 1.0539 1.0665 1.1262 -0.2939 0.1702  -0.0793 82  GLY B O   
4822  N N   . THR B  83  ? 1.0521 1.0884 1.1616 -0.2876 0.1562  -0.0774 83  THR B N   
4823  C CA  . THR B  83  ? 0.9644 0.9828 1.0588 -0.2805 0.1478  -0.0683 83  THR B CA  
4824  C C   . THR B  83  ? 0.9868 0.9940 1.0668 -0.2862 0.1478  -0.0659 83  THR B C   
4825  O O   . THR B  83  ? 1.0260 1.0131 1.0842 -0.2839 0.1464  -0.0607 83  THR B O   
4826  C CB  . THR B  83  ? 0.5707 0.5980 0.6837 -0.2722 0.1361  -0.0638 83  THR B CB  
4827  O OG1 . THR B  83  ? 0.4956 0.5310 0.6189 -0.2761 0.1313  -0.0634 83  THR B OG1 
4828  C CG2 . THR B  83  ? 0.5607 0.6065 0.6972 -0.2689 0.1359  -0.0681 83  THR B CG2 
4829  N N   . GLU B  84  ? 0.6646 0.6854 0.7580 -0.2937 0.1492  -0.0702 84  GLU B N   
4830  C CA  . GLU B  84  ? 0.6321 0.6448 0.7153 -0.2997 0.1489  -0.0688 84  GLU B CA  
4831  C C   . GLU B  84  ? 0.5734 0.5673 0.6303 -0.3055 0.1571  -0.0688 84  GLU B C   
4832  O O   . GLU B  84  ? 0.5616 0.5390 0.6017 -0.3059 0.1549  -0.0645 84  GLU B O   
4833  C CB  . GLU B  84  ? 0.8751 0.9078 0.9787 -0.3077 0.1502  -0.0746 84  GLU B CB  
4834  C CG  . GLU B  84  ? 0.9521 0.9834 1.0569 -0.3099 0.1438  -0.0719 84  GLU B CG  
4835  C CD  . GLU B  84  ? 0.9856 1.0220 1.1031 -0.3011 0.1316  -0.0668 84  GLU B CD  
4836  O OE1 . GLU B  84  ? 0.9620 1.0117 1.0974 -0.2957 0.1279  -0.0670 84  GLU B OE1 
4837  O OE2 . GLU B  84  ? 1.0254 1.0524 1.1350 -0.3000 0.1258  -0.0626 84  GLU B OE2 
4838  N N   . MET B  85  ? 0.6940 0.6900 0.7472 -0.3098 0.1664  -0.0737 85  MET B N   
4839  C CA  . MET B  85  ? 0.7180 0.6975 0.7470 -0.3170 0.1746  -0.0740 85  MET B CA  
4840  C C   . MET B  85  ? 0.7492 0.7041 0.7537 -0.3110 0.1710  -0.0665 85  MET B C   
4841  O O   . MET B  85  ? 0.7590 0.6980 0.7434 -0.3167 0.1752  -0.0650 85  MET B O   
4842  C CB  . MET B  85  ? 0.6508 0.6375 0.6800 -0.3227 0.1852  -0.0808 85  MET B CB  
4843  C CG  . MET B  85  ? 0.6269 0.6135 0.6566 -0.3147 0.1847  -0.0805 85  MET B CG  
4844  S SD  . MET B  85  ? 0.7466 0.7475 0.7827 -0.3219 0.1973  -0.0907 85  MET B SD  
4845  C CE  . MET B  85  ? 0.6241 0.6012 0.6256 -0.3296 0.2055  -0.0889 85  MET B CE  
4846  N N   . TRP B  86  ? 0.7935 0.7454 0.8002 -0.2998 0.1634  -0.0618 86  TRP B N   
4847  C CA  . TRP B  86  ? 0.8006 0.7302 0.7852 -0.2937 0.1601  -0.0555 86  TRP B CA  
4848  C C   . TRP B  86  ? 0.8315 0.7517 0.8106 -0.2910 0.1529  -0.0516 86  TRP B C   
4849  O O   . TRP B  86  ? 0.8575 0.7587 0.8174 -0.2874 0.1508  -0.0474 86  TRP B O   
4850  C CB  . TRP B  86  ? 0.6873 0.6170 0.6741 -0.2837 0.1568  -0.0532 86  TRP B CB  
4851  C CG  . TRP B  86  ? 0.6917 0.6324 0.6849 -0.2875 0.1649  -0.0594 86  TRP B CG  
4852  C CD1 . TRP B  86  ? 0.6946 0.6559 0.7113 -0.2860 0.1651  -0.0642 86  TRP B CD1 
4853  C CD2 . TRP B  86  ? 0.7001 0.6324 0.6764 -0.2939 0.1742  -0.0621 86  TRP B CD2 
4854  N NE1 . TRP B  86  ? 0.7000 0.6667 0.7160 -0.2909 0.1745  -0.0704 86  TRP B NE1 
4855  C CE2 . TRP B  86  ? 0.7019 0.6509 0.6925 -0.2960 0.1803  -0.0692 86  TRP B CE2 
4856  C CE3 . TRP B  86  ? 0.7273 0.6395 0.6779 -0.2981 0.1778  -0.0592 86  TRP B CE3 
4857  C CZ2 . TRP B  86  ? 0.7229 0.6693 0.7020 -0.3027 0.1901  -0.0738 86  TRP B CZ2 
4858  C CZ3 . TRP B  86  ? 0.7580 0.6671 0.6969 -0.3048 0.1870  -0.0630 86  TRP B CZ3 
4859  C CH2 . TRP B  86  ? 0.7530 0.6792 0.7057 -0.3072 0.1933  -0.0704 86  TRP B CH2 
4860  N N   . ASN B  87  ? 0.7972 0.7310 0.7936 -0.2927 0.1491  -0.0532 87  ASN B N   
4861  C CA  . ASN B  87  ? 0.7762 0.7033 0.7690 -0.2914 0.1428  -0.0504 87  ASN B CA  
4862  C C   . ASN B  87  ? 0.7662 0.6773 0.7393 -0.2997 0.1475  -0.0509 87  ASN B C   
4863  O O   . ASN B  87  ? 0.7918 0.7009 0.7582 -0.3078 0.1556  -0.0538 87  ASN B O   
4864  C CB  . ASN B  87  ? 0.8001 0.7472 0.8170 -0.2926 0.1379  -0.0525 87  ASN B CB  
4865  C CG  . ASN B  87  ? 0.8127 0.7719 0.8475 -0.2829 0.1301  -0.0500 87  ASN B CG  
4866  O OD1 . ASN B  87  ? 0.8359 0.7856 0.8630 -0.2744 0.1262  -0.0458 87  ASN B OD1 
4867  N ND2 . ASN B  87  ? 0.7998 0.7799 0.8591 -0.2843 0.1274  -0.0525 87  ASN B ND2 
4868  N N   . PRO B  88  ? 0.7580 0.6574 0.7217 -0.2980 0.1427  -0.0482 88  PRO B N   
4869  C CA  . PRO B  88  ? 0.7768 0.6610 0.7232 -0.3062 0.1469  -0.0487 88  PRO B CA  
4870  C C   . PRO B  88  ? 0.7833 0.6793 0.7401 -0.3171 0.1512  -0.0537 88  PRO B C   
4871  O O   . PRO B  88  ? 0.7603 0.6733 0.7364 -0.3170 0.1472  -0.0557 88  PRO B O   
4872  C CB  . PRO B  88  ? 0.6066 0.4794 0.5454 -0.3008 0.1399  -0.0454 88  PRO B CB  
4873  C CG  . PRO B  88  ? 0.5817 0.4694 0.5386 -0.2929 0.1324  -0.0444 88  PRO B CG  
4874  C CD  . PRO B  88  ? 0.5696 0.4674 0.5361 -0.2886 0.1337  -0.0445 88  PRO B CD  
4875  N N   . ASN B  89  ? 0.6930 0.5805 0.6374 -0.3266 0.1590  -0.0555 89  ASN B N   
4876  C CA  . ASN B  89  ? 0.7152 0.6116 0.6668 -0.3380 0.1639  -0.0603 89  ASN B CA  
4877  C C   . ASN B  89  ? 0.7518 0.6341 0.6912 -0.3437 0.1635  -0.0598 89  ASN B C   
4878  O O   . ASN B  89  ? 0.7399 0.6279 0.6843 -0.3534 0.1670  -0.0636 89  ASN B O   
4879  C CB  . ASN B  89  ? 0.6758 0.5741 0.6236 -0.3462 0.1736  -0.0634 89  ASN B CB  
4880  C CG  . ASN B  89  ? 0.6961 0.5707 0.6175 -0.3484 0.1779  -0.0600 89  ASN B CG  
4881  O OD1 . ASN B  89  ? 0.7033 0.5592 0.6091 -0.3463 0.1747  -0.0560 89  ASN B OD1 
4882  N ND2 . ASN B  89  ? 0.7061 0.5817 0.6228 -0.3528 0.1852  -0.0616 89  ASN B ND2 
4883  N N   . ARG B  90  ? 0.8815 0.7452 0.8053 -0.3377 0.1593  -0.0553 90  ARG B N   
4884  C CA  . ARG B  90  ? 0.9211 0.7718 0.8352 -0.3413 0.1577  -0.0547 90  ARG B CA  
4885  C C   . ARG B  90  ? 0.9770 0.8295 0.8966 -0.3321 0.1487  -0.0528 90  ARG B C   
4886  O O   . ARG B  90  ? 0.9653 0.8301 0.8973 -0.3241 0.1440  -0.0519 90  ARG B O   
4887  C CB  . ARG B  90  ? 0.8395 0.6649 0.7292 -0.3432 0.1609  -0.0512 90  ARG B CB  
4888  C CG  . ARG B  90  ? 0.8632 0.6839 0.7448 -0.3548 0.1698  -0.0530 90  ARG B CG  
4889  C CD  . ARG B  90  ? 0.8793 0.7029 0.7650 -0.3658 0.1726  -0.0569 90  ARG B CD  
4890  N NE  . ARG B  90  ? 0.9007 0.7167 0.7759 -0.3771 0.1813  -0.0579 90  ARG B NE  
4891  C CZ  . ARG B  90  ? 0.9010 0.7310 0.7841 -0.3835 0.1877  -0.0615 90  ARG B CZ  
4892  N NH1 . ARG B  90  ? 0.8555 0.7077 0.7583 -0.3792 0.1863  -0.0646 90  ARG B NH1 
4893  N NH2 . ARG B  90  ? 0.9326 0.7543 0.8044 -0.3942 0.1956  -0.0622 90  ARG B NH2 
4894  N N   . GLU B  91  ? 1.1632 1.0036 1.0740 -0.3337 0.1464  -0.0522 91  GLU B N   
4895  C CA  . GLU B  91  ? 1.1483 0.9900 1.0631 -0.3263 0.1385  -0.0510 91  GLU B CA  
4896  C C   . GLU B  91  ? 1.0732 0.8999 0.9749 -0.3161 0.1350  -0.0462 91  GLU B C   
4897  O O   . GLU B  91  ? 1.1118 0.9209 0.9968 -0.3167 0.1385  -0.0438 91  GLU B O   
4898  C CB  . GLU B  91  ? 1.1752 1.0108 1.0865 -0.3329 0.1380  -0.0532 91  GLU B CB  
4899  C CG  . GLU B  91  ? 1.2036 1.0506 1.1269 -0.3295 0.1309  -0.0544 91  GLU B CG  
4900  C CD  . GLU B  91  ? 1.2684 1.1050 1.1841 -0.3344 0.1301  -0.0562 91  GLU B CD  
4901  O OE1 . GLU B  91  ? 1.2800 1.1001 1.1818 -0.3404 0.1351  -0.0562 91  GLU B OE1 
4902  O OE2 . GLU B  91  ? 1.2984 1.1432 1.2221 -0.3326 0.1245  -0.0575 91  GLU B OE2 
4903  N N   . LEU B  92  ? 0.6831 0.5170 0.5928 -0.3070 0.1281  -0.0446 92  LEU B N   
4904  C CA  . LEU B  92  ? 0.6282 0.4498 0.5274 -0.2968 0.1242  -0.0405 92  LEU B CA  
4905  C C   . LEU B  92  ? 0.6390 0.4434 0.5247 -0.2963 0.1222  -0.0396 92  LEU B C   
4906  O O   . LEU B  92  ? 0.6402 0.4488 0.5311 -0.2982 0.1191  -0.0417 92  LEU B O   
4907  C CB  . LEU B  92  ? 0.6019 0.4374 0.5148 -0.2877 0.1174  -0.0391 92  LEU B CB  
4908  C CG  . LEU B  92  ? 0.5855 0.4390 0.5147 -0.2851 0.1171  -0.0392 92  LEU B CG  
4909  C CD1 . LEU B  92  ? 0.5631 0.4214 0.4987 -0.2744 0.1099  -0.0362 92  LEU B CD1 
4910  C CD2 . LEU B  92  ? 0.5937 0.4417 0.5156 -0.2863 0.1232  -0.0386 92  LEU B CD2 
4911  N N   . SER B  93  ? 0.6498 0.4352 0.5189 -0.2936 0.1235  -0.0366 93  SER B N   
4912  C CA  . SER B  93  ? 0.6573 0.4269 0.5154 -0.2912 0.1208  -0.0355 93  SER B CA  
4913  C C   . SER B  93  ? 0.6574 0.4117 0.5025 -0.2831 0.1194  -0.0311 93  SER B C   
4914  O O   . SER B  93  ? 0.6599 0.4114 0.5003 -0.2823 0.1223  -0.0291 93  SER B O   
4915  C CB  . SER B  93  ? 0.6826 0.4408 0.5329 -0.3014 0.1250  -0.0374 93  SER B CB  
4916  O OG  . SER B  93  ? 0.6982 0.4342 0.5320 -0.2997 0.1254  -0.0344 93  SER B OG  
4917  N N   . GLU B  94  ? 0.6550 0.3998 0.4947 -0.2774 0.1151  -0.0300 94  GLU B N   
4918  C CA  . GLU B  94  ? 0.6554 0.3858 0.4836 -0.2695 0.1132  -0.0261 94  GLU B CA  
4919  C C   . GLU B  94  ? 0.6820 0.3923 0.4950 -0.2748 0.1172  -0.0243 94  GLU B C   
4920  O O   . GLU B  94  ? 0.9090 0.6063 0.7114 -0.2699 0.1166  -0.0206 94  GLU B O   
4921  C CB  . GLU B  94  ? 0.8152 0.5425 0.6435 -0.2621 0.1075  -0.0258 94  GLU B CB  
4922  C CG  . GLU B  94  ? 0.6193 0.3588 0.4560 -0.2524 0.1028  -0.0246 94  GLU B CG  
4923  C CD  . GLU B  94  ? 0.6126 0.3452 0.4458 -0.2447 0.0978  -0.0237 94  GLU B CD  
4924  O OE1 . GLU B  94  ? 0.6130 0.3472 0.4491 -0.2467 0.0960  -0.0263 94  GLU B OE1 
4925  O OE2 . GLU B  94  ? 0.6069 0.3330 0.4347 -0.2368 0.0959  -0.0206 94  GLU B OE2 
4926  N N   . ASP B  95  ? 0.7000 0.4078 0.5122 -0.2851 0.1212  -0.0267 95  ASP B N   
4927  C CA  . ASP B  95  ? 0.7627 0.4514 0.5609 -0.2914 0.1252  -0.0246 95  ASP B CA  
4928  C C   . ASP B  95  ? 0.7406 0.4365 0.5396 -0.2976 0.1308  -0.0248 95  ASP B C   
4929  O O   . ASP B  95  ? 0.7417 0.4443 0.5456 -0.3072 0.1350  -0.0280 95  ASP B O   
4930  C CB  . ASP B  95  ? 0.8599 0.5437 0.6587 -0.2998 0.1266  -0.0277 95  ASP B CB  
4931  C CG  . ASP B  95  ? 0.9106 0.5741 0.6960 -0.3076 0.1307  -0.0256 95  ASP B CG  
4932  O OD1 . ASP B  95  ? 0.9743 0.6313 0.7511 -0.3096 0.1340  -0.0226 95  ASP B OD1 
4933  O OD2 . ASP B  95  ? 0.8892 0.5432 0.6728 -0.3120 0.1305  -0.0272 95  ASP B OD2 
4934  N N   . CYS B  96  ? 0.7269 0.4214 0.5211 -0.2923 0.1309  -0.0218 96  CYS B N   
4935  C CA  . CYS B  96  ? 0.7312 0.4324 0.5255 -0.2975 0.1363  -0.0220 96  CYS B CA  
4936  C C   . CYS B  96  ? 0.7523 0.4370 0.5301 -0.3005 0.1399  -0.0182 96  CYS B C   
4937  O O   . CYS B  96  ? 0.7558 0.4470 0.5337 -0.3051 0.1447  -0.0188 96  CYS B O   
4938  C CB  . CYS B  96  ? 0.8680 0.5895 0.6761 -0.2917 0.1349  -0.0234 96  CYS B CB  
4939  S SG  . CYS B  96  ? 0.9681 0.6885 0.7756 -0.2771 0.1282  -0.0201 96  CYS B SG  
4940  N N   . LEU B  97  ? 0.8561 0.5201 0.6202 -0.2979 0.1375  -0.0142 97  LEU B N   
4941  C CA  . LEU B  97  ? 0.8946 0.5446 0.6436 -0.2988 0.1396  -0.0098 97  LEU B CA  
4942  C C   . LEU B  97  ? 0.9529 0.5907 0.6914 -0.3111 0.1455  -0.0089 97  LEU B C   
4943  O O   . LEU B  97  ? 1.0001 0.6197 0.7292 -0.3139 0.1445  -0.0063 97  LEU B O   
4944  C CB  . LEU B  97  ? 0.7837 0.4172 0.5230 -0.2896 0.1339  -0.0052 97  LEU B CB  
4945  C CG  . LEU B  97  ? 0.7546 0.3986 0.5032 -0.2774 0.1280  -0.0059 97  LEU B CG  
4946  C CD1 . LEU B  97  ? 0.7574 0.3851 0.4964 -0.2690 0.1228  -0.0016 97  LEU B CD1 
4947  C CD2 . LEU B  97  ? 0.7372 0.3973 0.4926 -0.2749 0.1296  -0.0070 97  LEU B CD2 
4948  N N   . TYR B  98  ? 0.9943 0.6419 0.7343 -0.3183 0.1515  -0.0107 98  TYR B N   
4949  C CA  . TYR B  98  ? 1.0091 0.6500 0.7415 -0.3314 0.1582  -0.0107 98  TYR B CA  
4950  C C   . TYR B  98  ? 1.0286 0.6755 0.7572 -0.3344 0.1631  -0.0105 98  TYR B C   
4951  O O   . TYR B  98  ? 1.0058 0.6712 0.7462 -0.3300 0.1632  -0.0135 98  TYR B O   
4952  C CB  . TYR B  98  ? 0.9507 0.6061 0.6970 -0.3390 0.1612  -0.0164 98  TYR B CB  
4953  C CG  . TYR B  98  ? 0.9425 0.5940 0.6937 -0.3366 0.1566  -0.0176 98  TYR B CG  
4954  C CD1 . TYR B  98  ? 0.9679 0.6004 0.7093 -0.3425 0.1571  -0.0156 98  TYR B CD1 
4955  C CD2 . TYR B  98  ? 0.9209 0.5869 0.6863 -0.3285 0.1517  -0.0204 98  TYR B CD2 
4956  C CE1 . TYR B  98  ? 0.9713 0.5998 0.7173 -0.3405 0.1531  -0.0170 98  TYR B CE1 
4957  C CE2 . TYR B  98  ? 0.9322 0.5946 0.7013 -0.3267 0.1477  -0.0217 98  TYR B CE2 
4958  C CZ  . TYR B  98  ? 0.9682 0.6119 0.7277 -0.3327 0.1486  -0.0203 98  TYR B CZ  
4959  O OH  . TYR B  98  ? 1.0049 0.6449 0.7685 -0.3312 0.1449  -0.0221 98  TYR B OH  
4960  N N   . LEU B  99  ? 1.0027 0.6343 0.7151 -0.3422 0.1673  -0.0069 99  LEU B N   
4961  C CA  . LEU B  99  ? 0.9886 0.6268 0.6971 -0.3470 0.1730  -0.0074 99  LEU B CA  
4962  C C   . LEU B  99  ? 0.9004 0.5437 0.6094 -0.3613 0.1813  -0.0105 99  LEU B C   
4963  O O   . LEU B  99  ? 0.9889 0.6293 0.7005 -0.3678 0.1825  -0.0120 99  LEU B O   
4964  C CB  . LEU B  99  ? 0.8952 0.5155 0.5850 -0.3444 0.1716  -0.0011 99  LEU B CB  
4965  C CG  . LEU B  99  ? 0.9217 0.5161 0.5955 -0.3466 0.1690  0.0049  99  LEU B CG  
4966  C CD1 . LEU B  99  ? 1.0202 0.6063 0.6825 -0.3608 0.1762  0.0063  99  LEU B CD1 
4967  C CD2 . LEU B  99  ? 0.9222 0.5018 0.5840 -0.3373 0.1632  0.0109  99  LEU B CD2 
4968  N N   . ASN B  100 ? 1.0303 0.6812 0.7368 -0.3663 0.1871  -0.0118 100 ASN B N   
4969  C CA  . ASN B  100 ? 1.0913 0.7511 0.8003 -0.3797 0.1957  -0.0157 100 ASN B CA  
4970  C C   . ASN B  100 ? 1.1792 0.8278 0.8699 -0.3868 0.2009  -0.0122 100 ASN B C   
4971  O O   . ASN B  100 ? 1.2003 0.8495 0.8864 -0.3809 0.1997  -0.0105 100 ASN B O   
4972  C CB  . ASN B  100 ? 0.9544 0.6424 0.6846 -0.3788 0.1985  -0.0230 100 ASN B CB  
4973  C CG  . ASN B  100 ? 0.8699 0.5706 0.6187 -0.3714 0.1928  -0.0262 100 ASN B CG  
4974  O OD1 . ASN B  100 ? 0.9502 0.6422 0.6984 -0.3719 0.1897  -0.0252 100 ASN B OD1 
4975  N ND2 . ASN B  100 ? 0.8423 0.5634 0.6078 -0.3646 0.1914  -0.0299 100 ASN B ND2 
4976  N N   . VAL B  101 ? 1.1500 0.7880 0.8300 -0.3997 0.2064  -0.0109 101 VAL B N   
4977  C CA  . VAL B  101 ? 1.2050 0.8325 0.8668 -0.4083 0.2119  -0.0073 101 VAL B CA  
4978  C C   . VAL B  101 ? 1.0173 0.6583 0.6834 -0.4223 0.2219  -0.0127 101 VAL B C   
4979  O O   . VAL B  101 ? 1.0232 0.6691 0.6975 -0.4294 0.2247  -0.0161 101 VAL B O   
4980  C CB  . VAL B  101 ? 1.0898 0.6878 0.7300 -0.4117 0.2094  0.0012  101 VAL B CB  
4981  C CG1 . VAL B  101 ? 1.0580 0.6453 0.6787 -0.4173 0.2131  0.0058  101 VAL B CG1 
4982  C CG2 . VAL B  101 ? 1.0220 0.6072 0.6611 -0.3984 0.1994  0.0056  101 VAL B CG2 
4983  N N   . TRP B  102 ? 1.0223 0.6700 0.6832 -0.4261 0.2274  -0.0139 102 TRP B N   
4984  C CA  . TRP B  102 ? 1.0631 0.7220 0.7255 -0.4402 0.2376  -0.0187 102 TRP B CA  
4985  C C   . TRP B  102 ? 1.1803 0.8217 0.8183 -0.4505 0.2424  -0.0132 102 TRP B C   
4986  O O   . TRP B  102 ? 1.1661 0.8015 0.7926 -0.4463 0.2410  -0.0097 102 TRP B O   
4987  C CB  . TRP B  102 ? 1.2043 0.8911 0.8851 -0.4379 0.2415  -0.0268 102 TRP B CB  
4988  C CG  . TRP B  102 ? 1.2285 0.9361 0.9347 -0.4335 0.2397  -0.0334 102 TRP B CG  
4989  C CD1 . TRP B  102 ? 1.2430 0.9663 0.9630 -0.4427 0.2455  -0.0399 102 TRP B CD1 
4990  C CD2 . TRP B  102 ? 1.2609 0.9767 0.9820 -0.4191 0.2315  -0.0342 102 TRP B CD2 
4991  N NE1 . TRP B  102 ? 1.2359 0.9763 0.9785 -0.4348 0.2410  -0.0444 102 TRP B NE1 
4992  C CE2 . TRP B  102 ? 1.2519 0.9879 0.9952 -0.4204 0.2325  -0.0409 102 TRP B CE2 
4993  C CE3 . TRP B  102 ? 1.2817 0.9900 0.9996 -0.4054 0.2234  -0.0299 102 TRP B CE3 
4994  C CZ2 . TRP B  102 ? 1.2552 1.0034 1.0167 -0.4087 0.2254  -0.0428 102 TRP B CZ2 
4995  C CZ3 . TRP B  102 ? 1.2517 0.9723 0.9878 -0.3940 0.2168  -0.0321 102 TRP B CZ3 
4996  C CH2 . TRP B  102 ? 1.2387 0.9787 0.9959 -0.3958 0.2177  -0.0383 102 TRP B CH2 
4997  N N   . THR B  103 ? 1.3955 1.0284 1.0256 -0.4641 0.2479  -0.0122 103 THR B N   
4998  C CA  . THR B  103 ? 1.4032 1.0232 1.0121 -0.4771 0.2545  -0.0081 103 THR B CA  
4999  C C   . THR B  103 ? 1.3649 1.0047 0.9833 -0.4904 0.2652  -0.0161 103 THR B C   
5000  O O   . THR B  103 ? 1.2619 0.9183 0.9001 -0.4907 0.2664  -0.0228 103 THR B O   
5001  C CB  . THR B  103 ? 1.1752 0.7666 0.7656 -0.4834 0.2522  0.0006  103 THR B CB  
5002  O OG1 . THR B  103 ? 1.1610 0.7402 0.7541 -0.4711 0.2421  0.0046  103 THR B OG1 
5003  C CG2 . THR B  103 ? 1.2069 0.7790 0.7715 -0.4896 0.2539  0.0085  103 THR B CG2 
5004  N N   . PRO B  104 ? 1.6062 1.2452 1.2109 -0.5013 0.2730  -0.0157 104 PRO B N   
5005  C CA  . PRO B  104 ? 1.6905 1.3455 1.3022 -0.5159 0.2838  -0.0229 104 PRO B CA  
5006  C C   . PRO B  104 ? 1.7924 1.4321 1.3960 -0.5276 0.2860  -0.0195 104 PRO B C   
5007  O O   . PRO B  104 ? 1.8172 1.4316 1.4060 -0.5254 0.2799  -0.0106 104 PRO B O   
5008  C CB  . PRO B  104 ? 1.5362 1.1912 1.1321 -0.5239 0.2908  -0.0222 104 PRO B CB  
5009  C CG  . PRO B  104 ? 1.5202 1.1493 1.0936 -0.5177 0.2836  -0.0115 104 PRO B CG  
5010  C CD  . PRO B  104 ? 1.4685 1.0966 1.0538 -0.5003 0.2728  -0.0103 104 PRO B CD  
5011  N N   . TYR B  105 ? 1.8059 1.4607 1.4200 -0.5395 0.2944  -0.0265 105 TYR B N   
5012  C CA  . TYR B  105 ? 1.8316 1.4712 1.4351 -0.5533 0.2982  -0.0230 105 TYR B CA  
5013  C C   . TYR B  105 ? 1.8248 1.4639 1.4129 -0.5691 0.3087  -0.0230 105 TYR B C   
5014  O O   . TYR B  105 ? 1.8040 1.4666 1.4036 -0.5757 0.3171  -0.0319 105 TYR B O   
5015  C CB  . TYR B  105 ? 1.7346 1.3889 1.3594 -0.5566 0.2999  -0.0303 105 TYR B CB  
5016  C CG  . TYR B  105 ? 1.7694 1.4037 1.3855 -0.5656 0.2996  -0.0253 105 TYR B CG  
5017  C CD1 . TYR B  105 ? 1.8085 1.4300 1.4070 -0.5820 0.3071  -0.0217 105 TYR B CD1 
5018  C CD2 . TYR B  105 ? 1.7627 1.3914 1.3887 -0.5581 0.2921  -0.0245 105 TYR B CD2 
5019  C CE1 . TYR B  105 ? 1.8354 1.4383 1.4268 -0.5904 0.3069  -0.0172 105 TYR B CE1 
5020  C CE2 . TYR B  105 ? 1.7829 1.3935 1.4021 -0.5664 0.2919  -0.0205 105 TYR B CE2 
5021  C CZ  . TYR B  105 ? 1.8173 1.4149 1.4195 -0.5824 0.2993  -0.0168 105 TYR B CZ  
5022  O OH  . TYR B  105 ? 1.8340 1.4129 1.4298 -0.5908 0.2991  -0.0125 105 TYR B OH  
5023  N N   . PRO B  106 ? 1.7111 1.3233 1.2732 -0.5756 0.3081  -0.0130 106 PRO B N   
5024  C CA  . PRO B  106 ? 1.6965 1.2800 1.2459 -0.5706 0.2992  -0.0026 106 PRO B CA  
5025  C C   . PRO B  106 ? 1.6554 1.2259 1.1953 -0.5558 0.2896  0.0042  106 PRO B C   
5026  O O   . PRO B  106 ? 1.6361 1.2197 1.1789 -0.5492 0.2898  0.0011  106 PRO B O   
5027  C CB  . PRO B  106 ? 1.7890 1.3523 1.3149 -0.5871 0.3050  0.0044  106 PRO B CB  
5028  C CG  . PRO B  106 ? 1.8095 1.3842 1.3268 -0.5939 0.3128  0.0018  106 PRO B CG  
5029  C CD  . PRO B  106 ? 1.7747 1.3831 1.3175 -0.5885 0.3164  -0.0108 106 PRO B CD  
5030  N N   . ARG B  107 ? 1.6308 1.1751 1.1592 -0.5513 0.2816  0.0135  107 ARG B N   
5031  C CA  . ARG B  107 ? 1.6019 1.1296 1.1191 -0.5383 0.2721  0.0214  107 ARG B CA  
5032  C C   . ARG B  107 ? 1.9460 1.4650 1.4406 -0.5443 0.2754  0.0269  107 ARG B C   
5033  O O   . ARG B  107 ? 1.9646 1.4936 1.4550 -0.5577 0.2853  0.0233  107 ARG B O   
5034  C CB  . ARG B  107 ? 1.6349 1.1368 1.1459 -0.5345 0.2639  0.0295  107 ARG B CB  
5035  C CG  . ARG B  107 ? 1.6246 1.1229 1.1430 -0.5158 0.2528  0.0311  107 ARG B CG  
5036  C CD  . ARG B  107 ? 1.6854 1.1587 1.1986 -0.5128 0.2453  0.0385  107 ARG B CD  
5037  N NE  . ARG B  107 ? 1.7292 1.2103 1.2599 -0.5145 0.2461  0.0326  107 ARG B NE  
5038  C CZ  . ARG B  107 ? 1.7609 1.2247 1.2922 -0.5125 0.2406  0.0365  107 ARG B CZ  
5039  N NH1 . ARG B  107 ? 1.7990 1.2362 1.3149 -0.5084 0.2338  0.0464  107 ARG B NH1 
5040  N NH2 . ARG B  107 ? 1.7371 1.2101 1.2849 -0.5146 0.2418  0.0304  107 ARG B NH2 
5041  N N   . PRO B  108 ? 2.0842 1.5859 1.5647 -0.5350 0.2674  0.0351  108 PRO B N   
5042  C CA  . PRO B  108 ? 2.0833 1.5908 1.5523 -0.5372 0.2712  0.0353  108 PRO B CA  
5043  C C   . PRO B  108 ? 2.0916 1.5847 1.5364 -0.5541 0.2779  0.0415  108 PRO B C   
5044  O O   . PRO B  108 ? 2.1327 1.6115 1.5702 -0.5646 0.2800  0.0457  108 PRO B O   
5045  C CB  . PRO B  108 ? 1.9783 1.4707 1.4391 -0.5225 0.2603  0.0426  108 PRO B CB  
5046  C CG  . PRO B  108 ? 1.9998 1.4645 1.4506 -0.5231 0.2540  0.0519  108 PRO B CG  
5047  C CD  . PRO B  108 ? 1.9890 1.4618 1.4564 -0.5283 0.2576  0.0460  108 PRO B CD  
5048  N N   . ALA B  109 ? 1.7785 1.2755 1.2110 -0.5570 0.2813  0.0421  109 ALA B N   
5049  C CA  . ALA B  109 ? 1.7584 1.2359 1.1634 -0.5699 0.2845  0.0511  109 ALA B CA  
5050  C C   . ALA B  109 ? 1.7429 1.1949 1.1325 -0.5591 0.2729  0.0626  109 ALA B C   
5051  O O   . ALA B  109 ? 1.6926 1.1209 1.0739 -0.5591 0.2671  0.0713  109 ALA B O   
5052  C CB  . ALA B  109 ? 1.7887 1.2827 1.1873 -0.5782 0.2935  0.0462  109 ALA B CB  
5053  N N   . SER B  110 ? 2.0682 1.5264 1.4563 -0.5491 0.2692  0.0621  110 SER B N   
5054  C CA  . SER B  110 ? 2.0695 1.5080 1.4472 -0.5365 0.2577  0.0713  110 SER B CA  
5055  C C   . SER B  110 ? 2.0240 1.4755 1.4253 -0.5184 0.2506  0.0652  110 SER B C   
5056  O O   . SER B  110 ? 1.9744 1.4491 1.3975 -0.5168 0.2550  0.0547  110 SER B O   
5057  C CB  . SER B  110 ? 1.8094 1.2460 1.1685 -0.5383 0.2585  0.0750  110 SER B CB  
5058  O OG  . SER B  110 ? 1.7972 1.2053 1.1341 -0.5365 0.2504  0.0880  110 SER B OG  
5059  N N   . PRO B  111 ? 1.9787 1.4154 1.3759 -0.5047 0.2396  0.0717  111 PRO B N   
5060  C CA  . PRO B  111 ? 1.9309 1.3828 1.3503 -0.4881 0.2339  0.0651  111 PRO B CA  
5061  C C   . PRO B  111 ? 1.9238 1.4018 1.3535 -0.4852 0.2388  0.0561  111 PRO B C   
5062  O O   . PRO B  111 ? 1.9299 1.4066 1.3461 -0.4863 0.2395  0.0586  111 PRO B O   
5063  C CB  . PRO B  111 ? 1.7059 1.1366 1.1154 -0.4757 0.2221  0.0743  111 PRO B CB  
5064  C CG  . PRO B  111 ? 1.7371 1.1400 1.1272 -0.4848 0.2205  0.0849  111 PRO B CG  
5065  C CD  . PRO B  111 ? 1.7879 1.1939 1.1652 -0.5032 0.2314  0.0846  111 PRO B CD  
5066  N N   . THR B  112 ? 1.8542 1.3557 1.3082 -0.4814 0.2418  0.0458  112 THR B N   
5067  C CA  . THR B  112 ? 1.8116 1.3394 1.2795 -0.4781 0.2464  0.0365  112 THR B CA  
5068  C C   . THR B  112 ? 1.7292 1.2629 1.2099 -0.4596 0.2375  0.0350  112 THR B C   
5069  O O   . THR B  112 ? 1.6921 1.2142 1.1765 -0.4498 0.2288  0.0389  112 THR B O   
5070  C CB  . THR B  112 ? 1.2974 0.8491 0.7847 -0.4858 0.2556  0.0258  112 THR B CB  
5071  O OG1 . THR B  112 ? 1.2053 0.7733 0.7178 -0.4733 0.2515  0.0192  112 THR B OG1 
5072  C CG2 . THR B  112 ? 1.2767 0.8169 0.7575 -0.4990 0.2596  0.0286  112 THR B CG2 
5073  N N   . PRO B  113 ? 1.5516 1.1028 1.0388 -0.4552 0.2397  0.0295  113 PRO B N   
5074  C CA  . PRO B  113 ? 1.4756 1.0351 0.9772 -0.4384 0.2321  0.0272  113 PRO B CA  
5075  C C   . PRO B  113 ? 1.4119 0.9860 0.9390 -0.4306 0.2300  0.0207  113 PRO B C   
5076  O O   . PRO B  113 ? 1.3522 0.9408 0.8918 -0.4381 0.2367  0.0142  113 PRO B O   
5077  C CB  . PRO B  113 ? 1.4969 1.0743 1.0004 -0.4398 0.2380  0.0207  113 PRO B CB  
5078  C CG  . PRO B  113 ? 1.5482 1.1160 1.0279 -0.4554 0.2452  0.0237  113 PRO B CG  
5079  C CD  . PRO B  113 ? 1.5905 1.1507 1.0677 -0.4662 0.2487  0.0263  113 PRO B CD  
5080  N N   . VAL B  114 ? 1.5816 1.1520 1.1162 -0.4157 0.2205  0.0226  114 VAL B N   
5081  C CA  . VAL B  114 ? 1.5459 1.1273 1.1026 -0.4072 0.2168  0.0179  114 VAL B CA  
5082  C C   . VAL B  114 ? 1.4805 1.0824 1.0562 -0.3952 0.2146  0.0118  114 VAL B C   
5083  O O   . VAL B  114 ? 1.4599 1.0587 1.0303 -0.3872 0.2103  0.0142  114 VAL B O   
5084  C CB  . VAL B  114 ? 1.4960 1.0564 1.0475 -0.3999 0.2075  0.0249  114 VAL B CB  
5085  C CG1 . VAL B  114 ? 1.4597 1.0312 1.0322 -0.3863 0.2012  0.0211  114 VAL B CG1 
5086  C CG2 . VAL B  114 ? 1.5298 1.0772 1.0738 -0.4113 0.2105  0.0279  114 VAL B CG2 
5087  N N   . LEU B  115 ? 1.4909 1.1136 1.0888 -0.3944 0.2174  0.0040  115 LEU B N   
5088  C CA  . LEU B  115 ? 1.4132 1.0558 1.0316 -0.3831 0.2149  -0.0017 115 LEU B CA  
5089  C C   . LEU B  115 ? 1.4010 1.0465 1.0354 -0.3730 0.2078  -0.0025 115 LEU B C   
5090  O O   . LEU B  115 ? 1.4502 1.1040 1.0963 -0.3774 0.2102  -0.0062 115 LEU B O   
5091  C CB  . LEU B  115 ? 1.0739 0.7415 0.7073 -0.3899 0.2240  -0.0107 115 LEU B CB  
5092  C CG  . LEU B  115 ? 1.0393 0.7087 0.6593 -0.3989 0.2318  -0.0126 115 LEU B CG  
5093  C CD1 . LEU B  115 ? 1.0229 0.7180 0.6596 -0.4051 0.2409  -0.0237 115 LEU B CD1 
5094  C CD2 . LEU B  115 ? 0.9985 0.6602 0.6084 -0.3901 0.2267  -0.0091 115 LEU B CD2 
5095  N N   . ILE B  116 ? 1.1878 0.8271 0.8227 -0.3598 0.1991  0.0009  116 ILE B N   
5096  C CA  . ILE B  116 ? 1.0460 0.6889 0.6958 -0.3495 0.1922  0.0001  116 ILE B CA  
5097  C C   . ILE B  116 ? 0.9798 0.6463 0.6516 -0.3413 0.1916  -0.0061 116 ILE B C   
5098  O O   . ILE B  116 ? 0.9636 0.6344 0.6350 -0.3358 0.1908  -0.0064 116 ILE B O   
5099  C CB  . ILE B  116 ? 0.9046 0.5288 0.5441 -0.3392 0.1830  0.0069  116 ILE B CB  
5100  C CG1 . ILE B  116 ? 0.9401 0.5394 0.5579 -0.3464 0.1826  0.0139  116 ILE B CG1 
5101  C CG2 . ILE B  116 ? 0.8804 0.5094 0.5352 -0.3296 0.1765  0.0055  116 ILE B CG2 
5102  C CD1 . ILE B  116 ? 0.9415 0.5217 0.5498 -0.3368 0.1734  0.0206  116 ILE B CD1 
5103  N N   . TRP B  117 ? 0.9232 0.6046 0.6140 -0.3406 0.1918  -0.0109 117 TRP B N   
5104  C CA  . TRP B  117 ? 0.9034 0.6076 0.6165 -0.3334 0.1910  -0.0165 117 TRP B CA  
5105  C C   . TRP B  117 ? 0.8994 0.6039 0.6227 -0.3205 0.1819  -0.0149 117 TRP B C   
5106  O O   . TRP B  117 ? 0.9124 0.6091 0.6354 -0.3201 0.1784  -0.0132 117 TRP B O   
5107  C CB  . TRP B  117 ? 0.8201 0.5434 0.5493 -0.3420 0.1978  -0.0233 117 TRP B CB  
5108  C CG  . TRP B  117 ? 0.7885 0.5354 0.5430 -0.3352 0.1964  -0.0288 117 TRP B CG  
5109  C CD1 . TRP B  117 ? 0.7720 0.5300 0.5442 -0.3325 0.1933  -0.0313 117 TRP B CD1 
5110  C CD2 . TRP B  117 ? 0.8123 0.5749 0.5779 -0.3307 0.1980  -0.0324 117 TRP B CD2 
5111  N NE1 . TRP B  117 ? 0.7453 0.5245 0.5388 -0.3265 0.1924  -0.0356 117 TRP B NE1 
5112  C CE2 . TRP B  117 ? 0.7588 0.5413 0.5493 -0.3252 0.1954  -0.0365 117 TRP B CE2 
5113  C CE3 . TRP B  117 ? 0.8297 0.5915 0.5869 -0.3311 0.2013  -0.0325 117 TRP B CE3 
5114  C CZ2 . TRP B  117 ? 0.7368 0.5375 0.5439 -0.3199 0.1961  -0.0407 117 TRP B CZ2 
5115  C CZ3 . TRP B  117 ? 0.7560 0.5350 0.5274 -0.3271 0.2032  -0.0381 117 TRP B CZ3 
5116  C CH2 . TRP B  117 ? 0.7298 0.5279 0.5263 -0.3215 0.2006  -0.0421 117 TRP B CH2 
5117  N N   . ILE B  118 ? 0.7723 0.4855 0.5044 -0.3103 0.1781  -0.0156 118 ILE B N   
5118  C CA  . ILE B  118 ? 0.7467 0.4636 0.4907 -0.2985 0.1701  -0.0149 118 ILE B CA  
5119  C C   . ILE B  118 ? 0.7199 0.4612 0.4878 -0.2950 0.1708  -0.0204 118 ILE B C   
5120  O O   . ILE B  118 ? 0.7106 0.4612 0.4832 -0.2928 0.1729  -0.0224 118 ILE B O   
5121  C CB  . ILE B  118 ? 0.7404 0.4453 0.4747 -0.2882 0.1637  -0.0102 118 ILE B CB  
5122  C CG1 . ILE B  118 ? 0.7684 0.4487 0.4791 -0.2915 0.1626  -0.0043 118 ILE B CG1 
5123  C CG2 . ILE B  118 ? 0.7152 0.4244 0.4619 -0.2769 0.1558  -0.0097 118 ILE B CG2 
5124  C CD1 . ILE B  118 ? 0.7647 0.4326 0.4650 -0.2818 0.1562  0.0005  118 ILE B CD1 
5125  N N   . TYR B  119 ? 0.9145 0.6661 0.6976 -0.2945 0.1689  -0.0228 119 TYR B N   
5126  C CA  . TYR B  119 ? 0.9024 0.6777 0.7097 -0.2921 0.1693  -0.0277 119 TYR B CA  
5127  C C   . TYR B  119 ? 0.8808 0.6636 0.6990 -0.2796 0.1631  -0.0269 119 TYR B C   
5128  O O   . TYR B  119 ? 0.9067 0.6769 0.7159 -0.2716 0.1571  -0.0225 119 TYR B O   
5129  C CB  . TYR B  119 ? 0.6872 0.4712 0.5076 -0.2951 0.1681  -0.0300 119 TYR B CB  
5130  C CG  . TYR B  119 ? 0.6766 0.4496 0.4933 -0.2895 0.1608  -0.0265 119 TYR B CG  
5131  C CD1 . TYR B  119 ? 0.6517 0.4310 0.4799 -0.2788 0.1534  -0.0255 119 TYR B CD1 
5132  C CD2 . TYR B  119 ? 0.6987 0.4560 0.5016 -0.2957 0.1617  -0.0245 119 TYR B CD2 
5133  C CE1 . TYR B  119 ? 0.6492 0.4195 0.4743 -0.2744 0.1474  -0.0229 119 TYR B CE1 
5134  C CE2 . TYR B  119 ? 0.6959 0.4440 0.4965 -0.2911 0.1555  -0.0220 119 TYR B CE2 
5135  C CZ  . TYR B  119 ? 0.6713 0.4262 0.4827 -0.2806 0.1486  -0.0215 119 TYR B CZ  
5136  O OH  . TYR B  119 ? 0.6702 0.4162 0.4787 -0.2767 0.1431  -0.0195 119 TYR B OH  
5137  N N   . GLY B  120 ? 0.6390 0.4424 0.4774 -0.2782 0.1646  -0.0311 120 GLY B N   
5138  C CA  . GLY B  120 ? 0.6126 0.4250 0.4642 -0.2672 0.1589  -0.0305 120 GLY B CA  
5139  C C   . GLY B  120 ? 0.6060 0.4273 0.4736 -0.2624 0.1526  -0.0304 120 GLY B C   
5140  O O   . GLY B  120 ? 0.6417 0.4554 0.5038 -0.2651 0.1509  -0.0291 120 GLY B O   
5141  N N   . GLY B  121 ? 0.5829 0.4204 0.4705 -0.2559 0.1492  -0.0316 121 GLY B N   
5142  C CA  . GLY B  121 ? 0.5720 0.4182 0.4749 -0.2511 0.1425  -0.0309 121 GLY B CA  
5143  C C   . GLY B  121 ? 0.5765 0.4182 0.4801 -0.2397 0.1341  -0.0268 121 GLY B C   
5144  O O   . GLY B  121 ? 0.5255 0.3705 0.4370 -0.2363 0.1283  -0.0255 121 GLY B O   
5145  N N   . GLY B  122 ? 0.6489 0.4831 0.5438 -0.2341 0.1336  -0.0248 122 GLY B N   
5146  C CA  . GLY B  122 ? 0.5147 0.3478 0.4132 -0.2232 0.1264  -0.0216 122 GLY B CA  
5147  C C   . GLY B  122 ? 0.5166 0.3351 0.4027 -0.2183 0.1207  -0.0178 122 GLY B C   
5148  O O   . GLY B  122 ? 0.5001 0.3200 0.3918 -0.2098 0.1144  -0.0155 122 GLY B O   
5149  N N   . PHE B  123 ? 0.5370 0.3419 0.4070 -0.2240 0.1231  -0.0172 123 PHE B N   
5150  C CA  . PHE B  123 ? 0.5602 0.3516 0.4195 -0.2204 0.1182  -0.0143 123 PHE B CA  
5151  C C   . PHE B  123 ? 0.5618 0.3625 0.4344 -0.2193 0.1137  -0.0149 123 PHE B C   
5152  O O   . PHE B  123 ? 0.5332 0.3244 0.3984 -0.2179 0.1105  -0.0135 123 PHE B O   
5153  C CB  . PHE B  123 ? 0.5336 0.3156 0.3848 -0.2109 0.1137  -0.0110 123 PHE B CB  
5154  C CG  . PHE B  123 ? 0.5469 0.3184 0.3835 -0.2122 0.1174  -0.0100 123 PHE B CG  
5155  C CD1 . PHE B  123 ? 0.5703 0.3242 0.3874 -0.2167 0.1195  -0.0083 123 PHE B CD1 
5156  C CD2 . PHE B  123 ? 0.5371 0.3159 0.3792 -0.2092 0.1187  -0.0108 123 PHE B CD2 
5157  C CE1 . PHE B  123 ? 0.5840 0.3277 0.3869 -0.2183 0.1225  -0.0070 123 PHE B CE1 
5158  C CE2 . PHE B  123 ? 0.5503 0.3194 0.3782 -0.2109 0.1221  -0.0100 123 PHE B CE2 
5159  C CZ  . PHE B  123 ? 0.5740 0.3255 0.3819 -0.2155 0.1238  -0.0079 123 PHE B CZ  
5160  N N   . TYR B  124 ? 0.5149 0.3338 0.4070 -0.2201 0.1135  -0.0171 124 TYR B N   
5161  C CA  . TYR B  124 ? 0.5052 0.3337 0.4101 -0.2201 0.1092  -0.0176 124 TYR B CA  
5162  C C   . TYR B  124 ? 0.5182 0.3514 0.4262 -0.2303 0.1135  -0.0208 124 TYR B C   
5163  O O   . TYR B  124 ? 0.7011 0.5425 0.6195 -0.2316 0.1103  -0.0215 124 TYR B O   
5164  C CB  . TYR B  124 ? 0.4816 0.3269 0.4073 -0.2142 0.1046  -0.0172 124 TYR B CB  
5165  C CG  . TYR B  124 ? 0.4773 0.3386 0.4189 -0.2182 0.1084  -0.0201 124 TYR B CG  
5166  C CD1 . TYR B  124 ? 0.4766 0.3518 0.4333 -0.2243 0.1090  -0.0227 124 TYR B CD1 
5167  C CD2 . TYR B  124 ? 0.4738 0.3370 0.4165 -0.2159 0.1112  -0.0205 124 TYR B CD2 
5168  C CE1 . TYR B  124 ? 0.4806 0.3714 0.4534 -0.2278 0.1124  -0.0258 124 TYR B CE1 
5169  C CE2 . TYR B  124 ? 0.5212 0.3995 0.4793 -0.2195 0.1150  -0.0238 124 TYR B CE2 
5170  C CZ  . TYR B  124 ? 0.5121 0.4044 0.4856 -0.2253 0.1155  -0.0265 124 TYR B CZ  
5171  O OH  . TYR B  124 ? 0.5204 0.4288 0.5104 -0.2289 0.1193  -0.0302 124 TYR B OH  
5172  N N   . SER B  125 ? 0.5365 0.3646 0.4354 -0.2379 0.1206  -0.0226 125 SER B N   
5173  C CA  . SER B  125 ? 0.5496 0.3836 0.4524 -0.2484 0.1256  -0.0260 125 SER B CA  
5174  C C   . SER B  125 ? 0.5716 0.3976 0.4613 -0.2565 0.1337  -0.0275 125 SER B C   
5175  O O   . SER B  125 ? 0.5747 0.3942 0.4553 -0.2543 0.1359  -0.0263 125 SER B O   
5176  C CB  . SER B  125 ? 0.5347 0.3911 0.4614 -0.2495 0.1253  -0.0289 125 SER B CB  
5177  O OG  . SER B  125 ? 0.5294 0.3925 0.4612 -0.2480 0.1285  -0.0299 125 SER B OG  
5178  N N   . GLY B  126 ? 0.5874 0.4144 0.4764 -0.2664 0.1382  -0.0302 126 GLY B N   
5179  C CA  . GLY B  126 ? 0.6087 0.4314 0.4881 -0.2758 0.1465  -0.0321 126 GLY B CA  
5180  C C   . GLY B  126 ? 0.6310 0.4439 0.5003 -0.2850 0.1495  -0.0328 126 GLY B C   
5181  O O   . GLY B  126 ? 0.6283 0.4398 0.5002 -0.2842 0.1453  -0.0324 126 GLY B O   
5182  N N   . ALA B  127 ? 0.6534 0.4597 0.5114 -0.2942 0.1569  -0.0339 127 ALA B N   
5183  C CA  . ALA B  127 ? 0.6785 0.4717 0.5235 -0.3034 0.1603  -0.0337 127 ALA B CA  
5184  C C   . ALA B  127 ? 0.7012 0.4901 0.5355 -0.3133 0.1688  -0.0349 127 ALA B C   
5185  O O   . ALA B  127 ? 0.6962 0.4987 0.5393 -0.3152 0.1731  -0.0381 127 ALA B O   
5186  C CB  . ALA B  127 ? 0.6766 0.4815 0.5355 -0.3087 0.1600  -0.0372 127 ALA B CB  
5187  N N   . ALA B  128 ? 0.7269 0.4976 0.5434 -0.3202 0.1714  -0.0327 128 ALA B N   
5188  C CA  . ALA B  128 ? 0.7520 0.5178 0.5575 -0.3313 0.1797  -0.0336 128 ALA B CA  
5189  C C   . ALA B  128 ? 0.8249 0.6043 0.6425 -0.3417 0.1848  -0.0389 128 ALA B C   
5190  O O   . ALA B  128 ? 0.8330 0.6172 0.6491 -0.3515 0.1926  -0.0418 128 ALA B O   
5191  C CB  . ALA B  128 ? 0.7775 0.5177 0.5595 -0.3344 0.1797  -0.0284 128 ALA B CB  
5192  N N   . SER B  129 ? 0.7812 0.5680 0.6116 -0.3394 0.1802  -0.0403 129 SER B N   
5193  C CA  . SER B  129 ? 0.7973 0.5976 0.6411 -0.3480 0.1834  -0.0453 129 SER B CA  
5194  C C   . SER B  129 ? 0.7566 0.5815 0.6201 -0.3501 0.1874  -0.0508 129 SER B C   
5195  O O   . SER B  129 ? 0.7417 0.5800 0.6176 -0.3579 0.1908  -0.0555 129 SER B O   
5196  C CB  . SER B  129 ? 1.0033 0.8064 0.8567 -0.3433 0.1763  -0.0452 129 SER B CB  
5197  O OG  . SER B  129 ? 1.0403 0.8225 0.8781 -0.3384 0.1714  -0.0403 129 SER B OG  
5198  N N   . LEU B  130 ? 0.8590 0.6901 0.7263 -0.3430 0.1866  -0.0504 130 LEU B N   
5199  C CA  . LEU B  130 ? 0.8505 0.7057 0.7392 -0.3428 0.1890  -0.0556 130 LEU B CA  
5200  C C   . LEU B  130 ? 0.8889 0.7521 0.7784 -0.3549 0.1991  -0.0606 130 LEU B C   
5201  O O   . LEU B  130 ? 0.9128 0.7609 0.7829 -0.3628 0.2046  -0.0593 130 LEU B O   
5202  C CB  . LEU B  130 ? 0.6883 0.5468 0.5801 -0.3323 0.1861  -0.0539 130 LEU B CB  
5203  C CG  . LEU B  130 ? 0.6616 0.5241 0.5641 -0.3199 0.1765  -0.0512 130 LEU B CG  
5204  C CD1 . LEU B  130 ? 0.6404 0.5262 0.5668 -0.3160 0.1762  -0.0549 130 LEU B CD1 
5205  C CD2 . LEU B  130 ? 0.6591 0.5199 0.5655 -0.3197 0.1710  -0.0502 130 LEU B CD2 
5206  N N   . ASP B  131 ? 0.8003 0.6874 0.7127 -0.3564 0.2012  -0.0664 131 ASP B N   
5207  C CA  . ASP B  131 ? 0.8495 0.7486 0.7669 -0.3674 0.2109  -0.0725 131 ASP B CA  
5208  C C   . ASP B  131 ? 0.7857 0.6795 0.6898 -0.3695 0.2176  -0.0731 131 ASP B C   
5209  O O   . ASP B  131 ? 0.7821 0.6664 0.6700 -0.3798 0.2250  -0.0736 131 ASP B O   
5210  C CB  . ASP B  131 ? 1.1377 1.0646 1.0844 -0.3672 0.2110  -0.0792 131 ASP B CB  
5211  C CG  . ASP B  131 ? 1.2076 1.1430 1.1656 -0.3742 0.2106  -0.0818 131 ASP B CG  
5212  O OD1 . ASP B  131 ? 1.2404 1.1596 1.1837 -0.3783 0.2096  -0.0788 131 ASP B OD1 
5213  O OD2 . ASP B  131 ? 1.2032 1.1614 1.1840 -0.3766 0.2120  -0.0882 131 ASP B OD2 
5214  N N   . VAL B  132 ? 0.7846 0.6844 0.6946 -0.3608 0.2154  -0.0735 132 VAL B N   
5215  C CA  . VAL B  132 ? 0.7991 0.6967 0.6983 -0.3634 0.2224  -0.0758 132 VAL B CA  
5216  C C   . VAL B  132 ? 0.8453 0.7168 0.7149 -0.3653 0.2231  -0.0692 132 VAL B C   
5217  O O   . VAL B  132 ? 0.8730 0.7399 0.7294 -0.3704 0.2298  -0.0708 132 VAL B O   
5218  C CB  . VAL B  132 ? 0.7317 0.6391 0.6428 -0.3526 0.2189  -0.0770 132 VAL B CB  
5219  C CG1 . VAL B  132 ? 0.6896 0.6239 0.6307 -0.3519 0.2193  -0.0842 132 VAL B CG1 
5220  C CG2 . VAL B  132 ? 0.7089 0.6031 0.6150 -0.3399 0.2080  -0.0688 132 VAL B CG2 
5221  N N   . TYR B  133 ? 0.8166 0.6715 0.6766 -0.3613 0.2160  -0.0621 133 TYR B N   
5222  C CA  . TYR B  133 ? 0.8723 0.7014 0.7049 -0.3629 0.2157  -0.0557 133 TYR B CA  
5223  C C   . TYR B  133 ? 0.9008 0.7209 0.7211 -0.3766 0.2220  -0.0561 133 TYR B C   
5224  O O   . TYR B  133 ? 0.9126 0.7101 0.7113 -0.3790 0.2210  -0.0504 133 TYR B O   
5225  C CB  . TYR B  133 ? 1.0310 0.8448 0.8568 -0.3521 0.2058  -0.0492 133 TYR B CB  
5226  C CG  . TYR B  133 ? 1.0158 0.8381 0.8540 -0.3385 0.1991  -0.0485 133 TYR B CG  
5227  C CD1 . TYR B  133 ? 0.9883 0.8224 0.8338 -0.3357 0.2018  -0.0513 133 TYR B CD1 
5228  C CD2 . TYR B  133 ? 0.9999 0.8187 0.8429 -0.3290 0.1902  -0.0452 133 TYR B CD2 
5229  C CE1 . TYR B  133 ? 0.9530 0.7944 0.8103 -0.3236 0.1955  -0.0504 133 TYR B CE1 
5230  C CE2 . TYR B  133 ? 0.9523 0.7786 0.8065 -0.3173 0.1840  -0.0443 133 TYR B CE2 
5231  C CZ  . TYR B  133 ? 0.9420 0.7792 0.8034 -0.3146 0.1866  -0.0467 133 TYR B CZ  
5232  O OH  . TYR B  133 ? 0.9406 0.7845 0.8133 -0.3030 0.1802  -0.0454 133 TYR B OH  
5233  N N   . ASP B  134 ? 1.1207 0.9585 0.9556 -0.3853 0.2282  -0.0627 134 ASP B N   
5234  C CA  . ASP B  134 ? 1.1568 0.9888 0.9828 -0.3991 0.2347  -0.0639 134 ASP B CA  
5235  C C   . ASP B  134 ? 1.1689 0.9823 0.9691 -0.4057 0.2397  -0.0601 134 ASP B C   
5236  O O   . ASP B  134 ? 1.1853 1.0050 0.9829 -0.4084 0.2455  -0.0631 134 ASP B O   
5237  C CB  . ASP B  134 ? 0.9621 0.8192 0.8081 -0.4075 0.2422  -0.0728 134 ASP B CB  
5238  C CG  . ASP B  134 ? 0.9445 0.8030 0.7936 -0.4181 0.2452  -0.0750 134 ASP B CG  
5239  O OD1 . ASP B  134 ? 0.9461 0.7835 0.7758 -0.4237 0.2455  -0.0703 134 ASP B OD1 
5240  O OD2 . ASP B  134 ? 0.9136 0.7943 0.7849 -0.4211 0.2475  -0.0819 134 ASP B OD2 
5241  N N   . GLY B  135 ? 0.9872 0.7776 0.7677 -0.4094 0.2381  -0.0541 135 GLY B N   
5242  C CA  . GLY B  135 ? 1.0538 0.8230 0.8088 -0.4120 0.2394  -0.0481 135 GLY B CA  
5243  C C   . GLY B  135 ? 1.1615 0.9278 0.9040 -0.4274 0.2495  -0.0497 135 GLY B C   
5244  O O   . GLY B  135 ? 1.2054 0.9572 0.9274 -0.4308 0.2518  -0.0454 135 GLY B O   
5245  N N   . ARG B  136 ? 1.3965 1.1774 1.1518 -0.4369 0.2555  -0.0558 136 ARG B N   
5246  C CA  . ARG B  136 ? 1.3848 1.1610 1.1283 -0.4530 0.2647  -0.0569 136 ARG B CA  
5247  C C   . ARG B  136 ? 1.3455 1.1309 1.0840 -0.4613 0.2742  -0.0614 136 ARG B C   
5248  O O   . ARG B  136 ? 1.3845 1.1566 1.1028 -0.4724 0.2800  -0.0586 136 ARG B O   
5249  C CB  . ARG B  136 ? 1.2234 1.0120 0.9827 -0.4606 0.2676  -0.0623 136 ARG B CB  
5250  C CG  . ARG B  136 ? 1.2224 1.0402 1.0036 -0.4655 0.2749  -0.0724 136 ARG B CG  
5251  C CD  . ARG B  136 ? 1.2066 1.0444 1.0151 -0.4566 0.2694  -0.0770 136 ARG B CD  
5252  N NE  . ARG B  136 ? 1.2418 1.0802 1.0574 -0.4621 0.2685  -0.0781 136 ARG B NE  
5253  C CZ  . ARG B  136 ? 1.2453 1.1061 1.0860 -0.4616 0.2681  -0.0847 136 ARG B CZ  
5254  N NH1 . ARG B  136 ? 1.2318 1.1154 1.0923 -0.4563 0.2687  -0.0908 136 ARG B NH1 
5255  N NH2 . ARG B  136 ? 1.2468 1.1071 1.0927 -0.4670 0.2671  -0.0856 136 ARG B NH2 
5256  N N   . PHE B  137 ? 0.9716 0.7790 0.7271 -0.4572 0.2765  -0.0692 137 PHE B N   
5257  C CA  . PHE B  137 ? 0.9849 0.8031 0.7369 -0.4661 0.2867  -0.0758 137 PHE B CA  
5258  C C   . PHE B  137 ? 1.0031 0.8017 0.7283 -0.4670 0.2872  -0.0696 137 PHE B C   
5259  O O   . PHE B  137 ? 1.0321 0.8269 0.7421 -0.4798 0.2958  -0.0708 137 PHE B O   
5260  C CB  . PHE B  137 ? 1.1844 1.0291 0.9613 -0.4595 0.2879  -0.0850 137 PHE B CB  
5261  C CG  . PHE B  137 ? 1.2334 1.0993 1.0373 -0.4597 0.2879  -0.0916 137 PHE B CG  
5262  C CD1 . PHE B  137 ? 1.2515 1.1174 1.0684 -0.4488 0.2778  -0.0880 137 PHE B CD1 
5263  C CD2 . PHE B  137 ? 1.2699 1.1562 1.0864 -0.4710 0.2978  -0.1016 137 PHE B CD2 
5264  C CE1 . PHE B  137 ? 1.2510 1.1364 1.0925 -0.4492 0.2773  -0.0938 137 PHE B CE1 
5265  C CE2 . PHE B  137 ? 1.2788 1.1850 1.1209 -0.4711 0.2974  -0.1076 137 PHE B CE2 
5266  C CZ  . PHE B  137 ? 1.2563 1.1617 1.1105 -0.4602 0.2869  -0.1034 137 PHE B CZ  
5267  N N   . LEU B  138 ? 1.1097 0.8957 0.8290 -0.4539 0.2779  -0.0628 138 LEU B N   
5268  C CA  . LEU B  138 ? 1.1525 0.9183 0.8462 -0.4536 0.2768  -0.0559 138 LEU B CA  
5269  C C   . LEU B  138 ? 1.1799 0.9221 0.8500 -0.4634 0.2777  -0.0479 138 LEU B C   
5270  O O   . LEU B  138 ? 1.1971 0.9288 0.8462 -0.4722 0.2828  -0.0455 138 LEU B O   
5271  C CB  . LEU B  138 ? 1.2280 0.9845 0.9216 -0.4369 0.2655  -0.0498 138 LEU B CB  
5272  C CG  . LEU B  138 ? 1.1779 0.9476 0.8811 -0.4277 0.2646  -0.0544 138 LEU B CG  
5273  C CD1 . LEU B  138 ? 1.1977 0.9690 0.8870 -0.4369 0.2734  -0.0580 138 LEU B CD1 
5274  C CD2 . LEU B  138 ? 1.1243 0.9201 0.8573 -0.4232 0.2653  -0.0631 138 LEU B CD2 
5275  N N   . ALA B  139 ? 1.2155 0.9492 0.8892 -0.4617 0.2725  -0.0436 139 ALA B N   
5276  C CA  . ALA B  139 ? 1.2877 0.9991 0.9416 -0.4710 0.2732  -0.0363 139 ALA B CA  
5277  C C   . ALA B  139 ? 1.3933 1.1097 1.0399 -0.4890 0.2851  -0.0405 139 ALA B C   
5278  O O   . ALA B  139 ? 1.4158 1.1186 1.0399 -0.4975 0.2892  -0.0363 139 ALA B O   
5279  C CB  . ALA B  139 ? 1.2126 0.9171 0.8736 -0.4679 0.2674  -0.0343 139 ALA B CB  
5280  N N   . GLN B  140 ? 1.6431 1.3793 1.3087 -0.4952 0.2908  -0.0489 140 GLN B N   
5281  C CA  . GLN B  140 ? 1.6704 1.4137 1.3317 -0.5128 0.3026  -0.0541 140 GLN B CA  
5282  C C   . GLN B  140 ? 1.6916 1.4419 1.3429 -0.5196 0.3109  -0.0585 140 GLN B C   
5283  O O   . GLN B  140 ? 1.7447 1.4824 1.3741 -0.5318 0.3166  -0.0550 140 GLN B O   
5284  C CB  . GLN B  140 ? 1.4172 1.1848 1.1047 -0.5163 0.3067  -0.0638 140 GLN B CB  
5285  C CG  . GLN B  140 ? 1.4268 1.2061 1.1134 -0.5342 0.3196  -0.0711 140 GLN B CG  
5286  C CD  . GLN B  140 ? 1.3965 1.2012 1.0957 -0.5360 0.3273  -0.0822 140 GLN B CD  
5287  O OE1 . GLN B  140 ? 1.3456 1.1709 1.0692 -0.5269 0.3250  -0.0891 140 GLN B OE1 
5288  N NE2 . GLN B  140 ? 1.4156 1.2190 1.0984 -0.5480 0.3365  -0.0842 140 GLN B NE2 
5289  N N   . VAL B  141 ? 1.3359 1.1062 1.0034 -0.5119 0.3113  -0.0661 141 VAL B N   
5290  C CA  . VAL B  141 ? 1.1216 0.9028 0.7838 -0.5184 0.3199  -0.0724 141 VAL B CA  
5291  C C   . VAL B  141 ? 1.1388 0.8987 0.7735 -0.5178 0.3177  -0.0642 141 VAL B C   
5292  O O   . VAL B  141 ? 1.1697 0.9250 0.7863 -0.5307 0.3256  -0.0644 141 VAL B O   
5293  C CB  . VAL B  141 ? 1.0882 0.8965 0.7765 -0.5099 0.3208  -0.0830 141 VAL B CB  
5294  C CG1 . VAL B  141 ? 1.0939 0.9079 0.7738 -0.5122 0.3266  -0.0874 141 VAL B CG1 
5295  C CG2 . VAL B  141 ? 1.0834 0.9162 0.7957 -0.5167 0.3276  -0.0935 141 VAL B CG2 
5296  N N   . GLU B  142 ? 1.1403 0.8875 0.7716 -0.5033 0.3070  -0.0571 142 GLU B N   
5297  C CA  . GLU B  142 ? 1.2166 0.9452 0.8231 -0.5023 0.3047  -0.0498 142 GLU B CA  
5298  C C   . GLU B  142 ? 1.2039 0.9023 0.7872 -0.5034 0.2984  -0.0367 142 GLU B C   
5299  O O   . GLU B  142 ? 1.2079 0.8890 0.7705 -0.5015 0.2949  -0.0293 142 GLU B O   
5300  C CB  . GLU B  142 ? 1.4735 1.2080 1.0879 -0.4875 0.2986  -0.0511 142 GLU B CB  
5301  C CG  . GLU B  142 ? 1.5056 1.2672 1.1367 -0.4891 0.3065  -0.0638 142 GLU B CG  
5302  C CD  . GLU B  142 ? 1.5571 1.3205 1.1710 -0.5035 0.3172  -0.0675 142 GLU B CD  
5303  O OE1 . GLU B  142 ? 1.5921 1.3347 1.1796 -0.5067 0.3155  -0.0591 142 GLU B OE1 
5304  O OE2 . GLU B  142 ? 1.5431 1.3293 1.1704 -0.5116 0.3271  -0.0789 142 GLU B OE2 
5305  N N   . GLY B  143 ? 1.1911 0.8836 0.7788 -0.5063 0.2969  -0.0339 143 GLY B N   
5306  C CA  . GLY B  143 ? 1.2244 0.8889 0.7921 -0.5085 0.2917  -0.0221 143 GLY B CA  
5307  C C   . GLY B  143 ? 1.2002 0.8485 0.7647 -0.4923 0.2790  -0.0137 143 GLY B C   
5308  O O   . GLY B  143 ? 1.2048 0.8300 0.7475 -0.4922 0.2747  -0.0039 143 GLY B O   
5309  N N   . ALA B  144 ? 1.1496 0.8102 0.7362 -0.4787 0.2729  -0.0174 144 ALA B N   
5310  C CA  . ALA B  144 ? 1.1380 0.7874 0.7239 -0.4628 0.2615  -0.0114 144 ALA B CA  
5311  C C   . ALA B  144 ? 1.1524 0.7932 0.7459 -0.4567 0.2544  -0.0088 144 ALA B C   
5312  O O   . ALA B  144 ? 1.0930 0.7479 0.7044 -0.4586 0.2566  -0.0148 144 ALA B O   
5313  C CB  . ALA B  144 ? 1.0797 0.7482 0.6814 -0.4519 0.2601  -0.0178 144 ALA B CB  
5314  N N   . VAL B  145 ? 1.5074 1.1253 1.0873 -0.4495 0.2458  -0.0001 145 VAL B N   
5315  C CA  . VAL B  145 ? 1.5595 1.1697 1.1475 -0.4413 0.2380  0.0021  145 VAL B CA  
5316  C C   . VAL B  145 ? 1.5252 1.1476 1.1297 -0.4251 0.2310  -0.0008 145 VAL B C   
5317  O O   . VAL B  145 ? 1.5058 1.1221 1.1029 -0.4165 0.2263  0.0028  145 VAL B O   
5318  C CB  . VAL B  145 ? 1.5587 1.1387 1.1260 -0.4409 0.2318  0.0126  145 VAL B CB  
5319  C CG1 . VAL B  145 ? 1.5419 1.1161 1.1195 -0.4317 0.2240  0.0137  145 VAL B CG1 
5320  C CG2 . VAL B  145 ? 1.6214 1.1879 1.1720 -0.4573 0.2384  0.0163  145 VAL B CG2 
5321  N N   . LEU B  146 ? 1.3188 0.9584 0.9455 -0.4211 0.2304  -0.0070 146 LEU B N   
5322  C CA  . LEU B  146 ? 1.2474 0.9032 0.8925 -0.4075 0.2254  -0.0110 146 LEU B CA  
5323  C C   . LEU B  146 ? 1.2203 0.8738 0.8766 -0.3976 0.2172  -0.0102 146 LEU B C   
5324  O O   . LEU B  146 ? 1.2189 0.8797 0.8869 -0.4015 0.2187  -0.0137 146 LEU B O   
5325  C CB  . LEU B  146 ? 1.1976 0.8813 0.8622 -0.4111 0.2325  -0.0204 146 LEU B CB  
5326  C CG  . LEU B  146 ? 1.1942 0.8961 0.8776 -0.3983 0.2285  -0.0245 146 LEU B CG  
5327  C CD1 . LEU B  146 ? 1.2024 0.9170 0.8863 -0.4008 0.2347  -0.0285 146 LEU B CD1 
5328  C CD2 . LEU B  146 ? 1.1869 0.9081 0.8949 -0.3965 0.2281  -0.0308 146 LEU B CD2 
5329  N N   . VAL B  147 ? 1.3103 0.9542 0.9630 -0.3851 0.2088  -0.0057 147 VAL B N   
5330  C CA  . VAL B  147 ? 1.2234 0.8640 0.8850 -0.3752 0.2007  -0.0046 147 VAL B CA  
5331  C C   . VAL B  147 ? 1.1189 0.7796 0.8008 -0.3635 0.1970  -0.0093 147 VAL B C   
5332  O O   . VAL B  147 ? 1.0822 0.7499 0.7653 -0.3582 0.1968  -0.0099 147 VAL B O   
5333  C CB  . VAL B  147 ? 0.9534 0.5691 0.5982 -0.3684 0.1931  0.0037  147 VAL B CB  
5334  C CG1 . VAL B  147 ? 0.9514 0.5590 0.6009 -0.3652 0.1879  0.0049  147 VAL B CG1 
5335  C CG2 . VAL B  147 ? 0.9899 0.5860 0.6116 -0.3781 0.1964  0.0096  147 VAL B CG2 
5336  N N   . SER B  148 ? 0.8879 0.5578 0.5858 -0.3600 0.1940  -0.0123 148 SER B N   
5337  C CA  . SER B  148 ? 0.8530 0.5389 0.5692 -0.3481 0.1889  -0.0153 148 SER B CA  
5338  C C   . SER B  148 ? 0.9202 0.6001 0.6413 -0.3411 0.1815  -0.0137 148 SER B C   
5339  O O   . SER B  148 ? 0.8523 0.5308 0.5762 -0.3473 0.1827  -0.0149 148 SER B O   
5340  C CB  . SER B  148 ? 0.8374 0.5494 0.5741 -0.3516 0.1940  -0.0228 148 SER B CB  
5341  O OG  . SER B  148 ? 0.8432 0.5611 0.5886 -0.3590 0.1964  -0.0260 148 SER B OG  
5342  N N   . MET B  149 ? 0.9145 0.5912 0.6366 -0.3286 0.1741  -0.0111 149 MET B N   
5343  C CA  . MET B  149 ? 0.8733 0.5439 0.5991 -0.3215 0.1670  -0.0096 149 MET B CA  
5344  C C   . MET B  149 ? 0.8254 0.5148 0.5712 -0.3118 0.1624  -0.0130 149 MET B C   
5345  O O   . MET B  149 ? 0.7630 0.4664 0.5177 -0.3076 0.1629  -0.0150 149 MET B O   
5346  C CB  . MET B  149 ? 0.8599 0.5085 0.5695 -0.3149 0.1613  -0.0031 149 MET B CB  
5347  C CG  . MET B  149 ? 0.8180 0.4709 0.5322 -0.3015 0.1551  -0.0021 149 MET B CG  
5348  S SD  . MET B  149 ? 0.8248 0.4873 0.5379 -0.3007 0.1588  -0.0030 149 MET B SD  
5349  C CE  . MET B  149 ? 0.8170 0.4538 0.5050 -0.3003 0.1567  0.0043  149 MET B CE  
5350  N N   . ASN B  150 ? 0.8249 0.5141 0.5775 -0.3090 0.1581  -0.0136 150 ASN B N   
5351  C CA  . ASN B  150 ? 0.7440 0.4470 0.5127 -0.2992 0.1524  -0.0155 150 ASN B CA  
5352  C C   . ASN B  150 ? 0.7379 0.4277 0.4984 -0.2886 0.1456  -0.0111 150 ASN B C   
5353  O O   . ASN B  150 ? 0.7646 0.4355 0.5117 -0.2895 0.1440  -0.0076 150 ASN B O   
5354  C CB  . ASN B  150 ? 0.8519 0.5616 0.6315 -0.3023 0.1513  -0.0185 150 ASN B CB  
5355  C CG  . ASN B  150 ? 0.8560 0.5827 0.6479 -0.3116 0.1571  -0.0235 150 ASN B CG  
5356  O OD1 . ASN B  150 ? 0.8614 0.6007 0.6597 -0.3130 0.1608  -0.0257 150 ASN B OD1 
5357  N ND2 . ASN B  150 ? 0.8460 0.5736 0.6421 -0.3181 0.1579  -0.0258 150 ASN B ND2 
5358  N N   . TYR B  151 ? 0.7134 0.4130 0.4823 -0.2786 0.1415  -0.0112 151 TYR B N   
5359  C CA  . TYR B  151 ? 0.7036 0.3941 0.4684 -0.2678 0.1345  -0.0079 151 TYR B CA  
5360  C C   . TYR B  151 ? 0.6761 0.3828 0.4586 -0.2607 0.1299  -0.0104 151 TYR B C   
5361  O O   . TYR B  151 ? 0.6633 0.3882 0.4606 -0.2629 0.1318  -0.0139 151 TYR B O   
5362  C CB  . TYR B  151 ? 0.7014 0.3869 0.4579 -0.2621 0.1336  -0.0050 151 TYR B CB  
5363  C CG  . TYR B  151 ? 0.7369 0.4408 0.5055 -0.2603 0.1357  -0.0078 151 TYR B CG  
5364  C CD1 . TYR B  151 ? 0.7418 0.4530 0.5114 -0.2692 0.1428  -0.0103 151 TYR B CD1 
5365  C CD2 . TYR B  151 ? 0.6568 0.3710 0.4365 -0.2499 0.1308  -0.0080 151 TYR B CD2 
5366  C CE1 . TYR B  151 ? 0.6761 0.4044 0.4580 -0.2676 0.1450  -0.0132 151 TYR B CE1 
5367  C CE2 . TYR B  151 ? 0.6406 0.3713 0.4326 -0.2484 0.1326  -0.0105 151 TYR B CE2 
5368  C CZ  . TYR B  151 ? 0.6504 0.3881 0.4436 -0.2572 0.1398  -0.0132 151 TYR B CZ  
5369  O OH  . TYR B  151 ? 0.6353 0.3895 0.4415 -0.2559 0.1419  -0.0160 151 TYR B OH  
5370  N N   . ARG B  152 ? 0.6681 0.3683 0.4493 -0.2527 0.1238  -0.0085 152 ARG B N   
5371  C CA  . ARG B  152 ? 0.6436 0.3577 0.4399 -0.2462 0.1190  -0.0104 152 ARG B CA  
5372  C C   . ARG B  152 ? 0.6205 0.3499 0.4282 -0.2397 0.1176  -0.0109 152 ARG B C   
5373  O O   . ARG B  152 ? 0.6205 0.3457 0.4218 -0.2363 0.1180  -0.0089 152 ARG B O   
5374  C CB  . ARG B  152 ? 0.6417 0.3445 0.4328 -0.2391 0.1132  -0.0083 152 ARG B CB  
5375  C CG  . ARG B  152 ? 0.6876 0.3839 0.4773 -0.2442 0.1131  -0.0096 152 ARG B CG  
5376  C CD  . ARG B  152 ? 0.6556 0.3385 0.4384 -0.2376 0.1082  -0.0074 152 ARG B CD  
5377  N NE  . ARG B  152 ? 0.6749 0.3385 0.4418 -0.2374 0.1088  -0.0035 152 ARG B NE  
5378  C CZ  . ARG B  152 ? 0.6794 0.3292 0.4390 -0.2315 0.1046  -0.0009 152 ARG B CZ  
5379  N NH1 . ARG B  152 ? 0.6656 0.3190 0.4322 -0.2254 0.1002  -0.0022 152 ARG B NH1 
5380  N NH2 . ARG B  152 ? 0.6983 0.3308 0.4440 -0.2318 0.1048  0.0030  152 ARG B NH2 
5381  N N   . VAL B  153 ? 0.6550 0.4020 0.4799 -0.2383 0.1157  -0.0134 153 VAL B N   
5382  C CA  . VAL B  153 ? 0.6327 0.3939 0.4700 -0.2317 0.1136  -0.0135 153 VAL B CA  
5383  C C   . VAL B  153 ? 0.6045 0.3739 0.4530 -0.2241 0.1069  -0.0132 153 VAL B C   
5384  O O   . VAL B  153 ? 0.5900 0.3548 0.4365 -0.2242 0.1043  -0.0134 153 VAL B O   
5385  C CB  . VAL B  153 ? 0.5753 0.3530 0.4258 -0.2376 0.1181  -0.0166 153 VAL B CB  
5386  C CG1 . VAL B  153 ? 0.5947 0.3652 0.4340 -0.2445 0.1249  -0.0169 153 VAL B CG1 
5387  C CG2 . VAL B  153 ? 0.5755 0.3634 0.4371 -0.2438 0.1184  -0.0196 153 VAL B CG2 
5388  N N   . GLY B  154 ? 0.5795 0.3609 0.4396 -0.2178 0.1044  -0.0128 154 GLY B N   
5389  C CA  . GLY B  154 ? 0.5684 0.3586 0.4397 -0.2108 0.0980  -0.0122 154 GLY B CA  
5390  C C   . GLY B  154 ? 0.5196 0.2966 0.3799 -0.2046 0.0940  -0.0100 154 GLY B C   
5391  O O   . GLY B  154 ? 0.5299 0.2930 0.3763 -0.2026 0.0949  -0.0082 154 GLY B O   
5392  N N   . THR B  155 ? 0.5104 0.2921 0.3770 -0.2017 0.0893  -0.0102 155 THR B N   
5393  C CA  . THR B  155 ? 0.5082 0.2794 0.3665 -0.1957 0.0854  -0.0087 155 THR B CA  
5394  C C   . THR B  155 ? 0.5310 0.2841 0.3730 -0.1997 0.0881  -0.0086 155 THR B C   
5395  O O   . THR B  155 ? 0.6164 0.3567 0.4477 -0.1950 0.0867  -0.0066 155 THR B O   
5396  C CB  . THR B  155 ? 0.4959 0.2760 0.3638 -0.1940 0.0808  -0.0096 155 THR B CB  
5397  O OG1 . THR B  155 ? 0.5054 0.2883 0.3756 -0.2023 0.0828  -0.0122 155 THR B OG1 
5398  C CG2 . THR B  155 ? 0.4746 0.2714 0.3586 -0.1900 0.0776  -0.0089 155 THR B CG2 
5399  N N   . PHE B  156 ? 0.6209 0.3730 0.4617 -0.2087 0.0919  -0.0106 156 PHE B N   
5400  C CA  . PHE B  156 ? 0.5683 0.3035 0.3952 -0.2136 0.0944  -0.0104 156 PHE B CA  
5401  C C   . PHE B  156 ? 0.6143 0.3358 0.4278 -0.2130 0.0968  -0.0078 156 PHE B C   
5402  O O   . PHE B  156 ? 0.6193 0.3246 0.4209 -0.2117 0.0958  -0.0059 156 PHE B O   
5403  C CB  . PHE B  156 ? 0.5806 0.3191 0.4101 -0.2239 0.0985  -0.0132 156 PHE B CB  
5404  C CG  . PHE B  156 ? 0.5846 0.3394 0.4290 -0.2252 0.0962  -0.0158 156 PHE B CG  
5405  C CD1 . PHE B  156 ? 0.5650 0.3183 0.4101 -0.2243 0.0929  -0.0170 156 PHE B CD1 
5406  C CD2 . PHE B  156 ? 0.5820 0.3540 0.4401 -0.2275 0.0973  -0.0172 156 PHE B CD2 
5407  C CE1 . PHE B  156 ? 0.5533 0.3214 0.4112 -0.2259 0.0905  -0.0192 156 PHE B CE1 
5408  C CE2 . PHE B  156 ? 0.5434 0.3304 0.4157 -0.2288 0.0945  -0.0191 156 PHE B CE2 
5409  C CZ  . PHE B  156 ? 0.5604 0.3454 0.4320 -0.2282 0.0910  -0.0200 156 PHE B CZ  
5410  N N   . GLY B  157 ? 0.6180 0.3458 0.4336 -0.2145 0.0998  -0.0076 157 GLY B N   
5411  C CA  . GLY B  157 ? 0.6461 0.3620 0.4490 -0.2139 0.1019  -0.0051 157 GLY B CA  
5412  C C   . GLY B  157 ? 0.6630 0.3760 0.4634 -0.2038 0.0976  -0.0026 157 GLY B C   
5413  O O   . GLY B  157 ? 0.7079 0.4057 0.4953 -0.2015 0.0967  0.0001  157 GLY B O   
5414  N N   . PHE B  158 ? 0.6143 0.3420 0.4277 -0.1980 0.0950  -0.0033 158 PHE B N   
5415  C CA  . PHE B  158 ? 0.5828 0.3090 0.3946 -0.1890 0.0915  -0.0011 158 PHE B CA  
5416  C C   . PHE B  158 ? 0.5979 0.3279 0.4161 -0.1799 0.0854  -0.0004 158 PHE B C   
5417  O O   . PHE B  158 ? 0.5195 0.2479 0.3361 -0.1728 0.0828  0.0013  158 PHE B O   
5418  C CB  . PHE B  158 ? 0.5555 0.2901 0.3717 -0.1894 0.0944  -0.0014 158 PHE B CB  
5419  C CG  . PHE B  158 ? 0.5594 0.2890 0.3674 -0.1986 0.1008  -0.0021 158 PHE B CG  
5420  C CD1 . PHE B  158 ? 0.5616 0.3013 0.3780 -0.2064 0.1049  -0.0049 158 PHE B CD1 
5421  C CD2 . PHE B  158 ? 0.7598 0.4745 0.5517 -0.1998 0.1026  0.0002  158 PHE B CD2 
5422  C CE1 . PHE B  158 ? 0.5994 0.3349 0.4083 -0.2153 0.1110  -0.0057 158 PHE B CE1 
5423  C CE2 . PHE B  158 ? 0.5963 0.3063 0.3800 -0.2088 0.1085  -0.0003 158 PHE B CE2 
5424  C CZ  . PHE B  158 ? 0.5980 0.3184 0.3902 -0.2166 0.1130  -0.0033 158 PHE B CZ  
5425  N N   . LEU B  159 ? 0.5216 0.2569 0.3468 -0.1803 0.0832  -0.0019 159 LEU B N   
5426  C CA  . LEU B  159 ? 0.5056 0.2447 0.3364 -0.1725 0.0778  -0.0014 159 LEU B CA  
5427  C C   . LEU B  159 ? 0.5146 0.2381 0.3331 -0.1678 0.0757  0.0005  159 LEU B C   
5428  O O   . LEU B  159 ? 0.5329 0.2433 0.3413 -0.1714 0.0770  0.0007  159 LEU B O   
5429  C CB  . LEU B  159 ? 0.5014 0.2470 0.3395 -0.1750 0.0762  -0.0035 159 LEU B CB  
5430  C CG  . LEU B  159 ? 0.4867 0.2364 0.3301 -0.1684 0.0710  -0.0033 159 LEU B CG  
5431  C CD1 . LEU B  159 ? 0.4762 0.2398 0.3318 -0.1712 0.0695  -0.0051 159 LEU B CD1 
5432  C CD2 . LEU B  159 ? 0.4981 0.2338 0.3313 -0.1670 0.0699  -0.0033 159 LEU B CD2 
5433  N N   . ALA B  160 ? 0.5117 0.2366 0.3316 -0.1597 0.0723  0.0020  160 ALA B N   
5434  C CA  . ALA B  160 ? 0.5111 0.2217 0.3201 -0.1550 0.0701  0.0039  160 ALA B CA  
5435  C C   . ALA B  160 ? 0.4968 0.2121 0.3120 -0.1469 0.0652  0.0041  160 ALA B C   
5436  O O   . ALA B  160 ? 0.4761 0.2044 0.3018 -0.1431 0.0634  0.0038  160 ALA B O   
5437  C CB  . ALA B  160 ? 0.5180 0.2219 0.3187 -0.1538 0.0714  0.0060  160 ALA B CB  
5438  N N   . LEU B  161 ? 0.6287 0.3328 0.4375 -0.1444 0.0631  0.0045  161 LEU B N   
5439  C CA  . LEU B  161 ? 0.6146 0.3203 0.4267 -0.1364 0.0588  0.0049  161 LEU B CA  
5440  C C   . LEU B  161 ? 0.6874 0.3786 0.4886 -0.1331 0.0577  0.0073  161 LEU B C   
5441  O O   . LEU B  161 ? 0.7457 0.4244 0.5405 -0.1331 0.0568  0.0077  161 LEU B O   
5442  C CB  . LEU B  161 ? 0.4916 0.1962 0.3062 -0.1368 0.0573  0.0030  161 LEU B CB  
5443  C CG  . LEU B  161 ? 0.4767 0.1964 0.3026 -0.1386 0.0569  0.0009  161 LEU B CG  
5444  C CD1 . LEU B  161 ? 0.6758 0.3937 0.5031 -0.1371 0.0548  -0.0008 161 LEU B CD1 
5445  C CD2 . LEU B  161 ? 0.4566 0.1894 0.2916 -0.1337 0.0548  0.0018  161 LEU B CD2 
5446  N N   . PRO B  162 ? 0.6549 0.3474 0.4542 -0.1306 0.0578  0.0090  162 PRO B N   
5447  C CA  . PRO B  162 ? 0.6772 0.3556 0.4645 -0.1289 0.0572  0.0116  162 PRO B CA  
5448  C C   . PRO B  162 ? 0.6535 0.3228 0.4382 -0.1229 0.0529  0.0126  162 PRO B C   
5449  O O   . PRO B  162 ? 0.5712 0.2485 0.3641 -0.1170 0.0499  0.0117  162 PRO B O   
5450  C CB  . PRO B  162 ? 0.7804 0.4665 0.5702 -0.1257 0.0571  0.0123  162 PRO B CB  
5451  C CG  . PRO B  162 ? 0.7623 0.4638 0.5632 -0.1290 0.0596  0.0103  162 PRO B CG  
5452  C CD  . PRO B  162 ? 0.7402 0.4477 0.5491 -0.1290 0.0582  0.0085  162 PRO B CD  
5453  N N   . GLY B  163 ? 0.8248 0.4773 0.5986 -0.1247 0.0527  0.0144  163 GLY B N   
5454  C CA  . GLY B  163 ? 0.8729 0.5154 0.6450 -0.1195 0.0486  0.0153  163 GLY B CA  
5455  C C   . GLY B  163 ? 0.9053 0.5426 0.6793 -0.1225 0.0490  0.0136  163 GLY B C   
5456  O O   . GLY B  163 ? 0.9671 0.5939 0.7398 -0.1194 0.0461  0.0141  163 GLY B O   
5457  N N   . SER B  164 ? 0.5958 0.2401 0.3733 -0.1288 0.0525  0.0114  164 SER B N   
5458  C CA  . SER B  164 ? 0.6128 0.2531 0.3924 -0.1325 0.0532  0.0092  164 SER B CA  
5459  C C   . SER B  164 ? 0.5868 0.2118 0.3566 -0.1394 0.0557  0.0106  164 SER B C   
5460  O O   . SER B  164 ? 0.5936 0.2164 0.3566 -0.1439 0.0585  0.0123  164 SER B O   
5461  C CB  . SER B  164 ? 1.0261 0.6822 0.8151 -0.1360 0.0553  0.0059  164 SER B CB  
5462  O OG  . SER B  164 ? 1.1104 0.7671 0.8965 -0.1440 0.0595  0.0056  164 SER B OG  
5463  N N   . ARG B  165 ? 0.6877 0.3018 0.4570 -0.1402 0.0546  0.0098  165 ARG B N   
5464  C CA  . ARG B  165 ? 0.7925 0.3911 0.5537 -0.1470 0.0566  0.0110  165 ARG B CA  
5465  C C   . ARG B  165 ? 0.7499 0.3559 0.5123 -0.1557 0.0615  0.0088  165 ARG B C   
5466  O O   . ARG B  165 ? 0.6417 0.2394 0.3961 -0.1624 0.0645  0.0105  165 ARG B O   
5467  C CB  . ARG B  165 ? 1.3122 0.8991 1.0756 -0.1457 0.0543  0.0097  165 ARG B CB  
5468  C CG  . ARG B  165 ? 1.4280 0.9991 1.1871 -0.1399 0.0499  0.0128  165 ARG B CG  
5469  C CD  . ARG B  165 ? 1.5481 1.1046 1.3091 -0.1413 0.0486  0.0115  165 ARG B CD  
5470  N NE  . ARG B  165 ? 1.6382 1.1822 1.3917 -0.1498 0.0515  0.0129  165 ARG B NE  
5471  C CZ  . ARG B  165 ? 1.6404 1.1870 1.3965 -0.1570 0.0551  0.0096  165 ARG B CZ  
5472  N NH1 . ARG B  165 ? 1.6210 1.1826 1.3867 -0.1568 0.0560  0.0049  165 ARG B NH1 
5473  N NH2 . ARG B  165 ? 1.6400 1.1744 1.3891 -0.1648 0.0576  0.0112  165 ARG B NH2 
5474  N N   . GLU B  166 ? 0.7909 0.4121 0.5633 -0.1559 0.0620  0.0052  166 GLU B N   
5475  C CA  . GLU B  166 ? 0.8031 0.4317 0.5786 -0.1640 0.0659  0.0024  166 GLU B CA  
5476  C C   . GLU B  166 ? 0.7642 0.4084 0.5435 -0.1667 0.0685  0.0020  166 GLU B C   
5477  O O   . GLU B  166 ? 0.7773 0.4274 0.5593 -0.1738 0.0717  -0.0001 166 GLU B O   
5478  C CB  . GLU B  166 ? 1.1015 0.7357 0.8852 -0.1641 0.0649  -0.0015 166 GLU B CB  
5479  C CG  . GLU B  166 ? 1.2489 0.8667 1.0297 -0.1650 0.0639  -0.0022 166 GLU B CG  
5480  C CD  . GLU B  166 ? 1.3555 0.9739 1.1423 -0.1578 0.0600  -0.0040 166 GLU B CD  
5481  O OE1 . GLU B  166 ? 1.3544 0.9869 1.1473 -0.1528 0.0585  -0.0046 166 GLU B OE1 
5482  O OE2 . GLU B  166 ? 1.4102 1.0150 1.1963 -0.1572 0.0585  -0.0048 166 GLU B OE2 
5483  N N   . ALA B  167 ? 0.7794 0.4307 0.5602 -0.1610 0.0670  0.0036  167 ALA B N   
5484  C CA  . ALA B  167 ? 0.7475 0.4109 0.5315 -0.1636 0.0696  0.0035  167 ALA B CA  
5485  C C   . ALA B  167 ? 0.7465 0.4070 0.5250 -0.1592 0.0689  0.0065  167 ALA B C   
5486  O O   . ALA B  167 ? 0.7087 0.3797 0.4936 -0.1533 0.0668  0.0066  167 ALA B O   
5487  C CB  . ALA B  167 ? 0.7276 0.4096 0.5245 -0.1619 0.0686  0.0011  167 ALA B CB  
5488  N N   . PRO B  168 ? 0.7736 0.4191 0.5400 -0.1624 0.0704  0.0091  168 PRO B N   
5489  C CA  . PRO B  168 ? 0.7681 0.4071 0.5266 -0.1588 0.0693  0.0123  168 PRO B CA  
5490  C C   . PRO B  168 ? 0.7181 0.3688 0.4794 -0.1604 0.0722  0.0118  168 PRO B C   
5491  O O   . PRO B  168 ? 0.7079 0.3596 0.4674 -0.1555 0.0707  0.0133  168 PRO B O   
5492  C CB  . PRO B  168 ? 0.9583 0.5781 0.7031 -0.1643 0.0709  0.0150  168 PRO B CB  
5493  C CG  . PRO B  168 ? 0.9834 0.5996 0.7301 -0.1703 0.0726  0.0131  168 PRO B CG  
5494  C CD  . PRO B  168 ? 0.9296 0.5643 0.6892 -0.1711 0.0738  0.0092  168 PRO B CD  
5495  N N   . GLY B  169 ? 0.6338 0.2932 0.4000 -0.1675 0.0763  0.0096  169 GLY B N   
5496  C CA  . GLY B  169 ? 0.6200 0.2906 0.3902 -0.1700 0.0796  0.0088  169 GLY B CA  
5497  C C   . GLY B  169 ? 0.6349 0.2959 0.3934 -0.1774 0.0841  0.0103  169 GLY B C   
5498  O O   . GLY B  169 ? 0.6188 0.2629 0.3644 -0.1793 0.0839  0.0129  169 GLY B O   
5499  N N   . ASN B  170 ? 0.6369 0.3089 0.4003 -0.1819 0.0883  0.0086  170 ASN B N   
5500  C CA  . ASN B  170 ? 0.6760 0.3419 0.4297 -0.1900 0.0935  0.0093  170 ASN B CA  
5501  C C   . ASN B  170 ? 0.7240 0.3787 0.4697 -0.1986 0.0964  0.0096  170 ASN B C   
5502  O O   . ASN B  170 ? 0.6562 0.3010 0.3903 -0.2053 0.1001  0.0112  170 ASN B O   
5503  C CB  . ASN B  170 ? 0.6221 0.2763 0.3628 -0.1872 0.0925  0.0126  170 ASN B CB  
5504  C CG  . ASN B  170 ? 0.6010 0.2641 0.3484 -0.1783 0.0892  0.0125  170 ASN B CG  
5505  O OD1 . ASN B  170 ? 0.5827 0.2617 0.3426 -0.1772 0.0905  0.0100  170 ASN B OD1 
5506  N ND2 . ASN B  170 ? 0.6356 0.2880 0.3752 -0.1718 0.0847  0.0154  170 ASN B ND2 
5507  N N   . VAL B  171 ? 0.6320 0.2886 0.3841 -0.1990 0.0950  0.0080  171 VAL B N   
5508  C CA  . VAL B  171 ? 0.6548 0.2994 0.3993 -0.2069 0.0974  0.0084  171 VAL B CA  
5509  C C   . VAL B  171 ? 0.6642 0.3147 0.4094 -0.2173 0.1039  0.0064  171 VAL B C   
5510  O O   . VAL B  171 ? 0.6880 0.3264 0.4230 -0.2251 0.1071  0.0077  171 VAL B O   
5511  C CB  . VAL B  171 ? 0.6515 0.2952 0.4018 -0.2053 0.0944  0.0068  171 VAL B CB  
5512  C CG1 . VAL B  171 ? 0.6377 0.2801 0.3904 -0.1947 0.0884  0.0079  171 VAL B CG1 
5513  C CG2 . VAL B  171 ? 0.6378 0.2985 0.4020 -0.2088 0.0962  0.0027  171 VAL B CG2 
5514  N N   . GLY B  172 ? 0.6465 0.3153 0.4038 -0.2175 0.1059  0.0035  172 GLY B N   
5515  C CA  . GLY B  172 ? 0.6545 0.3302 0.4135 -0.2270 0.1123  0.0014  172 GLY B CA  
5516  C C   . GLY B  172 ? 0.7118 0.3765 0.4562 -0.2314 0.1160  0.0039  172 GLY B C   
5517  O O   . GLY B  172 ? 0.7338 0.3940 0.4716 -0.2413 0.1214  0.0037  172 GLY B O   
5518  N N   . LEU B  173 ? 0.7943 0.4543 0.5331 -0.2242 0.1129  0.0065  173 LEU B N   
5519  C CA  . LEU B  173 ? 0.7991 0.4476 0.5227 -0.2277 0.1155  0.0093  173 LEU B CA  
5520  C C   . LEU B  173 ? 0.8264 0.4536 0.5342 -0.2321 0.1150  0.0131  173 LEU B C   
5521  O O   . LEU B  173 ? 0.8593 0.4771 0.5549 -0.2403 0.1192  0.0150  173 LEU B O   
5522  C CB  . LEU B  173 ? 0.6765 0.3243 0.3979 -0.2185 0.1116  0.0112  173 LEU B CB  
5523  C CG  . LEU B  173 ? 0.6524 0.3188 0.3873 -0.2146 0.1124  0.0082  173 LEU B CG  
5524  C CD1 . LEU B  173 ? 0.6454 0.3073 0.3755 -0.2060 0.1082  0.0106  173 LEU B CD1 
5525  C CD2 . LEU B  173 ? 0.6599 0.3340 0.3953 -0.2236 0.1198  0.0058  173 LEU B CD2 
5526  N N   . LEU B  174 ? 0.7144 0.3342 0.4230 -0.2269 0.1099  0.0144  174 LEU B N   
5527  C CA  . LEU B  174 ? 0.7403 0.3396 0.4360 -0.2304 0.1088  0.0180  174 LEU B CA  
5528  C C   . LEU B  174 ? 0.7575 0.3551 0.4523 -0.2417 0.1142  0.0166  174 LEU B C   
5529  O O   . LEU B  174 ? 0.7846 0.3655 0.4663 -0.2481 0.1156  0.0200  174 LEU B O   
5530  C CB  . LEU B  174 ? 0.7902 0.3840 0.4896 -0.2222 0.1025  0.0188  174 LEU B CB  
5531  C CG  . LEU B  174 ? 0.7187 0.3123 0.4181 -0.2112 0.0970  0.0206  174 LEU B CG  
5532  C CD1 . LEU B  174 ? 0.7189 0.3032 0.4193 -0.2050 0.0914  0.0218  174 LEU B CD1 
5533  C CD2 . LEU B  174 ? 0.7356 0.3172 0.4202 -0.2124 0.0973  0.0247  174 LEU B CD2 
5534  N N   . ASP B  175 ? 0.8058 0.4207 0.5147 -0.2443 0.1168  0.0117  175 ASP B N   
5535  C CA  . ASP B  175 ? 0.8246 0.4411 0.5345 -0.2554 0.1223  0.0095  175 ASP B CA  
5536  C C   . ASP B  175 ? 0.7733 0.3877 0.4737 -0.2636 0.1283  0.0105  175 ASP B C   
5537  O O   . ASP B  175 ? 0.7993 0.4021 0.4896 -0.2731 0.1320  0.0122  175 ASP B O   
5538  C CB  . ASP B  175 ? 0.7350 0.3728 0.4632 -0.2561 0.1237  0.0041  175 ASP B CB  
5539  C CG  . ASP B  175 ? 0.7745 0.4146 0.5116 -0.2496 0.1183  0.0028  175 ASP B CG  
5540  O OD1 . ASP B  175 ? 0.8063 0.4305 0.5356 -0.2475 0.1151  0.0054  175 ASP B OD1 
5541  O OD2 . ASP B  175 ? 0.7183 0.3762 0.4704 -0.2467 0.1173  -0.0007 175 ASP B OD2 
5542  N N   . GLN B  176 ? 0.7593 0.3846 0.4629 -0.2604 0.1292  0.0095  176 GLN B N   
5543  C CA  . GLN B  176 ? 0.7758 0.3989 0.4695 -0.2681 0.1350  0.0104  176 GLN B CA  
5544  C C   . GLN B  176 ? 0.8045 0.4040 0.4773 -0.2706 0.1339  0.0165  176 GLN B C   
5545  O O   . GLN B  176 ? 0.8302 0.4210 0.4921 -0.2811 0.1389  0.0181  176 GLN B O   
5546  C CB  . GLN B  176 ? 0.7560 0.3933 0.4564 -0.2631 0.1356  0.0084  176 GLN B CB  
5547  C CG  . GLN B  176 ? 0.7335 0.3942 0.4535 -0.2636 0.1384  0.0026  176 GLN B CG  
5548  C CD  . GLN B  176 ? 0.7116 0.3848 0.4396 -0.2563 0.1373  0.0012  176 GLN B CD  
5549  O OE1 . GLN B  176 ? 0.7163 0.3810 0.4336 -0.2530 0.1360  0.0041  176 GLN B OE1 
5550  N NE2 . GLN B  176 ? 0.8182 0.5112 0.5654 -0.2537 0.1374  -0.0030 176 GLN B NE2 
5551  N N   . ARG B  177 ? 0.8956 0.4848 0.5633 -0.2612 0.1273  0.0202  177 ARG B N   
5552  C CA  . ARG B  177 ? 0.9466 0.5141 0.5955 -0.2623 0.1252  0.0264  177 ARG B CA  
5553  C C   . ARG B  177 ? 1.0065 0.5580 0.6476 -0.2699 0.1260  0.0291  177 ARG B C   
5554  O O   . ARG B  177 ? 1.0663 0.6041 0.6925 -0.2782 0.1289  0.0330  177 ARG B O   
5555  C CB  . ARG B  177 ? 0.8157 0.3765 0.4634 -0.2500 0.1173  0.0293  177 ARG B CB  
5556  C CG  . ARG B  177 ? 0.8426 0.3800 0.4724 -0.2503 0.1138  0.0361  177 ARG B CG  
5557  C CD  . ARG B  177 ? 0.8307 0.3631 0.4617 -0.2381 0.1059  0.0383  177 ARG B CD  
5558  N NE  . ARG B  177 ? 0.8138 0.3560 0.4462 -0.2322 0.1050  0.0374  177 ARG B NE  
5559  C CZ  . ARG B  177 ? 0.7997 0.3435 0.4366 -0.2210 0.0988  0.0378  177 ARG B CZ  
5560  N NH1 . ARG B  177 ? 0.7936 0.3306 0.4344 -0.2145 0.0932  0.0389  177 ARG B NH1 
5561  N NH2 . ARG B  177 ? 0.7823 0.3348 0.4204 -0.2164 0.0984  0.0369  177 ARG B NH2 
5562  N N   . LEU B  178 ? 0.8826 0.4357 0.5336 -0.2673 0.1236  0.0270  178 LEU B N   
5563  C CA  . LEU B  178 ? 0.9053 0.4440 0.5512 -0.2743 0.1244  0.0289  178 LEU B CA  
5564  C C   . LEU B  178 ? 0.8858 0.4272 0.5287 -0.2878 0.1323  0.0273  178 LEU B C   
5565  O O   . LEU B  178 ? 0.9154 0.4400 0.5461 -0.2958 0.1341  0.0312  178 LEU B O   
5566  C CB  . LEU B  178 ? 0.8536 0.3970 0.5127 -0.2698 0.1212  0.0257  178 LEU B CB  
5567  C CG  . LEU B  178 ? 0.8773 0.4070 0.5328 -0.2775 0.1225  0.0268  178 LEU B CG  
5568  C CD1 . LEU B  178 ? 0.9021 0.4070 0.5435 -0.2761 0.1182  0.0335  178 LEU B CD1 
5569  C CD2 . LEU B  178 ? 0.8602 0.3986 0.5303 -0.2740 0.1203  0.0223  178 LEU B CD2 
5570  N N   . ALA B  179 ? 0.8682 0.4307 0.5229 -0.2904 0.1370  0.0217  179 ALA B N   
5571  C CA  . ALA B  179 ? 0.8839 0.4510 0.5365 -0.3032 0.1450  0.0197  179 ALA B CA  
5572  C C   . ALA B  179 ? 0.9290 0.4831 0.5632 -0.3090 0.1477  0.0245  179 ALA B C   
5573  O O   . ALA B  179 ? 0.9632 0.5080 0.5875 -0.3204 0.1525  0.0264  179 ALA B O   
5574  C CB  . ALA B  179 ? 0.8597 0.4521 0.5283 -0.3036 0.1489  0.0131  179 ALA B CB  
5575  N N   . LEU B  180 ? 1.0969 0.6498 0.7261 -0.3015 0.1444  0.0268  180 LEU B N   
5576  C CA  . LEU B  180 ? 1.1219 0.6622 0.7328 -0.3064 0.1462  0.0318  180 LEU B CA  
5577  C C   . LEU B  180 ? 1.1703 0.6841 0.7641 -0.3092 0.1429  0.0394  180 LEU B C   
5578  O O   . LEU B  180 ? 1.2304 0.7330 0.8094 -0.3192 0.1469  0.0431  180 LEU B O   
5579  C CB  . LEU B  180 ? 0.9760 0.5223 0.5865 -0.2975 0.1433  0.0320  180 LEU B CB  
5580  C CG  . LEU B  180 ? 0.9171 0.4833 0.5346 -0.3004 0.1493  0.0269  180 LEU B CG  
5581  C CD1 . LEU B  180 ? 0.8790 0.4646 0.5140 -0.3048 0.1544  0.0200  180 LEU B CD1 
5582  C CD2 . LEU B  180 ? 0.8695 0.4441 0.4931 -0.2886 0.1448  0.0260  180 LEU B CD2 
5583  N N   . GLN B  181 ? 0.9523 0.4559 0.5485 -0.3008 0.1358  0.0417  181 GLN B N   
5584  C CA  . GLN B  181 ? 0.9826 0.4609 0.5647 -0.3031 0.1322  0.0488  181 GLN B CA  
5585  C C   . GLN B  181 ? 1.0267 0.4984 0.6074 -0.3147 0.1369  0.0488  181 GLN B C   
5586  O O   . GLN B  181 ? 1.1026 0.5545 0.6685 -0.3219 0.1373  0.0549  181 GLN B O   
5587  C CB  . GLN B  181 ? 1.2811 0.7511 0.8680 -0.2912 0.1236  0.0507  181 GLN B CB  
5588  C CG  . GLN B  181 ? 1.3537 0.8288 0.9420 -0.2795 0.1184  0.0511  181 GLN B CG  
5589  C CD  . GLN B  181 ? 1.4129 0.8839 1.0094 -0.2679 0.1107  0.0513  181 GLN B CD  
5590  O OE1 . GLN B  181 ? 1.4793 0.9361 1.0747 -0.2688 0.1082  0.0537  181 GLN B OE1 
5591  N NE2 . GLN B  181 ? 1.3687 0.8524 0.9740 -0.2572 0.1072  0.0486  181 GLN B NE2 
5592  N N   . TRP B  182 ? 1.2604 0.7483 0.8565 -0.3167 0.1403  0.0421  182 TRP B N   
5593  C CA  . TRP B  182 ? 1.2807 0.7653 0.8767 -0.3287 0.1457  0.0410  182 TRP B CA  
5594  C C   . TRP B  182 ? 1.2862 0.7719 0.8715 -0.3409 0.1533  0.0418  182 TRP B C   
5595  O O   . TRP B  182 ? 1.3394 0.8118 0.9148 -0.3516 0.1568  0.0450  182 TRP B O   
5596  C CB  . TRP B  182 ? 1.1889 0.6934 0.8042 -0.3285 0.1479  0.0331  182 TRP B CB  
5597  C CG  . TRP B  182 ? 1.1945 0.6972 0.8111 -0.3409 0.1535  0.0313  182 TRP B CG  
5598  C CD1 . TRP B  182 ? 1.2024 0.6962 0.8231 -0.3424 0.1516  0.0311  182 TRP B CD1 
5599  C CD2 . TRP B  182 ? 1.1954 0.7060 0.8100 -0.3538 0.1621  0.0289  182 TRP B CD2 
5600  N NE1 . TRP B  182 ? 1.2189 0.7141 0.8399 -0.3553 0.1582  0.0290  182 TRP B NE1 
5601  C CE2 . TRP B  182 ? 1.1909 0.6965 0.8082 -0.3625 0.1647  0.0276  182 TRP B CE2 
5602  C CE3 . TRP B  182 ? 1.1718 0.6933 0.7827 -0.3590 0.1679  0.0274  182 TRP B CE3 
5603  C CZ2 . TRP B  182 ? 1.1505 0.6619 0.7672 -0.3761 0.1730  0.0250  182 TRP B CZ2 
5604  C CZ3 . TRP B  182 ? 1.1515 0.6789 0.7619 -0.3725 0.1763  0.0247  182 TRP B CZ3 
5605  C CH2 . TRP B  182 ? 1.1419 0.6644 0.7551 -0.3809 0.1787  0.0236  182 TRP B CH2 
5606  N N   . VAL B  183 ? 1.0946 0.5962 0.6821 -0.3397 0.1564  0.0387  183 VAL B N   
5607  C CA  . VAL B  183 ? 1.1259 0.6290 0.7032 -0.3517 0.1641  0.0391  183 VAL B CA  
5608  C C   . VAL B  183 ? 1.1726 0.6532 0.7275 -0.3546 0.1622  0.0478  183 VAL B C   
5609  O O   . VAL B  183 ? 1.2059 0.6797 0.7481 -0.3667 0.1680  0.0503  183 VAL B O   
5610  C CB  . VAL B  183 ? 1.1962 0.7235 0.7832 -0.3508 0.1687  0.0328  183 VAL B CB  
5611  C CG1 . VAL B  183 ? 1.1919 0.7152 0.7673 -0.3467 0.1670  0.0363  183 VAL B CG1 
5612  C CG2 . VAL B  183 ? 1.2155 0.7529 0.8037 -0.3648 0.1784  0.0287  183 VAL B CG2 
5613  N N   . GLN B  184 ? 1.2264 0.6953 0.7766 -0.3438 0.1540  0.0525  184 GLN B N   
5614  C CA  . GLN B  184 ? 1.2299 0.6769 0.7593 -0.3455 0.1510  0.0613  184 GLN B CA  
5615  C C   . GLN B  184 ? 1.2401 0.6634 0.7593 -0.3520 0.1495  0.0678  184 GLN B C   
5616  O O   . GLN B  184 ? 1.2292 0.6353 0.7299 -0.3599 0.1505  0.0748  184 GLN B O   
5617  C CB  . GLN B  184 ? 1.1218 0.5651 0.6507 -0.3315 0.1426  0.0639  184 GLN B CB  
5618  C CG  . GLN B  184 ? 1.1339 0.5602 0.6423 -0.3326 0.1399  0.0719  184 GLN B CG  
5619  C CD  . GLN B  184 ? 1.1357 0.5740 0.6380 -0.3380 0.1459  0.0698  184 GLN B CD  
5620  O OE1 . GLN B  184 ? 1.1042 0.5592 0.6136 -0.3454 0.1539  0.0637  184 GLN B OE1 
5621  N NE2 . GLN B  184 ? 1.1599 0.5901 0.6494 -0.3343 0.1421  0.0747  184 GLN B NE2 
5622  N N   . GLU B  185 ? 1.1451 0.5671 0.6763 -0.3487 0.1468  0.0656  185 GLU B N   
5623  C CA  . GLU B  185 ? 1.1883 0.5896 0.7130 -0.3554 0.1461  0.0705  185 GLU B CA  
5624  C C   . GLU B  185 ? 1.1977 0.6031 0.7221 -0.3703 0.1550  0.0679  185 GLU B C   
5625  O O   . GLU B  185 ? 1.2580 0.6460 0.7679 -0.3807 0.1573  0.0739  185 GLU B O   
5626  C CB  . GLU B  185 ? 1.4134 0.8118 0.9517 -0.3463 0.1400  0.0687  185 GLU B CB  
5627  C CG  . GLU B  185 ? 1.4861 0.8754 1.0240 -0.3324 0.1306  0.0723  185 GLU B CG  
5628  C CD  . GLU B  185 ? 1.5416 0.9371 1.0972 -0.3225 0.1259  0.0676  185 GLU B CD  
5629  O OE1 . GLU B  185 ? 1.5696 0.9750 1.1367 -0.3268 0.1297  0.0619  185 GLU B OE1 
5630  O OE2 . GLU B  185 ? 1.5446 0.9352 1.1024 -0.3108 0.1186  0.0694  185 GLU B OE2 
5631  N N   . ASN B  186 ? 1.1364 0.5646 0.6770 -0.3715 0.1598  0.0592  186 ASN B N   
5632  C CA  . ASN B  186 ? 1.1495 0.5827 0.6936 -0.3845 0.1674  0.0556  186 ASN B CA  
5633  C C   . ASN B  186 ? 1.1541 0.6027 0.6963 -0.3959 0.1770  0.0517  186 ASN B C   
5634  O O   . ASN B  186 ? 1.1671 0.6191 0.7121 -0.4073 0.1834  0.0489  186 ASN B O   
5635  C CB  . ASN B  186 ? 1.3902 0.8354 0.9541 -0.3805 0.1663  0.0488  186 ASN B CB  
5636  C CG  . ASN B  186 ? 1.4358 0.8644 1.0016 -0.3721 0.1582  0.0523  186 ASN B CG  
5637  O OD1 . ASN B  186 ? 1.5000 0.9089 1.0589 -0.3782 0.1575  0.0569  186 ASN B OD1 
5638  N ND2 . ASN B  186 ? 1.3976 0.8340 0.9733 -0.3583 0.1519  0.0501  186 ASN B ND2 
5639  N N   . ILE B  187 ? 1.3894 0.8478 0.9277 -0.3934 0.1784  0.0510  187 ILE B N   
5640  C CA  . ILE B  187 ? 1.3867 0.8628 0.9265 -0.4034 0.1878  0.0457  187 ILE B CA  
5641  C C   . ILE B  187 ? 1.4237 0.8849 0.9445 -0.4185 0.1936  0.0512  187 ILE B C   
5642  O O   . ILE B  187 ? 1.4223 0.8948 0.9450 -0.4303 0.2023  0.0468  187 ILE B O   
5643  C CB  . ILE B  187 ? 1.1200 0.6132 0.6635 -0.3966 0.1883  0.0423  187 ILE B CB  
5644  C CG1 . ILE B  187 ? 1.1125 0.6291 0.6653 -0.4051 0.1978  0.0343  187 ILE B CG1 
5645  C CG2 . ILE B  187 ? 1.1402 0.6182 0.6632 -0.3969 0.1864  0.0497  187 ILE B CG2 
5646  C CD1 . ILE B  187 ? 1.1053 0.6342 0.6742 -0.4102 0.2016  0.0280  187 ILE B CD1 
5647  N N   . ALA B  188 ? 1.3703 0.8061 0.8731 -0.4182 0.1886  0.0608  188 ALA B N   
5648  C CA  . ALA B  188 ? 1.3932 0.8113 0.8754 -0.4320 0.1928  0.0678  188 ALA B CA  
5649  C C   . ALA B  188 ? 1.4242 0.8431 0.9097 -0.4455 0.1999  0.0652  188 ALA B C   
5650  O O   . ALA B  188 ? 1.2932 0.7165 0.7712 -0.4588 0.2084  0.0643  188 ALA B O   
5651  C CB  . ALA B  188 ? 1.3136 0.7028 0.7799 -0.4279 0.1845  0.0787  188 ALA B CB  
5652  N N   . ALA B  189 ? 1.2658 0.6818 0.7635 -0.4420 0.1966  0.0635  189 ALA B N   
5653  C CA  . ALA B  189 ? 1.3095 0.7262 0.8126 -0.4538 0.2024  0.0606  189 ALA B CA  
5654  C C   . ALA B  189 ? 1.2961 0.7402 0.8119 -0.4613 0.2118  0.0507  189 ALA B C   
5655  O O   . ALA B  189 ? 1.2936 0.7397 0.8120 -0.4734 0.2182  0.0482  189 ALA B O   
5656  C CB  . ALA B  189 ? 1.2697 0.6805 0.7856 -0.4466 0.1964  0.0596  189 ALA B CB  
5657  N N   . PHE B  190 ? 1.2544 0.7197 0.7793 -0.4541 0.2125  0.0450  190 PHE B N   
5658  C CA  . PHE B  190 ? 1.2517 0.7435 0.7893 -0.4604 0.2210  0.0357  190 PHE B CA  
5659  C C   . PHE B  190 ? 1.2694 0.7637 0.7930 -0.4696 0.2279  0.0368  190 PHE B C   
5660  O O   . PHE B  190 ? 1.2313 0.7473 0.7636 -0.4753 0.2355  0.0294  190 PHE B O   
5661  C CB  . PHE B  190 ? 1.1946 0.7094 0.7532 -0.4473 0.2178  0.0281  190 PHE B CB  
5662  C CG  . PHE B  190 ? 1.2053 0.7206 0.7786 -0.4394 0.2119  0.0260  190 PHE B CG  
5663  C CD1 . PHE B  190 ? 1.1541 0.6528 0.7237 -0.4282 0.2026  0.0315  190 PHE B CD1 
5664  C CD2 . PHE B  190 ? 1.2042 0.7365 0.7951 -0.4436 0.2158  0.0184  190 PHE B CD2 
5665  C CE1 . PHE B  190 ? 1.1384 0.6377 0.7212 -0.4215 0.1976  0.0292  190 PHE B CE1 
5666  C CE2 . PHE B  190 ? 1.1313 0.6639 0.7350 -0.4370 0.2104  0.0164  190 PHE B CE2 
5667  C CZ  . PHE B  190 ? 1.1272 0.6433 0.7266 -0.4261 0.2015  0.0217  190 PHE B CZ  
5668  N N   . GLY B  191 ? 1.3878 0.8601 0.8900 -0.4707 0.2249  0.0462  191 GLY B N   
5669  C CA  . GLY B  191 ? 1.4365 0.9085 0.9225 -0.4798 0.2309  0.0483  191 GLY B CA  
5670  C C   . GLY B  191 ? 1.4311 0.9186 0.9213 -0.4703 0.2297  0.0448  191 GLY B C   
5671  O O   . GLY B  191 ? 1.4523 0.9501 0.9368 -0.4774 0.2366  0.0422  191 GLY B O   
5672  N N   . GLY B  192 ? 1.4597 0.9494 0.9605 -0.4544 0.2212  0.0441  192 GLY B N   
5673  C CA  . GLY B  192 ? 1.4384 0.9386 0.9417 -0.4441 0.2184  0.0424  192 GLY B CA  
5674  C C   . GLY B  192 ? 1.4506 0.9277 0.9336 -0.4394 0.2114  0.0524  192 GLY B C   
5675  O O   . GLY B  192 ? 1.4637 0.9181 0.9369 -0.4391 0.2060  0.0600  192 GLY B O   
5676  N N   . ASP B  193 ? 1.3324 0.8152 0.8096 -0.4359 0.2114  0.0523  193 ASP B N   
5677  C CA  . ASP B  193 ? 1.3290 0.7917 0.7875 -0.4310 0.2045  0.0615  193 ASP B CA  
5678  C C   . ASP B  193 ? 1.2381 0.7020 0.7074 -0.4132 0.1947  0.0613  193 ASP B C   
5679  O O   . ASP B  193 ? 1.1828 0.6665 0.6659 -0.4055 0.1950  0.0546  193 ASP B O   
5680  C CB  . ASP B  193 ? 1.5554 1.0228 1.0002 -0.4374 0.2097  0.0619  193 ASP B CB  
5681  C CG  . ASP B  193 ? 1.6301 1.0741 1.0517 -0.4359 0.2034  0.0727  193 ASP B CG  
5682  O OD1 . ASP B  193 ? 1.6302 1.0572 1.0495 -0.4264 0.1939  0.0789  193 ASP B OD1 
5683  O OD2 . ASP B  193 ? 1.6800 1.1228 1.0856 -0.4443 0.2079  0.0749  193 ASP B OD2 
5684  N N   . PRO B  194 ? 1.2148 0.6578 0.6785 -0.4067 0.1861  0.0684  194 PRO B N   
5685  C CA  . PRO B  194 ? 1.2181 0.6595 0.6896 -0.3901 0.1764  0.0692  194 PRO B CA  
5686  C C   . PRO B  194 ? 1.2494 0.6915 0.7123 -0.3838 0.1733  0.0714  194 PRO B C   
5687  O O   . PRO B  194 ? 1.2127 0.6594 0.6850 -0.3701 0.1666  0.0700  194 PRO B O   
5688  C CB  . PRO B  194 ? 1.2026 0.6179 0.6653 -0.3883 0.1692  0.0777  194 PRO B CB  
5689  C CG  . PRO B  194 ? 1.2267 0.6370 0.6873 -0.4017 0.1755  0.0778  194 PRO B CG  
5690  C CD  . PRO B  194 ? 1.2403 0.6614 0.6933 -0.4147 0.1854  0.0752  194 PRO B CD  
5691  N N   . MET B  195 ? 1.4364 0.8738 0.8814 -0.3938 0.1780  0.0748  195 MET B N   
5692  C CA  . MET B  195 ? 1.4544 0.8933 0.8905 -0.3892 0.1758  0.0765  195 MET B CA  
5693  C C   . MET B  195 ? 1.4476 0.9119 0.8926 -0.3918 0.1837  0.0677  195 MET B C   
5694  O O   . MET B  195 ? 1.4210 0.8890 0.8608 -0.3877 0.1824  0.0680  195 MET B O   
5695  C CB  . MET B  195 ? 1.3981 0.8137 0.8075 -0.3965 0.1740  0.0871  195 MET B CB  
5696  C CG  . MET B  195 ? 1.3856 0.7766 0.7870 -0.3886 0.1632  0.0963  195 MET B CG  
5697  S SD  . MET B  195 ? 2.1813 1.5421 1.5542 -0.4016 0.1626  0.1092  195 MET B SD  
5698  C CE  . MET B  195 ? 1.3292 0.7020 0.6942 -0.4209 0.1766  0.1053  195 MET B CE  
5699  N N   . SER B  196 ? 1.4630 0.9445 0.9216 -0.3986 0.1917  0.0600  196 SER B N   
5700  C CA  . SER B  196 ? 1.4705 0.9786 0.9445 -0.3976 0.1977  0.0503  196 SER B CA  
5701  C C   . SER B  196 ? 1.4636 0.9884 0.9636 -0.3891 0.1964  0.0429  196 SER B C   
5702  O O   . SER B  196 ? 1.4675 0.9983 0.9765 -0.3955 0.2008  0.0392  196 SER B O   
5703  C CB  . SER B  196 ? 1.4458 0.9637 0.9147 -0.4137 0.2094  0.0464  196 SER B CB  
5704  O OG  . SER B  196 ? 1.4181 0.9626 0.9043 -0.4124 0.2152  0.0365  196 SER B OG  
5705  N N   . VAL B  197 ? 1.4506 0.9836 0.9624 -0.3751 0.1904  0.0406  197 VAL B N   
5706  C CA  . VAL B  197 ? 1.4092 0.9588 0.9454 -0.3663 0.1885  0.0339  197 VAL B CA  
5707  C C   . VAL B  197 ? 1.3560 0.9257 0.9055 -0.3585 0.1890  0.0279  197 VAL B C   
5708  O O   . VAL B  197 ? 1.3122 0.8774 0.8574 -0.3494 0.1833  0.0306  197 VAL B O   
5709  C CB  . VAL B  197 ? 1.1415 0.6776 0.6806 -0.3555 0.1787  0.0382  197 VAL B CB  
5710  C CG1 . VAL B  197 ? 1.0947 0.6471 0.6553 -0.3421 0.1742  0.0328  197 VAL B CG1 
5711  C CG2 . VAL B  197 ? 1.1440 0.6709 0.6826 -0.3629 0.1801  0.0397  197 VAL B CG2 
5712  N N   . THR B  198 ? 1.4215 1.0135 0.9879 -0.3622 0.1959  0.0195  198 THR B N   
5713  C CA  . THR B  198 ? 1.4046 1.0170 0.9864 -0.3551 0.1969  0.0133  198 THR B CA  
5714  C C   . THR B  198 ? 1.4004 1.0293 1.0074 -0.3467 0.1944  0.0076  198 THR B C   
5715  O O   . THR B  198 ? 1.4148 1.0563 1.0342 -0.3528 0.1996  0.0025  198 THR B O   
5716  C CB  . THR B  198 ? 1.1973 0.8223 0.7761 -0.3672 0.2077  0.0071  198 THR B CB  
5717  O OG1 . THR B  198 ? 1.2279 0.8370 0.7813 -0.3740 0.2092  0.0122  198 THR B OG1 
5718  C CG2 . THR B  198 ? 1.1429 0.7888 0.7383 -0.3612 0.2097  -0.0011 198 THR B CG2 
5719  N N   . LEU B  199 ? 1.1055 0.7347 0.7200 -0.3330 0.1864  0.0088  199 LEU B N   
5720  C CA  . LEU B  199 ? 1.0303 0.6748 0.6679 -0.3243 0.1832  0.0042  199 LEU B CA  
5721  C C   . LEU B  199 ? 0.9960 0.6646 0.6511 -0.3235 0.1881  -0.0032 199 LEU B C   
5722  O O   . LEU B  199 ? 0.8435 0.5145 0.4951 -0.3205 0.1885  -0.0041 199 LEU B O   
5723  C CB  . LEU B  199 ? 0.8520 0.4889 0.4909 -0.3101 0.1733  0.0079  199 LEU B CB  
5724  C CG  . LEU B  199 ? 0.8707 0.4834 0.4932 -0.3081 0.1669  0.0154  199 LEU B CG  
5725  C CD1 . LEU B  199 ? 1.0423 0.6509 0.6668 -0.2941 0.1581  0.0180  199 LEU B CD1 
5726  C CD2 . LEU B  199 ? 0.8749 0.4847 0.5028 -0.3111 0.1665  0.0152  199 LEU B CD2 
5727  N N   . PHE B  200 ? 0.8370 0.5227 0.5102 -0.3267 0.1921  -0.0092 200 PHE B N   
5728  C CA  . PHE B  200 ? 0.8199 0.5282 0.5117 -0.3245 0.1957  -0.0167 200 PHE B CA  
5729  C C   . PHE B  200 ? 0.7835 0.5070 0.5000 -0.3159 0.1910  -0.0193 200 PHE B C   
5730  O O   . PHE B  200 ? 0.7858 0.5082 0.5069 -0.3183 0.1900  -0.0192 200 PHE B O   
5731  C CB  . PHE B  200 ? 0.8319 0.5509 0.5221 -0.3384 0.2072  -0.0235 200 PHE B CB  
5732  C CG  . PHE B  200 ? 0.8381 0.5661 0.5382 -0.3469 0.2120  -0.0270 200 PHE B CG  
5733  C CD1 . PHE B  200 ? 0.8525 0.5670 0.5454 -0.3500 0.2094  -0.0217 200 PHE B CD1 
5734  C CD2 . PHE B  200 ? 0.8309 0.5810 0.5478 -0.3525 0.2196  -0.0361 200 PHE B CD2 
5735  C CE1 . PHE B  200 ? 0.8592 0.5821 0.5611 -0.3585 0.2141  -0.0253 200 PHE B CE1 
5736  C CE2 . PHE B  200 ? 0.8374 0.5967 0.5639 -0.3609 0.2242  -0.0398 200 PHE B CE2 
5737  C CZ  . PHE B  200 ? 0.8515 0.5971 0.5701 -0.3640 0.2214  -0.0343 200 PHE B CZ  
5738  N N   . GLY B  201 ? 0.8295 0.5653 0.5595 -0.3073 0.1887  -0.0224 201 GLY B N   
5739  C CA  . GLY B  201 ? 0.8151 0.5650 0.5681 -0.2988 0.1837  -0.0242 201 GLY B CA  
5740  C C   . GLY B  201 ? 0.7988 0.5689 0.5700 -0.2958 0.1863  -0.0308 201 GLY B C   
5741  O O   . GLY B  201 ? 0.8094 0.5816 0.5753 -0.2978 0.1910  -0.0338 201 GLY B O   
5742  N N   . GLU B  202 ? 0.6860 0.4713 0.4793 -0.2912 0.1833  -0.0332 202 GLU B N   
5743  C CA  . GLU B  202 ? 0.6655 0.4704 0.4785 -0.2879 0.1850  -0.0391 202 GLU B CA  
5744  C C   . GLU B  202 ? 0.6602 0.4695 0.4880 -0.2746 0.1753  -0.0360 202 GLU B C   
5745  O O   . GLU B  202 ? 0.6306 0.4351 0.4605 -0.2705 0.1687  -0.0316 202 GLU B O   
5746  C CB  . GLU B  202 ? 0.6682 0.4914 0.4967 -0.2969 0.1922  -0.0463 202 GLU B CB  
5747  C CG  . GLU B  202 ? 0.7246 0.5679 0.5718 -0.2959 0.1964  -0.0538 202 GLU B CG  
5748  C CD  . GLU B  202 ? 0.6635 0.5214 0.5356 -0.2867 0.1895  -0.0540 202 GLU B CD  
5749  O OE1 . GLU B  202 ? 0.6493 0.5039 0.5249 -0.2833 0.1828  -0.0495 202 GLU B OE1 
5750  O OE2 . GLU B  202 ? 0.6334 0.5059 0.5217 -0.2831 0.1907  -0.0587 202 GLU B OE2 
5751  N N   . SER B  203 ? 0.7425 0.5608 0.5801 -0.2684 0.1746  -0.0384 203 SER B N   
5752  C CA  . SER B  203 ? 0.6725 0.4965 0.5251 -0.2562 0.1658  -0.0358 203 SER B CA  
5753  C C   . SER B  203 ? 0.6664 0.4731 0.5064 -0.2479 0.1571  -0.0280 203 SER B C   
5754  O O   . SER B  203 ? 0.6676 0.4600 0.4899 -0.2464 0.1568  -0.0252 203 SER B O   
5755  C CB  . SER B  203 ? 0.6405 0.4812 0.5161 -0.2560 0.1636  -0.0380 203 SER B CB  
5756  O OG  . SER B  203 ? 0.6198 0.4702 0.5127 -0.2459 0.1570  -0.0371 203 SER B OG  
5757  N N   . ALA B  204 ? 0.6030 0.4108 0.4513 -0.2433 0.1507  -0.0256 204 ALA B N   
5758  C CA  . ALA B  204 ? 0.5810 0.3716 0.4155 -0.2379 0.1443  -0.0205 204 ALA B CA  
5759  C C   . ALA B  204 ? 0.6482 0.4200 0.4593 -0.2451 0.1476  -0.0183 204 ALA B C   
5760  O O   . ALA B  204 ? 0.6168 0.3722 0.4122 -0.2409 0.1439  -0.0140 204 ALA B O   
5761  C CB  . ALA B  204 ? 0.5702 0.3655 0.4157 -0.2354 0.1392  -0.0200 204 ALA B CB  
5762  N N   . GLY B  205 ? 0.7419 0.5164 0.5514 -0.2559 0.1543  -0.0210 205 GLY B N   
5763  C CA  . GLY B  205 ? 0.7560 0.5135 0.5439 -0.2643 0.1582  -0.0190 205 GLY B CA  
5764  C C   . GLY B  205 ? 0.7566 0.5042 0.5289 -0.2639 0.1599  -0.0169 205 GLY B C   
5765  O O   . GLY B  205 ? 0.7557 0.4843 0.5093 -0.2631 0.1571  -0.0121 205 GLY B O   
5766  N N   . ALA B  206 ? 0.6781 0.4389 0.4587 -0.2646 0.1642  -0.0207 206 ALA B N   
5767  C CA  . ALA B  206 ? 0.6975 0.4501 0.4632 -0.2650 0.1665  -0.0201 206 ALA B CA  
5768  C C   . ALA B  206 ? 0.6576 0.3988 0.4175 -0.2533 0.1576  -0.0143 206 ALA B C   
5769  O O   . ALA B  206 ? 0.6744 0.3987 0.4146 -0.2536 0.1564  -0.0102 206 ALA B O   
5770  C CB  . ALA B  206 ? 0.6592 0.4285 0.4365 -0.2669 0.1727  -0.0272 206 ALA B CB  
5771  N N   . ALA B  207 ? 0.6319 0.3819 0.4080 -0.2437 0.1517  -0.0145 207 ALA B N   
5772  C CA  . ALA B  207 ? 0.6532 0.3940 0.4251 -0.2329 0.1438  -0.0104 207 ALA B CA  
5773  C C   . ALA B  207 ? 0.6608 0.3814 0.4148 -0.2334 0.1401  -0.0055 207 ALA B C   
5774  O O   . ALA B  207 ? 0.6527 0.3600 0.3947 -0.2278 0.1354  -0.0016 207 ALA B O   
5775  C CB  . ALA B  207 ? 0.5928 0.3470 0.3856 -0.2243 0.1384  -0.0115 207 ALA B CB  
5776  N N   . SER B  208 ? 0.7716 0.4898 0.5244 -0.2403 0.1422  -0.0060 208 SER B N   
5777  C CA  . SER B  208 ? 0.8006 0.4999 0.5380 -0.2413 0.1391  -0.0016 208 SER B CA  
5778  C C   . SER B  208 ? 0.8360 0.5192 0.5516 -0.2482 0.1424  0.0014  208 SER B C   
5779  O O   . SER B  208 ? 0.8647 0.5300 0.5651 -0.2459 0.1382  0.0063  208 SER B O   
5780  C CB  . SER B  208 ? 0.6748 0.3768 0.4180 -0.2472 0.1407  -0.0032 208 SER B CB  
5781  O OG  . SER B  208 ? 0.6508 0.3722 0.4157 -0.2442 0.1400  -0.0071 208 SER B OG  
5782  N N   . VAL B  209 ? 0.7080 0.3981 0.4223 -0.2569 0.1499  -0.0015 209 VAL B N   
5783  C CA  . VAL B  209 ? 0.7363 0.4125 0.4299 -0.2647 0.1537  0.0013  209 VAL B CA  
5784  C C   . VAL B  209 ? 0.7347 0.4018 0.4182 -0.2573 0.1491  0.0049  209 VAL B C   
5785  O O   . VAL B  209 ? 0.7538 0.4017 0.4192 -0.2572 0.1456  0.0104  209 VAL B O   
5786  C CB  . VAL B  209 ? 0.8412 0.5302 0.5381 -0.2747 0.1630  -0.0035 209 VAL B CB  
5787  C CG1 . VAL B  209 ? 0.8714 0.5474 0.5467 -0.2819 0.1666  -0.0006 209 VAL B CG1 
5788  C CG2 . VAL B  209 ? 0.8478 0.5442 0.5527 -0.2833 0.1678  -0.0068 209 VAL B CG2 
5789  N N   . GLY B  210 ? 0.7119 0.3929 0.4078 -0.2511 0.1488  0.0018  210 GLY B N   
5790  C CA  . GLY B  210 ? 0.7066 0.3812 0.3957 -0.2432 0.1441  0.0045  210 GLY B CA  
5791  C C   . GLY B  210 ? 0.7728 0.4355 0.4588 -0.2336 0.1351  0.0089  210 GLY B C   
5792  O O   . GLY B  210 ? 0.7080 0.3577 0.3814 -0.2290 0.1305  0.0131  210 GLY B O   
5793  N N   . MET B  211 ? 0.6892 0.3566 0.3871 -0.2308 0.1326  0.0079  211 MET B N   
5794  C CA  . MET B  211 ? 0.6831 0.3414 0.3802 -0.2222 0.1247  0.0112  211 MET B CA  
5795  C C   . MET B  211 ? 0.7513 0.3874 0.4279 -0.2260 0.1229  0.0165  211 MET B C   
5796  O O   . MET B  211 ? 0.7730 0.3970 0.4423 -0.2191 0.1165  0.0204  211 MET B O   
5797  C CB  . MET B  211 ? 0.6663 0.3353 0.3801 -0.2200 0.1233  0.0086  211 MET B CB  
5798  C CG  . MET B  211 ? 0.6474 0.3165 0.3684 -0.2087 0.1156  0.0098  211 MET B CG  
5799  S SD  . MET B  211 ? 0.6666 0.3539 0.4058 -0.1991 0.1131  0.0071  211 MET B SD  
5800  C CE  . MET B  211 ? 0.5993 0.3082 0.3594 -0.2038 0.1180  0.0019  211 MET B CE  
5801  N N   . HIS B  212 ? 0.7885 0.4191 0.4562 -0.2372 0.1286  0.0168  212 HIS B N   
5802  C CA  . HIS B  212 ? 0.8495 0.4584 0.4977 -0.2416 0.1270  0.0224  212 HIS B CA  
5803  C C   . HIS B  212 ? 0.8426 0.4410 0.4746 -0.2419 0.1264  0.0261  212 HIS B C   
5804  O O   . HIS B  212 ? 0.8536 0.4351 0.4732 -0.2382 0.1206  0.0314  212 HIS B O   
5805  C CB  . HIS B  212 ? 0.8367 0.4425 0.4800 -0.2541 0.1334  0.0219  212 HIS B CB  
5806  C CG  . HIS B  212 ? 0.8624 0.4745 0.5188 -0.2541 0.1331  0.0193  212 HIS B CG  
5807  N ND1 . HIS B  212 ? 0.8701 0.4729 0.5271 -0.2480 0.1268  0.0218  212 HIS B ND1 
5808  C CD2 . HIS B  212 ? 0.7694 0.3967 0.4391 -0.2595 0.1382  0.0143  212 HIS B CD2 
5809  C CE1 . HIS B  212 ? 0.7668 0.3785 0.4362 -0.2499 0.1281  0.0184  212 HIS B CE1 
5810  N NE2 . HIS B  212 ? 0.7630 0.3895 0.4403 -0.2568 0.1348  0.0140  212 HIS B NE2 
5811  N N   . ILE B  213 ? 0.7780 0.3869 0.4108 -0.2465 0.1321  0.0231  213 ILE B N   
5812  C CA  . ILE B  213 ? 0.8006 0.4022 0.4191 -0.2470 0.1321  0.0258  213 ILE B CA  
5813  C C   . ILE B  213 ? 0.8086 0.4039 0.4263 -0.2348 0.1234  0.0288  213 ILE B C   
5814  O O   . ILE B  213 ? 0.7956 0.3754 0.3968 -0.2341 0.1198  0.0340  213 ILE B O   
5815  C CB  . ILE B  213 ? 0.7793 0.3984 0.4054 -0.2505 0.1389  0.0205  213 ILE B CB  
5816  C CG1 . ILE B  213 ? 0.7956 0.4203 0.4201 -0.2638 0.1480  0.0176  213 ILE B CG1 
5817  C CG2 . ILE B  213 ? 0.7882 0.4004 0.4004 -0.2496 0.1380  0.0226  213 ILE B CG2 
5818  C CD1 . ILE B  213 ? 0.7893 0.4300 0.4198 -0.2690 0.1561  0.0103  213 ILE B CD1 
5819  N N   . LEU B  214 ? 0.7482 0.3555 0.3838 -0.2253 0.1199  0.0256  214 LEU B N   
5820  C CA  . LEU B  214 ? 0.8267 0.4305 0.4633 -0.2137 0.1122  0.0277  214 LEU B CA  
5821  C C   . LEU B  214 ? 0.8267 0.4160 0.4587 -0.2084 0.1051  0.0319  214 LEU B C   
5822  O O   . LEU B  214 ? 0.8108 0.3933 0.4397 -0.2000 0.0985  0.0345  214 LEU B O   
5823  C CB  . LEU B  214 ? 0.7008 0.3239 0.3580 -0.2057 0.1114  0.0228  214 LEU B CB  
5824  C CG  . LEU B  214 ? 0.6922 0.3246 0.3514 -0.2053 0.1143  0.0204  214 LEU B CG  
5825  C CD1 . LEU B  214 ? 0.7040 0.3431 0.3610 -0.2167 0.1234  0.0175  214 LEU B CD1 
5826  C CD2 . LEU B  214 ? 0.7653 0.4148 0.4453 -0.1967 0.1124  0.0166  214 LEU B CD2 
5827  N N   . SER B  215 ? 0.9515 0.5364 0.5835 -0.2134 0.1065  0.0323  215 SER B N   
5828  C CA  . SER B  215 ? 1.0105 0.5832 0.6407 -0.2086 0.1003  0.0355  215 SER B CA  
5829  C C   . SER B  215 ? 1.0917 0.6421 0.7015 -0.2141 0.0990  0.0418  215 SER B C   
5830  O O   . SER B  215 ? 1.1241 0.6695 0.7248 -0.2249 0.1045  0.0428  215 SER B O   
5831  C CB  . SER B  215 ? 1.0350 0.6155 0.6780 -0.2103 0.1021  0.0323  215 SER B CB  
5832  O OG  . SER B  215 ? 1.0368 0.6081 0.6809 -0.2043 0.0960  0.0345  215 SER B OG  
5833  N N   . LEU B  216 ? 1.1806 0.7177 0.7838 -0.2070 0.0916  0.0462  216 LEU B N   
5834  C CA  . LEU B  216 ? 1.2326 0.7480 0.8157 -0.2116 0.0896  0.0529  216 LEU B CA  
5835  C C   . LEU B  216 ? 1.2076 0.7107 0.7839 -0.2204 0.0920  0.0556  216 LEU B C   
5836  O O   . LEU B  216 ? 1.2132 0.7081 0.7757 -0.2306 0.0963  0.0584  216 LEU B O   
5837  C CB  . LEU B  216 ? 1.2489 0.7525 0.8270 -0.2018 0.0807  0.0572  216 LEU B CB  
5838  C CG  . LEU B  216 ? 1.2979 0.7842 0.8552 -0.2056 0.0787  0.0638  216 LEU B CG  
5839  C CD1 . LEU B  216 ? 1.3258 0.7910 0.8692 -0.2122 0.0776  0.0701  216 LEU B CD1 
5840  C CD2 . LEU B  216 ? 1.3051 0.7993 0.8560 -0.2133 0.0855  0.0621  216 LEU B CD2 
5841  N N   . PRO B  217 ? 1.1034 0.6054 0.6892 -0.2170 0.0895  0.0546  217 PRO B N   
5842  C CA  . PRO B  217 ? 1.1098 0.5994 0.6892 -0.2256 0.0918  0.0572  217 PRO B CA  
5843  C C   . PRO B  217 ? 1.1383 0.6366 0.7178 -0.2375 0.1008  0.0541  217 PRO B C   
5844  O O   . PRO B  217 ? 1.1835 0.6699 0.7534 -0.2469 0.1037  0.0570  217 PRO B O   
5845  C CB  . PRO B  217 ? 0.8767 0.3688 0.4701 -0.2192 0.0882  0.0549  217 PRO B CB  
5846  C CG  . PRO B  217 ? 0.8496 0.3450 0.4491 -0.2068 0.0815  0.0546  217 PRO B CG  
5847  C CD  . PRO B  217 ? 0.8609 0.3697 0.4613 -0.2056 0.0839  0.0522  217 PRO B CD  
5848  N N   . SER B  218 ? 1.0566 0.5753 0.6474 -0.2372 0.1052  0.0482  218 SER B N   
5849  C CA  . SER B  218 ? 1.0631 0.5917 0.6558 -0.2481 0.1137  0.0447  218 SER B CA  
5850  C C   . SER B  218 ? 1.1040 0.6242 0.6789 -0.2574 0.1180  0.0481  218 SER B C   
5851  O O   . SER B  218 ? 1.0899 0.6095 0.6597 -0.2688 0.1246  0.0477  218 SER B O   
5852  C CB  . SER B  218 ? 0.9801 0.5333 0.5919 -0.2447 0.1168  0.0374  218 SER B CB  
5853  O OG  . SER B  218 ? 0.9403 0.5016 0.5674 -0.2411 0.1154  0.0341  218 SER B OG  
5854  N N   . ARG B  219 ? 1.2642 0.7776 0.8294 -0.2527 0.1140  0.0516  219 ARG B N   
5855  C CA  . ARG B  219 ? 1.3390 0.8464 0.8874 -0.2603 0.1175  0.0546  219 ARG B CA  
5856  C C   . ARG B  219 ? 1.3892 0.8799 0.9201 -0.2727 0.1208  0.0598  219 ARG B C   
5857  O O   . ARG B  219 ? 1.4219 0.9149 0.9439 -0.2830 0.1277  0.0596  219 ARG B O   
5858  C CB  . ARG B  219 ? 1.3026 0.8016 0.8421 -0.2524 0.1108  0.0587  219 ARG B CB  
5859  C CG  . ARG B  219 ? 1.3096 0.8259 0.8619 -0.2434 0.1098  0.0537  219 ARG B CG  
5860  C CD  . ARG B  219 ? 1.3328 0.8691 0.8939 -0.2495 0.1185  0.0471  219 ARG B CD  
5861  N NE  . ARG B  219 ? 1.3386 0.8714 0.8849 -0.2621 0.1255  0.0485  219 ARG B NE  
5862  C CZ  . ARG B  219 ? 1.2858 0.8212 0.8239 -0.2644 0.1279  0.0485  219 ARG B CZ  
5863  N NH1 . ARG B  219 ? 1.2082 0.7493 0.7514 -0.2548 0.1237  0.0474  219 ARG B NH1 
5864  N NH2 . ARG B  219 ? 1.3027 0.8354 0.8274 -0.2768 0.1347  0.0496  219 ARG B NH2 
5865  N N   . SER B  220 ? 1.2567 0.7306 0.7830 -0.2718 0.1161  0.0647  220 SER B N   
5866  C CA  . SER B  220 ? 1.2416 0.6971 0.7508 -0.2829 0.1182  0.0708  220 SER B CA  
5867  C C   . SER B  220 ? 1.2203 0.6822 0.7350 -0.2934 0.1260  0.0671  220 SER B C   
5868  O O   . SER B  220 ? 1.2388 0.6869 0.7407 -0.3037 0.1287  0.0715  220 SER B O   
5869  C CB  . SER B  220 ? 1.2397 0.6734 0.7423 -0.2776 0.1098  0.0777  220 SER B CB  
5870  O OG  . SER B  220 ? 1.2174 0.6537 0.7347 -0.2735 0.1081  0.0747  220 SER B OG  
5871  N N   . LEU B  221 ? 1.2221 0.7048 0.7562 -0.2908 0.1292  0.0592  221 LEU B N   
5872  C CA  . LEU B  221 ? 1.1854 0.6755 0.7271 -0.2997 0.1358  0.0552  221 LEU B CA  
5873  C C   . LEU B  221 ? 1.1241 0.6300 0.6672 -0.3094 0.1452  0.0502  221 LEU B C   
5874  O O   . LEU B  221 ? 1.1053 0.6193 0.6549 -0.3176 0.1514  0.0464  221 LEU B O   
5875  C CB  . LEU B  221 ? 1.1343 0.6362 0.6965 -0.2917 0.1332  0.0499  221 LEU B CB  
5876  C CG  . LEU B  221 ? 1.1057 0.5930 0.6679 -0.2827 0.1246  0.0540  221 LEU B CG  
5877  C CD1 . LEU B  221 ? 1.0684 0.5699 0.6509 -0.2745 0.1223  0.0484  221 LEU B CD1 
5878  C CD2 . LEU B  221 ? 1.1342 0.6007 0.6844 -0.2908 0.1247  0.0596  221 LEU B CD2 
5879  N N   . PHE B  222 ? 1.0094 0.5205 0.5470 -0.3085 0.1464  0.0500  222 PHE B N   
5880  C CA  . PHE B  222 ? 1.0771 0.6040 0.6167 -0.3176 0.1556  0.0449  222 PHE B CA  
5881  C C   . PHE B  222 ? 1.0831 0.6065 0.6074 -0.3205 0.1571  0.0475  222 PHE B C   
5882  O O   . PHE B  222 ? 1.0949 0.6037 0.6071 -0.3149 0.1505  0.0536  222 PHE B O   
5883  C CB  . PHE B  222 ? 1.3267 0.8790 0.8902 -0.3121 0.1579  0.0361  222 PHE B CB  
5884  C CG  . PHE B  222 ? 1.3276 0.8876 0.8996 -0.2990 0.1523  0.0347  222 PHE B CG  
5885  C CD1 . PHE B  222 ? 1.3198 0.8737 0.8971 -0.2871 0.1436  0.0368  222 PHE B CD1 
5886  C CD2 . PHE B  222 ? 1.3039 0.8780 0.8796 -0.2988 0.1561  0.0307  222 PHE B CD2 
5887  C CE1 . PHE B  222 ? 1.3066 0.8679 0.8917 -0.2756 0.1387  0.0355  222 PHE B CE1 
5888  C CE2 . PHE B  222 ? 1.2947 0.8756 0.8784 -0.2872 0.1511  0.0295  222 PHE B CE2 
5889  C CZ  . PHE B  222 ? 1.2956 0.8700 0.8838 -0.2756 0.1424  0.0320  222 PHE B CZ  
5890  N N   . HIS B  223 ? 1.0382 0.5756 0.5637 -0.3295 0.1660  0.0427  223 HIS B N   
5891  C CA  . HIS B  223 ? 1.0808 0.6155 0.5903 -0.3357 0.1694  0.0448  223 HIS B CA  
5892  C C   . HIS B  223 ? 1.0398 0.5964 0.5600 -0.3352 0.1751  0.0366  223 HIS B C   
5893  O O   . HIS B  223 ? 0.9895 0.5450 0.5031 -0.3308 0.1729  0.0369  223 HIS B O   
5894  C CB  . HIS B  223 ? 1.3927 0.9156 0.8841 -0.3511 0.1755  0.0488  223 HIS B CB  
5895  C CG  . HIS B  223 ? 1.4322 0.9316 0.9119 -0.3520 0.1699  0.0568  223 HIS B CG  
5896  N ND1 . HIS B  223 ? 1.4176 0.9149 0.9029 -0.3573 0.1721  0.0560  223 HIS B ND1 
5897  C CD2 . HIS B  223 ? 1.4444 0.9218 0.9084 -0.3479 0.1619  0.0657  223 HIS B CD2 
5898  C CE1 . HIS B  223 ? 1.4246 0.8992 0.8981 -0.3565 0.1660  0.0640  223 HIS B CE1 
5899  N NE2 . HIS B  223 ? 1.4372 0.8994 0.8978 -0.3508 0.1597  0.0701  223 HIS B NE2 
5900  N N   . ARG B  224 ? 1.1556 0.7303 0.6901 -0.3411 0.1829  0.0288  224 ARG B N   
5901  C CA  . ARG B  224 ? 1.1459 0.7414 0.6922 -0.3411 0.1887  0.0197  224 ARG B CA  
5902  C C   . ARG B  224 ? 1.1282 0.7425 0.7024 -0.3323 0.1872  0.0135  224 ARG B C   
5903  O O   . ARG B  224 ? 1.1403 0.7536 0.7244 -0.3292 0.1837  0.0152  224 ARG B O   
5904  C CB  . ARG B  224 ? 1.2015 0.8042 0.7399 -0.3572 0.2003  0.0148  224 ARG B CB  
5905  C CG  . ARG B  224 ? 1.2875 0.8742 0.7982 -0.3660 0.2022  0.0203  224 ARG B CG  
5906  C CD  . ARG B  224 ? 1.3742 0.9599 0.8731 -0.3833 0.2118  0.0194  224 ARG B CD  
5907  N NE  . ARG B  224 ? 1.4187 0.9865 0.9078 -0.3872 0.2088  0.0275  224 ARG B NE  
5908  C CZ  . ARG B  224 ? 1.4318 0.9766 0.8990 -0.3885 0.2037  0.0376  224 ARG B CZ  
5909  N NH1 . ARG B  224 ? 1.4267 0.9636 0.8789 -0.3861 0.2006  0.0410  224 ARG B NH1 
5910  N NH2 . ARG B  224 ? 1.4377 0.9673 0.8985 -0.3922 0.2013  0.0444  224 ARG B NH2 
5911  N N   . ALA B  225 ? 1.0949 0.7259 0.6817 -0.3279 0.1893  0.0067  225 ALA B N   
5912  C CA  . ALA B  225 ? 1.0395 0.6887 0.6527 -0.3201 0.1879  0.0012  225 ALA B CA  
5913  C C   . ALA B  225 ? 0.9841 0.6564 0.6134 -0.3223 0.1953  -0.0087 225 ALA B C   
5914  O O   . ALA B  225 ? 0.9931 0.6690 0.6183 -0.3220 0.1977  -0.0116 225 ALA B O   
5915  C CB  . ALA B  225 ? 1.0902 0.7347 0.7106 -0.3047 0.1771  0.0054  225 ALA B CB  
5916  N N   . VAL B  226 ? 0.8951 0.5835 0.5437 -0.3243 0.1986  -0.0140 226 VAL B N   
5917  C CA  . VAL B  226 ? 0.8932 0.6048 0.5610 -0.3254 0.2049  -0.0236 226 VAL B CA  
5918  C C   . VAL B  226 ? 0.9009 0.6253 0.5930 -0.3124 0.1985  -0.0252 226 VAL B C   
5919  O O   . VAL B  226 ? 0.9328 0.6581 0.6354 -0.3083 0.1937  -0.0230 226 VAL B O   
5920  C CB  . VAL B  226 ? 0.8353 0.5587 0.5089 -0.3383 0.2144  -0.0296 226 VAL B CB  
5921  C CG1 . VAL B  226 ? 0.8179 0.5658 0.5124 -0.3393 0.2209  -0.0398 226 VAL B CG1 
5922  C CG2 . VAL B  226 ? 0.8721 0.5836 0.5221 -0.3517 0.2209  -0.0278 226 VAL B CG2 
5923  N N   . LEU B  227 ? 0.8874 0.6217 0.5883 -0.3063 0.1985  -0.0292 227 LEU B N   
5924  C CA  . LEU B  227 ? 0.8560 0.6029 0.5796 -0.2944 0.1927  -0.0307 227 LEU B CA  
5925  C C   . LEU B  227 ? 0.7199 0.4904 0.4648 -0.2973 0.1997  -0.0403 227 LEU B C   
5926  O O   . LEU B  227 ? 0.7205 0.4982 0.4656 -0.2995 0.2051  -0.0457 227 LEU B O   
5927  C CB  . LEU B  227 ? 0.7207 0.4595 0.4397 -0.2832 0.1856  -0.0269 227 LEU B CB  
5928  C CG  . LEU B  227 ? 0.7290 0.4466 0.4319 -0.2778 0.1771  -0.0177 227 LEU B CG  
5929  C CD1 . LEU B  227 ? 0.7592 0.4597 0.4358 -0.2850 0.1797  -0.0144 227 LEU B CD1 
5930  C CD2 . LEU B  227 ? 0.8688 0.5859 0.5799 -0.2636 0.1681  -0.0148 227 LEU B CD2 
5931  N N   . GLN B  228 ? 0.7078 0.4909 0.4713 -0.2972 0.1993  -0.0425 228 GLN B N   
5932  C CA  . GLN B  228 ? 0.8431 0.6492 0.6283 -0.3005 0.2057  -0.0515 228 GLN B CA  
5933  C C   . GLN B  228 ? 0.8112 0.6299 0.6201 -0.2886 0.1990  -0.0520 228 GLN B C   
5934  O O   . GLN B  228 ? 0.8206 0.6405 0.6394 -0.2836 0.1925  -0.0484 228 GLN B O   
5935  C CB  . GLN B  228 ? 0.7972 0.6101 0.5873 -0.3104 0.2107  -0.0542 228 GLN B CB  
5936  C CG  . GLN B  228 ? 0.8325 0.6284 0.5978 -0.3207 0.2145  -0.0507 228 GLN B CG  
5937  C CD  . GLN B  228 ? 0.9026 0.7073 0.6729 -0.3324 0.2217  -0.0551 228 GLN B CD  
5938  O OE1 . GLN B  228 ? 0.9661 0.7575 0.7192 -0.3406 0.2237  -0.0515 228 GLN B OE1 
5939  N NE2 . GLN B  228 ? 0.8824 0.7098 0.6768 -0.3333 0.2254  -0.0630 228 GLN B NE2 
5940  N N   . SER B  229 ? 0.7040 0.5320 0.5219 -0.2845 0.2007  -0.0565 229 SER B N   
5941  C CA  . SER B  229 ? 0.6559 0.4967 0.4973 -0.2737 0.1947  -0.0571 229 SER B CA  
5942  C C   . SER B  229 ? 0.6723 0.5018 0.5118 -0.2621 0.1830  -0.0482 229 SER B C   
5943  O O   . SER B  229 ? 0.5854 0.4244 0.4435 -0.2559 0.1772  -0.0471 229 SER B O   
5944  C CB  . SER B  229 ? 0.6698 0.5320 0.5368 -0.2764 0.1973  -0.0630 229 SER B CB  
5945  O OG  . SER B  229 ? 0.6177 0.4950 0.4928 -0.2845 0.2076  -0.0729 229 SER B OG  
5946  N N   . GLY B  230 ? 0.6158 0.4258 0.4336 -0.2595 0.1794  -0.0421 230 GLY B N   
5947  C CA  . GLY B  230 ? 0.6019 0.4017 0.4180 -0.2483 0.1686  -0.0346 230 GLY B CA  
5948  C C   . GLY B  230 ? 0.7310 0.5110 0.5234 -0.2461 0.1662  -0.0296 230 GLY B C   
5949  O O   . GLY B  230 ? 0.6397 0.4106 0.4139 -0.2548 0.1721  -0.0303 230 GLY B O   
5950  N N   . THR B  231 ? 0.5999 0.3734 0.3927 -0.2348 0.1574  -0.0245 231 THR B N   
5951  C CA  . THR B  231 ? 0.6104 0.3661 0.3829 -0.2314 0.1540  -0.0197 231 THR B CA  
5952  C C   . THR B  231 ? 0.5972 0.3453 0.3711 -0.2206 0.1434  -0.0132 231 THR B C   
5953  O O   . THR B  231 ? 0.5749 0.3337 0.3673 -0.2140 0.1387  -0.0130 231 THR B O   
5954  C CB  . THR B  231 ? 0.6440 0.4034 0.4182 -0.2277 0.1553  -0.0227 231 THR B CB  
5955  O OG1 . THR B  231 ? 0.6689 0.4446 0.4675 -0.2204 0.1524  -0.0250 231 THR B OG1 
5956  C CG2 . THR B  231 ? 0.6200 0.3829 0.3867 -0.2387 0.1660  -0.0290 231 THR B CG2 
5957  N N   . PRO B  232 ? 0.6648 0.3949 0.4198 -0.2186 0.1396  -0.0079 232 PRO B N   
5958  C CA  . PRO B  232 ? 0.6430 0.3653 0.3982 -0.2086 0.1303  -0.0029 232 PRO B CA  
5959  C C   . PRO B  232 ? 0.6517 0.3804 0.4174 -0.1978 0.1251  -0.0028 232 PRO B C   
5960  O O   . PRO B  232 ? 0.6709 0.3986 0.4421 -0.1899 0.1186  -0.0009 232 PRO B O   
5961  C CB  . PRO B  232 ? 0.7121 0.4131 0.4429 -0.2111 0.1290  0.0018  232 PRO B CB  
5962  C CG  . PRO B  232 ? 0.7427 0.4423 0.4626 -0.2179 0.1354  -0.0001 232 PRO B CG  
5963  C CD  . PRO B  232 ? 0.7557 0.4713 0.4873 -0.2261 0.1439  -0.0068 232 PRO B CD  
5964  N N   . ASN B  233 ? 0.6810 0.4134 0.4453 -0.1993 0.1294  -0.0060 233 ASN B N   
5965  C CA  . ASN B  233 ? 0.6992 0.4369 0.4724 -0.1902 0.1255  -0.0064 233 ASN B CA  
5966  C C   . ASN B  233 ? 0.7320 0.4891 0.5292 -0.1885 0.1269  -0.0107 233 ASN B C   
5967  O O   . ASN B  233 ? 0.7560 0.5223 0.5623 -0.1945 0.1309  -0.0134 233 ASN B O   
5968  C CB  . ASN B  233 ? 0.6430 0.3738 0.4015 -0.1935 0.1301  -0.0085 233 ASN B CB  
5969  C CG  . ASN B  233 ? 0.6479 0.3857 0.4050 -0.2052 0.1410  -0.0150 233 ASN B CG  
5970  O OD1 . ASN B  233 ? 0.6675 0.4015 0.4154 -0.2144 0.1457  -0.0153 233 ASN B OD1 
5971  N ND2 . ASN B  233 ? 0.6201 0.3688 0.3871 -0.2051 0.1454  -0.0205 233 ASN B ND2 
5972  N N   . GLY B  234 ? 0.8605 0.6238 0.6685 -0.1805 0.1235  -0.0111 234 GLY B N   
5973  C CA  . GLY B  234 ? 0.8526 0.6338 0.6837 -0.1793 0.1249  -0.0152 234 GLY B CA  
5974  C C   . GLY B  234 ? 0.8231 0.6127 0.6725 -0.1702 0.1161  -0.0118 234 GLY B C   
5975  O O   . GLY B  234 ? 0.8754 0.6577 0.7205 -0.1639 0.1088  -0.0068 234 GLY B O   
5976  N N   . PRO B  235 ? 0.5461 0.3517 0.4168 -0.1699 0.1169  -0.0149 235 PRO B N   
5977  C CA  . PRO B  235 ? 0.4683 0.2838 0.3583 -0.1620 0.1087  -0.0122 235 PRO B CA  
5978  C C   . PRO B  235 ? 0.4527 0.2675 0.3436 -0.1627 0.1051  -0.0095 235 PRO B C   
5979  O O   . PRO B  235 ? 0.4307 0.2426 0.3226 -0.1564 0.0986  -0.0066 235 PRO B O   
5980  C CB  . PRO B  235 ? 0.4242 0.2560 0.3345 -0.1648 0.1127  -0.0173 235 PRO B CB  
5981  C CG  . PRO B  235 ? 0.4435 0.2760 0.3466 -0.1757 0.1229  -0.0227 235 PRO B CG  
5982  C CD  . PRO B  235 ? 0.4622 0.2783 0.3405 -0.1779 0.1260  -0.0219 235 PRO B CD  
5983  N N   . TRP B  236 ? 0.4468 0.2635 0.3359 -0.1713 0.1103  -0.0117 236 TRP B N   
5984  C CA  . TRP B  236 ? 0.4934 0.3112 0.3854 -0.1737 0.1084  -0.0109 236 TRP B CA  
5985  C C   . TRP B  236 ? 0.5263 0.3285 0.3984 -0.1776 0.1090  -0.0091 236 TRP B C   
5986  O O   . TRP B  236 ? 0.5166 0.3193 0.3913 -0.1790 0.1069  -0.0085 236 TRP B O   
5987  C CB  . TRP B  236 ? 0.4817 0.3145 0.3892 -0.1807 0.1128  -0.0147 236 TRP B CB  
5988  C CG  . TRP B  236 ? 0.5261 0.3566 0.4234 -0.1901 0.1220  -0.0184 236 TRP B CG  
5989  C CD1 . TRP B  236 ? 0.5471 0.3833 0.4464 -0.1946 0.1294  -0.0238 236 TRP B CD1 
5990  C CD2 . TRP B  236 ? 0.5407 0.3613 0.4223 -0.1978 0.1259  -0.0181 236 TRP B CD2 
5991  N NE1 . TRP B  236 ? 0.5688 0.3998 0.4542 -0.2046 0.1377  -0.0269 236 TRP B NE1 
5992  C CE2 . TRP B  236 ? 0.5853 0.4065 0.4597 -0.2067 0.1354  -0.0231 236 TRP B CE2 
5993  C CE3 . TRP B  236 ? 0.5539 0.3633 0.4238 -0.1997 0.1239  -0.0157 236 TRP B CE3 
5994  C CZ2 . TRP B  236 ? 0.6415 0.4542 0.5004 -0.2160 0.1411  -0.0237 236 TRP B CZ2 
5995  C CZ3 . TRP B  236 ? 0.6067 0.4072 0.4618 -0.2087 0.1295  -0.0164 236 TRP B CZ3 
5996  C CH2 . TRP B  236 ? 0.6366 0.4396 0.4876 -0.2161 0.1372  -0.0196 236 TRP B CH2 
5997  N N   . ALA B  237 ? 0.4920 0.2801 0.3446 -0.1796 0.1116  -0.0082 237 ALA B N   
5998  C CA  . ALA B  237 ? 0.5174 0.2913 0.3522 -0.1853 0.1133  -0.0068 237 ALA B CA  
5999  C C   . ALA B  237 ? 0.5106 0.2704 0.3338 -0.1798 0.1074  -0.0031 237 ALA B C   
6000  O O   . ALA B  237 ? 0.6435 0.3927 0.4553 -0.1840 0.1079  -0.0020 237 ALA B O   
6001  C CB  . ALA B  237 ? 0.5287 0.2947 0.3483 -0.1929 0.1200  -0.0077 237 ALA B CB  
6002  N N   . THR B  238 ? 0.4958 0.2557 0.3223 -0.1705 0.1018  -0.0013 238 THR B N   
6003  C CA  . THR B  238 ? 0.4978 0.2459 0.3149 -0.1648 0.0961  0.0017  238 THR B CA  
6004  C C   . THR B  238 ? 0.4744 0.2315 0.3057 -0.1558 0.0899  0.0023  238 THR B C   
6005  O O   . THR B  238 ? 0.4579 0.2275 0.3035 -0.1529 0.0896  0.0012  238 THR B O   
6006  C CB  . THR B  238 ? 0.5113 0.2440 0.3103 -0.1627 0.0953  0.0041  238 THR B CB  
6007  O OG1 . THR B  238 ? 0.4974 0.2354 0.3018 -0.1565 0.0936  0.0041  238 THR B OG1 
6008  C CG2 . THR B  238 ? 0.5349 0.2588 0.3194 -0.1718 0.1013  0.0040  238 THR B CG2 
6009  N N   . VAL B  239 ? 0.4733 0.2245 0.3014 -0.1517 0.0851  0.0040  239 VAL B N   
6010  C CA  . VAL B  239 ? 0.4538 0.2109 0.2916 -0.1428 0.0792  0.0050  239 VAL B CA  
6011  C C   . VAL B  239 ? 0.4600 0.2039 0.2849 -0.1375 0.0754  0.0073  239 VAL B C   
6012  O O   . VAL B  239 ? 0.4795 0.2093 0.2888 -0.1406 0.0767  0.0084  239 VAL B O   
6013  C CB  . VAL B  239 ? 0.4416 0.2080 0.2922 -0.1419 0.0761  0.0046  239 VAL B CB  
6014  C CG1 . VAL B  239 ? 0.5221 0.3033 0.3885 -0.1459 0.0784  0.0027  239 VAL B CG1 
6015  C CG2 . VAL B  239 ? 0.4559 0.2127 0.2967 -0.1456 0.0762  0.0047  239 VAL B CG2 
6016  N N   . SER B  240 ? 0.5700 0.3186 0.4021 -0.1295 0.0707  0.0080  240 SER B N   
6017  C CA  . SER B  240 ? 0.5863 0.3248 0.4092 -0.1235 0.0665  0.0099  240 SER B CA  
6018  C C   . SER B  240 ? 0.6050 0.3386 0.4254 -0.1238 0.0643  0.0102  240 SER B C   
6019  O O   . SER B  240 ? 0.6092 0.3503 0.4380 -0.1268 0.0649  0.0090  240 SER B O   
6020  C CB  . SER B  240 ? 0.5385 0.2859 0.3726 -0.1156 0.0623  0.0102  240 SER B CB  
6021  O OG  . SER B  240 ? 0.5377 0.2981 0.3873 -0.1150 0.0608  0.0094  240 SER B OG  
6022  N N   . ALA B  241 ? 0.5289 0.2500 0.3381 -0.1207 0.0617  0.0118  241 ALA B N   
6023  C CA  . ALA B  241 ? 0.5179 0.2347 0.3262 -0.1196 0.0591  0.0119  241 ALA B CA  
6024  C C   . ALA B  241 ? 0.4665 0.1972 0.2901 -0.1153 0.0560  0.0108  241 ALA B C   
6025  O O   . ALA B  241 ? 0.4507 0.1848 0.2789 -0.1175 0.0558  0.0097  241 ALA B O   
6026  C CB  . ALA B  241 ? 0.6316 0.3350 0.4289 -0.1153 0.0559  0.0138  241 ALA B CB  
6027  N N   . GLY B  242 ? 0.5046 0.2430 0.3357 -0.1096 0.0537  0.0111  242 GLY B N   
6028  C CA  . GLY B  242 ? 0.5143 0.2651 0.3594 -0.1055 0.0505  0.0107  242 GLY B CA  
6029  C C   . GLY B  242 ? 0.5232 0.2852 0.3794 -0.1101 0.0521  0.0095  242 GLY B C   
6030  O O   . GLY B  242 ? 0.5403 0.3064 0.4016 -0.1107 0.0504  0.0089  242 GLY B O   
6031  N N   . GLU B  243 ? 0.4861 0.2533 0.3463 -0.1138 0.0553  0.0091  243 GLU B N   
6032  C CA  . GLU B  243 ? 0.4657 0.2447 0.3386 -0.1178 0.0564  0.0082  243 GLU B CA  
6033  C C   . GLU B  243 ? 0.5095 0.2843 0.3770 -0.1247 0.0589  0.0070  243 GLU B C   
6034  O O   . GLU B  243 ? 0.4934 0.2768 0.3703 -0.1273 0.0581  0.0063  243 GLU B O   
6035  C CB  . GLU B  243 ? 0.4485 0.2338 0.3275 -0.1201 0.0596  0.0077  243 GLU B CB  
6036  C CG  . GLU B  243 ? 0.4962 0.2948 0.3906 -0.1239 0.0602  0.0069  243 GLU B CG  
6037  C CD  . GLU B  243 ? 0.5331 0.3439 0.4441 -0.1189 0.0552  0.0082  243 GLU B CD  
6038  O OE1 . GLU B  243 ? 0.5476 0.3567 0.4578 -0.1126 0.0513  0.0094  243 GLU B OE1 
6039  O OE2 . GLU B  243 ? 0.5394 0.3614 0.4645 -0.1217 0.0551  0.0080  243 GLU B OE2 
6040  N N   . ALA B  244 ? 0.4380 0.1993 0.2904 -0.1277 0.0615  0.0070  244 ALA B N   
6041  C CA  . ALA B  244 ? 0.4378 0.1935 0.2845 -0.1341 0.0636  0.0060  244 ALA B CA  
6042  C C   . ALA B  244 ? 0.4314 0.1887 0.2816 -0.1315 0.0599  0.0057  244 ALA B C   
6043  O O   . ALA B  244 ? 0.4273 0.1924 0.2853 -0.1350 0.0598  0.0045  244 ALA B O   
6044  C CB  . ALA B  244 ? 0.4592 0.1985 0.2890 -0.1367 0.0660  0.0067  244 ALA B CB  
6045  N N   . ARG B  245 ? 0.4301 0.1810 0.2754 -0.1254 0.0567  0.0067  245 ARG B N   
6046  C CA  . ARG B  245 ? 0.4251 0.1767 0.2729 -0.1229 0.0535  0.0061  245 ARG B CA  
6047  C C   . ARG B  245 ? 0.4070 0.1738 0.2693 -0.1219 0.0512  0.0056  245 ARG B C   
6048  O O   . ARG B  245 ? 0.4061 0.1760 0.2714 -0.1244 0.0503  0.0045  245 ARG B O   
6049  C CB  . ARG B  245 ? 0.4909 0.2352 0.3334 -0.1160 0.0503  0.0072  245 ARG B CB  
6050  C CG  . ARG B  245 ? 0.5151 0.2639 0.3635 -0.1123 0.0468  0.0064  245 ARG B CG  
6051  C CD  . ARG B  245 ? 0.5676 0.3058 0.4088 -0.1075 0.0446  0.0069  245 ARG B CD  
6052  N NE  . ARG B  245 ? 0.6795 0.4113 0.5173 -0.1101 0.0448  0.0054  245 ARG B NE  
6053  C CZ  . ARG B  245 ? 0.7800 0.5182 0.6242 -0.1095 0.0432  0.0038  245 ARG B CZ  
6054  N NH1 . ARG B  245 ? 0.7829 0.5338 0.6370 -0.1064 0.0410  0.0040  245 ARG B NH1 
6055  N NH2 . ARG B  245 ? 0.8178 0.5493 0.6585 -0.1123 0.0437  0.0021  245 ARG B NH2 
6056  N N   . ARG B  246 ? 0.3934 0.1694 0.2647 -0.1186 0.0500  0.0067  246 ARG B N   
6057  C CA  . ARG B  246 ? 0.3763 0.1666 0.2626 -0.1174 0.0473  0.0071  246 ARG B CA  
6058  C C   . ARG B  246 ? 0.4192 0.2164 0.3118 -0.1244 0.0489  0.0060  246 ARG B C   
6059  O O   . ARG B  246 ? 0.3951 0.1989 0.2942 -0.1254 0.0465  0.0057  246 ARG B O   
6060  C CB  . ARG B  246 ? 0.4985 0.2958 0.3933 -0.1135 0.0465  0.0084  246 ARG B CB  
6061  C CG  . ARG B  246 ? 0.5209 0.3303 0.4303 -0.1093 0.0422  0.0098  246 ARG B CG  
6062  C CD  . ARG B  246 ? 0.5503 0.3719 0.4738 -0.1134 0.0417  0.0102  246 ARG B CD  
6063  N NE  . ARG B  246 ? 0.5601 0.3860 0.4900 -0.1152 0.0441  0.0103  246 ARG B NE  
6064  C CZ  . ARG B  246 ? 0.5366 0.3729 0.4798 -0.1190 0.0442  0.0106  246 ARG B CZ  
6065  N NH1 . ARG B  246 ? 0.4910 0.3347 0.4425 -0.1212 0.0415  0.0111  246 ARG B NH1 
6066  N NH2 . ARG B  246 ? 0.5555 0.3951 0.5040 -0.1206 0.0468  0.0102  246 ARG B NH2 
6067  N N   . ARG B  247 ? 0.3878 0.1833 0.2780 -0.1296 0.0530  0.0053  247 ARG B N   
6068  C CA  . ARG B  247 ? 0.3902 0.1928 0.2872 -0.1365 0.0549  0.0041  247 ARG B CA  
6069  C C   . ARG B  247 ? 0.4022 0.1990 0.2919 -0.1415 0.0558  0.0025  247 ARG B C   
6070  O O   . ARG B  247 ? 0.3996 0.2043 0.2968 -0.1455 0.0550  0.0016  247 ARG B O   
6071  C CB  . ARG B  247 ? 0.5079 0.3099 0.4036 -0.1410 0.0596  0.0035  247 ARG B CB  
6072  C CG  . ARG B  247 ? 0.4838 0.2936 0.3892 -0.1376 0.0592  0.0046  247 ARG B CG  
6073  C CD  . ARG B  247 ? 0.4973 0.3073 0.4019 -0.1429 0.0645  0.0034  247 ARG B CD  
6074  N NE  . ARG B  247 ? 0.5307 0.3450 0.4413 -0.1387 0.0644  0.0042  247 ARG B NE  
6075  C CZ  . ARG B  247 ? 0.5327 0.3486 0.4440 -0.1421 0.0689  0.0030  247 ARG B CZ  
6076  N NH1 . ARG B  247 ? 0.5271 0.3411 0.4337 -0.1499 0.0739  0.0011  247 ARG B NH1 
6077  N NH2 . ARG B  247 ? 0.5285 0.3480 0.4454 -0.1379 0.0685  0.0035  247 ARG B NH2 
6078  N N   . ALA B  248 ? 0.4163 0.1989 0.2916 -0.1414 0.0574  0.0020  248 ALA B N   
6079  C CA  . ALA B  248 ? 0.4288 0.2044 0.2971 -0.1459 0.0583  0.0004  248 ALA B CA  
6080  C C   . ALA B  248 ? 0.4189 0.1997 0.2922 -0.1433 0.0543  -0.0001 248 ALA B C   
6081  O O   . ALA B  248 ? 0.4209 0.2056 0.2971 -0.1480 0.0542  -0.0017 248 ALA B O   
6082  C CB  . ALA B  248 ? 0.4449 0.2040 0.2984 -0.1452 0.0599  0.0007  248 ALA B CB  
6083  N N   . THR B  249 ? 0.4731 0.2540 0.3473 -0.1360 0.0512  0.0012  249 THR B N   
6084  C CA  . THR B  249 ? 0.4941 0.2799 0.3727 -0.1332 0.0475  0.0009  249 THR B CA  
6085  C C   . THR B  249 ? 0.3874 0.1879 0.2788 -0.1358 0.0455  0.0011  249 THR B C   
6086  O O   . THR B  249 ? 0.3878 0.1914 0.2805 -0.1388 0.0443  -0.0002 249 THR B O   
6087  C CB  . THR B  249 ? 0.6285 0.4136 0.5075 -0.1251 0.0447  0.0025  249 THR B CB  
6088  O OG1 . THR B  249 ? 0.6256 0.3968 0.4928 -0.1230 0.0459  0.0023  249 THR B OG1 
6089  C CG2 . THR B  249 ? 0.6842 0.4757 0.5685 -0.1227 0.0411  0.0022  249 THR B CG2 
6090  N N   . LEU B  250 ? 0.4528 0.2622 0.3541 -0.1347 0.0450  0.0029  250 LEU B N   
6091  C CA  . LEU B  250 ? 0.4280 0.2514 0.3434 -0.1372 0.0428  0.0036  250 LEU B CA  
6092  C C   . LEU B  250 ? 0.4010 0.2271 0.3174 -0.1455 0.0448  0.0017  250 LEU B C   
6093  O O   . LEU B  250 ? 0.3724 0.2067 0.2955 -0.1483 0.0423  0.0015  250 LEU B O   
6094  C CB  . LEU B  250 ? 0.3561 0.1878 0.2832 -0.1344 0.0420  0.0059  250 LEU B CB  
6095  C CG  . LEU B  250 ? 0.3481 0.1936 0.2912 -0.1379 0.0403  0.0068  250 LEU B CG  
6096  C CD1 . LEU B  250 ? 0.3379 0.1908 0.2881 -0.1362 0.0354  0.0082  250 LEU B CD1 
6097  C CD2 . LEU B  250 ? 0.3402 0.1914 0.2937 -0.1356 0.0405  0.0085  250 LEU B CD2 
6098  N N   . LEU B  251 ? 0.3898 0.2092 0.2996 -0.1498 0.0492  0.0003  251 LEU B N   
6099  C CA  . LEU B  251 ? 0.4413 0.2636 0.3526 -0.1580 0.0514  -0.0017 251 LEU B CA  
6100  C C   . LEU B  251 ? 0.4574 0.2744 0.3611 -0.1608 0.0509  -0.0039 251 LEU B C   
6101  O O   . LEU B  251 ? 0.4398 0.2643 0.3491 -0.1656 0.0496  -0.0050 251 LEU B O   
6102  C CB  . LEU B  251 ? 0.4128 0.2286 0.3180 -0.1626 0.0567  -0.0029 251 LEU B CB  
6103  C CG  . LEU B  251 ? 0.4229 0.2420 0.3301 -0.1715 0.0590  -0.0053 251 LEU B CG  
6104  C CD1 . LEU B  251 ? 0.4195 0.2494 0.3386 -0.1750 0.0607  -0.0052 251 LEU B CD1 
6105  C CD2 . LEU B  251 ? 0.4424 0.2469 0.3348 -0.1755 0.0632  -0.0071 251 LEU B CD2 
6106  N N   . ALA B  252 ? 0.5141 0.3182 0.4056 -0.1579 0.0517  -0.0044 252 ALA B N   
6107  C CA  . ALA B  252 ? 0.5280 0.3269 0.4132 -0.1595 0.0510  -0.0066 252 ALA B CA  
6108  C C   . ALA B  252 ? 0.5098 0.3206 0.4038 -0.1584 0.0467  -0.0061 252 ALA B C   
6109  O O   . ALA B  252 ? 0.5279 0.3429 0.4232 -0.1637 0.0461  -0.0081 252 ALA B O   
6110  C CB  . ALA B  252 ? 0.5292 0.3148 0.4037 -0.1543 0.0513  -0.0065 252 ALA B CB  
6111  N N   . ARG B  253 ? 0.4062 0.2227 0.3064 -0.1520 0.0436  -0.0035 253 ARG B N   
6112  C CA  . ARG B  253 ? 0.4040 0.2304 0.3114 -0.1505 0.0392  -0.0026 253 ARG B CA  
6113  C C   . ARG B  253 ? 0.3767 0.2162 0.2955 -0.1558 0.0374  -0.0021 253 ARG B C   
6114  O O   . ARG B  253 ? 0.3724 0.2188 0.2943 -0.1574 0.0343  -0.0021 253 ARG B O   
6115  C CB  . ARG B  253 ? 0.4529 0.2817 0.3648 -0.1424 0.0365  0.0003  253 ARG B CB  
6116  C CG  . ARG B  253 ? 0.4276 0.2634 0.3437 -0.1401 0.0323  0.0014  253 ARG B CG  
6117  C CD  . ARG B  253 ? 0.4272 0.2582 0.3402 -0.1325 0.0311  0.0024  253 ARG B CD  
6118  N NE  . ARG B  253 ? 0.4661 0.2915 0.3777 -0.1283 0.0330  0.0034  253 ARG B NE  
6119  C CZ  . ARG B  253 ? 0.5415 0.3734 0.4625 -0.1256 0.0320  0.0060  253 ARG B CZ  
6120  N NH1 . ARG B  253 ? 0.5506 0.3944 0.4842 -0.1264 0.0290  0.0080  253 ARG B NH1 
6121  N NH2 . ARG B  253 ? 0.5754 0.4017 0.4936 -0.1224 0.0340  0.0065  253 ARG B NH2 
6122  N N   . LEU B  254 ? 0.3789 0.2218 0.3035 -0.1589 0.0394  -0.0018 254 LEU B N   
6123  C CA  . LEU B  254 ? 0.3756 0.2314 0.3126 -0.1641 0.0377  -0.0014 254 LEU B CA  
6124  C C   . LEU B  254 ? 0.3876 0.2435 0.3207 -0.1722 0.0390  -0.0047 254 LEU B C   
6125  O O   . LEU B  254 ? 0.3843 0.2508 0.3254 -0.1760 0.0359  -0.0046 254 LEU B O   
6126  C CB  . LEU B  254 ? 0.3732 0.2336 0.3196 -0.1646 0.0396  -0.0002 254 LEU B CB  
6127  C CG  . LEU B  254 ? 0.3578 0.2243 0.3147 -0.1579 0.0366  0.0033  254 LEU B CG  
6128  C CD1 . LEU B  254 ? 0.3557 0.2266 0.3220 -0.1584 0.0388  0.0041  254 LEU B CD1 
6129  C CD2 . LEU B  254 ? 0.3476 0.2256 0.3157 -0.1579 0.0314  0.0052  254 LEU B CD2 
6130  N N   . VAL B  255 ? 0.4649 0.3090 0.3861 -0.1750 0.0433  -0.0075 255 VAL B N   
6131  C CA  . VAL B  255 ? 0.5188 0.3598 0.4335 -0.1818 0.0446  -0.0110 255 VAL B CA  
6132  C C   . VAL B  255 ? 0.6164 0.4508 0.5222 -0.1784 0.0432  -0.0119 255 VAL B C   
6133  O O   . VAL B  255 ? 0.6732 0.5078 0.5799 -0.1716 0.0409  -0.0096 255 VAL B O   
6134  C CB  . VAL B  255 ? 0.4308 0.2616 0.3376 -0.1862 0.0499  -0.0133 255 VAL B CB  
6135  C CG1 . VAL B  255 ? 0.4290 0.2650 0.3437 -0.1874 0.0518  -0.0119 255 VAL B CG1 
6136  C CG2 . VAL B  255 ? 0.4380 0.2529 0.3318 -0.1816 0.0522  -0.0135 255 VAL B CG2 
6137  N N   . GLY B  256 ? 0.6179 0.4466 0.5159 -0.1832 0.0447  -0.0155 256 GLY B N   
6138  C CA  . GLY B  256 ? 0.6567 0.4810 0.5481 -0.1806 0.0433  -0.0168 256 GLY B CA  
6139  C C   . GLY B  256 ? 0.6264 0.4406 0.5116 -0.1727 0.0437  -0.0156 256 GLY B C   
6140  O O   . GLY B  256 ? 0.6101 0.4256 0.4943 -0.1692 0.0414  -0.0155 256 GLY B O   
6141  N N   . CYS B  257 ? 0.5442 0.3490 0.4254 -0.1701 0.0465  -0.0147 257 CYS B N   
6142  C CA  . CYS B  257 ? 0.5732 0.3645 0.4457 -0.1650 0.0479  -0.0149 257 CYS B CA  
6143  C C   . CYS B  257 ? 0.6587 0.4501 0.5328 -0.1563 0.0456  -0.0119 257 CYS B C   
6144  O O   . CYS B  257 ? 0.6636 0.4620 0.5442 -0.1536 0.0444  -0.0091 257 CYS B O   
6145  C CB  . CYS B  257 ? 0.5712 0.3504 0.4367 -0.1676 0.0519  -0.0155 257 CYS B CB  
6146  S SG  . CYS B  257 ? 0.9009 0.6799 0.7653 -0.1783 0.0549  -0.0190 257 CYS B SG  
6147  N N   . PRO B  258 ? 0.8195 0.6032 0.6882 -0.1519 0.0452  -0.0128 258 PRO B N   
6148  C CA  . PRO B  258 ? 0.9054 0.6814 0.7682 -0.1546 0.0465  -0.0164 258 PRO B CA  
6149  C C   . PRO B  258 ? 0.9683 0.7554 0.8353 -0.1578 0.0443  -0.0180 258 PRO B C   
6150  O O   . PRO B  258 ? 0.9502 0.7488 0.8241 -0.1558 0.0413  -0.0155 258 PRO B O   
6151  C CB  . PRO B  258 ? 1.0146 0.7815 0.8736 -0.1474 0.0459  -0.0159 258 PRO B CB  
6152  C CG  . PRO B  258 ? 0.9968 0.7720 0.8615 -0.1415 0.0432  -0.0126 258 PRO B CG  
6153  C CD  . PRO B  258 ? 0.9750 0.7577 0.8446 -0.1437 0.0433  -0.0103 258 PRO B CD  
6154  N N   . PRO B  259 ? 1.2602 1.0441 1.1233 -0.1628 0.0456  -0.0221 259 PRO B N   
6155  C CA  . PRO B  259 ? 1.3002 1.0957 1.1665 -0.1679 0.0438  -0.0238 259 PRO B CA  
6156  C C   . PRO B  259 ? 1.3439 1.1475 1.2133 -0.1638 0.0405  -0.0224 259 PRO B C   
6157  O O   . PRO B  259 ? 1.3639 1.1613 1.2301 -0.1597 0.0408  -0.0236 259 PRO B O   
6158  C CB  . PRO B  259 ? 0.8832 0.6712 0.7436 -0.1734 0.0464  -0.0291 259 PRO B CB  
6159  C CG  . PRO B  259 ? 0.8675 0.6402 0.7229 -0.1721 0.0496  -0.0296 259 PRO B CG  
6160  C CD  . PRO B  259 ? 0.8500 0.6195 0.7061 -0.1640 0.0485  -0.0254 259 PRO B CD  
6161  N N   . GLY B  260 ? 1.0419 0.8589 0.9179 -0.1653 0.0372  -0.0198 260 GLY B N   
6162  C CA  . GLY B  260 ? 1.0644 0.8896 0.9435 -0.1624 0.0338  -0.0179 260 GLY B CA  
6163  C C   . GLY B  260 ? 1.1328 0.9545 1.0132 -0.1536 0.0329  -0.0153 260 GLY B C   
6164  O O   . GLY B  260 ? 1.1330 0.9594 1.0146 -0.1512 0.0307  -0.0145 260 GLY B O   
6165  N N   . GLY B  261 ? 1.4004 1.2138 1.2799 -0.1493 0.0347  -0.0141 261 GLY B N   
6166  C CA  . GLY B  261 ? 1.3780 1.1882 1.2588 -0.1411 0.0338  -0.0116 261 GLY B CA  
6167  C C   . GLY B  261 ? 1.3277 1.1292 1.2037 -0.1369 0.0348  -0.0138 261 GLY B C   
6168  O O   . GLY B  261 ? 1.2932 1.0975 1.1719 -0.1319 0.0328  -0.0123 261 GLY B O   
6169  N N   . ALA B  262 ? 1.2171 1.0076 1.0867 -0.1390 0.0377  -0.0172 262 ALA B N   
6170  C CA  . ALA B  262 ? 1.2084 0.9897 1.0749 -0.1350 0.0386  -0.0195 262 ALA B CA  
6171  C C   . ALA B  262 ? 1.1860 0.9601 1.0524 -0.1276 0.0382  -0.0168 262 ALA B C   
6172  O O   . ALA B  262 ? 1.1905 0.9585 1.0563 -0.1230 0.0379  -0.0178 262 ALA B O   
6173  C CB  . ALA B  262 ? 1.2126 0.9840 1.0739 -0.1396 0.0415  -0.0240 262 ALA B CB  
6174  N N   . GLY B  263 ? 1.1147 0.8897 0.9818 -0.1269 0.0381  -0.0136 263 GLY B N   
6175  C CA  . GLY B  263 ? 1.0989 0.8674 0.9649 -0.1208 0.0379  -0.0111 263 GLY B CA  
6176  C C   . GLY B  263 ? 1.1135 0.8668 0.9729 -0.1199 0.0397  -0.0127 263 GLY B C   
6177  O O   . GLY B  263 ? 1.1348 0.8824 0.9911 -0.1247 0.0415  -0.0158 263 GLY B O   
6178  N N   . GLY B  264 ? 1.1341 0.8809 0.9920 -0.1140 0.0388  -0.0106 264 GLY B N   
6179  C CA  . GLY B  264 ? 1.1366 0.8686 0.9893 -0.1123 0.0394  -0.0114 264 GLY B CA  
6180  C C   . GLY B  264 ? 1.1420 0.8643 0.9881 -0.1154 0.0414  -0.0101 264 GLY B C   
6181  O O   . GLY B  264 ? 1.1419 0.8685 0.9873 -0.1166 0.0421  -0.0077 264 GLY B O   
6182  N N   . ASN B  265 ? 1.0278 0.7368 0.8695 -0.1171 0.0424  -0.0119 265 ASN B N   
6183  C CA  . ASN B  265 ? 0.9823 0.6786 0.8168 -0.1190 0.0438  -0.0102 265 ASN B CA  
6184  C C   . ASN B  265 ? 0.8362 0.5361 0.6678 -0.1251 0.0465  -0.0090 265 ASN B C   
6185  O O   . ASN B  265 ? 0.7811 0.4885 0.6154 -0.1306 0.0480  -0.0111 265 ASN B O   
6186  C CB  . ASN B  265 ? 1.2614 0.9426 1.0930 -0.1204 0.0441  -0.0125 265 ASN B CB  
6187  C CG  . ASN B  265 ? 1.3216 1.0054 1.1562 -0.1256 0.0455  -0.0172 265 ASN B CG  
6188  O OD1 . ASN B  265 ? 1.3145 1.0056 1.1490 -0.1318 0.0477  -0.0181 265 ASN B OD1 
6189  N ND2 . ASN B  265 ? 1.3698 1.0480 1.2078 -0.1232 0.0442  -0.0206 265 ASN B ND2 
6190  N N   . ASP B  266 ? 0.7389 0.4336 0.5655 -0.1241 0.0469  -0.0059 266 ASP B N   
6191  C CA  . ASP B  266 ? 0.7467 0.4442 0.5709 -0.1297 0.0497  -0.0048 266 ASP B CA  
6192  C C   . ASP B  266 ? 0.6631 0.3524 0.4833 -0.1371 0.0524  -0.0069 266 ASP B C   
6193  O O   . ASP B  266 ? 0.6194 0.3148 0.4407 -0.1433 0.0547  -0.0077 266 ASP B O   
6194  C CB  . ASP B  266 ? 1.1669 0.8582 0.9850 -0.1275 0.0499  -0.0014 266 ASP B CB  
6195  C CG  . ASP B  266 ? 1.2095 0.9106 1.0323 -0.1210 0.0476  0.0004  266 ASP B CG  
6196  O OD1 . ASP B  266 ? 1.1783 0.8923 1.0095 -0.1193 0.0462  -0.0007 266 ASP B OD1 
6197  O OD2 . ASP B  266 ? 1.2375 0.9327 1.0553 -0.1180 0.0470  0.0029  266 ASP B OD2 
6198  N N   . THR B  267 ? 0.7162 0.3917 0.5328 -0.1364 0.0518  -0.0078 267 THR B N   
6199  C CA  . THR B  267 ? 0.7381 0.4037 0.5512 -0.1432 0.0541  -0.0099 267 THR B CA  
6200  C C   . THR B  267 ? 0.6446 0.3207 0.4629 -0.1490 0.0556  -0.0137 267 THR B C   
6201  O O   . THR B  267 ? 0.5913 0.2666 0.4076 -0.1562 0.0584  -0.0147 267 THR B O   
6202  C CB  . THR B  267 ? 1.0567 0.7073 0.8684 -0.1403 0.0522  -0.0109 267 THR B CB  
6203  O OG1 . THR B  267 ? 1.1127 0.7692 0.9309 -0.1340 0.0494  -0.0125 267 THR B OG1 
6204  C CG2 . THR B  267 ? 1.0702 0.7064 0.8747 -0.1374 0.0511  -0.0069 267 THR B CG2 
6205  N N   . GLU B  268 ? 0.7183 0.4044 0.5429 -0.1461 0.0538  -0.0158 268 GLU B N   
6206  C CA  . GLU B  268 ? 0.7428 0.4398 0.5720 -0.1516 0.0547  -0.0192 268 GLU B CA  
6207  C C   . GLU B  268 ? 0.7183 0.4295 0.5508 -0.1542 0.0553  -0.0176 268 GLU B C   
6208  O O   . GLU B  268 ? 0.7677 0.4848 0.6021 -0.1609 0.0568  -0.0197 268 GLU B O   
6209  C CB  . GLU B  268 ? 1.0691 0.7724 0.9035 -0.1482 0.0526  -0.0218 268 GLU B CB  
6210  C CG  . GLU B  268 ? 1.1953 0.8955 1.0303 -0.1534 0.0537  -0.0269 268 GLU B CG  
6211  C CD  . GLU B  268 ? 1.2841 0.9888 1.1234 -0.1499 0.0519  -0.0299 268 GLU B CD  
6212  O OE1 . GLU B  268 ? 1.2667 0.9806 1.1093 -0.1448 0.0499  -0.0278 268 GLU B OE1 
6213  O OE2 . GLU B  268 ? 1.3471 1.0460 1.1868 -0.1524 0.0526  -0.0346 268 GLU B OE2 
6214  N N   . LEU B  269 ? 0.7268 0.4435 0.5609 -0.1492 0.0540  -0.0142 269 LEU B N   
6215  C CA  . LEU B  269 ? 0.6421 0.3718 0.4811 -0.1516 0.0543  -0.0129 269 LEU B CA  
6216  C C   . LEU B  269 ? 0.6265 0.3519 0.4618 -0.1583 0.0577  -0.0127 269 LEU B C   
6217  O O   . LEU B  269 ? 0.6357 0.3701 0.4753 -0.1641 0.0588  -0.0139 269 LEU B O   
6218  C CB  . LEU B  269 ? 0.5714 0.3075 0.4139 -0.1448 0.0522  -0.0096 269 LEU B CB  
6219  C CG  . LEU B  269 ? 0.5156 0.2658 0.3656 -0.1463 0.0519  -0.0083 269 LEU B CG  
6220  C CD1 . LEU B  269 ? 0.4989 0.2595 0.3563 -0.1399 0.0485  -0.0065 269 LEU B CD1 
6221  C CD2 . LEU B  269 ? 0.4961 0.2427 0.3430 -0.1480 0.0545  -0.0065 269 LEU B CD2 
6222  N N   . ILE B  270 ? 0.5069 0.2182 0.3342 -0.1580 0.0593  -0.0112 270 ILE B N   
6223  C CA  . ILE B  270 ? 0.5220 0.2277 0.3446 -0.1648 0.0628  -0.0110 270 ILE B CA  
6224  C C   . ILE B  270 ? 0.6707 0.3726 0.4925 -0.1721 0.0647  -0.0144 270 ILE B C   
6225  O O   . ILE B  270 ? 0.5418 0.2465 0.3641 -0.1794 0.0674  -0.0155 270 ILE B O   
6226  C CB  . ILE B  270 ? 0.5363 0.2267 0.3495 -0.1630 0.0637  -0.0082 270 ILE B CB  
6227  C CG1 . ILE B  270 ? 0.5234 0.2178 0.3374 -0.1557 0.0617  -0.0052 270 ILE B CG1 
6228  C CG2 . ILE B  270 ? 0.5523 0.2375 0.3604 -0.1708 0.0677  -0.0078 270 ILE B CG2 
6229  C CD1 . ILE B  270 ? 0.5100 0.2188 0.3304 -0.1568 0.0626  -0.0047 270 ILE B CD1 
6230  N N   . ALA B  271 ? 0.7926 0.4884 0.6138 -0.1703 0.0632  -0.0165 271 ALA B N   
6231  C CA  . ALA B  271 ? 0.7684 0.4599 0.5892 -0.1768 0.0648  -0.0204 271 ALA B CA  
6232  C C   . ALA B  271 ? 0.6912 0.3987 0.5188 -0.1818 0.0649  -0.0229 271 ALA B C   
6233  O O   . ALA B  271 ? 0.7099 0.4177 0.5376 -0.1894 0.0672  -0.0253 271 ALA B O   
6234  C CB  . ALA B  271 ? 0.8040 0.4876 0.6245 -0.1732 0.0629  -0.0225 271 ALA B CB  
6235  N N   . CYS B  272 ? 0.6392 0.3600 0.4730 -0.1774 0.0622  -0.0221 272 CYS B N   
6236  C CA  . CYS B  272 ? 0.6124 0.3489 0.4534 -0.1813 0.0613  -0.0238 272 CYS B CA  
6237  C C   . CYS B  272 ? 0.6491 0.3933 0.4935 -0.1855 0.0629  -0.0223 272 CYS B C   
6238  O O   . CYS B  272 ? 0.6516 0.4029 0.4997 -0.1927 0.0639  -0.0245 272 CYS B O   
6239  C CB  . CYS B  272 ? 0.4914 0.2387 0.3379 -0.1751 0.0576  -0.0228 272 CYS B CB  
6240  S SG  . CYS B  272 ? 0.8523 0.6195 0.7083 -0.1789 0.0553  -0.0233 272 CYS B SG  
6241  N N   . LEU B  273 ? 0.6455 0.3884 0.4891 -0.1814 0.0632  -0.0188 273 LEU B N   
6242  C CA  . LEU B  273 ? 0.6115 0.3614 0.4590 -0.1850 0.0651  -0.0175 273 LEU B CA  
6243  C C   . LEU B  273 ? 0.6447 0.3878 0.4879 -0.1936 0.0691  -0.0195 273 LEU B C   
6244  O O   . LEU B  273 ? 0.6491 0.4010 0.4976 -0.1995 0.0706  -0.0203 273 LEU B O   
6245  C CB  . LEU B  273 ? 0.5010 0.2473 0.3459 -0.1797 0.0654  -0.0140 273 LEU B CB  
6246  C CG  . LEU B  273 ? 0.4809 0.2403 0.3348 -0.1744 0.0628  -0.0118 273 LEU B CG  
6247  C CD1 . LEU B  273 ? 0.4824 0.2361 0.3320 -0.1708 0.0641  -0.0091 273 LEU B CD1 
6248  C CD2 . LEU B  273 ? 0.4735 0.2481 0.3382 -0.1794 0.0627  -0.0126 273 LEU B CD2 
6249  N N   . ARG B  274 ? 0.5573 0.2844 0.3914 -0.1945 0.0706  -0.0202 274 ARG B N   
6250  C CA  . ARG B  274 ? 0.5601 0.2784 0.3893 -0.2026 0.0744  -0.0217 274 ARG B CA  
6251  C C   . ARG B  274 ? 0.5685 0.2950 0.4030 -0.2101 0.0750  -0.0256 274 ARG B C   
6252  O O   . ARG B  274 ? 0.6078 0.3329 0.4415 -0.2179 0.0783  -0.0269 274 ARG B O   
6253  C CB  . ARG B  274 ? 0.6956 0.3943 0.5151 -0.2016 0.0752  -0.0213 274 ARG B CB  
6254  C CG  . ARG B  274 ? 0.7744 0.4622 0.5862 -0.1996 0.0766  -0.0175 274 ARG B CG  
6255  C CD  . ARG B  274 ? 0.8725 0.5404 0.6754 -0.2011 0.0775  -0.0171 274 ARG B CD  
6256  N NE  . ARG B  274 ? 0.9188 0.5773 0.7181 -0.1926 0.0744  -0.0148 274 ARG B NE  
6257  C CZ  . ARG B  274 ? 0.9609 0.6110 0.7538 -0.1890 0.0741  -0.0108 274 ARG B CZ  
6258  N NH1 . ARG B  274 ? 0.9663 0.6162 0.7551 -0.1932 0.0771  -0.0088 274 ARG B NH1 
6259  N NH2 . ARG B  274 ? 0.9947 0.6367 0.7852 -0.1814 0.0709  -0.0090 274 ARG B NH2 
6260  N N   . THR B  275 ? 0.6445 0.3799 0.4842 -0.2083 0.0719  -0.0275 275 THR B N   
6261  C CA  . THR B  275 ? 0.6646 0.4078 0.5087 -0.2155 0.0720  -0.0316 275 THR B CA  
6262  C C   . THR B  275 ? 0.6095 0.3718 0.4641 -0.2180 0.0703  -0.0315 275 THR B C   
6263  O O   . THR B  275 ? 0.5958 0.3666 0.4548 -0.2233 0.0694  -0.0346 275 THR B O   
6264  C CB  . THR B  275 ? 0.6936 0.4354 0.5369 -0.2136 0.0697  -0.0344 275 THR B CB  
6265  O OG1 . THR B  275 ? 0.6963 0.4537 0.5468 -0.2106 0.0660  -0.0338 275 THR B OG1 
6266  C CG2 . THR B  275 ? 0.6880 0.4148 0.5245 -0.2070 0.0694  -0.0332 275 THR B CG2 
6267  N N   . ARG B  276 ? 0.5279 0.2972 0.3871 -0.2141 0.0696  -0.0281 276 ARG B N   
6268  C CA  . ARG B  276 ? 0.5159 0.3028 0.3868 -0.2165 0.0679  -0.0277 276 ARG B CA  
6269  C C   . ARG B  276 ? 0.6262 0.4143 0.4991 -0.2240 0.0719  -0.0286 276 ARG B C   
6270  O O   . ARG B  276 ? 0.5382 0.3151 0.4040 -0.2246 0.0756  -0.0277 276 ARG B O   
6271  C CB  . ARG B  276 ? 0.4975 0.2919 0.3743 -0.2087 0.0651  -0.0239 276 ARG B CB  
6272  C CG  . ARG B  276 ? 0.6841 0.4772 0.5588 -0.2015 0.0615  -0.0229 276 ARG B CG  
6273  C CD  . ARG B  276 ? 0.6774 0.4844 0.5602 -0.2029 0.0574  -0.0238 276 ARG B CD  
6274  N NE  . ARG B  276 ? 0.6982 0.5037 0.5781 -0.1974 0.0545  -0.0236 276 ARG B NE  
6275  C CZ  . ARG B  276 ? 0.7530 0.5540 0.6274 -0.1999 0.0545  -0.0269 276 ARG B CZ  
6276  N NH1 . ARG B  276 ? 0.8044 0.6020 0.6760 -0.2075 0.0571  -0.0306 276 ARG B NH1 
6277  N NH2 . ARG B  276 ? 0.7464 0.5468 0.6186 -0.1951 0.0522  -0.0269 276 ARG B NH2 
6278  N N   . PRO B  277 ? 0.5243 0.3262 0.4069 -0.2300 0.0710  -0.0305 277 PRO B N   
6279  C CA  . PRO B  277 ? 0.6093 0.4162 0.4970 -0.2372 0.0744  -0.0316 277 PRO B CA  
6280  C C   . PRO B  277 ? 0.5592 0.3671 0.4492 -0.2339 0.0763  -0.0285 277 PRO B C   
6281  O O   . PRO B  277 ? 0.5100 0.3259 0.4067 -0.2274 0.0731  -0.0258 277 PRO B O   
6282  C CB  . PRO B  277 ? 0.5891 0.4145 0.4902 -0.2407 0.0708  -0.0329 277 PRO B CB  
6283  C CG  . PRO B  277 ? 0.5200 0.3447 0.4178 -0.2396 0.0674  -0.0344 277 PRO B CG  
6284  C CD  . PRO B  277 ? 0.5152 0.3288 0.4045 -0.2309 0.0666  -0.0320 277 PRO B CD  
6285  N N   . ALA B  278 ? 0.5417 0.3421 0.4264 -0.2388 0.0815  -0.0289 278 ALA B N   
6286  C CA  . ALA B  278 ? 0.5783 0.3788 0.4636 -0.2367 0.0841  -0.0265 278 ALA B CA  
6287  C C   . ALA B  278 ? 0.5292 0.3483 0.4307 -0.2348 0.0817  -0.0255 278 ALA B C   
6288  O O   . ALA B  278 ? 0.5104 0.3317 0.4145 -0.2286 0.0810  -0.0228 278 ALA B O   
6289  C CB  . ALA B  278 ? 0.7111 0.5040 0.5903 -0.2447 0.0903  -0.0279 278 ALA B CB  
6290  N N   . GLN B  279 ? 0.6134 0.4460 0.5265 -0.2403 0.0803  -0.0277 279 GLN B N   
6291  C CA  . GLN B  279 ? 0.6408 0.4915 0.5712 -0.2392 0.0776  -0.0267 279 GLN B CA  
6292  C C   . GLN B  279 ? 0.6308 0.4870 0.5668 -0.2303 0.0715  -0.0236 279 GLN B C   
6293  O O   . GLN B  279 ? 0.6468 0.5144 0.5956 -0.2270 0.0694  -0.0216 279 GLN B O   
6294  C CB  . GLN B  279 ? 0.7369 0.6012 0.6793 -0.2474 0.0769  -0.0297 279 GLN B CB  
6295  C CG  . GLN B  279 ? 0.7347 0.6186 0.6976 -0.2466 0.0736  -0.0286 279 GLN B CG  
6296  C CD  . GLN B  279 ? 0.7172 0.6037 0.6850 -0.2444 0.0769  -0.0272 279 GLN B CD  
6297  O OE1 . GLN B  279 ? 0.7294 0.6073 0.6884 -0.2480 0.0831  -0.0285 279 GLN B OE1 
6298  N NE2 . GLN B  279 ? 0.6615 0.5597 0.6436 -0.2387 0.0727  -0.0245 279 GLN B NE2 
6299  N N   . ASP B  280 ? 0.5438 0.3917 0.4705 -0.2264 0.0689  -0.0232 280 ASP B N   
6300  C CA  . ASP B  280 ? 0.5524 0.4049 0.4834 -0.2183 0.0635  -0.0203 280 ASP B CA  
6301  C C   . ASP B  280 ? 0.5145 0.3614 0.4425 -0.2108 0.0644  -0.0173 280 ASP B C   
6302  O O   . ASP B  280 ? 0.4891 0.3452 0.4277 -0.2054 0.0610  -0.0146 280 ASP B O   
6303  C CB  . ASP B  280 ? 0.7227 0.5686 0.6447 -0.2168 0.0609  -0.0213 280 ASP B CB  
6304  C CG  . ASP B  280 ? 0.7602 0.6156 0.6879 -0.2232 0.0584  -0.0238 280 ASP B CG  
6305  O OD1 . ASP B  280 ? 0.7895 0.6596 0.7314 -0.2260 0.0563  -0.0235 280 ASP B OD1 
6306  O OD2 . ASP B  280 ? 0.7401 0.5886 0.6588 -0.2254 0.0584  -0.0263 280 ASP B OD2 
6307  N N   . LEU B  281 ? 0.4717 0.3034 0.3857 -0.2106 0.0687  -0.0177 281 LEU B N   
6308  C CA  . LEU B  281 ? 0.4683 0.2936 0.3777 -0.2045 0.0700  -0.0152 281 LEU B CA  
6309  C C   . LEU B  281 ? 0.4622 0.2986 0.3834 -0.2058 0.0715  -0.0146 281 LEU B C   
6310  O O   . LEU B  281 ? 0.4485 0.2903 0.3767 -0.1998 0.0694  -0.0122 281 LEU B O   
6311  C CB  . LEU B  281 ? 0.4864 0.2940 0.3793 -0.2061 0.0745  -0.0158 281 LEU B CB  
6312  C CG  . LEU B  281 ? 0.4951 0.2908 0.3769 -0.2056 0.0735  -0.0168 281 LEU B CG  
6313  C CD1 . LEU B  281 ? 0.5120 0.2898 0.3790 -0.2059 0.0772  -0.0163 281 LEU B CD1 
6314  C CD2 . LEU B  281 ? 0.4803 0.2781 0.3638 -0.1976 0.0684  -0.0153 281 LEU B CD2 
6315  N N   . VAL B  282 ? 0.4725 0.3129 0.3971 -0.2140 0.0753  -0.0170 282 VAL B N   
6316  C CA  . VAL B  282 ? 0.4671 0.3194 0.4046 -0.2159 0.0771  -0.0170 282 VAL B CA  
6317  C C   . VAL B  282 ? 0.4472 0.3166 0.4041 -0.2122 0.0715  -0.0153 282 VAL B C   
6318  O O   . VAL B  282 ? 0.4370 0.3129 0.4030 -0.2085 0.0712  -0.0137 282 VAL B O   
6319  C CB  . VAL B  282 ? 0.4815 0.3368 0.4207 -0.2258 0.0820  -0.0203 282 VAL B CB  
6320  C CG1 . VAL B  282 ? 0.4765 0.3440 0.4290 -0.2277 0.0844  -0.0207 282 VAL B CG1 
6321  C CG2 . VAL B  282 ? 0.5017 0.3393 0.4222 -0.2294 0.0873  -0.0213 282 VAL B CG2 
6322  N N   . ASP B  283 ? 0.4590 0.3352 0.4220 -0.2134 0.0668  -0.0155 283 ASP B N   
6323  C CA  . ASP B  283 ? 0.5224 0.4139 0.5033 -0.2103 0.0607  -0.0134 283 ASP B CA  
6324  C C   . ASP B  283 ? 0.5890 0.4791 0.5712 -0.2008 0.0574  -0.0098 283 ASP B C   
6325  O O   . ASP B  283 ? 0.6205 0.5207 0.6176 -0.1978 0.0554  -0.0078 283 ASP B O   
6326  C CB  . ASP B  283 ? 0.6589 0.5551 0.6420 -0.2130 0.0562  -0.0142 283 ASP B CB  
6327  C CG  . ASP B  283 ? 0.7407 0.6442 0.7295 -0.2224 0.0578  -0.0176 283 ASP B CG  
6328  O OD1 . ASP B  283 ? 0.7869 0.6966 0.7839 -0.2263 0.0613  -0.0188 283 ASP B OD1 
6329  O OD2 . ASP B  283 ? 0.7459 0.6495 0.7312 -0.2261 0.0558  -0.0193 283 ASP B OD2 
6330  N N   . HIS B  284 ? 0.5448 0.4225 0.5124 -0.1962 0.0567  -0.0090 284 HIS B N   
6331  C CA  . HIS B  284 ? 0.5044 0.3812 0.4734 -0.1874 0.0534  -0.0057 284 HIS B CA  
6332  C C   . HIS B  284 ? 0.4726 0.3419 0.4356 -0.1837 0.0571  -0.0050 284 HIS B C   
6333  O O   . HIS B  284 ? 0.4530 0.3206 0.4162 -0.1764 0.0548  -0.0026 284 HIS B O   
6334  C CB  . HIS B  284 ? 0.6124 0.4814 0.5705 -0.1837 0.0505  -0.0053 284 HIS B CB  
6335  C CG  . HIS B  284 ? 0.6712 0.5486 0.6354 -0.1866 0.0462  -0.0057 284 HIS B CG  
6336  N ND1 . HIS B  284 ? 0.6988 0.5894 0.6786 -0.1844 0.0409  -0.0031 284 HIS B ND1 
6337  C CD2 . HIS B  284 ? 0.7003 0.5750 0.6573 -0.1919 0.0464  -0.0083 284 HIS B CD2 
6338  C CE1 . HIS B  284 ? 0.7255 0.6212 0.7064 -0.1884 0.0379  -0.0041 284 HIS B CE1 
6339  N NE2 . HIS B  284 ? 0.7231 0.6096 0.6903 -0.1930 0.0412  -0.0075 284 HIS B NE2 
6340  N N   . GLU B  285 ? 0.4128 0.2778 0.3704 -0.1889 0.0629  -0.0072 285 GLU B N   
6341  C CA  . GLU B  285 ? 0.4696 0.3258 0.4183 -0.1864 0.0670  -0.0069 285 GLU B CA  
6342  C C   . GLU B  285 ? 0.5023 0.3671 0.4635 -0.1813 0.0655  -0.0049 285 GLU B C   
6343  O O   . GLU B  285 ? 0.4004 0.2582 0.3548 -0.1758 0.0660  -0.0036 285 GLU B O   
6344  C CB  . GLU B  285 ? 0.9378 0.7894 0.8797 -0.1942 0.0737  -0.0096 285 GLU B CB  
6345  C CG  . GLU B  285 ? 0.9956 0.8325 0.9212 -0.1927 0.0780  -0.0093 285 GLU B CG  
6346  C CD  . GLU B  285 ? 1.0453 0.8832 0.9704 -0.1988 0.0843  -0.0112 285 GLU B CD  
6347  O OE1 . GLU B  285 ? 1.0625 0.9112 0.9984 -0.2053 0.0860  -0.0133 285 GLU B OE1 
6348  O OE2 . GLU B  285 ? 1.0585 0.8870 0.9728 -0.1974 0.0876  -0.0107 285 GLU B OE2 
6349  N N   . TRP B  286 ? 0.8723 0.7525 0.8525 -0.1832 0.0633  -0.0046 286 TRP B N   
6350  C CA  . TRP B  286 ? 0.9322 0.8210 0.9258 -0.1798 0.0627  -0.0033 286 TRP B CA  
6351  C C   . TRP B  286 ? 0.9184 0.8104 0.9198 -0.1715 0.0563  0.0003  286 TRP B C   
6352  O O   . TRP B  286 ? 0.9299 0.8280 0.9423 -0.1680 0.0552  0.0017  286 TRP B O   
6353  C CB  . TRP B  286 ? 1.0793 0.9832 1.0909 -0.1858 0.0636  -0.0049 286 TRP B CB  
6354  C CG  . TRP B  286 ? 1.1540 1.0543 1.1579 -0.1926 0.0715  -0.0085 286 TRP B CG  
6355  C CD1 . TRP B  286 ? 1.1335 1.0336 1.1336 -0.2008 0.0752  -0.0115 286 TRP B CD1 
6356  C CD2 . TRP B  286 ? 1.2081 1.1039 1.2060 -0.1920 0.0769  -0.0097 286 TRP B CD2 
6357  N NE1 . TRP B  286 ? 1.1291 1.0249 1.1216 -0.2055 0.0826  -0.0142 286 TRP B NE1 
6358  C CE2 . TRP B  286 ? 1.1761 1.0692 1.1667 -0.2003 0.0839  -0.0132 286 TRP B CE2 
6359  C CE3 . TRP B  286 ? 1.2283 1.1221 1.2262 -0.1857 0.0767  -0.0082 286 TRP B CE3 
6360  C CZ2 . TRP B  286 ? 1.2041 1.0927 1.1870 -0.2026 0.0907  -0.0151 286 TRP B CZ2 
6361  C CZ3 . TRP B  286 ? 1.2125 1.1019 1.2028 -0.1878 0.0834  -0.0104 286 TRP B CZ3 
6362  C CH2 . TRP B  286 ? 1.2113 1.0982 1.1940 -0.1963 0.0903  -0.0137 286 TRP B CH2 
6363  N N   . HIS B  287 ? 0.7573 0.6449 0.7526 -0.1687 0.0524  0.0016  287 HIS B N   
6364  C CA  . HIS B  287 ? 0.7034 0.5943 0.7058 -0.1615 0.0465  0.0049  287 HIS B CA  
6365  C C   . HIS B  287 ? 0.5995 0.4801 0.5909 -0.1543 0.0466  0.0061  287 HIS B C   
6366  O O   . HIS B  287 ? 0.5785 0.4626 0.5775 -0.1483 0.0422  0.0088  287 HIS B O   
6367  C CB  . HIS B  287 ? 1.0004 0.8928 1.0021 -0.1623 0.0423  0.0054  287 HIS B CB  
6368  C CG  . HIS B  287 ? 1.1195 1.0247 1.1362 -0.1680 0.0401  0.0050  287 HIS B CG  
6369  N ND1 . HIS B  287 ? 1.1562 1.0686 1.1822 -0.1736 0.0429  0.0033  287 HIS B ND1 
6370  C CD2 . HIS B  287 ? 1.1796 1.0920 1.2036 -0.1692 0.0353  0.0059  287 HIS B CD2 
6371  C CE1 . HIS B  287 ? 1.1979 1.1217 1.2373 -0.1778 0.0395  0.0032  287 HIS B CE1 
6372  N NE2 . HIS B  287 ? 1.2202 1.1439 1.2583 -0.1752 0.0349  0.0049  287 HIS B NE2 
6373  N N   . VAL B  288 ? 0.5812 0.4494 0.5554 -0.1549 0.0513  0.0043  288 VAL B N   
6374  C CA  . VAL B  288 ? 0.5945 0.4525 0.5574 -0.1482 0.0508  0.0054  288 VAL B CA  
6375  C C   . VAL B  288 ? 0.6149 0.4734 0.5811 -0.1443 0.0522  0.0061  288 VAL B C   
6376  O O   . VAL B  288 ? 0.6101 0.4606 0.5673 -0.1389 0.0520  0.0068  288 VAL B O   
6377  C CB  . VAL B  288 ? 0.3709 0.2139 0.3132 -0.1495 0.0538  0.0036  288 VAL B CB  
6378  C CG1 . VAL B  288 ? 0.3781 0.2211 0.3179 -0.1549 0.0534  0.0020  288 VAL B CG1 
6379  C CG2 . VAL B  288 ? 0.5322 0.3670 0.4643 -0.1528 0.0598  0.0020  288 VAL B CG2 
6380  N N   . LEU B  289 ? 0.7846 0.6530 0.7644 -0.1473 0.0535  0.0058  289 LEU B N   
6381  C CA  . LEU B  289 ? 0.8255 0.6948 0.8086 -0.1445 0.0553  0.0058  289 LEU B CA  
6382  C C   . LEU B  289 ? 0.9480 0.8228 0.9428 -0.1372 0.0496  0.0088  289 LEU B C   
6383  O O   . LEU B  289 ? 0.9878 0.8720 0.9972 -0.1365 0.0445  0.0109  289 LEU B O   
6384  C CB  . LEU B  289 ? 0.5778 0.4562 0.5716 -0.1506 0.0591  0.0038  289 LEU B CB  
6385  C CG  . LEU B  289 ? 0.5348 0.4048 0.5133 -0.1569 0.0664  0.0006  289 LEU B CG  
6386  C CD1 . LEU B  289 ? 0.5559 0.4364 0.5456 -0.1641 0.0706  -0.0021 289 LEU B CD1 
6387  C CD2 . LEU B  289 ? 0.4941 0.3524 0.4577 -0.1538 0.0697  0.0003  289 LEU B CD2 
6388  N N   . PRO B  290 ? 0.9946 0.8633 0.9830 -0.1322 0.0503  0.0091  290 PRO B N   
6389  C CA  . PRO B  290 ? 1.0126 0.8845 1.0098 -0.1250 0.0452  0.0117  290 PRO B CA  
6390  C C   . PRO B  290 ? 1.0502 0.9355 1.0695 -0.1251 0.0417  0.0133  290 PRO B C   
6391  O O   . PRO B  290 ? 1.0494 0.9404 1.0805 -0.1216 0.0355  0.0164  290 PRO B O   
6392  C CB  . PRO B  290 ? 0.9280 0.7907 0.9129 -0.1216 0.0483  0.0106  290 PRO B CB  
6393  C CG  . PRO B  290 ? 0.9443 0.7960 0.9104 -0.1258 0.0538  0.0083  290 PRO B CG  
6394  C CD  . PRO B  290 ? 0.9389 0.7963 0.9101 -0.1333 0.0562  0.0069  290 PRO B CD  
6395  N N   . GLN B  291 ? 1.0358 0.9259 1.0608 -0.1293 0.0456  0.0110  291 GLN B N   
6396  C CA  . GLN B  291 ? 1.0471 0.9500 1.0929 -0.1300 0.0421  0.0120  291 GLN B CA  
6397  C C   . GLN B  291 ? 1.0293 0.9415 1.0844 -0.1376 0.0448  0.0098  291 GLN B C   
6398  O O   . GLN B  291 ? 0.9882 0.8965 1.0333 -0.1424 0.0496  0.0076  291 GLN B O   
6399  C CB  . GLN B  291 ? 1.1515 1.0533 1.1977 -0.1273 0.0441  0.0104  291 GLN B CB  
6400  C CG  . GLN B  291 ? 1.1737 1.0655 1.2087 -0.1202 0.0428  0.0116  291 GLN B CG  
6401  C CD  . GLN B  291 ? 1.2182 1.0983 1.2334 -0.1208 0.0500  0.0086  291 GLN B CD  
6402  O OE1 . GLN B  291 ? 1.2335 1.1133 1.2444 -0.1264 0.0565  0.0054  291 GLN B OE1 
6403  N NE2 . GLN B  291 ? 1.2364 1.1070 1.2394 -0.1153 0.0487  0.0097  291 GLN B NE2 
6404  N N   . GLU B  292 ? 1.2183 1.1430 1.2924 -0.1390 0.0413  0.0104  292 GLU B N   
6405  C CA  . GLU B  292 ? 1.2561 1.1916 1.3410 -0.1461 0.0441  0.0076  292 GLU B CA  
6406  C C   . GLU B  292 ? 1.2275 1.1605 1.3050 -0.1489 0.0535  0.0022  292 GLU B C   
6407  O O   . GLU B  292 ? 1.2313 1.1626 1.3084 -0.1458 0.0553  0.0006  292 GLU B O   
6408  C CB  . GLU B  292 ? 1.1430 1.0932 1.2497 -0.1469 0.0367  0.0099  292 GLU B CB  
6409  C CG  . GLU B  292 ? 1.1558 1.1168 1.2747 -0.1529 0.0341  0.0105  292 GLU B CG  
6410  C CD  . GLU B  292 ? 1.1871 1.1412 1.2975 -0.1528 0.0333  0.0124  292 GLU B CD  
6411  O OE1 . GLU B  292 ? 1.1765 1.1286 1.2890 -0.1487 0.0266  0.0170  292 GLU B OE1 
6412  O OE2 . GLU B  292 ? 1.1991 1.1496 1.2996 -0.1574 0.0401  0.0087  292 GLU B OE2 
6413  N N   . SER B  293 ? 0.9093 0.8413 0.9797 -0.1552 0.0602  -0.0012 293 SER B N   
6414  C CA  . SER B  293 ? 0.8689 0.7961 0.9283 -0.1586 0.0699  -0.0062 293 SER B CA  
6415  C C   . SER B  293 ? 0.8674 0.8014 0.9292 -0.1680 0.0778  -0.0117 293 SER B C   
6416  O O   . SER B  293 ? 0.8256 0.7665 0.8951 -0.1719 0.0755  -0.0111 293 SER B O   
6417  C CB  . SER B  293 ? 0.8958 0.8055 0.9309 -0.1559 0.0726  -0.0053 293 SER B CB  
6418  O OG  . SER B  293 ? 0.8910 0.7938 0.9160 -0.1568 0.0706  -0.0033 293 SER B OG  
6419  N N   . ILE B  294 ? 1.2287 1.1606 1.2833 -0.1717 0.0872  -0.0174 294 ILE B N   
6420  C CA  . ILE B  294 ? 1.2742 1.2137 1.3320 -0.1808 0.0961  -0.0239 294 ILE B CA  
6421  C C   . ILE B  294 ? 1.2663 1.1927 1.3008 -0.1858 0.1028  -0.0248 294 ILE B C   
6422  O O   . ILE B  294 ? 1.3306 1.2572 1.3622 -0.1912 0.1038  -0.0248 294 ILE B O   
6423  C CB  . ILE B  294 ? 1.1706 1.1206 1.2414 -0.1824 0.1024  -0.0310 294 ILE B CB  
6424  C CG1 . ILE B  294 ? 1.1759 1.1426 1.2738 -0.1801 0.0961  -0.0313 294 ILE B CG1 
6425  C CG2 . ILE B  294 ? 1.1909 1.1461 1.2597 -0.1917 0.1136  -0.0387 294 ILE B CG2 
6426  C CD1 . ILE B  294 ? 1.1746 1.1506 1.2834 -0.1839 0.0913  -0.0292 294 ILE B CD1 
6427  N N   . PHE B  295 ? 0.7286 0.6430 0.7463 -0.1842 0.1069  -0.0253 295 PHE B N   
6428  C CA  . PHE B  295 ? 0.7142 0.6122 0.7074 -0.1862 0.1097  -0.0234 295 PHE B CA  
6429  C C   . PHE B  295 ? 0.7559 0.6454 0.7443 -0.1778 0.1001  -0.0165 295 PHE B C   
6430  O O   . PHE B  295 ? 0.7726 0.6702 0.7756 -0.1748 0.0935  -0.0143 295 PHE B O   
6431  C CB  . PHE B  295 ? 1.0231 0.9120 1.0007 -0.1879 0.1171  -0.0264 295 PHE B CB  
6432  C CG  . PHE B  295 ? 1.0579 0.9460 1.0257 -0.1987 0.1277  -0.0319 295 PHE B CG  
6433  C CD1 . PHE B  295 ? 1.0637 0.9381 1.0110 -0.2029 0.1295  -0.0297 295 PHE B CD1 
6434  C CD2 . PHE B  295 ? 1.0076 0.9089 0.9872 -0.2047 0.1357  -0.0396 295 PHE B CD2 
6435  C CE1 . PHE B  295 ? 1.0094 0.8824 0.9470 -0.2132 0.1388  -0.0342 295 PHE B CE1 
6436  C CE2 . PHE B  295 ? 0.9598 0.8606 0.9300 -0.2147 0.1454  -0.0448 295 PHE B CE2 
6437  C CZ  . PHE B  295 ? 0.9758 0.8622 0.9245 -0.2192 0.1468  -0.0417 295 PHE B CZ  
6438  N N   . ARG B  296 ? 1.3477 1.2204 1.3145 -0.1759 0.1004  -0.0144 296 ARG B N   
6439  C CA  . ARG B  296 ? 1.4051 1.2700 1.3665 -0.1692 0.0932  -0.0101 296 ARG B CA  
6440  C C   . ARG B  296 ? 1.4600 1.3253 1.4222 -0.1719 0.0904  -0.0091 296 ARG B C   
6441  O O   . ARG B  296 ? 1.5002 1.3763 1.4787 -0.1703 0.0853  -0.0080 296 ARG B O   
6442  C CB  . ARG B  296 ? 1.0539 0.9259 1.0300 -0.1609 0.0865  -0.0079 296 ARG B CB  
6443  C CG  . ARG B  296 ? 1.0080 0.8696 0.9732 -0.1538 0.0845  -0.0058 296 ARG B CG  
6444  C CD  . ARG B  296 ? 1.0039 0.8561 0.9529 -0.1568 0.0913  -0.0080 296 ARG B CD  
6445  N NE  . ARG B  296 ? 0.9480 0.8101 0.9068 -0.1611 0.0969  -0.0118 296 ARG B NE  
6446  C CZ  . ARG B  296 ? 0.9007 0.7653 0.8639 -0.1584 0.0984  -0.0138 296 ARG B CZ  
6447  N NH1 . ARG B  296 ? 0.8445 0.7042 0.8062 -0.1499 0.0924  -0.0104 296 ARG B NH1 
6448  N NH2 . ARG B  296 ? 0.9238 0.7959 0.8931 -0.1646 0.1065  -0.0201 296 ARG B NH2 
6449  N N   . PHE B  297 ? 1.1187 0.9724 1.0634 -0.1768 0.0940  -0.0097 297 PHE B N   
6450  C CA  . PHE B  297 ? 1.0422 0.8936 0.9842 -0.1798 0.0921  -0.0092 297 PHE B CA  
6451  C C   . PHE B  297 ? 0.9424 0.7806 0.8708 -0.1742 0.0875  -0.0063 297 PHE B C   
6452  O O   . PHE B  297 ? 0.9170 0.7441 0.8324 -0.1703 0.0878  -0.0051 297 PHE B O   
6453  C CB  . PHE B  297 ? 1.1212 0.9680 1.0534 -0.1893 0.0989  -0.0119 297 PHE B CB  
6454  C CG  . PHE B  297 ? 1.1680 1.0187 1.1009 -0.1938 0.1058  -0.0148 297 PHE B CG  
6455  C CD1 . PHE B  297 ? 1.1889 1.0563 1.1403 -0.1980 0.1082  -0.0179 297 PHE B CD1 
6456  C CD2 . PHE B  297 ? 1.1999 1.0378 1.1151 -0.1943 0.1097  -0.0147 297 PHE B CD2 
6457  C CE1 . PHE B  297 ? 1.2010 1.0728 1.1533 -0.2026 0.1152  -0.0214 297 PHE B CE1 
6458  C CE2 . PHE B  297 ? 1.2156 1.0573 1.1308 -0.1993 0.1165  -0.0177 297 PHE B CE2 
6459  C CZ  . PHE B  297 ? 1.2041 1.0631 1.1379 -0.2035 0.1196  -0.0214 297 PHE B CZ  
6460  N N   . SER B  298 ? 0.5009 0.3412 0.4331 -0.1741 0.0833  -0.0055 298 SER B N   
6461  C CA  . SER B  298 ? 0.4164 0.2478 0.3400 -0.1685 0.0785  -0.0033 298 SER B CA  
6462  C C   . SER B  298 ? 0.6035 0.4168 0.5055 -0.1681 0.0802  -0.0028 298 SER B C   
6463  O O   . SER B  298 ? 0.4284 0.2345 0.3236 -0.1614 0.0774  -0.0010 298 SER B O   
6464  C CB  . SER B  298 ? 0.4142 0.2509 0.3441 -0.1710 0.0753  -0.0035 298 SER B CB  
6465  O OG  . SER B  298 ? 0.3965 0.2474 0.3452 -0.1681 0.0704  -0.0023 298 SER B OG  
6466  N N   . PHE B  299 ? 0.4503 0.2562 0.3422 -0.1754 0.0844  -0.0043 299 PHE B N   
6467  C CA  . PHE B  299 ? 0.4669 0.2553 0.3395 -0.1757 0.0856  -0.0035 299 PHE B CA  
6468  C C   . PHE B  299 ? 0.4963 0.2767 0.3575 -0.1812 0.0916  -0.0041 299 PHE B C   
6469  O O   . PHE B  299 ? 0.4949 0.2792 0.3581 -0.1892 0.0964  -0.0062 299 PHE B O   
6470  C CB  . PHE B  299 ? 0.4758 0.2593 0.3441 -0.1794 0.0847  -0.0042 299 PHE B CB  
6471  C CG  . PHE B  299 ? 0.4610 0.2504 0.3374 -0.1743 0.0789  -0.0036 299 PHE B CG  
6472  C CD1 . PHE B  299 ? 0.4482 0.2529 0.3410 -0.1756 0.0769  -0.0044 299 PHE B CD1 
6473  C CD2 . PHE B  299 ? 0.4728 0.2527 0.3409 -0.1683 0.0754  -0.0021 299 PHE B CD2 
6474  C CE1 . PHE B  299 ? 0.4359 0.2456 0.3352 -0.1714 0.0715  -0.0036 299 PHE B CE1 
6475  C CE2 . PHE B  299 ? 0.4475 0.2330 0.3226 -0.1641 0.0705  -0.0018 299 PHE B CE2 
6476  C CZ  . PHE B  299 ? 0.6517 0.4519 0.5418 -0.1658 0.0686  -0.0025 299 PHE B CZ  
6477  N N   . VAL B  300 ? 0.4891 0.2587 0.3385 -0.1771 0.0914  -0.0023 300 VAL B N   
6478  C CA  . VAL B  300 ? 0.5054 0.2672 0.3432 -0.1819 0.0967  -0.0025 300 VAL B CA  
6479  C C   . VAL B  300 ? 0.5407 0.2839 0.3599 -0.1794 0.0952  0.0002  300 VAL B C   
6480  O O   . VAL B  300 ? 0.5574 0.2956 0.3748 -0.1740 0.0904  0.0016  300 VAL B O   
6481  C CB  . VAL B  300 ? 0.4943 0.2654 0.3400 -0.1795 0.0982  -0.0032 300 VAL B CB  
6482  C CG1 . VAL B  300 ? 0.4841 0.2730 0.3482 -0.1835 0.1007  -0.0060 300 VAL B CG1 
6483  C CG2 . VAL B  300 ? 0.4782 0.2496 0.3268 -0.1694 0.0926  -0.0012 300 VAL B CG2 
6484  N N   . PRO B  301 ? 0.5374 0.2706 0.3430 -0.1837 0.0993  0.0009  301 PRO B N   
6485  C CA  . PRO B  301 ? 0.5959 0.3117 0.3847 -0.1805 0.0969  0.0040  301 PRO B CA  
6486  C C   . PRO B  301 ? 0.5802 0.2975 0.3726 -0.1699 0.0912  0.0055  301 PRO B C   
6487  O O   . PRO B  301 ? 0.5591 0.2890 0.3636 -0.1660 0.0905  0.0044  301 PRO B O   
6488  C CB  . PRO B  301 ? 0.5667 0.2765 0.3443 -0.1862 0.1021  0.0043  301 PRO B CB  
6489  C CG  . PRO B  301 ? 0.5717 0.2903 0.3554 -0.1953 0.1080  0.0014  301 PRO B CG  
6490  C CD  . PRO B  301 ? 0.5495 0.2856 0.3533 -0.1926 0.1062  -0.0010 301 PRO B CD  
6491  N N   . VAL B  302 ? 0.5394 0.2442 0.3225 -0.1654 0.0870  0.0079  302 VAL B N   
6492  C CA  . VAL B  302 ? 0.5244 0.2305 0.3108 -0.1556 0.0816  0.0091  302 VAL B CA  
6493  C C   . VAL B  302 ? 0.5386 0.2297 0.3094 -0.1534 0.0802  0.0119  302 VAL B C   
6494  O O   . VAL B  302 ? 0.5606 0.2372 0.3176 -0.1579 0.0814  0.0136  302 VAL B O   
6495  C CB  . VAL B  302 ? 0.5163 0.2231 0.3080 -0.1513 0.0771  0.0091  302 VAL B CB  
6496  C CG1 . VAL B  302 ? 0.5365 0.2303 0.3179 -0.1564 0.0780  0.0098  302 VAL B CG1 
6497  C CG2 . VAL B  302 ? 0.5058 0.2107 0.2978 -0.1419 0.0716  0.0106  302 VAL B CG2 
6498  N N   . VAL B  303 ? 0.5479 0.2418 0.3207 -0.1466 0.0775  0.0125  303 VAL B N   
6499  C CA  . VAL B  303 ? 0.5845 0.2641 0.3426 -0.1443 0.0755  0.0153  303 VAL B CA  
6500  C C   . VAL B  303 ? 0.6361 0.3093 0.3933 -0.1377 0.0697  0.0168  303 VAL B C   
6501  O O   . VAL B  303 ? 0.5689 0.2499 0.3356 -0.1302 0.0658  0.0163  303 VAL B O   
6502  C CB  . VAL B  303 ? 0.5289 0.2146 0.2902 -0.1397 0.0749  0.0150  303 VAL B CB  
6503  C CG1 . VAL B  303 ? 0.5660 0.2374 0.3124 -0.1368 0.0721  0.0180  303 VAL B CG1 
6504  C CG2 . VAL B  303 ? 0.6632 0.3574 0.4281 -0.1460 0.0810  0.0129  303 VAL B CG2 
6505  N N   . ASP B  304 ? 0.9068 0.5655 0.6528 -0.1411 0.0694  0.0187  304 ASP B N   
6506  C CA  . ASP B  304 ? 1.0079 0.6598 0.7538 -0.1366 0.0648  0.0197  304 ASP B CA  
6507  C C   . ASP B  304 ? 1.0178 0.6556 0.7529 -0.1316 0.0603  0.0229  304 ASP B C   
6508  O O   . ASP B  304 ? 0.9961 0.6303 0.7333 -0.1260 0.0559  0.0234  304 ASP B O   
6509  C CB  . ASP B  304 ? 1.1430 0.7875 0.8850 -0.1434 0.0671  0.0196  304 ASP B CB  
6510  C CG  . ASP B  304 ? 1.1864 0.8211 0.9159 -0.1524 0.0718  0.0210  304 ASP B CG  
6511  O OD1 . ASP B  304 ? 1.1999 0.8362 0.9252 -0.1541 0.0741  0.0214  304 ASP B OD1 
6512  O OD2 . ASP B  304 ? 1.1707 0.7961 0.8946 -0.1583 0.0734  0.0217  304 ASP B OD2 
6513  N N   . GLY B  305 ? 1.0923 0.7230 0.8164 -0.1336 0.0615  0.0248  305 GLY B N   
6514  C CA  . GLY B  305 ? 1.1255 0.7399 0.8366 -0.1310 0.0575  0.0285  305 GLY B CA  
6515  C C   . GLY B  305 ? 1.1469 0.7441 0.8452 -0.1374 0.0584  0.0314  305 GLY B C   
6516  O O   . GLY B  305 ? 1.1953 0.7772 0.8831 -0.1356 0.0545  0.0350  305 GLY B O   
6517  N N   . ASP B  306 ? 0.9115 0.5109 0.6112 -0.1451 0.0632  0.0300  306 ASP B N   
6518  C CA  . ASP B  306 ? 0.9455 0.5286 0.6334 -0.1520 0.0646  0.0327  306 ASP B CA  
6519  C C   . ASP B  306 ? 0.9091 0.4911 0.5890 -0.1622 0.0710  0.0329  306 ASP B C   
6520  O O   . ASP B  306 ? 0.9148 0.4850 0.5806 -0.1656 0.0714  0.0363  306 ASP B O   
6521  C CB  . ASP B  306 ? 1.2429 0.8260 0.9383 -0.1526 0.0641  0.0312  306 ASP B CB  
6522  C CG  . ASP B  306 ? 1.3652 0.9314 1.0496 -0.1602 0.0657  0.0339  306 ASP B CG  
6523  O OD1 . ASP B  306 ? 1.4105 0.9610 1.0808 -0.1622 0.0645  0.0383  306 ASP B OD1 
6524  O OD2 . ASP B  306 ? 1.4033 0.9717 1.0930 -0.1645 0.0681  0.0319  306 ASP B OD2 
6525  N N   . PHE B  307 ? 0.9116 0.5059 0.6005 -0.1674 0.0760  0.0293  307 PHE B N   
6526  C CA  . PHE B  307 ? 0.8637 0.4582 0.5464 -0.1776 0.0825  0.0289  307 PHE B CA  
6527  C C   . PHE B  307 ? 0.8657 0.4657 0.5456 -0.1775 0.0844  0.0286  307 PHE B C   
6528  O O   . PHE B  307 ? 0.8830 0.4754 0.5505 -0.1845 0.0879  0.0305  307 PHE B O   
6529  C CB  . PHE B  307 ? 0.7042 0.3127 0.3994 -0.1825 0.0870  0.0246  307 PHE B CB  
6530  C CG  . PHE B  307 ? 0.7035 0.3115 0.3928 -0.1938 0.0940  0.0240  307 PHE B CG  
6531  C CD1 . PHE B  307 ? 0.7112 0.3288 0.4016 -0.1970 0.0984  0.0222  307 PHE B CD1 
6532  C CD2 . PHE B  307 ? 0.7066 0.3052 0.3903 -0.2014 0.0963  0.0249  307 PHE B CD2 
6533  C CE1 . PHE B  307 ? 0.6975 0.3156 0.3832 -0.2077 0.1052  0.0213  307 PHE B CE1 
6534  C CE2 . PHE B  307 ? 0.7220 0.3208 0.4007 -0.2122 0.1029  0.0242  307 PHE B CE2 
6535  C CZ  . PHE B  307 ? 0.7174 0.3263 0.3971 -0.2153 0.1074  0.0223  307 PHE B CZ  
6536  N N   . LEU B  308 ? 0.9244 0.5379 0.6161 -0.1698 0.0823  0.0262  308 LEU B N   
6537  C CA  . LEU B  308 ? 0.9005 0.5178 0.5898 -0.1677 0.0827  0.0262  308 LEU B CA  
6538  C C   . LEU B  308 ? 0.9124 0.5244 0.6004 -0.1577 0.0756  0.0284  308 LEU B C   
6539  O O   . LEU B  308 ? 0.8646 0.4835 0.5641 -0.1505 0.0718  0.0270  308 LEU B O   
6540  C CB  . LEU B  308 ? 0.6213 0.2593 0.3269 -0.1670 0.0861  0.0217  308 LEU B CB  
6541  C CG  . LEU B  308 ? 0.6228 0.2698 0.3345 -0.1759 0.0927  0.0187  308 LEU B CG  
6542  C CD1 . LEU B  308 ? 0.5959 0.2635 0.3269 -0.1729 0.0941  0.0146  308 LEU B CD1 
6543  C CD2 . LEU B  308 ? 0.6451 0.2857 0.3438 -0.1855 0.0986  0.0194  308 LEU B CD2 
6544  N N   . SER B  309 ? 0.9597 0.5591 0.6332 -0.1576 0.0738  0.0318  309 SER B N   
6545  C CA  . SER B  309 ? 0.9803 0.5732 0.6512 -0.1487 0.0668  0.0342  309 SER B CA  
6546  C C   . SER B  309 ? 0.9588 0.5664 0.6415 -0.1413 0.0653  0.0314  309 SER B C   
6547  O O   . SER B  309 ? 0.9377 0.5465 0.6260 -0.1327 0.0598  0.0316  309 SER B O   
6548  C CB  . SER B  309 ? 0.9471 0.5219 0.5987 -0.1514 0.0651  0.0390  309 SER B CB  
6549  O OG  . SER B  309 ? 0.9338 0.5118 0.5793 -0.1560 0.0692  0.0385  309 SER B OG  
6550  N N   . ASP B  310 ? 0.8777 0.4962 0.5645 -0.1451 0.0706  0.0288  310 ASP B N   
6551  C CA  . ASP B  310 ? 0.8553 0.4892 0.5554 -0.1393 0.0702  0.0258  310 ASP B CA  
6552  C C   . ASP B  310 ? 0.7817 0.4300 0.4924 -0.1451 0.0769  0.0221  310 ASP B C   
6553  O O   . ASP B  310 ? 0.7928 0.4387 0.4994 -0.1534 0.0815  0.0218  310 ASP B O   
6554  C CB  . ASP B  310 ? 1.0414 0.6703 0.7323 -0.1373 0.0688  0.0273  310 ASP B CB  
6555  C CG  . ASP B  310 ? 1.0799 0.7220 0.7843 -0.1292 0.0665  0.0250  310 ASP B CG  
6556  O OD1 . ASP B  310 ? 1.1004 0.7571 0.8216 -0.1268 0.0673  0.0221  310 ASP B OD1 
6557  O OD2 . ASP B  310 ? 1.0772 0.7148 0.7754 -0.1255 0.0636  0.0263  310 ASP B OD2 
6558  N N   . THR B  311 ? 0.7356 0.3988 0.4604 -0.1409 0.0773  0.0193  311 THR B N   
6559  C CA  . THR B  311 ? 0.6935 0.3714 0.4304 -0.1456 0.0831  0.0157  311 THR B CA  
6560  C C   . THR B  311 ? 0.6950 0.3691 0.4211 -0.1547 0.0895  0.0153  311 THR B C   
6561  O O   . THR B  311 ? 0.7195 0.3842 0.4324 -0.1551 0.0891  0.0172  311 THR B O   
6562  C CB  . THR B  311 ? 0.6688 0.3614 0.4218 -0.1390 0.0818  0.0135  311 THR B CB  
6563  O OG1 . THR B  311 ? 0.6138 0.3032 0.3595 -0.1385 0.0825  0.0138  311 THR B OG1 
6564  C CG2 . THR B  311 ? 0.6999 0.3946 0.4608 -0.1297 0.0749  0.0145  311 THR B CG2 
6565  N N   . PRO B  312 ? 0.6761 0.3581 0.4080 -0.1622 0.0954  0.0127  312 PRO B N   
6566  C CA  . PRO B  312 ? 0.7234 0.4040 0.4465 -0.1720 0.1025  0.0116  312 PRO B CA  
6567  C C   . PRO B  312 ? 0.7802 0.4637 0.5013 -0.1711 0.1043  0.0106  312 PRO B C   
6568  O O   . PRO B  312 ? 0.8422 0.5157 0.5457 -0.1785 0.1085  0.0110  312 PRO B O   
6569  C CB  . PRO B  312 ? 0.6153 0.3111 0.3540 -0.1769 0.1076  0.0076  312 PRO B CB  
6570  C CG  . PRO B  312 ? 0.5774 0.2741 0.3237 -0.1729 0.1032  0.0084  312 PRO B CG  
6571  C CD  . PRO B  312 ? 0.5619 0.2555 0.3096 -0.1622 0.0958  0.0105  312 PRO B CD  
6572  N N   . GLU B  313 ? 0.7147 0.4096 0.4506 -0.1635 0.1019  0.0088  313 GLU B N   
6573  C CA  . GLU B  313 ? 0.8235 0.5165 0.5522 -0.1637 0.1044  0.0066  313 GLU B CA  
6574  C C   . GLU B  313 ? 0.8127 0.4877 0.5200 -0.1629 0.1009  0.0107  313 GLU B C   
6575  O O   . GLU B  313 ? 0.8405 0.5062 0.5298 -0.1705 0.1058  0.0098  313 GLU B O   
6576  C CB  . GLU B  313 ? 1.3868 1.0921 1.1339 -0.1543 0.1006  0.0050  313 GLU B CB  
6577  C CG  . GLU B  313 ? 1.5461 1.2692 1.3146 -0.1554 0.1041  0.0010  313 GLU B CG  
6578  C CD  . GLU B  313 ? 1.6925 1.4196 1.4578 -0.1657 0.1144  -0.0047 313 GLU B CD  
6579  O OE1 . GLU B  313 ? 1.7520 1.4725 1.5044 -0.1688 0.1183  -0.0067 313 GLU B OE1 
6580  O OE2 . GLU B  313 ? 1.7239 1.4614 1.5000 -0.1710 0.1188  -0.0076 313 GLU B OE2 
6581  N N   . ALA B  314 ? 0.9093 0.5796 0.6188 -0.1541 0.0924  0.0150  314 ALA B N   
6582  C CA  . ALA B  314 ? 0.9414 0.5955 0.6332 -0.1517 0.0877  0.0191  314 ALA B CA  
6583  C C   . ALA B  314 ? 1.0210 0.6600 0.6926 -0.1610 0.0904  0.0219  314 ALA B C   
6584  O O   . ALA B  314 ? 1.0996 0.7246 0.7519 -0.1637 0.0898  0.0243  314 ALA B O   
6585  C CB  . ALA B  314 ? 0.8628 0.5129 0.5584 -0.1423 0.0795  0.0215  314 ALA B CB  
6586  N N   . LEU B  315 ? 1.1586 0.7994 0.8332 -0.1666 0.0936  0.0216  315 LEU B N   
6587  C CA  . LEU B  315 ? 1.1309 0.7569 0.7873 -0.1753 0.0957  0.0249  315 LEU B CA  
6588  C C   . LEU B  315 ? 1.1667 0.7913 0.8104 -0.1868 0.1042  0.0227  315 LEU B C   
6589  O O   . LEU B  315 ? 1.2455 0.8550 0.8687 -0.1933 0.1050  0.0262  315 LEU B O   
6590  C CB  . LEU B  315 ? 0.7555 0.3804 0.4158 -0.1783 0.0964  0.0250  315 LEU B CB  
6591  C CG  . LEU B  315 ? 0.6684 0.2910 0.3359 -0.1693 0.0892  0.0262  315 LEU B CG  
6592  C CD1 . LEU B  315 ? 0.6707 0.2864 0.3356 -0.1739 0.0898  0.0275  315 LEU B CD1 
6593  C CD2 . LEU B  315 ? 0.6555 0.2656 0.3130 -0.1622 0.0820  0.0302  315 LEU B CD2 
6594  N N   . ILE B  316 ? 0.7782 0.4177 0.4331 -0.1903 0.1109  0.0166  316 ILE B N   
6595  C CA  . ILE B  316 ? 0.7818 0.4210 0.4247 -0.2019 0.1200  0.0130  316 ILE B CA  
6596  C C   . ILE B  316 ? 0.8403 0.4755 0.4730 -0.2009 0.1203  0.0117  316 ILE B C   
6597  O O   . ILE B  316 ? 0.8036 0.4358 0.4224 -0.2106 0.1272  0.0092  316 ILE B O   
6598  C CB  . ILE B  316 ? 0.7829 0.4400 0.4420 -0.2075 0.1281  0.0063  316 ILE B CB  
6599  C CG1 . ILE B  316 ? 0.7782 0.4505 0.4565 -0.2001 0.1277  0.0017  316 ILE B CG1 
6600  C CG2 . ILE B  316 ? 0.7567 0.4179 0.4262 -0.2082 0.1272  0.0076  316 ILE B CG2 
6601  C CD1 . ILE B  316 ? 0.7796 0.4695 0.4733 -0.2062 0.1361  -0.0053 316 ILE B CD1 
6602  N N   . ASN B  317 ? 1.1833 0.8189 0.8231 -0.1894 0.1131  0.0130  317 ASN B N   
6603  C CA  . ASN B  317 ? 1.2638 0.8926 0.8917 -0.1877 0.1119  0.0128  317 ASN B CA  
6604  C C   . ASN B  317 ? 1.3241 0.9329 0.9294 -0.1877 0.1062  0.0193  317 ASN B C   
6605  O O   . ASN B  317 ? 1.3639 0.9643 0.9512 -0.1935 0.1088  0.0192  317 ASN B O   
6606  C CB  . ASN B  317 ? 1.1559 0.7949 0.8011 -0.1766 0.1078  0.0106  317 ASN B CB  
6607  C CG  . ASN B  317 ? 1.1812 0.8310 0.8321 -0.1804 0.1156  0.0036  317 ASN B CG  
6608  O OD1 . ASN B  317 ? 1.1965 0.8393 0.8325 -0.1842 0.1183  0.0021  317 ASN B OD1 
6609  N ND2 . ASN B  317 ? 1.1659 0.8328 0.8384 -0.1800 0.1195  -0.0009 317 ASN B ND2 
6610  N N   . THR B  318 ? 1.1530 0.7547 0.7598 -0.1813 0.0984  0.0248  318 THR B N   
6611  C CA  . THR B  318 ? 1.1618 0.7445 0.7486 -0.1810 0.0925  0.0313  318 THR B CA  
6612  C C   . THR B  318 ? 1.1909 0.7621 0.7634 -0.1904 0.0947  0.0355  318 THR B C   
6613  O O   . THR B  318 ? 1.2312 0.7858 0.7855 -0.1918 0.0905  0.0413  318 THR B O   
6614  C CB  . THR B  318 ? 1.2469 0.8263 0.8419 -0.1682 0.0820  0.0353  318 THR B CB  
6615  O OG1 . THR B  318 ? 1.2623 0.8437 0.8679 -0.1667 0.0801  0.0373  318 THR B OG1 
6616  C CG2 . THR B  318 ? 1.2061 0.7987 0.8188 -0.1582 0.0793  0.0315  318 THR B CG2 
6617  N N   . GLY B  319 ? 1.2209 0.8005 0.8013 -0.1969 0.1010  0.0329  319 GLY B N   
6618  C CA  . GLY B  319 ? 1.2884 0.8577 0.8586 -0.2045 0.1022  0.0372  319 GLY B CA  
6619  C C   . GLY B  319 ? 1.3512 0.9074 0.8962 -0.2162 0.1065  0.0398  319 GLY B C   
6620  O O   . GLY B  319 ? 1.3547 0.9162 0.8941 -0.2224 0.1128  0.0355  319 GLY B O   
6621  N N   . ASP B  320 ? 1.4935 1.0330 1.0234 -0.2196 0.1032  0.0468  320 ASP B N   
6622  C CA  . ASP B  320 ? 1.5540 1.0815 1.0595 -0.2318 0.1074  0.0499  320 ASP B CA  
6623  C C   . ASP B  320 ? 1.5430 1.0736 1.0469 -0.2440 0.1160  0.0484  320 ASP B C   
6624  O O   . ASP B  320 ? 1.5761 1.1005 1.0813 -0.2452 0.1143  0.0522  320 ASP B O   
6625  C CB  . ASP B  320 ? 1.6704 1.1766 1.1575 -0.2300 0.0993  0.0590  320 ASP B CB  
6626  C CG  . ASP B  320 ? 1.7602 1.2540 1.2213 -0.2431 0.1034  0.0629  320 ASP B CG  
6627  O OD1 . ASP B  320 ? 1.7824 1.2819 1.2358 -0.2492 0.1092  0.0589  320 ASP B OD1 
6628  O OD2 . ASP B  320 ? 1.7983 1.2772 1.2469 -0.2476 0.1012  0.0699  320 ASP B OD2 
6629  N N   . PHE B  321 ? 1.3475 0.8882 0.8488 -0.2534 0.1253  0.0426  321 PHE B N   
6630  C CA  . PHE B  321 ? 1.3223 0.8708 0.8261 -0.2649 0.1346  0.0390  321 PHE B CA  
6631  C C   . PHE B  321 ? 1.3544 0.8921 0.8349 -0.2795 0.1402  0.0424  321 PHE B C   
6632  O O   . PHE B  321 ? 1.3550 0.9017 0.8366 -0.2904 0.1496  0.0378  321 PHE B O   
6633  C CB  . PHE B  321 ? 1.3209 0.8919 0.8453 -0.2648 0.1416  0.0293  321 PHE B CB  
6634  C CG  . PHE B  321 ? 1.2568 0.8376 0.8052 -0.2519 0.1361  0.0275  321 PHE B CG  
6635  C CD1 . PHE B  321 ? 1.2383 0.8199 0.7975 -0.2499 0.1339  0.0293  321 PHE B CD1 
6636  C CD2 . PHE B  321 ? 1.2262 0.8147 0.7854 -0.2419 0.1326  0.0245  321 PHE B CD2 
6637  C CE1 . PHE B  321 ? 1.2113 0.8023 0.7918 -0.2385 0.1287  0.0279  321 PHE B CE1 
6638  C CE2 . PHE B  321 ? 1.1918 0.7895 0.7725 -0.2303 0.1273  0.0234  321 PHE B CE2 
6639  C CZ  . PHE B  321 ? 1.1830 0.7823 0.7742 -0.2287 0.1254  0.0251  321 PHE B CZ  
6640  N N   . GLN B  322 ? 1.4298 0.9487 0.8894 -0.2796 0.1343  0.0504  322 GLN B N   
6641  C CA  . GLN B  322 ? 1.4717 0.9793 0.9060 -0.2929 0.1385  0.0545  322 GLN B CA  
6642  C C   . GLN B  322 ? 1.4754 0.9861 0.9075 -0.3060 0.1473  0.0531  322 GLN B C   
6643  O O   . GLN B  322 ? 1.4614 0.9828 0.8904 -0.3168 0.1571  0.0472  322 GLN B O   
6644  C CB  . GLN B  322 ? 1.5588 1.0435 0.9750 -0.2897 0.1288  0.0654  322 GLN B CB  
6645  C CG  . GLN B  322 ? 1.5704 1.0490 0.9776 -0.2826 0.1222  0.0676  322 GLN B CG  
6646  C CD  . GLN B  322 ? 1.6157 1.0981 1.0071 -0.2928 0.1292  0.0646  322 GLN B CD  
6647  O OE1 . GLN B  322 ? 1.5959 1.0945 0.9979 -0.2921 0.1345  0.0562  322 GLN B OE1 
6648  N NE2 . GLN B  322 ? 1.6706 1.1385 1.0369 -0.3027 0.1295  0.0715  322 GLN B NE2 
6649  N N   . ASP B  323 ? 1.4946 0.9969 0.9293 -0.3057 0.1444  0.0579  323 ASP B N   
6650  C CA  . ASP B  323 ? 1.5138 1.0204 0.9479 -0.3183 0.1532  0.0558  323 ASP B CA  
6651  C C   . ASP B  323 ? 1.4167 0.9406 0.8776 -0.3134 0.1555  0.0488  323 ASP B C   
6652  O O   . ASP B  323 ? 1.3790 0.8990 0.8503 -0.3069 0.1503  0.0517  323 ASP B O   
6653  C CB  . ASP B  323 ? 1.7519 1.2379 1.1700 -0.3235 0.1498  0.0655  323 ASP B CB  
6654  C CG  . ASP B  323 ? 1.8345 1.3025 1.2251 -0.3286 0.1468  0.0735  323 ASP B CG  
6655  O OD1 . ASP B  323 ? 1.8366 1.3045 1.2223 -0.3229 0.1432  0.0733  323 ASP B OD1 
6656  O OD2 . ASP B  323 ? 1.8885 1.3423 1.2621 -0.3384 0.1481  0.0802  323 ASP B OD2 
6657  N N   . LEU B  324 ? 1.3791 0.9225 0.8511 -0.3171 0.1638  0.0394  324 LEU B N   
6658  C CA  . LEU B  324 ? 1.3170 0.8787 0.8139 -0.3145 0.1673  0.0322  324 LEU B CA  
6659  C C   . LEU B  324 ? 1.2697 0.8481 0.7696 -0.3262 0.1793  0.0236  324 LEU B C   
6660  O O   . LEU B  324 ? 1.2774 0.8611 0.7713 -0.3293 0.1833  0.0197  324 LEU B O   
6661  C CB  . LEU B  324 ? 1.2720 0.8437 0.7883 -0.2996 0.1613  0.0290  324 LEU B CB  
6662  C CG  . LEU B  324 ? 1.2442 0.8307 0.7861 -0.2938 0.1613  0.0244  324 LEU B CG  
6663  C CD1 . LEU B  324 ? 1.2641 0.8386 0.8061 -0.2913 0.1555  0.0310  324 LEU B CD1 
6664  C CD2 . LEU B  324 ? 1.1867 0.7845 0.7467 -0.2805 0.1565  0.0208  324 LEU B CD2 
6665  N N   . GLN B  325 ? 1.2490 0.8364 0.7593 -0.3327 0.1851  0.0199  325 GLN B N   
6666  C CA  . GLN B  325 ? 1.2439 0.8506 0.7624 -0.3423 0.1964  0.0103  325 GLN B CA  
6667  C C   . GLN B  325 ? 1.1693 0.7949 0.7165 -0.3358 0.1970  0.0035  325 GLN B C   
6668  O O   . GLN B  325 ? 1.1971 0.8207 0.7534 -0.3325 0.1934  0.0061  325 GLN B O   
6669  C CB  . GLN B  325 ? 1.4233 1.0260 0.9270 -0.3587 0.2046  0.0109  325 GLN B CB  
6670  C CG  . GLN B  325 ? 1.4894 1.0777 0.9649 -0.3676 0.2062  0.0159  325 GLN B CG  
6671  C CD  . GLN B  325 ? 1.5313 1.0944 0.9876 -0.3672 0.1984  0.0280  325 GLN B CD  
6672  O OE1 . GLN B  325 ? 1.5568 1.1126 1.0075 -0.3752 0.2007  0.0315  325 GLN B OE1 
6673  N NE2 . GLN B  325 ? 1.5278 1.0774 0.9746 -0.3580 0.1893  0.0344  325 GLN B NE2 
6674  N N   . VAL B  326 ? 0.9802 0.6241 0.5416 -0.3339 0.2014  -0.0050 326 VAL B N   
6675  C CA  . VAL B  326 ? 0.8826 0.5449 0.4717 -0.3266 0.2012  -0.0111 326 VAL B CA  
6676  C C   . VAL B  326 ? 0.8761 0.5602 0.4782 -0.3350 0.2122  -0.0219 326 VAL B C   
6677  O O   . VAL B  326 ? 0.8837 0.5731 0.4798 -0.3400 0.2181  -0.0267 326 VAL B O   
6678  C CB  . VAL B  326 ? 0.8880 0.5525 0.4879 -0.3118 0.1935  -0.0107 326 VAL B CB  
6679  C CG1 . VAL B  326 ? 0.8497 0.5325 0.4776 -0.3047 0.1927  -0.0159 326 VAL B CG1 
6680  C CG2 . VAL B  326 ? 0.9024 0.5466 0.4907 -0.3028 0.1824  -0.0007 326 VAL B CG2 
6681  N N   . LEU B  327 ? 1.0467 0.7441 0.6671 -0.3367 0.2152  -0.0261 327 LEU B N   
6682  C CA  . LEU B  327 ? 1.0737 0.7942 0.7110 -0.3426 0.2248  -0.0371 327 LEU B CA  
6683  C C   . LEU B  327 ? 1.0612 0.7973 0.7264 -0.3310 0.2206  -0.0408 327 LEU B C   
6684  O O   . LEU B  327 ? 1.1028 0.8415 0.7801 -0.3276 0.2170  -0.0390 327 LEU B O   
6685  C CB  . LEU B  327 ? 0.9036 0.6288 0.5397 -0.3560 0.2327  -0.0399 327 LEU B CB  
6686  C CG  . LEU B  327 ? 0.8667 0.6173 0.5257 -0.3612 0.2415  -0.0511 327 LEU B CG  
6687  C CD1 . LEU B  327 ? 0.8679 0.6318 0.5290 -0.3655 0.2494  -0.0599 327 LEU B CD1 
6688  C CD2 . LEU B  327 ? 0.8893 0.6407 0.5444 -0.3739 0.2479  -0.0520 327 LEU B CD2 
6689  N N   . VAL B  328 ? 0.8824 0.6288 0.5575 -0.3252 0.2212  -0.0458 328 VAL B N   
6690  C CA  . VAL B  328 ? 0.8177 0.5782 0.5187 -0.3136 0.2167  -0.0486 328 VAL B CA  
6691  C C   . VAL B  328 ? 0.7971 0.5819 0.5195 -0.3171 0.2253  -0.0601 328 VAL B C   
6692  O O   . VAL B  328 ? 0.7709 0.5620 0.4876 -0.3263 0.2343  -0.0667 328 VAL B O   
6693  C CB  . VAL B  328 ? 0.7510 0.5033 0.4495 -0.3014 0.2087  -0.0444 328 VAL B CB  
6694  C CG1 . VAL B  328 ? 0.7507 0.4844 0.4391 -0.2937 0.1982  -0.0340 328 VAL B CG1 
6695  C CG2 . VAL B  328 ? 0.7679 0.5143 0.4488 -0.3062 0.2130  -0.0463 328 VAL B CG2 
6696  N N   . GLY B  329 ? 0.7286 0.5283 0.4766 -0.3098 0.2224  -0.0627 329 GLY B N   
6697  C CA  . GLY B  329 ? 0.7165 0.5397 0.4869 -0.3118 0.2298  -0.0736 329 GLY B CA  
6698  C C   . GLY B  329 ? 0.6870 0.5265 0.4867 -0.3034 0.2256  -0.0757 329 GLY B C   
6699  O O   . GLY B  329 ? 0.6752 0.5083 0.4781 -0.2962 0.2169  -0.0685 329 GLY B O   
6700  N N   . VAL B  330 ? 0.6755 0.5366 0.4973 -0.3043 0.2316  -0.0857 330 VAL B N   
6701  C CA  . VAL B  330 ? 0.6913 0.5692 0.5428 -0.2965 0.2275  -0.0879 330 VAL B CA  
6702  C C   . VAL B  330 ? 0.6495 0.5502 0.5220 -0.3042 0.2357  -0.0980 330 VAL B C   
6703  O O   . VAL B  330 ? 0.7217 0.6270 0.5872 -0.3152 0.2456  -0.1049 330 VAL B O   
6704  C CB  . VAL B  330 ? 0.6300 0.5134 0.4951 -0.2856 0.2235  -0.0892 330 VAL B CB  
6705  C CG1 . VAL B  330 ? 0.6276 0.4894 0.4699 -0.2800 0.2176  -0.0811 330 VAL B CG1 
6706  C CG2 . VAL B  330 ? 0.6247 0.5261 0.5035 -0.2899 0.2331  -0.1015 330 VAL B CG2 
6707  N N   . VAL B  331 ? 0.6290 0.5440 0.5269 -0.2989 0.2315  -0.0989 331 VAL B N   
6708  C CA  . VAL B  331 ? 0.6625 0.6017 0.5847 -0.3044 0.2386  -0.1096 331 VAL B CA  
6709  C C   . VAL B  331 ? 0.6937 0.6504 0.6400 -0.2981 0.2400  -0.1176 331 VAL B C   
6710  O O   . VAL B  331 ? 0.6995 0.6489 0.6435 -0.2894 0.2350  -0.1141 331 VAL B O   
6711  C CB  . VAL B  331 ? 0.7774 0.7249 0.7159 -0.3037 0.2340  -0.1073 331 VAL B CB  
6712  C CG1 . VAL B  331 ? 0.8235 0.7548 0.7396 -0.3109 0.2339  -0.1008 331 VAL B CG1 
6713  C CG2 . VAL B  331 ? 0.7622 0.7098 0.7152 -0.2907 0.2223  -0.1006 331 VAL B CG2 
6714  N N   . LYS B  332 ? 0.7139 0.6938 0.6844 -0.3021 0.2465  -0.1286 332 LYS B N   
6715  C CA  . LYS B  332 ? 0.7119 0.7088 0.7039 -0.2982 0.2503  -0.1387 332 LYS B CA  
6716  C C   . LYS B  332 ? 0.6662 0.6684 0.6803 -0.2846 0.2404  -0.1352 332 LYS B C   
6717  O O   . LYS B  332 ? 0.6128 0.6106 0.6260 -0.2781 0.2385  -0.1351 332 LYS B O   
6718  C CB  . LYS B  332 ? 0.8142 0.8355 0.8276 -0.3057 0.2599  -0.1524 332 LYS B CB  
6719  C CG  . LYS B  332 ? 0.8302 0.8678 0.8620 -0.3035 0.2658  -0.1647 332 LYS B CG  
6720  C CD  . LYS B  332 ? 0.8407 0.9034 0.8954 -0.3103 0.2749  -0.1789 332 LYS B CD  
6721  C CE  . LYS B  332 ? 0.8224 0.9066 0.9128 -0.3014 0.2741  -0.1889 332 LYS B CE  
6722  N NZ  . LYS B  332 ? 0.8035 0.8930 0.9172 -0.2905 0.2624  -0.1823 332 LYS B NZ  
6723  N N   . ASP B  333 ? 0.6884 0.6995 0.7217 -0.2807 0.2336  -0.1321 333 ASP B N   
6724  C CA  . ASP B  333 ? 0.7448 0.7586 0.7963 -0.2684 0.2229  -0.1269 333 ASP B CA  
6725  C C   . ASP B  333 ? 0.7487 0.7456 0.7856 -0.2650 0.2130  -0.1136 333 ASP B C   
6726  O O   . ASP B  333 ? 0.7836 0.7854 0.8270 -0.2676 0.2103  -0.1114 333 ASP B O   
6727  C CB  . ASP B  333 ? 0.9659 1.0052 1.0546 -0.2655 0.2216  -0.1342 333 ASP B CB  
6728  C CG  . ASP B  333 ? 1.0565 1.1147 1.1581 -0.2738 0.2335  -0.1487 333 ASP B CG  
6729  O OD1 . ASP B  333 ? 1.1100 1.1636 1.1930 -0.2846 0.2416  -0.1511 333 ASP B OD1 
6730  O OD2 . ASP B  333 ? 1.0585 1.1364 1.1896 -0.2693 0.2344  -0.1578 333 ASP B OD2 
6731  N N   . GLU B  334 ? 0.6816 0.6596 0.7000 -0.2588 0.2073  -0.1052 334 GLU B N   
6732  C CA  . GLU B  334 ? 0.6403 0.6015 0.6439 -0.2548 0.1978  -0.0931 334 GLU B CA  
6733  C C   . GLU B  334 ? 0.6090 0.5781 0.6346 -0.2457 0.1868  -0.0882 334 GLU B C   
6734  O O   . GLU B  334 ? 0.4881 0.4573 0.5160 -0.2464 0.1818  -0.0835 334 GLU B O   
6735  C CB  . GLU B  334 ? 0.7224 0.6617 0.7002 -0.2508 0.1952  -0.0865 334 GLU B CB  
6736  C CG  . GLU B  334 ? 0.7907 0.7168 0.7408 -0.2602 0.2032  -0.0877 334 GLU B CG  
6737  C CD  . GLU B  334 ? 0.8632 0.7749 0.7947 -0.2640 0.2002  -0.0802 334 GLU B CD  
6738  O OE1 . GLU B  334 ? 0.8703 0.7793 0.8075 -0.2576 0.1910  -0.0733 334 GLU B OE1 
6739  O OE2 . GLU B  334 ? 0.9079 0.8110 0.8196 -0.2735 0.2069  -0.0814 334 GLU B OE2 
6740  N N   . GLY B  335 ? 0.6501 0.6264 0.6923 -0.2376 0.1834  -0.0897 335 GLY B N   
6741  C CA  . GLY B  335 ? 0.6429 0.6221 0.7009 -0.2280 0.1716  -0.0830 335 GLY B CA  
6742  C C   . GLY B  335 ? 0.6655 0.6626 0.7490 -0.2286 0.1677  -0.0845 335 GLY B C   
6743  O O   . GLY B  335 ? 0.6911 0.6869 0.7803 -0.2233 0.1573  -0.0768 335 GLY B O   
6744  N N   . SER B  336 ? 0.6579 0.6720 0.7562 -0.2354 0.1760  -0.0945 336 SER B N   
6745  C CA  . SER B  336 ? 0.5849 0.6196 0.7117 -0.2360 0.1732  -0.0982 336 SER B CA  
6746  C C   . SER B  336 ? 0.5855 0.6168 0.7103 -0.2364 0.1648  -0.0897 336 SER B C   
6747  O O   . SER B  336 ? 0.5758 0.6148 0.7187 -0.2306 0.1550  -0.0855 336 SER B O   
6748  C CB  . SER B  336 ? 0.5633 0.6115 0.6961 -0.2457 0.1850  -0.1095 336 SER B CB  
6749  O OG  . SER B  336 ? 0.5741 0.6074 0.6781 -0.2540 0.1913  -0.1077 336 SER B OG  
6750  N N   . TYR B  337 ? 0.6674 0.6865 0.7696 -0.2433 0.1686  -0.0872 337 TYR B N   
6751  C CA  . TYR B  337 ? 0.7026 0.7173 0.8005 -0.2450 0.1623  -0.0805 337 TYR B CA  
6752  C C   . TYR B  337 ? 0.6944 0.7025 0.7945 -0.2354 0.1494  -0.0707 337 TYR B C   
6753  O O   . TYR B  337 ? 0.7002 0.7152 0.8126 -0.2346 0.1420  -0.0673 337 TYR B O   
6754  C CB  . TYR B  337 ? 0.7978 0.7942 0.8659 -0.2517 0.1674  -0.0778 337 TYR B CB  
6755  C CG  . TYR B  337 ? 0.8516 0.8424 0.9142 -0.2538 0.1620  -0.0719 337 TYR B CG  
6756  C CD1 . TYR B  337 ? 0.8511 0.8275 0.9028 -0.2470 0.1525  -0.0626 337 TYR B CD1 
6757  C CD2 . TYR B  337 ? 0.9093 0.9097 0.9780 -0.2629 0.1666  -0.0764 337 TYR B CD2 
6758  C CE1 . TYR B  337 ? 0.8890 0.8608 0.9364 -0.2491 0.1481  -0.0582 337 TYR B CE1 
6759  C CE2 . TYR B  337 ? 0.9387 0.9342 1.0028 -0.2652 0.1620  -0.0717 337 TYR B CE2 
6760  C CZ  . TYR B  337 ? 0.9424 0.9235 0.9959 -0.2583 0.1528  -0.0627 337 TYR B CZ  
6761  O OH  . TYR B  337 ? 0.9653 0.9418 1.0146 -0.2607 0.1486  -0.0590 337 TYR B OH  
6762  N N   . PHE B  338 ? 0.6627 0.6578 0.7509 -0.2286 0.1468  -0.0666 338 PHE B N   
6763  C CA  . PHE B  338 ? 0.5990 0.5848 0.6842 -0.2199 0.1353  -0.0571 338 PHE B CA  
6764  C C   . PHE B  338 ? 0.5726 0.5726 0.6839 -0.2135 0.1273  -0.0563 338 PHE B C   
6765  O O   . PHE B  338 ? 0.5954 0.5932 0.7098 -0.2088 0.1171  -0.0490 338 PHE B O   
6766  C CB  . PHE B  338 ? 0.5812 0.5480 0.6440 -0.2150 0.1354  -0.0532 338 PHE B CB  
6767  C CG  . PHE B  338 ? 0.6440 0.5944 0.6798 -0.2203 0.1405  -0.0517 338 PHE B CG  
6768  C CD1 . PHE B  338 ? 0.6888 0.6278 0.7123 -0.2193 0.1347  -0.0449 338 PHE B CD1 
6769  C CD2 . PHE B  338 ? 0.6787 0.6256 0.7021 -0.2268 0.1511  -0.0575 338 PHE B CD2 
6770  C CE1 . PHE B  338 ? 0.7370 0.6607 0.7368 -0.2241 0.1390  -0.0437 338 PHE B CE1 
6771  C CE2 . PHE B  338 ? 0.7253 0.6567 0.7238 -0.2322 0.1551  -0.0557 338 PHE B CE2 
6772  C CZ  . PHE B  338 ? 0.7516 0.6712 0.7387 -0.2307 0.1489  -0.0486 338 PHE B CZ  
6773  N N   . LEU B  339 ? 0.4780 0.4928 0.6084 -0.2136 0.1317  -0.0641 339 LEU B N   
6774  C CA  . LEU B  339 ? 0.4626 0.4895 0.6175 -0.2067 0.1237  -0.0634 339 LEU B CA  
6775  C C   . LEU B  339 ? 0.4931 0.5318 0.6655 -0.2071 0.1147  -0.0597 339 LEU B C   
6776  O O   . LEU B  339 ? 0.4598 0.5011 0.6434 -0.2010 0.1044  -0.0542 339 LEU B O   
6777  C CB  . LEU B  339 ? 0.4254 0.4676 0.6000 -0.2068 0.1309  -0.0741 339 LEU B CB  
6778  C CG  . LEU B  339 ? 0.4300 0.4622 0.5895 -0.2064 0.1395  -0.0784 339 LEU B CG  
6779  C CD1 . LEU B  339 ? 0.4529 0.5014 0.6282 -0.2109 0.1502  -0.0915 339 LEU B CD1 
6780  C CD2 . LEU B  339 ? 0.3669 0.3924 0.5283 -0.1969 0.1326  -0.0740 339 LEU B CD2 
6781  N N   . VAL B  340 ? 0.6836 0.7290 0.8576 -0.2148 0.1185  -0.0626 340 VAL B N   
6782  C CA  . VAL B  340 ? 0.7214 0.7792 0.9125 -0.2162 0.1106  -0.0601 340 VAL B CA  
6783  C C   . VAL B  340 ? 0.7763 0.8209 0.9536 -0.2139 0.1012  -0.0496 340 VAL B C   
6784  O O   . VAL B  340 ? 0.8211 0.8736 1.0106 -0.2140 0.0926  -0.0457 340 VAL B O   
6785  C CB  . VAL B  340 ? 0.6444 0.7134 0.8413 -0.2254 0.1178  -0.0669 340 VAL B CB  
6786  C CG1 . VAL B  340 ? 0.6403 0.7265 0.8567 -0.2271 0.1259  -0.0781 340 VAL B CG1 
6787  C CG2 . VAL B  340 ? 0.6487 0.7010 0.8174 -0.2313 0.1253  -0.0662 340 VAL B CG2 
6788  N N   . TYR B  341 ? 0.6850 0.7097 0.8373 -0.2114 0.1026  -0.0454 341 TYR B N   
6789  C CA  . TYR B  341 ? 0.6476 0.6585 0.7853 -0.2083 0.0950  -0.0367 341 TYR B CA  
6790  C C   . TYR B  341 ? 0.6664 0.6746 0.8091 -0.1994 0.0846  -0.0300 341 TYR B C   
6791  O O   . TYR B  341 ? 0.7083 0.7024 0.8359 -0.1949 0.0798  -0.0237 341 TYR B O   
6792  C CB  . TYR B  341 ? 0.5802 0.5719 0.6897 -0.2100 0.1009  -0.0357 341 TYR B CB  
6793  C CG  . TYR B  341 ? 0.5892 0.5813 0.6925 -0.2189 0.1064  -0.0387 341 TYR B CG  
6794  C CD1 . TYR B  341 ? 0.5652 0.5530 0.6640 -0.2200 0.1010  -0.0344 341 TYR B CD1 
6795  C CD2 . TYR B  341 ? 0.6116 0.6087 0.7137 -0.2265 0.1172  -0.0463 341 TYR B CD2 
6796  C CE1 . TYR B  341 ? 0.5549 0.5428 0.6482 -0.2283 0.1060  -0.0373 341 TYR B CE1 
6797  C CE2 . TYR B  341 ? 0.6129 0.6101 0.7092 -0.2350 0.1221  -0.0489 341 TYR B CE2 
6798  C CZ  . TYR B  341 ? 0.5866 0.5791 0.6787 -0.2358 0.1163  -0.0443 341 TYR B CZ  
6799  O OH  . TYR B  341 ? 0.6101 0.6024 0.6967 -0.2445 0.1212  -0.0471 341 TYR B OH  
6800  N N   . GLY B  342 ? 0.6782 0.7004 0.8424 -0.1970 0.0816  -0.0321 342 GLY B N   
6801  C CA  . GLY B  342 ? 0.6604 0.6818 0.8312 -0.1897 0.0713  -0.0258 342 GLY B CA  
6802  C C   . GLY B  342 ? 0.6575 0.6792 0.8339 -0.1837 0.0714  -0.0276 342 GLY B C   
6803  O O   . GLY B  342 ? 0.6731 0.6923 0.8520 -0.1780 0.0625  -0.0217 342 GLY B O   
6804  N N   . VAL B  343 ? 0.6527 0.6776 0.8316 -0.1851 0.0815  -0.0360 343 VAL B N   
6805  C CA  . VAL B  343 ? 0.6224 0.6557 0.8185 -0.1802 0.0813  -0.0403 343 VAL B CA  
6806  C C   . VAL B  343 ? 0.6263 0.6805 0.8508 -0.1816 0.0767  -0.0431 343 VAL B C   
6807  O O   . VAL B  343 ? 0.6825 0.7484 0.9164 -0.1876 0.0817  -0.0488 343 VAL B O   
6808  C CB  . VAL B  343 ? 0.5220 0.5569 0.7178 -0.1819 0.0940  -0.0503 343 VAL B CB  
6809  C CG1 . VAL B  343 ? 0.4935 0.5349 0.7069 -0.1753 0.0933  -0.0548 343 VAL B CG1 
6810  C CG2 . VAL B  343 ? 0.5343 0.5500 0.7004 -0.1832 0.1002  -0.0486 343 VAL B CG2 
6811  N N   . PRO B  344 ? 0.6114 0.6707 0.8495 -0.1761 0.0669  -0.0392 344 PRO B N   
6812  C CA  . PRO B  344 ? 0.5984 0.6780 0.8644 -0.1766 0.0618  -0.0422 344 PRO B CA  
6813  C C   . PRO B  344 ? 0.6423 0.7376 0.9307 -0.1767 0.0706  -0.0546 344 PRO B C   
6814  O O   . PRO B  344 ? 0.6764 0.7685 0.9661 -0.1727 0.0769  -0.0603 344 PRO B O   
6815  C CB  . PRO B  344 ? 0.3264 0.4049 0.5993 -0.1694 0.0517  -0.0370 344 PRO B CB  
6816  C CG  . PRO B  344 ? 0.3485 0.4072 0.5936 -0.1685 0.0480  -0.0277 344 PRO B CG  
6817  C CD  . PRO B  344 ? 0.3841 0.4303 0.6105 -0.1700 0.0587  -0.0309 344 PRO B CD  
6818  N N   . GLY B  345 ? 0.5066 0.6189 0.8125 -0.1813 0.0709  -0.0589 345 GLY B N   
6819  C CA  . GLY B  345 ? 0.4564 0.5869 0.7886 -0.1806 0.0772  -0.0709 345 GLY B CA  
6820  C C   . GLY B  345 ? 0.4577 0.5901 0.7823 -0.1884 0.0899  -0.0786 345 GLY B C   
6821  O O   . GLY B  345 ? 0.4909 0.6384 0.8348 -0.1892 0.0970  -0.0898 345 GLY B O   
6822  N N   . PHE B  346 ? 0.5135 0.6306 0.8100 -0.1939 0.0928  -0.0732 346 PHE B N   
6823  C CA  . PHE B  346 ? 0.5807 0.6976 0.8668 -0.2019 0.1051  -0.0800 346 PHE B CA  
6824  C C   . PHE B  346 ? 0.6635 0.7837 0.9463 -0.2090 0.1028  -0.0767 346 PHE B C   
6825  O O   . PHE B  346 ? 0.7057 0.8125 0.9705 -0.2098 0.0969  -0.0672 346 PHE B O   
6826  C CB  . PHE B  346 ? 0.4372 0.5331 0.6929 -0.2027 0.1125  -0.0784 346 PHE B CB  
6827  C CG  . PHE B  346 ? 0.4255 0.5187 0.6838 -0.1969 0.1168  -0.0834 346 PHE B CG  
6828  C CD1 . PHE B  346 ? 0.3936 0.4827 0.6578 -0.1881 0.1078  -0.0781 346 PHE B CD1 
6829  C CD2 . PHE B  346 ? 0.4242 0.5187 0.6782 -0.2006 0.1298  -0.0935 346 PHE B CD2 
6830  C CE1 . PHE B  346 ? 0.3617 0.4482 0.6292 -0.1827 0.1118  -0.0831 346 PHE B CE1 
6831  C CE2 . PHE B  346 ? 0.4148 0.5069 0.6713 -0.1956 0.1338  -0.0986 346 PHE B CE2 
6832  C CZ  . PHE B  346 ? 0.3816 0.4697 0.6455 -0.1863 0.1247  -0.0935 346 PHE B CZ  
6833  N N   . SER B  347 ? 0.6271 0.7655 0.9285 -0.2140 0.1076  -0.0852 347 SER B N   
6834  C CA  . SER B  347 ? 0.6441 0.7875 0.9444 -0.2217 0.1071  -0.0841 347 SER B CA  
6835  C C   . SER B  347 ? 0.6652 0.8124 0.9606 -0.2296 0.1212  -0.0942 347 SER B C   
6836  O O   . SER B  347 ? 0.6726 0.8220 0.9700 -0.2288 0.1302  -0.1025 347 SER B O   
6837  C CB  . SER B  347 ? 0.6179 0.7823 0.9477 -0.2206 0.0977  -0.0844 347 SER B CB  
6838  O OG  . SER B  347 ? 0.6259 0.7994 0.9595 -0.2287 0.0996  -0.0867 347 SER B OG  
6839  N N   . LYS B  348 ? 0.5731 0.7201 0.8605 -0.2375 0.1235  -0.0936 348 LYS B N   
6840  C CA  . LYS B  348 ? 0.6222 0.7758 0.9083 -0.2460 0.1362  -0.1036 348 LYS B CA  
6841  C C   . LYS B  348 ? 0.6384 0.8189 0.9583 -0.2470 0.1361  -0.1126 348 LYS B C   
6842  O O   . LYS B  348 ? 0.6574 0.8487 0.9839 -0.2524 0.1468  -0.1234 348 LYS B O   
6843  C CB  . LYS B  348 ? 0.8480 0.9902 1.1122 -0.2543 0.1390  -0.0999 348 LYS B CB  
6844  C CG  . LYS B  348 ? 0.8806 1.0315 1.1566 -0.2566 0.1298  -0.0955 348 LYS B CG  
6845  C CD  . LYS B  348 ? 0.8776 1.0316 1.1481 -0.2672 0.1372  -0.1000 348 LYS B CD  
6846  C CE  . LYS B  348 ? 0.8477 1.0019 1.1195 -0.2695 0.1280  -0.0933 348 LYS B CE  
6847  N NZ  . LYS B  348 ? 0.8205 0.9934 1.1212 -0.2653 0.1165  -0.0918 348 LYS B NZ  
6848  N N   . ASP B  349 ? 0.7138 0.9051 1.0548 -0.2416 0.1236  -0.1081 349 ASP B N   
6849  C CA  . ASP B  349 ? 0.7215 0.9384 1.0954 -0.2419 0.1209  -0.1151 349 ASP B CA  
6850  C C   . ASP B  349 ? 0.7311 0.9620 1.1300 -0.2347 0.1222  -0.1238 349 ASP B C   
6851  O O   . ASP B  349 ? 0.7181 0.9614 1.1285 -0.2375 0.1326  -0.1360 349 ASP B O   
6852  C CB  . ASP B  349 ? 0.7471 0.9694 1.1312 -0.2405 0.1063  -0.1059 349 ASP B CB  
6853  C CG  . ASP B  349 ? 0.7746 0.9854 1.1377 -0.2479 0.1055  -0.0994 349 ASP B CG  
6854  O OD1 . ASP B  349 ? 0.7659 0.9767 1.1207 -0.2561 0.1158  -0.1054 349 ASP B OD1 
6855  O OD2 . ASP B  349 ? 0.8022 1.0036 1.1568 -0.2458 0.0949  -0.0887 349 ASP B OD2 
6856  N N   . ASN B  350 ? 0.7778 1.0068 1.1852 -0.2253 0.1121  -0.1181 350 ASN B N   
6857  C CA  . ASN B  350 ? 0.7692 1.0076 1.1975 -0.2175 0.1141  -0.1266 350 ASN B CA  
6858  C C   . ASN B  350 ? 0.7740 0.9996 1.1828 -0.2188 0.1271  -0.1322 350 ASN B C   
6859  O O   . ASN B  350 ? 0.8135 1.0200 1.1915 -0.2233 0.1311  -0.1264 350 ASN B O   
6860  C CB  . ASN B  350 ? 0.7178 0.9575 1.1613 -0.2070 0.1003  -0.1199 350 ASN B CB  
6861  C CG  . ASN B  350 ? 0.7447 0.9617 1.1620 -0.2042 0.0942  -0.1072 350 ASN B CG  
6862  O OD1 . ASN B  350 ? 0.7331 0.9321 1.1217 -0.2081 0.1011  -0.1044 350 ASN B OD1 
6863  N ND2 . ASN B  350 ? 0.8089 1.0268 1.2367 -0.1970 0.0810  -0.0997 350 ASN B ND2 
6864  N N   . GLU B  351 ? 0.5934 0.8295 1.0195 -0.2151 0.1339  -0.1440 351 GLU B N   
6865  C CA  . GLU B  351 ? 0.6315 0.8571 1.0385 -0.2180 0.1470  -0.1503 351 GLU B CA  
6866  C C   . GLU B  351 ? 0.5924 0.8013 0.9874 -0.2102 0.1439  -0.1447 351 GLU B C   
6867  O O   . GLU B  351 ? 0.5638 0.7649 0.9464 -0.2107 0.1533  -0.1503 351 GLU B O   
6868  C CB  . GLU B  351 ? 1.0518 1.2951 1.4772 -0.2207 0.1586  -0.1669 351 GLU B CB  
6869  C CG  . GLU B  351 ? 1.1234 1.3780 1.5761 -0.2111 0.1578  -0.1760 351 GLU B CG  
6870  C CD  . GLU B  351 ? 1.1893 1.4503 1.6427 -0.2152 0.1729  -0.1913 351 GLU B CD  
6871  O OE1 . GLU B  351 ? 1.1659 1.4285 1.6061 -0.2259 0.1832  -0.1960 351 GLU B OE1 
6872  O OE2 . GLU B  351 ? 1.2394 1.5033 1.7060 -0.2080 0.1745  -0.1988 351 GLU B OE2 
6873  N N   . SER B  352 ? 0.8507 1.0551 1.2500 -0.2034 0.1302  -0.1339 352 SER B N   
6874  C CA  . SER B  352 ? 0.8388 1.0235 1.2193 -0.1980 0.1254  -0.1246 352 SER B CA  
6875  C C   . SER B  352 ? 0.8149 0.9988 1.2048 -0.1901 0.1282  -0.1311 352 SER B C   
6876  O O   . SER B  352 ? 0.8420 1.0087 1.2100 -0.1890 0.1314  -0.1279 352 SER B O   
6877  C CB  . SER B  352 ? 0.7472 0.9105 1.0895 -0.2049 0.1313  -0.1183 352 SER B CB  
6878  O OG  . SER B  352 ? 0.7411 0.9003 1.0723 -0.2101 0.1259  -0.1096 352 SER B OG  
6879  N N   . LEU B  353 ? 0.6224 0.8247 1.0454 -0.1844 0.1268  -0.1404 353 LEU B N   
6880  C CA  . LEU B  353 ? 0.5747 0.7764 1.0109 -0.1751 0.1267  -0.1457 353 LEU B CA  
6881  C C   . LEU B  353 ? 0.5452 0.7359 0.9794 -0.1674 0.1130  -0.1329 353 LEU B C   
6882  O O   . LEU B  353 ? 0.5364 0.7316 0.9789 -0.1662 0.1019  -0.1251 353 LEU B O   
6883  C CB  . LEU B  353 ? 0.6368 0.8605 1.1102 -0.1703 0.1275  -0.1589 353 LEU B CB  
6884  C CG  . LEU B  353 ? 0.6857 0.9213 1.1597 -0.1796 0.1409  -0.1711 353 LEU B CG  
6885  C CD1 . LEU B  353 ? 0.7086 0.9683 1.2190 -0.1771 0.1387  -0.1810 353 LEU B CD1 
6886  C CD2 . LEU B  353 ? 0.6916 0.9215 1.1531 -0.1819 0.1545  -0.1812 353 LEU B CD2 
6887  N N   . ILE B  354 ? 0.5515 0.7273 0.9730 -0.1627 0.1137  -0.1306 354 ILE B N   
6888  C CA  . ILE B  354 ? 0.5364 0.6991 0.9501 -0.1567 0.1018  -0.1177 354 ILE B CA  
6889  C C   . ILE B  354 ? 0.5322 0.6945 0.9649 -0.1454 0.0971  -0.1204 354 ILE B C   
6890  O O   . ILE B  354 ? 0.5357 0.7049 0.9830 -0.1425 0.1046  -0.1326 354 ILE B O   
6891  C CB  . ILE B  354 ? 0.4961 0.6368 0.8712 -0.1617 0.1042  -0.1081 354 ILE B CB  
6892  C CG1 . ILE B  354 ? 0.5062 0.6382 0.8661 -0.1634 0.1168  -0.1155 354 ILE B CG1 
6893  C CG2 . ILE B  354 ? 0.5039 0.6436 0.8623 -0.1713 0.1056  -0.1034 354 ILE B CG2 
6894  C CD1 . ILE B  354 ? 0.4884 0.5971 0.8134 -0.1648 0.1169  -0.1058 354 ILE B CD1 
6895  N N   . SER B  355 ? 0.4747 0.6290 0.9074 -0.1391 0.0846  -0.1094 355 SER B N   
6896  C CA  . SER B  355 ? 0.4625 0.6139 0.9117 -0.1281 0.0791  -0.1105 355 SER B CA  
6897  C C   . SER B  355 ? 0.4121 0.5468 0.8390 -0.1276 0.0861  -0.1106 355 SER B C   
6898  O O   . SER B  355 ? 0.4036 0.5286 0.8021 -0.1355 0.0938  -0.1087 355 SER B O   
6899  C CB  . SER B  355 ? 0.5729 0.7205 1.0276 -0.1221 0.0636  -0.0983 355 SER B CB  
6900  O OG  . SER B  355 ? 0.5911 0.7210 1.0147 -0.1251 0.0605  -0.0861 355 SER B OG  
6901  N N   . ARG B  356 ? 0.4390 0.5695 0.8782 -0.1182 0.0829  -0.1126 356 ARG B N   
6902  C CA  . ARG B  356 ? 0.4461 0.5603 0.8636 -0.1176 0.0883  -0.1116 356 ARG B CA  
6903  C C   . ARG B  356 ? 0.3968 0.4937 0.7878 -0.1181 0.0805  -0.0964 356 ARG B C   
6904  O O   . ARG B  356 ? 0.3665 0.4493 0.7277 -0.1229 0.0860  -0.0928 356 ARG B O   
6905  C CB  . ARG B  356 ? 0.5460 0.6605 0.9843 -0.1077 0.0875  -0.1187 356 ARG B CB  
6906  C CG  . ARG B  356 ? 0.5558 0.6528 0.9714 -0.1065 0.0910  -0.1160 356 ARG B CG  
6907  C CD  . ARG B  356 ? 0.5931 0.6935 1.0252 -0.1013 0.0975  -0.1291 356 ARG B CD  
6908  N NE  . ARG B  356 ? 0.6092 0.6948 1.0167 -0.1028 0.1038  -0.1285 356 ARG B NE  
6909  C CZ  . ARG B  356 ? 0.5925 0.6740 0.9757 -0.1119 0.1160  -0.1327 356 ARG B CZ  
6910  N NH1 . ARG B  356 ? 0.6096 0.7007 0.9896 -0.1205 0.1235  -0.1377 356 ARG B NH1 
6911  N NH2 . ARG B  356 ? 0.5386 0.6059 0.8999 -0.1127 0.1205  -0.1315 356 ARG B NH2 
6912  N N   . ALA B  357 ? 0.3565 0.4543 0.7581 -0.1130 0.0676  -0.0876 357 ALA B N   
6913  C CA  . ALA B  357 ? 0.3802 0.4631 0.7583 -0.1132 0.0594  -0.0737 357 ALA B CA  
6914  C C   . ALA B  357 ? 0.4139 0.4919 0.7642 -0.1237 0.0626  -0.0683 357 ALA B C   
6915  O O   . ALA B  357 ? 0.4233 0.4851 0.7445 -0.1260 0.0615  -0.0599 357 ALA B O   
6916  C CB  . ALA B  357 ? 0.5019 0.5889 0.8979 -0.1068 0.0457  -0.0666 357 ALA B CB  
6917  N N   . GLN B  358 ? 0.6317 0.7236 0.9915 -0.1298 0.0662  -0.0734 358 GLN B N   
6918  C CA  . GLN B  358 ? 0.7007 0.7888 1.0368 -0.1399 0.0703  -0.0698 358 GLN B CA  
6919  C C   . GLN B  358 ? 0.7423 0.8160 1.0515 -0.1437 0.0807  -0.0715 358 GLN B C   
6920  O O   . GLN B  358 ? 0.7886 0.8474 1.0696 -0.1471 0.0794  -0.0630 358 GLN B O   
6921  C CB  . GLN B  358 ? 0.6135 0.7199 0.9668 -0.1454 0.0741  -0.0771 358 GLN B CB  
6922  C CG  . GLN B  358 ? 0.6355 0.7502 0.9966 -0.1472 0.0636  -0.0701 358 GLN B CG  
6923  C CD  . GLN B  358 ? 0.6844 0.8187 1.0660 -0.1517 0.0667  -0.0779 358 GLN B CD  
6924  O OE1 . GLN B  358 ? 0.7043 0.8510 1.1085 -0.1488 0.0723  -0.0892 358 GLN B OE1 
6925  N NE2 . GLN B  358 ? 0.7043 0.8420 1.0786 -0.1586 0.0630  -0.0724 358 GLN B NE2 
6926  N N   . PHE B  359 ? 0.6231 0.7016 0.9413 -0.1428 0.0907  -0.0828 359 PHE B N   
6927  C CA  . PHE B  359 ? 0.5550 0.6208 0.8488 -0.1464 0.1011  -0.0857 359 PHE B CA  
6928  C C   . PHE B  359 ? 0.5125 0.5590 0.7855 -0.1417 0.0960  -0.0766 359 PHE B C   
6929  O O   . PHE B  359 ? 0.5264 0.5577 0.7697 -0.1457 0.0986  -0.0711 359 PHE B O   
6930  C CB  . PHE B  359 ? 0.3683 0.4436 0.6786 -0.1452 0.1114  -0.0999 359 PHE B CB  
6931  C CG  . PHE B  359 ? 0.3584 0.4203 0.6446 -0.1479 0.1212  -0.1029 359 PHE B CG  
6932  C CD1 . PHE B  359 ? 0.3117 0.3677 0.5734 -0.1573 0.1305  -0.1040 359 PHE B CD1 
6933  C CD2 . PHE B  359 ? 0.2910 0.3463 0.5795 -0.1412 0.1209  -0.1048 359 PHE B CD2 
6934  C CE1 . PHE B  359 ? 0.4976 0.5410 0.7364 -0.1601 0.1391  -0.1064 359 PHE B CE1 
6935  C CE2 . PHE B  359 ? 0.2993 0.3427 0.5655 -0.1441 0.1297  -0.1076 359 PHE B CE2 
6936  C CZ  . PHE B  359 ? 0.3144 0.3518 0.5553 -0.1536 0.1387  -0.1083 359 PHE B CZ  
6937  N N   . LEU B  360 ? 0.4700 0.5171 0.7591 -0.1328 0.0885  -0.0751 360 LEU B N   
6938  C CA  . LEU B  360 ? 0.4610 0.4913 0.7336 -0.1274 0.0831  -0.0671 360 LEU B CA  
6939  C C   . LEU B  360 ? 0.4463 0.4635 0.6920 -0.1302 0.0762  -0.0544 360 LEU B C   
6940  O O   . LEU B  360 ? 0.4577 0.4586 0.6780 -0.1297 0.0767  -0.0494 360 LEU B O   
6941  C CB  . LEU B  360 ? 0.4225 0.4570 0.7195 -0.1174 0.0743  -0.0665 360 LEU B CB  
6942  C CG  . LEU B  360 ? 0.4126 0.4573 0.7360 -0.1125 0.0800  -0.0791 360 LEU B CG  
6943  C CD1 . LEU B  360 ? 0.3973 0.4432 0.7437 -0.1015 0.0703  -0.0773 360 LEU B CD1 
6944  C CD2 . LEU B  360 ? 0.4112 0.4467 0.7163 -0.1153 0.0912  -0.0849 360 LEU B CD2 
6945  N N   . ALA B  361 ? 0.3496 0.3743 0.6015 -0.1328 0.0694  -0.0497 361 ALA B N   
6946  C CA  . ALA B  361 ? 0.3183 0.3322 0.5467 -0.1357 0.0625  -0.0385 361 ALA B CA  
6947  C C   . ALA B  361 ? 0.3210 0.3290 0.5281 -0.1436 0.0693  -0.0382 361 ALA B C   
6948  O O   . ALA B  361 ? 0.2777 0.2716 0.4603 -0.1445 0.0665  -0.0305 361 ALA B O   
6949  C CB  . ALA B  361 ? 0.3449 0.3690 0.5872 -0.1361 0.0529  -0.0339 361 ALA B CB  
6950  N N   . GLY B  362 ? 0.4017 0.4209 0.6196 -0.1486 0.0784  -0.0472 362 GLY B N   
6951  C CA  . GLY B  362 ? 0.4065 0.4209 0.6062 -0.1562 0.0863  -0.0485 362 GLY B CA  
6952  C C   . GLY B  362 ? 0.3645 0.3617 0.5390 -0.1553 0.0919  -0.0478 362 GLY B C   
6953  O O   . GLY B  362 ? 0.3522 0.3377 0.5037 -0.1587 0.0934  -0.0434 362 GLY B O   
6954  N N   . VAL B  363 ? 0.3242 0.3198 0.5040 -0.1505 0.0949  -0.0524 363 VAL B N   
6955  C CA  . VAL B  363 ? 0.3636 0.3430 0.5200 -0.1492 0.0993  -0.0515 363 VAL B CA  
6956  C C   . VAL B  363 ? 0.3812 0.3452 0.5179 -0.1450 0.0895  -0.0397 363 VAL B C   
6957  O O   . VAL B  363 ? 0.3792 0.3298 0.4915 -0.1467 0.0917  -0.0363 363 VAL B O   
6958  C CB  . VAL B  363 ? 0.3416 0.3227 0.5095 -0.1441 0.1029  -0.0584 363 VAL B CB  
6959  C CG1 . VAL B  363 ? 0.3038 0.2672 0.4461 -0.1425 0.1057  -0.0561 363 VAL B CG1 
6960  C CG2 . VAL B  363 ? 0.3375 0.3337 0.5234 -0.1485 0.1138  -0.0715 363 VAL B CG2 
6961  N N   . ARG B  364 ? 0.3864 0.3530 0.5339 -0.1395 0.0787  -0.0340 364 ARG B N   
6962  C CA  . ARG B  364 ? 0.3986 0.3530 0.5294 -0.1357 0.0688  -0.0233 364 ARG B CA  
6963  C C   . ARG B  364 ? 0.4098 0.3598 0.5261 -0.1405 0.0681  -0.0188 364 ARG B C   
6964  O O   . ARG B  364 ? 0.4351 0.3724 0.5322 -0.1381 0.0652  -0.0130 364 ARG B O   
6965  C CB  . ARG B  364 ? 0.3834 0.3432 0.5277 -0.1314 0.0578  -0.0184 364 ARG B CB  
6966  C CG  . ARG B  364 ? 0.4404 0.4028 0.5994 -0.1248 0.0572  -0.0221 364 ARG B CG  
6967  C CD  . ARG B  364 ? 0.4827 0.4344 0.6293 -0.1220 0.0634  -0.0253 364 ARG B CD  
6968  N NE  . ARG B  364 ? 0.4765 0.4130 0.5998 -0.1183 0.0575  -0.0172 364 ARG B NE  
6969  C CZ  . ARG B  364 ? 0.4807 0.4121 0.6030 -0.1115 0.0509  -0.0137 364 ARG B CZ  
6970  N NH1 . ARG B  364 ? 0.4351 0.3744 0.5787 -0.1073 0.0496  -0.0173 364 ARG B NH1 
6971  N NH2 . ARG B  364 ? 0.5206 0.4397 0.6224 -0.1083 0.0456  -0.0072 364 ARG B NH2 
6972  N N   . ILE B  365 ? 0.3923 0.3539 0.5197 -0.1467 0.0710  -0.0220 365 ILE B N   
6973  C CA  . ILE B  365 ? 0.4097 0.3678 0.5252 -0.1515 0.0711  -0.0187 365 ILE B CA  
6974  C C   . ILE B  365 ? 0.4250 0.3726 0.5200 -0.1550 0.0808  -0.0218 365 ILE B C   
6975  O O   . ILE B  365 ? 0.4846 0.4200 0.5612 -0.1538 0.0789  -0.0169 365 ILE B O   
6976  C CB  . ILE B  365 ? 0.4178 0.3913 0.5508 -0.1574 0.0711  -0.0213 365 ILE B CB  
6977  C CG1 . ILE B  365 ? 0.4326 0.4154 0.5830 -0.1545 0.0603  -0.0170 365 ILE B CG1 
6978  C CG2 . ILE B  365 ? 0.4131 0.3823 0.5338 -0.1623 0.0720  -0.0186 365 ILE B CG2 
6979  C CD1 . ILE B  365 ? 0.4541 0.4514 0.6200 -0.1601 0.0577  -0.0175 365 ILE B CD1 
6980  N N   . GLY B  366 ? 0.3549 0.3073 0.4529 -0.1595 0.0913  -0.0304 366 GLY B N   
6981  C CA  . GLY B  366 ? 0.3567 0.3000 0.4344 -0.1649 0.1007  -0.0335 366 GLY B CA  
6982  C C   . GLY B  366 ? 0.3730 0.3001 0.4297 -0.1611 0.1024  -0.0317 366 GLY B C   
6983  O O   . GLY B  366 ? 0.3843 0.3008 0.4203 -0.1650 0.1081  -0.0321 366 GLY B O   
6984  N N   . VAL B  367 ? 0.3323 0.2577 0.3944 -0.1537 0.0973  -0.0298 367 VAL B N   
6985  C CA  . VAL B  367 ? 0.3871 0.2973 0.4303 -0.1489 0.0967  -0.0270 367 VAL B CA  
6986  C C   . VAL B  367 ? 0.3651 0.2720 0.4106 -0.1405 0.0845  -0.0188 367 VAL B C   
6987  O O   . VAL B  367 ? 0.3366 0.2437 0.3892 -0.1347 0.0806  -0.0183 367 VAL B O   
6988  C CB  . VAL B  367 ? 0.3350 0.2458 0.3816 -0.1479 0.1030  -0.0335 367 VAL B CB  
6989  C CG1 . VAL B  367 ? 0.3443 0.2387 0.3662 -0.1464 0.1054  -0.0318 367 VAL B CG1 
6990  C CG2 . VAL B  367 ? 0.4912 0.4135 0.5480 -0.1557 0.1141  -0.0435 367 VAL B CG2 
6991  N N   . PRO B  368 ? 0.3686 0.2723 0.4080 -0.1401 0.0787  -0.0129 368 PRO B N   
6992  C CA  . PRO B  368 ? 0.4036 0.3075 0.4484 -0.1335 0.0672  -0.0058 368 PRO B CA  
6993  C C   . PRO B  368 ? 0.4471 0.3402 0.4804 -0.1257 0.0628  -0.0022 368 PRO B C   
6994  O O   . PRO B  368 ? 0.4368 0.3316 0.4774 -0.1200 0.0545  0.0019  368 PRO B O   
6995  C CB  . PRO B  368 ? 0.3291 0.2321 0.3688 -0.1363 0.0651  -0.0026 368 PRO B CB  
6996  C CG  . PRO B  368 ? 0.3425 0.2384 0.3660 -0.1423 0.0746  -0.0064 368 PRO B CG  
6997  C CD  . PRO B  368 ? 0.3327 0.2284 0.3544 -0.1448 0.0831  -0.0126 368 PRO B CD  
6998  N N   . GLN B  369 ? 0.5398 0.4220 0.5550 -0.1261 0.0686  -0.0039 369 GLN B N   
6999  C CA  . GLN B  369 ? 0.6660 0.5380 0.6695 -0.1194 0.0653  -0.0012 369 GLN B CA  
7000  C C   . GLN B  369 ? 0.6476 0.5210 0.6577 -0.1158 0.0654  -0.0035 369 GLN B C   
7001  O O   . GLN B  369 ? 0.6687 0.5355 0.6722 -0.1096 0.0618  -0.0013 369 GLN B O   
7002  C CB  . GLN B  369 ? 1.1939 1.0525 1.1740 -0.1216 0.0709  -0.0020 369 GLN B CB  
7003  C CG  . GLN B  369 ? 1.3797 1.2319 1.3488 -0.1229 0.0696  0.0003  369 GLN B CG  
7004  C CD  . GLN B  369 ? 1.5142 1.3719 1.4871 -0.1305 0.0731  -0.0013 369 GLN B CD  
7005  O OE1 . GLN B  369 ? 1.5621 1.4258 1.5401 -0.1359 0.0786  -0.0046 369 GLN B OE1 
7006  N NE2 . GLN B  369 ? 1.5415 1.3978 1.5122 -0.1311 0.0702  0.0007  369 GLN B NE2 
7007  N N   . ALA B  370 ? 0.5887 0.4710 0.6128 -0.1197 0.0702  -0.0087 370 ALA B N   
7008  C CA  . ALA B  370 ? 0.5368 0.4205 0.5686 -0.1170 0.0722  -0.0128 370 ALA B CA  
7009  C C   . ALA B  370 ? 0.4793 0.3668 0.5239 -0.1099 0.0617  -0.0086 370 ALA B C   
7010  O O   . ALA B  370 ? 0.4347 0.3296 0.4904 -0.1099 0.0551  -0.0052 370 ALA B O   
7011  C CB  . ALA B  370 ? 0.6048 0.4985 0.6501 -0.1233 0.0815  -0.0213 370 ALA B CB  
7012  N N   . SER B  371 ? 0.4956 0.3778 0.5374 -0.1043 0.0600  -0.0088 371 SER B N   
7013  C CA  . SER B  371 ? 0.5550 0.4404 0.6080 -0.0981 0.0511  -0.0060 371 SER B CA  
7014  C C   . SER B  371 ? 0.5714 0.4672 0.6457 -0.0997 0.0552  -0.0125 371 SER B C   
7015  O O   . SER B  371 ? 0.5912 0.4921 0.6716 -0.1053 0.0648  -0.0194 371 SER B O   
7016  C CB  . SER B  371 ? 0.7769 0.6538 0.8207 -0.0917 0.0485  -0.0050 371 SER B CB  
7017  O OG  . SER B  371 ? 0.8025 0.6768 0.8455 -0.0932 0.0579  -0.0122 371 SER B OG  
7018  N N   . ASP B  372 ? 0.5964 0.4958 0.6826 -0.0946 0.0485  -0.0111 372 ASP B N   
7019  C CA  . ASP B  372 ? 0.6178 0.5285 0.7294 -0.0939 0.0519  -0.0178 372 ASP B CA  
7020  C C   . ASP B  372 ? 0.5706 0.4821 0.6887 -0.0945 0.0623  -0.0273 372 ASP B C   
7021  O O   . ASP B  372 ? 0.5407 0.4632 0.6781 -0.0976 0.0694  -0.0355 372 ASP B O   
7022  C CB  . ASP B  372 ? 0.8303 0.7427 0.9517 -0.0867 0.0436  -0.0147 372 ASP B CB  
7023  C CG  . ASP B  372 ? 0.9005 0.8151 1.0195 -0.0876 0.0353  -0.0077 372 ASP B CG  
7024  O OD1 . ASP B  372 ? 0.9355 0.8451 1.0366 -0.0919 0.0328  -0.0027 372 ASP B OD1 
7025  O OD2 . ASP B  372 ? 0.9142 0.8360 1.0507 -0.0838 0.0314  -0.0075 372 ASP B OD2 
7026  N N   . LEU B  373 ? 0.6285 0.5291 0.7306 -0.0916 0.0632  -0.0267 373 LEU B N   
7027  C CA  . LEU B  373 ? 0.5646 0.4641 0.6688 -0.0926 0.0730  -0.0357 373 LEU B CA  
7028  C C   . LEU B  373 ? 0.5849 0.4842 0.6794 -0.1018 0.0845  -0.0411 373 LEU B C   
7029  O O   . LEU B  373 ? 0.5818 0.4899 0.6903 -0.1057 0.0939  -0.0512 373 LEU B O   
7030  C CB  . LEU B  373 ? 0.3326 0.2203 0.4209 -0.0873 0.0698  -0.0329 373 LEU B CB  
7031  C CG  . LEU B  373 ? 0.3038 0.1898 0.3941 -0.0878 0.0789  -0.0422 373 LEU B CG  
7032  C CD1 . LEU B  373 ? 0.2627 0.1623 0.3841 -0.0860 0.0822  -0.0513 373 LEU B CD1 
7033  C CD2 . LEU B  373 ? 0.2914 0.1668 0.3683 -0.0816 0.0735  -0.0385 373 LEU B CD2 
7034  N N   . ALA B  374 ? 0.5513 0.4416 0.6226 -0.1051 0.0837  -0.0351 374 ALA B N   
7035  C CA  . ALA B  374 ? 0.5125 0.4017 0.5718 -0.1140 0.0940  -0.0391 374 ALA B CA  
7036  C C   . ALA B  374 ? 0.4834 0.3878 0.5632 -0.1192 0.0984  -0.0448 374 ALA B C   
7037  O O   . ALA B  374 ? 0.5330 0.4426 0.6145 -0.1261 0.1094  -0.0534 374 ALA B O   
7038  C CB  . ALA B  374 ? 0.4709 0.3498 0.5071 -0.1152 0.0902  -0.0310 374 ALA B CB  
7039  N N   . ALA B  375 ? 0.3849 0.2971 0.4800 -0.1161 0.0895  -0.0401 375 ALA B N   
7040  C CA  . ALA B  375 ? 0.3831 0.3113 0.5012 -0.1198 0.0920  -0.0452 375 ALA B CA  
7041  C C   . ALA B  375 ? 0.4605 0.4002 0.6034 -0.1186 0.0986  -0.0566 375 ALA B C   
7042  O O   . ALA B  375 ? 0.4428 0.3937 0.5968 -0.1245 0.1076  -0.0657 375 ALA B O   
7043  C CB  . ALA B  375 ? 0.2737 0.2067 0.4023 -0.1162 0.0804  -0.0377 375 ALA B CB  
7044  N N   . GLU B  376 ? 0.6041 0.5419 0.7563 -0.1108 0.0940  -0.0567 376 GLU B N   
7045  C CA  . GLU B  376 ? 0.6514 0.5998 0.8293 -0.1080 0.0991  -0.0678 376 GLU B CA  
7046  C C   . GLU B  376 ? 0.6008 0.5491 0.7704 -0.1150 0.1130  -0.0784 376 GLU B C   
7047  O O   . GLU B  376 ? 0.6091 0.5711 0.8001 -0.1169 0.1207  -0.0904 376 GLU B O   
7048  C CB  . GLU B  376 ? 0.7921 0.7348 0.9752 -0.0984 0.0917  -0.0650 376 GLU B CB  
7049  C CG  . GLU B  376 ? 0.8880 0.8442 1.1071 -0.0915 0.0884  -0.0709 376 GLU B CG  
7050  C CD  . GLU B  376 ? 0.9812 0.9389 1.2098 -0.0853 0.0753  -0.0611 376 GLU B CD  
7051  O OE1 . GLU B  376 ? 1.0006 0.9500 1.2079 -0.0870 0.0693  -0.0505 376 GLU B OE1 
7052  O OE2 . GLU B  376 ? 1.0173 0.9846 1.2748 -0.0787 0.0709  -0.0642 376 GLU B OE2 
7053  N N   . ALA B  377 ? 0.4915 0.4245 0.6292 -0.1188 0.1159  -0.0739 377 ALA B N   
7054  C CA  . ALA B  377 ? 0.4652 0.3947 0.5875 -0.1266 0.1287  -0.0819 377 ALA B CA  
7055  C C   . ALA B  377 ? 0.4751 0.4142 0.5977 -0.1361 0.1373  -0.0872 377 ALA B C   
7056  O O   . ALA B  377 ? 0.4885 0.4366 0.6172 -0.1422 0.1487  -0.0990 377 ALA B O   
7057  C CB  . ALA B  377 ? 0.3202 0.2293 0.4073 -0.1271 0.1273  -0.0737 377 ALA B CB  
7058  N N   . VAL B  378 ? 0.4268 0.3646 0.5427 -0.1376 0.1317  -0.0788 378 VAL B N   
7059  C CA  . VAL B  378 ? 0.4423 0.3887 0.5578 -0.1463 0.1386  -0.0827 378 VAL B CA  
7060  C C   . VAL B  378 ? 0.4754 0.4436 0.6260 -0.1461 0.1415  -0.0933 378 VAL B C   
7061  O O   . VAL B  378 ? 0.5123 0.4910 0.6678 -0.1532 0.1522  -0.1037 378 VAL B O   
7062  C CB  . VAL B  378 ? 0.3563 0.2970 0.4594 -0.1472 0.1308  -0.0716 378 VAL B CB  
7063  C CG1 . VAL B  378 ? 0.3565 0.3082 0.4640 -0.1556 0.1370  -0.0761 378 VAL B CG1 
7064  C CG2 . VAL B  378 ? 0.3400 0.2605 0.4097 -0.1474 0.1289  -0.0631 378 VAL B CG2 
7065  N N   . VAL B  379 ? 0.4550 0.4301 0.6300 -0.1376 0.1318  -0.0908 379 VAL B N   
7066  C CA  . VAL B  379 ? 0.4177 0.4132 0.6284 -0.1354 0.1324  -0.1000 379 VAL B CA  
7067  C C   . VAL B  379 ? 0.3869 0.3907 0.6117 -0.1354 0.1421  -0.1144 379 VAL B C   
7068  O O   . VAL B  379 ? 0.3840 0.4030 0.6235 -0.1399 0.1504  -0.1257 379 VAL B O   
7069  C CB  . VAL B  379 ? 0.3802 0.3795 0.6128 -0.1258 0.1189  -0.0936 379 VAL B CB  
7070  C CG1 . VAL B  379 ? 0.3883 0.4083 0.6589 -0.1227 0.1192  -0.1038 379 VAL B CG1 
7071  C CG2 . VAL B  379 ? 0.3584 0.3520 0.5783 -0.1268 0.1096  -0.0807 379 VAL B CG2 
7072  N N   . LEU B  380 ? 0.3078 0.3020 0.5279 -0.1303 0.1411  -0.1143 380 LEU B N   
7073  C CA  . LEU B  380 ? 0.3109 0.3113 0.5412 -0.1307 0.1505  -0.1281 380 LEU B CA  
7074  C C   . LEU B  380 ? 0.3225 0.3258 0.5362 -0.1424 0.1649  -0.1370 380 LEU B C   
7075  O O   . LEU B  380 ? 0.4503 0.4690 0.6820 -0.1449 0.1736  -0.1513 380 LEU B O   
7076  C CB  . LEU B  380 ? 0.3827 0.3680 0.5997 -0.1259 0.1479  -0.1248 380 LEU B CB  
7077  C CG  . LEU B  380 ? 0.3125 0.2986 0.5237 -0.1308 0.1604  -0.1376 380 LEU B CG  
7078  C CD1 . LEU B  380 ? 0.3027 0.3026 0.5489 -0.1235 0.1603  -0.1498 380 LEU B CD1 
7079  C CD2 . LEU B  380 ? 0.3204 0.2853 0.4975 -0.1323 0.1605  -0.1304 380 LEU B CD2 
7080  N N   . HIS B  381 ? 0.3930 0.3815 0.5722 -0.1494 0.1669  -0.1284 381 HIS B N   
7081  C CA  . HIS B  381 ? 0.4291 0.4175 0.5877 -0.1610 0.1798  -0.1350 381 HIS B CA  
7082  C C   . HIS B  381 ? 0.4228 0.4290 0.5969 -0.1666 0.1849  -0.1424 381 HIS B C   
7083  O O   . HIS B  381 ? 0.4310 0.4477 0.6081 -0.1732 0.1962  -0.1551 381 HIS B O   
7084  C CB  . HIS B  381 ? 0.6310 0.5976 0.7490 -0.1660 0.1790  -0.1232 381 HIS B CB  
7085  C CG  . HIS B  381 ? 0.7016 0.6622 0.7933 -0.1767 0.1914  -0.1291 381 HIS B CG  
7086  N ND1 . HIS B  381 ? 0.7307 0.6787 0.8029 -0.1778 0.1951  -0.1301 381 HIS B ND1 
7087  C CD2 . HIS B  381 ? 0.7218 0.6872 0.8028 -0.1872 0.2004  -0.1342 381 HIS B CD2 
7088  C CE1 . HIS B  381 ? 0.7531 0.6981 0.8026 -0.1887 0.2057  -0.1352 381 HIS B CE1 
7089  N NE2 . HIS B  381 ? 0.7589 0.7143 0.8134 -0.1944 0.2091  -0.1378 381 HIS B NE2 
7090  N N   . TYR B  382 ? 0.4999 0.5099 0.6834 -0.1642 0.1764  -0.1346 382 TYR B N   
7091  C CA  . TYR B  382 ? 0.4915 0.5168 0.6868 -0.1700 0.1804  -0.1398 382 TYR B CA  
7092  C C   . TYR B  382 ? 0.5091 0.5569 0.7458 -0.1644 0.1784  -0.1496 382 TYR B C   
7093  O O   . TYR B  382 ? 0.5202 0.5826 0.7691 -0.1691 0.1827  -0.1563 382 TYR B O   
7094  C CB  . TYR B  382 ? 0.3708 0.3883 0.5513 -0.1723 0.1734  -0.1269 382 TYR B CB  
7095  C CG  . TYR B  382 ? 0.3984 0.3972 0.5395 -0.1800 0.1778  -0.1206 382 TYR B CG  
7096  C CD1 . TYR B  382 ? 0.4125 0.3914 0.5296 -0.1770 0.1742  -0.1123 382 TYR B CD1 
7097  C CD2 . TYR B  382 ? 0.3922 0.3933 0.5208 -0.1900 0.1850  -0.1229 382 TYR B CD2 
7098  C CE1 . TYR B  382 ? 0.4462 0.4076 0.5282 -0.1831 0.1772  -0.1064 382 TYR B CE1 
7099  C CE2 . TYR B  382 ? 0.5016 0.4848 0.5949 -0.1964 0.1881  -0.1169 382 TYR B CE2 
7100  C CZ  . TYR B  382 ? 0.4972 0.4605 0.5675 -0.1927 0.1839  -0.1086 382 TYR B CZ  
7101  O OH  . TYR B  382 ? 0.5464 0.4911 0.5822 -0.1982 0.1858  -0.1023 382 TYR B OH  
7102  N N   . THR B  383 ? 0.5078 0.5578 0.7662 -0.1541 0.1714  -0.1504 383 THR B N   
7103  C CA  . THR B  383 ? 0.4730 0.5424 0.7717 -0.1469 0.1680  -0.1595 383 THR B CA  
7104  C C   . THR B  383 ? 0.4818 0.5641 0.7921 -0.1500 0.1802  -0.1773 383 THR B C   
7105  O O   . THR B  383 ? 0.5121 0.5869 0.8076 -0.1522 0.1871  -0.1819 383 THR B O   
7106  C CB  . THR B  383 ? 0.3033 0.3683 0.6193 -0.1346 0.1565  -0.1546 383 THR B CB  
7107  O OG1 . THR B  383 ? 0.4646 0.5217 0.7758 -0.1311 0.1439  -0.1393 383 THR B OG1 
7108  C CG2 . THR B  383 ? 0.2959 0.3785 0.6521 -0.1267 0.1541  -0.1659 383 THR B CG2 
7109  N N   . ASP B  384 ? 0.5042 0.6060 0.8404 -0.1504 0.1827  -0.1877 384 ASP B N   
7110  C CA  . ASP B  384 ? 0.5632 0.6786 0.9175 -0.1502 0.1916  -0.2058 384 ASP B CA  
7111  C C   . ASP B  384 ? 0.5890 0.7113 0.9788 -0.1369 0.1825  -0.2101 384 ASP B C   
7112  O O   . ASP B  384 ? 0.6235 0.7562 1.0407 -0.1306 0.1741  -0.2095 384 ASP B O   
7113  C CB  . ASP B  384 ? 0.5768 0.7097 0.9413 -0.1572 0.1994  -0.2167 384 ASP B CB  
7114  C CG  . ASP B  384 ? 0.5851 0.7343 0.9761 -0.1545 0.2055  -0.2357 384 ASP B CG  
7115  O OD1 . ASP B  384 ? 0.6052 0.7501 0.9932 -0.1526 0.2093  -0.2423 384 ASP B OD1 
7116  O OD2 . ASP B  384 ? 0.5722 0.7385 0.9873 -0.1542 0.2061  -0.2442 384 ASP B OD2 
7117  N N   . TRP B  385 ? 0.5633 0.6794 0.9524 -0.1329 0.1842  -0.2148 385 TRP B N   
7118  C CA  . TRP B  385 ? 0.5325 0.6489 0.9492 -0.1197 0.1736  -0.2150 385 TRP B CA  
7119  C C   . TRP B  385 ? 0.5936 0.7273 1.0464 -0.1141 0.1737  -0.2305 385 TRP B C   
7120  O O   . TRP B  385 ? 0.6273 0.7621 1.1070 -0.1027 0.1633  -0.2305 385 TRP B O   
7121  C CB  . TRP B  385 ? 0.3831 0.4859 0.7858 -0.1175 0.1748  -0.2140 385 TRP B CB  
7122  C CG  . TRP B  385 ? 0.3768 0.4611 0.7489 -0.1200 0.1705  -0.1969 385 TRP B CG  
7123  C CD1 . TRP B  385 ? 0.4090 0.4812 0.7437 -0.1302 0.1786  -0.1924 385 TRP B CD1 
7124  C CD2 . TRP B  385 ? 0.3510 0.4253 0.7252 -0.1122 0.1563  -0.1812 385 TRP B CD2 
7125  N NE1 . TRP B  385 ? 0.3957 0.4507 0.7098 -0.1286 0.1700  -0.1754 385 TRP B NE1 
7126  C CE2 . TRP B  385 ? 0.3511 0.4077 0.6887 -0.1179 0.1565  -0.1685 385 TRP B CE2 
7127  C CE3 . TRP B  385 ? 0.3173 0.3952 0.7197 -0.1011 0.1430  -0.1766 385 TRP B CE3 
7128  C CZ2 . TRP B  385 ? 0.3137 0.3571 0.6421 -0.1128 0.1442  -0.1522 385 TRP B CZ2 
7129  C CZ3 . TRP B  385 ? 0.2906 0.3556 0.6830 -0.0969 0.1312  -0.1599 385 TRP B CZ3 
7130  C CH2 . TRP B  385 ? 0.2912 0.3397 0.6470 -0.1027 0.1320  -0.1483 385 TRP B CH2 
7131  N N   . LEU B  386 ? 0.4516 0.5979 0.9040 -0.1223 0.1851  -0.2434 386 LEU B N   
7132  C CA  . LEU B  386 ? 0.4658 0.6288 0.9513 -0.1179 0.1856  -0.2588 386 LEU B CA  
7133  C C   . LEU B  386 ? 0.5199 0.6921 1.0284 -0.1134 0.1761  -0.2537 386 LEU B C   
7134  O O   . LEU B  386 ? 0.5287 0.7087 1.0697 -0.1040 0.1683  -0.2592 386 LEU B O   
7135  C CB  . LEU B  386 ? 0.4460 0.6193 0.9219 -0.1289 0.2009  -0.2744 386 LEU B CB  
7136  C CG  . LEU B  386 ? 0.4723 0.6558 0.9715 -0.1251 0.2040  -0.2927 386 LEU B CG  
7137  C CD1 . LEU B  386 ? 0.4903 0.6792 0.9692 -0.1377 0.2198  -0.3055 386 LEU B CD1 
7138  C CD2 . LEU B  386 ? 0.4863 0.6850 1.0235 -0.1180 0.1975  -0.2999 386 LEU B CD2 
7139  N N   . HIS B  387 ? 0.6393 0.8095 1.1298 -0.1202 0.1760  -0.2426 387 HIS B N   
7140  C CA  . HIS B  387 ? 0.6466 0.8242 1.1546 -0.1169 0.1662  -0.2352 387 HIS B CA  
7141  C C   . HIS B  387 ? 0.5960 0.7601 1.0826 -0.1181 0.1582  -0.2155 387 HIS B C   
7142  O O   . HIS B  387 ? 0.6122 0.7772 1.0821 -0.1267 0.1611  -0.2099 387 HIS B O   
7143  C CB  . HIS B  387 ? 0.7442 0.9380 1.2565 -0.1254 0.1747  -0.2444 387 HIS B CB  
7144  C CG  . HIS B  387 ? 0.8437 1.0507 1.3718 -0.1266 0.1843  -0.2643 387 HIS B CG  
7145  N ND1 . HIS B  387 ? 0.9023 1.1067 1.4097 -0.1346 0.1975  -0.2736 387 HIS B ND1 
7146  C CD2 . HIS B  387 ? 0.9059 1.1286 1.4678 -0.1213 0.1824  -0.2767 387 HIS B CD2 
7147  C CE1 . HIS B  387 ? 0.9501 1.1686 1.4778 -0.1344 0.2034  -0.2912 387 HIS B CE1 
7148  N NE2 . HIS B  387 ? 0.9555 1.1851 1.5168 -0.1262 0.1945  -0.2936 387 HIS B NE2 
7149  N N   . PRO B  388 ? 0.3813 0.5326 0.8683 -0.1097 0.1476  -0.2051 388 PRO B N   
7150  C CA  . PRO B  388 ? 0.3587 0.4954 0.8237 -0.1104 0.1396  -0.1867 388 PRO B CA  
7151  C C   . PRO B  388 ? 0.3874 0.5297 0.8584 -0.1113 0.1308  -0.1770 388 PRO B C   
7152  O O   . PRO B  388 ? 0.3529 0.4843 0.8004 -0.1153 0.1269  -0.1634 388 PRO B O   
7153  C CB  . PRO B  388 ? 0.4181 0.5444 0.8930 -0.0991 0.1291  -0.1810 388 PRO B CB  
7154  C CG  . PRO B  388 ? 0.4190 0.5502 0.9097 -0.0953 0.1356  -0.1967 388 PRO B CG  
7155  C CD  . PRO B  388 ? 0.4467 0.5962 0.9552 -0.0989 0.1427  -0.2110 388 PRO B CD  
7156  N N   . GLU B  389 ? 0.5848 0.7432 1.0865 -0.1073 0.1270  -0.1838 389 GLU B N   
7157  C CA  . GLU B  389 ? 0.6148 0.7799 1.1251 -0.1077 0.1177  -0.1751 389 GLU B CA  
7158  C C   . GLU B  389 ? 0.5968 0.7748 1.1039 -0.1177 0.1256  -0.1802 389 GLU B C   
7159  O O   . GLU B  389 ? 0.5538 0.7371 1.0647 -0.1194 0.1186  -0.1728 389 GLU B O   
7160  C CB  . GLU B  389 ? 0.7024 0.8756 1.2489 -0.0962 0.1058  -0.1767 389 GLU B CB  
7161  C CG  . GLU B  389 ? 0.7198 0.8799 1.2716 -0.0859 0.0963  -0.1705 389 GLU B CG  
7162  C CD  . GLU B  389 ? 0.7356 0.8839 1.2732 -0.0846 0.0844  -0.1521 389 GLU B CD  
7163  O OE1 . GLU B  389 ? 0.7420 0.8904 1.2610 -0.0926 0.0849  -0.1443 389 GLU B OE1 
7164  O OE2 . GLU B  389 ? 0.7345 0.8732 1.2792 -0.0757 0.0746  -0.1457 389 GLU B OE2 
7165  N N   . ASP B  390 ? 0.6517 0.8346 1.1508 -0.1249 0.1400  -0.1927 390 ASP B N   
7166  C CA  . ASP B  390 ? 0.7262 0.9227 1.2255 -0.1341 0.1482  -0.1996 390 ASP B CA  
7167  C C   . ASP B  390 ? 0.7756 0.9644 1.2472 -0.1432 0.1476  -0.1869 390 ASP B C   
7168  O O   . ASP B  390 ? 0.8269 1.0009 1.2661 -0.1496 0.1535  -0.1816 390 ASP B O   
7169  C CB  . ASP B  390 ? 0.8076 1.0088 1.3003 -0.1404 0.1641  -0.2153 390 ASP B CB  
7170  C CG  . ASP B  390 ? 0.8709 1.0798 1.3500 -0.1530 0.1747  -0.2198 390 ASP B CG  
7171  O OD1 . ASP B  390 ? 0.9040 1.1238 1.3953 -0.1548 0.1707  -0.2178 390 ASP B OD1 
7172  O OD2 . ASP B  390 ? 0.8782 1.0821 1.3340 -0.1615 0.1873  -0.2255 390 ASP B OD2 
7173  N N   . PRO B  391 ? 0.7796 0.9783 1.2638 -0.1438 0.1403  -0.1822 391 PRO B N   
7174  C CA  . PRO B  391 ? 0.7628 0.9546 1.2247 -0.1512 0.1370  -0.1694 391 PRO B CA  
7175  C C   . PRO B  391 ? 0.7385 0.9270 1.1734 -0.1637 0.1501  -0.1724 391 PRO B C   
7176  O O   . PRO B  391 ? 0.7702 0.9432 1.1751 -0.1691 0.1498  -0.1615 391 PRO B O   
7177  C CB  . PRO B  391 ? 0.7009 0.9097 1.1899 -0.1491 0.1284  -0.1691 391 PRO B CB  
7178  C CG  . PRO B  391 ? 0.6912 0.9080 1.2129 -0.1373 0.1216  -0.1750 391 PRO B CG  
7179  C CD  . PRO B  391 ? 0.7013 0.9178 1.2234 -0.1367 0.1333  -0.1885 391 PRO B CD  
7180  N N   . THR B  392 ? 0.6012 0.8036 1.0464 -0.1683 0.1611  -0.1869 392 THR B N   
7181  C CA  . THR B  392 ? 0.5927 0.7920 1.0123 -0.1807 0.1741  -0.1906 392 THR B CA  
7182  C C   . THR B  392 ? 0.6521 0.8307 1.0380 -0.1837 0.1801  -0.1865 392 THR B C   
7183  O O   . THR B  392 ? 0.6912 0.8558 1.0459 -0.1915 0.1827  -0.1781 392 THR B O   
7184  C CB  . THR B  392 ? 0.4767 0.6944 0.9137 -0.1844 0.1854  -0.2084 392 THR B CB  
7185  O OG1 . THR B  392 ? 0.4487 0.6851 0.9241 -0.1769 0.1780  -0.2141 392 THR B OG1 
7186  C CG2 . THR B  392 ? 0.3897 0.6093 0.8077 -0.1976 0.1954  -0.2106 392 THR B CG2 
7187  N N   . HIS B  393 ? 0.7170 0.8931 1.1094 -0.1772 0.1815  -0.1923 393 HIS B N   
7188  C CA  . HIS B  393 ? 0.7009 0.8578 1.0628 -0.1794 0.1863  -0.1884 393 HIS B CA  
7189  C C   . HIS B  393 ? 0.6172 0.7554 0.9591 -0.1768 0.1761  -0.1709 393 HIS B C   
7190  O O   . HIS B  393 ? 0.6436 0.7663 0.9531 -0.1836 0.1797  -0.1638 393 HIS B O   
7191  C CB  . HIS B  393 ? 0.7743 0.9322 1.1481 -0.1726 0.1890  -0.1978 393 HIS B CB  
7192  C CG  . HIS B  393 ? 0.8354 0.9738 1.1776 -0.1752 0.1937  -0.1937 393 HIS B CG  
7193  N ND1 . HIS B  393 ? 0.8699 1.0004 1.1813 -0.1864 0.2053  -0.1959 393 HIS B ND1 
7194  C CD2 . HIS B  393 ? 0.8507 0.9756 1.1870 -0.1681 0.1879  -0.1872 393 HIS B CD2 
7195  C CE1 . HIS B  393 ? 0.8740 0.9871 1.1619 -0.1860 0.2063  -0.1909 393 HIS B CE1 
7196  N NE2 . HIS B  393 ? 0.8654 0.9752 1.1683 -0.1749 0.1961  -0.1858 393 HIS B NE2 
7197  N N   . LEU B  394 ? 0.4636 0.6027 0.8243 -0.1669 0.1630  -0.1639 394 LEU B N   
7198  C CA  . LEU B  394 ? 0.4276 0.5496 0.7698 -0.1644 0.1527  -0.1475 394 LEU B CA  
7199  C C   . LEU B  394 ? 0.4102 0.5246 0.7275 -0.1733 0.1531  -0.1387 394 LEU B C   
7200  O O   . LEU B  394 ? 0.4524 0.5478 0.7405 -0.1752 0.1515  -0.1285 394 LEU B O   
7201  C CB  . LEU B  394 ? 0.3118 0.4396 0.6796 -0.1546 0.1383  -0.1416 394 LEU B CB  
7202  C CG  . LEU B  394 ? 0.3016 0.4322 0.6925 -0.1438 0.1345  -0.1468 394 LEU B CG  
7203  C CD1 . LEU B  394 ? 0.6092 0.7487 1.0281 -0.1356 0.1207  -0.1421 394 LEU B CD1 
7204  C CD2 . LEU B  394 ? 0.2968 0.4079 0.6664 -0.1406 0.1331  -0.1398 394 LEU B CD2 
7205  N N   . ARG B  395 ? 0.3425 0.4716 0.6719 -0.1785 0.1552  -0.1431 395 ARG B N   
7206  C CA  . ARG B  395 ? 0.3520 0.4752 0.6601 -0.1873 0.1561  -0.1362 395 ARG B CA  
7207  C C   . ARG B  395 ? 0.3688 0.4787 0.6447 -0.1959 0.1680  -0.1380 395 ARG B C   
7208  O O   . ARG B  395 ? 0.3725 0.4635 0.6192 -0.1984 0.1660  -0.1276 395 ARG B O   
7209  C CB  . ARG B  395 ? 0.3560 0.4992 0.6858 -0.1913 0.1566  -0.1419 395 ARG B CB  
7210  C CG  . ARG B  395 ? 0.3676 0.5060 0.6773 -0.2009 0.1590  -0.1368 395 ARG B CG  
7211  C CD  . ARG B  395 ? 0.5650 0.7131 0.8735 -0.2101 0.1728  -0.1490 395 ARG B CD  
7212  N NE  . ARG B  395 ? 0.5740 0.7463 0.9156 -0.2098 0.1727  -0.1584 395 ARG B NE  
7213  C CZ  . ARG B  395 ? 0.5914 0.7779 0.9429 -0.2153 0.1839  -0.1722 395 ARG B CZ  
7214  N NH1 . ARG B  395 ? 0.6130 0.7920 0.9428 -0.2223 0.1963  -0.1782 395 ARG B NH1 
7215  N NH2 . ARG B  395 ? 0.5810 0.7895 0.9641 -0.2140 0.1823  -0.1801 395 ARG B NH2 
7216  N N   . ASP B  396 ? 0.3799 0.4995 0.6609 -0.2003 0.1799  -0.1515 396 ASP B N   
7217  C CA  . ASP B  396 ? 0.4714 0.5797 0.7216 -0.2100 0.1914  -0.1538 396 ASP B CA  
7218  C C   . ASP B  396 ? 0.4219 0.5079 0.6449 -0.2075 0.1903  -0.1461 396 ASP B C   
7219  O O   . ASP B  396 ? 0.4112 0.4802 0.6020 -0.2137 0.1936  -0.1401 396 ASP B O   
7220  C CB  . ASP B  396 ? 0.6807 0.8040 0.9418 -0.2151 0.2041  -0.1703 396 ASP B CB  
7221  C CG  . ASP B  396 ? 0.7598 0.9017 1.0380 -0.2209 0.2075  -0.1772 396 ASP B CG  
7222  O OD1 . ASP B  396 ? 0.7782 0.9165 1.0477 -0.2250 0.2035  -0.1689 396 ASP B OD1 
7223  O OD2 . ASP B  396 ? 0.7909 0.9511 1.0916 -0.2213 0.2140  -0.1913 396 ASP B OD2 
7224  N N   . ALA B  397 ? 0.4851 0.5711 0.7223 -0.1978 0.1846  -0.1459 397 ALA B N   
7225  C CA  . ALA B  397 ? 0.4507 0.5180 0.6676 -0.1939 0.1828  -0.1398 397 ALA B CA  
7226  C C   . ALA B  397 ? 0.4228 0.4729 0.6207 -0.1915 0.1724  -0.1238 397 ALA B C   
7227  O O   . ALA B  397 ? 0.4366 0.4679 0.6052 -0.1932 0.1734  -0.1175 397 ALA B O   
7228  C CB  . ALA B  397 ? 0.3657 0.4396 0.6069 -0.1841 0.1795  -0.1451 397 ALA B CB  
7229  N N   . MET B  398 ? 0.3626 0.4191 0.5765 -0.1875 0.1620  -0.1175 398 MET B N   
7230  C CA  . MET B  398 ? 0.3587 0.4001 0.5540 -0.1861 0.1523  -0.1032 398 MET B CA  
7231  C C   . MET B  398 ? 0.3848 0.4153 0.5518 -0.1952 0.1575  -0.0996 398 MET B C   
7232  O O   . MET B  398 ? 0.3795 0.3906 0.5197 -0.1948 0.1543  -0.0903 398 MET B O   
7233  C CB  . MET B  398 ? 0.3448 0.3968 0.5629 -0.1815 0.1408  -0.0981 398 MET B CB  
7234  C CG  . MET B  398 ? 0.3409 0.3792 0.5416 -0.1803 0.1306  -0.0842 398 MET B CG  
7235  S SD  . MET B  398 ? 0.4405 0.4649 0.6359 -0.1699 0.1195  -0.0745 398 MET B SD  
7236  C CE  . MET B  398 ? 0.7982 0.7997 0.9569 -0.1717 0.1258  -0.0716 398 MET B CE  
7237  N N   . SER B  399 ? 0.3875 0.4303 0.5608 -0.2032 0.1652  -0.1074 399 SER B N   
7238  C CA  . SER B  399 ? 0.4166 0.4493 0.5634 -0.2126 0.1717  -0.1058 399 SER B CA  
7239  C C   . SER B  399 ? 0.4208 0.4361 0.5388 -0.2152 0.1786  -0.1059 399 SER B C   
7240  O O   . SER B  399 ? 0.4303 0.4275 0.5200 -0.2181 0.1780  -0.0983 399 SER B O   
7241  C CB  . SER B  399 ? 0.5176 0.5677 0.6771 -0.2211 0.1805  -0.1161 399 SER B CB  
7242  O OG  . SER B  399 ? 0.5382 0.5784 0.6713 -0.2310 0.1897  -0.1175 399 SER B OG  
7243  N N   . ALA B  400 ? 0.4194 0.4404 0.5450 -0.2139 0.1850  -0.1148 400 ALA B N   
7244  C CA  . ALA B  400 ? 0.4813 0.4868 0.5806 -0.2165 0.1913  -0.1154 400 ALA B CA  
7245  C C   . ALA B  400 ? 0.4490 0.4346 0.5310 -0.2089 0.1823  -0.1039 400 ALA B C   
7246  O O   . ALA B  400 ? 0.4462 0.4139 0.4990 -0.2118 0.1845  -0.0996 400 ALA B O   
7247  C CB  . ALA B  400 ? 0.6189 0.6364 0.7321 -0.2170 0.2000  -0.1286 400 ALA B CB  
7248  N N   . VAL B  401 ? 0.5129 0.5018 0.6129 -0.1993 0.1720  -0.0989 401 VAL B N   
7249  C CA  . VAL B  401 ? 0.4793 0.4509 0.5650 -0.1917 0.1633  -0.0887 401 VAL B CA  
7250  C C   . VAL B  401 ? 0.4763 0.4328 0.5382 -0.1936 0.1584  -0.0783 401 VAL B C   
7251  O O   . VAL B  401 ? 0.4279 0.3664 0.4629 -0.1940 0.1589  -0.0735 401 VAL B O   
7252  C CB  . VAL B  401 ? 0.3720 0.3504 0.4818 -0.1816 0.1524  -0.0849 401 VAL B CB  
7253  C CG1 . VAL B  401 ? 0.3651 0.3254 0.4579 -0.1744 0.1436  -0.0743 401 VAL B CG1 
7254  C CG2 . VAL B  401 ? 0.3645 0.3574 0.4999 -0.1785 0.1564  -0.0955 401 VAL B CG2 
7255  N N   . VAL B  402 ? 0.3981 0.3624 0.4705 -0.1950 0.1539  -0.0754 402 VAL B N   
7256  C CA  . VAL B  402 ? 0.4045 0.3557 0.4570 -0.1964 0.1492  -0.0665 402 VAL B CA  
7257  C C   . VAL B  402 ? 0.4278 0.3674 0.4536 -0.2050 0.1579  -0.0681 402 VAL B C   
7258  O O   . VAL B  402 ? 0.4348 0.3564 0.4369 -0.2038 0.1547  -0.0609 402 VAL B O   
7259  C CB  . VAL B  402 ? 0.3984 0.3608 0.4667 -0.1977 0.1440  -0.0644 402 VAL B CB  
7260  C CG1 . VAL B  402 ? 0.4077 0.3571 0.4555 -0.2003 0.1412  -0.0573 402 VAL B CG1 
7261  C CG2 . VAL B  402 ? 0.3774 0.3462 0.4655 -0.1890 0.1331  -0.0599 402 VAL B CG2 
7262  N N   . GLY B  403 ? 0.4404 0.3903 0.4705 -0.2135 0.1686  -0.0777 403 GLY B N   
7263  C CA  . GLY B  403 ? 0.5228 0.4624 0.5279 -0.2227 0.1772  -0.0797 403 GLY B CA  
7264  C C   . GLY B  403 ? 0.5417 0.4643 0.5224 -0.2221 0.1798  -0.0782 403 GLY B C   
7265  O O   . GLY B  403 ? 0.4890 0.3939 0.4434 -0.2246 0.1791  -0.0724 403 GLY B O   
7266  N N   . ASP B  404 ? 0.7525 0.6806 0.7425 -0.2189 0.1827  -0.0839 404 ASP B N   
7267  C CA  . ASP B  404 ? 0.7392 0.6528 0.7078 -0.2186 0.1854  -0.0835 404 ASP B CA  
7268  C C   . ASP B  404 ? 0.7253 0.6203 0.6779 -0.2106 0.1749  -0.0717 404 ASP B C   
7269  O O   . ASP B  404 ? 0.7756 0.6531 0.7014 -0.2127 0.1753  -0.0675 404 ASP B O   
7270  C CB  . ASP B  404 ? 0.6224 0.5467 0.6083 -0.2152 0.1892  -0.0918 404 ASP B CB  
7271  C CG  . ASP B  404 ? 0.6375 0.5810 0.6395 -0.2229 0.2005  -0.1052 404 ASP B CG  
7272  O OD1 . ASP B  404 ? 0.6654 0.6125 0.6618 -0.2318 0.2061  -0.1080 404 ASP B OD1 
7273  O OD2 . ASP B  404 ? 0.6305 0.5861 0.6518 -0.2199 0.2037  -0.1137 404 ASP B OD2 
7274  N N   . HIS B  405 ? 0.5453 0.4446 0.5149 -0.2014 0.1650  -0.0665 405 HIS B N   
7275  C CA  . HIS B  405 ? 0.5005 0.3846 0.4579 -0.1928 0.1545  -0.0561 405 HIS B CA  
7276  C C   . HIS B  405 ? 0.4690 0.3400 0.4064 -0.1952 0.1514  -0.0492 405 HIS B C   
7277  O O   . HIS B  405 ? 0.4626 0.3168 0.3777 -0.1936 0.1493  -0.0444 405 HIS B O   
7278  C CB  . HIS B  405 ? 0.5160 0.4089 0.4965 -0.1835 0.1445  -0.0522 405 HIS B CB  
7279  C CG  . HIS B  405 ? 0.4992 0.3789 0.4694 -0.1746 0.1337  -0.0423 405 HIS B CG  
7280  N ND1 . HIS B  405 ? 0.5112 0.3746 0.4596 -0.1719 0.1328  -0.0390 405 HIS B ND1 
7281  C CD2 . HIS B  405 ? 0.4433 0.3250 0.4231 -0.1679 0.1231  -0.0356 405 HIS B CD2 
7282  C CE1 . HIS B  405 ? 0.4831 0.3399 0.4294 -0.1635 0.1224  -0.0312 405 HIS B CE1 
7283  N NE2 . HIS B  405 ? 0.4407 0.3083 0.4054 -0.1611 0.1166  -0.0291 405 HIS B NE2 
7284  N N   . ASN B  406 ? 0.4535 0.3324 0.3997 -0.1990 0.1508  -0.0490 406 ASN B N   
7285  C CA  . ASN B  406 ? 0.4634 0.3305 0.3934 -0.2006 0.1472  -0.0427 406 ASN B CA  
7286  C C   . ASN B  406 ? 0.4903 0.3476 0.3982 -0.2106 0.1551  -0.0446 406 ASN B C   
7287  O O   . ASN B  406 ? 0.5005 0.3425 0.3896 -0.2106 0.1519  -0.0388 406 ASN B O   
7288  C CB  . ASN B  406 ? 0.4524 0.3301 0.3996 -0.1998 0.1421  -0.0408 406 ASN B CB  
7289  C CG  . ASN B  406 ? 0.5059 0.3893 0.4702 -0.1897 0.1322  -0.0366 406 ASN B CG  
7290  O OD1 . ASN B  406 ? 0.4850 0.3582 0.4412 -0.1826 0.1242  -0.0298 406 ASN B OD1 
7291  N ND2 . ASN B  406 ? 0.4158 0.3163 0.4046 -0.1891 0.1323  -0.0408 406 ASN B ND2 
7292  N N   . VAL B  407 ? 0.5123 0.3787 0.4232 -0.2194 0.1654  -0.0529 407 VAL B N   
7293  C CA  . VAL B  407 ? 0.5847 0.4425 0.4748 -0.2299 0.1731  -0.0548 407 VAL B CA  
7294  C C   . VAL B  407 ? 0.5958 0.4495 0.4723 -0.2352 0.1815  -0.0602 407 VAL B C   
7295  O O   . VAL B  407 ? 0.6090 0.4450 0.4608 -0.2366 0.1811  -0.0561 407 VAL B O   
7296  C CB  . VAL B  407 ? 0.5354 0.4053 0.4353 -0.2387 0.1786  -0.0594 407 VAL B CB  
7297  C CG1 . VAL B  407 ? 0.5641 0.4264 0.4432 -0.2505 0.1877  -0.0624 407 VAL B CG1 
7298  C CG2 . VAL B  407 ? 0.5281 0.3960 0.4322 -0.2355 0.1707  -0.0530 407 VAL B CG2 
7299  N N   . VAL B  408 ? 0.5390 0.4092 0.4319 -0.2382 0.1889  -0.0696 408 VAL B N   
7300  C CA  . VAL B  408 ? 0.5576 0.4260 0.4374 -0.2461 0.1987  -0.0763 408 VAL B CA  
7301  C C   . VAL B  408 ? 0.6087 0.4600 0.4680 -0.2420 0.1960  -0.0722 408 VAL B C   
7302  O O   . VAL B  408 ? 0.5850 0.4216 0.4187 -0.2481 0.1986  -0.0700 408 VAL B O   
7303  C CB  . VAL B  408 ? 0.5584 0.4488 0.4612 -0.2493 0.2072  -0.0885 408 VAL B CB  
7304  C CG1 . VAL B  408 ? 0.5717 0.4590 0.4585 -0.2572 0.2167  -0.0951 408 VAL B CG1 
7305  C CG2 . VAL B  408 ? 0.5537 0.4607 0.4733 -0.2557 0.2116  -0.0938 408 VAL B CG2 
7306  N N   . CYS B  409 ? 0.6893 0.5421 0.5598 -0.2319 0.1903  -0.0707 409 CYS B N   
7307  C CA  . CYS B  409 ? 0.6821 0.5190 0.5345 -0.2273 0.1872  -0.0667 409 CYS B CA  
7308  C C   . CYS B  409 ? 0.6589 0.4740 0.4868 -0.2244 0.1792  -0.0560 409 CYS B C   
7309  O O   . CYS B  409 ? 0.6383 0.4387 0.4435 -0.2264 0.1799  -0.0539 409 CYS B O   
7310  C CB  . CYS B  409 ? 0.6386 0.4829 0.5104 -0.2171 0.1828  -0.0677 409 CYS B CB  
7311  S SG  . CYS B  409 ? 1.1328 1.0022 1.0337 -0.2207 0.1928  -0.0816 409 CYS B SG  
7312  N N   . PRO B  410 ? 0.6576 0.4713 0.4910 -0.2195 0.1714  -0.0494 410 PRO B N   
7313  C CA  . PRO B  410 ? 0.6540 0.4491 0.4658 -0.2188 0.1657  -0.0411 410 PRO B CA  
7314  C C   . PRO B  410 ? 0.6667 0.4524 0.4564 -0.2306 0.1728  -0.0423 410 PRO B C   
7315  O O   . PRO B  410 ? 0.6691 0.4374 0.4361 -0.2310 0.1705  -0.0376 410 PRO B O   
7316  C CB  . PRO B  410 ? 0.5456 0.3468 0.3716 -0.2154 0.1599  -0.0375 410 PRO B CB  
7317  C CG  . PRO B  410 ? 0.5195 0.3364 0.3714 -0.2084 0.1570  -0.0398 410 PRO B CG  
7318  C CD  . PRO B  410 ? 0.5247 0.3519 0.3841 -0.2123 0.1656  -0.0485 410 PRO B CD  
7319  N N   . VAL B  411 ? 0.5969 0.3944 0.3939 -0.2402 0.1809  -0.0484 411 VAL B N   
7320  C CA  . VAL B  411 ? 0.6261 0.4167 0.4041 -0.2524 0.1880  -0.0497 411 VAL B CA  
7321  C C   . VAL B  411 ? 0.6430 0.4257 0.4027 -0.2570 0.1929  -0.0521 411 VAL B C   
7322  O O   . VAL B  411 ? 0.6655 0.4311 0.4007 -0.2612 0.1922  -0.0473 411 VAL B O   
7323  C CB  . VAL B  411 ? 0.6294 0.4381 0.4223 -0.2616 0.1968  -0.0578 411 VAL B CB  
7324  C CG1 . VAL B  411 ? 0.6598 0.4642 0.4340 -0.2751 0.2062  -0.0614 411 VAL B CG1 
7325  C CG2 . VAL B  411 ? 0.6212 0.4337 0.4254 -0.2600 0.1924  -0.0544 411 VAL B CG2 
7326  N N   . ALA B  412 ? 0.6749 0.4704 0.4474 -0.2560 0.1977  -0.0596 412 ALA B N   
7327  C CA  . ALA B  412 ? 0.7194 0.5094 0.4766 -0.2601 0.2026  -0.0630 412 ALA B CA  
7328  C C   . ALA B  412 ? 0.7613 0.5304 0.4987 -0.2530 0.1939  -0.0541 412 ALA B C   
7329  O O   . ALA B  412 ? 0.8315 0.5869 0.5445 -0.2589 0.1955  -0.0520 412 ALA B O   
7330  C CB  . ALA B  412 ? 0.7209 0.5293 0.4995 -0.2585 0.2083  -0.0729 412 ALA B CB  
7331  N N   . GLN B  413 ? 0.6266 0.3936 0.3743 -0.2405 0.1844  -0.0489 413 GLN B N   
7332  C CA  . GLN B  413 ? 0.6431 0.3918 0.3742 -0.2330 0.1757  -0.0409 413 GLN B CA  
7333  C C   . GLN B  413 ? 0.6719 0.4023 0.3800 -0.2364 0.1719  -0.0332 413 GLN B C   
7334  O O   . GLN B  413 ? 0.6976 0.4128 0.3836 -0.2383 0.1705  -0.0298 413 GLN B O   
7335  C CB  . GLN B  413 ? 0.8286 0.5795 0.5757 -0.2191 0.1660  -0.0367 413 GLN B CB  
7336  C CG  . GLN B  413 ? 0.9418 0.6739 0.6716 -0.2116 0.1568  -0.0286 413 GLN B CG  
7337  C CD  . GLN B  413 ? 1.0073 0.7426 0.7522 -0.1981 0.1481  -0.0256 413 GLN B CD  
7338  O OE1 . GLN B  413 ? 0.9954 0.7319 0.7498 -0.1911 0.1405  -0.0207 413 GLN B OE1 
7339  N NE2 . GLN B  413 ? 1.0346 0.7717 0.7819 -0.1949 0.1492  -0.0287 413 GLN B NE2 
7340  N N   . LEU B  414 ? 0.7023 0.4342 0.4157 -0.2376 0.1701  -0.0305 414 LEU B N   
7341  C CA  . LEU B  414 ? 0.6739 0.3893 0.3673 -0.2418 0.1675  -0.0239 414 LEU B CA  
7342  C C   . LEU B  414 ? 0.7585 0.4675 0.4311 -0.2548 0.1756  -0.0261 414 LEU B C   
7343  O O   . LEU B  414 ? 0.7880 0.4794 0.4383 -0.2564 0.1725  -0.0203 414 LEU B O   
7344  C CB  . LEU B  414 ? 0.9136 0.6338 0.6174 -0.2431 0.1665  -0.0225 414 LEU B CB  
7345  C CG  . LEU B  414 ? 0.6931 0.3963 0.3783 -0.2471 0.1636  -0.0156 414 LEU B CG  
7346  C CD1 . LEU B  414 ? 0.6864 0.3761 0.3661 -0.2360 0.1528  -0.0081 414 LEU B CD1 
7347  C CD2 . LEU B  414 ? 0.6930 0.4028 0.3882 -0.2514 0.1655  -0.0162 414 LEU B CD2 
7348  N N   . ALA B  415 ? 0.7089 0.4329 0.3894 -0.2640 0.1859  -0.0346 415 ALA B N   
7349  C CA  . ALA B  415 ? 0.7384 0.4595 0.4009 -0.2773 0.1947  -0.0378 415 ALA B CA  
7350  C C   . ALA B  415 ? 0.7526 0.4611 0.3955 -0.2768 0.1930  -0.0355 415 ALA B C   
7351  O O   . ALA B  415 ? 0.7925 0.4836 0.4117 -0.2809 0.1906  -0.0291 415 ALA B O   
7352  C CB  . ALA B  415 ? 0.7347 0.4773 0.4133 -0.2849 0.2056  -0.0490 415 ALA B CB  
7353  N N   . GLY B  416 ? 0.8618 0.5788 0.5149 -0.2716 0.1940  -0.0406 416 GLY B N   
7354  C CA  . GLY B  416 ? 0.9040 0.6102 0.5403 -0.2703 0.1921  -0.0390 416 GLY B CA  
7355  C C   . GLY B  416 ? 0.9345 0.6191 0.5538 -0.2624 0.1807  -0.0281 416 GLY B C   
7356  O O   . GLY B  416 ? 1.0081 0.6791 0.6049 -0.2660 0.1796  -0.0247 416 GLY B O   
7357  N N   . ARG B  417 ? 0.8132 0.4954 0.4438 -0.2517 0.1720  -0.0230 417 ARG B N   
7358  C CA  . ARG B  417 ? 0.8475 0.5113 0.4654 -0.2432 0.1609  -0.0136 417 ARG B CA  
7359  C C   . ARG B  417 ? 0.8377 0.4861 0.4346 -0.2507 0.1601  -0.0073 417 ARG B C   
7360  O O   . ARG B  417 ? 0.8340 0.4653 0.4115 -0.2493 0.1543  -0.0008 417 ARG B O   
7361  C CB  . ARG B  417 ? 1.1908 0.8580 0.8274 -0.2303 0.1522  -0.0103 417 ARG B CB  
7362  C CG  . ARG B  417 ? 1.2449 0.9260 0.9033 -0.2212 0.1511  -0.0148 417 ARG B CG  
7363  C CD  . ARG B  417 ? 1.3273 1.0024 0.9776 -0.2167 0.1490  -0.0150 417 ARG B CD  
7364  N NE  . ARG B  417 ? 1.4361 1.0921 1.0675 -0.2123 0.1403  -0.0071 417 ARG B NE  
7365  C CZ  . ARG B  417 ? 1.5435 1.1863 1.1516 -0.2180 0.1412  -0.0051 417 ARG B CZ  
7366  N NH1 . ARG B  417 ? 1.5900 1.2373 1.1905 -0.2287 0.1507  -0.0109 417 ARG B NH1 
7367  N NH2 . ARG B  417 ? 1.5700 1.1959 1.1630 -0.2130 0.1324  0.0024  417 ARG B NH2 
7368  N N   . LEU B  418 ? 0.9645 0.6190 0.5656 -0.2587 0.1656  -0.0091 418 LEU B N   
7369  C CA  . LEU B  418 ? 1.0147 0.6551 0.5972 -0.2664 0.1653  -0.0031 418 LEU B CA  
7370  C C   . LEU B  418 ? 1.1007 0.7343 0.6606 -0.2777 0.1712  -0.0037 418 LEU B C   
7371  O O   . LEU B  418 ? 1.1902 0.8061 0.7286 -0.2806 0.1674  0.0037  418 LEU B O   
7372  C CB  . LEU B  418 ? 0.7989 0.4481 0.3921 -0.2726 0.1702  -0.0054 418 LEU B CB  
7373  C CG  . LEU B  418 ? 0.7799 0.4306 0.3893 -0.2633 0.1632  -0.0021 418 LEU B CG  
7374  C CD1 . LEU B  418 ? 0.7859 0.4421 0.4007 -0.2716 0.1684  -0.0036 418 LEU B CD1 
7375  C CD2 . LEU B  418 ? 0.7822 0.4145 0.3808 -0.2548 0.1524  0.0070  418 LEU B CD2 
7376  N N   . ALA B  419 ? 1.0150 0.6632 0.5802 -0.2842 0.1805  -0.0125 419 ALA B N   
7377  C CA  . ALA B  419 ? 0.9921 0.6367 0.5370 -0.2952 0.1868  -0.0140 419 ALA B CA  
7378  C C   . ALA B  419 ? 1.0342 0.6638 0.5622 -0.2896 0.1795  -0.0084 419 ALA B C   
7379  O O   . ALA B  419 ? 1.0923 0.7078 0.5964 -0.2961 0.1786  -0.0029 419 ALA B O   
7380  C CB  . ALA B  419 ? 0.8705 0.5361 0.4279 -0.3020 0.1980  -0.0257 419 ALA B CB  
7381  N N   . ALA B  420 ? 1.0933 0.7259 0.6336 -0.2776 0.1741  -0.0095 420 ALA B N   
7382  C CA  . ALA B  420 ? 1.1357 0.7552 0.6620 -0.2713 0.1668  -0.0048 420 ALA B CA  
7383  C C   . ALA B  420 ? 1.1701 0.7681 0.6799 -0.2669 0.1563  0.0065  420 ALA B C   
7384  O O   . ALA B  420 ? 1.1812 0.7658 0.6733 -0.2652 0.1510  0.0115  420 ALA B O   
7385  C CB  . ALA B  420 ? 1.1182 0.7458 0.6633 -0.2590 0.1631  -0.0083 420 ALA B CB  
7386  N N   . GLN B  421 ? 1.2239 0.8194 0.7406 -0.2650 0.1533  0.0102  421 GLN B N   
7387  C CA  . GLN B  421 ? 1.2927 0.8690 0.7961 -0.2613 0.1442  0.0202  421 GLN B CA  
7388  C C   . GLN B  421 ? 1.3550 0.9198 0.8379 -0.2737 0.1473  0.0252  421 GLN B C   
7389  O O   . GLN B  421 ? 1.3652 0.9151 0.8396 -0.2716 0.1406  0.0332  421 GLN B O   
7390  C CB  . GLN B  421 ? 1.2851 0.8626 0.8069 -0.2495 0.1366  0.0226  421 GLN B CB  
7391  C CG  . GLN B  421 ? 1.2690 0.8411 0.7939 -0.2359 0.1267  0.0255  421 GLN B CG  
7392  C CD  . GLN B  421 ? 1.2546 0.8419 0.7970 -0.2296 0.1285  0.0184  421 GLN B CD  
7393  O OE1 . GLN B  421 ? 1.2558 0.8575 0.8068 -0.2358 0.1375  0.0111  421 GLN B OE1 
7394  N NE2 . GLN B  421 ? 1.2458 0.8306 0.7944 -0.2172 0.1200  0.0205  421 GLN B NE2 
7395  N N   . GLY B  422 ? 1.4990 1.0715 0.9749 -0.2867 0.1577  0.0201  422 GLY B N   
7396  C CA  . GLY B  422 ? 1.5196 1.0819 0.9750 -0.2994 0.1614  0.0246  422 GLY B CA  
7397  C C   . GLY B  422 ? 1.4875 1.0530 0.9517 -0.3040 0.1648  0.0245  422 GLY B C   
7398  O O   . GLY B  422 ? 1.5691 1.1200 1.0212 -0.3071 0.1615  0.0321  422 GLY B O   
7399  N N   . ALA B  423 ? 1.0727 0.6576 0.5590 -0.3040 0.1711  0.0159  423 ALA B N   
7400  C CA  . ALA B  423 ? 1.0355 0.6263 0.5297 -0.3109 0.1763  0.0142  423 ALA B CA  
7401  C C   . ALA B  423 ? 1.0101 0.6165 0.5053 -0.3242 0.1892  0.0054  423 ALA B C   
7402  O O   . ALA B  423 ? 0.9688 0.5876 0.4694 -0.3247 0.1940  -0.0018 423 ALA B O   
7403  C CB  . ALA B  423 ? 1.1470 0.7480 0.6671 -0.3002 0.1727  0.0118  423 ALA B CB  
7404  N N   . ARG B  424 ? 1.0916 0.6976 0.5819 -0.3353 0.1949  0.0058  424 ARG B N   
7405  C CA  . ARG B  424 ? 1.1547 0.7776 0.6493 -0.3480 0.2075  -0.0033 424 ARG B CA  
7406  C C   . ARG B  424 ? 1.0710 0.7132 0.5945 -0.3439 0.2104  -0.0109 424 ARG B C   
7407  O O   . ARG B  424 ? 1.1045 0.7439 0.6368 -0.3399 0.2064  -0.0076 424 ARG B O   
7408  C CB  . ARG B  424 ? 1.6198 1.2335 1.0957 -0.3622 0.2124  0.0007  424 ARG B CB  
7409  C CG  . ARG B  424 ? 1.7145 1.3461 1.1947 -0.3761 0.2257  -0.0090 424 ARG B CG  
7410  C CD  . ARG B  424 ? 1.8045 1.4248 1.2615 -0.3910 0.2304  -0.0041 424 ARG B CD  
7411  N NE  . ARG B  424 ? 1.8641 1.4652 1.2939 -0.3927 0.2256  0.0046  424 ARG B NE  
7412  C CZ  . ARG B  424 ? 1.8810 1.4855 1.2996 -0.3968 0.2291  0.0017  424 ARG B CZ  
7413  N NH1 . ARG B  424 ? 1.8514 1.4781 1.2842 -0.3997 0.2378  -0.0102 424 ARG B NH1 
7414  N NH2 . ARG B  424 ? 1.9173 1.5034 1.3108 -0.3980 0.2237  0.0106  424 ARG B NH2 
7415  N N   . VAL B  425 ? 0.9910 0.6532 0.5298 -0.3446 0.2173  -0.0213 425 VAL B N   
7416  C CA  . VAL B  425 ? 0.9561 0.6370 0.5239 -0.3387 0.2187  -0.0282 425 VAL B CA  
7417  C C   . VAL B  425 ? 0.9629 0.6655 0.5423 -0.3493 0.2312  -0.0398 425 VAL B C   
7418  O O   . VAL B  425 ? 1.0054 0.7147 0.5792 -0.3552 0.2376  -0.0455 425 VAL B O   
7419  C CB  . VAL B  425 ? 1.0381 0.7240 0.6201 -0.3248 0.2128  -0.0298 425 VAL B CB  
7420  C CG1 . VAL B  425 ? 1.0213 0.7280 0.6338 -0.3194 0.2148  -0.0372 425 VAL B CG1 
7421  C CG2 . VAL B  425 ? 1.0267 0.6930 0.5997 -0.3132 0.2002  -0.0192 425 VAL B CG2 
7422  N N   . TYR B  426 ? 1.1153 0.8298 0.7116 -0.3518 0.2347  -0.0436 426 TYR B N   
7423  C CA  . TYR B  426 ? 1.1673 0.9045 0.7783 -0.3608 0.2463  -0.0555 426 TYR B CA  
7424  C C   . TYR B  426 ? 1.1449 0.9013 0.7877 -0.3518 0.2454  -0.0619 426 TYR B C   
7425  O O   . TYR B  426 ? 1.1755 0.9302 0.8287 -0.3458 0.2397  -0.0578 426 TYR B O   
7426  C CB  . TYR B  426 ? 1.2499 0.9865 0.8524 -0.3746 0.2530  -0.0556 426 TYR B CB  
7427  C CG  . TYR B  426 ? 1.3186 1.0371 0.8897 -0.3849 0.2546  -0.0493 426 TYR B CG  
7428  C CD1 . TYR B  426 ? 1.3426 1.0372 0.8950 -0.3826 0.2461  -0.0370 426 TYR B CD1 
7429  C CD2 . TYR B  426 ? 1.3465 1.0724 0.9072 -0.3970 0.2643  -0.0556 426 TYR B CD2 
7430  C CE1 . TYR B  426 ? 1.3718 1.0495 0.8957 -0.3919 0.2470  -0.0304 426 TYR B CE1 
7431  C CE2 . TYR B  426 ? 1.3804 1.0898 0.9117 -0.4067 0.2654  -0.0491 426 TYR B CE2 
7432  C CZ  . TYR B  426 ? 1.3822 1.0671 0.8950 -0.4040 0.2565  -0.0362 426 TYR B CZ  
7433  O OH  . TYR B  426 ? 1.3943 1.0624 0.8781 -0.4135 0.2571  -0.0291 426 TYR B OH  
7434  N N   . ALA B  427 ? 1.0102 0.7847 0.6687 -0.3507 0.2508  -0.0718 427 ALA B N   
7435  C CA  . ALA B  427 ? 0.9009 0.6941 0.5903 -0.3417 0.2498  -0.0779 427 ALA B CA  
7436  C C   . ALA B  427 ? 0.8905 0.7071 0.5996 -0.3501 0.2600  -0.0892 427 ALA B C   
7437  O O   . ALA B  427 ? 0.8281 0.6514 0.5299 -0.3619 0.2696  -0.0959 427 ALA B O   
7438  C CB  . ALA B  427 ? 0.7883 0.5861 0.4852 -0.3331 0.2480  -0.0812 427 ALA B CB  
7439  N N   . TYR B  428 ? 0.7834 0.6128 0.5175 -0.3440 0.2576  -0.0913 428 TYR B N   
7440  C CA  . TYR B  428 ? 0.7818 0.6344 0.5370 -0.3510 0.2664  -0.1021 428 TYR B CA  
7441  C C   . TYR B  428 ? 0.7483 0.6191 0.5361 -0.3406 0.2633  -0.1067 428 TYR B C   
7442  O O   . TYR B  428 ? 0.7956 0.6595 0.5891 -0.3296 0.2533  -0.0991 428 TYR B O   
7443  C CB  . TYR B  428 ? 0.9449 0.7932 0.6936 -0.3595 0.2680  -0.0988 428 TYR B CB  
7444  C CG  . TYR B  428 ? 0.9069 0.7496 0.6646 -0.3507 0.2584  -0.0909 428 TYR B CG  
7445  C CD1 . TYR B  428 ? 0.8878 0.7495 0.6742 -0.3467 0.2580  -0.0958 428 TYR B CD1 
7446  C CD2 . TYR B  428 ? 0.8874 0.7065 0.6255 -0.3464 0.2496  -0.0788 428 TYR B CD2 
7447  C CE1 . TYR B  428 ? 0.8758 0.7331 0.6701 -0.3391 0.2491  -0.0888 428 TYR B CE1 
7448  C CE2 . TYR B  428 ? 0.8710 0.6860 0.6178 -0.3386 0.2411  -0.0725 428 TYR B CE2 
7449  C CZ  . TYR B  428 ? 0.8704 0.7045 0.6447 -0.3352 0.2410  -0.0775 428 TYR B CZ  
7450  O OH  . TYR B  428 ? 0.8548 0.6855 0.6375 -0.3280 0.2325  -0.0713 428 TYR B OH  
7451  N N   . ILE B  429 ? 0.7422 0.6370 0.5524 -0.3440 0.2714  -0.1191 429 ILE B N   
7452  C CA  . ILE B  429 ? 0.7255 0.6392 0.5688 -0.3351 0.2686  -0.1237 429 ILE B CA  
7453  C C   . ILE B  429 ? 0.7687 0.7014 0.6297 -0.3430 0.2754  -0.1317 429 ILE B C   
7454  O O   . ILE B  429 ? 0.8210 0.7639 0.6805 -0.3538 0.2857  -0.1409 429 ILE B O   
7455  C CB  . ILE B  429 ? 0.7622 0.6891 0.6228 -0.3285 0.2703  -0.1318 429 ILE B CB  
7456  C CG1 . ILE B  429 ? 0.7321 0.6792 0.6285 -0.3197 0.2670  -0.1363 429 ILE B CG1 
7457  C CG2 . ILE B  429 ? 0.7869 0.7254 0.6453 -0.3390 0.2822  -0.1438 429 ILE B CG2 
7458  C CD1 . ILE B  429 ? 0.7160 0.6698 0.6285 -0.3092 0.2642  -0.1397 429 ILE B CD1 
7459  N N   . PHE B  430 ? 0.9419 0.8797 0.8195 -0.3378 0.2694  -0.1283 430 PHE B N   
7460  C CA  . PHE B  430 ? 0.9816 0.9337 0.8724 -0.3456 0.2744  -0.1335 430 PHE B CA  
7461  C C   . PHE B  430 ? 1.0118 0.9921 0.9389 -0.3419 0.2772  -0.1449 430 PHE B C   
7462  O O   . PHE B  430 ? 1.0310 1.0175 0.9785 -0.3311 0.2692  -0.1423 430 PHE B O   
7463  C CB  . PHE B  430 ? 0.9172 0.8573 0.8038 -0.3421 0.2656  -0.1227 430 PHE B CB  
7464  C CG  . PHE B  430 ? 0.8776 0.8271 0.7717 -0.3509 0.2697  -0.1257 430 PHE B CG  
7465  C CD1 . PHE B  430 ? 0.8626 0.8345 0.7879 -0.3484 0.2695  -0.1320 430 PHE B CD1 
7466  C CD2 . PHE B  430 ? 0.8765 0.8116 0.7468 -0.3614 0.2730  -0.1215 430 PHE B CD2 
7467  C CE1 . PHE B  430 ? 0.8865 0.8670 0.8188 -0.3564 0.2730  -0.1347 430 PHE B CE1 
7468  C CE2 . PHE B  430 ? 0.9132 0.8564 0.7903 -0.3696 0.2768  -0.1242 430 PHE B CE2 
7469  C CZ  . PHE B  430 ? 0.9200 0.8862 0.8282 -0.3672 0.2769  -0.1309 430 PHE B CZ  
7470  N N   . GLU B  431 ? 0.8892 0.8867 0.8248 -0.3508 0.2882  -0.1575 431 GLU B N   
7471  C CA  . GLU B  431 ? 0.8724 0.8969 0.8427 -0.3467 0.2914  -0.1699 431 GLU B CA  
7472  C C   . GLU B  431 ? 0.8393 0.8832 0.8347 -0.3493 0.2927  -0.1752 431 GLU B C   
7473  O O   . GLU B  431 ? 0.7890 0.8550 0.8164 -0.3439 0.2928  -0.1839 431 GLU B O   
7474  C CB  . GLU B  431 ? 1.0439 1.0792 1.0137 -0.3537 0.3026  -0.1827 431 GLU B CB  
7475  C CG  . GLU B  431 ? 1.0933 1.1102 1.0356 -0.3542 0.3030  -0.1787 431 GLU B CG  
7476  C CD  . GLU B  431 ? 1.0973 1.1166 1.0529 -0.3417 0.2979  -0.1797 431 GLU B CD  
7477  O OE1 . GLU B  431 ? 1.0809 1.0952 1.0457 -0.3303 0.2876  -0.1714 431 GLU B OE1 
7478  O OE2 . GLU B  431 ? 1.0990 1.1256 1.0560 -0.3436 0.3044  -0.1890 431 GLU B OE2 
7479  N N   . HIS B  432 ? 0.9633 0.9992 0.9452 -0.3574 0.2934  -0.1701 432 HIS B N   
7480  C CA  . HIS B  432 ? 0.9862 1.0413 0.9890 -0.3629 0.2971  -0.1769 432 HIS B CA  
7481  C C   . HIS B  432 ? 0.9249 0.9827 0.9446 -0.3555 0.2869  -0.1700 432 HIS B C   
7482  O O   . HIS B  432 ? 0.9108 0.9498 0.9134 -0.3540 0.2799  -0.1581 432 HIS B O   
7483  C CB  . HIS B  432 ? 1.0983 1.1484 1.0808 -0.3783 0.3062  -0.1787 432 HIS B CB  
7484  C CG  . HIS B  432 ? 1.1420 1.2085 1.1429 -0.3841 0.3089  -0.1836 432 HIS B CG  
7485  N ND1 . HIS B  432 ? 1.1514 1.2067 1.1419 -0.3879 0.3051  -0.1751 432 HIS B ND1 
7486  C CD2 . HIS B  432 ? 1.1486 1.2423 1.1789 -0.3865 0.3146  -0.1965 432 HIS B CD2 
7487  C CE1 . HIS B  432 ? 1.1485 1.2233 1.1605 -0.3928 0.3086  -0.1823 432 HIS B CE1 
7488  N NE2 . HIS B  432 ? 1.1508 1.2491 1.1873 -0.3919 0.3143  -0.1953 432 HIS B NE2 
7489  N N   . ARG B  433 ? 0.7501 0.8322 0.8041 -0.3511 0.2862  -0.1780 433 ARG B N   
7490  C CA  . ARG B  433 ? 0.7148 0.8034 0.7886 -0.3447 0.2767  -0.1729 433 ARG B CA  
7491  C C   . ARG B  433 ? 0.7798 0.8775 0.8583 -0.3549 0.2811  -0.1762 433 ARG B C   
7492  O O   . ARG B  433 ? 0.7848 0.9018 0.8781 -0.3619 0.2901  -0.1884 433 ARG B O   
7493  C CB  . ARG B  433 ? 0.6936 0.8038 0.8030 -0.3344 0.2726  -0.1795 433 ARG B CB  
7494  C CG  . ARG B  433 ? 0.6545 0.7785 0.7904 -0.3297 0.2646  -0.1777 433 ARG B CG  
7495  C CD  . ARG B  433 ? 0.6463 0.7907 0.8167 -0.3195 0.2606  -0.1844 433 ARG B CD  
7496  N NE  . ARG B  433 ? 0.6744 0.8343 0.8722 -0.3156 0.2527  -0.1834 433 ARG B NE  
7497  C CZ  . ARG B  433 ? 0.6896 0.8460 0.8963 -0.3056 0.2399  -0.1738 433 ARG B CZ  
7498  N NH1 . ARG B  433 ? 0.6740 0.8122 0.8653 -0.2981 0.2337  -0.1646 433 ARG B NH1 
7499  N NH2 . ARG B  433 ? 0.7127 0.8841 0.9439 -0.3035 0.2331  -0.1734 433 ARG B NH2 
7500  N N   . ALA B  434 ? 1.0653 1.1493 1.1315 -0.3559 0.2750  -0.1659 434 ALA B N   
7501  C CA  . ALA B  434 ? 1.1358 1.2267 1.2051 -0.3660 0.2789  -0.1685 434 ALA B CA  
7502  C C   . ALA B  434 ? 1.1918 1.3109 1.2988 -0.3635 0.2777  -0.1768 434 ALA B C   
7503  O O   . ALA B  434 ? 1.1782 1.3063 1.3070 -0.3522 0.2693  -0.1757 434 ALA B O   
7504  C CB  . ALA B  434 ? 0.9069 0.9777 0.9576 -0.3664 0.2717  -0.1560 434 ALA B CB  
7505  N N   . SER B  435 ? 1.1143 1.2469 1.2286 -0.3743 0.2858  -0.1851 435 SER B N   
7506  C CA  . SER B  435 ? 1.0816 1.2416 1.2310 -0.3737 0.2855  -0.1939 435 SER B CA  
7507  C C   . SER B  435 ? 1.1009 1.2595 1.2583 -0.3702 0.2749  -0.1853 435 SER B C   
7508  O O   . SER B  435 ? 1.0577 1.2362 1.2454 -0.3656 0.2697  -0.1888 435 SER B O   
7509  C CB  . SER B  435 ? 0.8759 1.0487 1.0269 -0.3875 0.2982  -0.2052 435 SER B CB  
7510  O OG  . SER B  435 ? 0.8608 1.0151 0.9836 -0.3976 0.3010  -0.1985 435 SER B OG  
7511  N N   . THR B  436 ? 1.2810 1.4157 1.4110 -0.3725 0.2714  -0.1741 436 THR B N   
7512  C CA  . THR B  436 ? 1.3030 1.4329 1.4355 -0.3702 0.2617  -0.1655 436 THR B CA  
7513  C C   . THR B  436 ? 1.2850 1.4078 1.4222 -0.3562 0.2486  -0.1561 436 THR B C   
7514  O O   . THR B  436 ? 1.2917 1.4082 1.4290 -0.3529 0.2393  -0.1479 436 THR B O   
7515  C CB  . THR B  436 ? 0.8632 0.9705 0.9646 -0.3792 0.2641  -0.1585 436 THR B CB  
7516  O OG1 . THR B  436 ? 0.9040 0.9863 0.9770 -0.3755 0.2624  -0.1502 436 THR B OG1 
7517  C CG2 . THR B  436 ? 0.8333 0.9472 0.9293 -0.3938 0.2772  -0.1675 436 THR B CG2 
7518  N N   . LEU B  437 ? 1.1085 1.2321 1.2493 -0.3484 0.2481  -0.1576 437 LEU B N   
7519  C CA  . LEU B  437 ? 1.0675 1.1842 1.2121 -0.3354 0.2364  -0.1491 437 LEU B CA  
7520  C C   . LEU B  437 ? 0.9565 1.0929 1.1340 -0.3284 0.2270  -0.1496 437 LEU B C   
7521  O O   . LEU B  437 ? 0.9073 1.0667 1.1123 -0.3275 0.2295  -0.1592 437 LEU B O   
7522  C CB  . LEU B  437 ? 1.2376 1.3511 1.3784 -0.3296 0.2391  -0.1516 437 LEU B CB  
7523  C CG  . LEU B  437 ? 1.2556 1.3435 1.3705 -0.3231 0.2334  -0.1406 437 LEU B CG  
7524  C CD1 . LEU B  437 ? 1.2495 1.3381 1.3657 -0.3173 0.2360  -0.1444 437 LEU B CD1 
7525  C CD2 . LEU B  437 ? 1.2348 1.3166 1.3545 -0.3142 0.2199  -0.1300 437 LEU B CD2 
7526  N N   . THR B  438 ? 0.8671 0.9939 1.0415 -0.3232 0.2159  -0.1391 438 THR B N   
7527  C CA  . THR B  438 ? 0.8316 0.9746 1.0339 -0.3175 0.2056  -0.1377 438 THR B CA  
7528  C C   . THR B  438 ? 0.8131 0.9586 1.0285 -0.3051 0.1971  -0.1345 438 THR B C   
7529  O O   . THR B  438 ? 0.7773 0.9381 1.0185 -0.2996 0.1884  -0.1340 438 THR B O   
7530  C CB  . THR B  438 ? 0.8478 0.9797 1.0406 -0.3184 0.1973  -0.1282 438 THR B CB  
7531  O OG1 . THR B  438 ? 0.8637 0.9817 1.0320 -0.3285 0.2048  -0.1279 438 THR B OG1 
7532  C CG2 . THR B  438 ? 0.8364 0.9897 1.0581 -0.3186 0.1907  -0.1303 438 THR B CG2 
7533  N N   . TRP B  439 ? 0.9408 1.0709 1.1379 -0.3011 0.1994  -0.1320 439 TRP B N   
7534  C CA  . TRP B  439 ? 0.8974 1.0273 1.1039 -0.2897 0.1922  -0.1289 439 TRP B CA  
7535  C C   . TRP B  439 ? 0.8915 1.0420 1.1226 -0.2879 0.1977  -0.1405 439 TRP B C   
7536  O O   . TRP B  439 ? 0.9149 1.0711 1.1434 -0.2953 0.2095  -0.1501 439 TRP B O   
7537  C CB  . TRP B  439 ? 0.7158 0.8214 0.8930 -0.2865 0.1929  -0.1224 439 TRP B CB  
7538  C CG  . TRP B  439 ? 0.5018 0.5865 0.6569 -0.2850 0.1856  -0.1106 439 TRP B CG  
7539  C CD1 . TRP B  439 ? 0.7499 0.8159 0.8766 -0.2914 0.1899  -0.1070 439 TRP B CD1 
7540  C CD2 . TRP B  439 ? 0.4840 0.5641 0.6437 -0.2765 0.1727  -0.1012 439 TRP B CD2 
7541  N NE1 . TRP B  439 ? 0.5132 0.5638 0.6276 -0.2868 0.1805  -0.0966 439 TRP B NE1 
7542  C CE2 . TRP B  439 ? 0.5009 0.5599 0.6347 -0.2779 0.1701  -0.0929 439 TRP B CE2 
7543  C CE3 . TRP B  439 ? 0.4634 0.5552 0.6465 -0.2681 0.1629  -0.0990 439 TRP B CE3 
7544  C CZ2 . TRP B  439 ? 0.4789 0.5288 0.6098 -0.2711 0.1586  -0.0833 439 TRP B CZ2 
7545  C CZ3 . TRP B  439 ? 0.4660 0.5482 0.6449 -0.2619 0.1512  -0.0887 439 TRP B CZ3 
7546  C CH2 . TRP B  439 ? 0.4641 0.5258 0.6172 -0.2635 0.1495  -0.0813 439 TRP B CH2 
7547  N N   . PRO B  440 ? 0.7847 0.9459 1.0395 -0.2781 0.1891  -0.1398 440 PRO B N   
7548  C CA  . PRO B  440 ? 0.7863 0.9679 1.0687 -0.2745 0.1927  -0.1512 440 PRO B CA  
7549  C C   . PRO B  440 ? 0.7737 0.9487 1.0418 -0.2763 0.2041  -0.1582 440 PRO B C   
7550  O O   . PRO B  440 ? 0.7626 0.9159 1.0005 -0.2778 0.2063  -0.1520 440 PRO B O   
7551  C CB  . PRO B  440 ? 0.8251 1.0096 1.1253 -0.2626 0.1796  -0.1449 440 PRO B CB  
7552  C CG  . PRO B  440 ? 0.7990 0.9595 1.0727 -0.2598 0.1722  -0.1311 440 PRO B CG  
7553  C CD  . PRO B  440 ? 0.8056 0.9578 1.0604 -0.2692 0.1753  -0.1280 440 PRO B CD  
7554  N N   . LEU B  441 ? 0.8878 1.0813 1.1771 -0.2765 0.2112  -0.1713 441 LEU B N   
7555  C CA  . LEU B  441 ? 0.9119 1.0999 1.1865 -0.2798 0.2228  -0.1789 441 LEU B CA  
7556  C C   . LEU B  441 ? 0.9129 1.0884 1.1801 -0.2708 0.2192  -0.1749 441 LEU B C   
7557  O O   . LEU B  441 ? 0.9569 1.1199 1.2016 -0.2740 0.2270  -0.1766 441 LEU B O   
7558  C CB  . LEU B  441 ? 0.8042 1.0154 1.1014 -0.2840 0.2329  -0.1955 441 LEU B CB  
7559  C CG  . LEU B  441 ? 0.8007 1.0321 1.1350 -0.2740 0.2287  -0.2037 441 LEU B CG  
7560  C CD1 . LEU B  441 ? 0.7992 1.0295 1.1317 -0.2713 0.2362  -0.2125 441 LEU B CD1 
7561  C CD2 . LEU B  441 ? 0.8084 1.0653 1.1723 -0.2772 0.2310  -0.2143 441 LEU B CD2 
7562  N N   . TRP B  442 ? 0.7059 0.8841 0.9909 -0.2600 0.2072  -0.1690 442 TRP B N   
7563  C CA  . TRP B  442 ? 0.6792 0.8467 0.9595 -0.2512 0.2037  -0.1657 442 TRP B CA  
7564  C C   . TRP B  442 ? 0.6440 0.7840 0.8867 -0.2527 0.2029  -0.1543 442 TRP B C   
7565  O O   . TRP B  442 ? 0.6476 0.7761 0.8797 -0.2476 0.2027  -0.1524 442 TRP B O   
7566  C CB  . TRP B  442 ? 0.8022 0.9780 1.1095 -0.2396 0.1905  -0.1614 442 TRP B CB  
7567  C CG  . TRP B  442 ? 0.8532 1.0198 1.1542 -0.2371 0.1780  -0.1472 442 TRP B CG  
7568  C CD1 . TRP B  442 ? 0.8855 1.0640 1.2037 -0.2377 0.1705  -0.1445 442 TRP B CD1 
7569  C CD2 . TRP B  442 ? 0.8656 1.0094 1.1416 -0.2337 0.1714  -0.1343 442 TRP B CD2 
7570  N NE1 . TRP B  442 ? 0.8874 1.0520 1.1921 -0.2353 0.1599  -0.1308 442 TRP B NE1 
7571  C CE2 . TRP B  442 ? 0.8719 1.0152 1.1511 -0.2326 0.1603  -0.1245 442 TRP B CE2 
7572  C CE3 . TRP B  442 ? 0.8776 1.0019 1.1290 -0.2316 0.1737  -0.1302 442 TRP B CE3 
7573  C CZ2 . TRP B  442 ? 0.8796 1.0039 1.1386 -0.2294 0.1518  -0.1115 442 TRP B CZ2 
7574  C CZ3 . TRP B  442 ? 0.8897 0.9949 1.1214 -0.2280 0.1650  -0.1171 442 TRP B CZ3 
7575  C CH2 . TRP B  442 ? 0.8930 0.9985 1.1289 -0.2268 0.1543  -0.1081 442 TRP B CH2 
7576  N N   . MET B  443 ? 0.6374 0.7673 0.8610 -0.2593 0.2022  -0.1472 443 MET B N   
7577  C CA  . MET B  443 ? 0.5837 0.6876 0.7719 -0.2609 0.2014  -0.1369 443 MET B CA  
7578  C C   . MET B  443 ? 0.5492 0.6441 0.7127 -0.2704 0.2139  -0.1421 443 MET B C   
7579  O O   . MET B  443 ? 0.5491 0.6225 0.6824 -0.2728 0.2140  -0.1343 443 MET B O   
7580  C CB  . MET B  443 ? 0.4721 0.5678 0.6510 -0.2630 0.1942  -0.1269 443 MET B CB  
7581  C CG  . MET B  443 ? 0.5534 0.6528 0.7491 -0.2543 0.1805  -0.1191 443 MET B CG  
7582  S SD  . MET B  443 ? 0.5713 0.6589 0.7515 -0.2579 0.1735  -0.1082 443 MET B SD  
7583  C CE  . MET B  443 ? 0.4456 0.5377 0.6452 -0.2472 0.1574  -0.0996 443 MET B CE  
7584  N N   . GLY B  444 ? 0.5865 0.6980 0.7627 -0.2760 0.2242  -0.1552 444 GLY B N   
7585  C CA  . GLY B  444 ? 0.6298 0.7339 0.7832 -0.2852 0.2363  -0.1610 444 GLY B CA  
7586  C C   . GLY B  444 ? 0.6440 0.7311 0.7677 -0.2944 0.2386  -0.1540 444 GLY B C   
7587  O O   . GLY B  444 ? 0.6604 0.7542 0.7897 -0.2999 0.2387  -0.1542 444 GLY B O   
7588  N N   . VAL B  445 ? 0.5552 0.6198 0.6477 -0.2956 0.2398  -0.1478 445 VAL B N   
7589  C CA  . VAL B  445 ? 0.5754 0.6214 0.6377 -0.3038 0.2418  -0.1411 445 VAL B CA  
7590  C C   . VAL B  445 ? 0.6164 0.6412 0.6627 -0.2960 0.2306  -0.1271 445 VAL B C   
7591  O O   . VAL B  445 ? 0.6253 0.6313 0.6479 -0.2944 0.2301  -0.1220 445 VAL B O   
7592  C CB  . VAL B  445 ? 0.5981 0.6339 0.6355 -0.3119 0.2519  -0.1452 445 VAL B CB  
7593  C CG1 . VAL B  445 ? 0.6232 0.6446 0.6342 -0.3228 0.2559  -0.1410 445 VAL B CG1 
7594  C CG2 . VAL B  445 ? 0.8896 0.9473 0.9458 -0.3163 0.2621  -0.1601 445 VAL B CG2 
7595  N N   . PRO B  446 ? 0.6493 0.6775 0.7086 -0.2914 0.2214  -0.1212 446 PRO B N   
7596  C CA  . PRO B  446 ? 0.6692 0.6824 0.7210 -0.2819 0.2096  -0.1094 446 PRO B CA  
7597  C C   . PRO B  446 ? 0.7325 0.7203 0.7512 -0.2844 0.2086  -0.1008 446 PRO B C   
7598  O O   . PRO B  446 ? 0.7388 0.7204 0.7408 -0.2944 0.2159  -0.1027 446 PRO B O   
7599  C CB  . PRO B  446 ? 0.5247 0.5498 0.5975 -0.2800 0.2022  -0.1070 446 PRO B CB  
7600  C CG  . PRO B  446 ? 0.5260 0.5755 0.6242 -0.2848 0.2087  -0.1184 446 PRO B CG  
7601  C CD  . PRO B  446 ? 0.5496 0.5968 0.6319 -0.2951 0.2215  -0.1257 446 PRO B CD  
7602  N N   . HIS B  447 ? 0.8411 0.8147 0.8514 -0.2751 0.1990  -0.0914 447 HIS B N   
7603  C CA  . HIS B  447 ? 0.8479 0.7973 0.8293 -0.2748 0.1960  -0.0827 447 HIS B CA  
7604  C C   . HIS B  447 ? 0.8800 0.8249 0.8528 -0.2829 0.1973  -0.0809 447 HIS B C   
7605  O O   . HIS B  447 ? 0.8956 0.8523 0.8856 -0.2836 0.1943  -0.0815 447 HIS B O   
7606  C CB  . HIS B  447 ? 0.7039 0.6449 0.6866 -0.2627 0.1840  -0.0739 447 HIS B CB  
7607  C CG  . HIS B  447 ? 0.7150 0.6321 0.6709 -0.2602 0.1797  -0.0653 447 HIS B CG  
7608  N ND1 . HIS B  447 ? 0.7249 0.6271 0.6588 -0.2609 0.1830  -0.0642 447 HIS B ND1 
7609  C CD2 . HIS B  447 ? 0.7153 0.6214 0.6639 -0.2568 0.1719  -0.0576 447 HIS B CD2 
7610  C CE1 . HIS B  447 ? 0.7292 0.6124 0.6442 -0.2577 0.1772  -0.0562 447 HIS B CE1 
7611  N NE2 . HIS B  447 ? 0.7253 0.6107 0.6490 -0.2551 0.1707  -0.0524 447 HIS B NE2 
7612  N N   . GLY B  448 ? 0.7386 0.6667 0.6853 -0.2895 0.2019  -0.0788 448 GLY B N   
7613  C CA  . GLY B  448 ? 0.7380 0.6583 0.6740 -0.2965 0.2024  -0.0760 448 GLY B CA  
7614  C C   . GLY B  448 ? 0.7723 0.7053 0.7146 -0.3088 0.2118  -0.0838 448 GLY B C   
7615  O O   . GLY B  448 ? 0.7999 0.7259 0.7329 -0.3154 0.2127  -0.0815 448 GLY B O   
7616  N N   . TYR B  449 ? 0.8616 0.8135 0.8202 -0.3120 0.2189  -0.0932 449 TYR B N   
7617  C CA  . TYR B  449 ? 0.8267 0.7933 0.7938 -0.3237 0.2283  -0.1018 449 TYR B CA  
7618  C C   . TYR B  449 ? 0.7699 0.7299 0.7165 -0.3351 0.2393  -0.1061 449 TYR B C   
7619  O O   . TYR B  449 ? 0.7544 0.7276 0.7081 -0.3451 0.2480  -0.1141 449 TYR B O   
7620  C CB  . TYR B  449 ? 0.7754 0.7694 0.7757 -0.3218 0.2296  -0.1106 449 TYR B CB  
7621  C CG  . TYR B  449 ? 0.8059 0.8071 0.8249 -0.3154 0.2197  -0.1063 449 TYR B CG  
7622  C CD1 . TYR B  449 ? 0.8385 0.8364 0.8542 -0.3207 0.2180  -0.1033 449 TYR B CD1 
7623  C CD2 . TYR B  449 ? 0.8294 0.8393 0.8680 -0.3044 0.2117  -0.1048 449 TYR B CD2 
7624  C CE1 . TYR B  449 ? 0.8556 0.8597 0.8872 -0.3154 0.2087  -0.0993 449 TYR B CE1 
7625  C CE2 . TYR B  449 ? 0.8542 0.8701 0.9086 -0.2991 0.2020  -0.1003 449 TYR B CE2 
7626  C CZ  . TYR B  449 ? 0.8531 0.8662 0.9038 -0.3047 0.2006  -0.0976 449 TYR B CZ  
7627  O OH  . TYR B  449 ? 0.8186 0.8377 0.8843 -0.3000 0.1909  -0.0933 449 TYR B OH  
7628  N N   . GLU B  450 ? 0.6719 0.6117 0.5933 -0.3339 0.2388  -0.1007 450 GLU B N   
7629  C CA  . GLU B  450 ? 0.7360 0.6656 0.6340 -0.3452 0.2477  -0.1024 450 GLU B CA  
7630  C C   . GLU B  450 ? 0.8230 0.7343 0.7009 -0.3510 0.2458  -0.0949 450 GLU B C   
7631  O O   . GLU B  450 ? 0.8658 0.7670 0.7234 -0.3614 0.2525  -0.0950 450 GLU B O   
7632  C CB  . GLU B  450 ? 0.8233 0.7403 0.7037 -0.3418 0.2479  -0.1004 450 GLU B CB  
7633  C CG  . GLU B  450 ? 0.8761 0.7656 0.7289 -0.3388 0.2414  -0.0890 450 GLU B CG  
7634  C CD  . GLU B  450 ? 0.8768 0.7596 0.7358 -0.3254 0.2291  -0.0809 450 GLU B CD  
7635  O OE1 . GLU B  450 ? 0.8716 0.7697 0.7550 -0.3198 0.2252  -0.0828 450 GLU B OE1 
7636  O OE2 . GLU B  450 ? 0.8719 0.7344 0.7116 -0.3205 0.2233  -0.0727 450 GLU B OE2 
7637  N N   . ILE B  451 ? 0.9463 0.8533 0.8302 -0.3444 0.2368  -0.0885 451 ILE B N   
7638  C CA  . ILE B  451 ? 0.9877 0.8781 0.8552 -0.3492 0.2347  -0.0819 451 ILE B CA  
7639  C C   . ILE B  451 ? 1.0425 0.9436 0.9161 -0.3618 0.2424  -0.0877 451 ILE B C   
7640  O O   . ILE B  451 ? 1.0745 0.9622 0.9289 -0.3711 0.2463  -0.0852 451 ILE B O   
7641  C CB  . ILE B  451 ? 0.8904 0.7735 0.7628 -0.3386 0.2229  -0.0740 451 ILE B CB  
7642  C CG1 . ILE B  451 ? 0.8427 0.7152 0.7089 -0.3263 0.2153  -0.0683 451 ILE B CG1 
7643  C CG2 . ILE B  451 ? 0.9038 0.7697 0.7599 -0.3436 0.2211  -0.0680 451 ILE B CG2 
7644  C CD1 . ILE B  451 ? 0.8096 0.6782 0.6834 -0.3154 0.2040  -0.0618 451 ILE B CD1 
7645  N N   . GLU B  452 ? 1.1039 1.0290 1.0043 -0.3622 0.2445  -0.0954 452 GLU B N   
7646  C CA  . GLU B  452 ? 1.0786 1.0171 0.9881 -0.3739 0.2521  -0.1022 452 GLU B CA  
7647  C C   . GLU B  452 ? 1.1199 1.0529 1.0102 -0.3869 0.2632  -0.1059 452 GLU B C   
7648  O O   . GLU B  452 ? 1.1560 1.0839 1.0367 -0.3975 0.2678  -0.1058 452 GLU B O   
7649  C CB  . GLU B  452 ? 0.8013 0.7686 0.7431 -0.3722 0.2541  -0.1117 452 GLU B CB  
7650  C CG  . GLU B  452 ? 0.7559 0.7312 0.7188 -0.3617 0.2435  -0.1084 452 GLU B CG  
7651  C CD  . GLU B  452 ? 0.7072 0.7099 0.7022 -0.3583 0.2441  -0.1169 452 GLU B CD  
7652  O OE1 . GLU B  452 ? 0.6994 0.7173 0.7029 -0.3654 0.2537  -0.1268 452 GLU B OE1 
7653  O OE2 . GLU B  452 ? 0.6676 0.6769 0.6800 -0.3486 0.2347  -0.1138 452 GLU B OE2 
7654  N N   . PHE B  453 ? 0.7733 0.7068 0.6577 -0.3859 0.2672  -0.1090 453 PHE B N   
7655  C CA  . PHE B  453 ? 0.8009 0.7322 0.6689 -0.3980 0.2780  -0.1137 453 PHE B CA  
7656  C C   . PHE B  453 ? 0.8247 0.7282 0.6592 -0.4021 0.2772  -0.1046 453 PHE B C   
7657  O O   . PHE B  453 ? 0.8528 0.7509 0.6725 -0.4147 0.2845  -0.1055 453 PHE B O   
7658  C CB  . PHE B  453 ? 0.9399 0.8862 0.8181 -0.3959 0.2832  -0.1224 453 PHE B CB  
7659  C CG  . PHE B  453 ? 0.9624 0.9379 0.8740 -0.3949 0.2862  -0.1332 453 PHE B CG  
7660  C CD1 . PHE B  453 ? 0.9421 0.9272 0.8771 -0.3843 0.2774  -0.1314 453 PHE B CD1 
7661  C CD2 . PHE B  453 ? 1.0092 1.0029 0.9294 -0.4046 0.2977  -0.1451 453 PHE B CD2 
7662  C CE1 . PHE B  453 ? 0.9311 0.9429 0.8976 -0.3831 0.2795  -0.1409 453 PHE B CE1 
7663  C CE2 . PHE B  453 ? 1.0022 1.0233 0.9549 -0.4031 0.3001  -0.1554 453 PHE B CE2 
7664  C CZ  . PHE B  453 ? 0.9532 0.9832 0.9292 -0.3922 0.2907  -0.1531 453 PHE B CZ  
7665  N N   . ILE B  454 ? 0.8145 0.7004 0.6373 -0.3916 0.2681  -0.0955 454 ILE B N   
7666  C CA  . ILE B  454 ? 0.9112 0.7703 0.7034 -0.3947 0.2662  -0.0864 454 ILE B CA  
7667  C C   . ILE B  454 ? 0.9237 0.7720 0.7079 -0.4016 0.2655  -0.0815 454 ILE B C   
7668  O O   . ILE B  454 ? 0.9052 0.7371 0.6663 -0.4108 0.2689  -0.0775 454 ILE B O   
7669  C CB  . ILE B  454 ? 0.8876 0.7301 0.6709 -0.3810 0.2555  -0.0776 454 ILE B CB  
7670  C CG1 . ILE B  454 ? 0.8395 0.6896 0.6268 -0.3753 0.2568  -0.0818 454 ILE B CG1 
7671  C CG2 . ILE B  454 ? 0.8453 0.6605 0.5990 -0.3837 0.2527  -0.0678 454 ILE B CG2 
7672  C CD1 . ILE B  454 ? 0.8500 0.6970 0.6193 -0.3859 0.2660  -0.0855 454 ILE B CD1 
7673  N N   . PHE B  455 ? 0.9956 0.8533 0.7991 -0.3976 0.2611  -0.0821 455 PHE B N   
7674  C CA  . PHE B  455 ? 0.9928 0.8406 0.7907 -0.4030 0.2595  -0.0776 455 PHE B CA  
7675  C C   . PHE B  455 ? 1.0033 0.8628 0.8053 -0.4179 0.2698  -0.0847 455 PHE B C   
7676  O O   . PHE B  455 ? 0.9778 0.8303 0.7753 -0.4244 0.2700  -0.0821 455 PHE B O   
7677  C CB  . PHE B  455 ? 0.8979 0.7473 0.7113 -0.3921 0.2492  -0.0738 455 PHE B CB  
7678  C CG  . PHE B  455 ? 0.9004 0.7271 0.6987 -0.3823 0.2393  -0.0635 455 PHE B CG  
7679  C CD1 . PHE B  455 ? 0.8818 0.7061 0.6809 -0.3700 0.2330  -0.0608 455 PHE B CD1 
7680  C CD2 . PHE B  455 ? 0.9221 0.7300 0.7058 -0.3855 0.2364  -0.0568 455 PHE B CD2 
7681  C CE1 . PHE B  455 ? 0.8572 0.6618 0.6434 -0.3610 0.2241  -0.0519 455 PHE B CE1 
7682  C CE2 . PHE B  455 ? 0.9018 0.6899 0.6731 -0.3763 0.2275  -0.0480 455 PHE B CE2 
7683  C CZ  . PHE B  455 ? 0.8637 0.6505 0.6363 -0.3641 0.2214  -0.0457 455 PHE B CZ  
7684  N N   . GLY B  456 ? 1.0856 0.9633 0.8965 -0.4233 0.2785  -0.0941 456 GLY B N   
7685  C CA  . GLY B  456 ? 1.1403 1.0299 0.9538 -0.4382 0.2895  -0.1019 456 GLY B CA  
7686  C C   . GLY B  456 ? 1.1471 1.0567 0.9867 -0.4395 0.2899  -0.1078 456 GLY B C   
7687  O O   . GLY B  456 ? 1.2108 1.1258 1.0511 -0.4516 0.2969  -0.1118 456 GLY B O   
7688  N N   . LEU B  457 ? 1.0033 0.9238 0.8643 -0.4272 0.2821  -0.1081 457 LEU B N   
7689  C CA  . LEU B  457 ? 0.9839 0.9254 0.8723 -0.4270 0.2812  -0.1137 457 LEU B CA  
7690  C C   . LEU B  457 ? 0.9705 0.9390 0.8791 -0.4357 0.2913  -0.1266 457 LEU B C   
7691  O O   . LEU B  457 ? 0.9789 0.9612 0.9045 -0.4400 0.2923  -0.1307 457 LEU B O   
7692  C CB  . LEU B  457 ? 1.0377 0.9836 0.9435 -0.4119 0.2696  -0.1101 457 LEU B CB  
7693  C CG  . LEU B  457 ? 1.0457 0.9757 0.9446 -0.4088 0.2610  -0.1012 457 LEU B CG  
7694  C CD1 . LEU B  457 ? 1.0574 0.9583 0.9257 -0.4087 0.2587  -0.0918 457 LEU B CD1 
7695  C CD2 . LEU B  457 ? 1.0198 0.9571 0.9377 -0.3953 0.2501  -0.0986 457 LEU B CD2 
7696  N N   . PRO B  458 ? 1.0576 1.0351 0.9665 -0.4376 0.2984  -0.1334 458 PRO B N   
7697  C CA  . PRO B  458 ? 1.0849 1.0876 1.0122 -0.4471 0.3088  -0.1462 458 PRO B CA  
7698  C C   . PRO B  458 ? 1.2639 1.2637 1.1783 -0.4638 0.3184  -0.1487 458 PRO B C   
7699  O O   . PRO B  458 ? 1.2653 1.2865 1.1979 -0.4716 0.3256  -0.1587 458 PRO B O   
7700  C CB  . PRO B  458 ? 1.1121 1.1226 1.0399 -0.4454 0.3142  -0.1527 458 PRO B CB  
7701  C CG  . PRO B  458 ? 1.0857 1.0824 1.0071 -0.4313 0.3042  -0.1444 458 PRO B CG  
7702  C CD  . PRO B  458 ? 1.0836 1.0540 0.9828 -0.4302 0.2970  -0.1317 458 PRO B CD  
7703  N N   . LEU B  459 ? 1.2512 1.2250 1.1355 -0.4692 0.3182  -0.1398 459 LEU B N   
7704  C CA  . LEU B  459 ? 1.2121 1.1800 1.0825 -0.4849 0.3262  -0.1404 459 LEU B CA  
7705  C C   . LEU B  459 ? 1.2352 1.2108 1.1213 -0.4876 0.3240  -0.1411 459 LEU B C   
7706  O O   . LEU B  459 ? 1.2781 1.2572 1.1617 -0.5010 0.3318  -0.1449 459 LEU B O   
7707  C CB  . LEU B  459 ? 0.9652 0.9018 0.8009 -0.4884 0.3245  -0.1291 459 LEU B CB  
7708  C CG  . LEU B  459 ? 0.9825 0.9097 0.7963 -0.4925 0.3300  -0.1287 459 LEU B CG  
7709  C CD1 . LEU B  459 ? 0.9574 0.8829 0.7735 -0.4781 0.3231  -0.1266 459 LEU B CD1 
7710  C CD2 . LEU B  459 ? 1.0134 0.9123 0.7947 -0.5004 0.3302  -0.1186 459 LEU B CD2 
7711  N N   . ASP B  460 ? 1.2801 1.2580 1.1817 -0.4753 0.3134  -0.1374 460 ASP B N   
7712  C CA  . ASP B  460 ? 1.2954 1.2847 1.2162 -0.4767 0.3106  -0.1393 460 ASP B CA  
7713  C C   . ASP B  460 ? 1.3075 1.3291 1.2585 -0.4792 0.3165  -0.1523 460 ASP B C   
7714  O O   . ASP B  460 ? 1.2806 1.3173 1.2507 -0.4692 0.3133  -0.1563 460 ASP B O   
7715  C CB  . ASP B  460 ? 1.1145 1.0966 1.0421 -0.4628 0.2972  -0.1313 460 ASP B CB  
7716  C CG  . ASP B  460 ? 1.0850 1.0766 1.0297 -0.4650 0.2938  -0.1326 460 ASP B CG  
7717  O OD1 . ASP B  460 ? 1.0800 1.0973 1.0521 -0.4649 0.2951  -0.1410 460 ASP B OD1 
7718  O OD2 . ASP B  460 ? 1.0593 1.0328 0.9906 -0.4667 0.2896  -0.1252 460 ASP B OD2 
7719  N N   . PRO B  461 ? 1.2828 1.3153 1.2388 -0.4928 0.3252  -0.1592 461 PRO B N   
7720  C CA  . PRO B  461 ? 1.2847 1.3481 1.2681 -0.4967 0.3323  -0.1727 461 PRO B CA  
7721  C C   . PRO B  461 ? 1.2520 1.3350 1.2675 -0.4864 0.3238  -0.1751 461 PRO B C   
7722  O O   . PRO B  461 ? 1.2327 1.3373 1.2718 -0.4804 0.3241  -0.1830 461 PRO B O   
7723  C CB  . PRO B  461 ? 1.2360 1.3021 1.2142 -0.5137 0.3421  -0.1773 461 PRO B CB  
7724  C CG  . PRO B  461 ? 1.2501 1.2845 1.1938 -0.5193 0.3416  -0.1661 461 PRO B CG  
7725  C CD  . PRO B  461 ? 1.2198 1.2368 1.1575 -0.5048 0.3285  -0.1550 461 PRO B CD  
7726  N N   . SER B  462 ? 1.2325 1.3069 1.2483 -0.4842 0.3157  -0.1682 462 SER B N   
7727  C CA  . SER B  462 ? 1.2134 1.3059 1.2583 -0.4768 0.3075  -0.1700 462 SER B CA  
7728  C C   . SER B  462 ? 1.2632 1.3591 1.3204 -0.4605 0.2976  -0.1668 462 SER B C   
7729  O O   . SER B  462 ? 1.2646 1.3763 1.3469 -0.4534 0.2900  -0.1680 462 SER B O   
7730  C CB  . SER B  462 ? 1.0043 1.0848 1.0435 -0.4793 0.3015  -0.1632 462 SER B CB  
7731  O OG  . SER B  462 ? 0.9780 1.0288 0.9896 -0.4753 0.2962  -0.1516 462 SER B OG  
7732  N N   . LEU B  463 ? 1.4322 1.5130 1.4713 -0.4548 0.2972  -0.1622 463 LEU B N   
7733  C CA  . LEU B  463 ? 1.4097 1.4910 1.4574 -0.4397 0.2881  -0.1584 463 LEU B CA  
7734  C C   . LEU B  463 ? 1.4268 1.5331 1.4995 -0.4353 0.2913  -0.1685 463 LEU B C   
7735  O O   . LEU B  463 ? 1.4282 1.5385 1.5130 -0.4229 0.2835  -0.1663 463 LEU B O   
7736  C CB  . LEU B  463 ? 1.0893 1.1430 1.1074 -0.4347 0.2852  -0.1487 463 LEU B CB  
7737  C CG  . LEU B  463 ? 1.0085 1.0384 1.0095 -0.4301 0.2757  -0.1367 463 LEU B CG  
7738  C CD1 . LEU B  463 ? 0.9842 0.9896 0.9586 -0.4247 0.2735  -0.1285 463 LEU B CD1 
7739  C CD2 . LEU B  463 ? 0.9482 0.9870 0.9706 -0.4192 0.2641  -0.1338 463 LEU B CD2 
7740  N N   . ASN B  464 ? 1.2028 1.3258 1.2837 -0.4457 0.3027  -0.1797 464 ASN B N   
7741  C CA  . ASN B  464 ? 1.1761 1.3244 1.2823 -0.4427 0.3071  -0.1912 464 ASN B CA  
7742  C C   . ASN B  464 ? 1.1449 1.2874 1.2416 -0.4369 0.3093  -0.1919 464 ASN B C   
7743  O O   . ASN B  464 ? 1.0809 1.2396 1.2001 -0.4279 0.3068  -0.1971 464 ASN B O   
7744  C CB  . ASN B  464 ? 1.2289 1.3983 1.3697 -0.4328 0.2978  -0.1933 464 ASN B CB  
7745  C CG  . ASN B  464 ? 1.2599 1.4393 1.4141 -0.4388 0.2958  -0.1944 464 ASN B CG  
7746  O OD1 . ASN B  464 ? 1.2946 1.4731 1.4396 -0.4518 0.3042  -0.1979 464 ASN B OD1 
7747  N ND2 . ASN B  464 ? 1.2371 1.4264 1.4133 -0.4299 0.2846  -0.1914 464 ASN B ND2 
7748  N N   . TYR B  465 ? 1.3346 1.4543 1.3988 -0.4421 0.3137  -0.1868 465 TYR B N   
7749  C CA  . TYR B  465 ? 1.3731 1.4881 1.4267 -0.4391 0.3175  -0.1887 465 TYR B CA  
7750  C C   . TYR B  465 ? 1.3837 1.5173 1.4446 -0.4495 0.3310  -0.2028 465 TYR B C   
7751  O O   . TYR B  465 ? 1.4290 1.5701 1.4909 -0.4616 0.3385  -0.2083 465 TYR B O   
7752  C CB  . TYR B  465 ? 1.3260 1.4093 1.3420 -0.4404 0.3161  -0.1775 465 TYR B CB  
7753  C CG  . TYR B  465 ? 1.3080 1.3733 1.3169 -0.4276 0.3029  -0.1648 465 TYR B CG  
7754  C CD1 . TYR B  465 ? 1.3158 1.3684 1.3180 -0.4274 0.2960  -0.1560 465 TYR B CD1 
7755  C CD2 . TYR B  465 ? 1.2874 1.3487 1.2966 -0.4158 0.2976  -0.1620 465 TYR B CD2 
7756  C CE1 . TYR B  465 ? 1.3044 1.3411 1.3002 -0.4159 0.2842  -0.1451 465 TYR B CE1 
7757  C CE2 . TYR B  465 ? 1.2847 1.3302 1.2877 -0.4044 0.2858  -0.1508 465 TYR B CE2 
7758  C CZ  . TYR B  465 ? 1.2912 1.3246 1.2876 -0.4044 0.2791  -0.1425 465 TYR B CZ  
7759  O OH  . TYR B  465 ? 1.2749 1.2933 1.2654 -0.3932 0.2676  -0.1320 465 TYR B OH  
7760  N N   . THR B  466 ? 1.1686 1.3099 1.2349 -0.4450 0.3342  -0.2092 466 THR B N   
7761  C CA  . THR B  466 ? 1.1584 1.3149 1.2277 -0.4551 0.3475  -0.2226 466 THR B CA  
7762  C C   . THR B  466 ? 1.1671 1.3025 1.1993 -0.4680 0.3554  -0.2188 466 THR B C   
7763  O O   . THR B  466 ? 1.1558 1.2646 1.1613 -0.4664 0.3496  -0.2058 466 THR B O   
7764  C CB  . THR B  466 ? 0.8853 1.0565 0.9721 -0.4465 0.3488  -0.2314 466 THR B CB  
7765  O OG1 . THR B  466 ? 0.8988 1.0505 0.9585 -0.4455 0.3498  -0.2265 466 THR B OG1 
7766  C CG2 . THR B  466 ? 0.8327 1.0141 0.9479 -0.4308 0.3370  -0.2291 466 THR B CG2 
7767  N N   . THR B  467 ? 1.2763 1.4234 1.3070 -0.4810 0.3681  -0.2297 467 THR B N   
7768  C CA  . THR B  467 ? 1.3113 1.4392 1.3074 -0.4947 0.3755  -0.2257 467 THR B CA  
7769  C C   . THR B  467 ? 1.3464 1.4559 1.3168 -0.4922 0.3754  -0.2207 467 THR B C   
7770  O O   . THR B  467 ? 1.3676 1.4501 1.3064 -0.4953 0.3727  -0.2089 467 THR B O   
7771  C CB  . THR B  467 ? 1.2139 1.3598 1.2148 -0.5105 0.3895  -0.2388 467 THR B CB  
7772  O OG1 . THR B  467 ? 1.2050 1.3707 1.2333 -0.5117 0.3893  -0.2446 467 THR B OG1 
7773  C CG2 . THR B  467 ? 1.2258 1.3502 1.1909 -0.5253 0.3957  -0.2325 467 THR B CG2 
7774  N N   . GLU B  468 ? 1.3809 1.5050 1.3657 -0.4864 0.3778  -0.2298 468 GLU B N   
7775  C CA  . GLU B  468 ? 1.3859 1.4946 1.3499 -0.4824 0.3766  -0.2255 468 GLU B CA  
7776  C C   . GLU B  468 ? 1.3415 1.4268 1.2935 -0.4698 0.3631  -0.2100 468 GLU B C   
7777  O O   . GLU B  468 ? 1.3410 1.4047 1.2664 -0.4687 0.3607  -0.2017 468 GLU B O   
7778  C CB  . GLU B  468 ? 1.3490 1.4794 1.3352 -0.4769 0.3806  -0.2387 468 GLU B CB  
7779  C CG  . GLU B  468 ? 1.3296 1.4823 1.3553 -0.4644 0.3747  -0.2447 468 GLU B CG  
7780  C CD  . GLU B  468 ? 1.3220 1.4962 1.3704 -0.4595 0.3793  -0.2586 468 GLU B CD  
7781  O OE1 . GLU B  468 ? 1.3212 1.4894 1.3524 -0.4630 0.3847  -0.2614 468 GLU B OE1 
7782  O OE2 . GLU B  468 ? 1.3044 1.5018 1.3883 -0.4521 0.3771  -0.2670 468 GLU B OE2 
7783  N N   . GLU B  469 ? 1.3242 1.4142 1.2961 -0.4606 0.3541  -0.2061 469 GLU B N   
7784  C CA  . GLU B  469 ? 1.2884 1.3573 1.2500 -0.4495 0.3414  -0.1916 469 GLU B CA  
7785  C C   . GLU B  469 ? 1.3344 1.3761 1.2638 -0.4567 0.3397  -0.1797 469 GLU B C   
7786  O O   . GLU B  469 ? 1.3648 1.3834 1.2740 -0.4501 0.3321  -0.1683 469 GLU B O   
7787  C CB  . GLU B  469 ? 1.0052 1.0869 0.9961 -0.4389 0.3323  -0.1907 469 GLU B CB  
7788  C CG  . GLU B  469 ? 0.7934 0.8926 0.8116 -0.4264 0.3285  -0.1967 469 GLU B CG  
7789  C CD  . GLU B  469 ? 0.7976 0.9049 0.8406 -0.4154 0.3175  -0.1928 469 GLU B CD  
7790  O OE1 . GLU B  469 ? 0.8002 0.9029 0.8411 -0.4190 0.3144  -0.1875 469 GLU B OE1 
7791  O OE2 . GLU B  469 ? 0.7588 0.8769 0.8229 -0.4036 0.3119  -0.1948 469 GLU B OE2 
7792  N N   . ARG B  470 ? 1.1732 1.2173 1.0985 -0.4697 0.3464  -0.1822 470 ARG B N   
7793  C CA  . ARG B  470 ? 1.1854 1.2032 1.0804 -0.4769 0.3451  -0.1710 470 ARG B CA  
7794  C C   . ARG B  470 ? 1.1891 1.1917 1.0535 -0.4863 0.3519  -0.1694 470 ARG B C   
7795  O O   . ARG B  470 ? 1.1892 1.1655 1.0259 -0.4877 0.3479  -0.1578 470 ARG B O   
7796  C CB  . ARG B  470 ? 1.3613 1.3838 1.2618 -0.4866 0.3480  -0.1720 470 ARG B CB  
7797  C CG  . ARG B  470 ? 1.4307 1.4679 1.3321 -0.5028 0.3617  -0.1830 470 ARG B CG  
7798  C CD  . ARG B  470 ? 1.4617 1.4866 1.3471 -0.5155 0.3648  -0.1782 470 ARG B CD  
7799  N NE  . ARG B  470 ? 1.4685 1.5136 1.3642 -0.5298 0.3770  -0.1902 470 ARG B NE  
7800  C CZ  . ARG B  470 ? 1.4655 1.5138 1.3484 -0.5418 0.3883  -0.1968 470 ARG B CZ  
7801  N NH1 . ARG B  470 ? 1.4591 1.4913 1.3178 -0.5415 0.3886  -0.1920 470 ARG B NH1 
7802  N NH2 . ARG B  470 ? 1.4669 1.5350 1.3613 -0.5544 0.3992  -0.2082 470 ARG B NH2 
7803  N N   . ILE B  471 ? 1.3153 1.3345 1.1850 -0.4925 0.3619  -0.1810 471 ILE B N   
7804  C CA  . ILE B  471 ? 1.3376 1.3429 1.1784 -0.5007 0.3677  -0.1794 471 ILE B CA  
7805  C C   . ILE B  471 ? 1.2971 1.2868 1.1268 -0.4880 0.3590  -0.1715 471 ILE B C   
7806  O O   . ILE B  471 ? 1.3380 1.3047 1.1379 -0.4908 0.3576  -0.1627 471 ILE B O   
7807  C CB  . ILE B  471 ? 1.1836 1.2109 1.0315 -0.5124 0.3815  -0.1945 471 ILE B CB  
7808  C CG1 . ILE B  471 ? 1.1632 1.2102 1.0334 -0.5029 0.3822  -0.2048 471 ILE B CG1 
7809  C CG2 . ILE B  471 ? 1.1703 1.2164 1.0354 -0.5226 0.3890  -0.2032 471 ILE B CG2 
7810  C CD1 . ILE B  471 ? 1.1548 1.2242 1.0332 -0.5137 0.3957  -0.2208 471 ILE B CD1 
7811  N N   . PHE B  472 ? 1.0060 1.0083 0.8606 -0.4740 0.3529  -0.1745 472 PHE B N   
7812  C CA  . PHE B  472 ? 0.9690 0.9581 0.8182 -0.4601 0.3431  -0.1668 472 PHE B CA  
7813  C C   . PHE B  472 ? 0.9280 0.8898 0.7575 -0.4555 0.3328  -0.1511 472 PHE B C   
7814  O O   . PHE B  472 ? 0.9189 0.8590 0.7244 -0.4526 0.3284  -0.1422 472 PHE B O   
7815  C CB  . PHE B  472 ? 1.2745 1.2843 1.1582 -0.4469 0.3383  -0.1728 472 PHE B CB  
7816  C CG  . PHE B  472 ? 1.2973 1.2976 1.1798 -0.4325 0.3291  -0.1668 472 PHE B CG  
7817  C CD1 . PHE B  472 ? 1.3372 1.3153 1.1909 -0.4321 0.3272  -0.1591 472 PHE B CD1 
7818  C CD2 . PHE B  472 ? 1.2699 1.2840 1.1808 -0.4194 0.3223  -0.1688 472 PHE B CD2 
7819  C CE1 . PHE B  472 ? 1.3241 1.2941 1.1774 -0.4191 0.3189  -0.1539 472 PHE B CE1 
7820  C CE2 . PHE B  472 ? 1.2738 1.2797 1.1842 -0.4066 0.3142  -0.1634 472 PHE B CE2 
7821  C CZ  . PHE B  472 ? 1.2984 1.2823 1.1800 -0.4064 0.3127  -0.1562 472 PHE B CZ  
7822  N N   . ALA B  473 ? 0.9958 0.9595 0.8365 -0.4546 0.3288  -0.1483 473 ALA B N   
7823  C CA  . ALA B  473 ? 0.9913 0.9313 0.8166 -0.4503 0.3193  -0.1348 473 ALA B CA  
7824  C C   . ALA B  473 ? 1.0303 0.9458 0.8209 -0.4602 0.3219  -0.1272 473 ALA B C   
7825  O O   . ALA B  473 ? 0.9991 0.8918 0.7701 -0.4540 0.3143  -0.1165 473 ALA B O   
7826  C CB  . ALA B  473 ? 0.9002 0.8482 0.7422 -0.4515 0.3171  -0.1351 473 ALA B CB  
7827  N N   . GLN B  474 ? 1.1830 1.1038 0.9666 -0.4758 0.3327  -0.1328 474 GLN B N   
7828  C CA  . GLN B  474 ? 1.2327 1.1321 0.9839 -0.4871 0.3363  -0.1262 474 GLN B CA  
7829  C C   . GLN B  474 ? 1.2653 1.1524 0.9970 -0.4838 0.3350  -0.1227 474 GLN B C   
7830  O O   . GLN B  474 ? 1.2816 1.1432 0.9872 -0.4836 0.3300  -0.1114 474 GLN B O   
7831  C CB  . GLN B  474 ? 1.2198 1.1310 0.9692 -0.5048 0.3493  -0.1346 474 GLN B CB  
7832  C CG  . GLN B  474 ? 1.2397 1.1599 1.0047 -0.5096 0.3506  -0.1368 474 GLN B CG  
7833  C CD  . GLN B  474 ? 1.2799 1.2154 1.0469 -0.5269 0.3640  -0.1469 474 GLN B CD  
7834  O OE1 . GLN B  474 ? 1.2546 1.2111 1.0458 -0.5294 0.3677  -0.1554 474 GLN B OE1 
7835  N NE2 . GLN B  474 ? 1.3260 1.2512 1.0676 -0.5389 0.3712  -0.1458 474 GLN B NE2 
7836  N N   . ARG B  475 ? 1.2185 1.1241 0.9641 -0.4808 0.3392  -0.1326 475 ARG B N   
7837  C CA  . ARG B  475 ? 1.1845 1.0811 0.9149 -0.4768 0.3378  -0.1305 475 ARG B CA  
7838  C C   . ARG B  475 ? 1.1590 1.0338 0.8798 -0.4631 0.3246  -0.1177 475 ARG B C   
7839  O O   . ARG B  475 ? 1.1731 1.0251 0.8668 -0.4642 0.3213  -0.1084 475 ARG B O   
7840  C CB  . ARG B  475 ? 1.1310 1.0519 0.8846 -0.4716 0.3417  -0.1429 475 ARG B CB  
7841  C CG  . ARG B  475 ? 1.1516 1.0930 0.9103 -0.4848 0.3555  -0.1566 475 ARG B CG  
7842  C CD  . ARG B  475 ? 1.1157 1.0780 0.8958 -0.4776 0.3579  -0.1679 475 ARG B CD  
7843  N NE  . ARG B  475 ? 1.0868 1.0341 0.8526 -0.4687 0.3514  -0.1614 475 ARG B NE  
7844  C CZ  . ARG B  475 ? 1.0349 0.9942 0.8169 -0.4592 0.3503  -0.1678 475 ARG B CZ  
7845  N NH1 . ARG B  475 ? 1.0013 0.9880 0.8153 -0.4567 0.3548  -0.1809 475 ARG B NH1 
7846  N NH2 . ARG B  475 ? 1.0245 0.9684 0.7913 -0.4521 0.3444  -0.1611 475 ARG B NH2 
7847  N N   . LEU B  476 ? 1.1804 1.0624 0.9238 -0.4502 0.3168  -0.1172 476 LEU B N   
7848  C CA  . LEU B  476 ? 1.1598 1.0248 0.8985 -0.4358 0.3042  -0.1066 476 LEU B CA  
7849  C C   . LEU B  476 ? 1.1137 0.9521 0.8296 -0.4372 0.2980  -0.0939 476 LEU B C   
7850  O O   . LEU B  476 ? 1.0736 0.8919 0.7720 -0.4305 0.2907  -0.0847 476 LEU B O   
7851  C CB  . LEU B  476 ? 1.1472 1.0271 0.9159 -0.4229 0.2977  -0.1090 476 LEU B CB  
7852  C CG  . LEU B  476 ? 1.1202 1.0245 0.9137 -0.4179 0.3012  -0.1202 476 LEU B CG  
7853  C CD1 . LEU B  476 ? 1.0762 0.9937 0.8984 -0.4060 0.2939  -0.1210 476 LEU B CD1 
7854  C CD2 . LEU B  476 ? 1.1048 1.0020 0.8868 -0.4127 0.3000  -0.1193 476 LEU B CD2 
7855  N N   . MET B  477 ? 0.9590 0.7977 0.6760 -0.4458 0.3010  -0.0936 477 MET B N   
7856  C CA  . MET B  477 ? 0.9859 0.8001 0.6824 -0.4483 0.2960  -0.0823 477 MET B CA  
7857  C C   . MET B  477 ? 1.0545 0.8495 0.7199 -0.4569 0.2990  -0.0767 477 MET B C   
7858  O O   . MET B  477 ? 1.0270 0.7982 0.6734 -0.4525 0.2913  -0.0657 477 MET B O   
7859  C CB  . MET B  477 ? 0.9885 0.8083 0.6928 -0.4573 0.2999  -0.0843 477 MET B CB  
7860  C CG  . MET B  477 ? 0.9574 0.7953 0.6917 -0.4489 0.2961  -0.0889 477 MET B CG  
7861  S SD  . MET B  477 ? 1.4923 1.3470 1.2422 -0.4614 0.3040  -0.0964 477 MET B SD  
7862  C CE  . MET B  477 ? 0.9864 0.8147 0.7181 -0.4639 0.2979  -0.0843 477 MET B CE  
7863  N N   . LYS B  478 ? 1.3136 1.1195 0.9743 -0.4692 0.3101  -0.0846 478 LYS B N   
7864  C CA  . LYS B  478 ? 1.3715 1.1617 1.0029 -0.4780 0.3135  -0.0802 478 LYS B CA  
7865  C C   . LYS B  478 ? 1.3555 1.1335 0.9770 -0.4664 0.3056  -0.0744 478 LYS B C   
7866  O O   . LYS B  478 ? 1.3417 1.0963 0.9386 -0.4667 0.3007  -0.0640 478 LYS B O   
7867  C CB  . LYS B  478 ? 1.3725 1.1806 1.0041 -0.4919 0.3270  -0.0914 478 LYS B CB  
7868  C CG  . LYS B  478 ? 1.4309 1.2296 1.0414 -0.5094 0.3346  -0.0890 478 LYS B CG  
7869  C CD  . LYS B  478 ? 1.4606 1.2453 1.0418 -0.5171 0.3374  -0.0847 478 LYS B CD  
7870  C CE  . LYS B  478 ? 1.4885 1.2552 1.0447 -0.5315 0.3408  -0.0771 478 LYS B CE  
7871  N NZ  . LYS B  478 ? 1.4776 1.2208 1.0259 -0.5246 0.3301  -0.0641 478 LYS B NZ  
7872  N N   . TYR B  479 ? 1.3507 1.1450 0.9924 -0.4560 0.3040  -0.0811 479 TYR B N   
7873  C CA  . TYR B  479 ? 1.3234 1.1088 0.9590 -0.4444 0.2966  -0.0769 479 TYR B CA  
7874  C C   . TYR B  479 ? 1.3044 1.0665 0.9303 -0.4337 0.2840  -0.0639 479 TYR B C   
7875  O O   . TYR B  479 ? 1.3377 1.0789 0.9402 -0.4327 0.2794  -0.0552 479 TYR B O   
7876  C CB  . TYR B  479 ? 1.2191 1.0270 0.8826 -0.4344 0.2965  -0.0862 479 TYR B CB  
7877  C CG  . TYR B  479 ? 1.2308 1.0591 0.9011 -0.4423 0.3077  -0.0987 479 TYR B CG  
7878  C CD1 . TYR B  479 ? 1.2544 1.0755 0.9027 -0.4493 0.3120  -0.0986 479 TYR B CD1 
7879  C CD2 . TYR B  479 ? 1.2343 1.0896 0.9334 -0.4428 0.3137  -0.1109 479 TYR B CD2 
7880  C CE1 . TYR B  479 ? 1.2848 1.1255 0.9398 -0.4569 0.3226  -0.1109 479 TYR B CE1 
7881  C CE2 . TYR B  479 ? 1.2591 1.1342 0.9661 -0.4498 0.3241  -0.1234 479 TYR B CE2 
7882  C CZ  . TYR B  479 ? 1.2845 1.1524 0.9693 -0.4570 0.3287  -0.1236 479 TYR B CZ  
7883  O OH  . TYR B  479 ? 1.2905 1.1787 0.9833 -0.4642 0.3393  -0.1367 479 TYR B OH  
7884  N N   . TRP B  480 ? 1.0446 0.8110 0.6889 -0.4260 0.2786  -0.0630 480 TRP B N   
7885  C CA  . TRP B  480 ? 1.0051 0.7532 0.6453 -0.4144 0.2666  -0.0524 480 TRP B CA  
7886  C C   . TRP B  480 ? 1.0275 0.7508 0.6418 -0.4214 0.2646  -0.0423 480 TRP B C   
7887  O O   . TRP B  480 ? 1.0004 0.7038 0.5996 -0.4146 0.2564  -0.0331 480 TRP B O   
7888  C CB  . TRP B  480 ? 0.9901 0.7497 0.6555 -0.4069 0.2623  -0.0543 480 TRP B CB  
7889  C CG  . TRP B  480 ? 0.9002 0.6703 0.5858 -0.3916 0.2554  -0.0563 480 TRP B CG  
7890  C CD1 . TRP B  480 ? 0.8771 0.6430 0.5730 -0.3793 0.2453  -0.0511 480 TRP B CD1 
7891  C CD2 . TRP B  480 ? 0.8824 0.6691 0.5807 -0.3875 0.2584  -0.0640 480 TRP B CD2 
7892  N NE1 . TRP B  480 ? 0.8467 0.6251 0.5601 -0.3680 0.2417  -0.0546 480 TRP B NE1 
7893  C CE2 . TRP B  480 ? 0.8493 0.6403 0.5648 -0.3727 0.2495  -0.0625 480 TRP B CE2 
7894  C CE3 . TRP B  480 ? 0.8918 0.6905 0.5891 -0.3951 0.2678  -0.0724 480 TRP B CE3 
7895  C CZ2 . TRP B  480 ? 0.8362 0.6422 0.5677 -0.3653 0.2497  -0.0685 480 TRP B CZ2 
7896  C CZ3 . TRP B  480 ? 0.8678 0.6817 0.5817 -0.3874 0.2680  -0.0790 480 TRP B CZ3 
7897  C CH2 . TRP B  480 ? 0.8356 0.6525 0.5661 -0.3727 0.2590  -0.0768 480 TRP B CH2 
7898  N N   . THR B  481 ? 1.1614 0.8859 0.7709 -0.4351 0.2722  -0.0441 481 THR B N   
7899  C CA  . THR B  481 ? 1.2676 0.9688 0.8536 -0.4426 0.2708  -0.0345 481 THR B CA  
7900  C C   . THR B  481 ? 1.3021 0.9879 0.8603 -0.4489 0.2724  -0.0294 481 THR B C   
7901  O O   . THR B  481 ? 1.2941 0.9561 0.8326 -0.4477 0.2660  -0.0186 481 THR B O   
7902  C CB  . THR B  481 ? 1.5558 1.2628 1.1444 -0.4563 0.2788  -0.0378 481 THR B CB  
7903  O OG1 . THR B  481 ? 1.6094 1.3386 1.2068 -0.4659 0.2901  -0.0492 481 THR B OG1 
7904  C CG2 . THR B  481 ? 1.5233 1.2365 1.1331 -0.4497 0.2741  -0.0384 481 THR B CG2 
7905  N N   . ASN B  482 ? 1.4361 1.1358 0.9932 -0.4557 0.2809  -0.0374 482 ASN B N   
7906  C CA  . ASN B  482 ? 1.4883 1.1763 1.0206 -0.4608 0.2824  -0.0337 482 ASN B CA  
7907  C C   . ASN B  482 ? 1.4485 1.1220 0.9745 -0.4464 0.2710  -0.0260 482 ASN B C   
7908  O O   . ASN B  482 ? 1.4617 1.1142 0.9634 -0.4480 0.2670  -0.0168 482 ASN B O   
7909  C CB  . ASN B  482 ? 1.6134 1.3222 1.1501 -0.4685 0.2930  -0.0451 482 ASN B CB  
7910  C CG  . ASN B  482 ? 1.6852 1.4039 1.2189 -0.4861 0.3052  -0.0513 482 ASN B CG  
7911  O OD1 . ASN B  482 ? 1.6822 1.4251 1.2340 -0.4904 0.3139  -0.0635 482 ASN B OD1 
7912  N ND2 . ASN B  482 ? 1.7415 1.4416 1.2527 -0.4965 0.3061  -0.0430 482 ASN B ND2 
7913  N N   . PHE B  483 ? 1.2307 0.9154 0.7787 -0.4323 0.2657  -0.0297 483 PHE B N   
7914  C CA  . PHE B  483 ? 1.1914 0.8630 0.7356 -0.4178 0.2544  -0.0227 483 PHE B CA  
7915  C C   . PHE B  483 ? 1.1779 0.8275 0.7135 -0.4123 0.2448  -0.0114 483 PHE B C   
7916  O O   . PHE B  483 ? 1.0568 0.6876 0.5763 -0.4068 0.2372  -0.0028 483 PHE B O   
7917  C CB  . PHE B  483 ? 1.2627 0.9516 0.8328 -0.4044 0.2511  -0.0291 483 PHE B CB  
7918  C CG  . PHE B  483 ? 1.2408 0.9170 0.8082 -0.3895 0.2396  -0.0222 483 PHE B CG  
7919  C CD1 . PHE B  483 ? 1.2625 0.9302 0.8137 -0.3881 0.2379  -0.0196 483 PHE B CD1 
7920  C CD2 . PHE B  483 ? 1.1956 0.8688 0.7764 -0.3773 0.2306  -0.0183 483 PHE B CD2 
7921  C CE1 . PHE B  483 ? 1.2408 0.8971 0.7898 -0.3746 0.2275  -0.0135 483 PHE B CE1 
7922  C CE2 . PHE B  483 ? 1.1801 0.8425 0.7588 -0.3640 0.2204  -0.0124 483 PHE B CE2 
7923  C CZ  . PHE B  483 ? 1.2024 0.8564 0.7654 -0.3625 0.2188  -0.0100 483 PHE B CZ  
7924  N N   . ALA B  484 ? 1.2188 0.8714 0.7661 -0.4139 0.2451  -0.0118 484 ALA B N   
7925  C CA  . ALA B  484 ? 1.2170 0.8503 0.7583 -0.4098 0.2371  -0.0022 484 ALA B CA  
7926  C C   . ALA B  484 ? 1.2883 0.8979 0.8004 -0.4182 0.2365  0.0072  484 ALA B C   
7927  O O   . ALA B  484 ? 1.2556 0.8464 0.7565 -0.4103 0.2273  0.0161  484 ALA B O   
7928  C CB  . ALA B  484 ? 1.1396 0.7811 0.6959 -0.4141 0.2400  -0.0053 484 ALA B CB  
7929  N N   . ARG B  485 ? 1.4446 1.0556 0.9447 -0.4342 0.2462  0.0052  485 ARG B N   
7930  C CA  . ARG B  485 ? 1.4919 1.0809 0.9633 -0.4440 0.2465  0.0143  485 ARG B CA  
7931  C C   . ARG B  485 ? 1.4522 1.0323 0.9052 -0.4418 0.2437  0.0181  485 ARG B C   
7932  O O   . ARG B  485 ? 1.4147 0.9729 0.8506 -0.4380 0.2358  0.0285  485 ARG B O   
7933  C CB  . ARG B  485 ? 1.6115 1.2053 1.0753 -0.4625 0.2581  0.0109  485 ARG B CB  
7934  C CG  . ARG B  485 ? 1.6433 1.2625 1.1170 -0.4703 0.2694  -0.0016 485 ARG B CG  
7935  C CD  . ARG B  485 ? 1.7096 1.3347 1.1783 -0.4885 0.2809  -0.0055 485 ARG B CD  
7936  N NE  . ARG B  485 ? 1.7256 1.3604 1.2143 -0.4891 0.2826  -0.0095 485 ARG B NE  
7937  C CZ  . ARG B  485 ? 1.7074 1.3658 1.2139 -0.4958 0.2920  -0.0208 485 ARG B CZ  
7938  N NH1 . ARG B  485 ? 1.7163 1.3916 1.2238 -0.5027 0.3009  -0.0298 485 ARG B NH1 
7939  N NH2 . ARG B  485 ? 1.6625 1.3282 1.1864 -0.4959 0.2924  -0.0235 485 ARG B NH2 
7940  N N   . THR B  486 ? 1.4892 1.0866 0.9464 -0.4439 0.2501  0.0094  486 THR B N   
7941  C CA  . THR B  486 ? 1.5086 1.0993 0.9476 -0.4442 0.2490  0.0120  486 THR B CA  
7942  C C   . THR B  486 ? 1.4793 1.0654 0.9233 -0.4273 0.2384  0.0148  486 THR B C   
7943  O O   . THR B  486 ? 1.5055 1.0739 0.9303 -0.4246 0.2322  0.0231  486 THR B O   
7944  C CB  . THR B  486 ? 1.5061 1.1180 0.9482 -0.4531 0.2603  0.0007  486 THR B CB  
7945  O OG1 . THR B  486 ? 1.5409 1.1665 0.9907 -0.4657 0.2708  -0.0063 486 THR B OG1 
7946  C CG2 . THR B  486 ? 1.5192 1.1208 0.9342 -0.4609 0.2621  0.0048  486 THR B CG2 
7947  N N   . GLY B  487 ? 1.3647 0.9666 0.8345 -0.4160 0.2363  0.0082  487 GLY B N   
7948  C CA  . GLY B  487 ? 1.2911 0.8967 0.7683 -0.4026 0.2301  0.0069  487 GLY B CA  
7949  C C   . GLY B  487 ? 1.2661 0.8889 0.7447 -0.4084 0.2389  -0.0025 487 GLY B C   
7950  O O   . GLY B  487 ? 1.2633 0.8825 0.7325 -0.4047 0.2364  -0.0016 487 GLY B O   
7951  N N   . ASP B  488 ? 1.1862 0.8283 0.6776 -0.4175 0.2492  -0.0121 488 ASP B N   
7952  C CA  . ASP B  488 ? 1.2030 0.8641 0.6980 -0.4251 0.2594  -0.0227 488 ASP B CA  
7953  C C   . ASP B  488 ? 1.1802 0.8615 0.6940 -0.4331 0.2688  -0.0322 488 ASP B C   
7954  O O   . ASP B  488 ? 1.1933 0.8689 0.7003 -0.4426 0.2720  -0.0295 488 ASP B O   
7955  C CB  . ASP B  488 ? 1.4004 1.0503 0.8661 -0.4381 0.2640  -0.0190 488 ASP B CB  
7956  C CG  . ASP B  488 ? 1.4185 1.0874 0.8856 -0.4465 0.2745  -0.0300 488 ASP B CG  
7957  O OD1 . ASP B  488 ? 1.4262 1.1175 0.9125 -0.4514 0.2835  -0.0413 488 ASP B OD1 
7958  O OD2 . ASP B  488 ? 1.4126 1.0742 0.8613 -0.4484 0.2739  -0.0274 488 ASP B OD2 
7959  N N   . PRO B  489 ? 1.1314 0.8365 0.6689 -0.4296 0.2735  -0.0437 489 PRO B N   
7960  C CA  . PRO B  489 ? 1.1170 0.8446 0.6777 -0.4344 0.2815  -0.0540 489 PRO B CA  
7961  C C   . PRO B  489 ? 1.1678 0.9056 0.7214 -0.4519 0.2943  -0.0610 489 PRO B C   
7962  O O   . PRO B  489 ? 1.1776 0.9313 0.7478 -0.4573 0.3006  -0.0682 489 PRO B O   
7963  C CB  . PRO B  489 ? 1.2509 0.9986 0.8365 -0.4242 0.2814  -0.0631 489 PRO B CB  
7964  C CG  . PRO B  489 ? 1.2655 1.0053 0.8361 -0.4211 0.2791  -0.0610 489 PRO B CG  
7965  C CD  . PRO B  489 ? 1.2762 0.9877 0.8209 -0.4194 0.2704  -0.0471 489 PRO B CD  
7966  N N   . ASN B  490 ? 1.2677 0.9982 0.7982 -0.4606 0.2981  -0.0596 490 ASN B N   
7967  C CA  . ASN B  490 ? 1.3394 1.0832 0.8647 -0.4771 0.3112  -0.0681 490 ASN B CA  
7968  C C   . ASN B  490 ? 1.4634 1.1963 0.9710 -0.4914 0.3156  -0.0630 490 ASN B C   
7969  O O   . ASN B  490 ? 1.4503 1.1627 0.9471 -0.4891 0.3082  -0.0518 490 ASN B O   
7970  C CB  . ASN B  490 ? 1.2319 0.9751 0.7408 -0.4810 0.3143  -0.0699 490 ASN B CB  
7971  C CG  . ASN B  490 ? 1.1797 0.9385 0.7080 -0.4699 0.3132  -0.0781 490 ASN B CG  
7972  O OD1 . ASN B  490 ? 1.0905 0.8742 0.6399 -0.4725 0.3216  -0.0914 490 ASN B OD1 
7973  N ND2 . ASN B  490 ? 1.1505 0.8951 0.6724 -0.4576 0.3029  -0.0704 490 ASN B ND2 
7974  N N   . ASP B  491 ? 1.7226 1.4697 1.2278 -0.5065 0.3279  -0.0718 491 ASP B N   
7975  C CA  . ASP B  491 ? 1.8543 1.5917 1.3398 -0.5224 0.3337  -0.0675 491 ASP B CA  
7976  C C   . ASP B  491 ? 1.9391 1.6541 1.3912 -0.5271 0.3306  -0.0569 491 ASP B C   
7977  O O   . ASP B  491 ? 1.9277 1.6451 1.3735 -0.5246 0.3304  -0.0589 491 ASP B O   
7978  C CB  . ASP B  491 ? 1.8467 1.6080 1.3406 -0.5373 0.3483  -0.0811 491 ASP B CB  
7979  C CG  . ASP B  491 ? 1.8205 1.6049 1.3479 -0.5336 0.3517  -0.0917 491 ASP B CG  
7980  O OD1 . ASP B  491 ? 1.7858 1.5816 1.3361 -0.5198 0.3471  -0.0964 491 ASP B OD1 
7981  O OD2 . ASP B  491 ? 1.8263 1.6175 1.3571 -0.5449 0.3590  -0.0953 491 ASP B OD2 
7982  N N   . PRO B  492 ? 1.9919 1.6849 1.4227 -0.5339 0.3278  -0.0454 492 PRO B N   
7983  C CA  . PRO B  492 ? 2.0604 1.7310 1.4579 -0.5401 0.3250  -0.0344 492 PRO B CA  
7984  C C   . PRO B  492 ? 2.1152 1.7977 1.4999 -0.5547 0.3364  -0.0417 492 PRO B C   
7985  O O   . PRO B  492 ? 2.1085 1.7835 1.4752 -0.5547 0.3343  -0.0381 492 PRO B O   
7986  C CB  . PRO B  492 ? 2.0184 1.6702 1.4020 -0.5481 0.3238  -0.0244 492 PRO B CB  
7987  C CG  . PRO B  492 ? 1.9765 1.6342 1.3858 -0.5389 0.3201  -0.0266 492 PRO B CG  
7988  C CD  . PRO B  492 ? 1.9361 1.6240 1.3740 -0.5357 0.3267  -0.0420 492 PRO B CD  
7989  N N   . ARG B  493 ? 2.2033 1.9052 1.5983 -0.5671 0.3485  -0.0524 493 ARG B N   
7990  C CA  . ARG B  493 ? 2.2399 1.9546 1.6234 -0.5835 0.3609  -0.0603 493 ARG B CA  
7991  C C   . ARG B  493 ? 2.2381 1.9848 1.6479 -0.5824 0.3697  -0.0781 493 ARG B C   
7992  O O   . ARG B  493 ? 2.2346 1.9896 1.6399 -0.5831 0.3726  -0.0834 493 ARG B O   
7993  C CB  . ARG B  493 ? 2.1051 1.8166 1.4771 -0.6009 0.3690  -0.0588 493 ARG B CB  
7994  C CG  . ARG B  493 ? 2.0704 1.7863 1.4637 -0.5983 0.3687  -0.0606 493 ARG B CG  
7995  C CD  . ARG B  493 ? 2.0556 1.8010 1.4700 -0.6084 0.3822  -0.0767 493 ARG B CD  
7996  N NE  . ARG B  493 ? 2.0054 1.7613 1.4484 -0.6008 0.3804  -0.0812 493 ARG B NE  
7997  C CZ  . ARG B  493 ? 1.9695 1.7511 1.4357 -0.6065 0.3901  -0.0949 493 ARG B CZ  
7998  N NH1 . ARG B  493 ? 1.9819 1.7820 1.4469 -0.6199 0.4026  -0.1061 493 ARG B NH1 
7999  N NH2 . ARG B  493 ? 1.9253 1.7148 1.4164 -0.5988 0.3872  -0.0975 493 ARG B NH2 
8000  N N   . ASP B  494 ? 2.2378 2.0025 1.6754 -0.5806 0.3735  -0.0872 494 ASP B N   
8001  C CA  . ASP B  494 ? 2.2168 2.0136 1.6811 -0.5826 0.3837  -0.1051 494 ASP B CA  
8002  C C   . ASP B  494 ? 2.1710 1.9803 1.6483 -0.5713 0.3817  -0.1123 494 ASP B C   
8003  O O   . ASP B  494 ? 2.1561 1.9569 1.6406 -0.5552 0.3708  -0.1067 494 ASP B O   
8004  C CB  . ASP B  494 ? 2.1187 1.9283 1.6119 -0.5779 0.3840  -0.1105 494 ASP B CB  
8005  C CG  . ASP B  494 ? 2.1052 1.9481 1.6270 -0.5810 0.3947  -0.1289 494 ASP B CG  
8006  O OD1 . ASP B  494 ? 2.1246 1.9808 1.6407 -0.5923 0.4049  -0.1380 494 ASP B OD1 
8007  O OD2 . ASP B  494 ? 2.0707 1.9270 1.6213 -0.5721 0.3927  -0.1345 494 ASP B OD2 
8008  N N   . SER B  495 ? 2.1297 1.9591 1.6096 -0.5804 0.3925  -0.1249 495 SER B N   
8009  C CA  . SER B  495 ? 2.0676 1.9134 1.5636 -0.5714 0.3929  -0.1347 495 SER B CA  
8010  C C   . SER B  495 ? 2.0398 1.9189 1.5597 -0.5791 0.4063  -0.1542 495 SER B C   
8011  O O   . SER B  495 ? 2.0808 1.9665 1.5870 -0.5951 0.4167  -0.1594 495 SER B O   
8012  C CB  . SER B  495 ? 1.9110 1.7432 1.3788 -0.5737 0.3906  -0.1284 495 SER B CB  
8013  O OG  . SER B  495 ? 1.8741 1.7219 1.3563 -0.5657 0.3913  -0.1379 495 SER B OG  
8014  N N   . LYS B  496 ? 1.9020 1.8026 1.4568 -0.5686 0.4067  -0.1655 496 LYS B N   
8015  C CA  . LYS B  496 ? 1.8271 1.7257 1.4041 -0.5504 0.3960  -0.1621 496 LYS B CA  
8016  C C   . LYS B  496 ? 2.0607 1.9393 1.6265 -0.5362 0.3835  -0.1507 496 LYS B C   
8017  O O   . LYS B  496 ? 2.0807 1.9554 1.6298 -0.5387 0.3845  -0.1503 496 LYS B O   
8018  C CB  . LYS B  496 ? 1.6886 1.5786 1.2682 -0.5517 0.3932  -0.1551 496 LYS B CB  
8019  C CG  . LYS B  496 ? 1.6390 1.5552 1.2479 -0.5558 0.4016  -0.1686 496 LYS B CG  
8020  C CD  . LYS B  496 ? 1.5739 1.4918 1.2079 -0.5414 0.3929  -0.1662 496 LYS B CD  
8021  C CE  . LYS B  496 ? 1.5548 1.4442 1.1702 -0.5381 0.3827  -0.1489 496 LYS B CE  
8022  N NZ  . LYS B  496 ? 1.5017 1.3904 1.1388 -0.5223 0.3726  -0.1452 496 LYS B NZ  
8023  N N   . SER B  497 ? 2.0749 1.9415 1.6492 -0.5217 0.3720  -0.1418 497 SER B N   
8024  C CA  . SER B  497 ? 2.0357 1.9159 1.6421 -0.5122 0.3696  -0.1467 497 SER B CA  
8025  C C   . SER B  497 ? 1.9644 1.8753 1.6050 -0.5071 0.3753  -0.1636 497 SER B C   
8026  O O   . SER B  497 ? 1.9556 1.8847 1.6214 -0.5073 0.3792  -0.1719 497 SER B O   
8027  C CB  . SER B  497 ? 1.8254 1.6856 1.4317 -0.4970 0.3553  -0.1333 497 SER B CB  
8028  O OG  . SER B  497 ? 1.7760 1.6444 1.4057 -0.4917 0.3531  -0.1348 497 SER B OG  
8029  N N   . PRO B  498 ? 1.9570 1.8743 1.5997 -0.5023 0.3758  -0.1689 498 PRO B N   
8030  C CA  . PRO B  498 ? 1.9550 1.8565 1.5735 -0.5008 0.3719  -0.1622 498 PRO B CA  
8031  C C   . PRO B  498 ? 1.9235 1.7975 1.5275 -0.4889 0.3578  -0.1455 498 PRO B C   
8032  O O   . PRO B  498 ? 1.9005 1.7731 1.5218 -0.4773 0.3504  -0.1421 498 PRO B O   
8033  C CB  . PRO B  498 ? 1.7911 1.7142 1.4324 -0.4939 0.3750  -0.1756 498 PRO B CB  
8034  C CG  . PRO B  498 ? 1.7847 1.7364 1.4540 -0.4994 0.3853  -0.1915 498 PRO B CG  
8035  C CD  . PRO B  498 ? 1.7896 1.7371 1.4665 -0.4986 0.3821  -0.1859 498 PRO B CD  
8036  N N   . GLN B  499 ? 1.9599 1.8132 1.5331 -0.4919 0.3542  -0.1355 499 GLN B N   
8037  C CA  . GLN B  499 ? 1.8968 1.7220 1.4523 -0.4826 0.3412  -0.1191 499 GLN B CA  
8038  C C   . GLN B  499 ? 1.8054 1.6306 1.3813 -0.4641 0.3313  -0.1173 499 GLN B C   
8039  O O   . GLN B  499 ? 1.7970 1.6355 1.3878 -0.4574 0.3322  -0.1253 499 GLN B O   
8040  C CB  . GLN B  499 ? 1.6733 1.4809 1.1963 -0.4875 0.3393  -0.1112 499 GLN B CB  
8041  C CG  . GLN B  499 ? 1.6971 1.4913 1.1917 -0.5032 0.3435  -0.1044 499 GLN B CG  
8042  C CD  . GLN B  499 ? 1.6884 1.4557 1.1676 -0.4993 0.3332  -0.0885 499 GLN B CD  
8043  O OE1 . GLN B  499 ? 1.6542 1.4062 1.1314 -0.4860 0.3217  -0.0795 499 GLN B OE1 
8044  N NE2 . GLN B  499 ? 1.7158 1.4777 1.1848 -0.5111 0.3375  -0.0853 499 GLN B NE2 
8045  N N   . TRP B  500 ? 1.5188 1.3288 1.0951 -0.4562 0.3220  -0.1069 500 TRP B N   
8046  C CA  . TRP B  500 ? 1.3559 1.1630 0.9485 -0.4390 0.3116  -0.1033 500 TRP B CA  
8047  C C   . TRP B  500 ? 1.2205 1.0052 0.7904 -0.4325 0.3026  -0.0924 500 TRP B C   
8048  O O   . TRP B  500 ? 1.2146 0.9763 0.7622 -0.4334 0.2962  -0.0800 500 TRP B O   
8049  C CB  . TRP B  500 ? 1.4519 1.2524 1.0528 -0.4345 0.3058  -0.0968 500 TRP B CB  
8050  C CG  . TRP B  500 ? 1.4450 1.2422 1.0627 -0.4174 0.2949  -0.0923 500 TRP B CG  
8051  C CD1 . TRP B  500 ? 1.4444 1.2318 1.0592 -0.4053 0.2863  -0.0871 500 TRP B CD1 
8052  C CD2 . TRP B  500 ? 1.4222 1.2261 1.0616 -0.4111 0.2914  -0.0923 500 TRP B CD2 
8053  N NE1 . TRP B  500 ? 1.3968 1.1847 1.0303 -0.3920 0.2779  -0.0842 500 TRP B NE1 
8054  C CE2 . TRP B  500 ? 1.3971 1.1952 1.0457 -0.3953 0.2808  -0.0871 500 TRP B CE2 
8055  C CE3 . TRP B  500 ? 1.4110 1.2258 1.0630 -0.4175 0.2963  -0.0963 500 TRP B CE3 
8056  C CZ2 . TRP B  500 ? 1.3746 1.1775 1.0440 -0.3860 0.2749  -0.0856 500 TRP B CZ2 
8057  C CZ3 . TRP B  500 ? 1.3763 1.1957 1.0490 -0.4081 0.2903  -0.0947 500 TRP B CZ3 
8058  C CH2 . TRP B  500 ? 1.3656 1.1791 1.0466 -0.3926 0.2797  -0.0894 500 TRP B CH2 
8059  N N   . PRO B  501 ? 0.9984 0.7904 0.5750 -0.4258 0.3020  -0.0974 501 PRO B N   
8060  C CA  . PRO B  501 ? 1.0027 0.7772 0.5596 -0.4200 0.2946  -0.0893 501 PRO B CA  
8061  C C   . PRO B  501 ? 0.9798 0.7382 0.5393 -0.4046 0.2813  -0.0789 501 PRO B C   
8062  O O   . PRO B  501 ? 0.9495 0.7177 0.5338 -0.3951 0.2786  -0.0820 501 PRO B O   
8063  C CB  . PRO B  501 ? 1.0075 0.8013 0.5782 -0.4183 0.3003  -0.1013 501 PRO B CB  
8064  C CG  . PRO B  501 ? 0.9682 0.7883 0.5723 -0.4175 0.3072  -0.1143 501 PRO B CG  
8065  C CD  . PRO B  501 ? 0.9706 0.7891 0.5789 -0.4213 0.3074  -0.1112 501 PRO B CD  
8066  N N   . PRO B  502 ? 1.3137 1.0482 0.8484 -0.4018 0.2729  -0.0668 502 PRO B N   
8067  C CA  . PRO B  502 ? 1.3429 1.0634 0.8813 -0.3864 0.2603  -0.0580 502 PRO B CA  
8068  C C   . PRO B  502 ? 1.3384 1.0693 0.8945 -0.3748 0.2578  -0.0635 502 PRO B C   
8069  O O   . PRO B  502 ? 1.4051 1.1407 0.9552 -0.3774 0.2615  -0.0682 502 PRO B O   
8070  C CB  . PRO B  502 ? 1.3351 1.0298 0.8423 -0.3877 0.2532  -0.0455 502 PRO B CB  
8071  C CG  . PRO B  502 ? 1.3673 1.0597 0.8567 -0.4039 0.2611  -0.0451 502 PRO B CG  
8072  C CD  . PRO B  502 ? 1.3494 1.0674 0.8524 -0.4129 0.2739  -0.0595 502 PRO B CD  
8073  N N   . TYR B  503 ? 1.0332 0.7679 0.6108 -0.3627 0.2518  -0.0631 503 TYR B N   
8074  C CA  . TYR B  503 ? 0.9782 0.7199 0.5722 -0.3505 0.2479  -0.0665 503 TYR B CA  
8075  C C   . TYR B  503 ? 0.9884 0.7095 0.5607 -0.3447 0.2393  -0.0573 503 TYR B C   
8076  O O   . TYR B  503 ? 0.9959 0.6969 0.5531 -0.3414 0.2308  -0.0462 503 TYR B O   
8077  C CB  . TYR B  503 ? 1.0068 0.7531 0.6246 -0.3388 0.2416  -0.0651 503 TYR B CB  
8078  C CG  . TYR B  503 ? 0.9594 0.7131 0.5960 -0.3258 0.2372  -0.0680 503 TYR B CG  
8079  C CD1 . TYR B  503 ? 0.9535 0.7306 0.6153 -0.3253 0.2442  -0.0799 503 TYR B CD1 
8080  C CD2 . TYR B  503 ? 0.9436 0.6813 0.5740 -0.3139 0.2260  -0.0590 503 TYR B CD2 
8081  C CE1 . TYR B  503 ? 0.9367 0.7204 0.6163 -0.3137 0.2403  -0.0824 503 TYR B CE1 
8082  C CE2 . TYR B  503 ? 0.9239 0.6681 0.5712 -0.3024 0.2221  -0.0615 503 TYR B CE2 
8083  C CZ  . TYR B  503 ? 0.9030 0.6699 0.5747 -0.3025 0.2294  -0.0729 503 TYR B CZ  
8084  O OH  . TYR B  503 ? 0.8260 0.5992 0.5151 -0.2914 0.2258  -0.0752 503 TYR B OH  
8085  N N   . THR B  504 ? 1.0740 0.8006 0.6452 -0.3438 0.2418  -0.0624 504 THR B N   
8086  C CA  . THR B  504 ? 1.0757 0.7851 0.6293 -0.3372 0.2335  -0.0548 504 THR B CA  
8087  C C   . THR B  504 ? 1.0537 0.7726 0.6268 -0.3258 0.2313  -0.0600 504 THR B C   
8088  O O   . THR B  504 ? 1.0411 0.7809 0.6389 -0.3253 0.2378  -0.0705 504 THR B O   
8089  C CB  . THR B  504 ? 1.1245 0.8290 0.6531 -0.3479 0.2382  -0.0548 504 THR B CB  
8090  O OG1 . THR B  504 ? 1.1114 0.8354 0.6515 -0.3505 0.2466  -0.0668 504 THR B OG1 
8091  C CG2 . THR B  504 ? 1.1700 0.8720 0.6834 -0.3622 0.2443  -0.0534 504 THR B CG2 
8092  N N   . THR B  505 ? 0.9892 0.6929 0.5520 -0.3165 0.2219  -0.0527 505 THR B N   
8093  C CA  . THR B  505 ? 0.9790 0.6894 0.5589 -0.3054 0.2190  -0.0564 505 THR B CA  
8094  C C   . THR B  505 ? 0.9777 0.7046 0.5632 -0.3106 0.2284  -0.0678 505 THR B C   
8095  O O   . THR B  505 ? 0.9280 0.6684 0.5353 -0.3040 0.2302  -0.0751 505 THR B O   
8096  C CB  . THR B  505 ? 1.1580 0.8475 0.7237 -0.2949 0.2068  -0.0459 505 THR B CB  
8097  O OG1 . THR B  505 ? 1.2056 0.8756 0.7451 -0.2995 0.2020  -0.0359 505 THR B OG1 
8098  C CG2 . THR B  505 ? 1.1395 0.8280 0.7240 -0.2814 0.1984  -0.0424 505 THR B CG2 
8099  N N   . ALA B  506 ? 1.1376 0.8641 0.7039 -0.3224 0.2347  -0.0695 506 ALA B N   
8100  C CA  . ALA B  506 ? 1.1577 0.9008 0.7280 -0.3281 0.2439  -0.0806 506 ALA B CA  
8101  C C   . ALA B  506 ? 1.2085 0.9767 0.8005 -0.3361 0.2559  -0.0938 506 ALA B C   
8102  O O   . ALA B  506 ? 1.2116 0.9988 0.8299 -0.3319 0.2604  -0.1044 506 ALA B O   
8103  C CB  . ALA B  506 ? 1.0997 0.8320 0.6394 -0.3367 0.2445  -0.0764 506 ALA B CB  
8104  N N   . ALA B  507 ? 1.2844 1.0526 0.8660 -0.3476 0.2610  -0.0933 507 ALA B N   
8105  C CA  . ALA B  507 ? 1.2961 1.0877 0.8964 -0.3563 0.2725  -0.1058 507 ALA B CA  
8106  C C   . ALA B  507 ? 1.2477 1.0519 0.8794 -0.3487 0.2719  -0.1101 507 ALA B C   
8107  O O   . ALA B  507 ? 1.2373 1.0650 0.8951 -0.3491 0.2795  -0.1231 507 ALA B O   
8108  C CB  . ALA B  507 ? 1.3183 1.1045 0.8987 -0.3701 0.2772  -0.1027 507 ALA B CB  
8109  N N   . GLN B  508 ? 1.0724 0.8612 0.7016 -0.3416 0.2626  -0.0992 508 GLN B N   
8110  C CA  . GLN B  508 ? 0.9701 0.7680 0.6256 -0.3342 0.2603  -0.1006 508 GLN B CA  
8111  C C   . GLN B  508 ? 0.9158 0.7320 0.5858 -0.3435 0.2697  -0.1093 508 GLN B C   
8112  O O   . GLN B  508 ? 0.8529 0.6881 0.5521 -0.3394 0.2725  -0.1175 508 GLN B O   
8113  C CB  . GLN B  508 ? 1.0098 0.8194 0.6908 -0.3225 0.2583  -0.1062 508 GLN B CB  
8114  C CG  . GLN B  508 ? 1.0162 0.8073 0.6873 -0.3111 0.2473  -0.0964 508 GLN B CG  
8115  C CD  . GLN B  508 ? 1.0047 0.8076 0.7022 -0.3000 0.2457  -0.1018 508 GLN B CD  
8116  O OE1 . GLN B  508 ? 1.0021 0.8024 0.7127 -0.2898 0.2383  -0.0967 508 GLN B OE1 
8117  N NE2 . GLN B  508 ? 0.9929 0.8098 0.6995 -0.3018 0.2527  -0.1124 508 GLN B NE2 
8118  N N   . GLN B  509 ? 1.0558 0.8665 0.7058 -0.3559 0.2743  -0.1074 509 GLN B N   
8119  C CA  . GLN B  509 ? 1.0811 0.9086 0.7430 -0.3657 0.2835  -0.1157 509 GLN B CA  
8120  C C   . GLN B  509 ? 1.0605 0.8845 0.7322 -0.3615 0.2783  -0.1098 509 GLN B C   
8121  O O   . GLN B  509 ? 1.0430 0.8460 0.6973 -0.3591 0.2702  -0.0975 509 GLN B O   
8122  C CB  . GLN B  509 ? 1.1427 0.9661 0.7798 -0.3813 0.2908  -0.1160 509 GLN B CB  
8123  C CG  . GLN B  509 ? 1.1549 0.9826 0.7807 -0.3866 0.2962  -0.1218 509 GLN B CG  
8124  C CD  . GLN B  509 ? 1.1861 1.0308 0.8109 -0.4017 0.3092  -0.1329 509 GLN B CD  
8125  O OE1 . GLN B  509 ? 1.2055 1.0434 0.8135 -0.4126 0.3123  -0.1289 509 GLN B OE1 
8126  N NE2 . GLN B  509 ? 1.1722 1.0397 0.8159 -0.4025 0.3170  -0.1472 509 GLN B NE2 
8127  N N   . TYR B  510 ? 0.9528 0.7983 0.6538 -0.3603 0.2827  -0.1190 510 TYR B N   
8128  C CA  . TYR B  510 ? 0.9330 0.7796 0.6447 -0.3590 0.2800  -0.1155 510 TYR B CA  
8129  C C   . TYR B  510 ? 0.9525 0.8208 0.6791 -0.3697 0.2911  -0.1272 510 TYR B C   
8130  O O   . TYR B  510 ? 0.9616 0.8473 0.6978 -0.3745 0.2998  -0.1392 510 TYR B O   
8131  C CB  . TYR B  510 ? 0.8695 0.7198 0.6045 -0.3441 0.2716  -0.1132 510 TYR B CB  
8132  C CG  . TYR B  510 ? 0.8277 0.7030 0.5951 -0.3391 0.2758  -0.1255 510 TYR B CG  
8133  C CD1 . TYR B  510 ? 0.8105 0.6912 0.5810 -0.3364 0.2783  -0.1317 510 TYR B CD1 
8134  C CD2 . TYR B  510 ? 0.8168 0.7100 0.6125 -0.3365 0.2768  -0.1307 510 TYR B CD2 
8135  C CE1 . TYR B  510 ? 0.7925 0.6958 0.5942 -0.3313 0.2818  -0.1432 510 TYR B CE1 
8136  C CE2 . TYR B  510 ? 0.7155 0.6314 0.5424 -0.3312 0.2798  -0.1416 510 TYR B CE2 
8137  C CZ  . TYR B  510 ? 0.7773 0.6981 0.6075 -0.3285 0.2824  -0.1480 510 TYR B CZ  
8138  O OH  . TYR B  510 ? 0.7493 0.6925 0.6118 -0.3228 0.2853  -0.1594 510 TYR B OH  
8139  N N   . VAL B  511 ? 1.0752 0.9434 0.8046 -0.3734 0.2911  -0.1244 511 VAL B N   
8140  C CA  . VAL B  511 ? 1.1001 0.9880 0.8418 -0.3845 0.3017  -0.1352 511 VAL B CA  
8141  C C   . VAL B  511 ? 1.0713 0.9784 0.8463 -0.3784 0.3011  -0.1408 511 VAL B C   
8142  O O   . VAL B  511 ? 1.0688 0.9699 0.8524 -0.3677 0.2917  -0.1334 511 VAL B O   
8143  C CB  . VAL B  511 ? 0.9951 0.8704 0.7124 -0.3976 0.3050  -0.1296 511 VAL B CB  
8144  C CG1 . VAL B  511 ? 1.0177 0.8652 0.7018 -0.3978 0.2986  -0.1168 511 VAL B CG1 
8145  C CG2 . VAL B  511 ? 0.9753 0.8510 0.7029 -0.3969 0.3021  -0.1259 511 VAL B CG2 
8146  N N   . SER B  512 ? 0.9093 0.8403 0.7038 -0.3852 0.3109  -0.1543 512 SER B N   
8147  C CA  . SER B  512 ? 0.8875 0.8387 0.7145 -0.3808 0.3110  -0.1605 512 SER B CA  
8148  C C   . SER B  512 ? 0.9358 0.8869 0.7587 -0.3905 0.3142  -0.1589 512 SER B C   
8149  O O   . SER B  512 ? 0.9813 0.9340 0.7907 -0.4039 0.3231  -0.1633 512 SER B O   
8150  C CB  . SER B  512 ? 0.9383 0.9170 0.7919 -0.3818 0.3197  -0.1771 512 SER B CB  
8151  O OG  . SER B  512 ? 0.9456 0.9455 0.8278 -0.3822 0.3225  -0.1849 512 SER B OG  
8152  N N   . LEU B  513 ? 0.9568 0.9060 0.7907 -0.3842 0.3070  -0.1525 513 LEU B N   
8153  C CA  . LEU B  513 ? 0.9625 0.9135 0.7957 -0.3931 0.3099  -0.1517 513 LEU B CA  
8154  C C   . LEU B  513 ? 0.9446 0.9234 0.8128 -0.3925 0.3138  -0.1629 513 LEU B C   
8155  O O   . LEU B  513 ? 0.8838 0.8691 0.7733 -0.3825 0.3066  -0.1608 513 LEU B O   
8156  C CB  . LEU B  513 ? 0.8902 0.8193 0.7097 -0.3883 0.2996  -0.1371 513 LEU B CB  
8157  C CG  . LEU B  513 ? 0.8238 0.7241 0.6097 -0.3880 0.2942  -0.1250 513 LEU B CG  
8158  C CD1 . LEU B  513 ? 0.8205 0.7027 0.5981 -0.3828 0.2843  -0.1125 513 LEU B CD1 
8159  C CD2 . LEU B  513 ? 0.8597 0.7527 0.6205 -0.4027 0.3028  -0.1263 513 LEU B CD2 
8160  N N   . ASN B  514 ? 1.1722 1.1673 1.0455 -0.4041 0.3252  -0.1745 514 ASN B N   
8161  C CA  . ASN B  514 ? 1.2278 1.2517 1.1356 -0.4035 0.3301  -0.1876 514 ASN B CA  
8162  C C   . ASN B  514 ? 1.3026 1.3347 1.2086 -0.4178 0.3390  -0.1929 514 ASN B C   
8163  O O   . ASN B  514 ? 1.3507 1.3655 1.2280 -0.4278 0.3414  -0.1865 514 ASN B O   
8164  C CB  . ASN B  514 ? 1.1832 1.2232 1.1037 -0.4022 0.3364  -0.2002 514 ASN B CB  
8165  C CG  . ASN B  514 ? 1.1839 1.2490 1.1444 -0.3926 0.3350  -0.2099 514 ASN B CG  
8166  O OD1 . ASN B  514 ? 1.1786 1.2593 1.1605 -0.3938 0.3359  -0.2143 514 ASN B OD1 
8167  N ND2 . ASN B  514 ? 1.1746 1.2438 1.1461 -0.3829 0.3323  -0.2132 514 ASN B ND2 
8168  N N   . LEU B  515 ? 1.2797 1.3378 1.2159 -0.4190 0.3438  -0.2047 515 LEU B N   
8169  C CA  . LEU B  515 ? 1.2941 1.3620 1.2292 -0.4334 0.3537  -0.2117 515 LEU B CA  
8170  C C   . LEU B  515 ? 1.3297 1.4015 1.2512 -0.4441 0.3648  -0.2208 515 LEU B C   
8171  O O   . LEU B  515 ? 1.3619 1.4233 1.2581 -0.4574 0.3709  -0.2186 515 LEU B O   
8172  C CB  . LEU B  515 ? 1.1227 1.2185 1.0948 -0.4319 0.3559  -0.2225 515 LEU B CB  
8173  C CG  . LEU B  515 ? 1.0629 1.1681 1.0647 -0.4170 0.3455  -0.2204 515 LEU B CG  
8174  C CD1 . LEU B  515 ? 1.0540 1.1744 1.0786 -0.4069 0.3451  -0.2293 515 LEU B CD1 
8175  C CD2 . LEU B  515 ? 1.0148 1.1386 1.0410 -0.4200 0.3468  -0.2256 515 LEU B CD2 
8176  N N   . LYS B  516 ? 1.3502 1.4369 1.2886 -0.4383 0.3671  -0.2309 516 LYS B N   
8177  C CA  . LYS B  516 ? 1.3453 1.4350 1.2706 -0.4468 0.3764  -0.2393 516 LYS B CA  
8178  C C   . LYS B  516 ? 1.3599 1.4195 1.2459 -0.4491 0.3725  -0.2254 516 LYS B C   
8179  O O   . LYS B  516 ? 1.3682 1.4093 1.2460 -0.4391 0.3616  -0.2125 516 LYS B O   
8180  C CB  . LYS B  516 ? 1.1570 1.2669 1.1094 -0.4380 0.3779  -0.2520 516 LYS B CB  
8181  C CG  . LYS B  516 ? 1.1683 1.2666 1.1212 -0.4231 0.3676  -0.2443 516 LYS B CG  
8182  C CD  . LYS B  516 ? 1.1756 1.2970 1.1622 -0.4137 0.3687  -0.2579 516 LYS B CD  
8183  C CE  . LYS B  516 ? 1.1679 1.2776 1.1469 -0.4039 0.3630  -0.2536 516 LYS B CE  
8184  N NZ  . LYS B  516 ? 1.1359 1.2239 1.1049 -0.3928 0.3501  -0.2369 516 LYS B NZ  
8185  N N   . PRO B  517 ? 1.2709 1.3255 1.1325 -0.4624 0.3810  -0.2279 517 PRO B N   
8186  C CA  . PRO B  517 ? 1.2646 1.2899 1.0868 -0.4674 0.3777  -0.2139 517 PRO B CA  
8187  C C   . PRO B  517 ? 1.2540 1.2631 1.0648 -0.4562 0.3690  -0.2057 517 PRO B C   
8188  O O   . PRO B  517 ? 1.2203 1.2415 1.0520 -0.4458 0.3671  -0.2122 517 PRO B O   
8189  C CB  . PRO B  517 ? 1.2028 1.2333 1.0083 -0.4840 0.3899  -0.2217 517 PRO B CB  
8190  C CG  . PRO B  517 ? 1.2090 1.2687 1.0435 -0.4827 0.3975  -0.2398 517 PRO B CG  
8191  C CD  . PRO B  517 ? 1.2027 1.2796 1.0734 -0.4727 0.3937  -0.2445 517 PRO B CD  
8192  N N   . LEU B  518 ? 1.2107 1.1923 0.9885 -0.4586 0.3639  -0.1914 518 LEU B N   
8193  C CA  . LEU B  518 ? 1.1915 1.1529 0.9545 -0.4481 0.3541  -0.1806 518 LEU B CA  
8194  C C   . LEU B  518 ? 1.1987 1.1707 0.9686 -0.4442 0.3569  -0.1895 518 LEU B C   
8195  O O   . LEU B  518 ? 1.1853 1.1669 0.9489 -0.4547 0.3665  -0.1986 518 LEU B O   
8196  C CB  . LEU B  518 ? 1.2245 1.1583 0.9484 -0.4562 0.3519  -0.1674 518 LEU B CB  
8197  C CG  . LEU B  518 ? 1.1950 1.0997 0.8978 -0.4475 0.3394  -0.1505 518 LEU B CG  
8198  C CD1 . LEU B  518 ? 1.1889 1.0876 0.8871 -0.4381 0.3344  -0.1488 518 LEU B CD1 
8199  C CD2 . LEU B  518 ? 1.1497 1.0510 0.8677 -0.4375 0.3308  -0.1440 518 LEU B CD2 
8200  N N   . GLU B  519 ? 1.4537 1.4247 1.2375 -0.4293 0.3485  -0.1870 519 GLU B N   
8201  C CA  . GLU B  519 ? 1.4780 1.4555 1.2676 -0.4236 0.3492  -0.1935 519 GLU B CA  
8202  C C   . GLU B  519 ? 1.4317 1.3845 1.2013 -0.4144 0.3386  -0.1798 519 GLU B C   
8203  O O   . GLU B  519 ? 1.4370 1.3746 1.2032 -0.4065 0.3289  -0.1680 519 GLU B O   
8204  C CB  . GLU B  519 ? 1.4149 1.4167 1.2445 -0.4130 0.3492  -0.2049 519 GLU B CB  
8205  C CG  . GLU B  519 ? 1.4440 1.4745 1.2967 -0.4204 0.3607  -0.2228 519 GLU B CG  
8206  C CD  . GLU B  519 ? 1.4413 1.4934 1.3306 -0.4088 0.3600  -0.2343 519 GLU B CD  
8207  O OE1 . GLU B  519 ? 1.4067 1.4505 1.2996 -0.3963 0.3515  -0.2284 519 GLU B OE1 
8208  O OE2 . GLU B  519 ? 1.4686 1.5461 1.3838 -0.4119 0.3677  -0.2492 519 GLU B OE2 
8209  N N   . VAL B  520 ? 1.1554 1.1049 0.9124 -0.4151 0.3401  -0.1817 520 VAL B N   
8210  C CA  . VAL B  520 ? 1.1401 1.0679 0.8803 -0.4058 0.3302  -0.1699 520 VAL B CA  
8211  C C   . VAL B  520 ? 1.1334 1.0734 0.8961 -0.3943 0.3284  -0.1773 520 VAL B C   
8212  O O   . VAL B  520 ? 1.1641 1.1199 0.9345 -0.3980 0.3360  -0.1894 520 VAL B O   
8213  C CB  . VAL B  520 ? 0.9078 0.8172 0.6111 -0.4149 0.3312  -0.1632 520 VAL B CB  
8214  C CG1 . VAL B  520 ? 0.8979 0.7886 0.5878 -0.4044 0.3215  -0.1534 520 VAL B CG1 
8215  C CG2 . VAL B  520 ? 0.9344 0.8270 0.6138 -0.4243 0.3307  -0.1531 520 VAL B CG2 
8216  N N   . ARG B  521 ? 1.0360 0.9695 0.8102 -0.3805 0.3185  -0.1703 521 ARG B N   
8217  C CA  . ARG B  521 ? 0.9905 0.9303 0.7812 -0.3690 0.3152  -0.1744 521 ARG B CA  
8218  C C   . ARG B  521 ? 0.9653 0.8796 0.7302 -0.3632 0.3063  -0.1615 521 ARG B C   
8219  O O   . ARG B  521 ? 0.9303 0.8225 0.6670 -0.3668 0.3018  -0.1492 521 ARG B O   
8220  C CB  . ARG B  521 ? 1.0855 1.0384 0.9104 -0.3572 0.3106  -0.1770 521 ARG B CB  
8221  C CG  . ARG B  521 ? 1.1117 1.0803 0.9552 -0.3619 0.3149  -0.1823 521 ARG B CG  
8222  C CD  . ARG B  521 ? 1.1113 1.0980 0.9930 -0.3504 0.3113  -0.1876 521 ARG B CD  
8223  N NE  . ARG B  521 ? 1.1363 1.1335 1.0333 -0.3530 0.3122  -0.1887 521 ARG B NE  
8224  C CZ  . ARG B  521 ? 1.1541 1.1735 1.0697 -0.3601 0.3212  -0.2016 521 ARG B CZ  
8225  N NH1 . ARG B  521 ? 1.1688 1.2032 1.0906 -0.3655 0.3303  -0.2152 521 ARG B NH1 
8226  N NH2 . ARG B  521 ? 1.1423 1.1697 1.0708 -0.3619 0.3209  -0.2014 521 ARG B NH2 
8227  N N   . ARG B  522 ? 1.1261 1.0435 0.9013 -0.3539 0.3036  -0.1644 522 ARG B N   
8228  C CA  . ARG B  522 ? 1.1593 1.0542 0.9134 -0.3471 0.2948  -0.1530 522 ARG B CA  
8229  C C   . ARG B  522 ? 1.1215 1.0195 0.8990 -0.3322 0.2876  -0.1520 522 ARG B C   
8230  O O   . ARG B  522 ? 1.1157 1.0356 0.9253 -0.3282 0.2911  -0.1627 522 ARG B O   
8231  C CB  . ARG B  522 ? 1.2348 1.1294 0.9736 -0.3521 0.2994  -0.1575 522 ARG B CB  
8232  C CG  . ARG B  522 ? 1.3394 1.2264 1.0490 -0.3666 0.3049  -0.1556 522 ARG B CG  
8233  C CD  . ARG B  522 ? 1.4225 1.3039 1.1121 -0.3696 0.3063  -0.1560 522 ARG B CD  
8234  N NE  . ARG B  522 ? 1.4744 1.3784 1.1871 -0.3673 0.3127  -0.1710 522 ARG B NE  
8235  C CZ  . ARG B  522 ? 1.4979 1.4000 1.2119 -0.3593 0.3093  -0.1715 522 ARG B CZ  
8236  N NH1 . ARG B  522 ? 1.5181 1.3962 1.2108 -0.3530 0.2993  -0.1578 522 ARG B NH1 
8237  N NH2 . ARG B  522 ? 1.4717 1.3960 1.2091 -0.3574 0.3155  -0.1862 522 ARG B NH2 
8238  N N   . GLY B  523 ? 1.0530 0.9297 0.8157 -0.3238 0.2773  -0.1395 523 GLY B N   
8239  C CA  . GLY B  523 ? 0.9963 0.8750 0.7793 -0.3098 0.2704  -0.1381 523 GLY B CA  
8240  C C   . GLY B  523 ? 0.9626 0.8509 0.7715 -0.3031 0.2666  -0.1373 523 GLY B C   
8241  O O   . GLY B  523 ? 0.9551 0.8641 0.7954 -0.2984 0.2693  -0.1469 523 GLY B O   
8242  N N   . LEU B  524 ? 0.9134 0.7882 0.7105 -0.3031 0.2606  -0.1265 524 LEU B N   
8243  C CA  . LEU B  524 ? 0.8716 0.7530 0.6905 -0.2959 0.2551  -0.1235 524 LEU B CA  
8244  C C   . LEU B  524 ? 0.8758 0.7578 0.7111 -0.2821 0.2476  -0.1212 524 LEU B C   
8245  O O   . LEU B  524 ? 0.8864 0.7493 0.7051 -0.2757 0.2395  -0.1111 524 LEU B O   
8246  C CB  . LEU B  524 ? 0.6765 0.5372 0.4739 -0.2960 0.2476  -0.1101 524 LEU B CB  
8247  C CG  . LEU B  524 ? 0.6728 0.5365 0.4777 -0.2976 0.2456  -0.1067 524 LEU B CG  
8248  C CD1 . LEU B  524 ? 0.6855 0.5248 0.4645 -0.2968 0.2377  -0.0935 524 LEU B CD1 
8249  C CD2 . LEU B  524 ? 0.6422 0.5197 0.4778 -0.2874 0.2406  -0.1076 524 LEU B CD2 
8250  N N   . ARG B  525 ? 0.9159 0.8192 0.7847 -0.2770 0.2493  -0.1296 525 ARG B N   
8251  C CA  . ARG B  525 ? 0.8946 0.7996 0.7798 -0.2648 0.2433  -0.1287 525 ARG B CA  
8252  C C   . ARG B  525 ? 0.8722 0.7695 0.7442 -0.2643 0.2455  -0.1312 525 ARG B C   
8253  O O   . ARG B  525 ? 0.8811 0.7942 0.7667 -0.2671 0.2536  -0.1437 525 ARG B O   
8254  C CB  . ARG B  525 ? 0.8277 0.7229 0.7164 -0.2545 0.2312  -0.1164 525 ARG B CB  
8255  C CG  . ARG B  525 ? 0.8489 0.7579 0.7589 -0.2543 0.2298  -0.1169 525 ARG B CG  
8256  C CD  . ARG B  525 ? 1.0129 0.9472 0.9475 -0.2604 0.2397  -0.1312 525 ARG B CD  
8257  N NE  . ARG B  525 ? 0.9990 0.9517 0.9679 -0.2520 0.2386  -0.1385 525 ARG B NE  
8258  C CZ  . ARG B  525 ? 0.9506 0.9197 0.9490 -0.2476 0.2354  -0.1406 525 ARG B CZ  
8259  N NH1 . ARG B  525 ? 0.9325 0.9028 0.9300 -0.2514 0.2337  -0.1364 525 ARG B NH1 
8260  N NH2 . ARG B  525 ? 0.9043 0.8889 0.9337 -0.2394 0.2336  -0.1468 525 ARG B NH2 
8261  N N   . ALA B  526 ? 0.7653 0.6399 0.6131 -0.2600 0.2379  -0.1199 526 ALA B N   
8262  C CA  . ALA B  526 ? 0.7510 0.6172 0.5877 -0.2574 0.2379  -0.1207 526 ALA B CA  
8263  C C   . ALA B  526 ? 0.8176 0.6945 0.6825 -0.2465 0.2352  -0.1246 526 ALA B C   
8264  O O   . ALA B  526 ? 0.8346 0.7018 0.7018 -0.2365 0.2253  -0.1151 526 ALA B O   
8265  C CB  . ALA B  526 ? 0.6215 0.4926 0.4459 -0.2686 0.2483  -0.1301 526 ALA B CB  
8266  N N   . GLN B  527 ? 1.0752 0.9705 0.9605 -0.2477 0.2430  -0.1381 527 GLN B N   
8267  C CA  . GLN B  527 ? 1.0884 0.9976 1.0084 -0.2370 0.2398  -0.1422 527 GLN B CA  
8268  C C   . GLN B  527 ? 1.0960 1.0111 1.0327 -0.2331 0.2339  -0.1368 527 GLN B C   
8269  O O   . GLN B  527 ? 1.1590 1.0795 1.0931 -0.2406 0.2377  -0.1384 527 GLN B O   
8270  C CB  . GLN B  527 ? 0.9597 0.8930 0.9071 -0.2386 0.2491  -0.1595 527 GLN B CB  
8271  C CG  . GLN B  527 ? 0.9746 0.9055 0.9148 -0.2387 0.2529  -0.1654 527 GLN B CG  
8272  C CD  . GLN B  527 ? 1.0159 0.9437 0.9289 -0.2511 0.2613  -0.1700 527 GLN B CD  
8273  O OE1 . GLN B  527 ? 1.0305 0.9574 0.9350 -0.2525 0.2647  -0.1751 527 GLN B OE1 
8274  N NE2 . GLN B  527 ? 1.0251 0.9521 0.9251 -0.2601 0.2641  -0.1681 527 GLN B NE2 
8275  N N   . THR B  528 ? 0.8710 0.7846 0.8235 -0.2217 0.2242  -0.1300 528 THR B N   
8276  C CA  . THR B  528 ? 0.8252 0.7400 0.7892 -0.2162 0.2153  -0.1215 528 THR B CA  
8277  C C   . THR B  528 ? 0.7992 0.6915 0.7332 -0.2160 0.2077  -0.1071 528 THR B C   
8278  O O   . THR B  528 ? 0.8083 0.6963 0.7481 -0.2079 0.1974  -0.0978 528 THR B O   
8279  C CB  . THR B  528 ? 0.5735 0.5086 0.5580 -0.2218 0.2205  -0.1291 528 THR B CB  
8280  O OG1 . THR B  528 ? 0.5659 0.5227 0.5890 -0.2159 0.2206  -0.1381 528 THR B OG1 
8281  C CG2 . THR B  528 ? 0.4845 0.4146 0.4646 -0.2214 0.2135  -0.1189 528 THR B CG2 
8282  N N   . CYS B  529 ? 0.7273 0.6047 0.6295 -0.2238 0.2115  -0.1049 529 CYS B N   
8283  C CA  . CYS B  529 ? 0.6891 0.5453 0.5660 -0.2216 0.2028  -0.0916 529 CYS B CA  
8284  C C   . CYS B  529 ? 0.6696 0.5078 0.5283 -0.2157 0.1973  -0.0853 529 CYS B C   
8285  O O   . CYS B  529 ? 0.6473 0.4696 0.4910 -0.2103 0.1880  -0.0744 529 CYS B O   
8286  C CB  . CYS B  529 ? 0.6832 0.5318 0.5371 -0.2324 0.2072  -0.0902 529 CYS B CB  
8287  S SG  . CYS B  529 ? 0.7389 0.5935 0.6036 -0.2328 0.2030  -0.0855 529 CYS B SG  
8288  N N   . ALA B  530 ? 0.6693 0.5114 0.5310 -0.2165 0.2030  -0.0929 530 ALA B N   
8289  C CA  . ALA B  530 ? 0.6584 0.4846 0.5043 -0.2112 0.1983  -0.0880 530 ALA B CA  
8290  C C   . ALA B  530 ? 0.6647 0.4960 0.5348 -0.1986 0.1896  -0.0845 530 ALA B C   
8291  O O   . ALA B  530 ? 0.6688 0.4866 0.5298 -0.1905 0.1807  -0.0761 530 ALA B O   
8292  C CB  . ALA B  530 ? 0.5789 0.4086 0.4199 -0.2174 0.2080  -0.0981 530 ALA B CB  
8293  N N   . PHE B  531 ? 0.8945 0.7464 0.7968 -0.1969 0.1916  -0.0911 531 PHE B N   
8294  C CA  . PHE B  531 ? 0.8668 0.7254 0.7948 -0.1854 0.1823  -0.0873 531 PHE B CA  
8295  C C   . PHE B  531 ? 0.8670 0.7134 0.7832 -0.1799 0.1710  -0.0741 531 PHE B C   
8296  O O   . PHE B  531 ? 0.9228 0.7572 0.8310 -0.1716 0.1620  -0.0661 531 PHE B O   
8297  C CB  . PHE B  531 ? 0.5112 0.3933 0.4733 -0.1858 0.1855  -0.0956 531 PHE B CB  
8298  C CG  . PHE B  531 ? 0.4165 0.3052 0.4035 -0.1751 0.1744  -0.0901 531 PHE B CG  
8299  C CD1 . PHE B  531 ? 0.4261 0.3160 0.4289 -0.1661 0.1691  -0.0903 531 PHE B CD1 
8300  C CD2 . PHE B  531 ? 0.4752 0.3691 0.4700 -0.1743 0.1690  -0.0848 531 PHE B CD2 
8301  C CE1 . PHE B  531 ? 0.3954 0.2913 0.4203 -0.1564 0.1579  -0.0847 531 PHE B CE1 
8302  C CE2 . PHE B  531 ? 0.4228 0.3230 0.4393 -0.1652 0.1583  -0.0794 531 PHE B CE2 
8303  C CZ  . PHE B  531 ? 0.3900 0.2909 0.4209 -0.1563 0.1526  -0.0791 531 PHE B CZ  
8304  N N   . TRP B  532 ? 0.5197 0.3698 0.4346 -0.1848 0.1718  -0.0726 532 TRP B N   
8305  C CA  . TRP B  532 ? 0.4768 0.3192 0.3852 -0.1803 0.1618  -0.0619 532 TRP B CA  
8306  C C   . TRP B  532 ? 0.4971 0.3179 0.3755 -0.1783 0.1566  -0.0534 532 TRP B C   
8307  O O   . TRP B  532 ? 0.4878 0.3023 0.3658 -0.1693 0.1460  -0.0451 532 TRP B O   
8308  C CB  . TRP B  532 ? 0.4602 0.3107 0.3721 -0.1876 0.1654  -0.0634 532 TRP B CB  
8309  C CG  . TRP B  532 ? 0.4445 0.3162 0.3883 -0.1871 0.1665  -0.0691 532 TRP B CG  
8310  C CD1 . TRP B  532 ? 0.4491 0.3368 0.4075 -0.1943 0.1765  -0.0800 532 TRP B CD1 
8311  C CD2 . TRP B  532 ? 0.4225 0.3023 0.3881 -0.1789 0.1568  -0.0642 532 TRP B CD2 
8312  N NE1 . TRP B  532 ? 0.4311 0.3363 0.4199 -0.1905 0.1733  -0.0823 532 TRP B NE1 
8313  C CE2 . TRP B  532 ? 0.4151 0.3152 0.4079 -0.1815 0.1611  -0.0723 532 TRP B CE2 
8314  C CE3 . TRP B  532 ? 0.4424 0.3150 0.4072 -0.1699 0.1447  -0.0542 532 TRP B CE3 
8315  C CZ2 . TRP B  532 ? 0.3959 0.3075 0.4136 -0.1756 0.1531  -0.0698 532 TRP B CZ2 
8316  C CZ3 . TRP B  532 ? 0.3900 0.2745 0.3789 -0.1646 0.1373  -0.0519 532 TRP B CZ3 
8317  C CH2 . TRP B  532 ? 0.3841 0.2872 0.3983 -0.1676 0.1413  -0.0593 532 TRP B CH2 
8318  N N   . ASN B  533 ? 0.4898 0.3000 0.3438 -0.1867 0.1634  -0.0555 533 ASN B N   
8319  C CA  . ASN B  533 ? 0.5042 0.2939 0.3301 -0.1853 0.1580  -0.0476 533 ASN B CA  
8320  C C   . ASN B  533 ? 0.5256 0.3042 0.3418 -0.1788 0.1539  -0.0452 533 ASN B C   
8321  O O   . ASN B  533 ? 0.5324 0.2992 0.3387 -0.1713 0.1444  -0.0370 533 ASN B O   
8322  C CB  . ASN B  533 ? 0.5997 0.3812 0.4024 -0.1971 0.1653  -0.0494 533 ASN B CB  
8323  C CG  . ASN B  533 ? 0.5946 0.3849 0.4045 -0.2032 0.1683  -0.0506 533 ASN B CG  
8324  O OD1 . ASN B  533 ? 0.5789 0.3761 0.4049 -0.1977 0.1624  -0.0472 533 ASN B OD1 
8325  N ND2 . ASN B  533 ? 0.6146 0.4049 0.4124 -0.2150 0.1774  -0.0555 533 ASN B ND2 
8326  N N   . ARG B  534 ? 0.5862 0.3692 0.4057 -0.1818 0.1612  -0.0528 534 ARG B N   
8327  C CA  . ARG B  534 ? 0.6599 0.4327 0.4708 -0.1762 0.1579  -0.0512 534 ARG B CA  
8328  C C   . ARG B  534 ? 0.6261 0.4077 0.4627 -0.1645 0.1506  -0.0499 534 ARG B C   
8329  O O   . ARG B  534 ? 0.6387 0.4119 0.4716 -0.1550 0.1402  -0.0422 534 ARG B O   
8330  C CB  . ARG B  534 ? 0.9907 0.7632 0.7918 -0.1851 0.1689  -0.0602 534 ARG B CB  
8331  C CG  . ARG B  534 ? 1.0919 0.8484 0.8595 -0.1939 0.1719  -0.0583 534 ARG B CG  
8332  C CD  . ARG B  534 ? 1.1785 0.9382 0.9388 -0.2034 0.1831  -0.0680 534 ARG B CD  
8333  N NE  . ARG B  534 ? 1.3052 1.0538 1.0365 -0.2137 0.1864  -0.0667 534 ARG B NE  
8334  C CZ  . ARG B  534 ? 1.3837 1.1376 1.1124 -0.2225 0.1914  -0.0685 534 ARG B CZ  
8335  N NH1 . ARG B  534 ? 1.3790 1.1491 1.1318 -0.2222 0.1938  -0.0720 534 ARG B NH1 
8336  N NH2 . ARG B  534 ? 1.4315 1.1746 1.1340 -0.2316 0.1936  -0.0664 534 ARG B NH2 
8337  N N   . PHE B  535 ? 0.5656 0.3650 0.4295 -0.1651 0.1556  -0.0577 535 PHE B N   
8338  C CA  . PHE B  535 ? 0.5044 0.3118 0.3928 -0.1552 0.1498  -0.0583 535 PHE B CA  
8339  C C   . PHE B  535 ? 0.4719 0.2857 0.3785 -0.1456 0.1381  -0.0508 535 PHE B C   
8340  O O   . PHE B  535 ? 0.4207 0.2294 0.3284 -0.1359 0.1280  -0.0444 535 PHE B O   
8341  C CB  . PHE B  535 ? 0.4311 0.2549 0.3432 -0.1590 0.1592  -0.0708 535 PHE B CB  
8342  C CG  . PHE B  535 ? 0.4085 0.2402 0.3472 -0.1488 0.1526  -0.0719 535 PHE B CG  
8343  C CD1 . PHE B  535 ? 0.4073 0.2299 0.3401 -0.1437 0.1497  -0.0718 535 PHE B CD1 
8344  C CD2 . PHE B  535 ? 0.3882 0.2359 0.3574 -0.1438 0.1482  -0.0726 535 PHE B CD2 
8345  C CE1 . PHE B  535 ? 0.3865 0.2165 0.3443 -0.1335 0.1424  -0.0726 535 PHE B CE1 
8346  C CE2 . PHE B  535 ? 0.3683 0.2226 0.3616 -0.1341 0.1409  -0.0730 535 PHE B CE2 
8347  C CZ  . PHE B  535 ? 0.3672 0.2128 0.3550 -0.1287 0.1378  -0.0730 535 PHE B CZ  
8348  N N   . LEU B  536 ? 0.7340 0.5601 0.6556 -0.1484 0.1393  -0.0521 536 LEU B N   
8349  C CA  . LEU B  536 ? 0.7678 0.6008 0.7065 -0.1406 0.1285  -0.0454 536 LEU B CA  
8350  C C   . LEU B  536 ? 0.8455 0.6670 0.7708 -0.1329 0.1170  -0.0347 536 LEU B C   
8351  O O   . LEU B  536 ? 0.8975 0.7237 0.8372 -0.1242 0.1073  -0.0301 536 LEU B O   
8352  C CB  . LEU B  536 ? 0.5442 0.3887 0.4939 -0.1463 0.1314  -0.0472 536 LEU B CB  
8353  C CG  . LEU B  536 ? 0.4800 0.3367 0.4557 -0.1394 0.1224  -0.0440 536 LEU B CG  
8354  C CD1 . LEU B  536 ? 0.4934 0.3605 0.4933 -0.1353 0.1228  -0.0500 536 LEU B CD1 
8355  C CD2 . LEU B  536 ? 0.4460 0.3135 0.4315 -0.1452 0.1248  -0.0455 536 LEU B CD2 
8356  N N   . PRO B  537 ? 0.7555 0.5631 0.6546 -0.1360 0.1177  -0.0311 537 PRO B N   
8357  C CA  . PRO B  537 ? 0.7440 0.5418 0.6323 -0.1281 0.1074  -0.0226 537 PRO B CA  
8358  C C   . PRO B  537 ? 0.7681 0.5628 0.6594 -0.1191 0.1011  -0.0208 537 PRO B C   
8359  O O   . PRO B  537 ? 0.7858 0.5831 0.6851 -0.1106 0.0909  -0.0151 537 PRO B O   
8360  C CB  . PRO B  537 ? 0.5532 0.3356 0.4126 -0.1343 0.1114  -0.0214 537 PRO B CB  
8361  C CG  . PRO B  537 ? 0.5628 0.3465 0.4164 -0.1455 0.1239  -0.0293 537 PRO B CG  
8362  C CD  . PRO B  537 ? 0.5622 0.3640 0.4426 -0.1468 0.1270  -0.0342 537 PRO B CD  
8363  N N   . LYS B  538 ? 0.6609 0.4508 0.5458 -0.1215 0.1071  -0.0258 538 LYS B N   
8364  C CA  . LYS B  538 ? 0.6326 0.4205 0.5220 -0.1135 0.1017  -0.0251 538 LYS B CA  
8365  C C   . LYS B  538 ? 0.6030 0.4055 0.5218 -0.1063 0.0951  -0.0249 538 LYS B C   
8366  O O   . LYS B  538 ? 0.5886 0.3921 0.5146 -0.0973 0.0855  -0.0207 538 LYS B O   
8367  C CB  . LYS B  538 ? 0.6736 0.4562 0.5551 -0.1188 0.1110  -0.0326 538 LYS B CB  
8368  C CG  . LYS B  538 ? 0.7176 0.4822 0.5695 -0.1204 0.1116  -0.0305 538 LYS B CG  
8369  C CD  . LYS B  538 ? 0.7828 0.5378 0.6102 -0.1306 0.1182  -0.0302 538 LYS B CD  
8370  C CE  . LYS B  538 ? 0.8348 0.5703 0.6312 -0.1322 0.1173  -0.0272 538 LYS B CE  
8371  N NZ  . LYS B  538 ? 0.8589 0.5883 0.6440 -0.1387 0.1259  -0.0340 538 LYS B NZ  
8372  N N   . LEU B  539 ? 0.7542 0.5685 0.6900 -0.1108 0.1000  -0.0295 539 LEU B N   
8373  C CA  . LEU B  539 ? 0.7805 0.6086 0.7443 -0.1055 0.0944  -0.0299 539 LEU B CA  
8374  C C   . LEU B  539 ? 0.8817 0.7147 0.8521 -0.1013 0.0844  -0.0221 539 LEU B C   
8375  O O   . LEU B  539 ? 0.8853 0.7268 0.8742 -0.0956 0.0766  -0.0199 539 LEU B O   
8376  C CB  . LEU B  539 ? 0.5770 0.4166 0.5578 -0.1123 0.1041  -0.0391 539 LEU B CB  
8377  C CG  . LEU B  539 ? 0.5160 0.3698 0.5275 -0.1071 0.0995  -0.0414 539 LEU B CG  
8378  C CD1 . LEU B  539 ? 0.5160 0.3670 0.5329 -0.0989 0.0938  -0.0413 539 LEU B CD1 
8379  C CD2 . LEU B  539 ? 0.5088 0.3751 0.5382 -0.1138 0.1102  -0.0522 539 LEU B CD2 
8380  N N   . LEU B  540 ? 1.0111 0.8387 0.9663 -0.1045 0.0847  -0.0183 540 LEU B N   
8381  C CA  . LEU B  540 ? 1.0348 0.8667 0.9953 -0.1011 0.0759  -0.0118 540 LEU B CA  
8382  C C   . LEU B  540 ? 1.1868 1.0144 1.1429 -0.0924 0.0661  -0.0060 540 LEU B C   
8383  O O   . LEU B  540 ? 1.2184 1.0524 1.1850 -0.0875 0.0574  -0.0014 540 LEU B O   
8384  C CB  . LEU B  540 ? 0.6814 0.5102 0.6297 -0.1077 0.0802  -0.0111 540 LEU B CB  
8385  C CG  . LEU B  540 ? 0.5670 0.4068 0.5293 -0.1134 0.0832  -0.0133 540 LEU B CG  
8386  C CD1 . LEU B  540 ? 0.5472 0.3992 0.5341 -0.1092 0.0778  -0.0136 540 LEU B CD1 
8387  C CD2 . LEU B  540 ? 0.4911 0.3311 0.4476 -0.1236 0.0956  -0.0203 540 LEU B CD2 
8388  N N   . SER B  541 ? 1.1397 0.9566 1.0798 -0.0911 0.0680  -0.0065 541 SER B N   
8389  C CA  . SER B  541 ? 1.1651 0.9799 1.1049 -0.0826 0.0597  -0.0029 541 SER B CA  
8390  C C   . SER B  541 ? 1.2290 1.0493 1.1840 -0.0789 0.0578  -0.0057 541 SER B C   
8391  O O   . SER B  541 ? 1.2182 1.0402 1.1783 -0.0834 0.0651  -0.0114 541 SER B O   
8392  C CB  . SER B  541 ? 1.0332 0.8341 0.9498 -0.0833 0.0623  -0.0026 541 SER B CB  
8393  O OG  . SER B  541 ? 1.0283 0.8226 0.9298 -0.0883 0.0654  -0.0011 541 SER B OG  
8394  N N   . ALA B  542 ? 1.2967 1.1206 1.2599 -0.0709 0.0482  -0.0024 542 ALA B N   
8395  C CA  . ALA B  542 ? 1.3757 1.2048 1.3537 -0.0665 0.0443  -0.0043 542 ALA B CA  
8396  C C   . ALA B  542 ? 1.4390 1.2786 1.4358 -0.0671 0.0414  -0.0046 542 ALA B C   
8397  O O   . ALA B  542 ? 1.4341 1.2778 1.4426 -0.0633 0.0371  -0.0058 542 ALA B O   
8398  C CB  . ALA B  542 ? 0.2875 0.1097 0.2592 -0.0686 0.0522  -0.0107 542 ALA B CB  
8399  N N   . THR B  543 ? 1.6414 1.4846 1.6400 -0.0719 0.0436  -0.0035 543 THR B N   
8400  C CA  . THR B  543 ? 1.6901 1.5428 1.7052 -0.0730 0.0407  -0.0032 543 THR B CA  
8401  C C   . THR B  543 ? 1.7191 1.5744 1.7340 -0.0742 0.0368  0.0017  543 THR B C   
8402  O O   . THR B  543 ? 1.7313 1.5821 1.7345 -0.0766 0.0402  0.0029  543 THR B O   
8403  C CB  . THR B  543 ? 1.1294 0.9861 1.1529 -0.0797 0.0513  -0.0103 543 THR B CB  
8404  O OG1 . THR B  543 ? 1.1539 1.0084 1.1674 -0.0865 0.0581  -0.0108 543 THR B OG1 
8405  C CG2 . THR B  543 ? 1.1140 0.9675 1.1384 -0.0797 0.0588  -0.0175 543 THR B CG2 
8406  O OXT . THR B  543 ? 1.5827 1.4436 1.6076 -0.0732 0.0310  0.0040  543 THR B OXT 
8407  N N   . GLU C  4   ? 0.7221 0.7380 0.4078 0.0450  0.1043  -0.0785 4   GLU C N   
8408  C CA  . GLU C  4   ? 0.7131 0.7358 0.3927 0.0448  0.1129  -0.0751 4   GLU C CA  
8409  C C   . GLU C  4   ? 0.6934 0.7242 0.3903 0.0412  0.1219  -0.0695 4   GLU C C   
8410  O O   . GLU C  4   ? 0.7180 0.7545 0.4123 0.0384  0.1274  -0.0620 4   GLU C O   
8411  C CB  . GLU C  4   ? 0.6933 0.7144 0.3624 0.0488  0.1155  -0.0842 4   GLU C CB  
8412  C CG  . GLU C  4   ? 0.7441 0.7580 0.3932 0.0515  0.1075  -0.0901 4   GLU C CG  
8413  C CD  . GLU C  4   ? 0.8178 0.8345 0.4496 0.0508  0.1072  -0.0838 4   GLU C CD  
8414  O OE1 . GLU C  4   ? 0.8429 0.8628 0.4775 0.0481  0.1068  -0.0739 4   GLU C OE1 
8415  O OE2 . GLU C  4   ? 0.8568 0.8720 0.4713 0.0532  0.1074  -0.0889 4   GLU C OE2 
8416  N N   . ASP C  5   ? 0.5151 0.5462 0.2290 0.0410  0.1230  -0.0731 5   ASP C N   
8417  C CA  . ASP C  5   ? 0.4738 0.5131 0.2042 0.0377  0.1314  -0.0701 5   ASP C CA  
8418  C C   . ASP C  5   ? 0.4627 0.5072 0.1992 0.0320  0.1334  -0.0599 5   ASP C C   
8419  O O   . ASP C  5   ? 0.4479 0.4901 0.1909 0.0304  0.1280  -0.0560 5   ASP C O   
8420  C CB  . ASP C  5   ? 0.5323 0.5699 0.2792 0.0387  0.1298  -0.0749 5   ASP C CB  
8421  C CG  . ASP C  5   ? 0.5107 0.5569 0.2748 0.0355  0.1380  -0.0730 5   ASP C CG  
8422  O OD1 . ASP C  5   ? 0.5301 0.5837 0.2944 0.0317  0.1450  -0.0681 5   ASP C OD1 
8423  O OD2 . ASP C  5   ? 0.4680 0.5131 0.2452 0.0367  0.1370  -0.0763 5   ASP C OD2 
8424  N N   . PRO C  6   ? 0.5427 0.5944 0.2769 0.0290  0.1413  -0.0554 6   PRO C N   
8425  C CA  . PRO C  6   ? 0.5565 0.6126 0.2939 0.0239  0.1432  -0.0453 6   PRO C CA  
8426  C C   . PRO C  6   ? 0.5539 0.6156 0.3132 0.0192  0.1441  -0.0425 6   PRO C C   
8427  O O   . PRO C  6   ? 0.5750 0.6387 0.3382 0.0159  0.1433  -0.0344 6   PRO C O   
8428  C CB  . PRO C  6   ? 0.5764 0.6388 0.3055 0.0218  0.1521  -0.0431 6   PRO C CB  
8429  C CG  . PRO C  6   ? 0.5717 0.6357 0.3024 0.0245  0.1569  -0.0523 6   PRO C CG  
8430  C CD  . PRO C  6   ? 0.5528 0.6081 0.2794 0.0306  0.1488  -0.0596 6   PRO C CD  
8431  N N   . GLN C  7   ? 0.4991 0.5626 0.2727 0.0197  0.1449  -0.0484 7   GLN C N   
8432  C CA  . GLN C  7   ? 0.5265 0.5960 0.3212 0.0158  0.1440  -0.0457 7   GLN C CA  
8433  C C   . GLN C  7   ? 0.5029 0.5670 0.3029 0.0168  0.1358  -0.0449 7   GLN C C   
8434  O O   . GLN C  7   ? 0.4996 0.5690 0.3140 0.0138  0.1338  -0.0403 7   GLN C O   
8435  C CB  . GLN C  7   ? 0.8174 0.8902 0.6249 0.0160  0.1482  -0.0517 7   GLN C CB  
8436  C CG  . GLN C  7   ? 0.8962 0.9800 0.7235 0.0103  0.1495  -0.0483 7   GLN C CG  
8437  C CD  . GLN C  7   ? 0.9799 1.0754 0.8070 0.0053  0.1548  -0.0423 7   GLN C CD  
8438  O OE1 . GLN C  7   ? 0.9623 1.0715 0.8026 0.0022  0.1530  -0.0364 7   GLN C OE1 
8439  N NE2 . GLN C  7   ? 1.0484 1.1410 0.8597 0.0062  0.1607  -0.0428 7   GLN C NE2 
8440  N N   . LEU C  8   ? 0.4947 0.5492 0.2830 0.0212  0.1309  -0.0494 8   LEU C N   
8441  C CA  . LEU C  8   ? 0.4668 0.5159 0.2602 0.0220  0.1237  -0.0497 8   LEU C CA  
8442  C C   . LEU C  8   ? 0.4640 0.5088 0.2497 0.0217  0.1193  -0.0429 8   LEU C C   
8443  O O   . LEU C  8   ? 0.4775 0.5190 0.2697 0.0216  0.1143  -0.0418 8   LEU C O   
8444  C CB  . LEU C  8   ? 0.5546 0.5952 0.3423 0.0268  0.1195  -0.0587 8   LEU C CB  
8445  C CG  . LEU C  8   ? 0.5987 0.6413 0.3944 0.0287  0.1237  -0.0648 8   LEU C CG  
8446  C CD1 . LEU C  8   ? 0.6448 0.6778 0.4354 0.0340  0.1186  -0.0732 8   LEU C CD1 
8447  C CD2 . LEU C  8   ? 0.5811 0.6312 0.3976 0.0248  0.1257  -0.0615 8   LEU C CD2 
8448  N N   . LEU C  9   ? 0.4313 0.4755 0.2034 0.0220  0.1210  -0.0377 9   LEU C N   
8449  C CA  . LEU C  9   ? 0.4181 0.4578 0.1844 0.0222  0.1173  -0.0298 9   LEU C CA  
8450  C C   . LEU C  9   ? 0.4243 0.4688 0.2008 0.0181  0.1217  -0.0205 9   LEU C C   
8451  O O   . LEU C  9   ? 0.3980 0.4487 0.1750 0.0155  0.1280  -0.0179 9   LEU C O   
8452  C CB  . LEU C  9   ? 0.4228 0.4578 0.1673 0.0259  0.1147  -0.0286 9   LEU C CB  
8453  C CG  . LEU C  9   ? 0.4472 0.4787 0.1859 0.0266  0.1117  -0.0190 9   LEU C CG  
8454  C CD1 . LEU C  9   ? 0.4327 0.4586 0.1586 0.0308  0.1027  -0.0213 9   LEU C CD1 
8455  C CD2 . LEU C  9   ? 0.4842 0.5176 0.2127 0.0261  0.1170  -0.0113 9   LEU C CD2 
8456  N N   . VAL C  10  ? 0.4632 0.5043 0.2477 0.0175  0.1184  -0.0160 10  VAL C N   
8457  C CA  . VAL C  10  ? 0.4479 0.4908 0.2436 0.0141  0.1215  -0.0077 10  VAL C CA  
8458  C C   . VAL C  10  ? 0.4430 0.4772 0.2339 0.0160  0.1179  -0.0010 10  VAL C C   
8459  O O   . VAL C  10  ? 0.4348 0.4648 0.2235 0.0184  0.1123  -0.0042 10  VAL C O   
8460  C CB  . VAL C  10  ? 0.3474 0.3963 0.1636 0.0115  0.1214  -0.0104 10  VAL C CB  
8461  C CG1 . VAL C  10  ? 0.3404 0.3893 0.1666 0.0082  0.1242  -0.0022 10  VAL C CG1 
8462  C CG2 . VAL C  10  ? 0.4748 0.5340 0.2969 0.0108  0.1242  -0.0174 10  VAL C CG2 
8463  N N   . ARG C  11  ? 0.5071 0.5383 0.2961 0.0150  0.1211  0.0082  11  ARG C N   
8464  C CA  . ARG C  11  ? 0.5181 0.5413 0.3038 0.0176  0.1182  0.0149  11  ARG C CA  
8465  C C   . ARG C  11  ? 0.4594 0.4804 0.2618 0.0142  0.1202  0.0189  11  ARG C C   
8466  O O   . ARG C  11  ? 0.4770 0.4999 0.2868 0.0104  0.1251  0.0216  11  ARG C O   
8467  C CB  . ARG C  11  ? 0.5595 0.5782 0.3285 0.0208  0.1194  0.0233  11  ARG C CB  
8468  C CG  . ARG C  11  ? 0.5845 0.5956 0.3550 0.0226  0.1194  0.0328  11  ARG C CG  
8469  C CD  . ARG C  11  ? 0.6075 0.6140 0.3603 0.0274  0.1193  0.0414  11  ARG C CD  
8470  N NE  . ARG C  11  ? 0.5747 0.5803 0.3174 0.0341  0.1119  0.0429  11  ARG C NE  
8471  C CZ  . ARG C  11  ? 0.5571 0.5662 0.2837 0.0381  0.1065  0.0399  11  ARG C CZ  
8472  N NH1 . ARG C  11  ? 0.5644 0.5764 0.2833 0.0361  0.1089  0.0354  11  ARG C NH1 
8473  N NH2 . ARG C  11  ? 0.5390 0.5497 0.2573 0.0440  0.0985  0.0410  11  ARG C NH2 
8474  N N   . VAL C  12  ? 0.3519 0.3689 0.1595 0.0156  0.1164  0.0190  12  VAL C N   
8475  C CA  . VAL C  12  ? 0.3405 0.3531 0.1614 0.0133  0.1179  0.0232  12  VAL C CA  
8476  C C   . VAL C  12  ? 0.5321 0.5370 0.3460 0.0177  0.1169  0.0313  12  VAL C C   
8477  O O   . VAL C  12  ? 0.5871 0.5910 0.3852 0.0228  0.1148  0.0347  12  VAL C O   
8478  C CB  . VAL C  12  ? 0.3360 0.3513 0.1711 0.0111  0.1150  0.0167  12  VAL C CB  
8479  C CG1 . VAL C  12  ? 0.3133 0.3370 0.1555 0.0086  0.1155  0.0097  12  VAL C CG1 
8480  C CG2 . VAL C  12  ? 0.3207 0.3348 0.1491 0.0147  0.1097  0.0136  12  VAL C CG2 
8481  N N   . ARG C  13  ? 0.4729 0.4728 0.2979 0.0166  0.1182  0.0346  13  ARG C N   
8482  C CA  . ARG C  13  ? 0.4693 0.4626 0.2892 0.0218  0.1179  0.0428  13  ARG C CA  
8483  C C   . ARG C  13  ? 0.5058 0.5032 0.3179 0.0274  0.1121  0.0418  13  ARG C C   
8484  O O   . ARG C  13  ? 0.5191 0.5157 0.3196 0.0341  0.1100  0.0487  13  ARG C O   
8485  C CB  . ARG C  13  ? 0.4457 0.4330 0.2800 0.0195  0.1207  0.0451  13  ARG C CB  
8486  C CG  . ARG C  13  ? 0.4432 0.4250 0.2746 0.0259  0.1207  0.0529  13  ARG C CG  
8487  C CD  . ARG C  13  ? 0.3649 0.3382 0.1860 0.0301  0.1243  0.0628  13  ARG C CD  
8488  N NE  . ARG C  13  ? 0.4671 0.4427 0.2728 0.0390  0.1205  0.0691  13  ARG C NE  
8489  C CZ  . ARG C  13  ? 0.4276 0.4023 0.2320 0.0466  0.1190  0.0759  13  ARG C CZ  
8490  N NH1 . ARG C  13  ? 0.4187 0.3887 0.2364 0.0461  0.1221  0.0769  13  ARG C NH1 
8491  N NH2 . ARG C  13  ? 0.4083 0.3883 0.1981 0.0552  0.1137  0.0816  13  ARG C NH2 
8492  N N   . GLY C  14  ? 0.5263 0.5286 0.3443 0.0250  0.1088  0.0335  14  GLY C N   
8493  C CA  . GLY C  14  ? 0.5151 0.5220 0.3259 0.0294  0.1029  0.0316  14  GLY C CA  
8494  C C   . GLY C  14  ? 0.5049 0.5161 0.2974 0.0334  0.0979  0.0291  14  GLY C C   
8495  O O   . GLY C  14  ? 0.3581 0.3747 0.1433 0.0375  0.0904  0.0286  14  GLY C O   
8496  N N   . GLY C  15  ? 0.5478 0.5582 0.3357 0.0310  0.1003  0.0265  15  GLY C N   
8497  C CA  . GLY C  15  ? 0.5635 0.5772 0.3342 0.0342  0.0959  0.0233  15  GLY C CA  
8498  C C   . GLY C  15  ? 0.5469 0.5616 0.3182 0.0301  0.0986  0.0157  15  GLY C C   
8499  O O   . GLY C  15  ? 0.5306 0.5453 0.3151 0.0252  0.1041  0.0149  15  GLY C O   
8500  N N   . GLN C  16  ? 0.5520 0.5689 0.3092 0.0325  0.0941  0.0100  16  GLN C N   
8501  C CA  . GLN C  16  ? 0.5438 0.5625 0.3002 0.0300  0.0965  0.0025  16  GLN C CA  
8502  C C   . GLN C  16  ? 0.5499 0.5687 0.3146 0.0280  0.0940  -0.0075 16  GLN C C   
8503  O O   . GLN C  16  ? 0.5789 0.5962 0.3411 0.0296  0.0878  -0.0108 16  GLN C O   
8504  C CB  . GLN C  16  ? 0.5486 0.5682 0.2849 0.0337  0.0932  0.0009  16  GLN C CB  
8505  C CG  . GLN C  16  ? 0.5835 0.6027 0.3110 0.0350  0.0973  0.0101  16  GLN C CG  
8506  C CD  . GLN C  16  ? 0.6118 0.6328 0.3260 0.0354  0.0991  0.0065  16  GLN C CD  
8507  O OE1 . GLN C  16  ? 0.5960 0.6187 0.3142 0.0320  0.1066  0.0077  16  GLN C OE1 
8508  N NE2 . GLN C  16  ? 0.6296 0.6509 0.3276 0.0392  0.0919  0.0018  16  GLN C NE2 
8509  N N   . LEU C  17  ? 0.4238 0.4451 0.1982 0.0248  0.0983  -0.0123 17  LEU C N   
8510  C CA  . LEU C  17  ? 0.4019 0.4227 0.1814 0.0243  0.0956  -0.0220 17  LEU C CA  
8511  C C   . LEU C  17  ? 0.4293 0.4535 0.2085 0.0240  0.0988  -0.0285 17  LEU C C   
8512  O O   . LEU C  17  ? 0.4449 0.4740 0.2248 0.0227  0.1046  -0.0253 17  LEU C O   
8513  C CB  . LEU C  17  ? 0.3404 0.3611 0.1376 0.0214  0.0961  -0.0215 17  LEU C CB  
8514  C CG  . LEU C  17  ? 0.3275 0.3528 0.1407 0.0179  0.1017  -0.0157 17  LEU C CG  
8515  C CD1 . LEU C  17  ? 0.4260 0.4585 0.2478 0.0166  0.1047  -0.0206 17  LEU C CD1 
8516  C CD2 . LEU C  17  ? 0.3119 0.3346 0.1376 0.0160  0.1006  -0.0133 17  LEU C CD2 
8517  N N   . ARG C  18  ? 0.3671 0.3883 0.1445 0.0255  0.0952  -0.0377 18  ARG C N   
8518  C CA  . ARG C  18  ? 0.3747 0.3976 0.1502 0.0265  0.0979  -0.0446 18  ARG C CA  
8519  C C   . ARG C  18  ? 0.3628 0.3848 0.1504 0.0265  0.0969  -0.0513 18  ARG C C   
8520  O O   . ARG C  18  ? 0.3624 0.3773 0.1473 0.0278  0.0910  -0.0559 18  ARG C O   
8521  C CB  . ARG C  18  ? 0.5827 0.6004 0.3387 0.0302  0.0937  -0.0498 18  ARG C CB  
8522  C CG  . ARG C  18  ? 0.6439 0.6594 0.3979 0.0323  0.0942  -0.0594 18  ARG C CG  
8523  C CD  . ARG C  18  ? 0.7674 0.7749 0.5051 0.0353  0.0863  -0.0665 18  ARG C CD  
8524  N NE  . ARG C  18  ? 0.8857 0.8940 0.6068 0.0363  0.0837  -0.0628 18  ARG C NE  
8525  C CZ  . ARG C  18  ? 0.9362 0.9410 0.6474 0.0368  0.0753  -0.0627 18  ARG C CZ  
8526  N NH1 . ARG C  18  ? 0.9181 0.9179 0.6341 0.0357  0.0691  -0.0664 18  ARG C NH1 
8527  N NH2 . ARG C  18  ? 0.9469 0.9539 0.6430 0.0383  0.0727  -0.0591 18  ARG C NH2 
8528  N N   . GLY C  19  ? 0.6692 0.6986 0.4694 0.0249  0.1024  -0.0518 19  GLY C N   
8529  C CA  . GLY C  19  ? 0.3430 0.3731 0.1556 0.0254  0.1016  -0.0571 19  GLY C CA  
8530  C C   . GLY C  19  ? 0.3558 0.3818 0.1628 0.0289  0.1027  -0.0655 19  GLY C C   
8531  O O   . GLY C  19  ? 0.4103 0.4325 0.2027 0.0314  0.1027  -0.0683 19  GLY C O   
8532  N N   . ILE C  20  ? 0.3673 0.3938 0.1860 0.0299  0.1031  -0.0691 20  ILE C N   
8533  C CA  . ILE C  20  ? 0.4040 0.4252 0.2185 0.0344  0.1041  -0.0771 20  ILE C CA  
8534  C C   . ILE C  20  ? 0.4163 0.4449 0.2431 0.0344  0.1108  -0.0766 20  ILE C C   
8535  O O   . ILE C  20  ? 0.3392 0.3747 0.1810 0.0309  0.1118  -0.0723 20  ILE C O   
8536  C CB  . ILE C  20  ? 0.3584 0.3687 0.1721 0.0373  0.0968  -0.0825 20  ILE C CB  
8537  C CG1 . ILE C  20  ? 0.4613 0.4630 0.2658 0.0433  0.0954  -0.0909 20  ILE C CG1 
8538  C CG2 . ILE C  20  ? 0.3832 0.3965 0.2126 0.0358  0.0963  -0.0806 20  ILE C CG2 
8539  C CD1 . ILE C  20  ? 0.4465 0.4500 0.2606 0.0472  0.0992  -0.0941 20  ILE C CD1 
8540  N N   . ARG C  21  ? 0.3711 0.3991 0.1910 0.0384  0.1152  -0.0814 21  ARG C N   
8541  C CA  . ARG C  21  ? 0.4570 0.4915 0.2865 0.0395  0.1222  -0.0815 21  ARG C CA  
8542  C C   . ARG C  21  ? 0.4454 0.4752 0.2802 0.0452  0.1203  -0.0872 21  ARG C C   
8543  O O   . ARG C  21  ? 0.5200 0.5431 0.3460 0.0513  0.1174  -0.0937 21  ARG C O   
8544  C CB  . ARG C  21  ? 0.6429 0.6799 0.4612 0.0424  0.1281  -0.0843 21  ARG C CB  
8545  C CG  . ARG C  21  ? 0.7171 0.7624 0.5440 0.0432  0.1368  -0.0836 21  ARG C CG  
8546  C CD  . ARG C  21  ? 0.8061 0.8535 0.6203 0.0469  0.1422  -0.0877 21  ARG C CD  
8547  N NE  . ARG C  21  ? 0.8935 0.9367 0.7044 0.0555  0.1401  -0.0957 21  ARG C NE  
8548  C CZ  . ARG C  21  ? 0.9604 1.0095 0.7787 0.0608  0.1454  -0.0987 21  ARG C CZ  
8549  N NH1 . ARG C  21  ? 0.9683 1.0273 0.7971 0.0578  0.1535  -0.0942 21  ARG C NH1 
8550  N NH2 . ARG C  21  ? 0.9930 1.0381 0.8082 0.0692  0.1426  -0.1061 21  ARG C NH2 
8551  N N   . LEU C  22  ? 0.3912 0.4240 0.2405 0.0438  0.1207  -0.0843 22  LEU C N   
8552  C CA  . LEU C  22  ? 0.3794 0.4077 0.2330 0.0497  0.1183  -0.0892 22  LEU C CA  
8553  C C   . LEU C  22  ? 0.3916 0.4284 0.2538 0.0537  0.1251  -0.0895 22  LEU C C   
8554  O O   . LEU C  22  ? 0.3548 0.3994 0.2227 0.0495  0.1311  -0.0841 22  LEU C O   
8555  C CB  . LEU C  22  ? 0.3376 0.3640 0.2009 0.0463  0.1135  -0.0857 22  LEU C CB  
8556  C CG  . LEU C  22  ? 0.3272 0.3515 0.1891 0.0404  0.1078  -0.0821 22  LEU C CG  
8557  C CD1 . LEU C  22  ? 0.3207 0.3489 0.1964 0.0366  0.1061  -0.0778 22  LEU C CD1 
8558  C CD2 . LEU C  22  ? 0.3357 0.3483 0.1859 0.0438  0.1011  -0.0878 22  LEU C CD2 
8559  N N   . LYS C  23  ? 0.4511 0.4867 0.3149 0.0621  0.1230  -0.0950 23  LYS C N   
8560  C CA  . LYS C  23  ? 0.4681 0.5148 0.3420 0.0670  0.1287  -0.0954 23  LYS C CA  
8561  C C   . LYS C  23  ? 0.4044 0.4552 0.2918 0.0677  0.1270  -0.0928 23  LYS C C   
8562  O O   . LYS C  23  ? 0.3621 0.4056 0.2498 0.0708  0.1202  -0.0952 23  LYS C O   
8563  C CB  . LYS C  23  ? 0.7534 0.8005 0.6220 0.0768  0.1292  -0.1027 23  LYS C CB  
8564  C CG  . LYS C  23  ? 0.8680 0.9022 0.7304 0.0836  0.1210  -0.1088 23  LYS C CG  
8565  C CD  . LYS C  23  ? 0.9708 1.0055 0.8288 0.0939  0.1226  -0.1160 23  LYS C CD  
8566  C CE  . LYS C  23  ? 1.0302 1.0631 0.8747 0.0930  0.1260  -0.1187 23  LYS C CE  
8567  N NZ  . LYS C  23  ? 1.0683 1.1032 0.9092 0.1029  0.1290  -0.1255 23  LYS C NZ  
8568  N N   . ALA C  24  ? 0.5175 0.5794 0.4153 0.0643  0.1332  -0.0876 24  ALA C N   
8569  C CA  . ALA C  24  ? 0.5498 0.6203 0.4613 0.0661  0.1327  -0.0855 24  ALA C CA  
8570  C C   . ALA C  24  ? 0.5490 0.6317 0.4666 0.0753  0.1349  -0.0904 24  ALA C C   
8571  O O   . ALA C  24  ? 0.5155 0.6000 0.4270 0.0784  0.1389  -0.0937 24  ALA C O   
8572  C CB  . ALA C  24  ? 0.5040 0.5804 0.4227 0.0587  0.1380  -0.0772 24  ALA C CB  
8573  N N   . PRO C  25  ? 0.5002 0.5921 0.4294 0.0801  0.1323  -0.0912 25  PRO C N   
8574  C CA  . PRO C  25  ? 0.5001 0.6033 0.4348 0.0905  0.1333  -0.0966 25  PRO C CA  
8575  C C   . PRO C  25  ? 0.4721 0.5898 0.4115 0.0894  0.1424  -0.0955 25  PRO C C   
8576  O O   . PRO C  25  ? 0.4583 0.5811 0.3961 0.0970  0.1450  -0.1006 25  PRO C O   
8577  C CB  . PRO C  25  ? 0.4681 0.5816 0.4161 0.0937  0.1293  -0.0960 25  PRO C CB  
8578  C CG  . PRO C  25  ? 0.4452 0.5458 0.3894 0.0878  0.1238  -0.0929 25  PRO C CG  
8579  C CD  . PRO C  25  ? 0.4569 0.5507 0.3947 0.0772  0.1284  -0.0877 25  PRO C CD  
8580  N N   . GLY C  26  ? 0.4673 0.5903 0.4113 0.0803  0.1476  -0.0889 26  GLY C N   
8581  C CA  . GLY C  26  ? 0.5017 0.6388 0.4509 0.0790  0.1566  -0.0873 26  GLY C CA  
8582  C C   . GLY C  26  ? 0.5172 0.6465 0.4545 0.0733  0.1631  -0.0845 26  GLY C C   
8583  O O   . GLY C  26  ? 0.5153 0.6552 0.4566 0.0711  0.1713  -0.0818 26  GLY C O   
8584  N N   . GLY C  27  ? 0.6885 0.8003 0.6114 0.0710  0.1594  -0.0853 27  GLY C N   
8585  C CA  . GLY C  27  ? 0.7266 0.8308 0.6374 0.0650  0.1644  -0.0824 27  GLY C CA  
8586  C C   . GLY C  27  ? 0.7255 0.8127 0.6251 0.0606  0.1578  -0.0819 27  GLY C C   
8587  O O   . GLY C  27  ? 0.7831 0.8647 0.6848 0.0623  0.1502  -0.0835 27  GLY C O   
8588  N N   . PRO C  28  ? 0.5085 0.5890 0.3967 0.0552  0.1592  -0.0797 28  PRO C N   
8589  C CA  . PRO C  28  ? 0.4536 0.5215 0.3340 0.0510  0.1512  -0.0790 28  PRO C CA  
8590  C C   . PRO C  28  ? 0.4380 0.5026 0.3240 0.0430  0.1499  -0.0698 28  PRO C C   
8591  O O   . PRO C  28  ? 0.4569 0.5270 0.3504 0.0413  0.1556  -0.0633 28  PRO C O   
8592  C CB  . PRO C  28  ? 0.3972 0.4620 0.2625 0.0501  0.1522  -0.0817 28  PRO C CB  
8593  C CG  . PRO C  28  ? 0.3932 0.4672 0.2596 0.0494  0.1619  -0.0795 28  PRO C CG  
8594  C CD  . PRO C  28  ? 0.4624 0.5465 0.3443 0.0523  0.1666  -0.0776 28  PRO C CD  
8595  N N   . VAL C  29  ? 0.3458 0.4016 0.2277 0.0391  0.1427  -0.0692 29  VAL C N   
8596  C CA  . VAL C  29  ? 0.3403 0.3910 0.2258 0.0320  0.1409  -0.0613 29  VAL C CA  
8597  C C   . VAL C  29  ? 0.3557 0.4062 0.2322 0.0266  0.1351  -0.0643 29  VAL C C   
8598  O O   . VAL C  29  ? 0.3421 0.3903 0.2088 0.0315  0.1319  -0.0702 29  VAL C O   
8599  C CB  . VAL C  29  ? 0.3202 0.3660 0.2133 0.0341  0.1361  -0.0579 29  VAL C CB  
8600  C CG1 . VAL C  29  ? 0.3373 0.3927 0.2412 0.0396  0.1397  -0.0540 29  VAL C CG1 
8601  C CG2 . VAL C  29  ? 0.3188 0.3626 0.2093 0.0365  0.1294  -0.0666 29  VAL C CG2 
8602  N N   . SER C  30  ? 0.5347 0.5938 0.4156 0.0178  0.1324  -0.0608 30  SER C N   
8603  C CA  . SER C  30  ? 0.5654 0.6333 0.4396 0.0177  0.1242  -0.0602 30  SER C CA  
8604  C C   . SER C  30  ? 0.5370 0.6124 0.4193 0.0207  0.1141  -0.0575 30  SER C C   
8605  O O   . SER C  30  ? 0.5639 0.6524 0.4568 0.0272  0.1100  -0.0497 30  SER C O   
8606  C CB  . SER C  30  ? 0.5113 0.5940 0.3842 0.0152  0.1245  -0.0535 30  SER C CB  
8607  O OG  . SER C  30  ? 0.5370 0.6164 0.4027 0.0130  0.1334  -0.0553 30  SER C OG  
8608  N N   . ALA C  31  ? 0.3503 0.4127 0.2224 0.0227  0.1106  -0.0593 31  ALA C N   
8609  C CA  . ALA C  31  ? 0.3276 0.3884 0.2034 0.0259  0.1038  -0.0557 31  ALA C CA  
8610  C C   . ALA C  31  ? 0.3786 0.4302 0.2429 0.0250  0.1018  -0.0531 31  ALA C C   
8611  O O   . ALA C  31  ? 0.4312 0.4744 0.2822 0.0251  0.1018  -0.0577 31  ALA C O   
8612  C CB  . ALA C  31  ? 0.2967 0.3494 0.1741 0.0282  0.1012  -0.0627 31  ALA C CB  
8613  N N   . PHE C  32  ? 0.3233 0.3740 0.1914 0.0238  0.1009  -0.0456 32  PHE C N   
8614  C CA  . PHE C  32  ? 0.2907 0.3331 0.1494 0.0222  0.0992  -0.0434 32  PHE C CA  
8615  C C   . PHE C  32  ? 0.2769 0.3104 0.1408 0.0218  0.0957  -0.0422 32  PHE C C   
8616  O O   . PHE C  32  ? 0.2654 0.2999 0.1401 0.0193  0.0968  -0.0370 32  PHE C O   
8617  C CB  . PHE C  32  ? 0.3223 0.3683 0.1807 0.0188  0.1027  -0.0353 32  PHE C CB  
8618  C CG  . PHE C  32  ? 0.3428 0.3962 0.1971 0.0180  0.1071  -0.0355 32  PHE C CG  
8619  C CD1 . PHE C  32  ? 0.3232 0.3869 0.1880 0.0176  0.1102  -0.0344 32  PHE C CD1 
8620  C CD2 . PHE C  32  ? 0.3507 0.3999 0.1893 0.0178  0.1083  -0.0365 32  PHE C CD2 
8621  C CE1 . PHE C  32  ? 0.3038 0.3741 0.1649 0.0162  0.1147  -0.0347 32  PHE C CE1 
8622  C CE2 . PHE C  32  ? 0.3259 0.3799 0.1594 0.0169  0.1131  -0.0364 32  PHE C CE2 
8623  C CZ  . PHE C  32  ? 0.3235 0.3882 0.1688 0.0155  0.1167  -0.0357 32  PHE C CZ  
8624  N N   . LEU C  33  ? 0.2857 0.3088 0.1413 0.0232  0.0916  -0.0476 33  LEU C N   
8625  C CA  . LEU C  33  ? 0.2871 0.3003 0.1468 0.0216  0.0888  -0.0479 33  LEU C CA  
8626  C C   . LEU C  33  ? 0.3369 0.3408 0.1886 0.0185  0.0863  -0.0466 33  LEU C C   
8627  O O   . LEU C  33  ? 0.3605 0.3609 0.1986 0.0199  0.0840  -0.0498 33  LEU C O   
8628  C CB  . LEU C  33  ? 0.2817 0.2890 0.1388 0.0250  0.0859  -0.0560 33  LEU C CB  
8629  C CG  . LEU C  33  ? 0.2818 0.3003 0.1443 0.0289  0.0885  -0.0590 33  LEU C CG  
8630  C CD1 . LEU C  33  ? 0.2940 0.3057 0.1494 0.0323  0.0860  -0.0685 33  LEU C CD1 
8631  C CD2 . LEU C  33  ? 0.2687 0.2919 0.1444 0.0284  0.0899  -0.0555 33  LEU C CD2 
8632  N N   . GLY C  34  ? 0.3323 0.3330 0.1922 0.0139  0.0868  -0.0424 34  GLY C N   
8633  C CA  . GLY C  34  ? 0.3531 0.3462 0.2070 0.0101  0.0849  -0.0419 34  GLY C CA  
8634  C C   . GLY C  34  ? 0.2762 0.2740 0.1257 0.0100  0.0867  -0.0360 34  GLY C C   
8635  O O   . GLY C  34  ? 0.2857 0.2799 0.1245 0.0093  0.0835  -0.0371 34  GLY C O   
8636  N N   . ILE C  35  ? 0.2694 0.2754 0.1274 0.0105  0.0905  -0.0297 35  ILE C N   
8637  C CA  . ILE C  35  ? 0.2724 0.2814 0.1278 0.0103  0.0927  -0.0228 35  ILE C CA  
8638  C C   . ILE C  35  ? 0.2643 0.2700 0.1270 0.0067  0.0932  -0.0188 35  ILE C C   
8639  O O   . ILE C  35  ? 0.2519 0.2578 0.1281 0.0040  0.0941  -0.0176 35  ILE C O   
8640  C CB  . ILE C  35  ? 0.2686 0.2849 0.1316 0.0101  0.0965  -0.0180 35  ILE C CB  
8641  C CG1 . ILE C  35  ? 0.2754 0.2971 0.1336 0.0129  0.0971  -0.0224 35  ILE C CG1 
8642  C CG2 . ILE C  35  ? 0.2749 0.2912 0.1333 0.0100  0.0988  -0.0109 35  ILE C CG2 
8643  C CD1 . ILE C  35  ? 0.2716 0.3009 0.1380 0.0116  0.1010  -0.0189 35  ILE C CD1 
8644  N N   . PRO C  36  ? 0.2722 0.2754 0.1256 0.0069  0.0922  -0.0171 36  PRO C N   
8645  C CA  . PRO C  36  ? 0.2630 0.2670 0.1284 0.0038  0.0903  -0.0131 36  PRO C CA  
8646  C C   . PRO C  36  ? 0.2588 0.2638 0.1302 0.0042  0.0972  -0.0053 36  PRO C C   
8647  O O   . PRO C  36  ? 0.2672 0.2739 0.1322 0.0076  0.0987  -0.0003 36  PRO C O   
8648  C CB  . PRO C  36  ? 0.2851 0.2929 0.1465 0.0048  0.0815  -0.0129 36  PRO C CB  
8649  C CG  . PRO C  36  ? 0.2851 0.2942 0.1308 0.0097  0.0815  -0.0129 36  PRO C CG  
8650  C CD  . PRO C  36  ? 0.2863 0.2917 0.1267 0.0104  0.0866  -0.0179 36  PRO C CD  
8651  N N   . PHE C  37  ? 0.2459 0.2504 0.1321 0.0007  0.0980  -0.0044 37  PHE C N   
8652  C CA  . PHE C  37  ? 0.2413 0.2463 0.1368 0.0004  0.1007  0.0017  37  PHE C CA  
8653  C C   . PHE C  37  ? 0.2389 0.2432 0.1399 0.0001  0.1021  0.0057  37  PHE C C   
8654  O O   . PHE C  37  ? 0.2590 0.2618 0.1666 0.0004  0.1044  0.0103  37  PHE C O   
8655  C CB  . PHE C  37  ? 0.2319 0.2371 0.1381 -0.0021 0.1006  0.0005  37  PHE C CB  
8656  C CG  . PHE C  37  ? 0.2443 0.2478 0.1599 -0.0054 0.0985  -0.0027 37  PHE C CG  
8657  C CD1 . PHE C  37  ? 0.2282 0.2311 0.1425 -0.0060 0.0961  -0.0083 37  PHE C CD1 
8658  C CD2 . PHE C  37  ? 0.2933 0.2948 0.2181 -0.0075 0.0992  -0.0001 37  PHE C CD2 
8659  C CE1 . PHE C  37  ? 0.2664 0.2667 0.1880 -0.0091 0.0945  -0.0106 37  PHE C CE1 
8660  C CE2 . PHE C  37  ? 0.3191 0.3190 0.2514 -0.0105 0.0972  -0.0029 37  PHE C CE2 
8661  C CZ  . PHE C  37  ? 0.3082 0.3074 0.2387 -0.0115 0.0949  -0.0078 37  PHE C CZ  
8662  N N   . ALA C  38  ? 0.3058 0.3118 0.2059 -0.0009 0.0991  0.0033  38  ALA C N   
8663  C CA  . ALA C  38  ? 0.3035 0.3133 0.2135 -0.0010 0.0972  0.0069  38  ALA C CA  
8664  C C   . ALA C  38  ? 0.3390 0.3561 0.2497 -0.0011 0.0875  0.0049  38  ALA C C   
8665  O O   . ALA C  38  ? 0.3887 0.4053 0.2945 -0.0034 0.0822  -0.0009 38  ALA C O   
8666  C CB  . ALA C  38  ? 0.3044 0.3116 0.2251 -0.0057 0.1007  0.0051  38  ALA C CB  
8667  N N   . GLU C  39  ? 0.2954 0.3193 0.2127 0.0012  0.0852  0.0094  39  GLU C N   
8668  C CA  . GLU C  39  ? 0.3269 0.3600 0.2486 -0.0006 0.0760  0.0072  39  GLU C CA  
8669  C C   . GLU C  39  ? 0.2982 0.3292 0.2280 -0.0078 0.0755  0.0020  39  GLU C C   
8670  O O   . GLU C  39  ? 0.2643 0.2912 0.2009 -0.0097 0.0820  0.0029  39  GLU C O   
8671  C CB  . GLU C  39  ? 0.4947 0.5375 0.4251 0.0034  0.0744  0.0131  39  GLU C CB  
8672  C CG  . GLU C  39  ? 0.5935 0.6387 0.5146 0.0112  0.0731  0.0187  39  GLU C CG  
8673  C CD  . GLU C  39  ? 0.6879 0.7385 0.5988 0.0116  0.0638  0.0155  39  GLU C CD  
8674  O OE1 . GLU C  39  ? 0.7553 0.8157 0.6726 0.0086  0.0556  0.0125  39  GLU C OE1 
8675  O OE2 . GLU C  39  ? 0.6763 0.7214 0.5724 0.0145  0.0649  0.0157  39  GLU C OE2 
8676  N N   . PRO C  40  ? 0.4058 0.4382 0.3336 -0.0120 0.0678  -0.0035 40  PRO C N   
8677  C CA  . PRO C  40  ? 0.3936 0.4220 0.3270 -0.0191 0.0668  -0.0082 40  PRO C CA  
8678  C C   . PRO C  40  ? 0.3428 0.3773 0.2906 -0.0220 0.0691  -0.0052 40  PRO C C   
8679  O O   . PRO C  40  ? 0.3091 0.3550 0.2642 -0.0212 0.0655  -0.0026 40  PRO C O   
8680  C CB  . PRO C  40  ? 0.3776 0.4080 0.3066 -0.0226 0.0571  -0.0134 40  PRO C CB  
8681  C CG  . PRO C  40  ? 0.3775 0.4177 0.3035 -0.0178 0.0525  -0.0106 40  PRO C CG  
8682  C CD  . PRO C  40  ? 0.3849 0.4222 0.3045 -0.0106 0.0594  -0.0056 40  PRO C CD  
8683  N N   . PRO C  41  ? 0.2568 0.2848 0.2087 -0.0252 0.0750  -0.0058 41  PRO C N   
8684  C CA  . PRO C  41  ? 0.2058 0.2387 0.1702 -0.0277 0.0788  -0.0032 41  PRO C CA  
8685  C C   . PRO C  41  ? 0.2061 0.2438 0.1773 -0.0349 0.0735  -0.0057 41  PRO C C   
8686  O O   . PRO C  41  ? 0.2084 0.2432 0.1846 -0.0398 0.0768  -0.0063 41  PRO C O   
8687  C CB  . PRO C  41  ? 0.2343 0.2570 0.1970 -0.0292 0.0859  -0.0041 41  PRO C CB  
8688  C CG  . PRO C  41  ? 0.2039 0.2175 0.1557 -0.0299 0.0835  -0.0085 41  PRO C CG  
8689  C CD  . PRO C  41  ? 0.2116 0.2281 0.1557 -0.0255 0.0789  -0.0086 41  PRO C CD  
8690  N N   . VAL C  42  ? 0.2124 0.2575 0.1836 -0.0360 0.0656  -0.0072 42  VAL C N   
8691  C CA  . VAL C  42  ? 0.2145 0.2637 0.1921 -0.0443 0.0603  -0.0100 42  VAL C CA  
8692  C C   . VAL C  42  ? 0.2245 0.2913 0.2168 -0.0448 0.0592  -0.0066 42  VAL C C   
8693  O O   . VAL C  42  ? 0.2098 0.2847 0.2062 -0.0376 0.0618  -0.0021 42  VAL C O   
8694  C CB  . VAL C  42  ? 0.3052 0.3505 0.2732 -0.0468 0.0517  -0.0151 42  VAL C CB  
8695  C CG1 . VAL C  42  ? 0.3012 0.3316 0.2549 -0.0433 0.0536  -0.0179 42  VAL C CG1 
8696  C CG2 . VAL C  42  ? 0.3349 0.3929 0.3031 -0.0427 0.0456  -0.0140 42  VAL C CG2 
8697  N N   . GLY C  43  ? 0.4126 0.4853 0.4130 -0.0533 0.0556  -0.0086 43  GLY C N   
8698  C CA  . GLY C  43  ? 0.4172 0.5092 0.4336 -0.0548 0.0545  -0.0059 43  GLY C CA  
8699  C C   . GLY C  43  ? 0.3837 0.4817 0.4100 -0.0501 0.0634  -0.0010 43  GLY C C   
8700  O O   . GLY C  43  ? 0.3795 0.4696 0.4065 -0.0529 0.0704  -0.0008 43  GLY C O   
8701  N N   . SER C  44  ? 0.2742 0.3860 0.3076 -0.0424 0.0628  0.0028  44  SER C N   
8702  C CA  . SER C  44  ? 0.2799 0.3982 0.3229 -0.0361 0.0708  0.0074  44  SER C CA  
8703  C C   . SER C  44  ? 0.2916 0.3931 0.3246 -0.0304 0.0789  0.0089  44  SER C C   
8704  O O   . SER C  44  ? 0.3112 0.4131 0.3499 -0.0267 0.0867  0.0115  44  SER C O   
8705  C CB  . SER C  44  ? 0.4042 0.5397 0.4551 -0.0278 0.0669  0.0112  44  SER C CB  
8706  O OG  . SER C  44  ? 0.4602 0.6015 0.5067 -0.0294 0.0564  0.0090  44  SER C OG  
8707  N N   . ARG C  45  ? 0.2574 0.3448 0.2757 -0.0299 0.0771  0.0069  45  ARG C N   
8708  C CA  . ARG C  45  ? 0.2658 0.3387 0.2750 -0.0255 0.0843  0.0080  45  ARG C CA  
8709  C C   . ARG C  45  ? 0.1914 0.2524 0.1974 -0.0318 0.0891  0.0049  45  ARG C C   
8710  O O   . ARG C  45  ? 0.2019 0.2523 0.2022 -0.0294 0.0953  0.0053  45  ARG C O   
8711  C CB  . ARG C  45  ? 0.4878 0.5534 0.4835 -0.0210 0.0811  0.0078  45  ARG C CB  
8712  C CG  . ARG C  45  ? 0.6355 0.7082 0.6315 -0.0121 0.0800  0.0128  45  ARG C CG  
8713  C CD  . ARG C  45  ? 0.8470 0.9100 0.8279 -0.0077 0.0795  0.0134  45  ARG C CD  
8714  N NE  . ARG C  45  ? 1.0265 1.0965 1.0049 0.0004  0.0762  0.0183  45  ARG C NE  
8715  C CZ  . ARG C  45  ? 1.1369 1.2166 1.1130 0.0010  0.0670  0.0175  45  ARG C CZ  
8716  N NH1 . ARG C  45  ? 1.1660 1.2486 1.1422 -0.0066 0.0603  0.0116  45  ARG C NH1 
8717  N NH2 . ARG C  45  ? 1.1633 1.2491 1.1361 0.0091  0.0641  0.0226  45  ARG C NH2 
8718  N N   . ARG C  46  ? 0.1909 0.2539 0.2006 -0.0400 0.0862  0.0021  46  ARG C N   
8719  C CA  . ARG C  46  ? 0.1885 0.2402 0.1944 -0.0457 0.0902  -0.0001 46  ARG C CA  
8720  C C   . ARG C  46  ? 0.1838 0.2333 0.1933 -0.0436 0.0997  0.0019  46  ARG C C   
8721  O O   . ARG C  46  ? 0.1821 0.2419 0.2021 -0.0416 0.1034  0.0044  46  ARG C O   
8722  C CB  . ARG C  46  ? 0.1909 0.2454 0.2010 -0.0550 0.0862  -0.0022 46  ARG C CB  
8723  C CG  . ARG C  46  ? 0.2406 0.2819 0.2444 -0.0605 0.0892  -0.0041 46  ARG C CG  
8724  C CD  . ARG C  46  ? 0.2213 0.2642 0.2291 -0.0701 0.0862  -0.0051 46  ARG C CD  
8725  N NE  . ARG C  46  ? 0.2031 0.2424 0.2058 -0.0738 0.0776  -0.0083 46  ARG C NE  
8726  C CZ  . ARG C  46  ? 0.2102 0.2456 0.2128 -0.0829 0.0742  -0.0099 46  ARG C CZ  
8727  N NH1 . ARG C  46  ? 0.2101 0.2460 0.2176 -0.0890 0.0790  -0.0080 46  ARG C NH1 
8728  N NH2 . ARG C  46  ? 0.2189 0.2492 0.2158 -0.0861 0.0663  -0.0135 46  ARG C NH2 
8729  N N   . PHE C  47  ? 0.1979 0.2340 0.1985 -0.0431 0.1019  0.0004  47  PHE C N   
8730  C CA  . PHE C  47  ? 0.2154 0.2461 0.2164 -0.0380 0.1019  0.0018  47  PHE C CA  
8731  C C   . PHE C  47  ? 0.2075 0.2398 0.2100 -0.0305 0.1047  0.0044  47  PHE C C   
8732  O O   . PHE C  47  ? 0.2027 0.2330 0.2074 -0.0275 0.1058  0.0051  47  PHE C O   
8733  C CB  . PHE C  47  ? 0.1956 0.2309 0.2038 -0.0405 0.1026  0.0025  47  PHE C CB  
8734  C CG  . PHE C  47  ? 0.1973 0.2341 0.2068 -0.0488 0.1010  0.0012  47  PHE C CG  
8735  C CD1 . PHE C  47  ? 0.2132 0.2382 0.2142 -0.0524 0.0983  -0.0011 47  PHE C CD1 
8736  C CD2 . PHE C  47  ? 0.1821 0.2324 0.2020 -0.0533 0.1024  0.0023  47  PHE C CD2 
8737  C CE1 . PHE C  47  ? 0.2075 0.2315 0.2083 -0.0604 0.0971  -0.0020 47  PHE C CE1 
8738  C CE2 . PHE C  47  ? 0.2330 0.2838 0.2540 -0.0623 0.1006  0.0012  47  PHE C CE2 
8739  C CZ  . PHE C  47  ? 0.2251 0.2614 0.2357 -0.0658 0.0980  -0.0008 47  PHE C CZ  
8740  N N   . MET C  48  ? 0.2653 0.2998 0.2652 -0.0275 0.1061  0.0058  48  MET C N   
8741  C CA  . MET C  48  ? 0.2736 0.3079 0.2740 -0.0201 0.1093  0.0090  48  MET C CA  
8742  C C   . MET C  48  ? 0.2743 0.2982 0.2645 -0.0175 0.1079  0.0088  48  MET C C   
8743  O O   . MET C  48  ? 0.2596 0.2807 0.2429 -0.0199 0.1055  0.0067  48  MET C O   
8744  C CB  . MET C  48  ? 0.1894 0.2362 0.1961 -0.0165 0.1118  0.0126  48  MET C CB  
8745  C CG  . MET C  48  ? 0.2393 0.2996 0.2583 -0.0199 0.1099  0.0123  48  MET C CG  
8746  S SD  . MET C  48  ? 0.5848 0.6566 0.6160 -0.0112 0.1142  0.0170  48  MET C SD  
8747  C CE  . MET C  48  ? 0.1919 0.2462 0.2155 -0.0073 0.1201  0.0168  48  MET C CE  
8748  N N   . PRO C  49  ? 0.2142 0.2322 0.2035 -0.0129 0.1100  0.0106  49  PRO C N   
8749  C CA  . PRO C  49  ? 0.1951 0.2043 0.1764 -0.0108 0.1096  0.0111  49  PRO C CA  
8750  C C   . PRO C  49  ? 0.2438 0.2564 0.2188 -0.0089 0.1099  0.0129  49  PRO C C   
8751  O O   . PRO C  49  ? 0.2436 0.2648 0.2213 -0.0065 0.1125  0.0158  49  PRO C O   
8752  C CB  . PRO C  49  ? 0.3744 0.3789 0.3575 -0.0058 0.1142  0.0143  49  PRO C CB  
8753  C CG  . PRO C  49  ? 0.1988 0.2055 0.1894 -0.0069 0.1151  0.0128  49  PRO C CG  
8754  C CD  . PRO C  49  ? 0.1937 0.2123 0.1896 -0.0098 0.1135  0.0122  49  PRO C CD  
8755  N N   . PRO C  50  ? 0.2000 0.2074 0.1671 -0.0098 0.1076  0.0113  50  PRO C N   
8756  C CA  . PRO C  50  ? 0.2053 0.2155 0.1641 -0.0082 0.1077  0.0121  50  PRO C CA  
8757  C C   . PRO C  50  ? 0.2481 0.2582 0.2025 -0.0015 0.1116  0.0182  50  PRO C C   
8758  O O   . PRO C  50  ? 0.2184 0.2220 0.1735 0.0009  0.1136  0.0207  50  PRO C O   
8759  C CB  . PRO C  50  ? 0.2037 0.2083 0.1566 -0.0102 0.1044  0.0086  50  PRO C CB  
8760  C CG  . PRO C  50  ? 0.2009 0.1998 0.1580 -0.0107 0.1044  0.0085  50  PRO C CG  
8761  C CD  . PRO C  50  ? 0.2501 0.2500 0.2154 -0.0119 0.1050  0.0084  50  PRO C CD  
8762  N N   . GLU C  51  ? 0.5214 0.5393 0.4730 0.0017  0.1073  0.0201  51  GLU C N   
8763  C CA  . GLU C  51  ? 0.6047 0.6231 0.5502 0.0090  0.1068  0.0261  51  GLU C CA  
8764  C C   . GLU C  51  ? 0.6184 0.6330 0.5504 0.0089  0.1052  0.0248  51  GLU C C   
8765  O O   . GLU C  51  ? 0.7137 0.7318 0.6428 0.0055  0.0994  0.0196  51  GLU C O   
8766  C CB  . GLU C  51  ? 0.7868 0.8182 0.7383 0.0130  0.0994  0.0285  51  GLU C CB  
8767  C CG  . GLU C  51  ? 0.9520 0.9860 0.9138 0.0178  0.1032  0.0331  51  GLU C CG  
8768  C CD  . GLU C  51  ? 1.1068 1.1573 1.0783 0.0209  0.0957  0.0345  51  GLU C CD  
8769  O OE1 . GLU C  51  ? 1.1518 1.2114 1.1236 0.0168  0.0876  0.0307  51  GLU C OE1 
8770  O OE2 . GLU C  51  ? 1.1476 1.2022 1.1268 0.0274  0.0980  0.0392  51  GLU C OE2 
8771  N N   . PRO C  52  ? 0.3759 0.3827 0.2993 0.0124  0.1109  0.0294  52  PRO C N   
8772  C CA  . PRO C  52  ? 0.3372 0.3404 0.2475 0.0124  0.1115  0.0285  52  PRO C CA  
8773  C C   . PRO C  52  ? 0.3088 0.3201 0.2116 0.0151  0.1025  0.0277  52  PRO C C   
8774  O O   . PRO C  52  ? 0.2626 0.2814 0.1684 0.0191  0.0968  0.0308  52  PRO C O   
8775  C CB  . PRO C  52  ? 0.4226 0.4177 0.3290 0.0157  0.1159  0.0347  52  PRO C CB  
8776  C CG  . PRO C  52  ? 0.4296 0.4257 0.3405 0.0218  0.1183  0.0412  52  PRO C CG  
8777  C CD  . PRO C  52  ? 0.4367 0.4380 0.3615 0.0177  0.1167  0.0363  52  PRO C CD  
8778  N N   . LYS C  53  ? 0.3401 0.3505 0.2335 0.0132  0.1011  0.0231  53  LYS C N   
8779  C CA  . LYS C  53  ? 0.3525 0.3695 0.2379 0.0148  0.0922  0.0204  53  LYS C CA  
8780  C C   . LYS C  53  ? 0.3938 0.4125 0.2691 0.0217  0.0910  0.0274  53  LYS C C   
8781  O O   . LYS C  53  ? 0.4235 0.4357 0.2891 0.0241  0.0976  0.0317  53  LYS C O   
8782  C CB  . LYS C  53  ? 0.3377 0.3517 0.2139 0.0123  0.0923  0.0138  53  LYS C CB  
8783  C CG  . LYS C  53  ? 0.2786 0.2976 0.1450 0.0136  0.0832  0.0096  53  LYS C CG  
8784  C CD  . LYS C  53  ? 0.3548 0.3784 0.2303 0.0092  0.0749  0.0041  53  LYS C CD  
8785  C CE  . LYS C  53  ? 0.2820 0.3082 0.1475 0.0089  0.0660  -0.0020 53  LYS C CE  
8786  N NZ  . LYS C  53  ? 0.5204 0.5546 0.3800 0.0134  0.0599  0.0020  53  LYS C NZ  
8787  N N   . ARG C  54  ? 0.2868 0.3147 0.1639 0.0247  0.0825  0.0288  54  ARG C N   
8788  C CA  . ARG C  54  ? 0.7896 0.8203 0.6556 0.0319  0.0796  0.0354  54  ARG C CA  
8789  C C   . ARG C  54  ? 0.3133 0.3439 0.1623 0.0323  0.0763  0.0316  54  ARG C C   
8790  O O   . ARG C  54  ? 0.5486 0.5817 0.3971 0.0279  0.0712  0.0233  54  ARG C O   
8791  C CB  . ARG C  54  ? 0.9423 0.9852 0.8166 0.0353  0.0708  0.0377  54  ARG C CB  
8792  C CG  . ARG C  54  ? 1.0398 1.0819 0.9176 0.0427  0.0742  0.0474  54  ARG C CG  
8793  C CD  . ARG C  54  ? 1.1554 1.2127 1.0433 0.0463  0.0649  0.0490  54  ARG C CD  
8794  N NE  . ARG C  54  ? 1.2291 1.2940 1.1340 0.0395  0.0623  0.0424  54  ARG C NE  
8795  C CZ  . ARG C  54  ? 1.2572 1.3316 1.1649 0.0338  0.0536  0.0353  54  ARG C CZ  
8796  N NH1 . ARG C  54  ? 1.2715 1.3494 1.1660 0.0344  0.0461  0.0328  54  ARG C NH1 
8797  N NH2 . ARG C  54  ? 1.2493 1.3290 1.1723 0.0272  0.0527  0.0304  54  ARG C NH2 
8798  N N   . PRO C  55  ? 0.3284 0.3552 0.1626 0.0376  0.0796  0.0379  55  PRO C N   
8799  C CA  . PRO C  55  ? 0.3415 0.3678 0.1574 0.0389  0.0783  0.0354  55  PRO C CA  
8800  C C   . PRO C  55  ? 0.3457 0.3809 0.1571 0.0382  0.0665  0.0282  55  PRO C C   
8801  O O   . PRO C  55  ? 0.3441 0.3882 0.1634 0.0387  0.0579  0.0282  55  PRO C O   
8802  C CB  . PRO C  55  ? 0.3591 0.3826 0.1621 0.0462  0.0810  0.0459  55  PRO C CB  
8803  C CG  . PRO C  55  ? 0.4479 0.4646 0.2621 0.0472  0.0886  0.0532  55  PRO C CG  
8804  C CD  . PRO C  55  ? 0.4014 0.4200 0.2352 0.0414  0.0885  0.0473  55  PRO C CD  
8805  N N   . TRP C  56  ? 0.5076 0.5403 0.3067 0.0367  0.0665  0.0216  56  TRP C N   
8806  C CA  . TRP C  56  ? 0.5614 0.5995 0.3547 0.0349  0.0562  0.0130  56  TRP C CA  
8807  C C   . TRP C  56  ? 0.6579 0.6967 0.4289 0.0400  0.0544  0.0139  56  TRP C C   
8808  O O   . TRP C  56  ? 0.7205 0.7544 0.4809 0.0437  0.0628  0.0200  56  TRP C O   
8809  C CB  . TRP C  56  ? 0.3983 0.4309 0.1954 0.0291  0.0580  0.0030  56  TRP C CB  
8810  C CG  . TRP C  56  ? 0.3679 0.3930 0.1567 0.0298  0.0686  0.0021  56  TRP C CG  
8811  C CD1 . TRP C  56  ? 0.3637 0.3872 0.1348 0.0326  0.0700  -0.0014 56  TRP C CD1 
8812  C CD2 . TRP C  56  ? 0.3371 0.3568 0.1356 0.0276  0.0791  0.0044  56  TRP C CD2 
8813  N NE1 . TRP C  56  ? 0.3792 0.3981 0.1498 0.0322  0.0809  -0.0012 56  TRP C NE1 
8814  C CE2 . TRP C  56  ? 0.3439 0.3605 0.1313 0.0289  0.0862  0.0023  56  TRP C CE2 
8815  C CE3 . TRP C  56  ? 0.3217 0.3397 0.1371 0.0245  0.0830  0.0077  56  TRP C CE3 
8816  C CZ2 . TRP C  56  ? 0.3329 0.3470 0.1333 0.0245  0.0934  0.0026  56  TRP C CZ2 
8817  C CZ3 . TRP C  56  ? 0.3142 0.3271 0.1343 0.0224  0.0930  0.0085  56  TRP C CZ3 
8818  C CH2 . TRP C  56  ? 0.3208 0.3330 0.1364 0.0215  0.0964  0.0057  56  TRP C CH2 
8819  N N   . SER C  57  ? 0.5873 0.6321 0.3506 0.0399  0.0435  0.0077  57  SER C N   
8820  C CA  . SER C  57  ? 0.6055 0.6513 0.3459 0.0446  0.0409  0.0073  57  SER C CA  
8821  C C   . SER C  57  ? 0.5371 0.5775 0.2674 0.0419  0.0416  -0.0039 57  SER C C   
8822  O O   . SER C  57  ? 0.5507 0.5888 0.2909 0.0364  0.0386  -0.0125 57  SER C O   
8823  C CB  . SER C  57  ? 0.8858 0.9426 0.6217 0.0470  0.0277  0.0081  57  SER C CB  
8824  O OG  . SER C  57  ? 0.9362 0.9985 0.6860 0.0408  0.0184  0.0002  57  SER C OG  
8825  N N   . GLY C  58  ? 0.4686 0.5063 0.1789 0.0462  0.0463  -0.0035 58  GLY C N   
8826  C CA  . GLY C  58  ? 0.4712 0.5041 0.1701 0.0453  0.0475  -0.0142 58  GLY C CA  
8827  C C   . GLY C  58  ? 0.4392 0.4651 0.1482 0.0425  0.0594  -0.0149 58  GLY C C   
8828  O O   . GLY C  58  ? 0.4307 0.4555 0.1524 0.0414  0.0667  -0.0074 58  GLY C O   
8829  N N   . VAL C  59  ? 0.4301 0.4514 0.1360 0.0405  0.0608  -0.0238 59  VAL C N   
8830  C CA  . VAL C  59  ? 0.5525 0.5698 0.2723 0.0370  0.0697  -0.0260 59  VAL C CA  
8831  C C   . VAL C  59  ? 0.5321 0.5463 0.2616 0.0347  0.0665  -0.0332 59  VAL C C   
8832  O O   . VAL C  59  ? 0.5238 0.5357 0.2455 0.0349  0.0583  -0.0419 59  VAL C O   
8833  C CB  . VAL C  59  ? 0.4271 0.4429 0.1411 0.0367  0.0735  -0.0315 59  VAL C CB  
8834  C CG1 . VAL C  59  ? 0.4123 0.4265 0.1417 0.0336  0.0793  -0.0362 59  VAL C CG1 
8835  C CG2 . VAL C  59  ? 0.4368 0.4554 0.1454 0.0375  0.0795  -0.0233 59  VAL C CG2 
8836  N N   . LEU C  60  ? 0.6228 0.6363 0.3691 0.0320  0.0726  -0.0295 60  LEU C N   
8837  C CA  . LEU C  60  ? 0.6099 0.6198 0.3664 0.0297  0.0709  -0.0346 60  LEU C CA  
8838  C C   . LEU C  60  ? 0.6288 0.6348 0.3911 0.0280  0.0737  -0.0424 60  LEU C C   
8839  O O   . LEU C  60  ? 0.6581 0.6674 0.4248 0.0276  0.0800  -0.0410 60  LEU C O   
8840  C CB  . LEU C  60  ? 0.3871 0.3983 0.1602 0.0269  0.0758  -0.0264 60  LEU C CB  
8841  C CG  . LEU C  60  ? 0.3554 0.3630 0.1454 0.0218  0.0737  -0.0301 60  LEU C CG  
8842  C CD1 . LEU C  60  ? 0.3566 0.3674 0.1593 0.0185  0.0693  -0.0243 60  LEU C CD1 
8843  C CD2 . LEU C  60  ? 0.3254 0.3317 0.1248 0.0209  0.0832  -0.0293 60  LEU C CD2 
8844  N N   . ASP C  61  ? 0.5080 0.5074 0.2704 0.0272  0.0688  -0.0506 61  ASP C N   
8845  C CA  . ASP C  61  ? 0.5379 0.5339 0.3044 0.0273  0.0704  -0.0581 61  ASP C CA  
8846  C C   . ASP C  61  ? 0.5151 0.5122 0.3001 0.0252  0.0754  -0.0563 61  ASP C C   
8847  O O   . ASP C  61  ? 0.5608 0.5513 0.3508 0.0232  0.0730  -0.0577 61  ASP C O   
8848  C CB  . ASP C  61  ? 0.6926 0.6789 0.4481 0.0278  0.0618  -0.0686 61  ASP C CB  
8849  C CG  . ASP C  61  ? 0.7763 0.7573 0.5379 0.0287  0.0631  -0.0760 61  ASP C CG  
8850  O OD1 . ASP C  61  ? 0.8063 0.7938 0.5767 0.0299  0.0701  -0.0741 61  ASP C OD1 
8851  O OD2 . ASP C  61  ? 0.8184 0.7884 0.5757 0.0281  0.0568  -0.0836 61  ASP C OD2 
8852  N N   . ALA C  62  ? 0.3987 0.4039 0.1932 0.0253  0.0818  -0.0536 62  ALA C N   
8853  C CA  . ALA C  62  ? 0.3859 0.3956 0.1981 0.0241  0.0854  -0.0520 62  ALA C CA  
8854  C C   . ALA C  62  ? 0.4288 0.4378 0.2446 0.0265  0.0852  -0.0598 62  ALA C C   
8855  O O   . ALA C  62  ? 0.4403 0.4557 0.2697 0.0265  0.0882  -0.0587 62  ALA C O   
8856  C CB  . ALA C  62  ? 0.4489 0.4687 0.2707 0.0221  0.0914  -0.0442 62  ALA C CB  
8857  N N   . THR C  63  ? 0.3411 0.3425 0.1442 0.0288  0.0817  -0.0676 63  THR C N   
8858  C CA  . THR C  63  ? 0.4587 0.4568 0.2639 0.0317  0.0819  -0.0751 63  THR C CA  
8859  C C   . THR C  63  ? 0.4569 0.4475 0.2694 0.0325  0.0782  -0.0782 63  THR C C   
8860  O O   . THR C  63  ? 0.4488 0.4368 0.2645 0.0354  0.0788  -0.0834 63  THR C O   
8861  C CB  . THR C  63  ? 0.3669 0.3561 0.1562 0.0345  0.0781  -0.0828 63  THR C CB  
8862  O OG1 . THR C  63  ? 0.3729 0.3519 0.1530 0.0333  0.0703  -0.0854 63  THR C OG1 
8863  C CG2 . THR C  63  ? 0.5508 0.5456 0.3303 0.0349  0.0817  -0.0808 63  THR C CG2 
8864  N N   . THR C  64  ? 0.6172 0.6019 0.4310 0.0298  0.0750  -0.0748 64  THR C N   
8865  C CA  . THR C  64  ? 0.5825 0.5565 0.4009 0.0294  0.0722  -0.0772 64  THR C CA  
8866  C C   . THR C  64  ? 0.5543 0.5253 0.3803 0.0237  0.0729  -0.0709 64  THR C C   
8867  O O   . THR C  64  ? 0.5514 0.5245 0.3755 0.0198  0.0736  -0.0660 64  THR C O   
8868  C CB  . THR C  64  ? 0.5214 0.4793 0.3269 0.0300  0.0654  -0.0855 64  THR C CB  
8869  O OG1 . THR C  64  ? 0.5655 0.5100 0.3731 0.0260  0.0624  -0.0858 64  THR C OG1 
8870  C CG2 . THR C  64  ? 0.5143 0.4704 0.3060 0.0280  0.0617  -0.0865 64  THR C CG2 
8871  N N   . PHE C  65  ? 0.4043 0.3705 0.2387 0.0231  0.0730  -0.0713 65  PHE C N   
8872  C CA  . PHE C  65  ? 0.3708 0.3349 0.2146 0.0170  0.0744  -0.0662 65  PHE C CA  
8873  C C   . PHE C  65  ? 0.2957 0.2514 0.1365 0.0101  0.0699  -0.0657 65  PHE C C   
8874  O O   . PHE C  65  ? 0.3186 0.2642 0.1523 0.0092  0.0630  -0.0708 65  PHE C O   
8875  C CB  . PHE C  65  ? 0.2910 0.2489 0.1403 0.0184  0.0738  -0.0686 65  PHE C CB  
8876  C CG  . PHE C  65  ? 0.2931 0.2643 0.1543 0.0220  0.0775  -0.0658 65  PHE C CG  
8877  C CD1 . PHE C  65  ? 0.2830 0.2666 0.1549 0.0192  0.0813  -0.0586 65  PHE C CD1 
8878  C CD2 . PHE C  65  ? 0.3220 0.2930 0.1838 0.0282  0.0768  -0.0707 65  PHE C CD2 
8879  C CE1 . PHE C  65  ? 0.2895 0.2850 0.1716 0.0217  0.0840  -0.0565 65  PHE C CE1 
8880  C CE2 . PHE C  65  ? 0.3189 0.3039 0.1916 0.0309  0.0800  -0.0689 65  PHE C CE2 
8881  C CZ  . PHE C  65  ? 0.2622 0.2593 0.1447 0.0274  0.0834  -0.0617 65  PHE C CZ  
8882  N N   . GLN C  66  ? 0.4202 0.3823 0.2709 0.0050  0.0719  -0.0587 66  GLN C N   
8883  C CA  . GLN C  66  ? 0.2809 0.2408 0.1358 -0.0015 0.0662  -0.0563 66  GLN C CA  
8884  C C   . GLN C  66  ? 0.2755 0.2281 0.1384 -0.0065 0.0641  -0.0557 66  GLN C C   
8885  O O   . GLN C  66  ? 0.2736 0.2218 0.1383 -0.0046 0.0662  -0.0571 66  GLN C O   
8886  C CB  . GLN C  66  ? 0.3347 0.3051 0.1954 -0.0034 0.0694  -0.0490 66  GLN C CB  
8887  C CG  . GLN C  66  ? 0.3744 0.3497 0.2261 -0.0010 0.0673  -0.0489 66  GLN C CG  
8888  C CD  . GLN C  66  ? 0.3996 0.3723 0.2489 -0.0049 0.0583  -0.0512 66  GLN C CD  
8889  O OE1 . GLN C  66  ? 0.4145 0.3816 0.2698 -0.0102 0.0542  -0.0527 66  GLN C OE1 
8890  N NE2 . GLN C  66  ? 0.4137 0.3911 0.2542 -0.0029 0.0550  -0.0516 66  GLN C NE2 
8891  N N   . ASN C  67  ? 0.2735 0.2260 0.1416 -0.0130 0.0600  -0.0532 67  ASN C N   
8892  C CA  . ASN C  67  ? 0.2713 0.2163 0.1454 -0.0186 0.0577  -0.0527 67  ASN C CA  
8893  C C   . ASN C  67  ? 0.2582 0.2062 0.1412 -0.0192 0.0636  -0.0483 67  ASN C C   
8894  O O   . ASN C  67  ? 0.2826 0.2405 0.1716 -0.0185 0.0690  -0.0437 67  ASN C O   
8895  C CB  . ASN C  67  ? 0.3530 0.3008 0.2324 -0.0257 0.0532  -0.0504 67  ASN C CB  
8896  C CG  . ASN C  67  ? 0.3977 0.3444 0.2688 -0.0261 0.0466  -0.0549 67  ASN C CG  
8897  O OD1 . ASN C  67  ? 0.4137 0.3499 0.2744 -0.0238 0.0431  -0.0612 67  ASN C OD1 
8898  N ND2 . ASN C  67  ? 0.4393 0.3969 0.3145 -0.0284 0.0445  -0.0518 67  ASN C ND2 
8899  N N   . VAL C  68  ? 0.2929 0.2312 0.1761 -0.0204 0.0624  -0.0497 68  VAL C N   
8900  C CA  . VAL C  68  ? 0.2816 0.2217 0.1725 -0.0221 0.0667  -0.0458 68  VAL C CA  
8901  C C   . VAL C  68  ? 0.2437 0.1879 0.1431 -0.0293 0.0671  -0.0410 68  VAL C C   
8902  O O   . VAL C  68  ? 0.2490 0.1897 0.1482 -0.0342 0.0623  -0.0415 68  VAL C O   
8903  C CB  . VAL C  68  ? 0.3600 0.2877 0.2471 -0.0213 0.0643  -0.0482 68  VAL C CB  
8904  C CG1 . VAL C  68  ? 0.3971 0.3267 0.2911 -0.0239 0.0679  -0.0441 68  VAL C CG1 
8905  C CG2 . VAL C  68  ? 0.3476 0.2729 0.2276 -0.0129 0.0645  -0.0531 68  VAL C CG2 
8906  N N   . CYS C  69  ? 0.3000 0.2520 0.2070 -0.0300 0.0729  -0.0367 69  CYS C N   
8907  C CA  . CYS C  69  ? 0.3270 0.2833 0.2425 -0.0358 0.0743  -0.0323 69  CYS C CA  
8908  C C   . CYS C  69  ? 0.3998 0.3472 0.3155 -0.0415 0.0714  -0.0322 69  CYS C C   
8909  O O   . CYS C  69  ? 0.4404 0.3786 0.3510 -0.0402 0.0704  -0.0340 69  CYS C O   
8910  C CB  . CYS C  69  ? 0.2479 0.2116 0.1698 -0.0349 0.0814  -0.0287 69  CYS C CB  
8911  S SG  . CYS C  69  ? 0.6694 0.6432 0.5928 -0.0310 0.0849  -0.0263 69  CYS C SG  
8912  N N   . TYR C  70  ? 0.2288 0.1794 0.1503 -0.0476 0.0702  -0.0299 70  TYR C N   
8913  C CA  . TYR C  70  ? 0.2365 0.1780 0.1571 -0.0540 0.0672  -0.0298 70  TYR C CA  
8914  C C   . TYR C  70  ? 0.4264 0.3637 0.3478 -0.0557 0.0711  -0.0272 70  TYR C C   
8915  O O   . TYR C  70  ? 0.2236 0.1692 0.1515 -0.0560 0.0766  -0.0241 70  TYR C O   
8916  C CB  . TYR C  70  ? 0.2366 0.1853 0.1647 -0.0606 0.0654  -0.0279 70  TYR C CB  
8917  C CG  . TYR C  70  ? 0.2496 0.1880 0.1744 -0.0675 0.0599  -0.0298 70  TYR C CG  
8918  C CD1 . TYR C  70  ? 0.2606 0.1940 0.1795 -0.0679 0.0534  -0.0343 70  TYR C CD1 
8919  C CD2 . TYR C  70  ? 0.2527 0.1856 0.1794 -0.0742 0.0614  -0.0270 70  TYR C CD2 
8920  C CE1 . TYR C  70  ? 0.2749 0.1971 0.1903 -0.0753 0.0483  -0.0364 70  TYR C CE1 
8921  C CE2 . TYR C  70  ? 0.2684 0.1903 0.1916 -0.0816 0.0568  -0.0283 70  TYR C CE2 
8922  C CZ  . TYR C  70  ? 0.2781 0.1942 0.1960 -0.0824 0.0502  -0.0331 70  TYR C CZ  
8923  O OH  . TYR C  70  ? 0.2941 0.1977 0.2081 -0.0906 0.0455  -0.0348 70  TYR C OH  
8924  N N   . GLN C  71  ? 0.2442 0.1678 0.1581 -0.0566 0.0681  -0.0285 71  GLN C N   
8925  C CA  . GLN C  71  ? 0.4138 0.3333 0.3262 -0.0564 0.0712  -0.0263 71  GLN C CA  
8926  C C   . GLN C  71  ? 0.4547 0.3583 0.3592 -0.0593 0.0679  -0.0258 71  GLN C C   
8927  O O   . GLN C  71  ? 0.4909 0.3836 0.3902 -0.0615 0.0628  -0.0279 71  GLN C O   
8928  C CB  . GLN C  71  ? 0.3829 0.3053 0.2930 -0.0484 0.0731  -0.0283 71  GLN C CB  
8929  C CG  . GLN C  71  ? 0.2464 0.1618 0.1490 -0.0425 0.0687  -0.0329 71  GLN C CG  
8930  C CD  . GLN C  71  ? 0.2395 0.1627 0.1426 -0.0351 0.0716  -0.0348 71  GLN C CD  
8931  O OE1 . GLN C  71  ? 0.2421 0.1621 0.1419 -0.0307 0.0714  -0.0360 71  GLN C OE1 
8932  N NE2 . GLN C  71  ? 0.2314 0.1655 0.1388 -0.0338 0.0745  -0.0348 71  GLN C NE2 
8933  N N   . TYR C  72  ? 0.4225 0.3239 0.3253 -0.0590 0.0706  -0.0232 72  TYR C N   
8934  C CA  . TYR C  72  ? 0.4554 0.3410 0.3490 -0.0600 0.0677  -0.0220 72  TYR C CA  
8935  C C   . TYR C  72  ? 0.4598 0.3358 0.3455 -0.0520 0.0631  -0.0262 72  TYR C C   
8936  O O   . TYR C  72  ? 0.4417 0.3263 0.3294 -0.0450 0.0640  -0.0291 72  TYR C O   
8937  C CB  . TYR C  72  ? 0.6489 0.5365 0.5415 -0.0598 0.0715  -0.0186 72  TYR C CB  
8938  C CG  . TYR C  72  ? 0.7469 0.6178 0.6290 -0.0610 0.0686  -0.0161 72  TYR C CG  
8939  C CD1 . TYR C  72  ? 0.8090 0.6712 0.6888 -0.0698 0.0687  -0.0124 72  TYR C CD1 
8940  C CD2 . TYR C  72  ? 0.7916 0.6556 0.6661 -0.0533 0.0657  -0.0171 72  TYR C CD2 
8941  C CE1 . TYR C  72  ? 0.8616 0.7066 0.7303 -0.0711 0.0662  -0.0093 72  TYR C CE1 
8942  C CE2 . TYR C  72  ? 0.8446 0.6919 0.7083 -0.0534 0.0626  -0.0141 72  TYR C CE2 
8943  C CZ  . TYR C  72  ? 0.8678 0.7045 0.7279 -0.0625 0.0630  -0.0100 72  TYR C CZ  
8944  O OH  . TYR C  72  ? 0.8722 0.6905 0.7202 -0.0630 0.0603  -0.0062 72  TYR C OH  
8945  N N   . VAL C  73  ? 0.6683 0.5265 0.5451 -0.0531 0.0583  -0.0267 73  VAL C N   
8946  C CA  . VAL C  73  ? 0.6407 0.4877 0.5088 -0.0444 0.0541  -0.0305 73  VAL C CA  
8947  C C   . VAL C  73  ? 0.7174 0.5518 0.5775 -0.0420 0.0527  -0.0274 73  VAL C C   
8948  O O   . VAL C  73  ? 0.7995 0.6228 0.6554 -0.0490 0.0524  -0.0232 73  VAL C O   
8949  C CB  . VAL C  73  ? 0.3275 0.1610 0.1898 -0.0461 0.0492  -0.0343 73  VAL C CB  
8950  C CG1 . VAL C  73  ? 0.3363 0.1581 0.1895 -0.0359 0.0455  -0.0387 73  VAL C CG1 
8951  C CG2 . VAL C  73  ? 0.3134 0.1601 0.1829 -0.0485 0.0499  -0.0371 73  VAL C CG2 
8952  N N   . ASP C  74  ? 0.4243 0.2608 0.2820 -0.0321 0.0519  -0.0292 74  ASP C N   
8953  C CA  . ASP C  74  ? 0.4803 0.3095 0.3316 -0.0291 0.0508  -0.0255 74  ASP C CA  
8954  C C   . ASP C  74  ? 0.5781 0.3823 0.4166 -0.0271 0.0454  -0.0247 74  ASP C C   
8955  O O   . ASP C  74  ? 0.5872 0.3824 0.4206 -0.0194 0.0417  -0.0291 74  ASP C O   
8956  C CB  . ASP C  74  ? 0.6750 0.5175 0.5296 -0.0194 0.0514  -0.0277 74  ASP C CB  
8957  C CG  . ASP C  74  ? 0.7429 0.5814 0.5918 -0.0165 0.0499  -0.0238 74  ASP C CG  
8958  O OD1 . ASP C  74  ? 0.7734 0.6091 0.6203 -0.0240 0.0517  -0.0188 74  ASP C OD1 
8959  O OD2 . ASP C  74  ? 0.7499 0.5890 0.5964 -0.0064 0.0469  -0.0258 74  ASP C OD2 
8960  N N   . THR C  75  ? 0.9206 0.7131 0.7532 -0.0341 0.0455  -0.0189 75  THR C N   
8961  C CA  . THR C  75  ? 1.0182 0.7843 0.8379 -0.0345 0.0411  -0.0170 75  THR C CA  
8962  C C   . THR C  75  ? 1.0178 0.7730 0.8272 -0.0263 0.0382  -0.0134 75  THR C C   
8963  O O   . THR C  75  ? 1.0920 0.8232 0.8892 -0.0253 0.0344  -0.0111 75  THR C O   
8964  C CB  . THR C  75  ? 1.1691 0.9264 0.9875 -0.0485 0.0429  -0.0125 75  THR C CB  
8965  O OG1 . THR C  75  ? 1.2235 0.9863 1.0417 -0.0531 0.0466  -0.0060 75  THR C OG1 
8966  C CG2 . THR C  75  ? 1.1605 0.9324 0.9907 -0.0559 0.0454  -0.0158 75  THR C CG2 
8967  N N   . LEU C  76  ? 0.7966 0.5689 0.6106 -0.0205 0.0396  -0.0128 76  LEU C N   
8968  C CA  . LEU C  76  ? 0.7746 0.5404 0.5796 -0.0137 0.0367  -0.0085 76  LEU C CA  
8969  C C   . LEU C  76  ? 0.7644 0.5120 0.5591 -0.0016 0.0305  -0.0098 76  LEU C C   
8970  O O   . LEU C  76  ? 0.7696 0.4964 0.5513 -0.0003 0.0273  -0.0045 76  LEU C O   
8971  C CB  . LEU C  76  ? 0.7460 0.5362 0.5593 -0.0097 0.0389  -0.0092 76  LEU C CB  
8972  C CG  . LEU C  76  ? 0.6842 0.4723 0.4894 -0.0021 0.0352  -0.0055 76  LEU C CG  
8973  C CD1 . LEU C  76  ? 0.6883 0.4617 0.4819 -0.0096 0.0357  0.0024  76  LEU C CD1 
8974  C CD2 . LEU C  76  ? 0.6143 0.4280 0.4291 0.0013  0.0369  -0.0079 76  LEU C CD2 
8975  N N   . TYR C  77  ? 0.8361 0.5918 0.6362 0.0079  0.0291  -0.0167 77  TYR C N   
8976  C CA  . TYR C  77  ? 0.8559 0.5971 0.6478 0.0211  0.0238  -0.0189 77  TYR C CA  
8977  C C   . TYR C  77  ? 0.8749 0.6098 0.6678 0.0234  0.0233  -0.0262 77  TYR C C   
8978  O O   . TYR C  77  ? 0.9030 0.6537 0.7036 0.0315  0.0240  -0.0322 77  TYR C O   
8979  C CB  . TYR C  77  ? 0.7612 0.5222 0.5593 0.0333  0.0225  -0.0209 77  TYR C CB  
8980  C CG  . TYR C  77  ? 0.7588 0.5238 0.5532 0.0341  0.0211  -0.0146 77  TYR C CG  
8981  C CD1 . TYR C  77  ? 0.7971 0.5386 0.5768 0.0328  0.0179  -0.0075 77  TYR C CD1 
8982  C CD2 . TYR C  77  ? 0.7619 0.5538 0.5667 0.0358  0.0228  -0.0157 77  TYR C CD2 
8983  C CE1 . TYR C  77  ? 0.8313 0.5764 0.6059 0.0339  0.0163  -0.0015 77  TYR C CE1 
8984  C CE2 . TYR C  77  ? 0.7860 0.5821 0.5866 0.0365  0.0209  -0.0105 77  TYR C CE2 
8985  C CZ  . TYR C  77  ? 0.8186 0.5915 0.6036 0.0359  0.0175  -0.0033 77  TYR C CZ  
8986  O OH  . TYR C  77  ? 0.8273 0.6037 0.6061 0.0367  0.0154  0.0021  77  TYR C OH  
8987  N N   . PRO C  78  ? 0.7907 0.5030 0.5756 0.0159  0.0222  -0.0258 78  PRO C N   
8988  C CA  . PRO C  78  ? 0.7745 0.4795 0.5587 0.0165  0.0213  -0.0331 78  PRO C CA  
8989  C C   . PRO C  78  ? 0.7770 0.4791 0.5582 0.0327  0.0184  -0.0394 78  PRO C C   
8990  O O   . PRO C  78  ? 0.7954 0.4839 0.5681 0.0428  0.0147  -0.0373 78  PRO C O   
8991  C CB  . PRO C  78  ? 0.6645 0.3396 0.4369 0.0076  0.0190  -0.0304 78  PRO C CB  
8992  C CG  . PRO C  78  ? 0.6533 0.3323 0.4273 -0.0040 0.0218  -0.0221 78  PRO C CG  
8993  C CD  . PRO C  78  ? 0.6667 0.3611 0.4434 0.0044  0.0223  -0.0186 78  PRO C CD  
8994  N N   . GLY C  79  ? 0.7700 0.4859 0.5581 0.0356  0.0202  -0.0468 79  GLY C N   
8995  C CA  . GLY C  79  ? 0.7888 0.5042 0.5748 0.0505  0.0186  -0.0537 79  GLY C CA  
8996  C C   . GLY C  79  ? 0.8072 0.5396 0.5989 0.0631  0.0185  -0.0528 79  GLY C C   
8997  O O   . GLY C  79  ? 0.8747 0.6011 0.6621 0.0772  0.0159  -0.0564 79  GLY C O   
8998  N N   . PHE C  80  ? 0.7438 0.4978 0.5452 0.0582  0.0212  -0.0482 80  PHE C N   
8999  C CA  . PHE C  80  ? 0.7204 0.4935 0.5286 0.0686  0.0209  -0.0476 80  PHE C CA  
9000  C C   . PHE C  80  ? 0.7040 0.5083 0.5272 0.0678  0.0261  -0.0517 80  PHE C C   
9001  O O   . PHE C  80  ? 0.7216 0.5396 0.5523 0.0567  0.0300  -0.0493 80  PHE C O   
9002  C CB  . PHE C  80  ? 0.6654 0.4376 0.4713 0.0644  0.0193  -0.0393 80  PHE C CB  
9003  C CG  . PHE C  80  ? 0.6653 0.4628 0.4807 0.0711  0.0193  -0.0387 80  PHE C CG  
9004  C CD1 . PHE C  80  ? 0.7101 0.5140 0.5272 0.0866  0.0163  -0.0421 80  PHE C CD1 
9005  C CD2 . PHE C  80  ? 0.6616 0.4768 0.4844 0.0618  0.0224  -0.0351 80  PHE C CD2 
9006  C CE1 . PHE C  80  ? 0.7097 0.5389 0.5366 0.0920  0.0159  -0.0419 80  PHE C CE1 
9007  C CE2 . PHE C  80  ? 0.6747 0.5131 0.5061 0.0669  0.0220  -0.0352 80  PHE C CE2 
9008  C CZ  . PHE C  80  ? 0.6882 0.5343 0.5221 0.0816  0.0186  -0.0386 80  PHE C CZ  
9009  N N   . GLU C  81  ? 0.6215 0.4366 0.4488 0.0797  0.0266  -0.0579 81  GLU C N   
9010  C CA  . GLU C  81  ? 0.6601 0.5028 0.5004 0.0792  0.0322  -0.0622 81  GLU C CA  
9011  C C   . GLU C  81  ? 0.6143 0.4807 0.4663 0.0719  0.0355  -0.0583 81  GLU C C   
9012  O O   . GLU C  81  ? 0.6063 0.4901 0.4673 0.0654  0.0409  -0.0598 81  GLU C O   
9013  C CB  . GLU C  81  ? 0.9823 0.8348 0.8256 0.0945  0.0322  -0.0685 81  GLU C CB  
9014  C CG  . GLU C  81  ? 1.0796 0.9588 0.9347 0.0942  0.0386  -0.0731 81  GLU C CG  
9015  C CD  . GLU C  81  ? 1.1902 1.0804 1.0488 0.1096  0.0391  -0.0793 81  GLU C CD  
9016  O OE1 . GLU C  81  ? 1.2343 1.1084 1.0836 0.1174  0.0378  -0.0843 81  GLU C OE1 
9017  O OE2 . GLU C  81  ? 1.2063 1.1215 1.0770 0.1139  0.0410  -0.0795 81  GLU C OE2 
9018  N N   . GLY C  82  ? 0.6746 0.5403 0.5254 0.0727  0.0322  -0.0533 82  GLY C N   
9019  C CA  . GLY C  82  ? 0.6336 0.5194 0.4936 0.0657  0.0348  -0.0502 82  GLY C CA  
9020  C C   . GLY C  82  ? 0.5884 0.4734 0.4499 0.0508  0.0390  -0.0473 82  GLY C C   
9021  O O   . GLY C  82  ? 0.5942 0.4983 0.4660 0.0453  0.0442  -0.0487 82  GLY C O   
9022  N N   . THR C  83  ? 0.4717 0.3351 0.3233 0.0442  0.0371  -0.0431 83  THR C N   
9023  C CA  . THR C  83  ? 0.4270 0.2899 0.2804 0.0306  0.0410  -0.0404 83  THR C CA  
9024  C C   . THR C  83  ? 0.4054 0.2654 0.2598 0.0276  0.0433  -0.0443 83  THR C C   
9025  O O   . THR C  83  ? 0.4036 0.2719 0.2638 0.0186  0.0475  -0.0436 83  THR C O   
9026  C CB  . THR C  83  ? 0.4088 0.2513 0.2521 0.0235  0.0387  -0.0343 83  THR C CB  
9027  O OG1 . THR C  83  ? 0.3669 0.1858 0.2000 0.0254  0.0352  -0.0352 83  THR C OG1 
9028  C CG2 . THR C  83  ? 0.4195 0.2611 0.2583 0.0273  0.0355  -0.0299 83  THR C CG2 
9029  N N   . GLU C  84  ? 0.3466 0.1943 0.1945 0.0356  0.0402  -0.0484 84  GLU C N   
9030  C CA  . GLU C  84  ? 0.3765 0.2173 0.2220 0.0329  0.0410  -0.0525 84  GLU C CA  
9031  C C   . GLU C  84  ? 0.3343 0.1969 0.1891 0.0349  0.0458  -0.0569 84  GLU C C   
9032  O O   . GLU C  84  ? 0.3296 0.1928 0.1845 0.0305  0.0476  -0.0592 84  GLU C O   
9033  C CB  . GLU C  84  ? 0.7062 0.5242 0.5398 0.0409  0.0360  -0.0559 84  GLU C CB  
9034  C CG  . GLU C  84  ? 0.8515 0.6546 0.6787 0.0350  0.0350  -0.0590 84  GLU C CG  
9035  C CD  . GLU C  84  ? 0.9500 0.7417 0.7748 0.0214  0.0344  -0.0537 84  GLU C CD  
9036  O OE1 . GLU C  84  ? 0.9840 0.7584 0.8014 0.0202  0.0314  -0.0493 84  GLU C OE1 
9037  O OE2 . GLU C  84  ? 0.9576 0.7581 0.7879 0.0123  0.0370  -0.0538 84  GLU C OE2 
9038  N N   . MET C  85  ? 0.3996 0.2805 0.2621 0.0413  0.0478  -0.0577 85  MET C N   
9039  C CA  . MET C  85  ? 0.3716 0.2735 0.2430 0.0429  0.0530  -0.0614 85  MET C CA  
9040  C C   . MET C  85  ? 0.3517 0.2634 0.2294 0.0315  0.0578  -0.0585 85  MET C C   
9041  O O   . MET C  85  ? 0.3442 0.2655 0.2251 0.0305  0.0617  -0.0608 85  MET C O   
9042  C CB  . MET C  85  ? 0.3162 0.2368 0.1956 0.0511  0.0542  -0.0629 85  MET C CB  
9043  C CG  . MET C  85  ? 0.2872 0.2256 0.1767 0.0446  0.0572  -0.0593 85  MET C CG  
9044  S SD  . MET C  85  ? 0.6088 0.5679 0.5073 0.0537  0.0565  -0.0612 85  MET C SD  
9045  C CE  . MET C  85  ? 0.4290 0.4055 0.3344 0.0612  0.0614  -0.0677 85  MET C CE  
9046  N N   . TRP C  86  ? 0.3588 0.2673 0.2374 0.0234  0.0575  -0.0533 86  TRP C N   
9047  C CA  . TRP C  86  ? 0.3920 0.3099 0.2771 0.0136  0.0622  -0.0504 86  TRP C CA  
9048  C C   . TRP C  86  ? 0.4614 0.3680 0.3425 0.0060  0.0616  -0.0490 86  TRP C C   
9049  O O   . TRP C  86  ? 0.4607 0.3752 0.3473 -0.0008 0.0653  -0.0470 86  TRP C O   
9050  C CB  . TRP C  86  ? 0.3692 0.2924 0.2581 0.0090  0.0631  -0.0462 86  TRP C CB  
9051  C CG  . TRP C  86  ? 0.3772 0.3120 0.2700 0.0157  0.0626  -0.0477 86  TRP C CG  
9052  C CD1 . TRP C  86  ? 0.3945 0.3237 0.2829 0.0209  0.0578  -0.0465 86  TRP C CD1 
9053  C CD2 . TRP C  86  ? 0.3855 0.3407 0.2880 0.0177  0.0669  -0.0504 86  TRP C CD2 
9054  N NE1 . TRP C  86  ? 0.4034 0.3499 0.2990 0.0263  0.0583  -0.0487 86  TRP C NE1 
9055  C CE2 . TRP C  86  ? 0.4098 0.3727 0.3145 0.0239  0.0641  -0.0513 86  TRP C CE2 
9056  C CE3 . TRP C  86  ? 0.3535 0.3211 0.2627 0.0147  0.0728  -0.0518 86  TRP C CE3 
9057  C CZ2 . TRP C  86  ? 0.3817 0.3656 0.2964 0.0263  0.0672  -0.0541 86  TRP C CZ2 
9058  C CZ3 . TRP C  86  ? 0.3337 0.3201 0.2517 0.0169  0.0763  -0.0541 86  TRP C CZ3 
9059  C CH2 . TRP C  86  ? 0.3195 0.3146 0.2408 0.0222  0.0736  -0.0555 86  TRP C CH2 
9060  N N   . ASN C  87  ? 0.5596 0.4478 0.4316 0.0073  0.0567  -0.0501 87  ASN C N   
9061  C CA  . ASN C  87  ? 0.5946 0.4726 0.4634 -0.0007 0.0553  -0.0491 87  ASN C CA  
9062  C C   . ASN C  87  ? 0.5631 0.4479 0.4331 -0.0005 0.0568  -0.0528 87  ASN C C   
9063  O O   . ASN C  87  ? 0.5903 0.4816 0.4598 0.0073  0.0579  -0.0570 87  ASN C O   
9064  C CB  . ASN C  87  ? 0.7411 0.5959 0.5991 -0.0002 0.0496  -0.0495 87  ASN C CB  
9065  C CG  . ASN C  87  ? 0.8273 0.6730 0.6832 -0.0060 0.0485  -0.0437 87  ASN C CG  
9066  O OD1 . ASN C  87  ? 0.8549 0.7022 0.7142 -0.0158 0.0504  -0.0399 87  ASN C OD1 
9067  N ND2 . ASN C  87  ? 0.8660 0.7024 0.7159 0.0004  0.0456  -0.0427 87  ASN C ND2 
9068  N N   . PRO C  88  ? 0.4179 0.3025 0.2896 -0.0088 0.0569  -0.0511 88  PRO C N   
9069  C CA  . PRO C  88  ? 0.3747 0.2655 0.2465 -0.0092 0.0575  -0.0539 88  PRO C CA  
9070  C C   . PRO C  88  ? 0.4217 0.3018 0.2837 -0.0031 0.0536  -0.0602 88  PRO C C   
9071  O O   . PRO C  88  ? 0.4412 0.3036 0.2957 -0.0040 0.0488  -0.0617 88  PRO C O   
9072  C CB  . PRO C  88  ? 0.2901 0.1785 0.1644 -0.0192 0.0562  -0.0508 88  PRO C CB  
9073  C CG  . PRO C  88  ? 0.2903 0.1813 0.1704 -0.0239 0.0588  -0.0453 88  PRO C CG  
9074  C CD  . PRO C  88  ? 0.3266 0.2086 0.2016 -0.0182 0.0572  -0.0458 88  PRO C CD  
9075  N N   . ASN C  89  ? 0.5614 0.4514 0.4228 0.0030  0.0561  -0.0638 89  ASN C N   
9076  C CA  . ASN C  89  ? 0.6167 0.4987 0.4681 0.0097  0.0534  -0.0706 89  ASN C CA  
9077  C C   . ASN C  89  ? 0.6033 0.4859 0.4502 0.0065  0.0517  -0.0733 89  ASN C C   
9078  O O   . ASN C  89  ? 0.6068 0.4847 0.4448 0.0120  0.0501  -0.0794 89  ASN C O   
9079  C CB  . ASN C  89  ? 0.6535 0.5458 0.5058 0.0200  0.0574  -0.0736 89  ASN C CB  
9080  C CG  . ASN C  89  ? 0.6287 0.5410 0.4878 0.0193  0.0636  -0.0717 89  ASN C CG  
9081  O OD1 . ASN C  89  ? 0.5917 0.5102 0.4556 0.0119  0.0650  -0.0673 89  ASN C OD1 
9082  N ND2 . ASN C  89  ? 0.6441 0.5666 0.5035 0.0273  0.0675  -0.0747 89  ASN C ND2 
9083  N N   . ARG C  90  ? 0.6516 0.5417 0.5045 -0.0018 0.0522  -0.0689 90  ARG C N   
9084  C CA  . ARG C  90  ? 0.6684 0.5589 0.5171 -0.0055 0.0491  -0.0711 90  ARG C CA  
9085  C C   . ARG C  90  ? 0.7382 0.6239 0.5910 -0.0160 0.0454  -0.0678 90  ARG C C   
9086  O O   . ARG C  90  ? 0.8016 0.6817 0.6587 -0.0198 0.0456  -0.0642 90  ARG C O   
9087  C CB  . ARG C  90  ? 0.4636 0.3719 0.3160 -0.0039 0.0538  -0.0690 90  ARG C CB  
9088  C CG  . ARG C  90  ? 0.4656 0.3792 0.3129 0.0055  0.0576  -0.0727 90  ARG C CG  
9089  C CD  . ARG C  90  ? 0.5422 0.4526 0.3777 0.0083  0.0545  -0.0786 90  ARG C CD  
9090  N NE  . ARG C  90  ? 0.5793 0.4962 0.4097 0.0174  0.0592  -0.0821 90  ARG C NE  
9091  C CZ  . ARG C  90  ? 0.6056 0.5171 0.4329 0.0249  0.0602  -0.0866 90  ARG C CZ  
9092  N NH1 . ARG C  90  ? 0.5865 0.4844 0.4143 0.0247  0.0565  -0.0876 90  ARG C NH1 
9093  N NH2 . ARG C  90  ? 0.6509 0.5757 0.4811 0.0321  0.0629  -0.0880 90  ARG C NH2 
9094  N N   . GLU C  91  ? 0.4574 0.3460 0.3088 -0.0206 0.0419  -0.0691 91  GLU C N   
9095  C CA  . GLU C  91  ? 0.4360 0.3220 0.2924 -0.0310 0.0383  -0.0666 91  GLU C CA  
9096  C C   . GLU C  91  ? 0.3102 0.2118 0.1798 -0.0350 0.0429  -0.0590 91  GLU C C   
9097  O O   . GLU C  91  ? 0.2885 0.2036 0.1620 -0.0309 0.0474  -0.0566 91  GLU C O   
9098  C CB  . GLU C  91  ? 0.8590 0.7436 0.7097 -0.0347 0.0320  -0.0712 91  GLU C CB  
9099  C CG  . GLU C  91  ? 0.9914 0.8944 0.8484 -0.0366 0.0325  -0.0681 91  GLU C CG  
9100  C CD  . GLU C  91  ? 1.0962 0.9990 0.9530 -0.0449 0.0253  -0.0706 91  GLU C CD  
9101  O OE1 . GLU C  91  ? 1.1401 1.0284 0.9865 -0.0463 0.0197  -0.0774 91  GLU C OE1 
9102  O OE2 . GLU C  91  ? 1.1065 1.0235 0.9736 -0.0498 0.0251  -0.0660 91  GLU C OE2 
9103  N N   . LEU C  92  ? 0.3504 0.2493 0.2266 -0.0429 0.0424  -0.0553 92  LEU C N   
9104  C CA  . LEU C  92  ? 0.3178 0.2303 0.2060 -0.0461 0.0474  -0.0487 92  LEU C CA  
9105  C C   . LEU C  92  ? 0.3091 0.2345 0.2042 -0.0508 0.0457  -0.0470 92  LEU C C   
9106  O O   . LEU C  92  ? 0.3339 0.2559 0.2284 -0.0572 0.0401  -0.0492 92  LEU C O   
9107  C CB  . LEU C  92  ? 0.2816 0.1871 0.1736 -0.0524 0.0483  -0.0452 92  LEU C CB  
9108  C CG  . LEU C  92  ? 0.2867 0.1793 0.1727 -0.0486 0.0494  -0.0456 92  LEU C CG  
9109  C CD1 . LEU C  92  ? 0.2834 0.1743 0.1746 -0.0551 0.0519  -0.0403 92  LEU C CD1 
9110  C CD2 . LEU C  92  ? 0.2775 0.1774 0.1632 -0.0394 0.0538  -0.0460 92  LEU C CD2 
9111  N N   . SER C  93  ? 0.4010 0.3411 0.3029 -0.0478 0.0503  -0.0431 93  SER C N   
9112  C CA  . SER C  93  ? 0.4224 0.3759 0.3325 -0.0513 0.0490  -0.0403 93  SER C CA  
9113  C C   . SER C  93  ? 0.4101 0.3754 0.3303 -0.0499 0.0558  -0.0342 93  SER C C   
9114  O O   . SER C  93  ? 0.4226 0.3872 0.3417 -0.0451 0.0613  -0.0329 93  SER C O   
9115  C CB  . SER C  93  ? 0.4072 0.3661 0.3112 -0.0474 0.0450  -0.0431 93  SER C CB  
9116  O OG  . SER C  93  ? 0.3961 0.3644 0.3065 -0.0529 0.0403  -0.0423 93  SER C OG  
9117  N N   . GLU C  94  ? 0.3286 0.3052 0.2588 -0.0540 0.0553  -0.0309 94  GLU C N   
9118  C CA  . GLU C  94  ? 0.2275 0.2149 0.1665 -0.0514 0.0617  -0.0256 94  GLU C CA  
9119  C C   . GLU C  94  ? 0.2266 0.2198 0.1615 -0.0439 0.0625  -0.0249 94  GLU C C   
9120  O O   . GLU C  94  ? 0.2188 0.2167 0.1572 -0.0400 0.0686  -0.0210 94  GLU C O   
9121  C CB  . GLU C  94  ? 0.2240 0.2230 0.1755 -0.0566 0.0613  -0.0224 94  GLU C CB  
9122  C CG  . GLU C  94  ? 0.2195 0.2163 0.1773 -0.0618 0.0659  -0.0201 94  GLU C CG  
9123  C CD  . GLU C  94  ? 0.2626 0.2711 0.2328 -0.0681 0.0652  -0.0178 94  GLU C CD  
9124  O OE1 . GLU C  94  ? 0.2459 0.2587 0.2179 -0.0726 0.0586  -0.0198 94  GLU C OE1 
9125  O OE2 . GLU C  94  ? 0.2794 0.2933 0.2575 -0.0688 0.0714  -0.0143 94  GLU C OE2 
9126  N N   . ASP C  95  ? 0.2363 0.2273 0.1622 -0.0420 0.0569  -0.0287 95  ASP C N   
9127  C CA  . ASP C  95  ? 0.2938 0.2899 0.2140 -0.0349 0.0580  -0.0276 95  ASP C CA  
9128  C C   . ASP C  95  ? 0.3227 0.3096 0.2338 -0.0307 0.0616  -0.0303 95  ASP C C   
9129  O O   . ASP C  95  ? 0.2488 0.2292 0.1496 -0.0290 0.0578  -0.0355 95  ASP C O   
9130  C CB  . ASP C  95  ? 0.2739 0.2727 0.1877 -0.0353 0.0497  -0.0311 95  ASP C CB  
9131  C CG  . ASP C  95  ? 0.2799 0.2836 0.1852 -0.0281 0.0499  -0.0300 95  ASP C CG  
9132  O OD1 . ASP C  95  ? 0.2907 0.2922 0.1921 -0.0229 0.0564  -0.0281 95  ASP C OD1 
9133  O OD2 . ASP C  95  ? 0.2734 0.2835 0.1755 -0.0280 0.0434  -0.0311 95  ASP C OD2 
9134  N N   . CYS C  96  ? 0.2295 0.2165 0.1446 -0.0288 0.0690  -0.0271 96  CYS C N   
9135  C CA  . CYS C  96  ? 0.2289 0.2100 0.1384 -0.0253 0.0732  -0.0293 96  CYS C CA  
9136  C C   . CYS C  96  ? 0.2256 0.2108 0.1332 -0.0202 0.0799  -0.0267 96  CYS C C   
9137  O O   . CYS C  96  ? 0.2258 0.2080 0.1295 -0.0177 0.0830  -0.0290 96  CYS C O   
9138  C CB  . CYS C  96  ? 0.2506 0.2255 0.1643 -0.0286 0.0752  -0.0299 96  CYS C CB  
9139  S SG  . CYS C  96  ? 0.4826 0.4623 0.4086 -0.0335 0.0791  -0.0246 96  CYS C SG  
9140  N N   . LEU C  97  ? 0.2914 0.2835 0.2020 -0.0187 0.0824  -0.0217 97  LEU C N   
9141  C CA  . LEU C  97  ? 0.2851 0.2786 0.1957 -0.0158 0.0902  -0.0185 97  LEU C CA  
9142  C C   . LEU C  97  ? 0.2956 0.2903 0.1957 -0.0110 0.0906  -0.0193 97  LEU C C   
9143  O O   . LEU C  97  ? 0.3060 0.3046 0.2022 -0.0085 0.0890  -0.0163 97  LEU C O   
9144  C CB  . LEU C  97  ? 0.2154 0.2131 0.1335 -0.0160 0.0939  -0.0123 97  LEU C CB  
9145  C CG  . LEU C  97  ? 0.2075 0.2054 0.1362 -0.0204 0.0947  -0.0113 97  LEU C CG  
9146  C CD1 . LEU C  97  ? 0.2050 0.2075 0.1412 -0.0192 0.0976  -0.0056 97  LEU C CD1 
9147  C CD2 . LEU C  97  ? 0.3411 0.3353 0.2755 -0.0210 0.0934  -0.0123 97  LEU C CD2 
9148  N N   . TYR C  98  ? 0.2287 0.2218 0.1267 -0.0090 0.0910  -0.0225 98  TYR C N   
9149  C CA  . TYR C  98  ? 0.2365 0.2319 0.1261 -0.0041 0.0908  -0.0238 98  TYR C CA  
9150  C C   . TYR C  98  ? 0.2923 0.2911 0.1904 -0.0027 0.0912  -0.0234 98  TYR C C   
9151  O O   . TYR C  98  ? 0.3187 0.3152 0.2238 -0.0049 0.0904  -0.0249 98  TYR C O   
9152  C CB  . TYR C  98  ? 0.2482 0.2381 0.1246 -0.0032 0.0877  -0.0314 98  TYR C CB  
9153  C CG  . TYR C  98  ? 0.3086 0.2983 0.1837 -0.0050 0.0798  -0.0315 98  TYR C CG  
9154  C CD1 . TYR C  98  ? 0.2490 0.2356 0.1314 -0.0100 0.0751  -0.0326 98  TYR C CD1 
9155  C CD2 . TYR C  98  ? 0.2624 0.2561 0.1293 -0.0023 0.0771  -0.0302 98  TYR C CD2 
9156  C CE1 . TYR C  98  ? 0.2535 0.2417 0.1362 -0.0127 0.0681  -0.0329 98  TYR C CE1 
9157  C CE2 . TYR C  98  ? 0.2669 0.2625 0.1337 -0.0043 0.0694  -0.0306 98  TYR C CE2 
9158  C CZ  . TYR C  98  ? 0.2621 0.2554 0.1376 -0.0098 0.0650  -0.0321 98  TYR C CZ  
9159  O OH  . TYR C  98  ? 0.2669 0.2639 0.1438 -0.0129 0.0572  -0.0327 98  TYR C OH  
9160  N N   . LEU C  99  ? 0.2450 0.2498 0.1419 0.0004  0.0928  -0.0215 99  LEU C N   
9161  C CA  . LEU C  99  ? 0.2266 0.2362 0.1310 0.0012  0.0935  -0.0219 99  LEU C CA  
9162  C C   . LEU C  99  ? 0.2344 0.2484 0.1320 0.0057  0.0936  -0.0259 99  LEU C C   
9163  O O   . LEU C  99  ? 0.2447 0.2568 0.1310 0.0082  0.0927  -0.0288 99  LEU C O   
9164  C CB  . LEU C  99  ? 0.2213 0.2349 0.1339 -0.0009 0.0959  -0.0161 99  LEU C CB  
9165  C CG  . LEU C  99  ? 0.2281 0.2428 0.1356 -0.0004 0.0982  -0.0113 99  LEU C CG  
9166  C CD1 . LEU C  99  ? 0.2357 0.2566 0.1378 0.0021  0.1001  -0.0117 99  LEU C CD1 
9167  C CD2 . LEU C  99  ? 0.2238 0.2368 0.1389 -0.0033 0.1000  -0.0061 99  LEU C CD2 
9168  N N   . ASN C  100 ? 0.3298 0.3499 0.2338 0.0067  0.0947  -0.0265 100 ASN C N   
9169  C CA  . ASN C  100 ? 0.3208 0.3465 0.2201 0.0116  0.0951  -0.0309 100 ASN C CA  
9170  C C   . ASN C  100 ? 0.3247 0.3611 0.2299 0.0118  0.0986  -0.0280 100 ASN C C   
9171  O O   . ASN C  100 ? 0.3192 0.3572 0.2337 0.0086  0.0996  -0.0248 100 ASN C O   
9172  C CB  . ASN C  100 ? 0.2642 0.2861 0.1645 0.0137  0.0928  -0.0367 100 ASN C CB  
9173  C CG  . ASN C  100 ? 0.2647 0.2746 0.1588 0.0122  0.0897  -0.0397 100 ASN C CG  
9174  O OD1 . ASN C  100 ? 0.2493 0.2546 0.1328 0.0134  0.0884  -0.0421 100 ASN C OD1 
9175  N ND2 . ASN C  100 ? 0.2329 0.2375 0.1327 0.0090  0.0885  -0.0396 100 ASN C ND2 
9176  N N   . VAL C  101 ? 0.2450 0.2884 0.1440 0.0150  0.1006  -0.0292 101 VAL C N   
9177  C CA  . VAL C  101 ? 0.2738 0.3278 0.1776 0.0148  0.1046  -0.0264 101 VAL C CA  
9178  C C   . VAL C  101 ? 0.2617 0.3246 0.1629 0.0204  0.1058  -0.0314 101 VAL C C   
9179  O O   . VAL C  101 ? 0.2622 0.3256 0.1547 0.0226  0.1050  -0.0354 101 VAL C O   
9180  C CB  . VAL C  101 ? 0.2517 0.3073 0.1511 0.0118  0.1076  -0.0212 101 VAL C CB  
9181  C CG1 . VAL C  101 ? 0.2513 0.3145 0.1576 0.0095  0.1119  -0.0171 101 VAL C CG1 
9182  C CG2 . VAL C  101 ? 0.2487 0.2944 0.1477 0.0082  0.1061  -0.0171 101 VAL C CG2 
9183  N N   . TRP C  102 ? 0.2489 0.3171 0.1582 0.0220  0.1072  -0.0313 102 TRP C N   
9184  C CA  . TRP C  102 ? 0.2570 0.3328 0.1656 0.0276  0.1089  -0.0342 102 TRP C CA  
9185  C C   . TRP C  102 ? 0.2599 0.3447 0.1722 0.0254  0.1143  -0.0286 102 TRP C C   
9186  O O   . TRP C  102 ? 0.2534 0.3387 0.1727 0.0203  0.1165  -0.0239 102 TRP C O   
9187  C CB  . TRP C  102 ? 0.2857 0.3593 0.1990 0.0323  0.1083  -0.0370 102 TRP C CB  
9188  C CG  . TRP C  102 ? 0.3168 0.3817 0.2255 0.0349  0.1032  -0.0433 102 TRP C CG  
9189  C CD1 . TRP C  102 ? 0.3189 0.3823 0.2215 0.0408  0.1007  -0.0501 102 TRP C CD1 
9190  C CD2 . TRP C  102 ? 0.3420 0.3985 0.2520 0.0310  0.1001  -0.0440 102 TRP C CD2 
9191  N NE1 . TRP C  102 ? 0.3119 0.3670 0.2128 0.0395  0.0961  -0.0561 102 TRP C NE1 
9192  C CE2 . TRP C  102 ? 0.3462 0.3952 0.2501 0.0346  0.0961  -0.0512 102 TRP C CE2 
9193  C CE3 . TRP C  102 ? 0.3304 0.3837 0.2462 0.0244  0.1001  -0.0394 102 TRP C CE3 
9194  C CZ2 . TRP C  102 ? 0.3451 0.3833 0.2472 0.0322  0.0932  -0.0531 102 TRP C CZ2 
9195  C CZ3 . TRP C  102 ? 0.3131 0.3556 0.2286 0.0217  0.0964  -0.0410 102 TRP C CZ3 
9196  C CH2 . TRP C  102 ? 0.3066 0.3414 0.2151 0.0254  0.0933  -0.0473 102 TRP C CH2 
9197  N N   . THR C  103 ? 0.2708 0.3628 0.1780 0.0286  0.1166  -0.0296 103 THR C N   
9198  C CA  . THR C  103 ? 0.2766 0.3773 0.1863 0.0271  0.1227  -0.0245 103 THR C CA  
9199  C C   . THR C  103 ? 0.3158 0.4192 0.2216 0.0360  0.1261  -0.0262 103 THR C C   
9200  O O   . THR C  103 ? 0.2953 0.3925 0.1937 0.0426  0.1233  -0.0310 103 THR C O   
9201  C CB  . THR C  103 ? 0.3126 0.4157 0.2157 0.0209  0.1241  -0.0219 103 THR C CB  
9202  O OG1 . THR C  103 ? 0.3340 0.4398 0.2275 0.0214  0.1228  -0.0284 103 THR C OG1 
9203  C CG2 . THR C  103 ? 0.3287 0.4215 0.2309 0.0155  0.1220  -0.0190 103 THR C CG2 
9204  N N   . PRO C  104 ? 0.4030 0.5098 0.3122 0.0367  0.1342  -0.0213 104 PRO C N   
9205  C CA  . PRO C  104 ? 0.3922 0.4822 0.2939 0.0435  0.1446  -0.0222 104 PRO C CA  
9206  C C   . PRO C  104 ? 0.4290 0.4944 0.3125 0.0435  0.1513  -0.0240 104 PRO C C   
9207  O O   . PRO C  104 ? 0.3757 0.5086 0.2709 0.0333  0.1300  -0.0332 104 PRO C O   
9208  C CB  . PRO C  104 ? 0.3905 0.4943 0.3023 0.0398  0.1517  -0.0183 104 PRO C CB  
9209  C CG  . PRO C  104 ? 0.3016 0.4170 0.2254 0.0322  0.1469  -0.0158 104 PRO C CG  
9210  C CD  . PRO C  104 ? 0.2920 0.4063 0.2109 0.0290  0.1382  -0.0163 104 PRO C CD  
9211  N N   . TYR C  105 ? 0.6632 0.7178 0.5458 0.0277  0.1609  -0.0425 105 TYR C N   
9212  C CA  . TYR C  105 ? 0.6776 0.7397 0.5509 0.0199  0.1619  -0.0527 105 TYR C CA  
9213  C C   . TYR C  105 ? 0.7912 0.8582 0.6637 0.0232  0.1722  -0.0504 105 TYR C C   
9214  O O   . TYR C  105 ? 0.8651 0.9390 0.7446 0.0306  0.1757  -0.0514 105 TYR C O   
9215  C CB  . TYR C  105 ? 0.3987 0.4620 0.2659 0.0261  0.1566  -0.0612 105 TYR C CB  
9216  C CG  . TYR C  105 ? 0.4078 0.4730 0.2596 0.0269  0.1558  -0.0655 105 TYR C CG  
9217  C CD1 . TYR C  105 ? 0.4620 0.5313 0.3069 0.0310  0.1629  -0.0686 105 TYR C CD1 
9218  C CD2 . TYR C  105 ? 0.4222 0.4850 0.2652 0.0252  0.1482  -0.0658 105 TYR C CD2 
9219  C CE1 . TYR C  105 ? 0.4957 0.5644 0.3240 0.0329  0.1625  -0.0719 105 TYR C CE1 
9220  C CE2 . TYR C  105 ? 0.4442 0.5054 0.2702 0.0281  0.1479  -0.0683 105 TYR C CE2 
9221  C CZ  . TYR C  105 ? 0.4774 0.5411 0.2957 0.0316  0.1549  -0.0716 105 TYR C CZ  
9222  O OH  . TYR C  105 ? 0.4940 0.5554 0.2942 0.0343  0.1546  -0.0743 105 TYR C OH  
9223  N N   . PRO C  106 ? 0.7329 0.8024 0.5989 0.0156  0.1761  -0.0492 106 PRO C N   
9224  C CA  . PRO C  106 ? 0.7272 0.8118 0.5908 0.0035  0.1669  -0.0518 106 PRO C CA  
9225  C C   . PRO C  106 ? 0.7122 0.8475 0.5971 0.0016  0.1498  -0.0469 106 PRO C C   
9226  O O   . PRO C  106 ? 0.6885 0.8231 0.5744 0.0439  0.1510  -0.0145 106 PRO C O   
9227  C CB  . PRO C  106 ? 0.6874 0.7812 0.5416 0.0006  0.1728  -0.0507 106 PRO C CB  
9228  C CG  . PRO C  106 ? 0.7008 0.7803 0.5600 0.0035  0.1866  -0.0461 106 PRO C CG  
9229  C CD  . PRO C  106 ? 0.6977 0.7704 0.5626 0.0180  0.1872  -0.0453 106 PRO C CD  
9230  N N   . ARG C  107 ? 0.8480 0.9836 0.7266 0.0080  0.1433  -0.0371 107 ARG C N   
9231  C CA  . ARG C  107 ? 0.8487 0.9854 0.7324 0.0138  0.1411  -0.0226 107 ARG C CA  
9232  C C   . ARG C  107 ? 0.9384 1.0841 0.8257 0.0143  0.1483  -0.0133 107 ARG C C   
9233  O O   . ARG C  107 ? 1.0125 1.1667 0.8935 0.0113  0.1527  -0.0149 107 ARG C O   
9234  C CB  . ARG C  107 ? 0.5144 0.6363 0.3870 0.0082  0.1403  -0.0206 107 ARG C CB  
9235  C CG  . ARG C  107 ? 0.4569 0.5675 0.3312 0.0101  0.1340  -0.0221 107 ARG C CG  
9236  C CD  . ARG C  107 ? 0.4505 0.5486 0.3115 0.0097  0.1316  -0.0287 107 ARG C CD  
9237  N NE  . ARG C  107 ? 0.5087 0.5993 0.3530 0.0076  0.1350  -0.0257 107 ARG C NE  
9238  C CZ  . ARG C  107 ? 0.5275 0.6164 0.3671 0.0051  0.1376  -0.0167 107 ARG C CZ  
9239  N NH1 . ARG C  107 ? 0.5212 0.6129 0.3716 0.0032  0.1383  -0.0097 107 ARG C NH1 
9240  N NH2 . ARG C  107 ? 0.5305 0.6124 0.3525 0.0048  0.1401  -0.0144 107 ARG C NH2 
9241  N N   . PRO C  108 ? 0.7739 0.9158 0.6712 0.0145  0.1507  -0.0059 108 PRO C N   
9242  C CA  . PRO C  108 ? 0.7418 0.8900 0.6438 0.0118  0.1590  0.0010  108 PRO C CA  
9243  C C   . PRO C  108 ? 0.7018 0.8484 0.5957 0.0029  0.1624  0.0060  108 PRO C C   
9244  O O   . PRO C  108 ? 0.7477 0.8840 0.6335 -0.0008 0.1591  0.0057  108 PRO C O   
9245  C CB  . PRO C  108 ? 0.7951 0.9380 0.7100 0.0092  0.1597  0.0033  108 PRO C CB  
9246  C CG  . PRO C  108 ? 0.7869 0.9190 0.7005 0.0074  0.1520  0.0007  108 PRO C CG  
9247  C CD  . PRO C  108 ? 0.7902 0.9217 0.6947 0.0132  0.1465  -0.0056 108 PRO C CD  
9248  N N   . ALA C  109 ? 0.5114 0.6656 0.4064 0.0001  0.1703  0.0115  109 ALA C N   
9249  C CA  . ALA C  109 ? 0.4968 0.6455 0.3858 -0.0087 0.1749  0.0185  109 ALA C CA  
9250  C C   . ALA C  109 ? 0.5513 0.6998 0.4532 -0.0135 0.1796  0.0235  109 ALA C C   
9251  O O   . ALA C  109 ? 0.5761 0.7328 0.4890 -0.0104 0.1823  0.0221  109 ALA C O   
9252  C CB  . ALA C  109 ? 0.5734 0.7299 0.4519 -0.0102 0.1807  0.0207  109 ALA C CB  
9253  N N   . SER C  110 ? 0.7605 0.8982 0.6604 -0.0212 0.1813  0.0290  110 SER C N   
9254  C CA  . SER C  110 ? 0.7780 0.9081 0.6896 -0.0275 0.1822  0.0310  110 SER C CA  
9255  C C   . SER C  110 ? 0.7105 0.8340 0.6294 -0.0245 0.1742  0.0254  110 SER C C   
9256  O O   . SER C  110 ? 0.7063 0.8377 0.6279 -0.0172 0.1708  0.0201  110 SER C O   
9257  C CB  . SER C  110 ? 0.7400 0.8819 0.6630 -0.0303 0.1894  0.0325  110 SER C CB  
9258  O OG  . SER C  110 ? 0.7255 0.8785 0.6569 -0.0229 0.1881  0.0270  110 SER C OG  
9259  N N   . PRO C  111 ? 0.4991 0.6076 0.4214 -0.0302 0.1719  0.0267  111 PRO C N   
9260  C CA  . PRO C  111 ? 0.4863 0.5868 0.4115 -0.0272 0.1641  0.0221  111 PRO C CA  
9261  C C   . PRO C  111 ? 0.5161 0.6231 0.4540 -0.0259 0.1620  0.0171  111 PRO C C   
9262  O O   . PRO C  111 ? 0.5373 0.6473 0.4842 -0.0314 0.1660  0.0177  111 PRO C O   
9263  C CB  . PRO C  111 ? 0.4808 0.5630 0.4044 -0.0333 0.1636  0.0256  111 PRO C CB  
9264  C CG  . PRO C  111 ? 0.4850 0.5639 0.4002 -0.0374 0.1702  0.0322  111 PRO C CG  
9265  C CD  . PRO C  111 ? 0.4908 0.5866 0.4110 -0.0384 0.1761  0.0325  111 PRO C CD  
9266  N N   . THR C  112 ? 0.4767 0.5846 0.4144 -0.0193 0.1559  0.0122  112 THR C N   
9267  C CA  . THR C  112 ? 0.4528 0.5647 0.4005 -0.0170 0.1533  0.0073  112 THR C CA  
9268  C C   . THR C  112 ? 0.3831 0.4821 0.3347 -0.0210 0.1480  0.0058  112 THR C C   
9269  O O   . THR C  112 ? 0.3187 0.4071 0.2637 -0.0207 0.1444  0.0069  112 THR C O   
9270  C CB  . THR C  112 ? 0.6230 0.7417 0.5669 -0.0070 0.1506  0.0029  112 THR C CB  
9271  O OG1 . THR C  112 ? 0.6497 0.7806 0.5922 -0.0029 0.1569  0.0038  112 THR C OG1 
9272  C CG2 . THR C  112 ? 0.6387 0.7564 0.5905 -0.0045 0.1467  -0.0021 112 THR C CG2 
9273  N N   . PRO C  113 ? 0.5775 0.6774 0.5396 -0.0250 0.1479  0.0032  113 PRO C N   
9274  C CA  . PRO C  113 ? 0.5446 0.6330 0.5100 -0.0285 0.1431  0.0013  113 PRO C CA  
9275  C C   . PRO C  113 ? 0.5184 0.6046 0.4818 -0.0221 0.1365  -0.0024 113 PRO C C   
9276  O O   . PRO C  113 ? 0.5093 0.6040 0.4732 -0.0160 0.1357  -0.0055 113 PRO C O   
9277  C CB  . PRO C  113 ? 0.2617 0.3555 0.2382 -0.0343 0.1453  -0.0014 113 PRO C CB  
9278  C CG  . PRO C  113 ? 0.2637 0.3729 0.2438 -0.0298 0.1482  -0.0031 113 PRO C CG  
9279  C CD  . PRO C  113 ? 0.2791 0.3916 0.2507 -0.0263 0.1522  0.0013  113 PRO C CD  
9280  N N   . VAL C  114 ? 0.3841 0.4580 0.3451 -0.0235 0.1323  -0.0022 114 VAL C N   
9281  C CA  . VAL C  114 ? 0.3377 0.4074 0.2954 -0.0185 0.1265  -0.0048 114 VAL C CA  
9282  C C   . VAL C  114 ? 0.3435 0.4103 0.3077 -0.0200 0.1227  -0.0086 114 VAL C C   
9283  O O   . VAL C  114 ? 0.3524 0.4143 0.3215 -0.0259 0.1233  -0.0086 114 VAL C O   
9284  C CB  . VAL C  114 ? 0.2391 0.2977 0.1897 -0.0188 0.1248  -0.0018 114 VAL C CB  
9285  C CG1 . VAL C  114 ? 0.2318 0.2868 0.1790 -0.0141 0.1194  -0.0045 114 VAL C CG1 
9286  C CG2 . VAL C  114 ? 0.2505 0.3116 0.1935 -0.0179 0.1288  0.0020  114 VAL C CG2 
9287  N N   . LEU C  115 ? 0.2934 0.3629 0.2568 -0.0146 0.1192  -0.0122 115 LEU C N   
9288  C CA  . LEU C  115 ? 0.2736 0.3400 0.2412 -0.0151 0.1153  -0.0158 115 LEU C CA  
9289  C C   . LEU C  115 ? 0.2911 0.3482 0.2532 -0.0126 0.1105  -0.0162 115 LEU C C   
9290  O O   . LEU C  115 ? 0.3062 0.3646 0.2627 -0.0071 0.1091  -0.0177 115 LEU C O   
9291  C CB  . LEU C  115 ? 0.2134 0.2899 0.1842 -0.0108 0.1157  -0.0198 115 LEU C CB  
9292  C CG  . LEU C  115 ? 0.3945 0.4794 0.3744 -0.0153 0.1189  -0.0212 115 LEU C CG  
9293  C CD1 . LEU C  115 ? 0.2143 0.3092 0.1980 -0.0104 0.1192  -0.0257 115 LEU C CD1 
9294  C CD2 . LEU C  115 ? 0.2093 0.2867 0.1926 -0.0217 0.1165  -0.0220 115 LEU C CD2 
9295  N N   . ILE C  116 ? 0.2047 0.2525 0.1681 -0.0165 0.1084  -0.0154 116 ILE C N   
9296  C CA  . ILE C  116 ? 0.2001 0.2400 0.1599 -0.0148 0.1043  -0.0160 116 ILE C CA  
9297  C C   . ILE C  116 ? 0.4353 0.4739 0.3980 -0.0150 0.1012  -0.0196 116 ILE C C   
9298  O O   . ILE C  116 ? 0.1914 0.2292 0.1591 -0.0191 0.1013  -0.0204 116 ILE C O   
9299  C CB  . ILE C  116 ? 0.2004 0.2309 0.1592 -0.0180 0.1043  -0.0126 116 ILE C CB  
9300  C CG1 . ILE C  116 ? 0.2083 0.2394 0.1629 -0.0177 0.1077  -0.0088 116 ILE C CG1 
9301  C CG2 . ILE C  116 ? 0.1967 0.2205 0.1522 -0.0163 0.1009  -0.0129 116 ILE C CG2 
9302  C CD1 . ILE C  116 ? 0.2107 0.2322 0.1634 -0.0196 0.1084  -0.0053 116 ILE C CD1 
9303  N N   . TRP C  117 ? 0.1932 0.2309 0.1517 -0.0107 0.0988  -0.0221 117 TRP C N   
9304  C CA  . TRP C  117 ? 0.2016 0.2369 0.1609 -0.0105 0.0962  -0.0254 117 TRP C CA  
9305  C C   . TRP C  117 ? 0.2248 0.2499 0.1818 -0.0125 0.0935  -0.0246 117 TRP C C   
9306  O O   . TRP C  117 ? 0.2367 0.2574 0.1886 -0.0108 0.0927  -0.0240 117 TRP C O   
9307  C CB  . TRP C  117 ? 0.1930 0.2323 0.1485 -0.0044 0.0958  -0.0294 117 TRP C CB  
9308  C CG  . TRP C  117 ? 0.1916 0.2268 0.1460 -0.0037 0.0933  -0.0329 117 TRP C CG  
9309  C CD1 . TRP C  117 ? 0.1934 0.2195 0.1415 -0.0025 0.0911  -0.0346 117 TRP C CD1 
9310  C CD2 . TRP C  117 ? 0.1900 0.2295 0.1487 -0.0045 0.0934  -0.0353 117 TRP C CD2 
9311  N NE1 . TRP C  117 ? 0.1935 0.2172 0.1412 -0.0023 0.0898  -0.0375 117 TRP C NE1 
9312  C CE2 . TRP C  117 ? 0.1911 0.2236 0.1453 -0.0031 0.0911  -0.0381 117 TRP C CE2 
9313  C CE3 . TRP C  117 ? 0.1888 0.2375 0.1546 -0.0066 0.0954  -0.0357 117 TRP C CE3 
9314  C CZ2 . TRP C  117 ? 0.1912 0.2261 0.1469 -0.0031 0.0907  -0.0410 117 TRP C CZ2 
9315  C CZ3 . TRP C  117 ? 0.1920 0.2441 0.1603 -0.0070 0.0948  -0.0389 117 TRP C CZ3 
9316  C CH2 . TRP C  117 ? 0.1893 0.2348 0.1523 -0.0049 0.0925  -0.0414 117 TRP C CH2 
9317  N N   . ILE C  118 ? 0.2354 0.2572 0.1958 -0.0162 0.0925  -0.0250 118 ILE C N   
9318  C CA  . ILE C  118 ? 0.2490 0.2622 0.2076 -0.0180 0.0905  -0.0244 118 ILE C CA  
9319  C C   . ILE C  118 ? 0.2402 0.2520 0.1970 -0.0175 0.0891  -0.0278 118 ILE C C   
9320  O O   . ILE C  118 ? 0.1789 0.1937 0.1389 -0.0194 0.0892  -0.0292 118 ILE C O   
9321  C CB  . ILE C  118 ? 0.2382 0.2472 0.2006 -0.0224 0.0908  -0.0221 118 ILE C CB  
9322  C CG1 . ILE C  118 ? 0.2532 0.2633 0.2172 -0.0231 0.0931  -0.0193 118 ILE C CG1 
9323  C CG2 . ILE C  118 ? 0.2658 0.2671 0.2265 -0.0235 0.0893  -0.0208 118 ILE C CG2 
9324  C CD1 . ILE C  118 ? 0.2707 0.2745 0.2369 -0.0265 0.0938  -0.0177 118 ILE C CD1 
9325  N N   . TYR C  119 ? 0.1831 0.1899 0.1341 -0.0154 0.0880  -0.0293 119 TYR C N   
9326  C CA  . TYR C  119 ? 0.1861 0.1894 0.1333 -0.0145 0.0871  -0.0326 119 TYR C CA  
9327  C C   . TYR C  119 ? 0.1840 0.1820 0.1319 -0.0190 0.0866  -0.0316 119 TYR C C   
9328  O O   . TYR C  119 ? 0.1804 0.1757 0.1312 -0.0225 0.0865  -0.0286 119 TYR C O   
9329  C CB  . TYR C  119 ? 0.2760 0.2720 0.2148 -0.0115 0.0865  -0.0351 119 TYR C CB  
9330  C CG  . TYR C  119 ? 0.2934 0.2818 0.2294 -0.0146 0.0862  -0.0330 119 TYR C CG  
9331  C CD1 . TYR C  119 ? 0.2980 0.2784 0.2320 -0.0188 0.0861  -0.0322 119 TYR C CD1 
9332  C CD2 . TYR C  119 ? 0.3258 0.3157 0.2604 -0.0133 0.0866  -0.0318 119 TYR C CD2 
9333  C CE1 . TYR C  119 ? 0.3066 0.2821 0.2390 -0.0219 0.0863  -0.0304 119 TYR C CE1 
9334  C CE2 . TYR C  119 ? 0.3564 0.3410 0.2885 -0.0158 0.0866  -0.0303 119 TYR C CE2 
9335  C CZ  . TYR C  119 ? 0.3360 0.3140 0.2675 -0.0202 0.0866  -0.0297 119 TYR C CZ  
9336  O OH  . TYR C  119 ? 0.3228 0.2979 0.2527 -0.0229 0.0871  -0.0283 119 TYR C OH  
9337  N N   . GLY C  120 ? 0.1878 0.1842 0.1320 -0.0182 0.0864  -0.0345 120 GLY C N   
9338  C CA  . GLY C  120 ? 0.1886 0.1792 0.1307 -0.0221 0.0861  -0.0338 120 GLY C CA  
9339  C C   . GLY C  120 ? 0.1955 0.1742 0.1288 -0.0228 0.0861  -0.0341 120 GLY C C   
9340  O O   . GLY C  120 ? 0.1975 0.1720 0.1282 -0.0221 0.0861  -0.0339 120 GLY C O   
9341  N N   . GLY C  121 ? 0.3212 0.2936 0.2480 -0.0243 0.0863  -0.0347 121 GLY C N   
9342  C CA  . GLY C  121 ? 0.3389 0.2978 0.2563 -0.0269 0.0869  -0.0340 121 GLY C CA  
9343  C C   . GLY C  121 ? 0.3232 0.2794 0.2423 -0.0331 0.0875  -0.0301 121 GLY C C   
9344  O O   . GLY C  121 ? 0.3493 0.2971 0.2640 -0.0367 0.0883  -0.0285 121 GLY C O   
9345  N N   . GLY C  122 ? 0.2592 0.2228 0.1849 -0.0345 0.0870  -0.0291 122 GLY C N   
9346  C CA  . GLY C  122 ? 0.2011 0.1623 0.1273 -0.0391 0.0872  -0.0265 122 GLY C CA  
9347  C C   . GLY C  122 ? 0.2975 0.2589 0.2305 -0.0413 0.0870  -0.0239 122 GLY C C   
9348  O O   . GLY C  122 ? 0.1970 0.1557 0.1297 -0.0445 0.0872  -0.0220 122 GLY C O   
9349  N N   . PHE C  123 ? 0.2216 0.1869 0.1602 -0.0392 0.0866  -0.0239 123 PHE C N   
9350  C CA  . PHE C  123 ? 0.3257 0.2917 0.2694 -0.0401 0.0865  -0.0216 123 PHE C CA  
9351  C C   . PHE C  123 ? 0.3397 0.2996 0.2789 -0.0432 0.0875  -0.0207 123 PHE C C   
9352  O O   . PHE C  123 ? 0.3275 0.2896 0.2710 -0.0441 0.0877  -0.0190 123 PHE C O   
9353  C CB  . PHE C  123 ? 0.2818 0.2505 0.2311 -0.0409 0.0864  -0.0202 123 PHE C CB  
9354  C CG  . PHE C  123 ? 0.1785 0.1518 0.1320 -0.0390 0.0861  -0.0211 123 PHE C CG  
9355  C CD1 . PHE C  123 ? 0.3347 0.3112 0.2918 -0.0365 0.0861  -0.0205 123 PHE C CD1 
9356  C CD2 . PHE C  123 ? 0.3712 0.3451 0.3242 -0.0404 0.0862  -0.0225 123 PHE C CD2 
9357  C CE1 . PHE C  123 ? 0.1737 0.1530 0.1339 -0.0358 0.0865  -0.0211 123 PHE C CE1 
9358  C CE2 . PHE C  123 ? 0.3668 0.3440 0.3232 -0.0400 0.0866  -0.0237 123 PHE C CE2 
9359  C CZ  . PHE C  123 ? 0.1750 0.1544 0.1350 -0.0379 0.0868  -0.0229 123 PHE C CZ  
9360  N N   . TYR C  124 ? 0.3424 0.2944 0.2722 -0.0452 0.0883  -0.0216 124 TYR C N   
9361  C CA  . TYR C  124 ? 0.3625 0.3061 0.2856 -0.0495 0.0896  -0.0208 124 TYR C CA  
9362  C C   . TYR C  124 ? 0.4003 0.3385 0.3175 -0.0469 0.0875  -0.0234 124 TYR C C   
9363  O O   . TYR C  124 ? 0.4466 0.3768 0.3605 -0.0493 0.0837  -0.0228 124 TYR C O   
9364  C CB  . TYR C  124 ? 0.3137 0.2483 0.2287 -0.0539 0.0903  -0.0189 124 TYR C CB  
9365  C CG  . TYR C  124 ? 0.3068 0.2344 0.2133 -0.0498 0.0867  -0.0203 124 TYR C CG  
9366  C CD1 . TYR C  124 ? 0.3478 0.2804 0.2536 -0.0473 0.0881  -0.0214 124 TYR C CD1 
9367  C CD2 . TYR C  124 ? 0.3029 0.2191 0.2029 -0.0477 0.0810  -0.0207 124 TYR C CD2 
9368  C CE1 . TYR C  124 ? 0.4144 0.3430 0.3141 -0.0424 0.0836  -0.0226 124 TYR C CE1 
9369  C CE2 . TYR C  124 ? 0.3738 0.2838 0.2669 -0.0422 0.0768  -0.0218 124 TYR C CE2 
9370  C CZ  . TYR C  124 ? 0.4563 0.3736 0.3497 -0.0392 0.0780  -0.0226 124 TYR C CZ  
9371  O OH  . TYR C  124 ? 0.5213 0.4348 0.4089 -0.0328 0.0735  -0.0236 124 TYR C OH  
9372  N N   . SER C  125 ? 0.2131 0.1556 0.1303 -0.0413 0.0874  -0.0264 125 SER C N   
9373  C CA  . SER C  125 ? 0.2605 0.1980 0.1731 -0.0366 0.0826  -0.0293 125 SER C CA  
9374  C C   . SER C  125 ? 0.2687 0.2142 0.1828 -0.0307 0.0842  -0.0324 125 SER C C   
9375  O O   . SER C  125 ? 0.2853 0.2406 0.2061 -0.0304 0.0874  -0.0314 125 SER C O   
9376  C CB  . SER C  125 ? 0.2312 0.1576 0.1362 -0.0344 0.0779  -0.0300 125 SER C CB  
9377  O OG  . SER C  125 ? 0.2287 0.1604 0.1339 -0.0299 0.0789  -0.0314 125 SER C OG  
9378  N N   . GLY C  126 ? 0.2228 0.1641 0.1319 -0.0256 0.0805  -0.0356 126 GLY C N   
9379  C CA  . GLY C  126 ? 0.2204 0.1697 0.1303 -0.0197 0.0824  -0.0387 126 GLY C CA  
9380  C C   . GLY C  126 ? 0.2206 0.1729 0.1296 -0.0183 0.0830  -0.0398 126 GLY C C   
9381  O O   . GLY C  126 ? 0.3694 0.3202 0.2791 -0.0223 0.0824  -0.0379 126 GLY C O   
9382  N N   . ALA C  127 ? 0.2222 0.1796 0.1296 -0.0125 0.0841  -0.0430 127 ALA C N   
9383  C CA  . ALA C  127 ? 0.2511 0.2125 0.1572 -0.0105 0.0839  -0.0434 127 ALA C CA  
9384  C C   . ALA C  127 ? 0.2198 0.1930 0.1307 -0.0048 0.0842  -0.0436 127 ALA C C   
9385  O O   . ALA C  127 ? 0.2403 0.2166 0.1528 -0.0011 0.0841  -0.0456 127 ALA C O   
9386  C CB  . ALA C  127 ? 0.2360 0.1863 0.1327 -0.0089 0.0790  -0.0472 127 ALA C CB  
9387  N N   . ALA C  128 ? 0.2593 0.2393 0.1716 -0.0038 0.0849  -0.0416 128 ALA C N   
9388  C CA  . ALA C  128 ? 0.2573 0.2484 0.1732 0.0008  0.0859  -0.0413 128 ALA C CA  
9389  C C   . ALA C  128 ? 0.2821 0.2709 0.1896 0.0073  0.0847  -0.0473 128 ALA C C   
9390  O O   . ALA C  128 ? 0.2911 0.2890 0.2010 0.0122  0.0856  -0.0486 128 ALA C O   
9391  C CB  . ALA C  128 ? 0.2129 0.2104 0.1312 -0.0003 0.0873  -0.0369 128 ALA C CB  
9392  N N   . SER C  129 ? 0.2375 0.2132 0.1348 0.0073  0.0825  -0.0513 129 SER C N   
9393  C CA  . SER C  129 ? 0.2656 0.2360 0.1532 0.0137  0.0804  -0.0576 129 SER C CA  
9394  C C   . SER C  129 ? 0.2581 0.2219 0.1433 0.0188  0.0788  -0.0623 129 SER C C   
9395  O O   . SER C  129 ? 0.2713 0.2279 0.1481 0.0247  0.0765  -0.0678 129 SER C O   
9396  C CB  . SER C  129 ? 0.2620 0.2201 0.1381 0.0115  0.0779  -0.0604 129 SER C CB  
9397  O OG  . SER C  129 ? 0.2622 0.2094 0.1379 0.0054  0.0753  -0.0593 129 SER C OG  
9398  N N   . LEU C  130 ? 0.3374 0.3028 0.2290 0.0171  0.0798  -0.0602 130 LEU C N   
9399  C CA  . LEU C  130 ? 0.3862 0.3456 0.2748 0.0231  0.0785  -0.0642 130 LEU C CA  
9400  C C   . LEU C  130 ? 0.4718 0.4452 0.3647 0.0314  0.0797  -0.0674 130 LEU C C   
9401  O O   . LEU C  130 ? 0.4999 0.4892 0.3996 0.0309  0.0821  -0.0652 130 LEU C O   
9402  C CB  . LEU C  130 ? 0.2990 0.2591 0.1934 0.0193  0.0791  -0.0609 130 LEU C CB  
9403  C CG  . LEU C  130 ? 0.3019 0.2529 0.1963 0.0107  0.0769  -0.0563 130 LEU C CG  
9404  C CD1 . LEU C  130 ? 0.3003 0.2522 0.1994 0.0083  0.0764  -0.0534 130 LEU C CD1 
9405  C CD2 . LEU C  130 ? 0.3413 0.2748 0.2266 0.0102  0.0711  -0.0577 130 LEU C CD2 
9406  N N   . ASP C  131 ? 0.4160 0.3827 0.3042 0.0394  0.0778  -0.0722 131 ASP C N   
9407  C CA  . ASP C  131 ? 0.4326 0.4119 0.3248 0.0472  0.0790  -0.0767 131 ASP C CA  
9408  C C   . ASP C  131 ? 0.3425 0.3421 0.2479 0.0474  0.0829  -0.0757 131 ASP C C   
9409  O O   . ASP C  131 ? 0.3233 0.3335 0.2346 0.0496  0.0870  -0.0778 131 ASP C O   
9410  C CB  . ASP C  131 ? 0.6979 0.6617 0.5807 0.0567  0.0747  -0.0819 131 ASP C CB  
9411  C CG  . ASP C  131 ? 0.7902 0.7353 0.6604 0.0560  0.0707  -0.0845 131 ASP C CG  
9412  O OD1 . ASP C  131 ? 0.8343 0.7810 0.7030 0.0492  0.0717  -0.0827 131 ASP C OD1 
9413  O OD2 . ASP C  131 ? 0.7984 0.7270 0.6599 0.0624  0.0662  -0.0883 131 ASP C OD2 
9414  N N   . VAL C  132 ? 0.4048 0.4051 0.3136 0.0435  0.0832  -0.0717 132 VAL C N   
9415  C CA  . VAL C  132 ? 0.4108 0.4287 0.3300 0.0446  0.0860  -0.0704 132 VAL C CA  
9416  C C   . VAL C  132 ? 0.4174 0.4457 0.3440 0.0373  0.0889  -0.0632 132 VAL C C   
9417  O O   . VAL C  132 ? 0.4808 0.5211 0.4163 0.0358  0.0920  -0.0607 132 VAL C O   
9418  C CB  . VAL C  132 ? 0.3793 0.3909 0.2989 0.0425  0.0842  -0.0696 132 VAL C CB  
9419  C CG1 . VAL C  132 ? 0.3603 0.3664 0.2804 0.0311  0.0852  -0.0644 132 VAL C CG1 
9420  C CG2 . VAL C  132 ? 0.3494 0.3797 0.2796 0.0460  0.0851  -0.0710 132 VAL C CG2 
9421  N N   . TYR C  133 ? 0.2895 0.3121 0.2130 0.0318  0.0879  -0.0604 133 TYR C N   
9422  C CA  . TYR C  133 ? 0.2573 0.2876 0.1865 0.0260  0.0901  -0.0542 133 TYR C CA  
9423  C C   . TYR C  133 ? 0.2842 0.3201 0.2103 0.0301  0.0919  -0.0540 133 TYR C C   
9424  O O   . TYR C  133 ? 0.2249 0.2639 0.1530 0.0256  0.0932  -0.0493 133 TYR C O   
9425  C CB  . TYR C  133 ? 0.3052 0.3261 0.2333 0.0180  0.0886  -0.0504 133 TYR C CB  
9426  C CG  . TYR C  133 ? 0.3136 0.3275 0.2431 0.0132  0.0874  -0.0497 133 TYR C CG  
9427  C CD1 . TYR C  133 ? 0.3249 0.3457 0.2604 0.0130  0.0882  -0.0502 133 TYR C CD1 
9428  C CD2 . TYR C  133 ? 0.2705 0.2712 0.1948 0.0088  0.0859  -0.0486 133 TYR C CD2 
9429  C CE1 . TYR C  133 ? 0.3109 0.3253 0.2461 0.0087  0.0872  -0.0496 133 TYR C CE1 
9430  C CE2 . TYR C  133 ? 0.2541 0.2483 0.1785 0.0044  0.0854  -0.0475 133 TYR C CE2 
9431  C CZ  . TYR C  133 ? 0.2690 0.2697 0.1983 0.0045  0.0860  -0.0480 133 TYR C CZ  
9432  O OH  . TYR C  133 ? 0.2100 0.2041 0.1378 0.0002  0.0856  -0.0470 133 TYR C OH  
9433  N N   . ASP C  134 ? 0.2859 0.3210 0.2058 0.0389  0.0918  -0.0592 134 ASP C N   
9434  C CA  . ASP C  134 ? 0.3039 0.3418 0.2198 0.0426  0.0932  -0.0589 134 ASP C CA  
9435  C C   . ASP C  134 ? 0.2745 0.3220 0.1966 0.0412  0.0994  -0.0531 134 ASP C C   
9436  O O   . ASP C  134 ? 0.2605 0.3120 0.1893 0.0418  0.1041  -0.0531 134 ASP C O   
9437  C CB  . ASP C  134 ? 0.4371 0.4555 0.3474 0.0431  0.0992  -0.0658 134 ASP C CB  
9438  C CG  . ASP C  134 ? 0.5337 0.5562 0.4421 0.0399  0.1006  -0.0726 134 ASP C CG  
9439  O OD1 . ASP C  134 ? 0.5380 0.5585 0.4430 0.0382  0.1048  -0.0657 134 ASP C OD1 
9440  O OD2 . ASP C  134 ? 0.5943 0.6128 0.4961 0.0463  0.0977  -0.0799 134 ASP C OD2 
9441  N N   . GLY C  135 ? 0.2940 0.3462 0.2147 0.0383  0.0999  -0.0497 135 GLY C N   
9442  C CA  . GLY C  135 ? 0.3026 0.3644 0.2293 0.0358  0.1051  -0.0443 135 GLY C CA  
9443  C C   . GLY C  135 ? 0.3687 0.4307 0.2933 0.0408  0.1112  -0.0448 135 GLY C C   
9444  O O   . GLY C  135 ? 0.3894 0.4608 0.3210 0.0386  0.1164  -0.0417 135 GLY C O   
9445  N N   . ARG C  136 ? 0.3462 0.3939 0.2615 0.0445  0.1129  -0.0500 136 ARG C N   
9446  C CA  . ARG C  136 ? 0.2840 0.3308 0.1983 0.0434  0.1209  -0.0546 136 ARG C CA  
9447  C C   . ARG C  136 ? 0.2832 0.3455 0.2092 0.0448  0.1262  -0.0553 136 ARG C C   
9448  O O   . ARG C  136 ? 0.3262 0.3952 0.2532 0.0446  0.1320  -0.0540 136 ARG C O   
9449  C CB  . ARG C  136 ? 0.2943 0.3352 0.2025 0.0433  0.1198  -0.0661 136 ARG C CB  
9450  C CG  . ARG C  136 ? 0.3362 0.3829 0.2491 0.0503  0.1192  -0.0735 136 ARG C CG  
9451  C CD  . ARG C  136 ? 0.3876 0.4242 0.2936 0.0533  0.1125  -0.0802 136 ARG C CD  
9452  N NE  . ARG C  136 ? 0.4672 0.4989 0.3629 0.0572  0.1109  -0.0859 136 ARG C NE  
9453  C CZ  . ARG C  136 ? 0.5174 0.5387 0.4029 0.0554  0.1058  -0.0882 136 ARG C CZ  
9454  N NH1 . ARG C  136 ? 0.5006 0.5177 0.3864 0.0494  0.1017  -0.0855 136 ARG C NH1 
9455  N NH2 . ARG C  136 ? 0.5494 0.5656 0.4246 0.0599  0.1045  -0.0932 136 ARG C NH2 
9456  N N   . PHE C  137 ? 0.3365 0.4055 0.2713 0.0460  0.1244  -0.0575 137 PHE C N   
9457  C CA  . PHE C  137 ? 0.3775 0.4640 0.3247 0.0473  0.1289  -0.0589 137 PHE C CA  
9458  C C   . PHE C  137 ? 0.4546 0.5518 0.4094 0.0420  0.1319  -0.0513 137 PHE C C   
9459  O O   . PHE C  137 ? 0.4650 0.5746 0.4267 0.0413  0.1374  -0.0508 137 PHE C O   
9460  C CB  . PHE C  137 ? 0.3157 0.4092 0.2715 0.0503  0.1241  -0.0641 137 PHE C CB  
9461  C CG  . PHE C  137 ? 0.3261 0.4093 0.2745 0.0561  0.1193  -0.0708 137 PHE C CG  
9462  C CD1 . PHE C  137 ? 0.3328 0.4212 0.2814 0.0640  0.1196  -0.0771 137 PHE C CD1 
9463  C CD2 . PHE C  137 ? 0.3231 0.3912 0.2637 0.0543  0.1141  -0.0707 137 PHE C CD2 
9464  C CE1 . PHE C  137 ? 0.3482 0.4259 0.2890 0.0707  0.1141  -0.0829 137 PHE C CE1 
9465  C CE2 . PHE C  137 ? 0.3271 0.3854 0.2606 0.0596  0.1090  -0.0770 137 PHE C CE2 
9466  C CZ  . PHE C  137 ? 0.3457 0.4080 0.2788 0.0684  0.1086  -0.0828 137 PHE C CZ  
9467  N N   . LEU C  138 ? 0.4489 0.5431 0.4034 0.0376  0.1276  -0.0460 138 LEU C N   
9468  C CA  . LEU C  138 ? 0.4128 0.5170 0.3750 0.0309  0.1291  -0.0402 138 LEU C CA  
9469  C C   . LEU C  138 ? 0.4121 0.5158 0.3676 0.0313  0.1331  -0.0355 138 LEU C C   
9470  O O   . LEU C  138 ? 0.4090 0.5229 0.3704 0.0278  0.1382  -0.0323 138 LEU C O   
9471  C CB  . LEU C  138 ? 0.2382 0.3385 0.2020 0.0248  0.1230  -0.0376 138 LEU C CB  
9472  C CG  . LEU C  138 ? 0.2306 0.3346 0.2033 0.0219  0.1200  -0.0410 138 LEU C CG  
9473  C CD1 . LEU C  138 ? 0.2209 0.3179 0.1932 0.0153  0.1154  -0.0383 138 LEU C CD1 
9474  C CD2 . LEU C  138 ? 0.2307 0.3506 0.2164 0.0180  0.1239  -0.0421 138 LEU C CD2 
9475  N N   . ALA C  139 ? 0.3793 0.4717 0.3227 0.0349  0.1299  -0.0357 139 ALA C N   
9476  C CA  . ALA C  139 ? 0.3487 0.4413 0.2850 0.0355  0.1322  -0.0318 139 ALA C CA  
9477  C C   . ALA C  139 ? 0.3385 0.4337 0.2753 0.0379  0.1409  -0.0340 139 ALA C C   
9478  O O   . ALA C  139 ? 0.3758 0.4796 0.3147 0.0358  0.1457  -0.0296 139 ALA C O   
9479  C CB  . ALA C  139 ? 0.3354 0.4177 0.2591 0.0389  0.1267  -0.0328 139 ALA C CB  
9480  N N   . GLN C  140 ? 0.2932 0.3838 0.2292 0.0410  0.1430  -0.0420 140 GLN C N   
9481  C CA  . GLN C  140 ? 0.3068 0.4034 0.2436 0.0427  0.1509  -0.0464 140 GLN C CA  
9482  C C   . GLN C  140 ? 0.3040 0.4201 0.2556 0.0416  0.1561  -0.0454 140 GLN C C   
9483  O O   . GLN C  140 ? 0.3123 0.4365 0.2657 0.0405  0.1629  -0.0430 140 GLN C O   
9484  C CB  . GLN C  140 ? 0.4118 0.5048 0.3448 0.0472  0.1502  -0.0569 140 GLN C CB  
9485  C CG  . GLN C  140 ? 0.4616 0.5627 0.3933 0.0503  0.1576  -0.0617 140 GLN C CG  
9486  C CD  . GLN C  140 ? 0.5204 0.6402 0.4661 0.0552  0.1600  -0.0661 140 GLN C CD  
9487  O OE1 . GLN C  140 ? 0.5482 0.6717 0.5006 0.0590  0.1538  -0.0702 140 GLN C OE1 
9488  N NE2 . GLN C  140 ? 0.5171 0.6498 0.4677 0.0552  0.1678  -0.0651 140 GLN C NE2 
9489  N N   . VAL C  141 ? 0.3471 0.4710 0.3093 0.0413  0.1528  -0.0477 141 VAL C N   
9490  C CA  . VAL C  141 ? 0.4637 0.6080 0.4420 0.0395  0.1554  -0.0491 141 VAL C CA  
9491  C C   . VAL C  141 ? 0.4913 0.6437 0.4767 0.0316  0.1573  -0.0421 141 VAL C C   
9492  O O   . VAL C  141 ? 0.5661 0.7320 0.5591 0.0291  0.1636  -0.0408 141 VAL C O   
9493  C CB  . VAL C  141 ? 0.3508 0.5027 0.3388 0.0415  0.1492  -0.0549 141 VAL C CB  
9494  C CG1 . VAL C  141 ? 0.3618 0.5378 0.3670 0.0400  0.1518  -0.0570 141 VAL C CG1 
9495  C CG2 . VAL C  141 ? 0.3308 0.4755 0.3121 0.0498  0.1461  -0.0621 141 VAL C CG2 
9496  N N   . GLU C  142 ? 0.2917 0.4368 0.2755 0.0272  0.1518  -0.0381 142 GLU C N   
9497  C CA  . GLU C  142 ? 0.3281 0.4805 0.3194 0.0183  0.1526  -0.0329 142 GLU C CA  
9498  C C   . GLU C  142 ? 0.3446 0.4901 0.3262 0.0166  0.1545  -0.0259 142 GLU C C   
9499  O O   . GLU C  142 ? 0.2709 0.4194 0.2565 0.0087  0.1550  -0.0215 142 GLU C O   
9500  C CB  . GLU C  142 ? 0.5085 0.6598 0.5061 0.0126  0.1460  -0.0340 142 GLU C CB  
9501  C CG  . GLU C  142 ? 0.5776 0.7434 0.5885 0.0118  0.1451  -0.0401 142 GLU C CG  
9502  C CD  . GLU C  142 ? 0.6358 0.8201 0.6586 0.0076  0.1514  -0.0404 142 GLU C CD  
9503  O OE1 . GLU C  142 ? 0.6565 0.8406 0.6788 0.0014  0.1555  -0.0350 142 GLU C OE1 
9504  O OE2 . GLU C  142 ? 0.6295 0.8297 0.6626 0.0105  0.1520  -0.0461 142 GLU C OE2 
9505  N N   . GLY C  143 ? 0.2810 0.4168 0.2493 0.0238  0.1551  -0.0256 143 GLY C N   
9506  C CA  . GLY C  143 ? 0.3163 0.4485 0.2750 0.0234  0.1557  -0.0200 143 GLY C CA  
9507  C C   . GLY C  143 ? 0.2877 0.4166 0.2446 0.0175  0.1501  -0.0157 143 GLY C C   
9508  O O   . GLY C  143 ? 0.2817 0.4139 0.2369 0.0129  0.1525  -0.0106 143 GLY C O   
9509  N N   . ALA C  144 ? 0.3518 0.4734 0.3087 0.0173  0.1434  -0.0181 144 ALA C N   
9510  C CA  . ALA C  144 ? 0.3645 0.4810 0.3222 0.0102  0.1388  -0.0154 144 ALA C CA  
9511  C C   . ALA C  144 ? 0.3337 0.4418 0.2808 0.0130  0.1333  -0.0157 144 ALA C C   
9512  O O   . ALA C  144 ? 0.3223 0.4265 0.2628 0.0198  0.1305  -0.0194 144 ALA C O   
9513  C CB  . ALA C  144 ? 0.2471 0.3615 0.2142 0.0057  0.1353  -0.0182 144 ALA C CB  
9514  N N   . VAL C  145 ? 0.3925 0.4951 0.3380 0.0066  0.1314  -0.0123 145 VAL C N   
9515  C CA  . VAL C  145 ? 0.3842 0.4781 0.3218 0.0072  0.1263  -0.0129 145 VAL C CA  
9516  C C   . VAL C  145 ? 0.3580 0.4428 0.3005 0.0045  0.1213  -0.0147 145 VAL C C   
9517  O O   . VAL C  145 ? 0.3416 0.4235 0.2912 -0.0015 0.1217  -0.0129 145 VAL C O   
9518  C CB  . VAL C  145 ? 0.2544 0.3443 0.1873 0.0020  0.1278  -0.0080 145 VAL C CB  
9519  C CG1 . VAL C  145 ? 0.2499 0.3284 0.1781 0.0011  0.1228  -0.0083 145 VAL C CG1 
9520  C CG2 . VAL C  145 ? 0.2662 0.3644 0.1911 0.0048  0.1317  -0.0069 145 VAL C CG2 
9521  N N   . LEU C  146 ? 0.3287 0.4085 0.2667 0.0088  0.1168  -0.0186 146 LEU C N   
9522  C CA  . LEU C  146 ? 0.3497 0.4220 0.2919 0.0069  0.1125  -0.0207 146 LEU C CA  
9523  C C   . LEU C  146 ? 0.3656 0.4280 0.3014 0.0069  0.1083  -0.0214 146 LEU C C   
9524  O O   . LEU C  146 ? 0.3720 0.4338 0.2998 0.0115  0.1070  -0.0243 146 LEU C O   
9525  C CB  . LEU C  146 ? 0.2260 0.3019 0.1702 0.0122  0.1120  -0.0255 146 LEU C CB  
9526  C CG  . LEU C  146 ? 0.2245 0.2940 0.1729 0.0098  0.1081  -0.0277 146 LEU C CG  
9527  C CD1 . LEU C  146 ? 0.2170 0.2937 0.1728 0.0106  0.1100  -0.0300 146 LEU C CD1 
9528  C CD2 . LEU C  146 ? 0.2252 0.2874 0.1662 0.0141  0.1041  -0.0318 146 LEU C CD2 
9529  N N   . VAL C  147 ? 0.3047 0.3590 0.2439 0.0016  0.1065  -0.0189 147 VAL C N   
9530  C CA  . VAL C  147 ? 0.2165 0.2613 0.1509 0.0009  0.1035  -0.0185 147 VAL C CA  
9531  C C   . VAL C  147 ? 0.2091 0.2475 0.1469 -0.0004 0.1000  -0.0209 147 VAL C C   
9532  O O   . VAL C  147 ? 0.2041 0.2434 0.1489 -0.0031 0.1000  -0.0210 147 VAL C O   
9533  C CB  . VAL C  147 ? 0.2172 0.2573 0.1519 -0.0034 0.1049  -0.0133 147 VAL C CB  
9534  C CG1 . VAL C  147 ? 0.2176 0.2499 0.1469 -0.0030 0.1026  -0.0126 147 VAL C CG1 
9535  C CG2 . VAL C  147 ? 0.2399 0.2859 0.1713 -0.0032 0.1090  -0.0104 147 VAL C CG2 
9536  N N   . SER C  148 ? 0.3047 0.3363 0.2369 0.0010  0.0973  -0.0230 148 SER C N   
9537  C CA  . SER C  148 ? 0.3522 0.3765 0.2869 -0.0013 0.0946  -0.0244 148 SER C CA  
9538  C C   . SER C  148 ? 0.3865 0.4027 0.3164 -0.0027 0.0931  -0.0234 148 SER C C   
9539  O O   . SER C  148 ? 0.4028 0.4175 0.3246 0.0000  0.0928  -0.0251 148 SER C O   
9540  C CB  . SER C  148 ? 0.2055 0.2301 0.1388 0.0020  0.0931  -0.0298 148 SER C CB  
9541  O OG  . SER C  148 ? 0.2139 0.2369 0.1382 0.0067  0.0925  -0.0336 148 SER C OG  
9542  N N   . MET C  149 ? 0.1995 0.2109 0.1341 -0.0067 0.0924  -0.0210 149 MET C N   
9543  C CA  . MET C  149 ? 0.2587 0.2641 0.1897 -0.0080 0.0917  -0.0199 149 MET C CA  
9544  C C   . MET C  149 ? 0.2616 0.2605 0.1927 -0.0103 0.0898  -0.0225 149 MET C C   
9545  O O   . MET C  149 ? 0.1942 0.1925 0.1299 -0.0118 0.0891  -0.0236 149 MET C O   
9546  C CB  . MET C  149 ? 0.1983 0.2032 0.1336 -0.0102 0.0930  -0.0148 149 MET C CB  
9547  C CG  . MET C  149 ? 0.1914 0.1929 0.1341 -0.0138 0.0922  -0.0139 149 MET C CG  
9548  S SD  . MET C  149 ? 0.1876 0.1924 0.1362 -0.0151 0.0923  -0.0154 149 MET C SD  
9549  C CE  . MET C  149 ? 0.1906 0.1975 0.1412 -0.0158 0.0953  -0.0115 149 MET C CE  
9550  N N   . ASN C  150 ? 0.2034 0.1976 0.1283 -0.0109 0.0894  -0.0237 150 ASN C N   
9551  C CA  . ASN C  150 ? 0.2313 0.2192 0.1563 -0.0146 0.0885  -0.0251 150 ASN C CA  
9552  C C   . ASN C  150 ? 0.2439 0.2327 0.1767 -0.0177 0.0893  -0.0205 150 ASN C C   
9553  O O   . ASN C  150 ? 0.2647 0.2567 0.1987 -0.0167 0.0905  -0.0170 150 ASN C O   
9554  C CB  . ASN C  150 ? 0.2119 0.1944 0.1266 -0.0152 0.0880  -0.0287 150 ASN C CB  
9555  C CG  . ASN C  150 ? 0.3213 0.2985 0.2274 -0.0126 0.0864  -0.0350 150 ASN C CG  
9556  O OD1 . ASN C  150 ? 0.2179 0.1958 0.1270 -0.0104 0.0860  -0.0362 150 ASN C OD1 
9557  N ND2 . ASN C  150 ? 0.2310 0.2026 0.1267 -0.0123 0.0840  -0.0391 150 ASN C ND2 
9558  N N   . TYR C  151 ? 0.1913 0.1774 0.1290 -0.0210 0.0887  -0.0205 151 TYR C N   
9559  C CA  . TYR C  151 ? 0.1868 0.1736 0.1309 -0.0232 0.0892  -0.0169 151 TYR C CA  
9560  C C   . TYR C  151 ? 0.2049 0.1876 0.1487 -0.0273 0.0890  -0.0181 151 TYR C C   
9561  O O   . TYR C  151 ? 0.2018 0.1798 0.1412 -0.0288 0.0885  -0.0213 151 TYR C O   
9562  C CB  . TYR C  151 ? 0.4702 0.4585 0.4208 -0.0231 0.0889  -0.0153 151 TYR C CB  
9563  C CG  . TYR C  151 ? 0.1793 0.1657 0.1308 -0.0247 0.0877  -0.0178 151 TYR C CG  
9564  C CD1 . TYR C  151 ? 0.1778 0.1608 0.1311 -0.0278 0.0872  -0.0179 151 TYR C CD1 
9565  C CD2 . TYR C  151 ? 0.1812 0.1702 0.1317 -0.0229 0.0875  -0.0199 151 TYR C CD2 
9566  C CE1 . TYR C  151 ? 0.1774 0.1588 0.1302 -0.0291 0.0865  -0.0200 151 TYR C CE1 
9567  C CE2 . TYR C  151 ? 0.1789 0.1674 0.1299 -0.0239 0.0868  -0.0221 151 TYR C CE2 
9568  C CZ  . TYR C  151 ? 0.1781 0.1623 0.1295 -0.0271 0.0863  -0.0221 151 TYR C CZ  
9569  O OH  . TYR C  151 ? 0.1787 0.1624 0.1293 -0.0280 0.0860  -0.0242 151 TYR C OH  
9570  N N   . ARG C  152 ? 0.1862 0.1708 0.1342 -0.0291 0.0899  -0.0154 152 ARG C N   
9571  C CA  . ARG C  152 ? 0.1877 0.1701 0.1361 -0.0341 0.0903  -0.0160 152 ARG C CA  
9572  C C   . ARG C  152 ? 0.3056 0.2842 0.2563 -0.0360 0.0893  -0.0165 152 ARG C C   
9573  O O   . ARG C  152 ? 0.1803 0.1605 0.1357 -0.0341 0.0887  -0.0151 152 ARG C O   
9574  C CB  . ARG C  152 ? 0.2156 0.2039 0.1704 -0.0348 0.0917  -0.0126 152 ARG C CB  
9575  C CG  . ARG C  152 ? 0.2246 0.2166 0.1760 -0.0367 0.0932  -0.0130 152 ARG C CG  
9576  C CD  . ARG C  152 ? 0.1897 0.1900 0.1490 -0.0363 0.0951  -0.0092 152 ARG C CD  
9577  N NE  . ARG C  152 ? 0.1875 0.1895 0.1490 -0.0300 0.0959  -0.0059 152 ARG C NE  
9578  C CZ  . ARG C  152 ? 0.1869 0.1946 0.1545 -0.0275 0.0981  -0.0022 152 ARG C CZ  
9579  N NH1 . ARG C  152 ? 0.1868 0.2015 0.1609 -0.0303 0.0998  -0.0011 152 ARG C NH1 
9580  N NH2 . ARG C  152 ? 0.1873 0.1939 0.1549 -0.0226 0.0992  0.0005  152 ARG C NH2 
9581  N N   . VAL C  153 ? 0.1899 0.1626 0.1354 -0.0400 0.0894  -0.0186 153 VAL C N   
9582  C CA  . VAL C  153 ? 0.1894 0.1581 0.1352 -0.0419 0.0888  -0.0187 153 VAL C CA  
9583  C C   . VAL C  153 ? 0.2235 0.1898 0.1696 -0.0476 0.0896  -0.0175 153 VAL C C   
9584  O O   . VAL C  153 ? 0.2232 0.1912 0.1699 -0.0510 0.0905  -0.0169 153 VAL C O   
9585  C CB  . VAL C  153 ? 0.1945 0.1569 0.1321 -0.0411 0.0887  -0.0219 153 VAL C CB  
9586  C CG1 . VAL C  153 ? 0.1911 0.1581 0.1298 -0.0356 0.0878  -0.0231 153 VAL C CG1 
9587  C CG2 . VAL C  153 ? 0.2050 0.1594 0.1327 -0.0439 0.0893  -0.0244 153 VAL C CG2 
9588  N N   . GLY C  154 ? 0.2384 0.2013 0.1839 -0.0494 0.0892  -0.0169 154 GLY C N   
9589  C CA  . GLY C  154 ? 0.2197 0.1807 0.1657 -0.0547 0.0896  -0.0151 154 GLY C CA  
9590  C C   . GLY C  154 ? 0.2112 0.1815 0.1671 -0.0540 0.0899  -0.0127 154 GLY C C   
9591  O O   . GLY C  154 ? 0.2106 0.1863 0.1714 -0.0491 0.0898  -0.0121 154 GLY C O   
9592  N N   . THR C  155 ? 0.1965 0.1685 0.1550 -0.0591 0.0905  -0.0110 155 THR C N   
9593  C CA  . THR C  155 ? 0.1926 0.1751 0.1609 -0.0585 0.0915  -0.0086 155 THR C CA  
9594  C C   . THR C  155 ? 0.2044 0.1938 0.1771 -0.0546 0.0921  -0.0083 155 THR C C   
9595  O O   . THR C  155 ? 0.2023 0.1982 0.1811 -0.0502 0.0931  -0.0066 155 THR C O   
9596  C CB  . THR C  155 ? 0.1981 0.1835 0.1698 -0.0657 0.0920  -0.0070 155 THR C CB  
9597  O OG1 . THR C  155 ? 0.2043 0.1848 0.1713 -0.0715 0.0912  -0.0086 155 THR C OG1 
9598  C CG2 . THR C  155 ? 0.2263 0.2063 0.1945 -0.0687 0.0919  -0.0060 155 THR C CG2 
9599  N N   . PHE C  156 ? 0.2416 0.2283 0.2093 -0.0562 0.0919  -0.0102 156 PHE C N   
9600  C CA  . PHE C  156 ? 0.1937 0.1868 0.1634 -0.0532 0.0929  -0.0099 156 PHE C CA  
9601  C C   . PHE C  156 ? 0.2744 0.2690 0.2457 -0.0454 0.0929  -0.0087 156 PHE C C   
9602  O O   . PHE C  156 ? 0.2746 0.2763 0.2507 -0.0422 0.0944  -0.0065 156 PHE C O   
9603  C CB  . PHE C  156 ? 0.1950 0.1832 0.1560 -0.0558 0.0921  -0.0130 156 PHE C CB  
9604  C CG  . PHE C  156 ? 0.2022 0.1868 0.1624 -0.0621 0.0868  -0.0140 156 PHE C CG  
9605  C CD1 . PHE C  156 ? 0.2033 0.1971 0.1719 -0.0663 0.0848  -0.0126 156 PHE C CD1 
9606  C CD2 . PHE C  156 ? 0.2090 0.1811 0.1607 -0.0641 0.0840  -0.0163 156 PHE C CD2 
9607  C CE1 . PHE C  156 ? 0.2113 0.2015 0.1796 -0.0735 0.0803  -0.0136 156 PHE C CE1 
9608  C CE2 . PHE C  156 ? 0.2181 0.1843 0.1682 -0.0705 0.0795  -0.0169 156 PHE C CE2 
9609  C CZ  . PHE C  156 ? 0.2193 0.1944 0.1778 -0.0759 0.0778  -0.0157 156 PHE C CZ  
9610  N N   . GLY C  157 ? 0.2542 0.2424 0.2214 -0.0429 0.0915  -0.0102 157 GLY C N   
9611  C CA  . GLY C  157 ? 0.1780 0.1672 0.1473 -0.0376 0.0913  -0.0091 157 GLY C CA  
9612  C C   . GLY C  157 ? 0.4317 0.4210 0.4051 -0.0368 0.0916  -0.0082 157 GLY C C   
9613  O O   . GLY C  157 ? 0.1747 0.1655 0.1509 -0.0335 0.0927  -0.0069 157 GLY C O   
9614  N N   . PHE C  158 ? 0.1770 0.1634 0.1491 -0.0400 0.0910  -0.0092 158 PHE C N   
9615  C CA  . PHE C  158 ? 0.1766 0.1620 0.1502 -0.0394 0.0914  -0.0093 158 PHE C CA  
9616  C C   . PHE C  158 ? 0.1848 0.1739 0.1624 -0.0410 0.0931  -0.0078 158 PHE C C   
9617  O O   . PHE C  158 ? 0.1792 0.1670 0.1568 -0.0404 0.0940  -0.0083 158 PHE C O   
9618  C CB  . PHE C  158 ? 0.1770 0.1566 0.1454 -0.0401 0.0899  -0.0118 158 PHE C CB  
9619  C CG  . PHE C  158 ? 0.1750 0.1536 0.1418 -0.0376 0.0890  -0.0129 158 PHE C CG  
9620  C CD1 . PHE C  158 ? 0.1757 0.1532 0.1389 -0.0378 0.0881  -0.0139 158 PHE C CD1 
9621  C CD2 . PHE C  158 ? 0.1761 0.1547 0.1448 -0.0354 0.0896  -0.0131 158 PHE C CD2 
9622  C CE1 . PHE C  158 ? 0.1744 0.1526 0.1367 -0.0353 0.0876  -0.0148 158 PHE C CE1 
9623  C CE2 . PHE C  158 ? 0.1728 0.1514 0.1407 -0.0338 0.0891  -0.0137 158 PHE C CE2 
9624  C CZ  . PHE C  158 ? 0.4154 0.3946 0.3803 -0.0334 0.0880  -0.0144 158 PHE C CZ  
9625  N N   . LEU C  159 ? 0.2168 0.2109 0.1976 -0.0437 0.0939  -0.0062 159 LEU C N   
9626  C CA  . LEU C  159 ? 0.1818 0.1810 0.1672 -0.0455 0.0958  -0.0045 159 LEU C CA  
9627  C C   . LEU C  159 ? 0.1805 0.1851 0.1714 -0.0411 0.0984  -0.0033 159 LEU C C   
9628  O O   . LEU C  159 ? 0.1788 0.1865 0.1724 -0.0381 0.0991  -0.0023 159 LEU C O   
9629  C CB  . LEU C  159 ? 0.1840 0.1891 0.1734 -0.0502 0.0963  -0.0030 159 LEU C CB  
9630  C CG  . LEU C  159 ? 0.1861 0.2000 0.1827 -0.0519 0.0989  -0.0007 159 LEU C CG  
9631  C CD1 . LEU C  159 ? 0.1912 0.2046 0.1873 -0.0592 0.0982  -0.0001 159 LEU C CD1 
9632  C CD2 . LEU C  159 ? 0.1839 0.2094 0.1898 -0.0492 0.1013  0.0013  159 LEU C CD2 
9633  N N   . ALA C  160 ? 0.2892 0.2942 0.2810 -0.0407 0.1003  -0.0034 160 ALA C N   
9634  C CA  . ALA C  160 ? 0.2916 0.2988 0.2870 -0.0364 0.1034  -0.0031 160 ALA C CA  
9635  C C   . ALA C  160 ? 0.2959 0.3095 0.2957 -0.0368 0.1069  -0.0021 160 ALA C C   
9636  O O   . ALA C  160 ? 0.3024 0.3141 0.2992 -0.0397 0.1069  -0.0029 160 ALA C O   
9637  C CB  . ALA C  160 ? 0.4941 0.4919 0.4840 -0.0347 0.1030  -0.0057 160 ALA C CB  
9638  N N   . LEU C  161 ? 0.4151 0.4369 0.4221 -0.0336 0.1103  -0.0005 161 LEU C N   
9639  C CA  . LEU C  161 ? 0.3639 0.3918 0.3754 -0.0322 0.1148  -0.0001 161 LEU C CA  
9640  C C   . LEU C  161 ? 0.3449 0.3680 0.3564 -0.0267 0.1183  -0.0013 161 LEU C C   
9641  O O   . LEU C  161 ? 0.3460 0.3758 0.3640 -0.0228 0.1213  0.0005  161 LEU C O   
9642  C CB  . LEU C  161 ? 0.2592 0.3025 0.2810 -0.0329 0.1169  0.0027  161 LEU C CB  
9643  C CG  . LEU C  161 ? 0.1921 0.2409 0.2156 -0.0392 0.1152  0.0042  161 LEU C CG  
9644  C CD1 . LEU C  161 ? 0.2824 0.3474 0.3171 -0.0392 0.1192  0.0064  161 LEU C CD1 
9645  C CD2 . LEU C  161 ? 0.3050 0.3451 0.3206 -0.0423 0.1143  0.0028  161 LEU C CD2 
9646  N N   . PRO C  162 ? 0.2264 0.2375 0.2307 -0.0266 0.1184  -0.0042 162 PRO C N   
9647  C CA  . PRO C  162 ? 0.2446 0.2466 0.2469 -0.0228 0.1213  -0.0055 162 PRO C CA  
9648  C C   . PRO C  162 ? 0.2990 0.3059 0.3079 -0.0175 0.1274  -0.0042 162 PRO C C   
9649  O O   . PRO C  162 ? 0.3162 0.3311 0.3296 -0.0168 0.1307  -0.0041 162 PRO C O   
9650  C CB  . PRO C  162 ? 0.2086 0.2014 0.2043 -0.0250 0.1221  -0.0091 162 PRO C CB  
9651  C CG  . PRO C  162 ? 0.4783 0.4720 0.4703 -0.0296 0.1173  -0.0095 162 PRO C CG  
9652  C CD  . PRO C  162 ? 0.1999 0.2052 0.1975 -0.0307 0.1161  -0.0063 162 PRO C CD  
9653  N N   . GLY C  163 ? 0.3664 0.3689 0.3762 -0.0133 0.1294  -0.0028 163 GLY C N   
9654  C CA  . GLY C  163 ? 0.4115 0.4160 0.4270 -0.0068 0.1359  -0.0013 163 GLY C CA  
9655  C C   . GLY C  163 ? 0.4554 0.4768 0.4809 -0.0040 0.1366  0.0020  163 GLY C C   
9656  O O   . GLY C  163 ? 0.5275 0.5529 0.5594 0.0027  0.1418  0.0040  163 GLY C O   
9657  N N   . SER C  164 ? 0.3920 0.4234 0.4194 -0.0091 0.1317  0.0028  164 SER C N   
9658  C CA  . SER C  164 ? 0.3902 0.4378 0.4272 -0.0079 0.1318  0.0057  164 SER C CA  
9659  C C   . SER C  164 ? 0.3824 0.4267 0.4180 -0.0047 0.1311  0.0081  164 SER C C   
9660  O O   . SER C  164 ? 0.3313 0.3622 0.3577 -0.0059 0.1285  0.0073  164 SER C O   
9661  C CB  . SER C  164 ? 0.4945 0.5509 0.5328 -0.0153 0.1272  0.0059  164 SER C CB  
9662  O OG  . SER C  164 ? 0.4759 0.5214 0.5050 -0.0192 0.1219  0.0050  164 SER C OG  
9663  N N   . ARG C  165 ? 0.4478 0.5056 0.4932 -0.0003 0.1334  0.0113  165 ARG C N   
9664  C CA  . ARG C  165 ? 0.4951 0.5515 0.5394 0.0040  0.1333  0.0146  165 ARG C CA  
9665  C C   . ARG C  165 ? 0.3855 0.4452 0.4266 -0.0027 0.1279  0.0143  165 ARG C C   
9666  O O   . ARG C  165 ? 0.3412 0.3917 0.3739 -0.0024 0.1261  0.0150  165 ARG C O   
9667  C CB  . ARG C  165 ? 0.8396 0.9107 0.8965 0.0130  0.1379  0.0190  165 ARG C CB  
9668  C CG  . ARG C  165 ? 0.9458 1.0149 1.0005 0.0202  0.1388  0.0243  165 ARG C CG  
9669  C CD  . ARG C  165 ? 1.0532 1.1456 1.1229 0.0273  0.1396  0.0296  165 ARG C CD  
9670  N NE  . ARG C  165 ? 1.1405 1.2360 1.2050 0.0253  0.1314  0.0313  165 ARG C NE  
9671  C CZ  . ARG C  165 ? 1.2119 1.2992 1.2673 0.0319  0.1287  0.0352  165 ARG C CZ  
9672  N NH1 . ARG C  165 ? 1.2369 1.3123 1.2885 0.0410  0.1349  0.0388  165 ARG C NH1 
9673  N NH2 . ARG C  165 ? 1.2184 1.3085 1.2676 0.0292  0.1200  0.0357  165 ARG C NH2 
9674  N N   . GLU C  166 ? 0.2538 0.3260 0.3013 -0.0088 0.1258  0.0134  166 GLU C N   
9675  C CA  . GLU C  166 ? 0.2777 0.3544 0.3244 -0.0148 0.1220  0.0134  166 GLU C CA  
9676  C C   . GLU C  166 ? 0.2535 0.3186 0.2899 -0.0224 0.1168  0.0104  166 GLU C C   
9677  O O   . GLU C  166 ? 0.2578 0.3241 0.2925 -0.0276 0.1140  0.0097  166 GLU C O   
9678  C CB  . GLU C  166 ? 0.6383 0.7365 0.7003 -0.0172 0.1231  0.0149  166 GLU C CB  
9679  C CG  . GLU C  166 ? 0.7659 0.8750 0.8379 -0.0168 0.1258  0.0147  166 GLU C CG  
9680  C CD  . GLU C  166 ? 0.8871 1.0104 0.9723 -0.0071 0.1303  0.0178  166 GLU C CD  
9681  O OE1 . GLU C  166 ? 0.9442 1.0680 1.0300 0.0001  0.1309  0.0216  166 GLU C OE1 
9682  O OE2 . GLU C  166 ? 0.9078 1.0421 1.0027 -0.0054 0.1331  0.0173  166 GLU C OE2 
9683  N N   . ALA C  167 ? 0.3308 0.3852 0.3611 -0.0227 0.1160  0.0084  167 ALA C N   
9684  C CA  . ALA C  167 ? 0.3111 0.3529 0.3314 -0.0269 0.1115  0.0059  167 ALA C CA  
9685  C C   . ALA C  167 ? 0.3470 0.3763 0.3608 -0.0242 0.1118  0.0041  167 ALA C C   
9686  O O   . ALA C  167 ? 0.3710 0.3962 0.3824 -0.0264 0.1112  0.0023  167 ALA C O   
9687  C CB  . ALA C  167 ? 0.2178 0.2622 0.2392 -0.0332 0.1096  0.0052  167 ALA C CB  
9688  N N   . PRO C  168 ? 0.1868 0.2097 0.1975 -0.0199 0.1131  0.0045  168 PRO C N   
9689  C CA  . PRO C  168 ? 0.1911 0.2025 0.1974 -0.0174 0.1149  0.0030  168 PRO C CA  
9690  C C   . PRO C  168 ? 0.3635 0.3658 0.3630 -0.0213 0.1112  -0.0002 168 PRO C C   
9691  O O   . PRO C  168 ? 0.3081 0.3032 0.3053 -0.0213 0.1129  -0.0023 168 PRO C O   
9692  C CB  . PRO C  168 ? 0.2919 0.2985 0.2953 -0.0137 0.1160  0.0049  168 PRO C CB  
9693  C CG  . PRO C  168 ? 0.2854 0.3033 0.2935 -0.0123 0.1165  0.0079  168 PRO C CG  
9694  C CD  . PRO C  168 ? 0.2788 0.3039 0.2887 -0.0180 0.1128  0.0065  168 PRO C CD  
9695  N N   . GLY C  169 ? 0.4789 0.4815 0.4753 -0.0244 0.1067  -0.0007 169 GLY C N   
9696  C CA  . GLY C  169 ? 0.4768 0.4719 0.4673 -0.0273 0.1033  -0.0036 169 GLY C CA  
9697  C C   . GLY C  169 ? 0.4659 0.4549 0.4524 -0.0259 0.1023  -0.0041 169 GLY C C   
9698  O O   . GLY C  169 ? 0.5208 0.5080 0.5079 -0.0227 0.1052  -0.0026 169 GLY C O   
9699  N N   . ASN C  170 ? 0.3321 0.3178 0.3144 -0.0283 0.0989  -0.0062 170 ASN C N   
9700  C CA  . ASN C  170 ? 0.3229 0.3046 0.3018 -0.0277 0.0977  -0.0071 170 ASN C CA  
9701  C C   . ASN C  170 ? 0.1785 0.1633 0.1566 -0.0257 0.0974  -0.0050 170 ASN C C   
9702  O O   . ASN C  170 ? 0.1827 0.1649 0.1585 -0.0246 0.0977  -0.0049 170 ASN C O   
9703  C CB  . ASN C  170 ? 0.1833 0.1585 0.1615 -0.0270 0.1004  -0.0081 170 ASN C CB  
9704  C CG  . ASN C  170 ? 0.1880 0.1590 0.1646 -0.0298 0.1004  -0.0113 170 ASN C CG  
9705  O OD1 . ASN C  170 ? 0.2023 0.1743 0.1770 -0.0322 0.0975  -0.0131 170 ASN C OD1 
9706  N ND2 . ASN C  170 ? 0.1905 0.1564 0.1676 -0.0295 0.1043  -0.0122 170 ASN C ND2 
9707  N N   . VAL C  171 ? 0.2130 0.2036 0.1926 -0.0257 0.0972  -0.0034 171 VAL C N   
9708  C CA  . VAL C  171 ? 0.2138 0.2075 0.1916 -0.0238 0.0977  -0.0017 171 VAL C CA  
9709  C C   . VAL C  171 ? 0.2242 0.2157 0.1968 -0.0248 0.0950  -0.0038 171 VAL C C   
9710  O O   . VAL C  171 ? 0.2424 0.2346 0.2118 -0.0228 0.0955  -0.0028 171 VAL C O   
9711  C CB  . VAL C  171 ? 0.1797 0.1811 0.1605 -0.0241 0.0990  0.0002  171 VAL C CB  
9712  C CG1 . VAL C  171 ? 0.1807 0.1865 0.1682 -0.0230 0.1019  0.0021  171 VAL C CG1 
9713  C CG2 . VAL C  171 ? 0.1780 0.1801 0.1573 -0.0285 0.0967  -0.0020 171 VAL C CG2 
9714  N N   . GLY C  172 ? 0.1753 0.1639 0.1465 -0.0275 0.0927  -0.0066 172 GLY C N   
9715  C CA  . GLY C  172 ? 0.1750 0.1617 0.1417 -0.0278 0.0909  -0.0088 172 GLY C CA  
9716  C C   . GLY C  172 ? 0.2373 0.2233 0.2036 -0.0258 0.0915  -0.0085 172 GLY C C   
9717  O O   . GLY C  172 ? 0.2171 0.2045 0.1804 -0.0242 0.0916  -0.0084 172 GLY C O   
9718  N N   . LEU C  173 ? 0.2942 0.2774 0.2631 -0.0264 0.0924  -0.0087 173 LEU C N   
9719  C CA  . LEU C  173 ? 0.2944 0.2755 0.2631 -0.0260 0.0938  -0.0086 173 LEU C CA  
9720  C C   . LEU C  173 ? 0.3290 0.3104 0.2968 -0.0233 0.0965  -0.0054 173 LEU C C   
9721  O O   . LEU C  173 ? 0.3498 0.3310 0.3155 -0.0228 0.0975  -0.0049 173 LEU C O   
9722  C CB  . LEU C  173 ? 0.1966 0.1732 0.1672 -0.0278 0.0952  -0.0100 173 LEU C CB  
9723  C CG  . LEU C  173 ? 0.1876 0.1641 0.1576 -0.0305 0.0930  -0.0133 173 LEU C CG  
9724  C CD1 . LEU C  173 ? 0.1794 0.1514 0.1501 -0.0327 0.0947  -0.0151 173 LEU C CD1 
9725  C CD2 . LEU C  173 ? 0.1756 0.1548 0.1441 -0.0310 0.0918  -0.0149 173 LEU C CD2 
9726  N N   . LEU C  174 ? 0.2800 0.2622 0.2490 -0.0216 0.0981  -0.0029 174 LEU C N   
9727  C CA  . LEU C  174 ? 0.2818 0.2643 0.2491 -0.0185 0.1011  0.0007  174 LEU C CA  
9728  C C   . LEU C  174 ? 0.2872 0.2739 0.2498 -0.0174 0.0999  0.0012  174 LEU C C   
9729  O O   . LEU C  174 ? 0.2925 0.2783 0.2516 -0.0156 0.1019  0.0033  174 LEU C O   
9730  C CB  . LEU C  174 ? 0.1917 0.1762 0.1618 -0.0165 0.1034  0.0032  174 LEU C CB  
9731  C CG  . LEU C  174 ? 0.1937 0.1734 0.1676 -0.0166 0.1060  0.0029  174 LEU C CG  
9732  C CD1 . LEU C  174 ? 0.2571 0.2388 0.2336 -0.0128 0.1101  0.0065  174 LEU C CD1 
9733  C CD2 . LEU C  174 ? 0.2827 0.2537 0.2546 -0.0173 0.1082  0.0021  174 LEU C CD2 
9734  N N   . ASP C  175 ? 0.1864 0.1768 0.1482 -0.0185 0.0972  -0.0010 175 ASP C N   
9735  C CA  . ASP C  175 ? 0.1883 0.1814 0.1444 -0.0175 0.0962  -0.0019 175 ASP C CA  
9736  C C   . ASP C  175 ? 0.1890 0.1815 0.1432 -0.0173 0.0959  -0.0030 175 ASP C C   
9737  O O   . ASP C  175 ? 0.1941 0.1883 0.1438 -0.0152 0.0973  -0.0015 175 ASP C O   
9738  C CB  . ASP C  175 ? 0.1856 0.1791 0.1406 -0.0198 0.0939  -0.0053 175 ASP C CB  
9739  C CG  . ASP C  175 ? 0.2254 0.2212 0.1814 -0.0210 0.0947  -0.0045 175 ASP C CG  
9740  O OD1 . ASP C  175 ? 0.1889 0.1878 0.1470 -0.0192 0.0971  -0.0011 175 ASP C OD1 
9741  O OD2 . ASP C  175 ? 0.2417 0.2364 0.1964 -0.0242 0.0935  -0.0073 175 ASP C OD2 
9742  N N   . GLN C  176 ? 0.1847 0.1756 0.1421 -0.0195 0.0944  -0.0055 176 GLN C N   
9743  C CA  . GLN C  176 ? 0.1852 0.1772 0.1424 -0.0198 0.0946  -0.0067 176 GLN C CA  
9744  C C   . GLN C  176 ? 0.3080 0.2987 0.2644 -0.0191 0.0978  -0.0037 176 GLN C C   
9745  O O   . GLN C  176 ? 0.1950 0.1886 0.1481 -0.0180 0.0991  -0.0029 176 GLN C O   
9746  C CB  . GLN C  176 ? 0.3614 0.3516 0.3226 -0.0227 0.0936  -0.0092 176 GLN C CB  
9747  C CG  . GLN C  176 ? 0.3574 0.3470 0.3187 -0.0238 0.0911  -0.0117 176 GLN C CG  
9748  C CD  . GLN C  176 ? 0.3506 0.3398 0.3142 -0.0262 0.0904  -0.0143 176 GLN C CD  
9749  O OE1 . GLN C  176 ? 0.3185 0.3080 0.2840 -0.0274 0.0918  -0.0146 176 GLN C OE1 
9750  N NE2 . GLN C  176 ? 0.3744 0.3627 0.3371 -0.0273 0.0886  -0.0164 176 GLN C NE2 
9751  N N   . ARG C  177 ? 0.3047 0.2904 0.2635 -0.0198 0.0998  -0.0019 177 ARG C N   
9752  C CA  . ARG C  177 ? 0.3006 0.2818 0.2580 -0.0195 0.1039  0.0009  177 ARG C CA  
9753  C C   . ARG C  177 ? 0.3251 0.3082 0.2769 -0.0164 0.1057  0.0045  177 ARG C C   
9754  O O   . ARG C  177 ? 0.3577 0.3399 0.3063 -0.0164 0.1083  0.0063  177 ARG C O   
9755  C CB  . ARG C  177 ? 0.2460 0.2200 0.2057 -0.0196 0.1064  0.0021  177 ARG C CB  
9756  C CG  . ARG C  177 ? 0.2145 0.1808 0.1720 -0.0195 0.1117  0.0048  177 ARG C CG  
9757  C CD  . ARG C  177 ? 0.2196 0.1776 0.1786 -0.0185 0.1153  0.0060  177 ARG C CD  
9758  N NE  . ARG C  177 ? 0.2533 0.2061 0.2151 -0.0221 0.1159  0.0021  177 ARG C NE  
9759  C CZ  . ARG C  177 ? 0.2871 0.2339 0.2509 -0.0217 0.1182  0.0013  177 ARG C CZ  
9760  N NH1 . ARG C  177 ? 0.2845 0.2308 0.2487 -0.0175 0.1200  0.0046  177 ARG C NH1 
9761  N NH2 . ARG C  177 ? 0.2948 0.2366 0.2599 -0.0254 0.1190  -0.0028 177 ARG C NH2 
9762  N N   . LEU C  178 ? 0.2066 0.1923 0.1565 -0.0140 0.1047  0.0057  178 LEU C N   
9763  C CA  . LEU C  178 ? 0.2144 0.2016 0.1576 -0.0107 0.1066  0.0093  178 LEU C CA  
9764  C C   . LEU C  178 ? 0.2159 0.2078 0.1541 -0.0105 0.1056  0.0077  178 LEU C C   
9765  O O   . LEU C  178 ? 0.2247 0.2164 0.1568 -0.0088 0.1081  0.0107  178 LEU C O   
9766  C CB  . LEU C  178 ? 0.2134 0.2040 0.1557 -0.0087 0.1058  0.0100  178 LEU C CB  
9767  C CG  . LEU C  178 ? 0.2226 0.2156 0.1560 -0.0048 0.1074  0.0134  178 LEU C CG  
9768  C CD1 . LEU C  178 ? 0.2336 0.2213 0.1635 -0.0013 0.1120  0.0196  178 LEU C CD1 
9769  C CD2 . LEU C  178 ? 0.2205 0.2182 0.1542 -0.0041 0.1064  0.0128  178 LEU C CD2 
9770  N N   . ALA C  179 ? 0.2086 0.2044 0.1489 -0.0119 0.1023  0.0033  179 ALA C N   
9771  C CA  . ALA C  179 ? 0.2105 0.2111 0.1469 -0.0111 0.1019  0.0013  179 ALA C CA  
9772  C C   . ALA C  179 ? 0.2143 0.2149 0.1521 -0.0126 0.1047  0.0027  179 ALA C C   
9773  O O   . ALA C  179 ? 0.2211 0.2251 0.1537 -0.0114 0.1066  0.0040  179 ALA C O   
9774  C CB  . ALA C  179 ? 0.2037 0.2068 0.1422 -0.0116 0.0986  -0.0035 179 ALA C CB  
9775  N N   . LEU C  180 ? 0.2695 0.2663 0.2136 -0.0156 0.1052  0.0024  180 LEU C N   
9776  C CA  . LEU C  180 ? 0.2866 0.2818 0.2319 -0.0181 0.1087  0.0036  180 LEU C CA  
9777  C C   . LEU C  180 ? 0.3312 0.3213 0.2709 -0.0173 0.1133  0.0088  180 LEU C C   
9778  O O   . LEU C  180 ? 0.3464 0.3384 0.2834 -0.0182 0.1163  0.0103  180 LEU C O   
9779  C CB  . LEU C  180 ? 0.2132 0.2035 0.1648 -0.0218 0.1088  0.0017  180 LEU C CB  
9780  C CG  . LEU C  180 ? 0.2916 0.2873 0.2479 -0.0240 0.1068  -0.0026 180 LEU C CG  
9781  C CD1 . LEU C  180 ? 0.2000 0.2016 0.1556 -0.0214 0.1028  -0.0051 180 LEU C CD1 
9782  C CD2 . LEU C  180 ? 0.2041 0.1941 0.1648 -0.0273 0.1065  -0.0047 180 LEU C CD2 
9783  N N   . GLN C  181 ? 0.2321 0.2158 0.1698 -0.0153 0.1143  0.0117  181 GLN C N   
9784  C CA  . GLN C  181 ? 0.2454 0.2231 0.1761 -0.0131 0.1188  0.0174  181 GLN C CA  
9785  C C   . GLN C  181 ? 0.2507 0.2348 0.1732 -0.0105 0.1185  0.0189  181 GLN C C   
9786  O O   . GLN C  181 ? 0.2682 0.2503 0.1845 -0.0103 0.1223  0.0226  181 GLN C O   
9787  C CB  . GLN C  181 ? 0.5189 0.4903 0.4490 -0.0098 0.1197  0.0204  181 GLN C CB  
9788  C CG  . GLN C  181 ? 0.5372 0.5046 0.4753 -0.0117 0.1190  0.0177  181 GLN C CG  
9789  C CD  . GLN C  181 ? 0.5983 0.5577 0.5359 -0.0081 0.1225  0.0217  181 GLN C CD  
9790  O OE1 . GLN C  181 ? 0.5714 0.5340 0.5120 -0.0061 0.1207  0.0212  181 GLN C OE1 
9791  N NE2 . GLN C  181 ? 0.6762 0.6247 0.6099 -0.0070 0.1283  0.0259  181 GLN C NE2 
9792  N N   . TRP C  182 ? 0.3226 0.3137 0.2439 -0.0086 0.1145  0.0158  182 TRP C N   
9793  C CA  . TRP C  182 ? 0.3223 0.3193 0.2346 -0.0060 0.1142  0.0159  182 TRP C CA  
9794  C C   . TRP C  182 ? 0.3229 0.3248 0.2349 -0.0079 0.1159  0.0149  182 TRP C C   
9795  O O   . TRP C  182 ? 0.3425 0.3452 0.2462 -0.0068 0.1187  0.0179  182 TRP C O   
9796  C CB  . TRP C  182 ? 0.3134 0.3160 0.2248 -0.0045 0.1098  0.0111  182 TRP C CB  
9797  C CG  . TRP C  182 ? 0.2513 0.2586 0.1515 -0.0014 0.1095  0.0103  182 TRP C CG  
9798  C CD1 . TRP C  182 ? 0.4208 0.4267 0.3101 0.0020  0.1095  0.0128  182 TRP C CD1 
9799  C CD2 . TRP C  182 ? 0.2525 0.2665 0.1502 -0.0011 0.1092  0.0066  182 TRP C CD2 
9800  N NE1 . TRP C  182 ? 0.2686 0.2789 0.1479 0.0041  0.1089  0.0103  182 TRP C NE1 
9801  C CE2 . TRP C  182 ? 0.2634 0.2789 0.1482 0.0022  0.1090  0.0063  182 TRP C CE2 
9802  C CE3 . TRP C  182 ? 0.2466 0.2658 0.1512 -0.0028 0.1093  0.0034  182 TRP C CE3 
9803  C CZ2 . TRP C  182 ? 0.2683 0.2902 0.1474 0.0037  0.1090  0.0025  182 TRP C CZ2 
9804  C CZ3 . TRP C  182 ? 0.3694 0.3960 0.2692 -0.0007 0.1096  0.0002  182 TRP C CZ3 
9805  C CH2 . TRP C  182 ? 0.3574 0.3851 0.2447 0.0024  0.1095  -0.0006 182 TRP C CH2 
9806  N N   . VAL C  183 ? 0.3023 0.3079 0.2229 -0.0106 0.1145  0.0109  183 VAL C N   
9807  C CA  . VAL C  183 ? 0.2456 0.2577 0.1675 -0.0123 0.1165  0.0098  183 VAL C CA  
9808  C C   . VAL C  183 ? 0.3608 0.3676 0.2803 -0.0148 0.1218  0.0148  183 VAL C C   
9809  O O   . VAL C  183 ? 0.2660 0.2776 0.1808 -0.0150 0.1249  0.0164  183 VAL C O   
9810  C CB  . VAL C  183 ? 0.2438 0.2595 0.1753 -0.0146 0.1144  0.0055  183 VAL C CB  
9811  C CG1 . VAL C  183 ? 0.2387 0.2616 0.1725 -0.0165 0.1176  0.0052  183 VAL C CG1 
9812  C CG2 . VAL C  183 ? 0.2265 0.2464 0.1586 -0.0117 0.1099  0.0009  183 VAL C CG2 
9813  N N   . GLN C  184 ? 0.3831 0.3794 0.3049 -0.0165 0.1235  0.0174  184 GLN C N   
9814  C CA  . GLN C  184 ? 0.3919 0.3803 0.3106 -0.0188 0.1293  0.0223  184 GLN C CA  
9815  C C   . GLN C  184 ? 0.4164 0.4030 0.3235 -0.0160 0.1323  0.0277  184 GLN C C   
9816  O O   . GLN C  184 ? 0.4723 0.4610 0.3756 -0.0179 0.1361  0.0300  184 GLN C O   
9817  C CB  . GLN C  184 ? 0.2756 0.2508 0.1971 -0.0201 0.1312  0.0239  184 GLN C CB  
9818  C CG  . GLN C  184 ? 0.2682 0.2434 0.1990 -0.0248 0.1306  0.0194  184 GLN C CG  
9819  C CD  . GLN C  184 ? 0.2774 0.2524 0.2088 -0.0296 0.1354  0.0202  184 GLN C CD  
9820  O OE1 . GLN C  184 ? 0.2912 0.2547 0.2189 -0.0313 0.1408  0.0240  184 GLN C OE1 
9821  N NE2 . GLN C  184 ? 0.2713 0.2585 0.2071 -0.0316 0.1341  0.0168  184 GLN C NE2 
9822  N N   . GLU C  185 ? 0.3075 0.2907 0.2085 -0.0114 0.1306  0.0299  185 GLU C N   
9823  C CA  . GLU C  185 ? 0.3508 0.3319 0.2388 -0.0080 0.1330  0.0354  185 GLU C CA  
9824  C C   . GLU C  185 ? 0.4109 0.4039 0.2935 -0.0076 0.1321  0.0328  185 GLU C C   
9825  O O   . GLU C  185 ? 0.4423 0.4355 0.3167 -0.0079 0.1359  0.0365  185 GLU C O   
9826  C CB  . GLU C  185 ? 0.3177 0.2940 0.1996 -0.0023 0.1312  0.0385  185 GLU C CB  
9827  C CG  . GLU C  185 ? 0.3886 0.3617 0.2556 0.0022  0.1334  0.0451  185 GLU C CG  
9828  C CD  . GLU C  185 ? 0.4520 0.4183 0.3131 0.0087  0.1328  0.0505  185 GLU C CD  
9829  O OE1 . GLU C  185 ? 0.4690 0.4346 0.3388 0.0093  0.1309  0.0484  185 GLU C OE1 
9830  O OE2 . GLU C  185 ? 0.4597 0.4222 0.3073 0.0138  0.1341  0.0574  185 GLU C OE2 
9831  N N   . ASN C  186 ? 0.4061 0.4081 0.2923 -0.0065 0.1273  0.0265  186 ASN C N   
9832  C CA  . ASN C  186 ? 0.3994 0.4110 0.2784 -0.0046 0.1263  0.0235  186 ASN C CA  
9833  C C   . ASN C  186 ? 0.2920 0.3153 0.1766 -0.0064 0.1267  0.0186  186 ASN C C   
9834  O O   . ASN C  186 ? 0.2976 0.3283 0.1751 -0.0044 0.1268  0.0163  186 ASN C O   
9835  C CB  . ASN C  186 ? 0.3834 0.3958 0.2578 -0.0006 0.1216  0.0203  186 ASN C CB  
9836  C CG  . ASN C  186 ? 0.3661 0.3693 0.2345 0.0024  0.1214  0.0258  186 ASN C CG  
9837  O OD1 . ASN C  186 ? 0.4371 0.4372 0.2927 0.0057  0.1229  0.0306  186 ASN C OD1 
9838  N ND2 . ASN C  186 ? 0.3023 0.3013 0.1794 0.0018  0.1198  0.0255  186 ASN C ND2 
9839  N N   . ILE C  187 ? 0.3571 0.3823 0.2533 -0.0097 0.1270  0.0169  187 ILE C N   
9840  C CA  . ILE C  187 ? 0.3834 0.4210 0.2849 -0.0096 0.1267  0.0120  187 ILE C CA  
9841  C C   . ILE C  187 ? 0.4127 0.4568 0.3098 -0.0110 0.1321  0.0147  187 ILE C C   
9842  O O   . ILE C  187 ? 0.4203 0.4763 0.3179 -0.0094 0.1329  0.0113  187 ILE C O   
9843  C CB  . ILE C  187 ? 0.3099 0.3487 0.2244 -0.0120 0.1251  0.0092  187 ILE C CB  
9844  C CG1 . ILE C  187 ? 0.2576 0.3078 0.1760 -0.0090 0.1231  0.0036  187 ILE C CG1 
9845  C CG2 . ILE C  187 ? 0.3075 0.3439 0.2268 -0.0172 0.1297  0.0126  187 ILE C CG2 
9846  C CD1 . ILE C  187 ? 0.2523 0.3019 0.1670 -0.0045 0.1182  -0.0008 187 ILE C CD1 
9847  N N   . ALA C  188 ? 0.3661 0.4017 0.2582 -0.0137 0.1363  0.0210  188 ALA C N   
9848  C CA  . ALA C  188 ? 0.3893 0.4291 0.2759 -0.0158 0.1421  0.0247  188 ALA C CA  
9849  C C   . ALA C  188 ? 0.3759 0.4239 0.2513 -0.0122 0.1422  0.0229  188 ALA C C   
9850  O O   . ALA C  188 ? 0.3618 0.4199 0.2353 -0.0131 0.1463  0.0230  188 ALA C O   
9851  C CB  . ALA C  188 ? 0.5664 0.5922 0.4472 -0.0184 0.1464  0.0323  188 ALA C CB  
9852  N N   . ALA C  189 ? 0.3236 0.3674 0.1916 -0.0082 0.1380  0.0210  189 ALA C N   
9853  C CA  . ALA C  189 ? 0.3773 0.4261 0.2327 -0.0049 0.1378  0.0185  189 ALA C CA  
9854  C C   . ALA C  189 ? 0.3608 0.4230 0.2209 -0.0028 0.1358  0.0100  189 ALA C C   
9855  O O   . ALA C  189 ? 0.3350 0.4031 0.1857 -0.0011 0.1370  0.0066  189 ALA C O   
9856  C CB  . ALA C  189 ? 0.3378 0.3767 0.1825 -0.0013 0.1340  0.0195  189 ALA C CB  
9857  N N   . PHE C  190 ? 0.4965 0.5623 0.3701 -0.0026 0.1331  0.0065  190 PHE C N   
9858  C CA  . PHE C  190 ? 0.4736 0.5510 0.3515 0.0008  0.1315  -0.0008 190 PHE C CA  
9859  C C   . PHE C  190 ? 0.5030 0.5924 0.3891 -0.0001 0.1360  0.0001  190 PHE C C   
9860  O O   . PHE C  190 ? 0.5660 0.6638 0.4572 0.0038  0.1348  -0.0048 190 PHE C O   
9861  C CB  . PHE C  190 ? 0.2877 0.3613 0.1731 0.0033  0.1257  -0.0051 190 PHE C CB  
9862  C CG  . PHE C  190 ? 0.2882 0.3517 0.1658 0.0047  0.1215  -0.0064 190 PHE C CG  
9863  C CD1 . PHE C  190 ? 0.2867 0.3392 0.1642 0.0025  0.1206  -0.0011 190 PHE C CD1 
9864  C CD2 . PHE C  190 ? 0.2917 0.3561 0.1618 0.0084  0.1187  -0.0131 190 PHE C CD2 
9865  C CE1 . PHE C  190 ? 0.2880 0.3325 0.1583 0.0044  0.1170  -0.0018 190 PHE C CE1 
9866  C CE2 . PHE C  190 ? 0.2939 0.3485 0.1559 0.0096  0.1149  -0.0140 190 PHE C CE2 
9867  C CZ  . PHE C  190 ? 0.2916 0.3373 0.1541 0.0079  0.1141  -0.0080 190 PHE C CZ  
9868  N N   . GLY C  191 ? 0.3845 0.4715 0.2722 -0.0049 0.1406  0.0067  191 GLY C N   
9869  C CA  . GLY C  191 ? 0.3952 0.4928 0.2910 -0.0065 0.1456  0.0084  191 GLY C CA  
9870  C C   . GLY C  191 ? 0.4070 0.4998 0.3158 -0.0094 0.1444  0.0092  191 GLY C C   
9871  O O   . GLY C  191 ? 0.4102 0.5107 0.3278 -0.0105 0.1477  0.0095  191 GLY C O   
9872  N N   . GLY C  192 ? 0.5026 0.5823 0.4122 -0.0107 0.1400  0.0095  192 GLY C N   
9873  C CA  . GLY C  192 ? 0.4890 0.5622 0.4092 -0.0144 0.1386  0.0096  192 GLY C CA  
9874  C C   . GLY C  192 ? 0.4884 0.5534 0.4096 -0.0210 0.1432  0.0151  192 GLY C C   
9875  O O   . GLY C  192 ? 0.5349 0.5963 0.4475 -0.0225 0.1470  0.0198  192 GLY C O   
9876  N N   . ASP C  193 ? 0.3457 0.4065 0.2764 -0.0252 0.1430  0.0143  193 ASP C N   
9877  C CA  . ASP C  193 ? 0.3435 0.3961 0.2762 -0.0321 0.1477  0.0182  193 ASP C CA  
9878  C C   . ASP C  193 ? 0.2875 0.3259 0.2230 -0.0341 0.1446  0.0175  193 ASP C C   
9879  O O   . ASP C  193 ? 0.4137 0.4525 0.3576 -0.0362 0.1425  0.0136  193 ASP C O   
9880  C CB  . ASP C  193 ? 0.4524 0.5149 0.3946 -0.0361 0.1513  0.0165  193 ASP C CB  
9881  C CG  . ASP C  193 ? 0.5099 0.5643 0.4541 -0.0442 0.1569  0.0199  193 ASP C CG  
9882  O OD1 . ASP C  193 ? 0.4973 0.5359 0.4363 -0.0464 0.1575  0.0230  193 ASP C OD1 
9883  O OD2 . ASP C  193 ? 0.5341 0.5977 0.4851 -0.0483 0.1612  0.0193  193 ASP C OD2 
9884  N N   . PRO C  194 ? 0.2936 0.3192 0.2215 -0.0332 0.1446  0.0211  194 PRO C N   
9885  C CA  . PRO C  194 ? 0.2967 0.3096 0.2271 -0.0337 0.1417  0.0202  194 PRO C CA  
9886  C C   . PRO C  194 ? 0.3164 0.3229 0.2538 -0.0400 0.1444  0.0190  194 PRO C C   
9887  O O   . PRO C  194 ? 0.2836 0.2815 0.2244 -0.0406 0.1420  0.0167  194 PRO C O   
9888  C CB  . PRO C  194 ? 0.3462 0.3469 0.2664 -0.0315 0.1435  0.0257  194 PRO C CB  
9889  C CG  . PRO C  194 ? 0.4006 0.4099 0.3125 -0.0281 0.1442  0.0277  194 PRO C CG  
9890  C CD  . PRO C  194 ? 0.4463 0.4686 0.3625 -0.0311 0.1474  0.0263  194 PRO C CD  
9891  N N   . MET C  195 ? 0.3532 0.3639 0.2924 -0.0449 0.1497  0.0203  195 MET C N   
9892  C CA  . MET C  195 ? 0.3723 0.3765 0.3172 -0.0520 0.1531  0.0188  195 MET C CA  
9893  C C   . MET C  195 ? 0.3544 0.3703 0.3096 -0.0548 0.1512  0.0130  195 MET C C   
9894  O O   . MET C  195 ? 0.3429 0.3546 0.3033 -0.0612 0.1535  0.0105  195 MET C O   
9895  C CB  . MET C  195 ? 0.4200 0.4188 0.3604 -0.0572 0.1608  0.0241  195 MET C CB  
9896  C CG  . MET C  195 ? 0.3375 0.3153 0.2709 -0.0583 0.1640  0.0281  195 MET C CG  
9897  S SD  . MET C  195 ? 1.2806 1.2509 1.2038 -0.0610 0.1723  0.0365  195 MET C SD  
9898  C CE  . MET C  195 ? 0.5983 0.5802 0.5298 -0.0702 0.1776  0.0349  195 MET C CE  
9899  N N   . SER C  196 ? 0.2832 0.3131 0.2410 -0.0499 0.1474  0.0105  196 SER C N   
9900  C CA  . SER C  196 ? 0.2723 0.3105 0.2389 -0.0508 0.1444  0.0049  196 SER C CA  
9901  C C   . SER C  196 ? 0.2582 0.2997 0.2242 -0.0437 0.1377  0.0022  196 SER C C   
9902  O O   . SER C  196 ? 0.2555 0.3070 0.2196 -0.0383 0.1366  0.0022  196 SER C O   
9903  C CB  . SER C  196 ? 0.3749 0.4285 0.3473 -0.0531 0.1485  0.0042  196 SER C CB  
9904  O OG  . SER C  196 ? 0.3864 0.4509 0.3665 -0.0517 0.1455  -0.0011 196 SER C OG  
9905  N N   . VAL C  197 ? 0.3536 0.3869 0.3213 -0.0439 0.1335  -0.0005 197 VAL C N   
9906  C CA  . VAL C  197 ? 0.3422 0.3765 0.3087 -0.0381 0.1275  -0.0026 197 VAL C CA  
9907  C C   . VAL C  197 ? 0.3668 0.4009 0.3395 -0.0404 0.1246  -0.0074 197 VAL C C   
9908  O O   . VAL C  197 ? 0.4258 0.4504 0.3997 -0.0448 0.1250  -0.0083 197 VAL C O   
9909  C CB  . VAL C  197 ? 0.2384 0.2606 0.1990 -0.0358 0.1255  -0.0001 197 VAL C CB  
9910  C CG1 . VAL C  197 ? 0.2279 0.2521 0.1874 -0.0305 0.1199  -0.0021 197 VAL C CG1 
9911  C CG2 . VAL C  197 ? 0.2864 0.3058 0.2397 -0.0347 0.1292  0.0051  197 VAL C CG2 
9912  N N   . THR C  198 ? 0.3628 0.4070 0.3388 -0.0373 0.1219  -0.0107 198 THR C N   
9913  C CA  . THR C  198 ? 0.3663 0.4113 0.3473 -0.0392 0.1190  -0.0152 198 THR C CA  
9914  C C   . THR C  198 ? 0.3775 0.4188 0.3557 -0.0344 0.1136  -0.0164 198 THR C C   
9915  O O   . THR C  198 ? 0.4065 0.4525 0.3818 -0.0287 0.1119  -0.0163 198 THR C O   
9916  C CB  . THR C  198 ? 0.2162 0.2754 0.2034 -0.0395 0.1204  -0.0184 198 THR C CB  
9917  O OG1 . THR C  198 ? 0.2588 0.3226 0.2494 -0.0448 0.1258  -0.0175 198 THR C OG1 
9918  C CG2 . THR C  198 ? 0.3072 0.3680 0.2989 -0.0418 0.1177  -0.0233 198 THR C CG2 
9919  N N   . LEU C  199 ? 0.3083 0.3409 0.2868 -0.0367 0.1112  -0.0177 199 LEU C N   
9920  C CA  . LEU C  199 ? 0.2553 0.2852 0.2319 -0.0332 0.1065  -0.0190 199 LEU C CA  
9921  C C   . LEU C  199 ? 0.2606 0.2983 0.2410 -0.0334 0.1052  -0.0233 199 LEU C C   
9922  O O   . LEU C  199 ? 0.2743 0.3154 0.2592 -0.0382 0.1069  -0.0258 199 LEU C O   
9923  C CB  . LEU C  199 ? 0.1952 0.2134 0.1704 -0.0354 0.1051  -0.0185 199 LEU C CB  
9924  C CG  . LEU C  199 ? 0.2000 0.2099 0.1719 -0.0352 0.1070  -0.0146 199 LEU C CG  
9925  C CD1 . LEU C  199 ? 0.1993 0.1990 0.1709 -0.0370 0.1063  -0.0150 199 LEU C CD1 
9926  C CD2 . LEU C  199 ? 0.1988 0.2103 0.1664 -0.0300 0.1056  -0.0120 199 LEU C CD2 
9927  N N   . PHE C  200 ? 0.2337 0.2747 0.2121 -0.0283 0.1026  -0.0246 200 PHE C N   
9928  C CA  . PHE C  200 ? 0.2461 0.2927 0.2272 -0.0282 0.1012  -0.0287 200 PHE C CA  
9929  C C   . PHE C  200 ? 0.2716 0.3127 0.2480 -0.0245 0.0976  -0.0294 200 PHE C C   
9930  O O   . PHE C  200 ? 0.1831 0.2204 0.1549 -0.0206 0.0965  -0.0278 200 PHE C O   
9931  C CB  . PHE C  200 ? 0.1894 0.2499 0.1748 -0.0263 0.1036  -0.0312 200 PHE C CB  
9932  C CG  . PHE C  200 ? 0.2682 0.3329 0.2500 -0.0186 0.1035  -0.0313 200 PHE C CG  
9933  C CD1 . PHE C  200 ? 0.2603 0.3192 0.2359 -0.0155 0.1032  -0.0282 200 PHE C CD1 
9934  C CD2 . PHE C  200 ? 0.2439 0.3186 0.2280 -0.0143 0.1040  -0.0351 200 PHE C CD2 
9935  C CE1 . PHE C  200 ? 0.2378 0.3000 0.2090 -0.0086 0.1033  -0.0292 200 PHE C CE1 
9936  C CE2 . PHE C  200 ? 0.2391 0.3162 0.2189 -0.0066 0.1043  -0.0360 200 PHE C CE2 
9937  C CZ  . PHE C  200 ? 0.2468 0.3171 0.2196 -0.0039 0.1039  -0.0332 200 PHE C CZ  
9938  N N   . GLY C  201 ? 0.3058 0.3460 0.2830 -0.0264 0.0960  -0.0320 201 GLY C N   
9939  C CA  . GLY C  201 ? 0.1793 0.2136 0.1516 -0.0237 0.0932  -0.0327 201 GLY C CA  
9940  C C   . GLY C  201 ? 0.1795 0.2171 0.1520 -0.0246 0.0924  -0.0363 201 GLY C C   
9941  O O   . GLY C  201 ? 0.1800 0.2241 0.1570 -0.0283 0.0935  -0.0385 201 GLY C O   
9942  N N   . GLU C  202 ? 0.1804 0.2134 0.1475 -0.0215 0.0906  -0.0374 202 GLU C N   
9943  C CA  . GLU C  202 ? 0.2234 0.2586 0.1886 -0.0217 0.0900  -0.0408 202 GLU C CA  
9944  C C   . GLU C  202 ? 0.2151 0.2383 0.1744 -0.0241 0.0884  -0.0391 202 GLU C C   
9945  O O   . GLU C  202 ? 0.2478 0.2624 0.2044 -0.0239 0.0877  -0.0364 202 GLU C O   
9946  C CB  . GLU C  202 ? 0.2895 0.3308 0.2524 -0.0147 0.0900  -0.0446 202 GLU C CB  
9947  C CG  . GLU C  202 ? 0.3431 0.3879 0.3029 -0.0132 0.0893  -0.0489 202 GLU C CG  
9948  C CD  . GLU C  202 ? 0.4040 0.4346 0.3531 -0.0117 0.0879  -0.0486 202 GLU C CD  
9949  O OE1 . GLU C  202 ? 0.4203 0.4404 0.3659 -0.0115 0.0875  -0.0459 202 GLU C OE1 
9950  O OE2 . GLU C  202 ? 0.4459 0.4756 0.3895 -0.0111 0.0869  -0.0511 202 GLU C OE2 
9951  N N   . SER C  203 ? 0.1849 0.2085 0.1422 -0.0269 0.0882  -0.0409 203 SER C N   
9952  C CA  . SER C  203 ? 0.1869 0.1998 0.1380 -0.0297 0.0873  -0.0391 203 SER C CA  
9953  C C   . SER C  203 ? 0.1828 0.1882 0.1365 -0.0332 0.0871  -0.0353 203 SER C C   
9954  O O   . SER C  203 ? 0.1806 0.1879 0.1392 -0.0363 0.0878  -0.0350 203 SER C O   
9955  C CB  . SER C  203 ? 0.1941 0.1990 0.1359 -0.0261 0.0868  -0.0396 203 SER C CB  
9956  O OG  . SER C  203 ? 0.1983 0.1955 0.1324 -0.0290 0.0865  -0.0388 203 SER C OG  
9957  N N   . ALA C  204 ? 0.2829 0.2796 0.2329 -0.0327 0.0865  -0.0329 204 ALA C N   
9958  C CA  . ALA C  204 ? 0.2622 0.2538 0.2153 -0.0347 0.0863  -0.0297 204 ALA C CA  
9959  C C   . ALA C  204 ? 0.2652 0.2602 0.2234 -0.0331 0.0866  -0.0286 204 ALA C C   
9960  O O   . ALA C  204 ? 0.2342 0.2264 0.1951 -0.0342 0.0869  -0.0264 204 ALA C O   
9961  C CB  . ALA C  204 ? 0.1816 0.1653 0.1304 -0.0349 0.0859  -0.0278 204 ALA C CB  
9962  N N   . GLY C  205 ? 0.3147 0.3158 0.2733 -0.0300 0.0870  -0.0300 205 GLY C N   
9963  C CA  . GLY C  205 ? 0.3088 0.3140 0.2711 -0.0286 0.0879  -0.0289 205 GLY C CA  
9964  C C   . GLY C  205 ? 0.3020 0.3116 0.2690 -0.0318 0.0894  -0.0296 205 GLY C C   
9965  O O   . GLY C  205 ? 0.3135 0.3219 0.2829 -0.0328 0.0907  -0.0277 205 GLY C O   
9966  N N   . ALA C  206 ? 0.1974 0.2118 0.1653 -0.0337 0.0897  -0.0327 206 ALA C N   
9967  C CA  . ALA C  206 ? 0.1780 0.1962 0.1500 -0.0381 0.0915  -0.0344 206 ALA C CA  
9968  C C   . ALA C  206 ? 0.1789 0.1880 0.1500 -0.0418 0.0917  -0.0335 206 ALA C C   
9969  O O   . ALA C  206 ? 0.1813 0.1885 0.1548 -0.0449 0.0938  -0.0337 206 ALA C O   
9970  C CB  . ALA C  206 ? 0.1799 0.2072 0.1529 -0.0395 0.0917  -0.0387 206 ALA C CB  
9971  N N   . ALA C  207 ? 0.1783 0.1814 0.1456 -0.0414 0.0901  -0.0327 207 ALA C N   
9972  C CA  . ALA C  207 ? 0.1885 0.1833 0.1548 -0.0436 0.0905  -0.0316 207 ALA C CA  
9973  C C   . ALA C  207 ? 0.1968 0.1876 0.1651 -0.0419 0.0913  -0.0286 207 ALA C C   
9974  O O   . ALA C  207 ? 0.1816 0.1677 0.1508 -0.0440 0.0934  -0.0287 207 ALA C O   
9975  C CB  . ALA C  207 ? 0.1790 0.1694 0.1413 -0.0428 0.0889  -0.0305 207 ALA C CB  
9976  N N   . SER C  208 ? 0.1758 0.1679 0.1438 -0.0382 0.0902  -0.0262 208 SER C N   
9977  C CA  . SER C  208 ? 0.2117 0.2011 0.1805 -0.0363 0.0911  -0.0232 208 SER C CA  
9978  C C   . SER C  208 ? 0.1931 0.1838 0.1641 -0.0378 0.0938  -0.0233 208 SER C C   
9979  O O   . SER C  208 ? 0.1829 0.1680 0.1541 -0.0385 0.0960  -0.0220 208 SER C O   
9980  C CB  . SER C  208 ? 0.1739 0.1656 0.1410 -0.0326 0.0897  -0.0215 208 SER C CB  
9981  O OG  . SER C  208 ? 0.1726 0.1607 0.1376 -0.0323 0.0882  -0.0209 208 SER C OG  
9982  N N   . VAL C  209 ? 0.1798 0.1777 0.1522 -0.0382 0.0943  -0.0250 209 VAL C N   
9983  C CA  . VAL C  209 ? 0.2240 0.2236 0.1985 -0.0405 0.0975  -0.0252 209 VAL C CA  
9984  C C   . VAL C  209 ? 0.2145 0.2077 0.1896 -0.0455 0.0999  -0.0273 209 VAL C C   
9985  O O   . VAL C  209 ? 0.2149 0.2022 0.1897 -0.0468 0.1031  -0.0261 209 VAL C O   
9986  C CB  . VAL C  209 ? 0.1842 0.1946 0.1613 -0.0406 0.0980  -0.0273 209 VAL C CB  
9987  C CG1 . VAL C  209 ? 0.1901 0.2028 0.1703 -0.0453 0.1018  -0.0287 209 VAL C CG1 
9988  C CG2 . VAL C  209 ? 0.1824 0.1973 0.1579 -0.0354 0.0971  -0.0251 209 VAL C CG2 
9989  N N   . GLY C  210 ? 0.2164 0.2099 0.1913 -0.0482 0.0990  -0.0307 210 GLY C N   
9990  C CA  . GLY C  210 ? 0.2463 0.2329 0.2204 -0.0530 0.1015  -0.0336 210 GLY C CA  
9991  C C   . GLY C  210 ? 0.2653 0.2412 0.2372 -0.0514 0.1027  -0.0313 210 GLY C C   
9992  O O   . GLY C  210 ? 0.2563 0.2243 0.2273 -0.0543 0.1067  -0.0327 210 GLY C O   
9993  N N   . MET C  211 ? 0.1917 0.1672 0.1627 -0.0468 0.1000  -0.0280 211 MET C N   
9994  C CA  . MET C  211 ? 0.2008 0.1687 0.1709 -0.0448 0.1013  -0.0257 211 MET C CA  
9995  C C   . MET C  211 ? 0.1985 0.1626 0.1688 -0.0435 0.1046  -0.0230 211 MET C C   
9996  O O   . MET C  211 ? 0.2049 0.1605 0.1742 -0.0435 0.1082  -0.0225 211 MET C O   
9997  C CB  . MET C  211 ? 0.2787 0.2491 0.2485 -0.0409 0.0979  -0.0230 211 MET C CB  
9998  C CG  . MET C  211 ? 0.2259 0.1918 0.1949 -0.0409 0.0982  -0.0232 211 MET C CG  
9999  S SD  . MET C  211 ? 0.3606 0.3296 0.3275 -0.0431 0.0954  -0.0258 211 MET C SD  
10000 C CE  . MET C  211 ? 0.8458 0.8087 0.8109 -0.0474 0.0990  -0.0298 211 MET C CE  
10001 N N   . HIS C  212 ? 0.1970 0.1668 0.1679 -0.0423 0.1040  -0.0213 212 HIS C N   
10002 C CA  . HIS C  212 ? 0.2324 0.1983 0.2024 -0.0415 0.1077  -0.0185 212 HIS C CA  
10003 C C   . HIS C  212 ? 0.2602 0.2207 0.2301 -0.0466 0.1125  -0.0211 212 HIS C C   
10004 O O   . HIS C  212 ? 0.2507 0.2025 0.2188 -0.0468 0.1171  -0.0194 212 HIS C O   
10005 C CB  . HIS C  212 ? 0.2007 0.1743 0.1705 -0.0388 0.1063  -0.0157 212 HIS C CB  
10006 C CG  . HIS C  212 ? 0.1943 0.1713 0.1631 -0.0343 0.1028  -0.0134 212 HIS C CG  
10007 N ND1 . HIS C  212 ? 0.1963 0.1694 0.1635 -0.0313 0.1037  -0.0101 212 HIS C ND1 
10008 C CD2 . HIS C  212 ? 0.1874 0.1708 0.1563 -0.0327 0.0989  -0.0143 212 HIS C CD2 
10009 C CE1 . HIS C  212 ? 0.1905 0.1684 0.1572 -0.0286 0.1005  -0.0092 212 HIS C CE1 
10010 N NE2 . HIS C  212 ? 0.3031 0.2861 0.2704 -0.0294 0.0976  -0.0119 212 HIS C NE2 
10011 N N   . ILE C  213 ? 0.3059 0.2712 0.2776 -0.0510 0.1119  -0.0253 213 ILE C N   
10012 C CA  . ILE C  213 ? 0.3124 0.2728 0.2840 -0.0572 0.1168  -0.0290 213 ILE C CA  
10013 C C   . ILE C  213 ? 0.3369 0.2844 0.3057 -0.0588 0.1202  -0.0310 213 ILE C C   
10014 O O   . ILE C  213 ? 0.2417 0.1793 0.2085 -0.0619 0.1260  -0.0322 213 ILE C O   
10015 C CB  . ILE C  213 ? 0.2204 0.1897 0.1945 -0.0620 0.1154  -0.0340 213 ILE C CB  
10016 C CG1 . ILE C  213 ? 0.2155 0.1976 0.1930 -0.0607 0.1136  -0.0326 213 ILE C CG1 
10017 C CG2 . ILE C  213 ? 0.2318 0.1958 0.2055 -0.0694 0.1205  -0.0387 213 ILE C CG2 
10018 C CD1 . ILE C  213 ? 0.2130 0.2057 0.1936 -0.0643 0.1122  -0.0372 213 ILE C CD1 
10019 N N   . LEU C  214 ? 0.2242 0.1714 0.1924 -0.0566 0.1172  -0.0315 214 LEU C N   
10020 C CA  . LEU C  214 ? 0.2315 0.1673 0.1971 -0.0576 0.1208  -0.0336 214 LEU C CA  
10021 C C   . LEU C  214 ? 0.2785 0.2059 0.2429 -0.0525 0.1236  -0.0292 214 LEU C C   
10022 O O   . LEU C  214 ? 0.3094 0.2253 0.2715 -0.0534 0.1288  -0.0308 214 LEU C O   
10023 C CB  . LEU C  214 ? 0.2447 0.1838 0.2098 -0.0582 0.1175  -0.0362 214 LEU C CB  
10024 C CG  . LEU C  214 ? 0.2269 0.1719 0.1920 -0.0642 0.1167  -0.0416 214 LEU C CG  
10025 C CD1 . LEU C  214 ? 0.2239 0.1709 0.1871 -0.0648 0.1141  -0.0437 214 LEU C CD1 
10026 C CD2 . LEU C  214 ? 0.2833 0.2197 0.2464 -0.0707 0.1230  -0.0463 214 LEU C CD2 
10027 N N   . SER C  215 ? 0.3042 0.2372 0.2699 -0.0473 0.1207  -0.0240 215 SER C N   
10028 C CA  . SER C  215 ? 0.3434 0.2702 0.3083 -0.0424 0.1235  -0.0196 215 SER C CA  
10029 C C   . SER C  215 ? 0.3335 0.2542 0.2963 -0.0420 0.1284  -0.0166 215 SER C C   
10030 O O   . SER C  215 ? 0.3325 0.2603 0.2956 -0.0419 0.1264  -0.0145 215 SER C O   
10031 C CB  . SER C  215 ? 0.4887 0.4251 0.4555 -0.0374 0.1181  -0.0159 215 SER C CB  
10032 O OG  . SER C  215 ? 0.5089 0.4413 0.4752 -0.0327 0.1210  -0.0115 215 SER C OG  
10033 N N   . LEU C  216 ? 0.4372 0.3440 0.3973 -0.0416 0.1354  -0.0161 216 LEU C N   
10034 C CA  . LEU C  216 ? 0.4730 0.3710 0.4298 -0.0421 0.1414  -0.0135 216 LEU C CA  
10035 C C   . LEU C  216 ? 0.5064 0.4089 0.4620 -0.0374 0.1405  -0.0068 216 LEU C C   
10036 O O   . LEU C  216 ? 0.5854 0.4877 0.5391 -0.0396 0.1424  -0.0052 216 LEU C O   
10037 C CB  . LEU C  216 ? 0.4086 0.2883 0.3616 -0.0417 0.1502  -0.0140 216 LEU C CB  
10038 C CG  . LEU C  216 ? 0.4249 0.2944 0.3747 -0.0484 0.1563  -0.0178 216 LEU C CG  
10039 C CD1 . LEU C  216 ? 0.3778 0.2397 0.3266 -0.0533 0.1592  -0.0253 216 LEU C CD1 
10040 C CD2 . LEU C  216 ? 0.4771 0.3315 0.4217 -0.0457 0.1645  -0.0128 216 LEU C CD2 
10041 N N   . PRO C  217 ? 0.3507 0.2574 0.3072 -0.0315 0.1381  -0.0030 217 PRO C N   
10042 C CA  . PRO C  217 ? 0.3342 0.2455 0.2884 -0.0275 0.1374  0.0028  217 PRO C CA  
10043 C C   . PRO C  217 ? 0.3148 0.2395 0.2701 -0.0297 0.1317  0.0021  217 PRO C C   
10044 O O   . PRO C  217 ? 0.3327 0.2593 0.2848 -0.0285 0.1328  0.0059  217 PRO C O   
10045 C CB  . PRO C  217 ? 0.2563 0.1722 0.2122 -0.0218 0.1351  0.0055  217 PRO C CB  
10046 C CG  . PRO C  217 ? 0.2601 0.1677 0.2177 -0.0216 0.1385  0.0031  217 PRO C CG  
10047 C CD  . PRO C  217 ? 0.2582 0.1644 0.2169 -0.0281 0.1375  -0.0033 217 PRO C CD  
10048 N N   . SER C  218 ? 0.3258 0.2593 0.2850 -0.0324 0.1264  -0.0025 218 SER C N   
10049 C CA  . SER C  218 ? 0.3544 0.3000 0.3149 -0.0337 0.1219  -0.0033 218 SER C CA  
10050 C C   . SER C  218 ? 0.3849 0.3297 0.3451 -0.0386 0.1250  -0.0048 218 SER C C   
10051 O O   . SER C  218 ? 0.4096 0.3638 0.3702 -0.0390 0.1233  -0.0042 218 SER C O   
10052 C CB  . SER C  218 ? 0.3037 0.2576 0.2677 -0.0342 0.1159  -0.0071 218 SER C CB  
10053 O OG  . SER C  218 ? 0.2137 0.1700 0.1781 -0.0303 0.1130  -0.0055 218 SER C OG  
10054 N N   . ARG C  219 ? 0.3724 0.3064 0.3320 -0.0425 0.1301  -0.0070 219 ARG C N   
10055 C CA  . ARG C  219 ? 0.3871 0.3206 0.3471 -0.0485 0.1334  -0.0094 219 ARG C CA  
10056 C C   . ARG C  219 ? 0.4373 0.3709 0.3943 -0.0484 0.1369  -0.0046 219 ARG C C   
10057 O O   . ARG C  219 ? 0.4638 0.4046 0.4225 -0.0524 0.1376  -0.0054 219 ARG C O   
10058 C CB  . ARG C  219 ? 0.3835 0.3038 0.3424 -0.0532 0.1388  -0.0134 219 ARG C CB  
10059 C CG  . ARG C  219 ? 0.4165 0.3393 0.3781 -0.0559 0.1358  -0.0195 219 ARG C CG  
10060 C CD  . ARG C  219 ? 0.4922 0.4291 0.4579 -0.0597 0.1317  -0.0229 219 ARG C CD  
10061 N NE  . ARG C  219 ? 0.5602 0.4979 0.5266 -0.0661 0.1359  -0.0247 219 ARG C NE  
10062 C CZ  . ARG C  219 ? 0.5854 0.5191 0.5521 -0.0734 0.1393  -0.0304 219 ARG C CZ  
10063 N NH1 . ARG C  219 ? 0.5849 0.5124 0.5502 -0.0752 0.1395  -0.0353 219 ARG C NH1 
10064 N NH2 . ARG C  219 ? 0.5932 0.5294 0.5613 -0.0795 0.1430  -0.0315 219 ARG C NH2 
10065 N N   . SER C  220 ? 0.3800 0.3063 0.3324 -0.0439 0.1395  0.0007  220 SER C N   
10066 C CA  . SER C  220 ? 0.4088 0.3345 0.3568 -0.0435 0.1430  0.0059  220 SER C CA  
10067 C C   . SER C  220 ? 0.3914 0.3316 0.3391 -0.0400 0.1383  0.0083  220 SER C C   
10068 O O   . SER C  220 ? 0.4360 0.3765 0.3789 -0.0387 0.1409  0.0131  220 SER C O   
10069 C CB  . SER C  220 ? 0.6293 0.5396 0.5710 -0.0398 0.1487  0.0112  220 SER C CB  
10070 O OG  . SER C  220 ? 0.6970 0.6068 0.6389 -0.0337 0.1460  0.0124  220 SER C OG  
10071 N N   . LEU C  221 ? 0.3942 0.3453 0.3460 -0.0381 0.1318  0.0052  221 LEU C N   
10072 C CA  . LEU C  221 ? 0.3453 0.3093 0.2963 -0.0350 0.1279  0.0064  221 LEU C CA  
10073 C C   . LEU C  221 ? 0.3629 0.3394 0.3182 -0.0376 0.1259  0.0030  221 LEU C C   
10074 O O   . LEU C  221 ? 0.4374 0.4240 0.3915 -0.0347 0.1237  0.0037  221 LEU C O   
10075 C CB  . LEU C  221 ? 0.2989 0.2662 0.2505 -0.0304 0.1227  0.0058  221 LEU C CB  
10076 C CG  . LEU C  221 ? 0.3344 0.2915 0.2833 -0.0274 0.1246  0.0088  221 LEU C CG  
10077 C CD1 . LEU C  221 ? 0.3526 0.3150 0.3031 -0.0239 0.1195  0.0078  221 LEU C CD1 
10078 C CD2 . LEU C  221 ? 0.3724 0.3245 0.3142 -0.0248 0.1291  0.0148  221 LEU C CD2 
10079 N N   . PHE C  222 ? 0.2503 0.2262 0.2101 -0.0427 0.1271  -0.0007 222 PHE C N   
10080 C CA  . PHE C  222 ? 0.2399 0.2284 0.2044 -0.0448 0.1258  -0.0039 222 PHE C CA  
10081 C C   . PHE C  222 ? 0.2909 0.2769 0.2586 -0.0520 0.1301  -0.0065 222 PHE C C   
10082 O O   . PHE C  222 ? 0.3186 0.2923 0.2852 -0.0552 0.1328  -0.0075 222 PHE C O   
10083 C CB  . PHE C  222 ? 0.2266 0.2214 0.1944 -0.0425 0.1199  -0.0076 222 PHE C CB  
10084 C CG  . PHE C  222 ? 0.2243 0.2125 0.1946 -0.0457 0.1189  -0.0115 222 PHE C CG  
10085 C CD1 . PHE C  222 ? 0.2244 0.2021 0.1924 -0.0441 0.1184  -0.0107 222 PHE C CD1 
10086 C CD2 . PHE C  222 ? 0.2232 0.2163 0.1979 -0.0502 0.1189  -0.0160 222 PHE C CD2 
10087 C CE1 . PHE C  222 ? 0.2236 0.1954 0.1930 -0.0468 0.1180  -0.0144 222 PHE C CE1 
10088 C CE2 . PHE C  222 ? 0.2225 0.2097 0.1983 -0.0534 0.1184  -0.0199 222 PHE C CE2 
10089 C CZ  . PHE C  222 ? 0.2229 0.1991 0.1957 -0.0516 0.1180  -0.0191 222 PHE C CZ  
10090 N N   . HIS C  223 ? 0.2490 0.2463 0.2203 -0.0546 0.1315  -0.0075 223 HIS C N   
10091 C CA  . HIS C  223 ? 0.2751 0.2721 0.2503 -0.0623 0.1356  -0.0106 223 HIS C CA  
10092 C C   . HIS C  223 ? 0.2495 0.2568 0.2316 -0.0654 0.1331  -0.0166 223 HIS C C   
10093 O O   . HIS C  223 ? 0.2562 0.2634 0.2417 -0.0727 0.1362  -0.0202 223 HIS C O   
10094 C CB  . HIS C  223 ? 0.4210 0.4223 0.3957 -0.0650 0.1410  -0.0071 223 HIS C CB  
10095 C CG  . HIS C  223 ? 0.4670 0.4620 0.4343 -0.0608 0.1427  -0.0008 223 HIS C CG  
10096 N ND1 . HIS C  223 ? 0.4470 0.4492 0.4114 -0.0537 0.1393  0.0017  223 HIS C ND1 
10097 C CD2 . HIS C  223 ? 0.5280 0.5099 0.4896 -0.0626 0.1479  0.0033  223 HIS C CD2 
10098 C CE1 . HIS C  223 ? 0.4897 0.4844 0.4468 -0.0517 0.1420  0.0069  223 HIS C CE1 
10099 N NE2 . HIS C  223 ? 0.5367 0.5188 0.4920 -0.0567 0.1472  0.0084  223 HIS C NE2 
10100 N N   . ARG C  224 ? 0.3866 0.4022 0.3702 -0.0602 0.1278  -0.0179 224 ARG C N   
10101 C CA  . ARG C  224 ? 0.3993 0.4264 0.3891 -0.0625 0.1261  -0.0230 224 ARG C CA  
10102 C C   . ARG C  224 ? 0.3837 0.4129 0.3730 -0.0574 0.1203  -0.0247 224 ARG C C   
10103 O O   . ARG C  224 ? 0.3983 0.4252 0.3837 -0.0511 0.1175  -0.0217 224 ARG C O   
10104 C CB  . ARG C  224 ? 0.4167 0.4589 0.4107 -0.0619 0.1283  -0.0223 224 ARG C CB  
10105 C CG  . ARG C  224 ? 0.4636 0.5154 0.4649 -0.0691 0.1308  -0.0270 224 ARG C CG  
10106 C CD  . ARG C  224 ? 0.4859 0.5385 0.4884 -0.0745 0.1370  -0.0247 224 ARG C CD  
10107 N NE  . ARG C  224 ? 0.4809 0.5413 0.4821 -0.0689 0.1385  -0.0200 224 ARG C NE  
10108 C CZ  . ARG C  224 ? 0.5000 0.5648 0.5023 -0.0722 0.1441  -0.0171 224 ARG C CZ  
10109 N NH1 . ARG C  224 ? 0.4952 0.5567 0.5004 -0.0815 0.1486  -0.0185 224 ARG C NH1 
10110 N NH2 . ARG C  224 ? 0.5363 0.6085 0.5363 -0.0665 0.1455  -0.0131 224 ARG C NH2 
10111 N N   . ALA C  225 ? 0.2171 0.2516 0.2104 -0.0604 0.1186  -0.0298 225 ALA C N   
10112 C CA  . ALA C  225 ? 0.2079 0.2422 0.1996 -0.0560 0.1136  -0.0310 225 ALA C CA  
10113 C C   . ALA C  225 ? 0.2035 0.2510 0.1998 -0.0558 0.1117  -0.0354 225 ALA C C   
10114 O O   . ALA C  225 ? 0.2069 0.2613 0.2080 -0.0619 0.1134  -0.0397 225 ALA C O   
10115 C CB  . ALA C  225 ? 0.3056 0.3267 0.2939 -0.0583 0.1126  -0.0321 225 ALA C CB  
10116 N N   . VAL C  226 ? 0.1970 0.2481 0.1916 -0.0490 0.1085  -0.0346 226 VAL C N   
10117 C CA  . VAL C  226 ? 0.2178 0.2791 0.2151 -0.0476 0.1063  -0.0387 226 VAL C CA  
10118 C C   . VAL C  226 ? 0.2099 0.2637 0.2022 -0.0448 0.1024  -0.0389 226 VAL C C   
10119 O O   . VAL C  226 ? 0.2011 0.2483 0.1887 -0.0396 0.1004  -0.0358 226 VAL C O   
10120 C CB  . VAL C  226 ? 0.2934 0.3678 0.2935 -0.0420 0.1070  -0.0391 226 VAL C CB  
10121 C CG1 . VAL C  226 ? 0.2927 0.3753 0.2940 -0.0385 0.1044  -0.0431 226 VAL C CG1 
10122 C CG2 . VAL C  226 ? 0.2887 0.3744 0.2957 -0.0462 0.1111  -0.0404 226 VAL C CG2 
10123 N N   . LEU C  227 ? 0.1884 0.2444 0.1819 -0.0490 0.1015  -0.0430 227 LEU C N   
10124 C CA  . LEU C  227 ? 0.1888 0.2393 0.1775 -0.0473 0.0984  -0.0436 227 LEU C CA  
10125 C C   . LEU C  227 ? 0.1848 0.2478 0.1748 -0.0451 0.0971  -0.0477 227 LEU C C   
10126 O O   . LEU C  227 ? 0.1868 0.2606 0.1809 -0.0496 0.0977  -0.0525 227 LEU C O   
10127 C CB  . LEU C  227 ? 0.1881 0.2294 0.1746 -0.0534 0.0987  -0.0448 227 LEU C CB  
10128 C CG  . LEU C  227 ? 0.1900 0.2176 0.1742 -0.0547 0.1000  -0.0415 227 LEU C CG  
10129 C CD1 . LEU C  227 ? 0.1957 0.2243 0.1834 -0.0592 0.1038  -0.0421 227 LEU C CD1 
10130 C CD2 . LEU C  227 ? 0.1919 0.2096 0.1722 -0.0578 0.0996  -0.0427 227 LEU C CD2 
10131 N N   . GLN C  228 ? 0.1845 0.2466 0.1707 -0.0380 0.0954  -0.0465 228 GLN C N   
10132 C CA  . GLN C  228 ? 0.2233 0.2959 0.2093 -0.0340 0.0942  -0.0506 228 GLN C CA  
10133 C C   . GLN C  228 ? 0.2236 0.2872 0.2013 -0.0332 0.0920  -0.0507 228 GLN C C   
10134 O O   . GLN C  228 ? 0.2164 0.2673 0.1879 -0.0306 0.0909  -0.0472 228 GLN C O   
10135 C CB  . GLN C  228 ? 0.3380 0.4154 0.3241 -0.0258 0.0945  -0.0505 228 GLN C CB  
10136 C CG  . GLN C  228 ? 0.3786 0.4628 0.3709 -0.0260 0.0972  -0.0492 228 GLN C CG  
10137 C CD  . GLN C  228 ? 0.3783 0.4639 0.3684 -0.0175 0.0976  -0.0485 228 GLN C CD  
10138 O OE1 . GLN C  228 ? 0.3605 0.4491 0.3530 -0.0168 0.1001  -0.0464 228 GLN C OE1 
10139 N NE2 . GLN C  228 ? 0.3565 0.4387 0.3406 -0.0111 0.0955  -0.0505 228 GLN C NE2 
10140 N N   . SER C  229 ? 0.1897 0.2607 0.1667 -0.0361 0.0913  -0.0548 229 SER C N   
10141 C CA  . SER C  229 ? 0.1907 0.2546 0.1581 -0.0356 0.0895  -0.0552 229 SER C CA  
10142 C C   . SER C  229 ? 0.1899 0.2356 0.1518 -0.0382 0.0893  -0.0501 229 SER C C   
10143 O O   . SER C  229 ? 0.1922 0.2282 0.1462 -0.0353 0.0882  -0.0481 229 SER C O   
10144 C CB  . SER C  229 ? 0.2654 0.3305 0.2266 -0.0272 0.0881  -0.0569 229 SER C CB  
10145 O OG  . SER C  229 ? 0.2925 0.3756 0.2611 -0.0222 0.0880  -0.0614 229 SER C OG  
10146 N N   . GLY C  230 ? 0.2444 0.2857 0.2105 -0.0434 0.0903  -0.0485 230 GLY C N   
10147 C CA  . GLY C  230 ? 0.1869 0.2139 0.1497 -0.0452 0.0900  -0.0446 230 GLY C CA  
10148 C C   . GLY C  230 ? 0.1871 0.2113 0.1542 -0.0505 0.0917  -0.0449 230 GLY C C   
10149 O O   . GLY C  230 ? 0.1878 0.2199 0.1603 -0.0529 0.0933  -0.0473 230 GLY C O   
10150 N N   . THR C  231 ? 0.1876 0.2005 0.1522 -0.0520 0.0917  -0.0426 231 THR C N   
10151 C CA  . THR C  231 ? 0.1918 0.1998 0.1577 -0.0571 0.0938  -0.0443 231 THR C CA  
10152 C C   . THR C  231 ? 0.1912 0.1874 0.1542 -0.0560 0.0937  -0.0412 231 THR C C   
10153 O O   . THR C  231 ? 0.2534 0.2469 0.2123 -0.0542 0.0921  -0.0396 231 THR C O   
10154 C CB  . THR C  231 ? 0.3486 0.3612 0.3120 -0.0629 0.0947  -0.0495 231 THR C CB  
10155 O OG1 . THR C  231 ? 0.3303 0.3452 0.2878 -0.0610 0.0927  -0.0495 231 THR C OG1 
10156 C CG2 . THR C  231 ? 0.1991 0.2239 0.1676 -0.0671 0.0962  -0.0543 231 THR C CG2 
10157 N N   . PRO C  232 ? 0.2933 0.2828 0.2583 -0.0572 0.0958  -0.0407 232 PRO C N   
10158 C CA  . PRO C  232 ? 0.1940 0.1739 0.1571 -0.0558 0.0964  -0.0384 232 PRO C CA  
10159 C C   . PRO C  232 ? 0.1998 0.1760 0.1587 -0.0595 0.0976  -0.0414 232 PRO C C   
10160 O O   . PRO C  232 ? 0.2002 0.1710 0.1572 -0.0578 0.0977  -0.0395 232 PRO C O   
10161 C CB  . PRO C  232 ? 0.1970 0.1718 0.1627 -0.0562 0.0994  -0.0380 232 PRO C CB  
10162 C CG  . PRO C  232 ? 0.3163 0.2951 0.2833 -0.0614 0.1016  -0.0422 232 PRO C CG  
10163 C CD  . PRO C  232 ? 0.3216 0.3121 0.2899 -0.0606 0.0988  -0.0429 232 PRO C CD  
10164 N N   . ASN C  233 ? 0.2049 0.1849 0.1624 -0.0648 0.0989  -0.0462 233 ASN C N   
10165 C CA  . ASN C  233 ? 0.2920 0.2693 0.2440 -0.0685 0.1000  -0.0493 233 ASN C CA  
10166 C C   . ASN C  233 ? 0.3640 0.3472 0.3116 -0.0672 0.0971  -0.0485 233 ASN C C   
10167 O O   . ASN C  233 ? 0.3916 0.3805 0.3409 -0.0637 0.0947  -0.0462 233 ASN C O   
10168 C CB  . ASN C  233 ? 0.3315 0.3101 0.2828 -0.0760 0.1032  -0.0558 233 ASN C CB  
10169 C CG  . ASN C  233 ? 0.3526 0.3431 0.3076 -0.0785 0.1024  -0.0586 233 ASN C CG  
10170 O OD1 . ASN C  233 ? 0.3382 0.3332 0.2977 -0.0742 0.1007  -0.0553 233 ASN C OD1 
10171 N ND2 . ASN C  233 ? 0.3875 0.3845 0.3406 -0.0855 0.1037  -0.0649 233 ASN C ND2 
10172 N N   . GLY C  234 ? 0.5015 0.4829 0.4426 -0.0700 0.0977  -0.0504 234 GLY C N   
10173 C CA  . GLY C  234 ? 0.4958 0.4814 0.4302 -0.0691 0.0954  -0.0495 234 GLY C CA  
10174 C C   . GLY C  234 ? 0.4692 0.4487 0.4003 -0.0653 0.0944  -0.0445 234 GLY C C   
10175 O O   . GLY C  234 ? 0.5308 0.5046 0.4661 -0.0629 0.0952  -0.0418 234 GLY C O   
10176 N N   . PRO C  235 ? 0.2337 0.2147 0.1566 -0.0649 0.0930  -0.0434 235 PRO C N   
10177 C CA  . PRO C  235 ? 0.2252 0.2003 0.1425 -0.0634 0.0928  -0.0394 235 PRO C CA  
10178 C C   . PRO C  235 ? 0.2181 0.1896 0.1403 -0.0596 0.0920  -0.0348 235 PRO C C   
10179 O O   . PRO C  235 ? 0.2186 0.1858 0.1415 -0.0592 0.0931  -0.0326 235 PRO C O   
10180 C CB  . PRO C  235 ? 0.2331 0.2109 0.1392 -0.0638 0.0912  -0.0394 235 PRO C CB  
10181 C CG  . PRO C  235 ? 0.2297 0.2157 0.1386 -0.0629 0.0898  -0.0421 235 PRO C CG  
10182 C CD  . PRO C  235 ? 0.2250 0.2144 0.1434 -0.0654 0.0913  -0.0458 235 PRO C CD  
10183 N N   . TRP C  236 ? 0.2126 0.1868 0.1378 -0.0570 0.0904  -0.0338 236 TRP C N   
10184 C CA  . TRP C  236 ? 0.2084 0.1791 0.1358 -0.0543 0.0896  -0.0299 236 TRP C CA  
10185 C C   . TRP C  236 ? 0.2698 0.2408 0.2067 -0.0518 0.0894  -0.0289 236 TRP C C   
10186 O O   . TRP C  236 ? 0.1975 0.1660 0.1357 -0.0503 0.0889  -0.0261 236 TRP C O   
10187 C CB  . TRP C  236 ? 0.2290 0.2007 0.1512 -0.0526 0.0884  -0.0295 236 TRP C CB  
10188 C CG  . TRP C  236 ? 0.2067 0.1861 0.1330 -0.0513 0.0879  -0.0327 236 TRP C CG  
10189 C CD1 . TRP C  236 ? 0.2325 0.2186 0.1557 -0.0526 0.0879  -0.0364 236 TRP C CD1 
10190 C CD2 . TRP C  236 ? 0.2402 0.2227 0.1746 -0.0485 0.0875  -0.0327 236 TRP C CD2 
10191 N NE1 . TRP C  236 ? 0.2337 0.2277 0.1640 -0.0510 0.0878  -0.0388 236 TRP C NE1 
10192 C CE2 . TRP C  236 ? 0.2422 0.2335 0.1789 -0.0484 0.0876  -0.0362 236 TRP C CE2 
10193 C CE3 . TRP C  236 ? 0.1935 0.1730 0.1328 -0.0464 0.0872  -0.0302 236 TRP C CE3 
10194 C CZ2 . TRP C  236 ? 0.2620 0.2586 0.2058 -0.0460 0.0876  -0.0368 236 TRP C CZ2 
10195 C CZ3 . TRP C  236 ? 0.2743 0.2583 0.2192 -0.0439 0.0869  -0.0307 236 TRP C CZ3 
10196 C CH2 . TRP C  236 ? 0.2811 0.2732 0.2282 -0.0436 0.0872  -0.0338 236 TRP C CH2 
10197 N N   . ALA C  237 ? 0.1968 0.1702 0.1391 -0.0519 0.0900  -0.0310 237 ALA C N   
10198 C CA  . ALA C  237 ? 0.1905 0.1642 0.1395 -0.0492 0.0896  -0.0295 237 ALA C CA  
10199 C C   . ALA C  237 ? 0.2409 0.2110 0.1935 -0.0479 0.0908  -0.0276 237 ALA C C   
10200 O O   . ALA C  237 ? 0.2264 0.1969 0.1829 -0.0453 0.0903  -0.0255 237 ALA C O   
10201 C CB  . ALA C  237 ? 0.1890 0.1666 0.1416 -0.0496 0.0901  -0.0318 237 ALA C CB  
10202 N N   . THR C  238 ? 0.2808 0.2479 0.2316 -0.0496 0.0927  -0.0284 238 THR C N   
10203 C CA  . THR C  238 ? 0.2485 0.2133 0.2027 -0.0480 0.0945  -0.0269 238 THR C CA  
10204 C C   . THR C  238 ? 0.2412 0.2049 0.1927 -0.0489 0.0959  -0.0261 238 THR C C   
10205 O O   . THR C  238 ? 0.2394 0.2029 0.1852 -0.0513 0.0955  -0.0268 238 THR C O   
10206 C CB  . THR C  238 ? 0.3574 0.3188 0.3137 -0.0485 0.0975  -0.0290 238 THR C CB  
10207 O OG1 . THR C  238 ? 0.3307 0.2896 0.2827 -0.0522 0.0996  -0.0327 238 THR C OG1 
10208 C CG2 . THR C  238 ? 0.3967 0.3594 0.3556 -0.0480 0.0968  -0.0295 238 THR C CG2 
10209 N N   . VAL C  239 ? 0.1981 0.1618 0.1532 -0.0470 0.0977  -0.0243 239 VAL C N   
10210 C CA  . VAL C  239 ? 0.2700 0.2339 0.2232 -0.0479 0.0998  -0.0237 239 VAL C CA  
10211 C C   . VAL C  239 ? 0.2794 0.2419 0.2356 -0.0464 0.1039  -0.0242 239 VAL C C   
10212 O O   . VAL C  239 ? 0.2260 0.1884 0.1872 -0.0438 0.1048  -0.0233 239 VAL C O   
10213 C CB  . VAL C  239 ? 0.2011 0.1686 0.1554 -0.0477 0.0986  -0.0202 239 VAL C CB  
10214 C CG1 . VAL C  239 ? 0.2108 0.1769 0.1587 -0.0502 0.0965  -0.0200 239 VAL C CG1 
10215 C CG2 . VAL C  239 ? 0.1946 0.1652 0.1550 -0.0451 0.0974  -0.0178 239 VAL C CG2 
10216 N N   . SER C  240 ? 0.3501 0.3112 0.3024 -0.0482 0.1067  -0.0257 240 SER C N   
10217 C CA  . SER C  240 ? 0.4128 0.3728 0.3671 -0.0468 0.1115  -0.0264 240 SER C CA  
10218 C C   . SER C  240 ? 0.3549 0.3206 0.3163 -0.0433 0.1119  -0.0226 240 SER C C   
10219 O O   . SER C  240 ? 0.4211 0.3921 0.3839 -0.0436 0.1094  -0.0197 240 SER C O   
10220 C CB  . SER C  240 ? 0.8665 0.8269 0.8153 -0.0489 0.1140  -0.0274 240 SER C CB  
10221 O OG  . SER C  240 ? 0.9659 0.9300 0.9184 -0.0467 0.1179  -0.0257 240 SER C OG  
10222 N N   . ALA C  241 ? 0.3367 0.3012 0.3023 -0.0404 0.1155  -0.0225 241 ALA C N   
10223 C CA  . ALA C  241 ? 0.3670 0.3385 0.3397 -0.0371 0.1161  -0.0188 241 ALA C CA  
10224 C C   . ALA C  241 ? 0.2156 0.1948 0.1900 -0.0376 0.1175  -0.0170 241 ALA C C   
10225 O O   . ALA C  241 ? 0.3090 0.2960 0.2880 -0.0374 0.1160  -0.0137 241 ALA C O   
10226 C CB  . ALA C  241 ? 0.2312 0.1995 0.2074 -0.0334 0.1207  -0.0190 241 ALA C CB  
10227 N N   . GLY C  242 ? 0.3204 0.2975 0.2906 -0.0390 0.1209  -0.0191 242 GLY C N   
10228 C CA  . GLY C  242 ? 0.3634 0.3479 0.3342 -0.0401 0.1228  -0.0173 242 GLY C CA  
10229 C C   . GLY C  242 ? 0.3751 0.3627 0.3443 -0.0434 0.1184  -0.0148 242 GLY C C   
10230 O O   . GLY C  242 ? 0.4389 0.4346 0.4125 -0.0441 0.1189  -0.0116 242 GLY C O   
10231 N N   . GLU C  243 ? 0.2752 0.2562 0.2380 -0.0457 0.1147  -0.0164 243 GLU C N   
10232 C CA  . GLU C  243 ? 0.2577 0.2390 0.2173 -0.0487 0.1111  -0.0144 243 GLU C CA  
10233 C C   . GLU C  243 ? 0.2778 0.2624 0.2430 -0.0480 0.1079  -0.0120 243 GLU C C   
10234 O O   . GLU C  243 ? 0.2604 0.2479 0.2263 -0.0504 0.1069  -0.0093 243 GLU C O   
10235 C CB  . GLU C  243 ? 0.2510 0.2252 0.2025 -0.0507 0.1086  -0.0170 243 GLU C CB  
10236 C CG  . GLU C  243 ? 0.2781 0.2510 0.2254 -0.0534 0.1052  -0.0151 243 GLU C CG  
10237 C CD  . GLU C  243 ? 0.3427 0.3153 0.2835 -0.0567 0.1070  -0.0135 243 GLU C CD  
10238 O OE1 . GLU C  243 ? 0.3650 0.3413 0.3070 -0.0568 0.1108  -0.0127 243 GLU C OE1 
10239 O OE2 . GLU C  243 ? 0.3493 0.3176 0.2830 -0.0592 0.1048  -0.0127 243 GLU C OE2 
10240 N N   . ALA C  244 ? 0.3659 0.3492 0.3344 -0.0451 0.1067  -0.0129 244 ALA C N   
10241 C CA  . ALA C  244 ? 0.3718 0.3589 0.3455 -0.0441 0.1045  -0.0106 244 ALA C CA  
10242 C C   . ALA C  244 ? 0.3777 0.3739 0.3580 -0.0444 0.1068  -0.0076 244 ALA C C   
10243 O O   . ALA C  244 ? 0.4013 0.4011 0.3836 -0.0468 0.1052  -0.0054 244 ALA C O   
10244 C CB  . ALA C  244 ? 0.3144 0.2998 0.2909 -0.0405 0.1044  -0.0115 244 ALA C CB  
10245 N N   . ARG C  245 ? 0.2800 0.2800 0.2633 -0.0425 0.1111  -0.0077 245 ARG C N   
10246 C CA  . ARG C  245 ? 0.2707 0.2816 0.2613 -0.0427 0.1141  -0.0049 245 ARG C CA  
10247 C C   . ARG C  245 ? 0.3115 0.3247 0.3001 -0.0476 0.1140  -0.0031 245 ARG C C   
10248 O O   . ARG C  245 ? 0.3259 0.3471 0.3203 -0.0501 0.1142  -0.0002 245 ARG C O   
10249 C CB  . ARG C  245 ? 0.2578 0.2719 0.2514 -0.0393 0.1195  -0.0059 245 ARG C CB  
10250 C CG  . ARG C  245 ? 0.2743 0.3018 0.2759 -0.0395 0.1235  -0.0032 245 ARG C CG  
10251 C CD  . ARG C  245 ? 0.3039 0.3352 0.3098 -0.0345 0.1292  -0.0044 245 ARG C CD  
10252 N NE  . ARG C  245 ? 0.3127 0.3445 0.3235 -0.0300 0.1293  -0.0042 245 ARG C NE  
10253 C CZ  . ARG C  245 ? 0.3612 0.4053 0.3815 -0.0284 0.1301  -0.0015 245 ARG C CZ  
10254 N NH1 . ARG C  245 ? 0.3844 0.4416 0.4111 -0.0316 0.1307  0.0011  245 ARG C NH1 
10255 N NH2 . ARG C  245 ? 0.3721 0.4157 0.3959 -0.0240 0.1306  -0.0011 245 ARG C NH2 
10256 N N   . ARG C  246 ? 0.3922 0.3982 0.3722 -0.0495 0.1140  -0.0048 246 ARG C N   
10257 C CA  . ARG C  246 ? 0.4162 0.4227 0.3923 -0.0542 0.1148  -0.0029 246 ARG C CA  
10258 C C   . ARG C  246 ? 0.4348 0.4398 0.4108 -0.0579 0.1112  -0.0008 246 ARG C C   
10259 O O   . ARG C  246 ? 0.4472 0.4583 0.4276 -0.0615 0.1123  0.0023  246 ARG C O   
10260 C CB  . ARG C  246 ? 0.3825 0.3801 0.3478 -0.0553 0.1148  -0.0053 246 ARG C CB  
10261 C CG  . ARG C  246 ? 0.4212 0.4204 0.3819 -0.0587 0.1180  -0.0036 246 ARG C CG  
10262 C CD  . ARG C  246 ? 0.4260 0.4201 0.3801 -0.0636 0.1157  -0.0012 246 ARG C CD  
10263 N NE  . ARG C  246 ? 0.4540 0.4382 0.3995 -0.0636 0.1121  -0.0035 246 ARG C NE  
10264 C CZ  . ARG C  246 ? 0.5501 0.5275 0.4879 -0.0671 0.1098  -0.0020 246 ARG C CZ  
10265 N NH1 . ARG C  246 ? 0.6134 0.5916 0.5508 -0.0714 0.1108  0.0019  246 ARG C NH1 
10266 N NH2 . ARG C  246 ? 0.5513 0.5211 0.4817 -0.0665 0.1069  -0.0041 246 ARG C NH2 
10267 N N   . ARG C  247 ? 0.2151 0.2120 0.1862 -0.0573 0.1073  -0.0027 247 ARG C N   
10268 C CA  . ARG C  247 ? 0.2153 0.2075 0.1832 -0.0608 0.1042  -0.0017 247 ARG C CA  
10269 C C   . ARG C  247 ? 0.2109 0.2101 0.1876 -0.0615 0.1037  0.0001  247 ARG C C   
10270 O O   . ARG C  247 ? 0.2147 0.2141 0.1919 -0.0664 0.1032  0.0020  247 ARG C O   
10271 C CB  . ARG C  247 ? 0.4873 0.4710 0.4489 -0.0591 0.1010  -0.0045 247 ARG C CB  
10272 C CG  . ARG C  247 ? 0.2162 0.1943 0.1698 -0.0586 0.1014  -0.0066 247 ARG C CG  
10273 C CD  . ARG C  247 ? 0.2139 0.1854 0.1621 -0.0579 0.0984  -0.0087 247 ARG C CD  
10274 N NE  . ARG C  247 ? 0.2183 0.1856 0.1592 -0.0580 0.0987  -0.0109 247 ARG C NE  
10275 C CZ  . ARG C  247 ? 0.2175 0.1805 0.1534 -0.0576 0.0966  -0.0129 247 ARG C CZ  
10276 N NH1 . ARG C  247 ? 0.2127 0.1744 0.1499 -0.0567 0.0943  -0.0130 247 ARG C NH1 
10277 N NH2 . ARG C  247 ? 0.2225 0.1832 0.1519 -0.0583 0.0972  -0.0149 247 ARG C NH2 
10278 N N   . ALA C  248 ? 0.2945 0.2990 0.2776 -0.0570 0.1041  -0.0006 248 ALA C N   
10279 C CA  . ALA C  248 ? 0.2606 0.2732 0.2523 -0.0576 0.1040  0.0011  248 ALA C CA  
10280 C C   . ALA C  248 ? 0.2145 0.2378 0.2138 -0.0614 0.1069  0.0042  248 ALA C C   
10281 O O   . ALA C  248 ? 0.2061 0.2336 0.2101 -0.0661 0.1061  0.0057  248 ALA C O   
10282 C CB  . ALA C  248 ? 0.1949 0.2114 0.1914 -0.0517 0.1047  0.0003  248 ALA C CB  
10283 N N   . THR C  249 ? 0.2089 0.2366 0.2094 -0.0602 0.1105  0.0048  249 THR C N   
10284 C CA  . THR C  249 ? 0.2496 0.2887 0.2579 -0.0636 0.1139  0.0078  249 THR C CA  
10285 C C   . THR C  249 ? 0.2824 0.3167 0.2861 -0.0709 0.1131  0.0096  249 THR C C   
10286 O O   . THR C  249 ? 0.2732 0.3148 0.2839 -0.0762 0.1137  0.0121  249 THR C O   
10287 C CB  . THR C  249 ? 0.2174 0.2624 0.2272 -0.0604 0.1187  0.0078  249 THR C CB  
10288 O OG1 . THR C  249 ? 0.2199 0.2658 0.2317 -0.0537 0.1197  0.0057  249 THR C OG1 
10289 C CG2 . THR C  249 ? 0.2211 0.2814 0.2417 -0.0632 0.1226  0.0112  249 THR C CG2 
10290 N N   . LEU C  250 ? 0.3997 0.4220 0.3918 -0.0716 0.1119  0.0084  250 LEU C N   
10291 C CA  . LEU C  250 ? 0.4145 0.4300 0.4002 -0.0783 0.1113  0.0104  250 LEU C CA  
10292 C C   . LEU C  250 ? 0.4282 0.4396 0.4146 -0.0828 0.1077  0.0106  250 LEU C C   
10293 O O   . LEU C  250 ? 0.4809 0.4918 0.4681 -0.0897 0.1078  0.0130  250 LEU C O   
10294 C CB  . LEU C  250 ? 0.3378 0.3408 0.3101 -0.0776 0.1105  0.0089  250 LEU C CB  
10295 C CG  . LEU C  250 ? 0.2497 0.2412 0.2121 -0.0835 0.1086  0.0106  250 LEU C CG  
10296 C CD1 . LEU C  250 ? 0.2603 0.2558 0.2249 -0.0897 0.1116  0.0147  250 LEU C CD1 
10297 C CD2 . LEU C  250 ? 0.2540 0.2351 0.2037 -0.0817 0.1080  0.0091  250 LEU C CD2 
10298 N N   . LEU C  251 ? 0.2477 0.2558 0.2336 -0.0793 0.1047  0.0079  251 LEU C N   
10299 C CA  . LEU C  251 ? 0.2356 0.2393 0.2212 -0.0837 0.1016  0.0074  251 LEU C CA  
10300 C C   . LEU C  251 ? 0.2268 0.2434 0.2249 -0.0877 0.1025  0.0091  251 LEU C C   
10301 O O   . LEU C  251 ? 0.2342 0.2486 0.2328 -0.0954 0.1012  0.0101  251 LEU C O   
10302 C CB  . LEU C  251 ? 0.2366 0.2350 0.2188 -0.0790 0.0989  0.0042  251 LEU C CB  
10303 C CG  . LEU C  251 ? 0.2224 0.2160 0.2032 -0.0842 0.0963  0.0034  251 LEU C CG  
10304 C CD1 . LEU C  251 ? 0.2278 0.2059 0.1957 -0.0844 0.0940  0.0015  251 LEU C CD1 
10305 C CD2 . LEU C  251 ? 0.2142 0.2163 0.2027 -0.0816 0.0959  0.0021  251 LEU C CD2 
10306 N N   . ALA C  252 ? 0.3141 0.3440 0.3224 -0.0829 0.1048  0.0094  252 ALA C N   
10307 C CA  . ALA C  252 ? 0.3250 0.3700 0.3469 -0.0866 0.1062  0.0112  252 ALA C CA  
10308 C C   . ALA C  252 ? 0.3545 0.4034 0.3797 -0.0939 0.1081  0.0141  252 ALA C C   
10309 O O   . ALA C  252 ? 0.3681 0.4229 0.4006 -0.1012 0.1071  0.0149  252 ALA C O   
10310 C CB  . ALA C  252 ? 0.2735 0.3325 0.3053 -0.0795 0.1093  0.0117  252 ALA C CB  
10311 N N   . ARG C  253 ? 0.2645 0.3101 0.2841 -0.0926 0.1109  0.0156  253 ARG C N   
10312 C CA  . ARG C  253 ? 0.3027 0.3496 0.3230 -0.0996 0.1132  0.0187  253 ARG C CA  
10313 C C   . ARG C  253 ? 0.2544 0.2884 0.2676 -0.1079 0.1095  0.0189  253 ARG C C   
10314 O O   . ARG C  253 ? 0.2601 0.2995 0.2808 -0.1156 0.1089  0.0202  253 ARG C O   
10315 C CB  . ARG C  253 ? 0.7498 0.7925 0.7619 -0.0966 0.1165  0.0197  253 ARG C CB  
10316 C CG  . ARG C  253 ? 0.9448 0.9985 0.9635 -0.1006 0.1218  0.0234  253 ARG C CG  
10317 C CD  . ARG C  253 ? 1.1153 1.1619 1.1227 -0.0998 0.1249  0.0245  253 ARG C CD  
10318 N NE  . ARG C  253 ? 1.2409 1.2748 1.2384 -0.1071 0.1237  0.0267  253 ARG C NE  
10319 C CZ  . ARG C  253 ? 1.3042 1.3419 1.3053 -0.1147 0.1264  0.0306  253 ARG C CZ  
10320 N NH1 . ARG C  253 ? 1.3061 1.3616 1.3217 -0.1160 0.1307  0.0325  253 ARG C NH1 
10321 N NH2 . ARG C  253 ? 1.3184 1.3422 1.3089 -0.1211 0.1252  0.0328  253 ARG C NH2 
10322 N N   . LEU C  254 ? 0.2567 0.2737 0.2555 -0.1066 0.1068  0.0173  254 LEU C N   
10323 C CA  . LEU C  254 ? 0.2676 0.2696 0.2573 -0.1137 0.1034  0.0176  254 LEU C CA  
10324 C C   . LEU C  254 ? 0.3719 0.3748 0.3672 -0.1196 0.0998  0.0160  254 LEU C C   
10325 O O   . LEU C  254 ? 0.3807 0.3745 0.3722 -0.1279 0.0976  0.0169  254 LEU C O   
10326 C CB  . LEU C  254 ? 0.2681 0.2534 0.2426 -0.1095 0.1011  0.0156  254 LEU C CB  
10327 C CG  . LEU C  254 ? 0.2699 0.2533 0.2375 -0.1052 0.1040  0.0167  254 LEU C CG  
10328 C CD1 . LEU C  254 ? 0.4124 0.3822 0.3670 -0.1008 0.1016  0.0144  254 LEU C CD1 
10329 C CD2 . LEU C  254 ? 0.2850 0.2649 0.2489 -0.1119 0.1062  0.0209  254 LEU C CD2 
10330 N N   . VAL C  255 ? 0.2563 0.2694 0.2600 -0.1159 0.0990  0.0135  255 VAL C N   
10331 C CA  . VAL C  255 ? 0.2775 0.2931 0.2867 -0.1221 0.0954  0.0115  255 VAL C CA  
10332 C C   . VAL C  255 ? 0.3040 0.3389 0.3300 -0.1274 0.0968  0.0130  255 VAL C C   
10333 O O   . VAL C  255 ? 0.2850 0.3276 0.3187 -0.1319 0.0937  0.0108  255 VAL C O   
10334 C CB  . VAL C  255 ? 0.3086 0.3233 0.3162 -0.1170 0.0931  0.0077  255 VAL C CB  
10335 C CG1 . VAL C  255 ? 0.3218 0.3169 0.3132 -0.1139 0.0912  0.0059  255 VAL C CG1 
10336 C CG2 . VAL C  255 ? 0.2959 0.3259 0.3129 -0.1082 0.0963  0.0079  255 VAL C CG2 
10337 N N   . GLY C  256 ? 0.4041 0.4485 0.4364 -0.1267 0.1014  0.0164  256 GLY C N   
10338 C CA  . GLY C  256 ? 0.4299 0.4937 0.4790 -0.1318 0.1034  0.0182  256 GLY C CA  
10339 C C   . GLY C  256 ? 0.4237 0.5074 0.4868 -0.1255 0.1050  0.0173  256 GLY C C   
10340 O O   . GLY C  256 ? 0.4277 0.5255 0.5035 -0.1300 0.1030  0.0161  256 GLY C O   
10341 N N   . CYS C  257 ? 0.3470 0.4318 0.4076 -0.1150 0.1084  0.0178  257 CYS C N   
10342 C CA  . CYS C  257 ? 0.3852 0.4868 0.4576 -0.1075 0.1106  0.0176  257 CYS C CA  
10343 C C   . CYS C  257 ? 0.5085 0.6201 0.5859 -0.1008 0.1168  0.0204  257 CYS C C   
10344 O O   . CYS C  257 ? 0.4419 0.5530 0.5162 -0.0913 0.1186  0.0198  257 CYS C O   
10345 C CB  . CYS C  257 ? 0.4138 0.5065 0.4780 -0.1003 0.1083  0.0147  257 CYS C CB  
10346 S SG  . CYS C  257 ? 0.6651 0.7638 0.7350 -0.1047 0.1034  0.0115  257 CYS C SG  
10347 N N   . PRO C  258 ? 0.9860 1.1065 1.0706 -0.1058 0.1203  0.0232  258 PRO C N   
10348 C CA  . PRO C  258 ? 1.0585 1.1945 1.1522 -0.0977 0.1260  0.0249  258 PRO C CA  
10349 C C   . PRO C  258 ? 1.7151 1.8704 1.8258 -0.0951 0.1257  0.0242  258 PRO C C   
10350 O O   . PRO C  258 ? 1.7175 1.8777 1.8296 -0.0853 0.1278  0.0239  258 PRO C O   
10351 C CB  . PRO C  258 ? 1.2304 1.3730 1.3282 -0.1025 0.1309  0.0283  258 PRO C CB  
10352 C CG  . PRO C  258 ? 1.2503 1.3736 1.3342 -0.1107 0.1278  0.0284  258 PRO C CG  
10353 C CD  . PRO C  258 ? 1.1932 1.3076 1.2740 -0.1147 0.1210  0.0254  258 PRO C CD  
10354 N N   . PRO C  259 ? 1.6223 1.7881 1.7449 -0.1037 0.1226  0.0236  259 PRO C N   
10355 C CA  . PRO C  259 ? 1.6356 1.8052 1.7641 -0.1154 0.1222  0.0248  259 PRO C CA  
10356 C C   . PRO C  259 ? 1.6779 1.8669 1.8211 -0.1141 0.1292  0.0281  259 PRO C C   
10357 O O   . PRO C  259 ? 1.6733 1.8828 1.8327 -0.1085 0.1317  0.0283  259 PRO C O   
10358 C CB  . PRO C  259 ? 1.3288 1.5075 1.4669 -0.1228 0.1159  0.0217  259 PRO C CB  
10359 C CG  . PRO C  259 ? 1.3049 1.4740 1.4336 -0.1169 0.1122  0.0188  259 PRO C CG  
10360 C CD  . PRO C  259 ? 1.3122 1.4824 1.4392 -0.1037 0.1176  0.0204  259 PRO C CD  
10361 N N   . GLY C  260 ? 1.7295 1.9125 1.8674 -0.1190 0.1325  0.0308  260 GLY C N   
10362 C CA  . GLY C  260 ? 1.7276 1.9248 1.8743 -0.1158 0.1404  0.0342  260 GLY C CA  
10363 C C   . GLY C  260 ? 1.7321 1.9125 1.8613 -0.1163 0.1432  0.0361  260 GLY C C   
10364 O O   . GLY C  260 ? 1.7502 1.9117 1.8657 -0.1226 0.1393  0.0357  260 GLY C O   
10365 N N   . GLY C  261 ? 1.5652 1.7532 1.6951 -0.1100 0.1501  0.0382  261 GLY C N   
10366 C CA  . GLY C  261 ? 1.5517 1.7239 1.6630 -0.1074 0.1520  0.0386  261 GLY C CA  
10367 C C   . GLY C  261 ? 1.5185 1.6774 1.6161 -0.0981 0.1489  0.0351  261 GLY C C   
10368 O O   . GLY C  261 ? 1.4927 1.6316 1.5735 -0.0991 0.1454  0.0337  261 GLY C O   
10369 N N   . ALA C  262 ? 1.6094 1.7799 1.7148 -0.0893 0.1501  0.0338  262 ALA C N   
10370 C CA  . ALA C  262 ? 1.5618 1.7219 1.6553 -0.0802 0.1486  0.0303  262 ALA C CA  
10371 C C   . ALA C  262 ? 1.5523 1.7085 1.6466 -0.0769 0.1430  0.0277  262 ALA C C   
10372 O O   . ALA C  262 ? 1.5632 1.7009 1.6445 -0.0777 0.1380  0.0255  262 ALA C O   
10373 C CB  . ALA C  262 ? 1.3310 1.5042 1.4284 -0.0718 0.1551  0.0298  262 ALA C CB  
10374 N N   . GLY C  263 ? 1.4781 1.6522 1.5879 -0.0731 0.1442  0.0282  263 GLY C N   
10375 C CA  . GLY C  263 ? 1.4498 1.6218 1.5598 -0.0681 0.1403  0.0258  263 GLY C CA  
10376 C C   . GLY C  263 ? 1.4155 1.5808 1.5161 -0.0581 0.1415  0.0227  263 GLY C C   
10377 O O   . GLY C  263 ? 1.3896 1.5378 1.4782 -0.0562 0.1375  0.0200  263 GLY C O   
10378 N N   . GLY C  264 ? 1.5382 1.7172 1.6449 -0.0520 0.1473  0.0225  264 GLY C N   
10379 C CA  . GLY C  264 ? 1.4959 1.6681 1.5943 -0.0435 0.1497  0.0183  264 GLY C CA  
10380 C C   . GLY C  264 ? 1.4250 1.5995 1.5271 -0.0358 0.1491  0.0155  264 GLY C C   
10381 O O   . GLY C  264 ? 1.4396 1.6137 1.5407 -0.0281 0.1531  0.0120  264 GLY C O   
10382 N N   . ASN C  265 ? 1.0840 1.2606 1.1912 -0.0378 0.1447  0.0168  265 ASN C N   
10383 C CA  . ASN C  265 ? 0.9528 1.1297 1.0627 -0.0310 0.1439  0.0146  265 ASN C CA  
10384 C C   . ASN C  265 ? 0.8024 0.9593 0.9003 -0.0334 0.1382  0.0141  265 ASN C C   
10385 O O   . ASN C  265 ? 0.8086 0.9642 0.9069 -0.0407 0.1341  0.0161  265 ASN C O   
10386 C CB  . ASN C  265 ? 1.0101 1.2134 1.1399 -0.0305 0.1443  0.0163  265 ASN C CB  
10387 C CG  . ASN C  265 ? 1.0601 1.2676 1.1961 -0.0209 0.1458  0.0132  265 ASN C CG  
10388 O OD1 . ASN C  265 ? 1.0619 1.2518 1.1884 -0.0176 0.1438  0.0125  265 ASN C OD1 
10389 N ND2 . ASN C  265 ? 1.1081 1.3376 1.2610 -0.0157 0.1498  0.0115  265 ASN C ND2 
10390 N N   . ASP C  266 ? 0.6207 0.7614 0.7086 -0.0274 0.1382  0.0114  266 ASP C N   
10391 C CA  . ASP C  266 ? 0.5179 0.6399 0.5939 -0.0290 0.1331  0.0108  266 ASP C CA  
10392 C C   . ASP C  266 ? 0.4609 0.5901 0.5436 -0.0306 0.1302  0.0124  266 ASP C C   
10393 O O   . ASP C  266 ? 0.4520 0.5715 0.5279 -0.0360 0.1256  0.0126  266 ASP C O   
10394 C CB  . ASP C  266 ? 0.5153 0.6209 0.5821 -0.0220 0.1344  0.0083  266 ASP C CB  
10395 C CG  . ASP C  266 ? 0.4825 0.5693 0.5350 -0.0246 0.1324  0.0061  266 ASP C CG  
10396 O OD1 . ASP C  266 ? 0.4995 0.5865 0.5493 -0.0301 0.1315  0.0065  266 ASP C OD1 
10397 O OD2 . ASP C  266 ? 0.4464 0.5184 0.4909 -0.0211 0.1321  0.0042  266 ASP C OD2 
10398 N N   . THR C  267 ? 0.4795 0.6257 0.5757 -0.0255 0.1331  0.0132  267 THR C N   
10399 C CA  . THR C  267 ? 0.4073 0.5635 0.5121 -0.0263 0.1309  0.0146  267 THR C CA  
10400 C C   . THR C  267 ? 0.4051 0.5705 0.5162 -0.0370 0.1276  0.0160  267 THR C C   
10401 O O   . THR C  267 ? 0.4292 0.5889 0.5372 -0.0422 0.1237  0.0155  267 THR C O   
10402 C CB  . THR C  267 ? 0.3690 0.5447 0.4907 -0.0178 0.1345  0.0155  267 THR C CB  
10403 O OG1 . THR C  267 ? 0.3588 0.5208 0.4737 -0.0070 0.1376  0.0155  267 THR C OG1 
10404 C CG2 . THR C  267 ? 0.3880 0.5767 0.5207 -0.0190 0.1316  0.0178  267 THR C CG2 
10405 N N   . GLU C  268 ? 0.3743 0.5519 0.4939 -0.0405 0.1294  0.0174  268 GLU C N   
10406 C CA  . GLU C  268 ? 0.3878 0.5719 0.5153 -0.0511 0.1267  0.0188  268 GLU C CA  
10407 C C   . GLU C  268 ? 0.2927 0.4541 0.4037 -0.0589 0.1226  0.0173  268 GLU C C   
10408 O O   . GLU C  268 ? 0.2542 0.4136 0.3653 -0.0672 0.1181  0.0158  268 GLU C O   
10409 C CB  . GLU C  268 ? 0.7454 0.9470 0.8867 -0.0528 0.1304  0.0212  268 GLU C CB  
10410 C CG  . GLU C  268 ? 0.8881 1.1166 1.0524 -0.0477 0.1327  0.0224  268 GLU C CG  
10411 C CD  . GLU C  268 ? 0.9934 1.2288 1.1647 -0.0492 0.1277  0.0195  268 GLU C CD  
10412 O OE1 . GLU C  268 ? 1.0287 1.2640 1.1985 -0.0606 0.1211  0.0173  268 GLU C OE1 
10413 O OE2 . GLU C  268 ? 1.0094 1.2518 1.1856 -0.0391 0.1294  0.0189  268 GLU C OE2 
10414 N N   . LEU C  269 ? 0.3787 0.5239 0.4755 -0.0562 0.1236  0.0169  269 LEU C N   
10415 C CA  . LEU C  269 ? 0.3734 0.4974 0.4545 -0.0611 0.1199  0.0154  269 LEU C CA  
10416 C C   . LEU C  269 ? 0.3450 0.4596 0.4200 -0.0618 0.1157  0.0133  269 LEU C C   
10417 O O   . LEU C  269 ? 0.3146 0.4223 0.3855 -0.0696 0.1119  0.0120  269 LEU C O   
10418 C CB  . LEU C  269 ? 0.1967 0.3064 0.2648 -0.0559 0.1211  0.0142  269 LEU C CB  
10419 C CG  . LEU C  269 ? 0.2004 0.2945 0.2568 -0.0620 0.1181  0.0135  269 LEU C CG  
10420 C CD1 . LEU C  269 ? 0.6267 0.7289 0.6882 -0.0664 0.1212  0.0158  269 LEU C CD1 
10421 C CD2 . LEU C  269 ? 0.4592 0.5364 0.5016 -0.0578 0.1170  0.0111  269 LEU C CD2 
10422 N N   . ILE C  270 ? 0.2830 0.3969 0.3565 -0.0538 0.1168  0.0127  270 ILE C N   
10423 C CA  . ILE C  270 ? 0.2977 0.4022 0.3641 -0.0538 0.1136  0.0109  270 ILE C CA  
10424 C C   . ILE C  270 ? 0.3072 0.4246 0.3832 -0.0606 0.1115  0.0101  270 ILE C C   
10425 O O   . ILE C  270 ? 0.3150 0.4238 0.3835 -0.0670 0.1075  0.0077  270 ILE C O   
10426 C CB  . ILE C  270 ? 0.1822 0.2833 0.2453 -0.0441 0.1156  0.0110  270 ILE C CB  
10427 C CG1 . ILE C  270 ? 0.1828 0.2640 0.2310 -0.0413 0.1141  0.0093  270 ILE C CG1 
10428 C CG2 . ILE C  270 ? 0.1800 0.2820 0.2428 -0.0439 0.1143  0.0103  270 ILE C CG2 
10429 C CD1 . ILE C  270 ? 0.1856 0.2610 0.2294 -0.0439 0.1139  0.0088  270 ILE C CD1 
10430 N N   . ALA C  271 ? 0.3307 0.4703 0.4235 -0.0598 0.1136  0.0113  271 ALA C N   
10431 C CA  . ALA C  271 ? 0.3432 0.4992 0.4454 -0.0647 0.1089  0.0097  271 ALA C CA  
10432 C C   . ALA C  271 ? 0.2408 0.3963 0.3429 -0.0783 0.1045  0.0078  271 ALA C C   
10433 O O   . ALA C  271 ? 0.2013 0.3552 0.3000 -0.0822 0.0953  0.0059  271 ALA C O   
10434 C CB  . ALA C  271 ? 0.6592 0.8403 0.7799 -0.0585 0.1094  0.0120  271 ALA C CB  
10435 N N   . CYS C  272 ? 0.2191 0.3692 0.3210 -0.0813 0.1068  0.0095  272 CYS C N   
10436 C CA  . CYS C  272 ? 0.2294 0.3733 0.3283 -0.0932 0.1029  0.0085  272 CYS C CA  
10437 C C   . CYS C  272 ? 0.2439 0.3625 0.3233 -0.0956 0.1000  0.0062  272 CYS C C   
10438 O O   . CYS C  272 ? 0.2139 0.3286 0.2896 -0.1048 0.0949  0.0034  272 CYS C O   
10439 C CB  . CYS C  272 ? 0.2089 0.3550 0.3125 -0.0947 0.1065  0.0116  272 CYS C CB  
10440 S SG  . CYS C  272 ? 0.8958 1.0281 0.9917 -0.1075 0.1035  0.0116  272 CYS C SG  
10441 N N   . LEU C  273 ? 0.2883 0.3909 0.3557 -0.0873 0.1025  0.0070  273 LEU C N   
10442 C CA  . LEU C  273 ? 0.1986 0.2794 0.2490 -0.0880 0.0998  0.0047  273 LEU C CA  
10443 C C   . LEU C  273 ? 0.2007 0.2812 0.2479 -0.0904 0.0968  0.0015  273 LEU C C   
10444 O O   . LEU C  273 ? 0.2320 0.2977 0.2676 -0.0949 0.0938  -0.0009 273 LEU C O   
10445 C CB  . LEU C  273 ? 0.1949 0.2641 0.2359 -0.0779 0.1019  0.0054  273 LEU C CB  
10446 C CG  . LEU C  273 ? 0.1984 0.2574 0.2323 -0.0771 0.1027  0.0065  273 LEU C CG  
10447 C CD1 . LEU C  273 ? 0.1945 0.2437 0.2197 -0.0685 0.1032  0.0057  273 LEU C CD1 
10448 C CD2 . LEU C  273 ? 0.2056 0.2519 0.2307 -0.0850 0.0996  0.0053  273 LEU C CD2 
10449 N N   . ARG C  274 ? 0.2247 0.3206 0.2810 -0.0856 0.0962  0.0018  274 ARG C N   
10450 C CA  . ARG C  274 ? 0.1942 0.2874 0.2447 -0.0816 0.0879  0.0000  274 ARG C CA  
10451 C C   . ARG C  274 ? 0.2017 0.2983 0.2539 -0.0903 0.0791  -0.0025 274 ARG C C   
10452 O O   . ARG C  274 ? 0.2059 0.2964 0.2498 -0.0889 0.0717  -0.0052 274 ARG C O   
10453 C CB  . ARG C  274 ? 0.2622 0.3693 0.3203 -0.0713 0.0880  0.0022  274 ARG C CB  
10454 C CG  . ARG C  274 ? 0.2551 0.3505 0.3029 -0.0615 0.0911  0.0030  274 ARG C CG  
10455 C CD  . ARG C  274 ? 0.2902 0.3971 0.3432 -0.0519 0.0891  0.0055  274 ARG C CD  
10456 N NE  . ARG C  274 ? 0.3434 0.4661 0.4111 -0.0482 0.0944  0.0085  274 ARG C NE  
10457 C CZ  . ARG C  274 ? 0.3714 0.4923 0.4400 -0.0393 0.1015  0.0110  274 ARG C CZ  
10458 N NH1 . ARG C  274 ? 0.2902 0.3945 0.3460 -0.0341 0.1041  0.0112  274 ARG C NH1 
10459 N NH2 . ARG C  274 ? 0.4254 0.5614 0.5080 -0.0358 0.1063  0.0133  274 ARG C NH2 
10460 N N   . THR C  275 ? 0.2744 0.3810 0.3372 -0.0997 0.0801  -0.0020 275 THR C N   
10461 C CA  . THR C  275 ? 0.2850 0.3954 0.3509 -0.1100 0.0722  -0.0045 275 THR C CA  
10462 C C   . THR C  275 ? 0.2874 0.3758 0.3403 -0.1190 0.0710  -0.0066 275 THR C C   
10463 O O   . THR C  275 ? 0.3409 0.4254 0.3918 -0.1273 0.0639  -0.0096 275 THR C O   
10464 C CB  . THR C  275 ? 0.2906 0.4239 0.3756 -0.1171 0.0740  -0.0028 275 THR C CB  
10465 O OG1 . THR C  275 ? 0.3232 0.4505 0.4082 -0.1246 0.0818  -0.0010 275 THR C OG1 
10466 C CG2 . THR C  275 ? 0.2733 0.4283 0.3721 -0.1070 0.0773  0.0000  275 THR C CG2 
10467 N N   . ARG C  276 ? 0.2215 0.2948 0.2651 -0.1173 0.0776  -0.0051 276 ARG C N   
10468 C CA  . ARG C  276 ? 0.2318 0.2829 0.2618 -0.1239 0.0761  -0.0065 276 ARG C CA  
10469 C C   . ARG C  276 ? 0.2759 0.3114 0.2921 -0.1200 0.0684  -0.0107 276 ARG C C   
10470 O O   . ARG C  276 ? 0.2746 0.3132 0.2886 -0.1103 0.0668  -0.0117 276 ARG C O   
10471 C CB  . ARG C  276 ? 0.2724 0.3124 0.2951 -0.1212 0.0841  -0.0039 276 ARG C CB  
10472 C CG  . ARG C  276 ? 0.3205 0.3598 0.3463 -0.1248 0.0852  -0.0007 276 ARG C CG  
10473 C CD  . ARG C  276 ? 0.3538 0.4146 0.3956 -0.1216 0.0890  0.0022  276 ARG C CD  
10474 N NE  . ARG C  276 ? 0.3815 0.4459 0.4292 -0.1287 0.0894  0.0047  276 ARG C NE  
10475 C CZ  . ARG C  276 ? 0.3994 0.4795 0.4605 -0.1367 0.0874  0.0045  276 ARG C CZ  
10476 N NH1 . ARG C  276 ? 0.3847 0.4793 0.4545 -0.1385 0.0840  0.0017  276 ARG C NH1 
10477 N NH2 . ARG C  276 ? 0.4509 0.5334 0.5169 -0.1430 0.0885  0.0071  276 ARG C NH2 
10478 N N   . PRO C  277 ? 0.3775 0.3957 0.3839 -0.1274 0.0641  -0.0131 277 PRO C N   
10479 C CA  . PRO C  277 ? 0.3654 0.3658 0.3569 -0.1233 0.0579  -0.0174 277 PRO C CA  
10480 C C   . PRO C  277 ? 0.3689 0.3559 0.3491 -0.1144 0.0623  -0.0166 277 PRO C C   
10481 O O   . PRO C  277 ? 0.2572 0.2389 0.2360 -0.1161 0.0682  -0.0134 277 PRO C O   
10482 C CB  . PRO C  277 ? 0.2755 0.2598 0.2606 -0.1346 0.0538  -0.0193 277 PRO C CB  
10483 C CG  . PRO C  277 ? 0.2769 0.2754 0.2761 -0.1455 0.0563  -0.0164 277 PRO C CG  
10484 C CD  . PRO C  277 ? 0.2618 0.2759 0.2707 -0.1404 0.0649  -0.0118 277 PRO C CD  
10485 N N   . ALA C  278 ? 0.3811 0.3632 0.3532 -0.1055 0.0594  -0.0195 278 ALA C N   
10486 C CA  . ALA C  278 ? 0.3756 0.3480 0.3387 -0.0970 0.0634  -0.0191 278 ALA C CA  
10487 C C   . ALA C  278 ? 0.3923 0.3464 0.3459 -0.1001 0.0649  -0.0184 278 ALA C C   
10488 O O   . ALA C  278 ? 0.3877 0.3395 0.3395 -0.0971 0.0706  -0.0158 278 ALA C O   
10489 C CB  . ALA C  278 ? 0.2465 0.2148 0.2012 -0.0890 0.0591  -0.0231 278 ALA C CB  
10490 N N   . GLN C  279 ? 0.2693 0.2099 0.2163 -0.1063 0.0595  -0.0208 279 GLN C N   
10491 C CA  . GLN C  279 ? 0.3472 0.2684 0.2837 -0.1085 0.0602  -0.0198 279 GLN C CA  
10492 C C   . GLN C  279 ? 0.3537 0.2779 0.2952 -0.1152 0.0663  -0.0144 279 GLN C C   
10493 O O   . GLN C  279 ? 0.2831 0.1962 0.2167 -0.1138 0.0693  -0.0120 279 GLN C O   
10494 C CB  . GLN C  279 ? 0.2997 0.2036 0.2275 -0.1137 0.0532  -0.0234 279 GLN C CB  
10495 C CG  . GLN C  279 ? 0.3134 0.1939 0.2272 -0.1124 0.0528  -0.0229 279 GLN C CG  
10496 C CD  . GLN C  279 ? 0.3065 0.1836 0.2132 -0.0999 0.0541  -0.0240 279 GLN C CD  
10497 O OE1 . GLN C  279 ? 0.3016 0.1828 0.2070 -0.0924 0.0518  -0.0282 279 GLN C OE1 
10498 N NE2 . GLN C  279 ? 0.3071 0.1773 0.2091 -0.0980 0.0578  -0.0204 279 GLN C NE2 
10499 N N   . ASP C  280 ? 0.2755 0.2158 0.2300 -0.1221 0.0683  -0.0124 280 ASP C N   
10500 C CA  . ASP C  280 ? 0.2760 0.2210 0.2359 -0.1293 0.0748  -0.0075 280 ASP C CA  
10501 C C   . ASP C  280 ? 0.2640 0.2142 0.2237 -0.1196 0.0803  -0.0051 280 ASP C C   
10502 O O   . ASP C  280 ? 0.2679 0.2121 0.2228 -0.1177 0.0818  -0.0022 280 ASP C O   
10503 C CB  . ASP C  280 ? 0.2711 0.2376 0.2476 -0.1347 0.0752  -0.0067 280 ASP C CB  
10504 C CG  . ASP C  280 ? 0.2754 0.2474 0.2579 -0.1374 0.0773  -0.0023 280 ASP C CG  
10505 O OD1 . ASP C  280 ? 0.2895 0.2456 0.2629 -0.1413 0.0760  -0.0007 280 ASP C OD1 
10506 O OD2 . ASP C  280 ? 0.2660 0.2580 0.2623 -0.1354 0.0805  -0.0002 280 ASP C OD2 
10507 N N   . LEU C  281 ? 0.2737 0.2353 0.2385 -0.1132 0.0825  -0.0065 281 LEU C N   
10508 C CA  . LEU C  281 ? 0.2667 0.2324 0.2312 -0.1027 0.0860  -0.0056 281 LEU C CA  
10509 C C   . LEU C  281 ? 0.2444 0.1929 0.1948 -0.0996 0.0857  -0.0063 281 LEU C C   
10510 O O   . LEU C  281 ? 0.2566 0.2033 0.2044 -0.0960 0.0870  -0.0044 281 LEU C O   
10511 C CB  . LEU C  281 ? 0.2274 0.2046 0.1977 -0.0967 0.0875  -0.0072 281 LEU C CB  
10512 C CG  . LEU C  281 ? 0.4022 0.3981 0.3866 -0.0931 0.0897  -0.0049 281 LEU C CG  
10513 C CD1 . LEU C  281 ? 0.2231 0.2284 0.2172 -0.1012 0.0890  -0.0031 281 LEU C CD1 
10514 C CD2 . LEU C  281 ? 0.2099 0.2153 0.1987 -0.0880 0.0909  -0.0060 281 LEU C CD2 
10515 N N   . VAL C  282 ? 0.2501 0.1872 0.1920 -0.0981 0.0814  -0.0094 282 VAL C N   
10516 C CA  . VAL C  282 ? 0.2556 0.1778 0.1852 -0.0934 0.0803  -0.0101 282 VAL C CA  
10517 C C   . VAL C  282 ? 0.2688 0.1779 0.1906 -0.0993 0.0813  -0.0066 282 VAL C C   
10518 O O   . VAL C  282 ? 0.2722 0.1783 0.1887 -0.0967 0.0846  -0.0047 282 VAL C O   
10519 C CB  . VAL C  282 ? 0.2618 0.1738 0.1838 -0.0883 0.0738  -0.0144 282 VAL C CB  
10520 C CG1 . VAL C  282 ? 0.3052 0.2031 0.2156 -0.0831 0.0727  -0.0147 282 VAL C CG1 
10521 C CG2 . VAL C  282 ? 0.3561 0.2801 0.2832 -0.0814 0.0736  -0.0172 282 VAL C CG2 
10522 N N   . ASP C  283 ? 0.2816 0.1832 0.2025 -0.1077 0.0784  -0.0058 283 ASP C N   
10523 C CA  . ASP C  283 ? 0.2965 0.1858 0.2103 -0.1133 0.0785  -0.0020 283 ASP C CA  
10524 C C   . ASP C  283 ? 0.2894 0.1916 0.2090 -0.1106 0.0821  0.0015  283 ASP C C   
10525 O O   . ASP C  283 ? 0.2994 0.1922 0.2107 -0.1110 0.0824  0.0046  283 ASP C O   
10526 C CB  . ASP C  283 ? 0.6322 0.5182 0.5493 -0.1227 0.0749  -0.0019 283 ASP C CB  
10527 C CG  . ASP C  283 ? 0.7808 0.6521 0.6910 -0.1237 0.0686  -0.0065 283 ASP C CG  
10528 O OD1 . ASP C  283 ? 0.8033 0.6732 0.7094 -0.1135 0.0660  -0.0101 283 ASP C OD1 
10529 O OD2 . ASP C  283 ? 0.8639 0.7273 0.7737 -0.1328 0.0652  -0.0070 283 ASP C OD2 
10530 N N   . HIS C  284 ? 0.3436 0.2659 0.2766 -0.1077 0.0846  0.0012  284 HIS C N   
10531 C CA  . HIS C  284 ? 0.3352 0.2669 0.2720 -0.1044 0.0876  0.0038  284 HIS C CA  
10532 C C   . HIS C  284 ? 0.3115 0.2480 0.2475 -0.0955 0.0895  0.0023  284 HIS C C   
10533 O O   . HIS C  284 ? 0.2925 0.2348 0.2303 -0.0930 0.0915  0.0039  284 HIS C O   
10534 C CB  . HIS C  284 ? 0.3508 0.2994 0.3020 -0.1073 0.0893  0.0055  284 HIS C CB  
10535 C CG  . HIS C  284 ? 0.4001 0.3444 0.3521 -0.1169 0.0877  0.0075  284 HIS C CG  
10536 N ND1 . HIS C  284 ? 0.4267 0.3693 0.3814 -0.1229 0.0845  0.0054  284 HIS C ND1 
10537 C CD2 . HIS C  284 ? 0.4702 0.4105 0.4198 -0.1220 0.0887  0.0112  284 HIS C CD2 
10538 C CE1 . HIS C  284 ? 0.4953 0.4333 0.4502 -0.1314 0.0832  0.0076  284 HIS C CE1 
10539 N NE2 . HIS C  284 ? 0.5188 0.4553 0.4706 -0.1309 0.0860  0.0114  284 HIS C NE2 
10540 N N   . GLU C  285 ? 0.2516 0.1856 0.1849 -0.0910 0.0888  -0.0008 285 GLU C N   
10541 C CA  . GLU C  285 ? 0.2400 0.1812 0.1757 -0.0831 0.0902  -0.0024 285 GLU C CA  
10542 C C   . GLU C  285 ? 0.3005 0.2350 0.2271 -0.0809 0.0907  -0.0017 285 GLU C C   
10543 O O   . GLU C  285 ? 0.2918 0.2338 0.2220 -0.0763 0.0917  -0.0025 285 GLU C O   
10544 C CB  . GLU C  285 ? 0.3369 0.2804 0.2741 -0.0784 0.0898  -0.0057 285 GLU C CB  
10545 C CG  . GLU C  285 ? 0.4001 0.3305 0.3258 -0.0781 0.0892  -0.0074 285 GLU C CG  
10546 C CD  . GLU C  285 ? 0.4639 0.3992 0.3923 -0.0733 0.0897  -0.0105 285 GLU C CD  
10547 O OE1 . GLU C  285 ? 0.4764 0.4216 0.4139 -0.0731 0.0897  -0.0107 285 GLU C OE1 
10548 O OE2 . GLU C  285 ? 0.5024 0.4327 0.4239 -0.0695 0.0901  -0.0124 285 GLU C OE2 
10549 N N   . TRP C  286 ? 0.3917 0.3114 0.3059 -0.0844 0.0898  -0.0001 286 TRP C N   
10550 C CA  . TRP C  286 ? 0.4311 0.3445 0.3354 -0.0826 0.0903  0.0011  286 TRP C CA  
10551 C C   . TRP C  286 ? 0.3848 0.3018 0.2897 -0.0850 0.0917  0.0042  286 TRP C C   
10552 O O   . TRP C  286 ? 0.3677 0.2829 0.2659 -0.0833 0.0925  0.0049  286 TRP C O   
10553 C CB  . TRP C  286 ? 0.7626 0.6567 0.6511 -0.0845 0.0888  0.0027  286 TRP C CB  
10554 C CG  . TRP C  286 ? 0.8945 0.7843 0.7792 -0.0807 0.0886  -0.0003 286 TRP C CG  
10555 C CD1 . TRP C  286 ? 0.9448 0.8267 0.8283 -0.0799 0.0845  -0.0021 286 TRP C CD1 
10556 C CD2 . TRP C  286 ? 0.8931 0.7895 0.7776 -0.0744 0.0897  -0.0031 286 TRP C CD2 
10557 N NE1 . TRP C  286 ? 0.9204 0.8058 0.8047 -0.0713 0.0818  -0.0062 286 TRP C NE1 
10558 C CE2 . TRP C  286 ? 0.8973 0.7917 0.7824 -0.0685 0.0852  -0.0067 286 TRP C CE2 
10559 C CE3 . TRP C  286 ? 0.8716 0.7779 0.7592 -0.0708 0.0903  -0.0043 286 TRP C CE3 
10560 C CZ2 . TRP C  286 ? 0.8814 0.7830 0.7683 -0.0615 0.0846  -0.0102 286 TRP C CZ2 
10561 C CZ3 . TRP C  286 ? 0.8789 0.7904 0.7668 -0.0656 0.0905  -0.0077 286 TRP C CZ3 
10562 C CH2 . TRP C  286 ? 0.8853 0.7950 0.7728 -0.0614 0.0884  -0.0104 286 TRP C CH2 
10563 N N   . HIS C  287 ? 0.4960 0.4186 0.4086 -0.0893 0.0924  0.0061  287 HIS C N   
10564 C CA  . HIS C  287 ? 0.5356 0.4607 0.4478 -0.0925 0.0945  0.0096  287 HIS C CA  
10565 C C   . HIS C  287 ? 0.5359 0.4739 0.4548 -0.0879 0.0970  0.0083  287 HIS C C   
10566 O O   . HIS C  287 ? 0.6162 0.5553 0.5318 -0.0891 0.0993  0.0105  287 HIS C O   
10567 C CB  . HIS C  287 ? 0.5480 0.4769 0.4679 -0.0989 0.0949  0.0120  287 HIS C CB  
10568 C CG  . HIS C  287 ? 0.5931 0.5077 0.5064 -0.1046 0.0919  0.0131  287 HIS C CG  
10569 N ND1 . HIS C  287 ? 0.5918 0.5078 0.5110 -0.1117 0.0915  0.0150  287 HIS C ND1 
10570 C CD2 . HIS C  287 ? 0.6014 0.4990 0.5024 -0.1044 0.0892  0.0126  287 HIS C CD2 
10571 C CE1 . HIS C  287 ? 0.6001 0.4997 0.5108 -0.1158 0.0881  0.0151  287 HIS C CE1 
10572 N NE2 . HIS C  287 ? 0.5990 0.4865 0.4981 -0.1111 0.0867  0.0138  287 HIS C NE2 
10573 N N   . VAL C  288 ? 0.3587 0.3054 0.2861 -0.0827 0.0967  0.0049  288 VAL C N   
10574 C CA  . VAL C  288 ? 0.3177 0.2753 0.2519 -0.0786 0.0989  0.0037  288 VAL C CA  
10575 C C   . VAL C  288 ? 0.3231 0.2776 0.2502 -0.0749 0.0990  0.0015  288 VAL C C   
10576 O O   . VAL C  288 ? 0.3188 0.2799 0.2498 -0.0718 0.1008  0.0001  288 VAL C O   
10577 C CB  . VAL C  288 ? 0.2349 0.2028 0.1815 -0.0750 0.0988  0.0019  288 VAL C CB  
10578 C CG1 . VAL C  288 ? 0.3391 0.3110 0.2925 -0.0794 0.0986  0.0040  288 VAL C CG1 
10579 C CG2 . VAL C  288 ? 0.3956 0.3601 0.3408 -0.0708 0.0963  -0.0013 288 VAL C CG2 
10580 N N   . LEU C  289 ? 0.5621 0.5062 0.4781 -0.0756 0.0973  0.0014  289 LEU C N   
10581 C CA  . LEU C  289 ? 0.5801 0.5221 0.4889 -0.0730 0.0973  -0.0005 289 LEU C CA  
10582 C C   . LEU C  289 ? 0.6078 0.5505 0.5112 -0.0749 0.1000  0.0014  289 LEU C C   
10583 O O   . LEU C  289 ? 0.6494 0.5890 0.5493 -0.0791 0.1012  0.0053  289 LEU C O   
10584 C CB  . LEU C  289 ? 0.4287 0.3599 0.3258 -0.0732 0.0952  -0.0005 289 LEU C CB  
10585 C CG  . LEU C  289 ? 0.3921 0.3232 0.2925 -0.0702 0.0933  -0.0034 289 LEU C CG  
10586 C CD1 . LEU C  289 ? 0.3849 0.3058 0.2718 -0.0699 0.0922  -0.0030 289 LEU C CD1 
10587 C CD2 . LEU C  289 ? 0.3722 0.3134 0.2826 -0.0658 0.0932  -0.0073 289 LEU C CD2 
10588 N N   . PRO C  290 ? 0.4277 0.3746 0.3310 -0.0722 0.1011  -0.0014 290 PRO C N   
10589 C CA  . PRO C  290 ? 0.4107 0.3584 0.3076 -0.0736 0.1040  -0.0006 290 PRO C CA  
10590 C C   . PRO C  290 ? 0.4523 0.3908 0.3328 -0.0761 0.1035  0.0018  290 PRO C C   
10591 O O   . PRO C  290 ? 0.4905 0.4273 0.3649 -0.0791 0.1058  0.0053  290 PRO C O   
10592 C CB  . PRO C  290 ? 0.3038 0.2568 0.2049 -0.0700 0.1048  -0.0053 290 PRO C CB  
10593 C CG  . PRO C  290 ? 0.3221 0.2737 0.2258 -0.0676 0.1015  -0.0080 290 PRO C CG  
10594 C CD  . PRO C  290 ? 0.3259 0.2766 0.2349 -0.0680 0.0998  -0.0058 290 PRO C CD  
10595 N N   . GLN C  291 ? 0.4612 0.3941 0.3342 -0.0749 0.1007  0.0006  291 GLN C N   
10596 C CA  . GLN C  291 ? 0.4998 0.4237 0.3554 -0.0766 0.0998  0.0035  291 GLN C CA  
10597 C C   . GLN C  291 ? 0.5297 0.4429 0.3768 -0.0767 0.0968  0.0061  291 GLN C C   
10598 O O   . GLN C  291 ? 0.6107 0.5247 0.4654 -0.0750 0.0953  0.0040  291 GLN C O   
10599 C CB  . GLN C  291 ? 0.4840 0.4112 0.3332 -0.0747 0.0995  -0.0001 291 GLN C CB  
10600 C CG  . GLN C  291 ? 0.5032 0.4378 0.3567 -0.0748 0.1028  -0.0027 291 GLN C CG  
10601 C CD  . GLN C  291 ? 0.5209 0.4632 0.3885 -0.0720 0.1030  -0.0080 291 GLN C CD  
10602 O OE1 . GLN C  291 ? 0.5154 0.4583 0.3878 -0.0701 0.1005  -0.0102 291 GLN C OE1 
10603 N NE2 . GLN C  291 ? 0.5652 0.5126 0.4385 -0.0716 0.1063  -0.0099 291 GLN C NE2 
10604 N N   . GLU C  292 ? 0.3820 0.2841 0.2118 -0.0783 0.0957  0.0108  292 GLU C N   
10605 C CA  . GLU C  292 ? 0.4231 0.3120 0.2407 -0.0773 0.0924  0.0137  292 GLU C CA  
10606 C C   . GLU C  292 ? 0.4155 0.3096 0.2308 -0.0728 0.0905  0.0090  292 GLU C C   
10607 O O   . GLU C  292 ? 0.3920 0.2909 0.2003 -0.0716 0.0900  0.0073  292 GLU C O   
10608 C CB  . GLU C  292 ? 0.7258 0.6000 0.5235 -0.0790 0.0910  0.0208  292 GLU C CB  
10609 C CG  . GLU C  292 ? 0.8442 0.7012 0.6247 -0.0762 0.0866  0.0247  292 GLU C CG  
10610 C CD  . GLU C  292 ? 0.9497 0.7904 0.7095 -0.0767 0.0842  0.0326  292 GLU C CD  
10611 O OE1 . GLU C  292 ? 0.9671 0.8118 0.7262 -0.0800 0.0867  0.0346  292 GLU C OE1 
10612 O OE2 . GLU C  292 ? 0.9965 0.8198 0.7404 -0.0731 0.0796  0.0370  292 GLU C OE2 
10613 N N   . SER C  293 ? 0.5431 0.4370 0.3642 -0.0705 0.0895  0.0066  293 SER C N   
10614 C CA  . SER C  293 ? 0.5141 0.4175 0.3392 -0.0666 0.0886  0.0009  293 SER C CA  
10615 C C   . SER C  293 ? 0.4908 0.3903 0.3172 -0.0622 0.0854  -0.0002 293 SER C C   
10616 O O   . SER C  293 ? 0.5424 0.4334 0.3710 -0.0628 0.0846  0.0023  293 SER C O   
10617 C CB  . SER C  293 ? 0.4855 0.4037 0.3311 -0.0666 0.0906  -0.0043 293 SER C CB  
10618 O OG  . SER C  293 ? 0.4744 0.3932 0.3328 -0.0671 0.0914  -0.0042 293 SER C OG  
10619 N N   . ILE C  294 ? 0.3668 0.2753 0.1967 -0.0564 0.0812  -0.0047 294 ILE C N   
10620 C CA  . ILE C  294 ? 0.3735 0.2852 0.2129 -0.0505 0.0774  -0.0078 294 ILE C CA  
10621 C C   . ILE C  294 ? 0.3829 0.3104 0.2348 -0.0510 0.0810  -0.0141 294 ILE C C   
10622 O O   . ILE C  294 ? 0.3601 0.2946 0.2114 -0.0546 0.0846  -0.0164 294 ILE C O   
10623 C CB  . ILE C  294 ? 0.3050 0.2133 0.1380 -0.0419 0.0686  -0.0072 294 ILE C CB  
10624 C CG1 . ILE C  294 ? 0.4516 0.3684 0.2785 -0.0401 0.0657  -0.0086 294 ILE C CG1 
10625 C CG2 . ILE C  294 ? 0.3228 0.2121 0.1443 -0.0406 0.0649  -0.0010 294 ILE C CG2 
10626 C CD1 . ILE C  294 ? 0.3117 0.2357 0.1408 -0.0308 0.0581  -0.0113 294 ILE C CD1 
10627 N N   . PHE C  295 ? 0.4066 0.3384 0.2687 -0.0474 0.0801  -0.0169 295 PHE C N   
10628 C CA  . PHE C  295 ? 0.3545 0.2994 0.2285 -0.0481 0.0840  -0.0221 295 PHE C CA  
10629 C C   . PHE C  295 ? 0.3450 0.2928 0.2280 -0.0531 0.0880  -0.0216 295 PHE C C   
10630 O O   . PHE C  295 ? 0.3122 0.2689 0.2040 -0.0535 0.0880  -0.0245 295 PHE C O   
10631 C CB  . PHE C  295 ? 0.3560 0.3123 0.2309 -0.0455 0.0811  -0.0263 295 PHE C CB  
10632 C CG  . PHE C  295 ? 0.3566 0.3247 0.2438 -0.0433 0.0822  -0.0310 295 PHE C CG  
10633 C CD1 . PHE C  295 ? 0.3734 0.3438 0.2714 -0.0456 0.0865  -0.0316 295 PHE C CD1 
10634 C CD2 . PHE C  295 ? 0.3290 0.3069 0.2190 -0.0380 0.0771  -0.0340 295 PHE C CD2 
10635 C CE1 . PHE C  295 ? 0.3451 0.3254 0.2545 -0.0434 0.0864  -0.0346 295 PHE C CE1 
10636 C CE2 . PHE C  295 ? 0.3094 0.2990 0.2108 -0.0368 0.0790  -0.0382 295 PHE C CE2 
10637 C CZ  . PHE C  295 ? 0.3160 0.3058 0.2247 -0.0404 0.0855  -0.0389 295 PHE C CZ  
10638 N N   . ARG C  296 ? 0.6148 0.5550 0.4980 -0.0554 0.0889  -0.0178 296 ARG C N   
10639 C CA  . ARG C  296 ? 0.6585 0.6030 0.5541 -0.0569 0.0896  -0.0175 296 ARG C CA  
10640 C C   . ARG C  296 ? 0.7110 0.6514 0.6109 -0.0573 0.0897  -0.0155 296 ARG C C   
10641 O O   . ARG C  296 ? 0.7852 0.7158 0.6760 -0.0594 0.0901  -0.0125 296 ARG C O   
10642 C CB  . ARG C  296 ? 0.4475 0.3901 0.3387 -0.0599 0.0906  -0.0156 296 ARG C CB  
10643 C CG  . ARG C  296 ? 0.4456 0.3917 0.3308 -0.0604 0.0906  -0.0178 296 ARG C CG  
10644 C CD  . ARG C  296 ? 0.4519 0.4066 0.3479 -0.0593 0.0907  -0.0222 296 ARG C CD  
10645 N NE  . ARG C  296 ? 0.4831 0.4407 0.3730 -0.0611 0.0911  -0.0248 296 ARG C NE  
10646 C CZ  . ARG C  296 ? 0.4864 0.4483 0.3705 -0.0610 0.0897  -0.0277 296 ARG C CZ  
10647 N NH1 . ARG C  296 ? 0.4755 0.4396 0.3597 -0.0584 0.0883  -0.0284 296 ARG C NH1 
10648 N NH2 . ARG C  296 ? 0.5004 0.4652 0.3782 -0.0632 0.0899  -0.0305 296 ARG C NH2 
10649 N N   . PHE C  297 ? 0.4274 0.3742 0.3397 -0.0556 0.0894  -0.0169 297 PHE C N   
10650 C CA  . PHE C  297 ? 0.3244 0.2694 0.2410 -0.0558 0.0894  -0.0156 297 PHE C CA  
10651 C C   . PHE C  297 ? 0.2489 0.1990 0.1746 -0.0563 0.0898  -0.0146 297 PHE C C   
10652 O O   . PHE C  297 ? 0.2330 0.1881 0.1634 -0.0549 0.0901  -0.0157 297 PHE C O   
10653 C CB  . PHE C  297 ? 0.3992 0.3479 0.3205 -0.0523 0.0886  -0.0180 297 PHE C CB  
10654 C CG  . PHE C  297 ? 0.4632 0.4135 0.3799 -0.0499 0.0883  -0.0205 297 PHE C CG  
10655 C CD1 . PHE C  297 ? 0.5217 0.4651 0.4274 -0.0488 0.0888  -0.0210 297 PHE C CD1 
10656 C CD2 . PHE C  297 ? 0.4614 0.4197 0.3837 -0.0486 0.0877  -0.0227 297 PHE C CD2 
10657 C CE1 . PHE C  297 ? 0.5186 0.4657 0.4203 -0.0452 0.0883  -0.0240 297 PHE C CE1 
10658 C CE2 . PHE C  297 ? 0.4839 0.4464 0.4033 -0.0466 0.0874  -0.0254 297 PHE C CE2 
10659 C CZ  . PHE C  297 ? 0.4998 0.4580 0.4095 -0.0444 0.0876  -0.0263 297 PHE C CZ  
10660 N N   . SER C  298 ? 0.2216 0.1702 0.1493 -0.0583 0.0901  -0.0126 298 SER C N   
10661 C CA  . SER C  298 ? 0.2122 0.1665 0.1472 -0.0591 0.0911  -0.0110 298 SER C CA  
10662 C C   . SER C  298 ? 0.2096 0.1718 0.1547 -0.0554 0.0911  -0.0118 298 SER C C   
10663 O O   . SER C  298 ? 0.2151 0.1818 0.1646 -0.0544 0.0924  -0.0114 298 SER C O   
10664 C CB  . SER C  298 ? 0.2652 0.2169 0.1997 -0.0633 0.0914  -0.0084 298 SER C CB  
10665 O OG  . SER C  298 ? 0.3368 0.2819 0.2629 -0.0672 0.0921  -0.0062 298 SER C OG  
10666 N N   . PHE C  299 ? 0.2380 0.2011 0.1858 -0.0533 0.0900  -0.0127 299 PHE C N   
10667 C CA  . PHE C  299 ? 0.2195 0.1890 0.1754 -0.0498 0.0901  -0.0127 299 PHE C CA  
10668 C C   . PHE C  299 ? 0.2196 0.1890 0.1756 -0.0466 0.0891  -0.0146 299 PHE C C   
10669 O O   . PHE C  299 ? 0.2312 0.1989 0.1849 -0.0461 0.0881  -0.0155 299 PHE C O   
10670 C CB  . PHE C  299 ? 0.2499 0.2224 0.2096 -0.0509 0.0904  -0.0111 299 PHE C CB  
10671 C CG  . PHE C  299 ? 0.3286 0.3027 0.2896 -0.0550 0.0916  -0.0089 299 PHE C CG  
10672 C CD1 . PHE C  299 ? 0.3561 0.3378 0.3242 -0.0539 0.0934  -0.0072 299 PHE C CD1 
10673 C CD2 . PHE C  299 ? 0.3678 0.3357 0.3227 -0.0599 0.0913  -0.0083 299 PHE C CD2 
10674 C CE1 . PHE C  299 ? 0.3774 0.3625 0.3479 -0.0578 0.0949  -0.0050 299 PHE C CE1 
10675 C CE2 . PHE C  299 ? 0.4083 0.3781 0.3650 -0.0643 0.0924  -0.0059 299 PHE C CE2 
10676 C CZ  . PHE C  299 ? 0.4027 0.3821 0.3678 -0.0632 0.0943  -0.0043 299 PHE C CZ  
10677 N N   . VAL C  300 ? 0.1841 0.1550 0.1426 -0.0448 0.0896  -0.0154 300 VAL C N   
10678 C CA  . VAL C  300 ? 0.2236 0.1945 0.1824 -0.0429 0.0889  -0.0173 300 VAL C CA  
10679 C C   . VAL C  300 ? 0.1886 0.1613 0.1525 -0.0406 0.0904  -0.0168 300 VAL C C   
10680 O O   . VAL C  300 ? 0.2001 0.1746 0.1671 -0.0400 0.0919  -0.0151 300 VAL C O   
10681 C CB  . VAL C  300 ? 0.2625 0.2313 0.2167 -0.0447 0.0889  -0.0196 300 VAL C CB  
10682 C CG1 . VAL C  300 ? 0.1894 0.1553 0.1370 -0.0469 0.0883  -0.0194 300 VAL C CG1 
10683 C CG2 . VAL C  300 ? 0.1879 0.1561 0.1423 -0.0457 0.0908  -0.0200 300 VAL C CG2 
10684 N N   . PRO C  301 ? 0.1786 0.1507 0.1432 -0.0395 0.0905  -0.0181 301 PRO C N   
10685 C CA  . PRO C  301 ? 0.1854 0.1566 0.1532 -0.0380 0.0928  -0.0177 301 PRO C CA  
10686 C C   . PRO C  301 ? 0.2013 0.1703 0.1688 -0.0391 0.0953  -0.0185 301 PRO C C   
10687 O O   . PRO C  301 ? 0.1871 0.1543 0.1511 -0.0416 0.0953  -0.0207 301 PRO C O   
10688 C CB  . PRO C  301 ? 0.2248 0.1943 0.1918 -0.0385 0.0931  -0.0197 301 PRO C CB  
10689 C CG  . PRO C  301 ? 0.1772 0.1497 0.1431 -0.0381 0.0906  -0.0197 301 PRO C CG  
10690 C CD  . PRO C  301 ? 0.1771 0.1500 0.1403 -0.0393 0.0891  -0.0195 301 PRO C CD  
10691 N N   . VAL C  302 ? 0.2551 0.2250 0.2261 -0.0371 0.0978  -0.0167 302 VAL C N   
10692 C CA  . VAL C  302 ? 0.2672 0.2355 0.2385 -0.0374 0.1011  -0.0174 302 VAL C CA  
10693 C C   . VAL C  302 ? 0.2564 0.2183 0.2272 -0.0371 0.1046  -0.0195 302 VAL C C   
10694 O O   . VAL C  302 ? 0.2459 0.2062 0.2182 -0.0354 0.1052  -0.0185 302 VAL C O   
10695 C CB  . VAL C  302 ? 0.2835 0.2572 0.2595 -0.0352 0.1029  -0.0144 302 VAL C CB  
10696 C CG1 . VAL C  302 ? 0.1884 0.1641 0.1680 -0.0320 0.1033  -0.0120 302 VAL C CG1 
10697 C CG2 . VAL C  302 ? 0.1969 0.1695 0.1737 -0.0347 0.1073  -0.0152 302 VAL C CG2 
10698 N N   . VAL C  303 ? 0.2116 0.1690 0.1796 -0.0390 0.1075  -0.0223 303 VAL C N   
10699 C CA  . VAL C  303 ? 0.2298 0.1792 0.1972 -0.0392 0.1121  -0.0245 303 VAL C CA  
10700 C C   . VAL C  303 ? 0.2367 0.1852 0.2071 -0.0359 0.1168  -0.0228 303 VAL C C   
10701 O O   . VAL C  303 ? 0.2209 0.1687 0.1902 -0.0363 0.1197  -0.0242 303 VAL C O   
10702 C CB  . VAL C  303 ? 0.2174 0.1610 0.1796 -0.0437 0.1139  -0.0293 303 VAL C CB  
10703 C CG1 . VAL C  303 ? 0.2262 0.1602 0.1875 -0.0448 0.1190  -0.0318 303 VAL C CG1 
10704 C CG2 . VAL C  303 ? 0.2126 0.1596 0.1723 -0.0467 0.1094  -0.0307 303 VAL C CG2 
10705 N N   . ASP C  304 ? 0.2858 0.2342 0.2595 -0.0324 0.1180  -0.0199 304 ASP C N   
10706 C CA  . ASP C  304 ? 0.3362 0.2871 0.3144 -0.0280 0.1218  -0.0169 304 ASP C CA  
10707 C C   . ASP C  304 ? 0.3731 0.3133 0.3508 -0.0258 0.1290  -0.0175 304 ASP C C   
10708 O O   . ASP C  304 ? 0.3876 0.3291 0.3690 -0.0212 0.1333  -0.0151 304 ASP C O   
10709 C CB  . ASP C  304 ? 0.4520 0.4102 0.4338 -0.0253 0.1189  -0.0128 304 ASP C CB  
10710 C CG  . ASP C  304 ? 0.7145 0.6678 0.6941 -0.0255 0.1177  -0.0125 304 ASP C CG  
10711 O OD1 . ASP C  304 ? 0.7338 0.6808 0.7096 -0.0289 0.1173  -0.0156 304 ASP C OD1 
10712 O OD2 . ASP C  304 ? 0.6550 0.6116 0.6364 -0.0226 0.1174  -0.0090 304 ASP C OD2 
10713 N N   . GLY C  305 ? 0.4616 0.3912 0.4348 -0.0289 0.1309  -0.0207 305 GLY C N   
10714 C CA  . GLY C  305 ? 0.5024 0.4189 0.4740 -0.0275 0.1385  -0.0212 305 GLY C CA  
10715 C C   . GLY C  305 ? 0.5329 0.4475 0.5060 -0.0237 0.1397  -0.0169 305 GLY C C   
10716 O O   . GLY C  305 ? 0.5797 0.4819 0.5510 -0.0217 0.1468  -0.0162 305 GLY C O   
10717 N N   . ASP C  306 ? 0.4979 0.4235 0.4735 -0.0227 0.1335  -0.0139 306 ASP C N   
10718 C CA  . ASP C  306 ? 0.4877 0.4120 0.4634 -0.0197 0.1343  -0.0099 306 ASP C CA  
10719 C C   . ASP C  306 ? 0.4331 0.3580 0.4061 -0.0234 0.1299  -0.0109 306 ASP C C   
10720 O O   . ASP C  306 ? 0.4445 0.3592 0.4142 -0.0252 0.1337  -0.0120 306 ASP C O   
10721 C CB  . ASP C  306 ? 0.5590 0.4946 0.5393 -0.0149 0.1325  -0.0051 306 ASP C CB  
10722 C CG  . ASP C  306 ? 0.6233 0.5540 0.6030 -0.0098 0.1372  -0.0003 306 ASP C CG  
10723 O OD1 . ASP C  306 ? 0.6974 0.6147 0.6749 -0.0074 0.1447  0.0003  306 ASP C OD1 
10724 O OD2 . ASP C  306 ? 0.5938 0.5326 0.5742 -0.0081 0.1339  0.0030  306 ASP C OD2 
10725 N N   . PHE C  307 ? 0.3697 0.3061 0.3440 -0.0246 0.1228  -0.0106 307 PHE C N   
10726 C CA  . PHE C  307 ? 0.3517 0.2904 0.3241 -0.0273 0.1189  -0.0115 307 PHE C CA  
10727 C C   . PHE C  307 ? 0.3341 0.2675 0.3041 -0.0324 0.1194  -0.0165 307 PHE C C   
10728 O O   . PHE C  307 ? 0.3541 0.2832 0.3222 -0.0350 0.1208  -0.0179 307 PHE C O   
10729 C CB  . PHE C  307 ? 0.3021 0.2526 0.2760 -0.0272 0.1122  -0.0105 307 PHE C CB  
10730 C CG  . PHE C  307 ? 0.3126 0.2664 0.2849 -0.0282 0.1091  -0.0103 307 PHE C CG  
10731 C CD1 . PHE C  307 ? 0.3384 0.2925 0.3095 -0.0319 0.1071  -0.0138 307 PHE C CD1 
10732 C CD2 . PHE C  307 ? 0.3188 0.2762 0.2908 -0.0254 0.1088  -0.0068 307 PHE C CD2 
10733 C CE1 . PHE C  307 ? 0.3276 0.2860 0.2980 -0.0325 0.1049  -0.0136 307 PHE C CE1 
10734 C CE2 . PHE C  307 ? 0.3215 0.2824 0.2918 -0.0262 0.1065  -0.0067 307 PHE C CE2 
10735 C CZ  . PHE C  307 ? 0.3166 0.2782 0.2865 -0.0296 0.1047  -0.0101 307 PHE C CZ  
10736 N N   . LEU C  308 ? 0.3238 0.2578 0.2937 -0.0342 0.1186  -0.0193 308 LEU C N   
10737 C CA  . LEU C  308 ? 0.3313 0.2593 0.2983 -0.0392 0.1205  -0.0244 308 LEU C CA  
10738 C C   . LEU C  308 ? 0.3962 0.3142 0.3619 -0.0389 0.1272  -0.0259 308 LEU C C   
10739 O O   . LEU C  308 ? 0.4306 0.3518 0.3975 -0.0370 0.1273  -0.0254 308 LEU C O   
10740 C CB  . LEU C  308 ? 0.2503 0.1861 0.2167 -0.0416 0.1153  -0.0265 308 LEU C CB  
10741 C CG  . LEU C  308 ? 0.2343 0.1790 0.2017 -0.0414 0.1095  -0.0251 308 LEU C CG  
10742 C CD1 . LEU C  308 ? 0.2206 0.1712 0.1870 -0.0425 0.1055  -0.0260 308 LEU C CD1 
10743 C CD2 . LEU C  308 ? 0.2094 0.1528 0.1758 -0.0448 0.1101  -0.0275 308 LEU C CD2 
10744 N N   . SER C  309 ? 0.3386 0.2444 0.3017 -0.0409 0.1336  -0.0280 309 SER C N   
10745 C CA  . SER C  309 ? 0.3055 0.1987 0.2664 -0.0405 0.1415  -0.0297 309 SER C CA  
10746 C C   . SER C  309 ? 0.3396 0.2318 0.2978 -0.0450 0.1420  -0.0349 309 SER C C   
10747 O O   . SER C  309 ? 0.3995 0.2856 0.3565 -0.0439 0.1471  -0.0359 309 SER C O   
10748 C CB  . SER C  309 ? 0.3138 0.1923 0.2711 -0.0430 0.1486  -0.0314 309 SER C CB  
10749 O OG  . SER C  309 ? 0.3100 0.1904 0.2654 -0.0497 0.1461  -0.0360 309 SER C OG  
10750 N N   . ASP C  310 ? 0.3130 0.2111 0.2697 -0.0500 0.1372  -0.0382 310 ASP C N   
10751 C CA  . ASP C  310 ? 0.3470 0.2462 0.3003 -0.0544 0.1368  -0.0427 310 ASP C CA  
10752 C C   . ASP C  310 ? 0.3280 0.2404 0.2822 -0.0555 0.1286  -0.0422 310 ASP C C   
10753 O O   . ASP C  310 ? 0.3229 0.2423 0.2805 -0.0528 0.1242  -0.0386 310 ASP C O   
10754 C CB  . ASP C  310 ? 0.5558 0.4430 0.5040 -0.0615 0.1429  -0.0492 310 ASP C CB  
10755 C CG  . ASP C  310 ? 0.6464 0.5312 0.5900 -0.0657 0.1453  -0.0539 310 ASP C CG  
10756 O OD1 . ASP C  310 ? 0.6732 0.5676 0.6153 -0.0680 0.1401  -0.0552 310 ASP C OD1 
10757 O OD2 . ASP C  310 ? 0.7017 0.5744 0.6422 -0.0665 0.1528  -0.0561 310 ASP C OD2 
10758 N N   . THR C  311 ? 0.3382 0.2535 0.2889 -0.0594 0.1272  -0.0456 311 THR C N   
10759 C CA  . THR C  311 ? 0.3537 0.2796 0.3043 -0.0607 0.1208  -0.0454 311 THR C CA  
10760 C C   . THR C  311 ? 0.3691 0.2962 0.3202 -0.0645 0.1200  -0.0478 311 THR C C   
10761 O O   . THR C  311 ? 0.3551 0.2744 0.3044 -0.0691 0.1249  -0.0520 311 THR C O   
10762 C CB  . THR C  311 ? 0.4505 0.3782 0.3959 -0.0644 0.1205  -0.0486 311 THR C CB  
10763 O OG1 . THR C  311 ? 0.4883 0.4120 0.4298 -0.0714 0.1235  -0.0548 311 THR C OG1 
10764 C CG2 . THR C  311 ? 0.4865 0.4097 0.4303 -0.0622 0.1244  -0.0481 311 THR C CG2 
10765 N N   . PRO C  312 ? 0.4302 0.3671 0.3837 -0.0629 0.1145  -0.0454 312 PRO C N   
10766 C CA  . PRO C  312 ? 0.4240 0.3653 0.3789 -0.0660 0.1135  -0.0473 312 PRO C CA  
10767 C C   . PRO C  312 ? 0.5189 0.4591 0.4702 -0.0738 0.1162  -0.0541 312 PRO C C   
10768 O O   . PRO C  312 ? 0.5840 0.5231 0.5362 -0.0781 0.1189  -0.0573 312 PRO C O   
10769 C CB  . PRO C  312 ? 0.2655 0.2177 0.2218 -0.0633 0.1076  -0.0445 312 PRO C CB  
10770 C CG  . PRO C  312 ? 0.2726 0.2242 0.2301 -0.0575 0.1058  -0.0395 312 PRO C CG  
10771 C CD  . PRO C  312 ? 0.3240 0.2681 0.2793 -0.0579 0.1095  -0.0406 312 PRO C CD  
10772 N N   . GLU C  313 ? 0.5724 0.5133 0.5193 -0.0759 0.1159  -0.0563 313 GLU C N   
10773 C CA  . GLU C  313 ? 0.6511 0.5911 0.5933 -0.0840 0.1189  -0.0633 313 GLU C CA  
10774 C C   . GLU C  313 ? 0.5763 0.5045 0.5176 -0.0888 0.1257  -0.0677 313 GLU C C   
10775 O O   . GLU C  313 ? 0.6046 0.5340 0.5464 -0.0951 0.1277  -0.0725 313 GLU C O   
10776 C CB  . GLU C  313 ? 0.9663 0.9056 0.9026 -0.0843 0.1187  -0.0639 313 GLU C CB  
10777 C CG  . GLU C  313 ? 1.0860 1.0299 1.0163 -0.0919 0.1192  -0.0702 313 GLU C CG  
10778 C CD  . GLU C  313 ? 1.1663 1.1229 1.0988 -0.0942 0.1153  -0.0715 313 GLU C CD  
10779 O OE1 . GLU C  313 ? 1.1423 1.1061 1.0768 -0.0886 0.1106  -0.0666 313 GLU C OE1 
10780 O OE2 . GLU C  313 ? 1.2358 1.1955 1.1680 -0.1019 0.1176  -0.0780 313 GLU C OE2 
10781 N N   . ALA C  314 ? 0.3776 0.2945 0.3177 -0.0859 0.1298  -0.0661 314 ALA C N   
10782 C CA  . ALA C  314 ? 0.3426 0.2452 0.2810 -0.0894 0.1375  -0.0696 314 ALA C CA  
10783 C C   . ALA C  314 ? 0.3387 0.2396 0.2806 -0.0893 0.1388  -0.0688 314 ALA C C   
10784 O O   . ALA C  314 ? 0.3790 0.2733 0.3186 -0.0963 0.1439  -0.0744 314 ALA C O   
10785 C CB  . ALA C  314 ? 0.2864 0.1793 0.2244 -0.0838 0.1412  -0.0662 314 ALA C CB  
10786 N N   . LEU C  315 ? 0.3471 0.2539 0.2939 -0.0816 0.1344  -0.0618 315 LEU C N   
10787 C CA  . LEU C  315 ? 0.3135 0.2179 0.2631 -0.0802 0.1361  -0.0594 315 LEU C CA  
10788 C C   . LEU C  315 ? 0.3788 0.2907 0.3294 -0.0866 0.1354  -0.0635 315 LEU C C   
10789 O O   . LEU C  315 ? 0.4577 0.3630 0.4076 -0.0904 0.1406  -0.0658 315 LEU C O   
10790 C CB  . LEU C  315 ? 0.2575 0.1683 0.2116 -0.0714 0.1312  -0.0514 315 LEU C CB  
10791 C CG  . LEU C  315 ? 0.2632 0.1688 0.2172 -0.0655 0.1323  -0.0476 315 LEU C CG  
10792 C CD1 . LEU C  315 ? 0.2955 0.2064 0.2535 -0.0579 0.1289  -0.0405 315 LEU C CD1 
10793 C CD2 . LEU C  315 ? 0.2734 0.1627 0.2238 -0.0673 0.1410  -0.0502 315 LEU C CD2 
10794 N N   . ILE C  316 ? 0.3638 0.2896 0.3160 -0.0882 0.1298  -0.0646 316 ILE C N   
10795 C CA  . ILE C  316 ? 0.4343 0.3698 0.3886 -0.0946 0.1294  -0.0688 316 ILE C CA  
10796 C C   . ILE C  316 ? 0.5023 0.4335 0.4519 -0.1049 0.1344  -0.0781 316 ILE C C   
10797 O O   . ILE C  316 ? 0.4856 0.4231 0.4367 -0.1120 0.1360  -0.0830 316 ILE C O   
10798 C CB  . ILE C  316 ? 0.4030 0.3558 0.3609 -0.0926 0.1225  -0.0671 316 ILE C CB  
10799 C CG1 . ILE C  316 ? 0.4903 0.4477 0.4442 -0.0966 0.1209  -0.0716 316 ILE C CG1 
10800 C CG2 . ILE C  316 ? 0.3337 0.2898 0.2945 -0.0830 0.1177  -0.0591 316 ILE C CG2 
10801 C CD1 . ILE C  316 ? 0.5376 0.5112 0.4940 -0.0951 0.1153  -0.0706 316 ILE C CD1 
10802 N N   . ASN C  317 ? 0.5992 0.5208 0.5433 -0.1063 0.1369  -0.0806 317 ASN C N   
10803 C CA  . ASN C  317 ? 0.6379 0.5546 0.5762 -0.1169 0.1420  -0.0900 317 ASN C CA  
10804 C C   . ASN C  317 ? 0.6211 0.5217 0.5559 -0.1215 0.1509  -0.0944 317 ASN C C   
10805 O O   . ASN C  317 ? 0.6097 0.5088 0.5404 -0.1316 0.1554  -0.1032 317 ASN C O   
10806 C CB  . ASN C  317 ? 0.7891 0.7018 0.7223 -0.1170 0.1420  -0.0908 317 ASN C CB  
10807 C CG  . ASN C  317 ? 0.8436 0.7694 0.7742 -0.1240 0.1390  -0.0960 317 ASN C CG  
10808 O OD1 . ASN C  317 ? 0.9025 0.8332 0.8322 -0.1339 0.1411  -0.1037 317 ASN C OD1 
10809 N ND2 . ASN C  317 ? 0.8088 0.7410 0.7376 -0.1190 0.1342  -0.0920 317 ASN C ND2 
10810 N N   . THR C  318 ? 0.7584 0.6475 0.6941 -0.1142 0.1536  -0.0885 318 THR C N   
10811 C CA  . THR C  318 ? 0.8074 0.6785 0.7383 -0.1170 0.1632  -0.0917 318 THR C CA  
10812 C C   . THR C  318 ? 0.9329 0.8044 0.8675 -0.1145 0.1645  -0.0871 318 THR C C   
10813 O O   . THR C  318 ? 1.0116 0.8813 0.9445 -0.1217 0.1693  -0.0915 318 THR C O   
10814 C CB  . THR C  318 ? 0.5509 0.4044 0.4784 -0.1116 0.1682  -0.0891 318 THR C CB  
10815 O OG1 . THR C  318 ? 0.5248 0.3788 0.4572 -0.1013 0.1658  -0.0795 318 THR C OG1 
10816 C CG2 . THR C  318 ? 0.5166 0.3732 0.4432 -0.1116 0.1650  -0.0891 318 THR C CG2 
10817 N N   . GLY C  319 ? 0.7886 0.6632 0.7282 -0.1049 0.1602  -0.0778 319 GLY C N   
10818 C CA  . GLY C  319 ? 0.8090 0.6791 0.7504 -0.1015 0.1629  -0.0722 319 GLY C CA  
10819 C C   . GLY C  319 ? 0.8106 0.6904 0.7555 -0.1071 0.1624  -0.0727 319 GLY C C   
10820 O O   . GLY C  319 ? 0.7465 0.6393 0.6938 -0.1134 0.1592  -0.0776 319 GLY C O   
10821 N N   . ASP C  320 ? 1.0648 0.9385 1.0101 -0.1051 0.1659  -0.0676 320 ASP C N   
10822 C CA  . ASP C  320 ? 1.1218 1.0028 1.0703 -0.1114 0.1668  -0.0678 320 ASP C CA  
10823 C C   . ASP C  320 ? 1.1006 0.9997 1.0566 -0.1075 0.1597  -0.0618 320 ASP C C   
10824 O O   . ASP C  320 ? 1.1083 1.0076 1.0654 -0.0994 0.1574  -0.0543 320 ASP C O   
10825 C CB  . ASP C  320 ? 1.0723 0.9368 1.0164 -0.1140 0.1755  -0.0662 320 ASP C CB  
10826 C CG  . ASP C  320 ? 1.0839 0.9540 1.0304 -0.1243 0.1778  -0.0694 320 ASP C CG  
10827 O OD1 . ASP C  320 ? 1.0652 0.9506 1.0159 -0.1303 0.1738  -0.0748 320 ASP C OD1 
10828 O OD2 . ASP C  320 ? 1.1072 0.9669 1.0515 -0.1267 0.1836  -0.0663 320 ASP C OD2 
10829 N N   . PHE C  321 ? 0.9298 0.8448 0.8907 -0.1135 0.1565  -0.0658 321 PHE C N   
10830 C CA  . PHE C  321 ? 0.8487 0.7823 0.8168 -0.1111 0.1508  -0.0618 321 PHE C CA  
10831 C C   . PHE C  321 ? 0.8899 0.8304 0.8624 -0.1169 0.1538  -0.0608 321 PHE C C   
10832 O O   . PHE C  321 ? 0.9065 0.8647 0.8857 -0.1167 0.1499  -0.0597 321 PHE C O   
10833 C CB  . PHE C  321 ? 0.6626 0.6114 0.6342 -0.1107 0.1443  -0.0652 321 PHE C CB  
10834 C CG  . PHE C  321 ? 0.5739 0.5171 0.5419 -0.1036 0.1407  -0.0636 321 PHE C CG  
10835 C CD1 . PHE C  321 ? 0.5149 0.4570 0.4833 -0.0940 0.1375  -0.0559 321 PHE C CD1 
10836 C CD2 . PHE C  321 ? 0.5520 0.4913 0.5160 -0.1071 0.1410  -0.0698 321 PHE C CD2 
10837 C CE1 . PHE C  321 ? 0.4933 0.4314 0.4593 -0.0882 0.1344  -0.0542 321 PHE C CE1 
10838 C CE2 . PHE C  321 ? 0.5141 0.4487 0.4753 -0.1009 0.1381  -0.0676 321 PHE C CE2 
10839 C CZ  . PHE C  321 ? 0.4791 0.4135 0.4418 -0.0915 0.1347  -0.0598 321 PHE C CZ  
10840 N N   . GLN C  322 ? 0.8846 0.8112 0.8533 -0.1223 0.1610  -0.0616 322 GLN C N   
10841 C CA  . GLN C  322 ? 0.9364 0.8677 0.9087 -0.1302 0.1649  -0.0614 322 GLN C CA  
10842 C C   . GLN C  322 ? 0.9479 0.8945 0.9266 -0.1267 0.1623  -0.0549 322 GLN C C   
10843 O O   . GLN C  322 ? 0.9425 0.9048 0.9282 -0.1326 0.1619  -0.0570 322 GLN C O   
10844 C CB  . GLN C  322 ? 1.0211 0.9309 0.9865 -0.1333 0.1731  -0.0598 322 GLN C CB  
10845 C CG  . GLN C  322 ? 1.0623 0.9590 1.0224 -0.1415 0.1784  -0.0679 322 GLN C CG  
10846 C CD  . GLN C  322 ? 1.0847 0.9926 1.0498 -0.1538 0.1793  -0.0744 322 GLN C CD  
10847 O OE1 . GLN C  322 ? 1.0847 0.9995 1.0506 -0.1590 0.1773  -0.0823 322 GLN C OE1 
10848 N NE2 . GLN C  322 ? 1.0868 0.9975 1.0556 -0.1590 0.1825  -0.0709 322 GLN C NE2 
10849 N N   . ASP C  323 ? 1.0270 0.9694 1.0032 -0.1174 0.1609  -0.0473 323 ASP C N   
10850 C CA  . ASP C  323 ? 1.0455 0.9988 1.0253 -0.1143 0.1603  -0.0407 323 ASP C CA  
10851 C C   . ASP C  323 ? 0.9288 0.9005 0.9138 -0.1075 0.1531  -0.0392 323 ASP C C   
10852 O O   . ASP C  323 ? 0.9530 0.9343 0.9402 -0.1037 0.1524  -0.0341 323 ASP C O   
10853 C CB  . ASP C  323 ? 1.3926 1.3312 1.3656 -0.1089 0.1637  -0.0331 323 ASP C CB  
10854 C CG  . ASP C  323 ? 1.4732 1.3959 1.4399 -0.1028 0.1632  -0.0329 323 ASP C CG  
10855 O OD1 . ASP C  323 ? 1.4661 1.3942 1.4342 -0.0984 0.1575  -0.0352 323 ASP C OD1 
10856 O OD2 . ASP C  323 ? 1.5117 1.4165 1.4720 -0.1024 0.1689  -0.0301 323 ASP C OD2 
10857 N N   . LEU C  324 ? 0.7092 0.6852 0.6953 -0.1061 0.1483  -0.0439 324 LEU C N   
10858 C CA  . LEU C  324 ? 0.5883 0.5769 0.5771 -0.0983 0.1415  -0.0421 324 LEU C CA  
10859 C C   . LEU C  324 ? 0.5039 0.5129 0.5007 -0.1011 0.1391  -0.0457 324 LEU C C   
10860 O O   . LEU C  324 ? 0.5030 0.5167 0.5026 -0.1083 0.1395  -0.0525 324 LEU C O   
10861 C CB  . LEU C  324 ? 0.4925 0.4738 0.4777 -0.0947 0.1378  -0.0444 324 LEU C CB  
10862 C CG  . LEU C  324 ? 0.2524 0.2406 0.2379 -0.0857 0.1313  -0.0411 324 LEU C CG  
10863 C CD1 . LEU C  324 ? 0.2978 0.2812 0.2803 -0.0787 0.1314  -0.0337 324 LEU C CD1 
10864 C CD2 . LEU C  324 ? 0.2478 0.2295 0.2302 -0.0844 0.1284  -0.0441 324 LEU C CD2 
10865 N N   . GLN C  325 ? 0.3776 0.3993 0.3778 -0.0952 0.1368  -0.0418 325 GLN C N   
10866 C CA  . GLN C  325 ? 0.3460 0.3873 0.3536 -0.0954 0.1339  -0.0453 325 GLN C CA  
10867 C C   . GLN C  325 ? 0.2979 0.3422 0.3040 -0.0869 0.1278  -0.0446 325 GLN C C   
10868 O O   . GLN C  325 ? 0.2897 0.3283 0.2913 -0.0791 0.1259  -0.0392 325 GLN C O   
10869 C CB  . GLN C  325 ? 0.5136 0.5699 0.5275 -0.0957 0.1366  -0.0431 325 GLN C CB  
10870 C CG  . GLN C  325 ? 0.5975 0.6502 0.6125 -0.1039 0.1430  -0.0425 325 GLN C CG  
10871 C CD  . GLN C  325 ? 0.6604 0.7057 0.6704 -0.0995 0.1460  -0.0347 325 GLN C CD  
10872 O OE1 . GLN C  325 ? 0.6755 0.7329 0.6889 -0.0973 0.1478  -0.0315 325 GLN C OE1 
10873 N NE2 . GLN C  325 ? 0.6654 0.6917 0.6672 -0.0976 0.1468  -0.0317 325 GLN C NE2 
10874 N N   . VAL C  326 ? 0.2344 0.2879 0.2438 -0.0890 0.1250  -0.0501 326 VAL C N   
10875 C CA  . VAL C  326 ? 0.2236 0.2786 0.2309 -0.0822 0.1198  -0.0499 326 VAL C CA  
10876 C C   . VAL C  326 ? 0.2192 0.2940 0.2335 -0.0826 0.1178  -0.0543 326 VAL C C   
10877 O O   . VAL C  326 ? 0.2235 0.3076 0.2427 -0.0902 0.1188  -0.0603 326 VAL C O   
10878 C CB  . VAL C  326 ? 0.2528 0.2948 0.2544 -0.0841 0.1182  -0.0523 326 VAL C CB  
10879 C CG1 . VAL C  326 ? 0.2145 0.2612 0.2149 -0.0792 0.1133  -0.0531 326 VAL C CG1 
10880 C CG2 . VAL C  326 ? 0.2261 0.2501 0.2212 -0.0810 0.1194  -0.0474 326 VAL C CG2 
10881 N N   . LEU C  327 ? 0.2343 0.3162 0.2492 -0.0741 0.1152  -0.0518 327 LEU C N   
10882 C CA  . LEU C  327 ? 0.2320 0.3320 0.2526 -0.0718 0.1129  -0.0558 327 LEU C CA  
10883 C C   . LEU C  327 ? 0.2299 0.3241 0.2445 -0.0664 0.1085  -0.0558 327 LEU C C   
10884 O O   . LEU C  327 ? 0.2050 0.2885 0.2135 -0.0596 0.1069  -0.0510 327 LEU C O   
10885 C CB  . LEU C  327 ? 0.2058 0.3174 0.2307 -0.0657 0.1143  -0.0535 327 LEU C CB  
10886 C CG  . LEU C  327 ? 0.2005 0.3269 0.2289 -0.0585 0.1116  -0.0559 327 LEU C CG  
10887 C CD1 . LEU C  327 ? 0.4331 0.5776 0.4697 -0.0636 0.1104  -0.0630 327 LEU C CD1 
10888 C CD2 . LEU C  327 ? 0.2021 0.3371 0.2336 -0.0528 0.1141  -0.0535 327 LEU C CD2 
10889 N N   . VAL C  328 ? 0.2770 0.3786 0.2930 -0.0702 0.1066  -0.0613 328 VAL C N   
10890 C CA  . VAL C  328 ? 0.2943 0.3916 0.3042 -0.0662 0.1030  -0.0617 328 VAL C CA  
10891 C C   . VAL C  328 ? 0.3018 0.4191 0.3162 -0.0635 0.1007  -0.0666 328 VAL C C   
10892 O O   . VAL C  328 ? 0.2999 0.4364 0.3234 -0.0671 0.1013  -0.0714 328 VAL C O   
10893 C CB  . VAL C  328 ? 0.1988 0.2858 0.2034 -0.0727 0.1027  -0.0639 328 VAL C CB  
10894 C CG1 . VAL C  328 ? 0.2017 0.2689 0.2015 -0.0742 0.1047  -0.0598 328 VAL C CG1 
10895 C CG2 . VAL C  328 ? 0.2037 0.3051 0.2139 -0.0818 0.1037  -0.0713 328 VAL C CG2 
10896 N N   . GLY C  329 ? 0.1905 0.3044 0.1986 -0.0572 0.0979  -0.0659 329 GLY C N   
10897 C CA  . GLY C  329 ? 0.1899 0.3235 0.2013 -0.0541 0.0955  -0.0712 329 GLY C CA  
10898 C C   . GLY C  329 ? 0.1896 0.3168 0.1912 -0.0471 0.0926  -0.0705 329 GLY C C   
10899 O O   . GLY C  329 ? 0.1890 0.2965 0.1823 -0.0446 0.0926  -0.0654 329 GLY C O   
10900 N N   . VAL C  330 ? 0.3317 0.4766 0.3341 -0.0435 0.0899  -0.0758 330 VAL C N   
10901 C CA  . VAL C  330 ? 0.3360 0.4696 0.3268 -0.0356 0.0840  -0.0733 330 VAL C CA  
10902 C C   . VAL C  330 ? 0.3465 0.4914 0.3405 -0.0233 0.0773  -0.0739 330 VAL C C   
10903 O O   . VAL C  330 ? 0.3802 0.5456 0.3864 -0.0216 0.0780  -0.0774 330 VAL C O   
10904 C CB  . VAL C  330 ? 0.2007 0.3293 0.1836 -0.0402 0.0796  -0.0737 330 VAL C CB  
10905 C CG1 . VAL C  330 ? 0.1991 0.3223 0.1819 -0.0525 0.0865  -0.0753 330 VAL C CG1 
10906 C CG2 . VAL C  330 ? 0.2053 0.3541 0.1937 -0.0378 0.0720  -0.0776 330 VAL C CG2 
10907 N N   . VAL C  331 ? 0.3051 0.4365 0.2885 -0.0147 0.0713  -0.0705 331 VAL C N   
10908 C CA  . VAL C  331 ? 0.3039 0.4436 0.2892 -0.0020 0.0646  -0.0709 331 VAL C CA  
10909 C C   . VAL C  331 ? 0.3683 0.5102 0.3480 0.0016  0.0554  -0.0704 331 VAL C C   
10910 O O   . VAL C  331 ? 0.4163 0.5472 0.3866 -0.0047 0.0542  -0.0685 331 VAL C O   
10911 C CB  . VAL C  331 ? 0.2420 0.3640 0.2194 0.0069  0.0645  -0.0676 331 VAL C CB  
10912 C CG1 . VAL C  331 ? 0.2490 0.3668 0.2293 0.0025  0.0733  -0.0675 331 VAL C CG1 
10913 C CG2 . VAL C  331 ? 0.2204 0.3185 0.1823 0.0074  0.0606  -0.0627 331 VAL C CG2 
10914 N N   . LYS C  332 ? 0.3345 0.4913 0.3196 0.0122  0.0489  -0.0720 332 LYS C N   
10915 C CA  . LYS C  332 ? 0.3482 0.5138 0.3308 0.0160  0.0396  -0.0722 332 LYS C CA  
10916 C C   . LYS C  332 ? 0.3457 0.4877 0.3100 0.0156  0.0355  -0.0670 332 LYS C C   
10917 O O   . LYS C  332 ? 0.3975 0.5410 0.3573 0.0082  0.0336  -0.0675 332 LYS C O   
10918 C CB  . LYS C  332 ? 0.4657 0.6453 0.4543 0.0309  0.0329  -0.0733 332 LYS C CB  
10919 C CG  . LYS C  332 ? 0.4965 0.6970 0.4895 0.0343  0.0238  -0.0754 332 LYS C CG  
10920 C CD  . LYS C  332 ? 0.5257 0.7318 0.5193 0.0519  0.0157  -0.0743 332 LYS C CD  
10921 C CE  . LYS C  332 ? 0.5570 0.7920 0.5605 0.0559  0.0073  -0.0776 332 LYS C CE  
10922 N NZ  . LYS C  332 ? 0.5807 0.8166 0.5772 0.0459  0.0031  -0.0775 332 LYS C NZ  
10923 N N   . ASP C  333 ? 0.2692 0.3891 0.2224 0.0226  0.0345  -0.0622 333 ASP C N   
10924 C CA  . ASP C  333 ? 0.2882 0.3850 0.2241 0.0204  0.0322  -0.0568 333 ASP C CA  
10925 C C   . ASP C  333 ? 0.2800 0.3553 0.2096 0.0141  0.0395  -0.0539 333 ASP C C   
10926 O O   . ASP C  333 ? 0.3317 0.3929 0.2572 0.0201  0.0398  -0.0514 333 ASP C O   
10927 C CB  . ASP C  333 ? 0.4100 0.4971 0.3359 0.0334  0.0234  -0.0527 333 ASP C CB  
10928 C CG  . ASP C  333 ? 0.4899 0.5998 0.4260 0.0440  0.0170  -0.0560 333 ASP C CG  
10929 O OD1 . ASP C  333 ? 0.5106 0.6289 0.4571 0.0505  0.0193  -0.0589 333 ASP C OD1 
10930 O OD2 . ASP C  333 ? 0.5253 0.6459 0.4593 0.0460  0.0097  -0.0560 333 ASP C OD2 
10931 N N   . GLU C  334 ? 0.2474 0.3196 0.1754 0.0023  0.0447  -0.0541 334 GLU C N   
10932 C CA  . GLU C  334 ? 0.2417 0.2970 0.1658 -0.0044 0.0520  -0.0517 334 GLU C CA  
10933 C C   . GLU C  334 ? 0.2517 0.2845 0.1605 -0.0044 0.0502  -0.0458 334 GLU C C   
10934 O O   . GLU C  334 ? 0.2494 0.2676 0.1550 -0.0068 0.0544  -0.0432 334 GLU C O   
10935 C CB  . GLU C  334 ? 0.4154 0.4770 0.3448 -0.0162 0.0588  -0.0546 334 GLU C CB  
10936 C CG  . GLU C  334 ? 0.4592 0.5392 0.4035 -0.0188 0.0630  -0.0597 334 GLU C CG  
10937 C CD  . GLU C  334 ? 0.5201 0.5935 0.4685 -0.0202 0.0703  -0.0589 334 GLU C CD  
10938 O OE1 . GLU C  334 ? 0.5201 0.5756 0.4604 -0.0197 0.0717  -0.0548 334 GLU C OE1 
10939 O OE2 . GLU C  334 ? 0.5732 0.6598 0.5327 -0.0222 0.0747  -0.0622 334 GLU C OE2 
10940 N N   . GLY C  335 ? 0.2637 0.2943 0.1628 -0.0023 0.0440  -0.0436 335 GLY C N   
10941 C CA  . GLY C  335 ? 0.2743 0.2845 0.1584 -0.0041 0.0433  -0.0378 335 GLY C CA  
10942 C C   . GLY C  335 ? 0.3324 0.3259 0.2082 0.0046  0.0389  -0.0331 335 GLY C C   
10943 O O   . GLY C  335 ? 0.3717 0.3462 0.2382 0.0015  0.0409  -0.0286 335 GLY C O   
10944 N N   . SER C  336 ? 0.3192 0.3195 0.1985 0.0155  0.0330  -0.0345 336 SER C N   
10945 C CA  . SER C  336 ? 0.3376 0.3208 0.2066 0.0252  0.0273  -0.0300 336 SER C CA  
10946 C C   . SER C  336 ? 0.3801 0.3427 0.2449 0.0233  0.0311  -0.0276 336 SER C C   
10947 O O   . SER C  336 ? 0.4039 0.3457 0.2554 0.0235  0.0291  -0.0221 336 SER C O   
10948 C CB  . SER C  336 ? 0.3123 0.3076 0.1879 0.0381  0.0213  -0.0329 336 SER C CB  
10949 O OG  . SER C  336 ? 0.4334 0.4496 0.3257 0.0371  0.0255  -0.0393 336 SER C OG  
10950 N N   . TYR C  337 ? 0.5131 0.4815 0.3887 0.0209  0.0368  -0.0315 337 TYR C N   
10951 C CA  . TYR C  337 ? 0.5560 0.5071 0.4284 0.0184  0.0402  -0.0299 337 TYR C CA  
10952 C C   . TYR C  337 ? 0.5034 0.4377 0.3654 0.0092  0.0425  -0.0245 337 TYR C C   
10953 O O   . TYR C  337 ? 0.5166 0.4310 0.3693 0.0098  0.0409  -0.0208 337 TYR C O   
10954 C CB  . TYR C  337 ? 0.6141 0.5765 0.4992 0.0148  0.0467  -0.0346 337 TYR C CB  
10955 C CG  . TYR C  337 ? 0.6243 0.5722 0.5072 0.0140  0.0490  -0.0341 337 TYR C CG  
10956 C CD1 . TYR C  337 ? 0.6396 0.5754 0.5182 0.0050  0.0526  -0.0309 337 TYR C CD1 
10957 C CD2 . TYR C  337 ? 0.6745 0.6219 0.5599 0.0223  0.0477  -0.0374 337 TYR C CD2 
10958 C CE1 . TYR C  337 ? 0.7076 0.6316 0.5847 0.0037  0.0540  -0.0308 337 TYR C CE1 
10959 C CE2 . TYR C  337 ? 0.7466 0.6807 0.6290 0.0213  0.0493  -0.0376 337 TYR C CE2 
10960 C CZ  . TYR C  337 ? 0.7799 0.7025 0.6583 0.0116  0.0521  -0.0342 337 TYR C CZ  
10961 O OH  . TYR C  337 ? 0.8250 0.7357 0.7009 0.0099  0.0530  -0.0348 337 TYR C OH  
10962 N N   . PHE C  338 ? 0.3562 0.2986 0.2196 0.0008  0.0463  -0.0244 338 PHE C N   
10963 C CA  . PHE C  338 ? 0.3443 0.2748 0.2008 -0.0086 0.0504  -0.0203 338 PHE C CA  
10964 C C   . PHE C  338 ? 0.3970 0.3135 0.2381 -0.0080 0.0462  -0.0143 338 PHE C C   
10965 O O   . PHE C  338 ? 0.4019 0.3057 0.2356 -0.0149 0.0493  -0.0100 338 PHE C O   
10966 C CB  . PHE C  338 ? 0.3964 0.3398 0.2595 -0.0172 0.0567  -0.0228 338 PHE C CB  
10967 C CG  . PHE C  338 ? 0.4445 0.3997 0.3214 -0.0187 0.0616  -0.0276 338 PHE C CG  
10968 C CD1 . PHE C  338 ? 0.4529 0.4251 0.3391 -0.0147 0.0604  -0.0324 338 PHE C CD1 
10969 C CD2 . PHE C  338 ? 0.4661 0.4162 0.3466 -0.0241 0.0672  -0.0269 338 PHE C CD2 
10970 C CE1 . PHE C  338 ? 0.4454 0.4275 0.3431 -0.0165 0.0655  -0.0362 338 PHE C CE1 
10971 C CE2 . PHE C  338 ? 0.4635 0.4235 0.3552 -0.0251 0.0716  -0.0306 338 PHE C CE2 
10972 C CZ  . PHE C  338 ? 0.4646 0.4398 0.3644 -0.0214 0.0710  -0.0350 338 PHE C CZ  
10973 N N   . LEU C  339 ? 0.5579 0.4774 0.3940 0.0003  0.0392  -0.0138 339 LEU C N   
10974 C CA  . LEU C  339 ? 0.5863 0.4925 0.4061 0.0016  0.0348  -0.0076 339 LEU C CA  
10975 C C   . LEU C  339 ? 0.6301 0.5111 0.4390 0.0031  0.0332  -0.0019 339 LEU C C   
10976 O O   . LEU C  339 ? 0.6778 0.5444 0.4748 -0.0029 0.0348  0.0039  339 LEU C O   
10977 C CB  . LEU C  339 ? 0.4806 0.3965 0.2979 0.0114  0.0268  -0.0082 339 LEU C CB  
10978 C CG  . LEU C  339 ? 0.4398 0.3790 0.2646 0.0081  0.0274  -0.0131 339 LEU C CG  
10979 C CD1 . LEU C  339 ? 0.4605 0.4106 0.2835 0.0183  0.0185  -0.0137 339 LEU C CD1 
10980 C CD2 . LEU C  339 ? 0.4205 0.3564 0.2367 -0.0023 0.0319  -0.0108 339 LEU C CD2 
10981 N N   . VAL C  340 ? 0.5662 0.4417 0.3791 0.0103  0.0308  -0.0040 340 VAL C N   
10982 C CA  . VAL C  340 ? 0.5525 0.4028 0.3548 0.0124  0.0285  0.0004  340 VAL C CA  
10983 C C   . VAL C  340 ? 0.6166 0.4572 0.4196 0.0007  0.0351  0.0019  340 VAL C C   
10984 O O   . VAL C  340 ? 0.7047 0.5242 0.4994 -0.0011 0.0344  0.0055  340 VAL C O   
10985 C CB  . VAL C  340 ? 0.4023 0.2496 0.2087 0.0234  0.0246  -0.0034 340 VAL C CB  
10986 C CG1 . VAL C  340 ? 0.3884 0.2495 0.1970 0.0356  0.0184  -0.0055 340 VAL C CG1 
10987 C CG2 . VAL C  340 ? 0.3682 0.2267 0.1890 0.0200  0.0299  -0.0097 340 VAL C CG2 
10988 N N   . TYR C  341 ? 0.5455 0.4019 0.3587 -0.0074 0.0413  -0.0010 341 TYR C N   
10989 C CA  . TYR C  341 ? 0.5548 0.4065 0.3707 -0.0183 0.0478  0.0002  341 TYR C CA  
10990 C C   . TYR C  341 ? 0.5759 0.4203 0.3822 -0.0272 0.0511  0.0062  341 TYR C C   
10991 O O   . TYR C  341 ? 0.5467 0.3937 0.3579 -0.0365 0.0575  0.0065  341 TYR C O   
10992 C CB  . TYR C  341 ? 0.5513 0.4208 0.3830 -0.0216 0.0530  -0.0056 341 TYR C CB  
10993 C CG  . TYR C  341 ? 0.5797 0.4469 0.4176 -0.0169 0.0516  -0.0095 341 TYR C CG  
10994 C CD1 . TYR C  341 ? 0.6187 0.4931 0.4604 -0.0066 0.0476  -0.0137 341 TYR C CD1 
10995 C CD2 . TYR C  341 ? 0.5726 0.4311 0.4122 -0.0227 0.0541  -0.0092 341 TYR C CD2 
10996 C CE1 . TYR C  341 ? 0.6223 0.4946 0.4685 -0.0021 0.0468  -0.0176 341 TYR C CE1 
10997 C CE2 . TYR C  341 ? 0.5818 0.4378 0.4255 -0.0186 0.0525  -0.0131 341 TYR C CE2 
10998 C CZ  . TYR C  341 ? 0.6117 0.4740 0.4580 -0.0082 0.0492  -0.0174 341 TYR C CZ  
10999 O OH  . TYR C  341 ? 0.6236 0.4832 0.4727 -0.0039 0.0481  -0.0216 341 TYR C OH  
11000 N N   . GLY C  342 ? 0.7727 0.6085 0.5653 -0.0240 0.0470  0.0110  342 GLY C N   
11001 C CA  . GLY C  342 ? 0.8251 0.6519 0.6062 -0.0322 0.0504  0.0173  342 GLY C CA  
11002 C C   . GLY C  342 ? 0.8322 0.6682 0.6063 -0.0333 0.0510  0.0188  342 GLY C C   
11003 O O   . GLY C  342 ? 0.8960 0.7280 0.6626 -0.0414 0.0559  0.0229  342 GLY C O   
11004 N N   . VAL C  343 ? 0.5821 0.4314 0.3588 -0.0256 0.0463  0.0149  343 VAL C N   
11005 C CA  . VAL C  343 ? 0.5177 0.3680 0.2812 -0.0229 0.0424  0.0181  343 VAL C CA  
11006 C C   . VAL C  343 ? 0.5197 0.3493 0.2687 -0.0154 0.0353  0.0247  343 VAL C C   
11007 O O   . VAL C  343 ? 0.4913 0.3159 0.2448 -0.0075 0.0309  0.0231  343 VAL C O   
11008 C CB  . VAL C  343 ? 0.4931 0.3650 0.2645 -0.0169 0.0385  0.0118  343 VAL C CB  
11009 C CG1 . VAL C  343 ? 0.4892 0.3607 0.2458 -0.0112 0.0314  0.0154  343 VAL C CG1 
11010 C CG2 . VAL C  343 ? 0.4870 0.3759 0.2694 -0.0251 0.0457  0.0060  343 VAL C CG2 
11011 N N   . PRO C  344 ? 0.5774 0.3935 0.3083 -0.0179 0.0348  0.0324  344 PRO C N   
11012 C CA  . PRO C  344 ? 0.5966 0.3903 0.3111 -0.0109 0.0282  0.0398  344 PRO C CA  
11013 C C   . PRO C  344 ? 0.6241 0.4255 0.3367 0.0029  0.0186  0.0384  344 PRO C C   
11014 O O   . PRO C  344 ? 0.6294 0.4524 0.3474 0.0044  0.0172  0.0338  344 PRO C O   
11015 C CB  . PRO C  344 ? 0.5199 0.3028 0.2159 -0.0181 0.0312  0.0479  344 PRO C CB  
11016 C CG  . PRO C  344 ? 0.5092 0.3022 0.2142 -0.0307 0.0412  0.0450  344 PRO C CG  
11017 C CD  . PRO C  344 ? 0.4968 0.3147 0.2210 -0.0287 0.0419  0.0350  344 PRO C CD  
11018 N N   . GLY C  345 ? 0.6109 0.3947 0.3164 0.0127  0.0122  0.0420  345 GLY C N   
11019 C CA  . GLY C  345 ? 0.6306 0.4198 0.3336 0.0274  0.0026  0.0416  345 GLY C CA  
11020 C C   . GLY C  345 ? 0.6442 0.4457 0.3648 0.0364  -0.0001 0.0337  345 GLY C C   
11021 O O   . GLY C  345 ? 0.6533 0.4556 0.3724 0.0502  -0.0081 0.0337  345 GLY C O   
11022 N N   . PHE C  346 ? 0.7838 0.5954 0.5209 0.0292  0.0066  0.0270  346 PHE C N   
11023 C CA  . PHE C  346 ? 0.8175 0.6445 0.5722 0.0363  0.0055  0.0189  346 PHE C CA  
11024 C C   . PHE C  346 ? 0.9162 0.7259 0.6734 0.0375  0.0072  0.0177  346 PHE C C   
11025 O O   . PHE C  346 ? 0.9701 0.7684 0.7266 0.0268  0.0132  0.0190  346 PHE C O   
11026 C CB  . PHE C  346 ? 0.6049 0.4586 0.3767 0.0287  0.0113  0.0114  346 PHE C CB  
11027 C CG  . PHE C  346 ? 0.5535 0.4273 0.3255 0.0288  0.0088  0.0101  346 PHE C CG  
11028 C CD1 . PHE C  346 ? 0.5324 0.4050 0.2947 0.0193  0.0120  0.0134  346 PHE C CD1 
11029 C CD2 . PHE C  346 ? 0.5150 0.4095 0.2966 0.0384  0.0031  0.0051  346 PHE C CD2 
11030 C CE1 . PHE C  346 ? 0.5022 0.3926 0.2633 0.0192  0.0092  0.0115  346 PHE C CE1 
11031 C CE2 . PHE C  346 ? 0.4889 0.4025 0.2707 0.0377  0.0001  0.0033  346 PHE C CE2 
11032 C CZ  . PHE C  346 ? 0.4819 0.3927 0.2528 0.0281  0.0029  0.0064  346 PHE C CZ  
11033 N N   . SER C  347 ? 0.8281 0.6373 0.5887 0.0508  0.0018  0.0148  347 SER C N   
11034 C CA  . SER C  347 ? 0.7955 0.5879 0.5573 0.0539  0.0024  0.0126  347 SER C CA  
11035 C C   . SER C  347 ? 0.7494 0.5572 0.5237 0.0666  -0.0005 0.0053  347 SER C C   
11036 O O   . SER C  347 ? 0.7470 0.5709 0.5246 0.0765  -0.0056 0.0042  347 SER C O   
11037 C CB  . SER C  347 ? 0.8869 0.6461 0.6294 0.0582  -0.0018 0.0202  347 SER C CB  
11038 O OG  . SER C  347 ? 0.9200 0.6625 0.6632 0.0617  -0.0017 0.0170  347 SER C OG  
11039 N N   . LYS C  348 ? 0.7642 0.5676 0.5455 0.0663  0.0027  0.0002  348 LYS C N   
11040 C CA  . LYS C  348 ? 0.7223 0.5403 0.5156 0.0775  0.0014  -0.0072 348 LYS C CA  
11041 C C   . LYS C  348 ? 0.7543 0.5588 0.5387 0.0942  -0.0063 -0.0056 348 LYS C C   
11042 O O   . LYS C  348 ? 0.7442 0.5636 0.5378 0.1064  -0.0086 -0.0110 348 LYS C O   
11043 C CB  . LYS C  348 ? 0.6004 0.4140 0.4001 0.0727  0.0067  -0.0127 348 LYS C CB  
11044 C CG  . LYS C  348 ? 0.5704 0.3509 0.3569 0.0743  0.0049  -0.0108 348 LYS C CG  
11045 C CD  . LYS C  348 ? 0.5095 0.2892 0.3030 0.0716  0.0091  -0.0177 348 LYS C CD  
11046 C CE  . LYS C  348 ? 0.5121 0.2777 0.3010 0.0855  0.0053  -0.0218 348 LYS C CE  
11047 N NZ  . LYS C  348 ? 0.5657 0.2965 0.3363 0.0878  0.0008  -0.0161 348 LYS C NZ  
11048 N N   . ASP C  349 ? 0.7626 0.5390 0.5289 0.0949  -0.0099 0.0020  349 ASP C N   
11049 C CA  . ASP C  349 ? 0.8170 0.5732 0.5723 0.1106  -0.0167 0.0042  349 ASP C CA  
11050 C C   . ASP C  349 ? 0.8459 0.6120 0.5975 0.1231  -0.0243 0.0081  349 ASP C C   
11051 O O   . ASP C  349 ? 0.8684 0.6471 0.6272 0.1384  -0.0285 0.0039  349 ASP C O   
11052 C CB  . ASP C  349 ? 0.8481 0.5655 0.5854 0.1056  -0.0167 0.0101  349 ASP C CB  
11053 C CG  . ASP C  349 ? 0.8888 0.5959 0.6303 0.0989  -0.0116 0.0042  349 ASP C CG  
11054 O OD1 . ASP C  349 ? 0.9154 0.6134 0.6569 0.1103  -0.0138 -0.0008 349 ASP C OD1 
11055 O OD2 . ASP C  349 ? 0.8786 0.5883 0.6239 0.0830  -0.0057 0.0042  349 ASP C OD2 
11056 N N   . ASN C  350 ? 0.7855 0.5467 0.5258 0.1170  -0.0259 0.0159  350 ASN C N   
11057 C CA  . ASN C  350 ? 0.7888 0.5608 0.5246 0.1280  -0.0337 0.0199  350 ASN C CA  
11058 C C   . ASN C  350 ? 0.7652 0.5774 0.5177 0.1261  -0.0337 0.0147  350 ASN C C   
11059 O O   . ASN C  350 ? 0.6804 0.5120 0.4479 0.1159  -0.0270 0.0084  350 ASN C O   
11060 C CB  . ASN C  350 ? 0.7752 0.5230 0.4889 0.1236  -0.0362 0.0309  350 ASN C CB  
11061 C CG  . ASN C  350 ? 0.7539 0.5042 0.4663 0.1040  -0.0290 0.0330  350 ASN C CG  
11062 O OD1 . ASN C  350 ? 0.7143 0.4790 0.4412 0.0934  -0.0219 0.0266  350 ASN C OD1 
11063 N ND2 . ASN C  350 ? 0.7928 0.5289 0.4874 0.0994  -0.0305 0.0422  350 ASN C ND2 
11064 N N   . GLU C  351 ? 0.8752 0.6992 0.6242 0.1360  -0.0414 0.0177  351 GLU C N   
11065 C CA  . GLU C  351 ? 0.8945 0.7565 0.6588 0.1351  -0.0428 0.0126  351 GLU C CA  
11066 C C   . GLU C  351 ? 0.8587 0.7283 0.6215 0.1173  -0.0376 0.0137  351 GLU C C   
11067 O O   . GLU C  351 ? 0.8356 0.7347 0.6106 0.1131  -0.0373 0.0089  351 GLU C O   
11068 C CB  . GLU C  351 ? 1.1059 0.9772 0.8653 0.1507  -0.0536 0.0159  351 GLU C CB  
11069 C CG  . GLU C  351 ? 1.1868 1.0981 0.9677 0.1573  -0.0564 0.0078  351 GLU C CG  
11070 C CD  . GLU C  351 ? 1.3018 1.2214 1.0795 0.1760  -0.0678 0.0107  351 GLU C CD  
11071 O OE1 . GLU C  351 ? 1.3371 1.2316 1.0937 0.1823  -0.0737 0.0199  351 GLU C OE1 
11072 O OE2 . GLU C  351 ? 1.3345 1.2861 1.1310 0.1844  -0.0707 0.0040  351 GLU C OE2 
11073 N N   . SER C  352 ? 0.9696 0.8122 0.7172 0.1069  -0.0334 0.0200  352 SER C N   
11074 C CA  . SER C  352 ? 0.9033 0.7491 0.6477 0.0901  -0.0273 0.0215  352 SER C CA  
11075 C C   . SER C  352 ? 0.8933 0.7595 0.6352 0.0892  -0.0316 0.0223  352 SER C C   
11076 O O   . SER C  352 ? 0.9021 0.7890 0.6542 0.0788  -0.0269 0.0172  352 SER C O   
11077 C CB  . SER C  352 ? 0.6383 0.4977 0.4002 0.0783  -0.0180 0.0139  352 SER C CB  
11078 O OG  . SER C  352 ? 0.6156 0.4523 0.3752 0.0743  -0.0131 0.0148  352 SER C OG  
11079 N N   . LEU C  353 ? 0.7385 0.5985 0.4663 0.1002  -0.0407 0.0285  353 LEU C N   
11080 C CA  . LEU C  353 ? 0.6867 0.5625 0.4077 0.0988  -0.0455 0.0303  353 LEU C CA  
11081 C C   . LEU C  353 ? 0.6816 0.5382 0.3838 0.0858  -0.0405 0.0374  353 LEU C C   
11082 O O   . LEU C  353 ? 0.7423 0.5685 0.4285 0.0857  -0.0394 0.0454  353 LEU C O   
11083 C CB  . LEU C  353 ? 0.5560 0.4319 0.2675 0.1162  -0.0575 0.0351  353 LEU C CB  
11084 C CG  . LEU C  353 ? 0.5527 0.4442 0.2802 0.1323  -0.0633 0.0297  353 LEU C CG  
11085 C CD1 . LEU C  353 ? 0.5784 0.4723 0.2948 0.1481  -0.0755 0.0352  353 LEU C CD1 
11086 C CD2 . LEU C  353 ? 0.5210 0.4492 0.2739 0.1279  -0.0604 0.0185  353 LEU C CD2 
11087 N N   . ILE C  354 ? 0.5400 0.4138 0.2437 0.0747  -0.0372 0.0345  354 ILE C N   
11088 C CA  . ILE C  354 ? 0.5349 0.3929 0.2235 0.0611  -0.0303 0.0398  354 ILE C CA  
11089 C C   . ILE C  354 ? 0.6247 0.4855 0.2946 0.0612  -0.0356 0.0448  354 ILE C C   
11090 O O   . ILE C  354 ? 0.6114 0.4939 0.2845 0.0685  -0.0437 0.0416  354 ILE C O   
11091 C CB  . ILE C  354 ? 0.5059 0.3767 0.2094 0.0462  -0.0196 0.0324  354 ILE C CB  
11092 C CG1 . ILE C  354 ? 0.4886 0.3914 0.2042 0.0441  -0.0213 0.0239  354 ILE C CG1 
11093 C CG2 . ILE C  354 ? 0.4890 0.3560 0.2088 0.0457  -0.0144 0.0280  354 ILE C CG2 
11094 C CD1 . ILE C  354 ? 0.4610 0.3770 0.1924 0.0313  -0.0115 0.0160  354 ILE C CD1 
11095 N N   . SER C  355 ? 0.7028 0.5424 0.3530 0.0531  -0.0311 0.0528  355 SER C N   
11096 C CA  . SER C  355 ? 0.7486 0.5900 0.3790 0.0517  -0.0348 0.0577  355 SER C CA  
11097 C C   . SER C  355 ? 0.6705 0.5365 0.3101 0.0404  -0.0297 0.0490  355 SER C C   
11098 O O   . SER C  355 ? 0.6173 0.4959 0.2774 0.0338  -0.0230 0.0405  355 SER C O   
11099 C CB  . SER C  355 ? 1.1278 0.9388 0.7342 0.0455  -0.0301 0.0690  355 SER C CB  
11100 O OG  . SER C  355 ? 1.1717 0.9806 0.7823 0.0297  -0.0177 0.0667  355 SER C OG  
11101 N N   . ARG C  356 ? 0.7661 0.6379 0.3895 0.0382  -0.0327 0.0510  356 ARG C N   
11102 C CA  . ARG C  356 ? 0.7639 0.6572 0.3947 0.0275  -0.0279 0.0420  356 ARG C CA  
11103 C C   . ARG C  356 ? 0.7739 0.6548 0.4022 0.0133  -0.0145 0.0429  356 ARG C C   
11104 O O   . ARG C  356 ? 0.7813 0.6755 0.4257 0.0046  -0.0071 0.0343  356 ARG C O   
11105 C CB  . ARG C  356 ? 0.7687 0.6740 0.3832 0.0293  -0.0355 0.0424  356 ARG C CB  
11106 C CG  . ARG C  356 ? 0.7648 0.6876 0.3838 0.0169  -0.0293 0.0332  356 ARG C CG  
11107 C CD  . ARG C  356 ? 0.7912 0.7382 0.4081 0.0198  -0.0389 0.0272  356 ARG C CD  
11108 N NE  . ARG C  356 ? 0.8076 0.7690 0.4312 0.0070  -0.0316 0.0172  356 ARG C NE  
11109 C CZ  . ARG C  356 ? 0.7804 0.7631 0.4277 0.0035  -0.0303 0.0060  356 ARG C CZ  
11110 N NH1 . ARG C  356 ? 0.7507 0.7451 0.4174 0.0119  -0.0360 0.0034  356 ARG C NH1 
11111 N NH2 . ARG C  356 ? 0.7662 0.7580 0.4171 -0.0083 -0.0231 -0.0026 356 ARG C NH2 
11112 N N   . ALA C  357 ? 0.7312 0.5866 0.3400 0.0112  -0.0113 0.0534  357 ALA C N   
11113 C CA  . ALA C  357 ? 0.7087 0.5527 0.3150 -0.0021 0.0016  0.0550  357 ALA C CA  
11114 C C   . ALA C  357 ? 0.6707 0.5143 0.2999 -0.0059 0.0084  0.0502  357 ALA C C   
11115 O O   . ALA C  357 ? 0.6574 0.5060 0.2957 -0.0166 0.0185  0.0457  357 ALA C O   
11116 C CB  . ALA C  357 ? 0.8148 0.6315 0.3968 -0.0034 0.0032  0.0677  357 ALA C CB  
11117 N N   . GLN C  358 ? 0.7315 0.5695 0.3694 0.0035  0.0027  0.0511  358 GLN C N   
11118 C CA  . GLN C  358 ? 0.7158 0.5550 0.3752 0.0016  0.0076  0.0458  358 GLN C CA  
11119 C C   . GLN C  358 ? 0.6733 0.5392 0.3537 -0.0019 0.0103  0.0343  358 GLN C C   
11120 O O   . GLN C  358 ? 0.6581 0.5270 0.3517 -0.0103 0.0191  0.0299  358 GLN C O   
11121 C CB  . GLN C  358 ? 0.7316 0.5612 0.3949 0.0139  0.0001  0.0479  358 GLN C CB  
11122 C CG  . GLN C  358 ? 0.8191 0.6176 0.4676 0.0139  0.0012  0.0579  358 GLN C CG  
11123 C CD  . GLN C  358 ? 0.8699 0.6566 0.5215 0.0264  -0.0057 0.0592  358 GLN C CD  
11124 O OE1 . GLN C  358 ? 0.8572 0.6569 0.5145 0.0386  -0.0142 0.0558  358 GLN C OE1 
11125 N NE2 . GLN C  358 ? 0.8993 0.6614 0.5473 0.0233  -0.0020 0.0637  358 GLN C NE2 
11126 N N   . PHE C  359 ? 0.4992 0.3844 0.1827 0.0046  0.0025  0.0295  359 PHE C N   
11127 C CA  . PHE C  359 ? 0.4712 0.3815 0.1734 0.0007  0.0047  0.0187  359 PHE C CA  
11128 C C   . PHE C  359 ? 0.4615 0.3745 0.1612 -0.0124 0.0144  0.0157  359 PHE C C   
11129 O O   . PHE C  359 ? 0.4857 0.4079 0.2015 -0.0191 0.0216  0.0089  359 PHE C O   
11130 C CB  . PHE C  359 ? 0.4725 0.4030 0.1757 0.0085  -0.0058 0.0147  359 PHE C CB  
11131 C CG  . PHE C  359 ? 0.4522 0.4075 0.1706 0.0020  -0.0033 0.0039  359 PHE C CG  
11132 C CD1 . PHE C  359 ? 0.4280 0.3954 0.1695 0.0010  0.0002  -0.0033 359 PHE C CD1 
11133 C CD2 . PHE C  359 ? 0.4591 0.4242 0.1678 -0.0035 -0.0042 0.0009  359 PHE C CD2 
11134 C CE1 . PHE C  359 ? 0.4115 0.3996 0.1663 -0.0056 0.0028  -0.0128 359 PHE C CE1 
11135 C CE2 . PHE C  359 ? 0.6458 0.6315 0.3680 -0.0103 -0.0018 -0.0095 359 PHE C CE2 
11136 C CZ  . PHE C  359 ? 0.4190 0.4158 0.1643 -0.0114 0.0018  -0.0160 359 PHE C CZ  
11137 N N   . LEU C  360 ? 0.5369 0.4406 0.2153 -0.0155 0.0148  0.0214  360 LEU C N   
11138 C CA  . LEU C  360 ? 0.5086 0.4139 0.1814 -0.0268 0.0240  0.0191  360 LEU C CA  
11139 C C   . LEU C  360 ? 0.5156 0.4107 0.1966 -0.0351 0.0356  0.0200  360 LEU C C   
11140 O O   . LEU C  360 ? 0.4791 0.3830 0.1691 -0.0430 0.0438  0.0137  360 LEU C O   
11141 C CB  . LEU C  360 ? 0.7008 0.5963 0.3467 -0.0273 0.0219  0.0262  360 LEU C CB  
11142 C CG  . LEU C  360 ? 0.7324 0.6444 0.3697 -0.0266 0.0158  0.0210  360 LEU C CG  
11143 C CD1 . LEU C  360 ? 0.7525 0.6781 0.4005 -0.0365 0.0242  0.0108  360 LEU C CD1 
11144 C CD2 . LEU C  360 ? 0.6987 0.6256 0.3437 -0.0159 0.0031  0.0179  360 LEU C CD2 
11145 N N   . ALA C  361 ? 0.5442 0.4205 0.2218 -0.0333 0.0362  0.0278  361 ALA C N   
11146 C CA  . ALA C  361 ? 0.4989 0.3661 0.1846 -0.0410 0.0461  0.0292  361 ALA C CA  
11147 C C   . ALA C  361 ? 0.4659 0.3441 0.1760 -0.0405 0.0480  0.0216  361 ALA C C   
11148 O O   . ALA C  361 ? 0.4440 0.3269 0.1655 -0.0480 0.0568  0.0178  361 ALA C O   
11149 C CB  . ALA C  361 ? 0.4838 0.3280 0.1587 -0.0398 0.0453  0.0391  361 ALA C CB  
11150 N N   . GLY C  362 ? 0.4654 0.3477 0.1831 -0.0312 0.0398  0.0197  362 GLY C N   
11151 C CA  . GLY C  362 ? 0.4579 0.3522 0.1973 -0.0294 0.0405  0.0125  362 GLY C CA  
11152 C C   . GLY C  362 ? 0.4684 0.3822 0.2199 -0.0351 0.0453  0.0036  362 GLY C C   
11153 O O   . GLY C  362 ? 0.3989 0.3177 0.1658 -0.0388 0.0513  -0.0007 362 GLY C O   
11154 N N   . VAL C  363 ? 0.5720 0.4961 0.3158 -0.0358 0.0426  0.0009  363 VAL C N   
11155 C CA  . VAL C  363 ? 0.5462 0.4863 0.2991 -0.0421 0.0473  -0.0078 363 VAL C CA  
11156 C C   . VAL C  363 ? 0.5257 0.4600 0.2803 -0.0513 0.0588  -0.0081 363 VAL C C   
11157 O O   . VAL C  363 ? 0.4570 0.3997 0.2255 -0.0555 0.0647  -0.0143 363 VAL C O   
11158 C CB  . VAL C  363 ? 0.4020 0.3515 0.1427 -0.0423 0.0423  -0.0105 363 VAL C CB  
11159 C CG1 . VAL C  363 ? 0.3901 0.3488 0.1344 -0.0512 0.0496  -0.0182 363 VAL C CG1 
11160 C CG2 . VAL C  363 ? 0.3981 0.3616 0.1448 -0.0339 0.0316  -0.0135 363 VAL C CG2 
11161 N N   . ARG C  364 ? 0.5892 0.5088 0.3295 -0.0541 0.0621  -0.0008 364 ARG C N   
11162 C CA  . ARG C  364 ? 0.6025 0.5178 0.3440 -0.0623 0.0731  -0.0005 364 ARG C CA  
11163 C C   . ARG C  364 ? 0.6164 0.5270 0.3729 -0.0634 0.0774  0.0007  364 ARG C C   
11164 O O   . ARG C  364 ? 0.6569 0.5730 0.4312 -0.0665 0.0827  -0.0016 364 ARG C O   
11165 C CB  . ARG C  364 ? 0.6181 0.5234 0.3447 -0.0642 0.0739  0.0067  364 ARG C CB  
11166 C CG  . ARG C  364 ? 0.7033 0.6113 0.4106 -0.0621 0.0681  0.0066  364 ARG C CG  
11167 C CD  . ARG C  364 ? 0.7814 0.6969 0.4909 -0.0659 0.0724  0.0034  364 ARG C CD  
11168 N NE  . ARG C  364 ? 0.8235 0.7465 0.5558 -0.0694 0.0794  -0.0022 364 ARG C NE  
11169 C CZ  . ARG C  364 ? 0.8588 0.7868 0.5963 -0.0722 0.0843  -0.0054 364 ARG C CZ  
11170 N NH1 . ARG C  364 ? 0.8503 0.7775 0.5721 -0.0727 0.0836  -0.0041 364 ARG C NH1 
11171 N NH2 . ARG C  364 ? 0.8788 0.8120 0.6364 -0.0740 0.0894  -0.0099 364 ARG C NH2 
11172 N N   . ILE C  365 ? 0.5899 0.4942 0.3498 -0.0575 0.0713  0.0040  365 ILE C N   
11173 C CA  . ILE C  365 ? 0.5343 0.4357 0.3088 -0.0581 0.0745  0.0038  365 ILE C CA  
11174 C C   . ILE C  365 ? 0.5457 0.4616 0.3383 -0.0565 0.0751  -0.0040 365 ILE C C   
11175 O O   . ILE C  365 ? 0.5863 0.5050 0.3908 -0.0603 0.0815  -0.0063 365 ILE C O   
11176 C CB  . ILE C  365 ? 0.3686 0.2571 0.1401 -0.0524 0.0681  0.0090  365 ILE C CB  
11177 C CG1 . ILE C  365 ? 0.3908 0.2619 0.1448 -0.0550 0.0684  0.0177  365 ILE C CG1 
11178 C CG2 . ILE C  365 ? 0.3536 0.2413 0.1403 -0.0530 0.0707  0.0072  365 ILE C CG2 
11179 C CD1 . ILE C  365 ? 0.4027 0.2577 0.1523 -0.0496 0.0623  0.0229  365 ILE C CD1 
11180 N N   . GLY C  366 ? 0.4876 0.4130 0.2823 -0.0507 0.0682  -0.0078 366 GLY C N   
11181 C CA  . GLY C  366 ? 0.4110 0.3507 0.2219 -0.0495 0.0687  -0.0150 366 GLY C CA  
11182 C C   . GLY C  366 ? 0.3747 0.3231 0.1905 -0.0565 0.0760  -0.0205 366 GLY C C   
11183 O O   . GLY C  366 ? 0.4001 0.3555 0.2298 -0.0580 0.0801  -0.0249 366 GLY C O   
11184 N N   . VAL C  367 ? 0.3222 0.2692 0.1257 -0.0606 0.0780  -0.0202 367 VAL C N   
11185 C CA  . VAL C  367 ? 0.3151 0.2694 0.1290 -0.0648 0.0824  -0.0249 367 VAL C CA  
11186 C C   . VAL C  367 ? 0.3633 0.3107 0.1785 -0.0673 0.0863  -0.0207 367 VAL C C   
11187 O O   . VAL C  367 ? 0.3450 0.2921 0.1512 -0.0692 0.0867  -0.0207 367 VAL C O   
11188 C CB  . VAL C  367 ? 0.3656 0.3297 0.1728 -0.0661 0.0795  -0.0308 367 VAL C CB  
11189 C CG1 . VAL C  367 ? 0.3886 0.3605 0.2124 -0.0690 0.0827  -0.0370 367 VAL C CG1 
11190 C CG2 . VAL C  367 ? 0.3233 0.2948 0.1278 -0.0614 0.0717  -0.0326 367 VAL C CG2 
11191 N N   . PRO C  368 ? 0.3959 0.3393 0.2229 -0.0673 0.0889  -0.0178 368 PRO C N   
11192 C CA  . PRO C  368 ? 0.4357 0.3735 0.2646 -0.0692 0.0920  -0.0135 368 PRO C CA  
11193 C C   . PRO C  368 ? 0.5597 0.5026 0.3952 -0.0708 0.0952  -0.0167 368 PRO C C   
11194 O O   . PRO C  368 ? 0.6233 0.5633 0.4542 -0.0724 0.0976  -0.0139 368 PRO C O   
11195 C CB  . PRO C  368 ? 0.3825 0.3191 0.2255 -0.0683 0.0928  -0.0122 368 PRO C CB  
11196 C CG  . PRO C  368 ? 0.3814 0.3205 0.2266 -0.0656 0.0904  -0.0148 368 PRO C CG  
11197 C CD  . PRO C  368 ? 0.3818 0.3285 0.2232 -0.0653 0.0890  -0.0198 368 PRO C CD  
11198 N N   . GLN C  369 ? 0.7306 0.6802 0.5761 -0.0704 0.0955  -0.0225 369 GLN C N   
11199 C CA  . GLN C  369 ? 0.7929 0.7449 0.6429 -0.0717 0.0987  -0.0259 369 GLN C CA  
11200 C C   . GLN C  369 ? 0.8067 0.7602 0.6430 -0.0738 0.0982  -0.0292 369 GLN C C   
11201 O O   . GLN C  369 ? 0.8525 0.8069 0.6891 -0.0753 0.1011  -0.0326 369 GLN C O   
11202 C CB  . GLN C  369 ? 0.8356 0.7913 0.7014 -0.0707 0.0996  -0.0300 369 GLN C CB  
11203 C CG  . GLN C  369 ? 0.9191 0.8793 0.7849 -0.0722 0.0983  -0.0360 369 GLN C CG  
11204 C CD  . GLN C  369 ? 0.9368 0.9008 0.8039 -0.0709 0.0949  -0.0364 369 GLN C CD  
11205 O OE1 . GLN C  369 ? 0.8993 0.8615 0.7593 -0.0694 0.0927  -0.0326 369 GLN C OE1 
11206 N NE2 . GLN C  369 ? 0.9544 0.9233 0.8299 -0.0718 0.0947  -0.0410 369 GLN C NE2 
11207 N N   . ALA C  370 ? 0.6143 0.5680 0.4374 -0.0735 0.0944  -0.0283 370 ALA C N   
11208 C CA  . ALA C  370 ? 0.5689 0.5254 0.3778 -0.0752 0.0925  -0.0317 370 ALA C CA  
11209 C C   . ALA C  370 ? 0.5958 0.5474 0.3916 -0.0760 0.0943  -0.0281 370 ALA C C   
11210 O O   . ALA C  370 ? 0.6246 0.5700 0.4124 -0.0751 0.0937  -0.0213 370 ALA C O   
11211 C CB  . ALA C  370 ? 0.4543 0.4139 0.2524 -0.0737 0.0866  -0.0322 370 ALA C CB  
11212 N N   . SER C  371 ? 0.5680 0.5217 0.3608 -0.0781 0.0966  -0.0326 371 SER C N   
11213 C CA  . SER C  371 ? 0.5865 0.5368 0.3657 -0.0788 0.0986  -0.0299 371 SER C CA  
11214 C C   . SER C  371 ? 0.5994 0.5492 0.3581 -0.0781 0.0930  -0.0279 371 SER C C   
11215 O O   . SER C  371 ? 0.5994 0.5525 0.3554 -0.0769 0.0874  -0.0294 371 SER C O   
11216 C CB  . SER C  371 ? 0.7182 0.6707 0.4984 -0.0808 0.1025  -0.0363 371 SER C CB  
11217 O OG  . SER C  371 ? 0.7332 0.6904 0.5092 -0.0825 0.0991  -0.0434 371 SER C OG  
11218 N N   . ASP C  372 ? 0.6624 0.6087 0.4061 -0.0785 0.0940  -0.0245 372 ASP C N   
11219 C CA  . ASP C  372 ? 0.6890 0.6334 0.4111 -0.0770 0.0880  -0.0210 372 ASP C CA  
11220 C C   . ASP C  372 ? 0.6045 0.5570 0.3199 -0.0769 0.0818  -0.0284 372 ASP C C   
11221 O O   . ASP C  372 ? 0.5769 0.5314 0.2835 -0.0745 0.0744  -0.0271 372 ASP C O   
11222 C CB  . ASP C  372 ? 1.0012 0.9410 0.7087 -0.0775 0.0908  -0.0164 372 ASP C CB  
11223 C CG  . ASP C  372 ? 1.0701 1.0012 0.7762 -0.0773 0.0931  -0.0066 372 ASP C CG  
11224 O OD1 . ASP C  372 ? 1.0781 1.0075 0.8002 -0.0776 0.0955  -0.0050 372 ASP C OD1 
11225 O OD2 . ASP C  372 ? 1.0959 1.0217 0.7845 -0.0769 0.0923  -0.0004 372 ASP C OD2 
11226 N N   . LEU C  373 ? 0.5770 0.5344 0.2965 -0.0797 0.0844  -0.0363 373 LEU C N   
11227 C CA  . LEU C  373 ? 0.5683 0.5342 0.2830 -0.0809 0.0786  -0.0443 373 LEU C CA  
11228 C C   . LEU C  373 ? 0.5307 0.5032 0.2595 -0.0811 0.0754  -0.0482 373 LEU C C   
11229 O O   . LEU C  373 ? 0.5255 0.5067 0.2490 -0.0810 0.0679  -0.0524 373 LEU C O   
11230 C CB  . LEU C  373 ? 0.6311 0.5986 0.3465 -0.0846 0.0826  -0.0522 373 LEU C CB  
11231 C CG  . LEU C  373 ? 0.6230 0.5993 0.3350 -0.0876 0.0770  -0.0619 373 LEU C CG  
11232 C CD1 . LEU C  373 ? 0.6289 0.6098 0.3199 -0.0855 0.0677  -0.0610 373 LEU C CD1 
11233 C CD2 . LEU C  373 ? 0.6011 0.5760 0.3161 -0.0917 0.0824  -0.0697 373 LEU C CD2 
11234 N N   . ALA C  374 ? 0.4894 0.4593 0.2366 -0.0813 0.0807  -0.0470 374 ALA C N   
11235 C CA  . ALA C  374 ? 0.4606 0.4368 0.2223 -0.0815 0.0789  -0.0506 374 ALA C CA  
11236 C C   . ALA C  374 ? 0.4493 0.4277 0.2034 -0.0776 0.0721  -0.0464 374 ALA C C   
11237 O O   . ALA C  374 ? 0.4280 0.4167 0.1834 -0.0775 0.0664  -0.0512 374 ALA C O   
11238 C CB  . ALA C  374 ? 0.4684 0.4404 0.2497 -0.0816 0.0855  -0.0492 374 ALA C CB  
11239 N N   . ALA C  375 ? 0.3928 0.3615 0.1389 -0.0746 0.0727  -0.0375 375 ALA C N   
11240 C CA  . ALA C  375 ? 0.4004 0.3670 0.1344 -0.0704 0.0661  -0.0321 375 ALA C CA  
11241 C C   . ALA C  375 ? 0.4188 0.3923 0.1348 -0.0690 0.0573  -0.0343 375 ALA C C   
11242 O O   . ALA C  375 ? 0.4847 0.4658 0.1979 -0.0659 0.0494  -0.0356 375 ALA C O   
11243 C CB  . ALA C  375 ? 0.5418 0.4943 0.2676 -0.0687 0.0686  -0.0220 375 ALA C CB  
11244 N N   . GLU C  376 ? 0.5029 0.4750 0.2079 -0.0706 0.0579  -0.0347 376 GLU C N   
11245 C CA  . GLU C  376 ? 0.5498 0.5291 0.2374 -0.0692 0.0489  -0.0370 376 GLU C CA  
11246 C C   . GLU C  376 ? 0.4795 0.4758 0.1764 -0.0707 0.0428  -0.0467 376 GLU C C   
11247 O O   . GLU C  376 ? 0.4868 0.4930 0.1750 -0.0673 0.0322  -0.0473 376 GLU C O   
11248 C CB  . GLU C  376 ? 0.9455 0.9225 0.6244 -0.0720 0.0524  -0.0388 376 GLU C CB  
11249 C CG  . GLU C  376 ? 1.0940 1.0645 0.7490 -0.0684 0.0481  -0.0312 376 GLU C CG  
11250 C CD  . GLU C  376 ? 1.2133 1.1942 0.8533 -0.0660 0.0365  -0.0347 376 GLU C CD  
11251 O OE1 . GLU C  376 ? 1.2491 1.2414 0.8943 -0.0645 0.0285  -0.0387 376 GLU C OE1 
11252 O OE2 . GLU C  376 ? 1.2436 1.2229 0.8674 -0.0656 0.0351  -0.0338 376 GLU C OE2 
11253 N N   . ALA C  377 ? 0.4508 0.4512 0.1666 -0.0757 0.0491  -0.0541 377 ALA C N   
11254 C CA  . ALA C  377 ? 0.4577 0.4741 0.1854 -0.0787 0.0451  -0.0636 377 ALA C CA  
11255 C C   . ALA C  377 ? 0.4659 0.4903 0.2028 -0.0747 0.0406  -0.0623 377 ALA C C   
11256 O O   . ALA C  377 ? 0.4660 0.5064 0.2093 -0.0720 0.0311  -0.0659 377 ALA C O   
11257 C CB  . ALA C  377 ? 0.5242 0.5393 0.2692 -0.0847 0.0538  -0.0699 377 ALA C CB  
11258 N N   . VAL C  378 ? 0.3949 0.4084 0.1398 -0.0718 0.0463  -0.0558 378 VAL C N   
11259 C CA  . VAL C  378 ? 0.3809 0.3995 0.1423 -0.0650 0.0420  -0.0530 378 VAL C CA  
11260 C C   . VAL C  378 ? 0.3936 0.4164 0.1468 -0.0558 0.0298  -0.0477 378 VAL C C   
11261 O O   . VAL C  378 ? 0.3914 0.4286 0.1566 -0.0506 0.0222  -0.0499 378 VAL C O   
11262 C CB  . VAL C  378 ? 0.3698 0.3739 0.1375 -0.0636 0.0496  -0.0464 378 VAL C CB  
11263 C CG1 . VAL C  378 ? 0.3602 0.3676 0.1405 -0.0555 0.0442  -0.0430 378 VAL C CG1 
11264 C CG2 . VAL C  378 ? 0.3558 0.3577 0.1347 -0.0710 0.0608  -0.0515 378 VAL C CG2 
11265 N N   . VAL C  379 ? 0.4123 0.4228 0.1447 -0.0537 0.0282  -0.0406 379 VAL C N   
11266 C CA  . VAL C  379 ? 0.4286 0.4387 0.1493 -0.0443 0.0171  -0.0339 379 VAL C CA  
11267 C C   . VAL C  379 ? 0.4368 0.4667 0.1558 -0.0431 0.0069  -0.0402 379 VAL C C   
11268 O O   . VAL C  379 ? 0.4573 0.4986 0.1829 -0.0347 -0.0030 -0.0393 379 VAL C O   
11269 C CB  . VAL C  379 ? 0.4496 0.4408 0.1462 -0.0439 0.0189  -0.0247 379 VAL C CB  
11270 C CG1 . VAL C  379 ? 0.4706 0.4619 0.1523 -0.0343 0.0065  -0.0182 379 VAL C CG1 
11271 C CG2 . VAL C  379 ? 0.4427 0.4157 0.1425 -0.0442 0.0271  -0.0176 379 VAL C CG2 
11272 N N   . LEU C  380 ? 0.4660 0.5006 0.1762 -0.0515 0.0092  -0.0469 380 LEU C N   
11273 C CA  . LEU C  380 ? 0.4754 0.5299 0.1842 -0.0520 -0.0006 -0.0542 380 LEU C CA  
11274 C C   . LEU C  380 ? 0.4915 0.5658 0.2260 -0.0508 -0.0043 -0.0607 380 LEU C C   
11275 O O   . LEU C  380 ? 0.5273 0.6189 0.2662 -0.0446 -0.0156 -0.0619 380 LEU C O   
11276 C CB  . LEU C  380 ? 0.4602 0.5163 0.1592 -0.0629 0.0042  -0.0629 380 LEU C CB  
11277 C CG  . LEU C  380 ? 0.4611 0.5408 0.1680 -0.0666 -0.0040 -0.0738 380 LEU C CG  
11278 C CD1 . LEU C  380 ? 0.5071 0.5968 0.1976 -0.0605 -0.0178 -0.0717 380 LEU C CD1 
11279 C CD2 . LEU C  380 ? 0.6172 0.6964 0.3254 -0.0782 0.0036  -0.0840 380 LEU C CD2 
11280 N N   . HIS C  381 ? 0.4137 0.4859 0.1654 -0.0565 0.0055  -0.0646 381 HIS C N   
11281 C CA  . HIS C  381 ? 0.4183 0.5092 0.1937 -0.0573 0.0038  -0.0714 381 HIS C CA  
11282 C C   . HIS C  381 ? 0.3905 0.4878 0.1773 -0.0456 -0.0029 -0.0658 381 HIS C C   
11283 O O   . HIS C  381 ? 0.3860 0.5047 0.1867 -0.0430 -0.0099 -0.0705 381 HIS C O   
11284 C CB  . HIS C  381 ? 0.5486 0.6341 0.3378 -0.0660 0.0163  -0.0762 381 HIS C CB  
11285 C CG  . HIS C  381 ? 0.5735 0.6782 0.3849 -0.0698 0.0157  -0.0842 381 HIS C CG  
11286 N ND1 . HIS C  381 ? 0.5952 0.7130 0.4096 -0.0792 0.0147  -0.0944 381 HIS C ND1 
11287 C CD2 . HIS C  381 ? 0.5971 0.7104 0.4283 -0.0658 0.0161  -0.0837 381 HIS C CD2 
11288 C CE1 . HIS C  381 ? 0.6190 0.7525 0.4547 -0.0814 0.0149  -0.0993 381 HIS C CE1 
11289 N NE2 . HIS C  381 ? 0.6192 0.7508 0.4653 -0.0731 0.0159  -0.0929 381 HIS C NE2 
11290 N N   . TYR C  382 ? 0.4812 0.5605 0.2624 -0.0386 -0.0007 -0.0564 382 TYR C N   
11291 C CA  . TYR C  382 ? 0.4889 0.5718 0.2806 -0.0271 -0.0061 -0.0518 382 TYR C CA  
11292 C C   . TYR C  382 ? 0.5158 0.5999 0.2951 -0.0149 -0.0184 -0.0452 382 TYR C C   
11293 O O   . TYR C  382 ? 0.5407 0.6315 0.3300 -0.0046 -0.0241 -0.0431 382 TYR C O   
11294 C CB  . TYR C  382 ? 0.4888 0.5527 0.2848 -0.0257 0.0025  -0.0463 382 TYR C CB  
11295 C CG  . TYR C  382 ? 0.5122 0.5813 0.3278 -0.0327 0.0116  -0.0524 382 TYR C CG  
11296 C CD1 . TYR C  382 ? 0.5124 0.5979 0.3477 -0.0290 0.0096  -0.0561 382 TYR C CD1 
11297 C CD2 . TYR C  382 ? 0.5402 0.5980 0.3541 -0.0426 0.0225  -0.0541 382 TYR C CD2 
11298 C CE1 . TYR C  382 ? 0.4949 0.5843 0.3467 -0.0353 0.0182  -0.0610 382 TYR C CE1 
11299 C CE2 . TYR C  382 ? 0.5329 0.5942 0.3637 -0.0482 0.0306  -0.0589 382 TYR C CE2 
11300 C CZ  . TYR C  382 ? 0.5040 0.5807 0.3531 -0.0448 0.0284  -0.0621 382 TYR C CZ  
11301 O OH  . TYR C  382 ? 0.4900 0.5696 0.3545 -0.0503 0.0365  -0.0662 382 TYR C OH  
11302 N N   . THR C  383 ? 0.4278 0.5054 0.1851 -0.0156 -0.0225 -0.0421 383 THR C N   
11303 C CA  . THR C  383 ? 0.4467 0.5244 0.1900 -0.0038 -0.0345 -0.0352 383 THR C CA  
11304 C C   . THR C  383 ? 0.4482 0.5552 0.2017 0.0005  -0.0460 -0.0416 383 THR C C   
11305 O O   . THR C  383 ? 0.4418 0.5663 0.2032 -0.0088 -0.0455 -0.0512 383 THR C O   
11306 C CB  . THR C  383 ? 0.4703 0.5339 0.1854 -0.0065 -0.0355 -0.0302 383 THR C CB  
11307 O OG1 . THR C  383 ? 0.4918 0.5313 0.1984 -0.0128 -0.0237 -0.0255 383 THR C OG1 
11308 C CG2 . THR C  383 ? 0.4939 0.5523 0.1927 0.0066  -0.0470 -0.0208 383 THR C CG2 
11309 N N   . ASP C  384 ? 0.6267 0.7390 0.3804 0.0146  -0.0564 -0.0364 384 ASP C N   
11310 C CA  . ASP C  384 ? 0.6877 0.8274 0.4456 0.0201  -0.0694 -0.0407 384 ASP C CA  
11311 C C   . ASP C  384 ? 0.7281 0.8599 0.4582 0.0242  -0.0778 -0.0343 384 ASP C C   
11312 O O   . ASP C  384 ? 0.7707 0.8844 0.4857 0.0350  -0.0817 -0.0237 384 ASP C O   
11313 C CB  . ASP C  384 ? 0.7152 0.8678 0.4893 0.0347  -0.0767 -0.0389 384 ASP C CB  
11314 C CG  . ASP C  384 ? 0.7628 0.9401 0.5361 0.0439  -0.0919 -0.0400 384 ASP C CG  
11315 O OD1 . ASP C  384 ? 0.7794 0.9762 0.5529 0.0353  -0.0957 -0.0476 384 ASP C OD1 
11316 O OD2 . ASP C  384 ? 0.7887 0.9657 0.5606 0.0599  -0.1003 -0.0335 384 ASP C OD2 
11317 N N   . TRP C  385 ? 0.6127 0.7575 0.3352 0.0155  -0.0809 -0.0409 385 TRP C N   
11318 C CA  . TRP C  385 ? 0.6036 0.7387 0.2965 0.0169  -0.0869 -0.0354 385 TRP C CA  
11319 C C   . TRP C  385 ? 0.6100 0.7607 0.2968 0.0308  -0.1035 -0.0316 385 TRP C C   
11320 O O   . TRP C  385 ? 0.6073 0.7497 0.2682 0.0348  -0.1102 -0.0252 385 TRP C O   
11321 C CB  . TRP C  385 ? 0.5323 0.6714 0.2164 0.0016  -0.0824 -0.0441 385 TRP C CB  
11322 C CG  . TRP C  385 ? 0.5183 0.6374 0.2035 -0.0097 -0.0662 -0.0453 385 TRP C CG  
11323 C CD1 . TRP C  385 ? 0.5466 0.6716 0.2535 -0.0190 -0.0568 -0.0538 385 TRP C CD1 
11324 C CD2 . TRP C  385 ? 0.5287 0.6191 0.1928 -0.0123 -0.0575 -0.0373 385 TRP C CD2 
11325 N NE1 . TRP C  385 ? 0.5328 0.6350 0.2337 -0.0266 -0.0433 -0.0517 385 TRP C NE1 
11326 C CE2 . TRP C  385 ? 0.5087 0.5905 0.1841 -0.0229 -0.0433 -0.0419 385 TRP C CE2 
11327 C CE3 . TRP C  385 ? 0.5540 0.6256 0.1906 -0.0069 -0.0601 -0.0265 385 TRP C CE3 
11328 C CZ2 . TRP C  385 ? 0.5121 0.5694 0.1740 -0.0280 -0.0320 -0.0365 385 TRP C CZ2 
11329 C CZ3 . TRP C  385 ? 0.5576 0.6042 0.1804 -0.0130 -0.0481 -0.0210 385 TRP C CZ3 
11330 C CH2 . TRP C  385 ? 0.5362 0.5769 0.1724 -0.0233 -0.0344 -0.0263 385 TRP C CH2 
11331 N N   . LEU C  386 ? 0.6968 0.8705 0.4071 0.0388  -0.1101 -0.0352 386 LEU C N   
11332 C CA  . LEU C  386 ? 0.7616 0.9483 0.4677 0.0550  -0.1256 -0.0301 386 LEU C CA  
11333 C C   . LEU C  386 ? 0.8060 0.9625 0.4959 0.0682  -0.1256 -0.0159 386 LEU C C   
11334 O O   . LEU C  386 ? 0.8472 0.9961 0.5149 0.0783  -0.1354 -0.0073 386 LEU C O   
11335 C CB  . LEU C  386 ? 0.5879 0.8076 0.3250 0.0608  -0.1315 -0.0375 386 LEU C CB  
11336 C CG  . LEU C  386 ? 0.6176 0.8713 0.3572 0.0637  -0.1466 -0.0433 386 LEU C CG  
11337 C CD1 . LEU C  386 ? 0.6019 0.8906 0.3761 0.0662  -0.1498 -0.0521 386 LEU C CD1 
11338 C CD2 . LEU C  386 ? 0.5835 0.8313 0.2997 0.0801  -0.1605 -0.0323 386 LEU C CD2 
11339 N N   . HIS C  387 ? 0.6907 0.8289 0.3909 0.0675  -0.1146 -0.0136 387 HIS C N   
11340 C CA  . HIS C  387 ? 0.7059 0.8127 0.3924 0.0778  -0.1128 -0.0011 387 HIS C CA  
11341 C C   . HIS C  387 ? 0.6127 0.6924 0.2967 0.0664  -0.0971 0.0007  387 HIS C C   
11342 O O   . HIS C  387 ? 0.5752 0.6491 0.2758 0.0675  -0.0903 -0.0003 387 HIS C O   
11343 C CB  . HIS C  387 ? 0.9379 1.0517 0.6424 0.0936  -0.1180 0.0004  387 HIS C CB  
11344 C CG  . HIS C  387 ? 0.9989 1.1503 0.7206 0.1017  -0.1302 -0.0063 387 HIS C CG  
11345 N ND1 . HIS C  387 ? 0.9889 1.1693 0.7403 0.0962  -0.1275 -0.0179 387 HIS C ND1 
11346 C CD2 . HIS C  387 ? 1.0461 1.2118 0.7599 0.1149  -0.1452 -0.0029 387 HIS C CD2 
11347 C CE1 . HIS C  387 ? 1.0133 1.2254 0.7755 0.1050  -0.1400 -0.0217 387 HIS C CE1 
11348 N NE2 . HIS C  387 ? 1.0509 1.2554 0.7910 0.1169  -0.1513 -0.0128 387 HIS C NE2 
11349 N N   . PRO C  388 ? 0.5674 0.6311 0.2302 0.0559  -0.0913 0.0032  388 PRO C N   
11350 C CA  . PRO C  388 ? 0.5552 0.5974 0.2166 0.0436  -0.0762 0.0038  388 PRO C CA  
11351 C C   . PRO C  388 ? 0.5603 0.5733 0.2167 0.0499  -0.0716 0.0140  388 PRO C C   
11352 O O   . PRO C  388 ? 0.5459 0.5444 0.2079 0.0415  -0.0597 0.0137  388 PRO C O   
11353 C CB  . PRO C  388 ? 0.8404 0.8731 0.4757 0.0349  -0.0741 0.0061  388 PRO C CB  
11354 C CG  . PRO C  388 ? 0.8865 0.9215 0.5022 0.0466  -0.0881 0.0130  388 PRO C CG  
11355 C CD  . PRO C  388 ? 0.8634 0.9274 0.5004 0.0564  -0.0992 0.0069  388 PRO C CD  
11356 N N   . GLU C  389 ? 0.6648 0.6693 0.3101 0.0646  -0.0816 0.0228  389 GLU C N   
11357 C CA  . GLU C  389 ? 0.7051 0.6784 0.3401 0.0709  -0.0788 0.0335  389 GLU C CA  
11358 C C   . GLU C  389 ? 0.6714 0.6453 0.3266 0.0813  -0.0800 0.0323  389 GLU C C   
11359 O O   . GLU C  389 ? 0.6505 0.5979 0.2991 0.0859  -0.0771 0.0399  389 GLU C O   
11360 C CB  . GLU C  389 ? 0.9539 0.9122 0.5609 0.0813  -0.0885 0.0452  389 GLU C CB  
11361 C CG  . GLU C  389 ? 1.0636 1.0147 0.6456 0.0717  -0.0862 0.0487  389 GLU C CG  
11362 C CD  . GLU C  389 ? 1.1742 1.0936 0.7418 0.0625  -0.0740 0.0564  389 GLU C CD  
11363 O OE1 . GLU C  389 ? 1.2109 1.1116 0.7851 0.0655  -0.0698 0.0605  389 GLU C OE1 
11364 O OE2 . GLU C  389 ? 1.2113 1.1249 0.7612 0.0521  -0.0687 0.0580  389 GLU C OE2 
11365 N N   . ASP C  390 ? 0.7825 0.7864 0.4619 0.0845  -0.0837 0.0225  390 ASP C N   
11366 C CA  . ASP C  390 ? 0.7671 0.7756 0.4639 0.0977  -0.0872 0.0215  390 ASP C CA  
11367 C C   . ASP C  390 ? 0.7509 0.7457 0.4613 0.0925  -0.0757 0.0193  390 ASP C C   
11368 O O   . ASP C  390 ? 0.7124 0.7217 0.4410 0.0818  -0.0678 0.0105  390 ASP C O   
11369 C CB  . ASP C  390 ? 0.6683 0.7154 0.3866 0.1029  -0.0951 0.0121  390 ASP C CB  
11370 C CG  . ASP C  390 ? 0.6857 0.7408 0.4247 0.1151  -0.0965 0.0094  390 ASP C CG  
11371 O OD1 . ASP C  390 ? 0.7359 0.7687 0.4658 0.1276  -0.0991 0.0172  390 ASP C OD1 
11372 O OD2 . ASP C  390 ? 0.6671 0.7498 0.4308 0.1121  -0.0946 -0.0005 390 ASP C OD2 
11373 N N   . PRO C  391 ? 0.7404 0.7070 0.4416 0.1007  -0.0752 0.0274  391 PRO C N   
11374 C CA  . PRO C  391 ? 0.7435 0.6896 0.4505 0.0958  -0.0651 0.0277  391 PRO C CA  
11375 C C   . PRO C  391 ? 0.7505 0.7165 0.4851 0.0955  -0.0608 0.0177  391 PRO C C   
11376 O O   . PRO C  391 ? 0.7518 0.7137 0.4949 0.0838  -0.0504 0.0139  391 PRO C O   
11377 C CB  . PRO C  391 ? 0.6575 0.5759 0.3502 0.1097  -0.0703 0.0372  391 PRO C CB  
11378 C CG  . PRO C  391 ? 0.6798 0.5931 0.3502 0.1153  -0.0791 0.0452  391 PRO C CG  
11379 C CD  . PRO C  391 ? 0.6744 0.6247 0.3559 0.1156  -0.0854 0.0376  391 PRO C CD  
11380 N N   . THR C  392 ? 0.7820 0.7695 0.5303 0.1083  -0.0686 0.0136  392 THR C N   
11381 C CA  . THR C  392 ? 0.7490 0.7570 0.5234 0.1080  -0.0642 0.0042  392 THR C CA  
11382 C C   . THR C  392 ? 0.7138 0.7442 0.5009 0.0920  -0.0579 -0.0042 392 THR C C   
11383 O O   . THR C  392 ? 0.7166 0.7506 0.5183 0.0835  -0.0485 -0.0098 392 THR C O   
11384 C CB  . THR C  392 ? 0.6414 0.6714 0.4288 0.1249  -0.0736 0.0012  392 THR C CB  
11385 O OG1 . THR C  392 ? 0.5863 0.6480 0.3995 0.1203  -0.0700 -0.0093 392 THR C OG1 
11386 C CG2 . THR C  392 ? 0.6850 0.7261 0.4612 0.1332  -0.0859 0.0051  392 THR C CG2 
11387 N N   . HIS C  393 ? 0.5232 0.5667 0.3029 0.0878  -0.0629 -0.0047 393 HIS C N   
11388 C CA  . HIS C  393 ? 0.4958 0.5593 0.2860 0.0731  -0.0576 -0.0130 393 HIS C CA  
11389 C C   . HIS C  393 ? 0.4503 0.4935 0.2328 0.0584  -0.0460 -0.0118 393 HIS C C   
11390 O O   . HIS C  393 ? 0.4181 0.4697 0.2148 0.0477  -0.0374 -0.0185 393 HIS C O   
11391 C CB  . HIS C  393 ? 0.6333 0.7155 0.4164 0.0720  -0.0662 -0.0146 393 HIS C CB  
11392 C CG  . HIS C  393 ? 0.6605 0.7620 0.4541 0.0567  -0.0609 -0.0240 393 HIS C CG  
11393 N ND1 . HIS C  393 ? 0.6824 0.7710 0.4636 0.0429  -0.0536 -0.0239 393 HIS C ND1 
11394 C CD2 . HIS C  393 ? 0.6690 0.8003 0.4847 0.0526  -0.0610 -0.0338 393 HIS C CD2 
11395 C CE1 . HIS C  393 ? 0.6867 0.7951 0.4809 0.0316  -0.0498 -0.0334 393 HIS C CE1 
11396 N NE2 . HIS C  393 ? 0.6828 0.8169 0.4980 0.0366  -0.0542 -0.0394 393 HIS C NE2 
11397 N N   . LEU C  394 ? 0.5750 0.5917 0.3350 0.0580  -0.0456 -0.0029 394 LEU C N   
11398 C CA  . LEU C  394 ? 0.6131 0.6105 0.3659 0.0450  -0.0345 -0.0011 394 LEU C CA  
11399 C C   . LEU C  394 ? 0.6068 0.5949 0.3733 0.0429  -0.0260 -0.0027 394 LEU C C   
11400 O O   . LEU C  394 ? 0.6350 0.6225 0.4082 0.0312  -0.0163 -0.0064 394 LEU C O   
11401 C CB  . LEU C  394 ? 0.5628 0.5336 0.2891 0.0456  -0.0358 0.0095  394 LEU C CB  
11402 C CG  . LEU C  394 ? 0.4968 0.4753 0.2066 0.0452  -0.0426 0.0112  394 LEU C CG  
11403 C CD1 . LEU C  394 ? 0.5262 0.4771 0.2089 0.0487  -0.0448 0.0231  394 LEU C CD1 
11404 C CD2 . LEU C  394 ? 0.4834 0.4731 0.1956 0.0302  -0.0353 0.0041  394 LEU C CD2 
11405 N N   . ARG C  395 ? 0.4769 0.4576 0.2470 0.0547  -0.0296 -0.0002 395 ARG C N   
11406 C CA  . ARG C  395 ? 0.4423 0.4154 0.2248 0.0538  -0.0226 -0.0024 395 ARG C CA  
11407 C C   . ARG C  395 ? 0.4427 0.4414 0.2482 0.0480  -0.0176 -0.0123 395 ARG C C   
11408 O O   . ARG C  395 ? 0.4473 0.4429 0.2595 0.0373  -0.0081 -0.0151 395 ARG C O   
11409 C CB  . ARG C  395 ? 0.4394 0.4017 0.2209 0.0689  -0.0285 0.0010  395 ARG C CB  
11410 C CG  . ARG C  395 ? 0.4262 0.3822 0.2200 0.0694  -0.0223 -0.0021 395 ARG C CG  
11411 C CD  . ARG C  395 ? 0.4159 0.3957 0.2285 0.0793  -0.0256 -0.0090 395 ARG C CD  
11412 N NE  . ARG C  395 ? 0.4354 0.4067 0.2431 0.0963  -0.0336 -0.0056 395 ARG C NE  
11413 C CZ  . ARG C  395 ? 0.4362 0.4297 0.2550 0.1086  -0.0404 -0.0093 395 ARG C CZ  
11414 N NH1 . ARG C  395 ? 0.4186 0.4446 0.2540 0.1047  -0.0403 -0.0164 395 ARG C NH1 
11415 N NH2 . ARG C  395 ? 0.4558 0.4390 0.2692 0.1249  -0.0471 -0.0059 395 ARG C NH2 
11416 N N   . ASP C  396 ? 0.4413 0.4657 0.2588 0.0549  -0.0241 -0.0175 396 ASP C N   
11417 C CA  . ASP C  396 ? 0.4717 0.5219 0.3108 0.0489  -0.0197 -0.0267 396 ASP C CA  
11418 C C   . ASP C  396 ? 0.3616 0.4159 0.2008 0.0327  -0.0125 -0.0305 396 ASP C C   
11419 O O   . ASP C  396 ? 0.3424 0.4060 0.1962 0.0245  -0.0048 -0.0363 396 ASP C O   
11420 C CB  . ASP C  396 ? 0.7650 0.8438 0.6156 0.0578  -0.0286 -0.0312 396 ASP C CB  
11421 C CG  . ASP C  396 ? 0.8626 0.9424 0.7203 0.0736  -0.0329 -0.0302 396 ASP C CG  
11422 O OD1 . ASP C  396 ? 0.8998 0.9543 0.7490 0.0782  -0.0306 -0.0252 396 ASP C OD1 
11423 O OD2 . ASP C  396 ? 0.8784 0.9845 0.7502 0.0813  -0.0385 -0.0348 396 ASP C OD2 
11424 N N   . ALA C  397 ? 0.3754 0.4216 0.1973 0.0286  -0.0148 -0.0268 397 ALA C N   
11425 C CA  . ALA C  397 ? 0.3693 0.4175 0.1882 0.0146  -0.0086 -0.0303 397 ALA C CA  
11426 C C   . ALA C  397 ? 0.3622 0.3896 0.1775 0.0061  0.0022  -0.0277 397 ALA C C   
11427 O O   . ALA C  397 ? 0.3495 0.3810 0.1709 -0.0046 0.0099  -0.0324 397 ALA C O   
11428 C CB  . ALA C  397 ? 0.3886 0.4356 0.1890 0.0141  -0.0149 -0.0274 397 ALA C CB  
11429 N N   . MET C  398 ? 0.3874 0.3924 0.1926 0.0108  0.0025  -0.0202 398 MET C N   
11430 C CA  . MET C  398 ? 0.3759 0.3626 0.1784 0.0029  0.0121  -0.0175 398 MET C CA  
11431 C C   . MET C  398 ? 0.3521 0.3462 0.1739 0.0012  0.0179  -0.0228 398 MET C C   
11432 O O   . MET C  398 ? 0.3314 0.3251 0.1593 -0.0084 0.0267  -0.0256 398 MET C O   
11433 C CB  . MET C  398 ? 0.4250 0.3867 0.2131 0.0083  0.0102  -0.0086 398 MET C CB  
11434 C CG  . MET C  398 ? 0.4056 0.3489 0.1894 -0.0006 0.0193  -0.0051 398 MET C CG  
11435 S SD  . MET C  398 ? 0.3967 0.3396 0.1688 -0.0124 0.0250  -0.0047 398 MET C SD  
11436 C CE  . MET C  398 ? 0.4124 0.3664 0.2037 -0.0220 0.0354  -0.0125 398 MET C CE  
11437 N N   . SER C  399 ? 0.4570 0.4582 0.2879 0.0113  0.0130  -0.0241 399 SER C N   
11438 C CA  . SER C  399 ? 0.4891 0.5007 0.3384 0.0107  0.0179  -0.0295 399 SER C CA  
11439 C C   . SER C  399 ? 0.4858 0.5156 0.3459 0.0007  0.0229  -0.0364 399 SER C C   
11440 O O   . SER C  399 ? 0.4693 0.4971 0.3366 -0.0071 0.0314  -0.0386 399 SER C O   
11441 C CB  . SER C  399 ? 0.4321 0.4546 0.2901 0.0235  0.0114  -0.0313 399 SER C CB  
11442 O OG  . SER C  399 ? 0.4008 0.4372 0.2767 0.0225  0.0163  -0.0371 399 SER C OG  
11443 N N   . ALA C  400 ? 0.3147 0.3610 0.1747 0.0006  0.0173  -0.0396 400 ALA C N   
11444 C CA  . ALA C  400 ? 0.3038 0.3679 0.1740 -0.0089 0.0210  -0.0469 400 ALA C CA  
11445 C C   . ALA C  400 ? 0.2998 0.3530 0.1644 -0.0209 0.0297  -0.0474 400 ALA C C   
11446 O O   . ALA C  400 ? 0.2865 0.3453 0.1622 -0.0283 0.0369  -0.0521 400 ALA C O   
11447 C CB  . ALA C  400 ? 0.3386 0.4209 0.2073 -0.0070 0.0123  -0.0499 400 ALA C CB  
11448 N N   . VAL C  401 ? 0.4057 0.4431 0.2529 -0.0224 0.0293  -0.0423 401 VAL C N   
11449 C CA  . VAL C  401 ? 0.3860 0.4127 0.2269 -0.0326 0.0378  -0.0424 401 VAL C CA  
11450 C C   . VAL C  401 ? 0.3438 0.3617 0.1938 -0.0355 0.0466  -0.0417 401 VAL C C   
11451 O O   . VAL C  401 ? 0.2990 0.3204 0.1569 -0.0431 0.0539  -0.0461 401 VAL C O   
11452 C CB  . VAL C  401 ? 0.3284 0.3384 0.1488 -0.0326 0.0365  -0.0358 401 VAL C CB  
11453 C CG1 . VAL C  401 ? 0.3265 0.3278 0.1419 -0.0424 0.0459  -0.0364 401 VAL C CG1 
11454 C CG2 . VAL C  401 ? 0.4115 0.4300 0.2214 -0.0296 0.0277  -0.0362 401 VAL C CG2 
11455 N N   . VAL C  402 ? 0.3261 0.3320 0.1746 -0.0295 0.0456  -0.0363 402 VAL C N   
11456 C CA  . VAL C  402 ? 0.2860 0.2841 0.1424 -0.0323 0.0532  -0.0356 402 VAL C CA  
11457 C C   . VAL C  402 ? 0.3645 0.3771 0.2382 -0.0335 0.0565  -0.0416 402 VAL C C   
11458 O O   . VAL C  402 ? 0.2598 0.2720 0.1400 -0.0401 0.0643  -0.0438 402 VAL C O   
11459 C CB  . VAL C  402 ? 0.3803 0.3633 0.2320 -0.0260 0.0509  -0.0297 402 VAL C CB  
11460 C CG1 . VAL C  402 ? 0.3690 0.3512 0.2327 -0.0258 0.0556  -0.0311 402 VAL C CG1 
11461 C CG2 . VAL C  402 ? 0.3895 0.3549 0.2265 -0.0299 0.0531  -0.0236 402 VAL C CG2 
11462 N N   . GLY C  403 ? 0.4084 0.4344 0.2894 -0.0268 0.0506  -0.0441 403 GLY C N   
11463 C CA  . GLY C  403 ? 0.4135 0.4549 0.3107 -0.0275 0.0535  -0.0495 403 GLY C CA  
11464 C C   . GLY C  403 ? 0.4272 0.4784 0.3308 -0.0375 0.0590  -0.0549 403 GLY C C   
11465 O O   . GLY C  403 ? 0.4250 0.4755 0.3367 -0.0421 0.0663  -0.0565 403 GLY C O   
11466 N N   . ASP C  404 ? 0.4203 0.4794 0.3193 -0.0408 0.0553  -0.0578 404 ASP C N   
11467 C CA  . ASP C  404 ? 0.4097 0.4766 0.3136 -0.0508 0.0602  -0.0639 404 ASP C CA  
11468 C C   . ASP C  404 ? 0.3892 0.4405 0.2871 -0.0580 0.0687  -0.0627 404 ASP C C   
11469 O O   . ASP C  404 ? 0.3933 0.4453 0.2986 -0.0644 0.0758  -0.0661 404 ASP C O   
11470 C CB  . ASP C  404 ? 0.3680 0.4464 0.2667 -0.0531 0.0537  -0.0678 404 ASP C CB  
11471 C CG  . ASP C  404 ? 0.4073 0.5007 0.3096 -0.0443 0.0438  -0.0678 404 ASP C CG  
11472 O OD1 . ASP C  404 ? 0.4360 0.5383 0.3508 -0.0390 0.0435  -0.0682 404 ASP C OD1 
11473 O OD2 . ASP C  404 ? 0.4193 0.5156 0.3112 -0.0422 0.0364  -0.0674 404 ASP C OD2 
11474 N N   . HIS C  405 ? 0.3928 0.4299 0.2769 -0.0567 0.0681  -0.0578 405 HIS C N   
11475 C CA  . HIS C  405 ? 0.4018 0.4259 0.2806 -0.0630 0.0762  -0.0569 405 HIS C CA  
11476 C C   . HIS C  405 ? 0.4049 0.4230 0.2945 -0.0634 0.0829  -0.0551 405 HIS C C   
11477 O O   . HIS C  405 ? 0.4083 0.4237 0.3072 -0.0671 0.0858  -0.0557 405 HIS C O   
11478 C CB  . HIS C  405 ? 0.3603 0.3709 0.2237 -0.0613 0.0749  -0.0511 405 HIS C CB  
11479 C CG  . HIS C  405 ? 0.3448 0.3433 0.2079 -0.0652 0.0818  -0.0484 405 HIS C CG  
11480 N ND1 . HIS C  405 ? 0.3353 0.3344 0.2076 -0.0696 0.0848  -0.0513 405 HIS C ND1 
11481 C CD2 . HIS C  405 ? 0.3432 0.3292 0.2033 -0.0636 0.0834  -0.0419 405 HIS C CD2 
11482 C CE1 . HIS C  405 ? 0.3479 0.3364 0.2226 -0.0696 0.0875  -0.0470 405 HIS C CE1 
11483 N NE2 . HIS C  405 ? 0.3577 0.3395 0.2262 -0.0663 0.0867  -0.0414 405 HIS C NE2 
11484 N N   . ASN C  406 ? 0.3405 0.3549 0.2318 -0.0575 0.0818  -0.0512 406 ASN C N   
11485 C CA  . ASN C  406 ? 0.2785 0.2874 0.1812 -0.0564 0.0851  -0.0482 406 ASN C CA  
11486 C C   . ASN C  406 ? 0.2551 0.2744 0.1718 -0.0559 0.0860  -0.0513 406 ASN C C   
11487 O O   . ASN C  406 ? 0.2493 0.2643 0.1758 -0.0564 0.0876  -0.0492 406 ASN C O   
11488 C CB  . ASN C  406 ? 0.2339 0.2331 0.1309 -0.0517 0.0847  -0.0435 406 ASN C CB  
11489 C CG  . ASN C  406 ? 0.2854 0.2728 0.1687 -0.0528 0.0843  -0.0393 406 ASN C CG  
11490 O OD1 . ASN C  406 ? 0.2983 0.2784 0.1850 -0.0550 0.0859  -0.0360 406 ASN C OD1 
11491 N ND2 . ASN C  406 ? 0.2555 0.2413 0.1298 -0.0483 0.0771  -0.0372 406 ASN C ND2 
11492 N N   . VAL C  407 ? 0.3612 0.3949 0.2787 -0.0545 0.0845  -0.0561 407 VAL C N   
11493 C CA  . VAL C  407 ? 0.4024 0.4469 0.3336 -0.0537 0.0858  -0.0584 407 VAL C CA  
11494 C C   . VAL C  407 ? 0.3917 0.4525 0.3299 -0.0590 0.0862  -0.0648 407 VAL C C   
11495 O O   . VAL C  407 ? 0.4065 0.4661 0.3537 -0.0637 0.0887  -0.0651 407 VAL C O   
11496 C CB  . VAL C  407 ? 0.2138 0.2623 0.1475 -0.0449 0.0822  -0.0571 407 VAL C CB  
11497 C CG1 . VAL C  407 ? 0.2065 0.2700 0.1534 -0.0448 0.0848  -0.0607 407 VAL C CG1 
11498 C CG2 . VAL C  407 ? 0.2129 0.2452 0.1413 -0.0416 0.0838  -0.0519 407 VAL C CG2 
11499 N N   . VAL C  408 ? 0.3075 0.3805 0.2450 -0.0561 0.0790  -0.0672 408 VAL C N   
11500 C CA  . VAL C  408 ? 0.2897 0.3816 0.2371 -0.0607 0.0781  -0.0733 408 VAL C CA  
11501 C C   . VAL C  408 ? 0.2561 0.3454 0.2022 -0.0718 0.0833  -0.0775 408 VAL C C   
11502 O O   . VAL C  408 ? 0.2697 0.3649 0.2252 -0.0782 0.0888  -0.0810 408 VAL C O   
11503 C CB  . VAL C  408 ? 0.2274 0.3344 0.1746 -0.0558 0.0682  -0.0753 408 VAL C CB  
11504 C CG1 . VAL C  408 ? 0.2246 0.3542 0.1861 -0.0603 0.0679  -0.0816 408 VAL C CG1 
11505 C CG2 . VAL C  408 ? 0.2281 0.3339 0.1740 -0.0436 0.0626  -0.0709 408 VAL C CG2 
11506 N N   . CYS C  409 ? 0.2314 0.3108 0.1652 -0.0742 0.0822  -0.0771 409 CYS C N   
11507 C CA  . CYS C  409 ? 0.2712 0.3470 0.2025 -0.0843 0.0871  -0.0820 409 CYS C CA  
11508 C C   . CYS C  409 ? 0.2436 0.3028 0.1824 -0.0862 0.0918  -0.0778 409 CYS C C   
11509 O O   . CYS C  409 ? 0.2331 0.2928 0.1774 -0.0935 0.0948  -0.0819 409 CYS C O   
11510 C CB  . CYS C  409 ? 0.3603 0.4302 0.2769 -0.0854 0.0833  -0.0825 409 CYS C CB  
11511 S SG  . CYS C  409 ? 0.3254 0.4139 0.2402 -0.0807 0.0705  -0.0845 409 CYS C SG  
11512 N N   . PRO C  410 ? 0.2257 0.2708 0.1638 -0.0798 0.0918  -0.0703 410 PRO C N   
11513 C CA  . PRO C  410 ? 0.2210 0.2538 0.1661 -0.0801 0.0946  -0.0670 410 PRO C CA  
11514 C C   . PRO C  410 ? 0.2186 0.2590 0.1747 -0.0811 0.0960  -0.0684 410 PRO C C   
11515 O O   . PRO C  410 ? 0.2362 0.2693 0.1961 -0.0848 0.0989  -0.0689 410 PRO C O   
11516 C CB  . PRO C  410 ? 0.2988 0.3210 0.2416 -0.0725 0.0931  -0.0597 410 PRO C CB  
11517 C CG  . PRO C  410 ? 0.3076 0.3290 0.2393 -0.0713 0.0912  -0.0592 410 PRO C CG  
11518 C CD  . PRO C  410 ? 0.3195 0.3571 0.2483 -0.0734 0.0894  -0.0652 410 PRO C CD  
11519 N N   . VAL C  411 ? 0.2530 0.3076 0.2134 -0.0776 0.0944  -0.0690 411 VAL C N   
11520 C CA  . VAL C  411 ? 0.2483 0.3124 0.2194 -0.0783 0.0958  -0.0702 411 VAL C CA  
11521 C C   . VAL C  411 ? 0.2434 0.3181 0.2192 -0.0880 0.0979  -0.0774 411 VAL C C   
11522 O O   . VAL C  411 ? 0.2149 0.2866 0.1965 -0.0919 0.1007  -0.0778 411 VAL C O   
11523 C CB  . VAL C  411 ? 0.2032 0.2817 0.1781 -0.0714 0.0938  -0.0699 411 VAL C CB  
11524 C CG1 . VAL C  411 ? 0.2015 0.2955 0.1880 -0.0739 0.0953  -0.0730 411 VAL C CG1 
11525 C CG2 . VAL C  411 ? 0.1983 0.2646 0.1704 -0.0631 0.0928  -0.0631 411 VAL C CG2 
11526 N N   . ALA C  412 ? 0.2742 0.3609 0.2462 -0.0922 0.0966  -0.0833 412 ALA C N   
11527 C CA  . ALA C  412 ? 0.2468 0.3460 0.2225 -0.1028 0.0983  -0.0916 412 ALA C CA  
11528 C C   . ALA C  412 ? 0.3250 0.4054 0.2974 -0.1096 0.1022  -0.0923 412 ALA C C   
11529 O O   . ALA C  412 ? 0.3531 0.4356 0.3313 -0.1173 0.1054  -0.0965 412 ALA C O   
11530 C CB  . ALA C  412 ? 0.2309 0.3443 0.1989 -0.1050 0.0952  -0.0976 412 ALA C CB  
11531 N N   . GLN C  413 ? 0.2613 0.3233 0.2241 -0.1065 0.1021  -0.0884 413 GLN C N   
11532 C CA  . GLN C  413 ? 0.3099 0.3546 0.2688 -0.1119 0.1061  -0.0899 413 GLN C CA  
11533 C C   . GLN C  413 ? 0.3164 0.3500 0.2812 -0.1100 0.1089  -0.0861 413 GLN C C   
11534 O O   . GLN C  413 ? 0.3526 0.3797 0.3179 -0.1170 0.1132  -0.0903 413 GLN C O   
11535 C CB  . GLN C  413 ? 0.4701 0.4997 0.4192 -0.1079 0.1055  -0.0862 413 GLN C CB  
11536 C CG  . GLN C  413 ? 0.5551 0.5705 0.5001 -0.1143 0.1101  -0.0898 413 GLN C CG  
11537 C CD  . GLN C  413 ? 0.6540 0.6545 0.5920 -0.1092 0.1101  -0.0851 413 GLN C CD  
11538 O OE1 . GLN C  413 ? 0.7414 0.7304 0.6751 -0.1134 0.1140  -0.0880 413 GLN C OE1 
11539 N NE2 . GLN C  413 ? 0.6327 0.6334 0.5696 -0.1005 0.1062  -0.0782 413 GLN C NE2 
11540 N N   . LEU C  414 ? 0.3504 0.3817 0.3182 -0.1007 0.1067  -0.0786 414 LEU C N   
11541 C CA  . LEU C  414 ? 0.3227 0.3462 0.2951 -0.0980 0.1087  -0.0747 414 LEU C CA  
11542 C C   . LEU C  414 ? 0.3243 0.3588 0.3039 -0.1042 0.1111  -0.0788 414 LEU C C   
11543 O O   . LEU C  414 ? 0.3397 0.3650 0.3194 -0.1087 0.1152  -0.0802 414 LEU C O   
11544 C CB  . LEU C  414 ? 0.2586 0.2811 0.2327 -0.0878 0.1056  -0.0668 414 LEU C CB  
11545 C CG  . LEU C  414 ? 0.2175 0.2317 0.1944 -0.0850 0.1076  -0.0625 414 LEU C CG  
11546 C CD1 . LEU C  414 ? 0.2222 0.2189 0.1942 -0.0846 0.1098  -0.0608 414 LEU C CD1 
11547 C CD2 . LEU C  414 ? 0.2084 0.2265 0.1877 -0.0767 0.1047  -0.0565 414 LEU C CD2 
11548 N N   . ALA C  415 ? 0.2791 0.3338 0.2649 -0.1044 0.1087  -0.0810 415 ALA C N   
11549 C CA  . ALA C  415 ? 0.2894 0.3578 0.2839 -0.1100 0.1106  -0.0846 415 ALA C CA  
11550 C C   . ALA C  415 ? 0.3204 0.3848 0.3132 -0.1213 0.1145  -0.0917 415 ALA C C   
11551 O O   . ALA C  415 ? 0.3694 0.4265 0.3640 -0.1248 0.1184  -0.0914 415 ALA C O   
11552 C CB  . ALA C  415 ? 0.2253 0.3194 0.2272 -0.1095 0.1074  -0.0880 415 ALA C CB  
11553 N N   . GLY C  416 ? 0.2994 0.3673 0.2873 -0.1271 0.1138  -0.0978 416 GLY C N   
11554 C CA  . GLY C  416 ? 0.3151 0.3795 0.3000 -0.1389 0.1176  -0.1059 416 GLY C CA  
11555 C C   . GLY C  416 ? 0.3291 0.3679 0.3071 -0.1402 0.1231  -0.1048 416 GLY C C   
11556 O O   . GLY C  416 ? 0.3315 0.3669 0.3114 -0.1468 0.1274  -0.1079 416 GLY C O   
11557 N N   . ARG C  417 ? 0.2690 0.2904 0.2394 -0.1337 0.1231  -0.1003 417 ARG C N   
11558 C CA  . ARG C  417 ? 0.2913 0.2897 0.2557 -0.1338 0.1285  -0.0995 417 ARG C CA  
11559 C C   . ARG C  417 ? 0.2779 0.2702 0.2469 -0.1295 0.1306  -0.0936 417 ARG C C   
11560 O O   . ARG C  417 ? 0.2889 0.2655 0.2544 -0.1315 0.1362  -0.0940 417 ARG C O   
11561 C CB  . ARG C  417 ? 0.7653 0.7499 0.7230 -0.1269 0.1275  -0.0953 417 ARG C CB  
11562 C CG  . ARG C  417 ? 0.9534 0.9407 0.9047 -0.1319 0.1267  -0.1007 417 ARG C CG  
11563 C CD  . ARG C  417 ? 1.1139 1.0853 1.0571 -0.1398 0.1332  -0.1076 417 ARG C CD  
11564 N NE  . ARG C  417 ? 1.2272 1.2059 1.1646 -0.1477 0.1327  -0.1145 417 ARG C NE  
11565 C CZ  . ARG C  417 ? 1.2492 1.2298 1.1822 -0.1430 0.1289  -0.1109 417 ARG C CZ  
11566 N NH1 . ARG C  417 ? 1.2504 1.2258 1.1843 -0.1312 0.1256  -0.1016 417 ARG C NH1 
11567 N NH2 . ARG C  417 ? 1.2312 1.2195 1.1577 -0.1495 0.1282  -0.1167 417 ARG C NH2 
11568 N N   . LEU C  418 ? 0.3114 0.3160 0.2877 -0.1235 0.1267  -0.0880 418 LEU C N   
11569 C CA  . LEU C  418 ? 0.3482 0.3492 0.3284 -0.1208 0.1290  -0.0828 418 LEU C CA  
11570 C C   . LEU C  418 ? 0.3480 0.3576 0.3332 -0.1304 0.1325  -0.0878 418 LEU C C   
11571 O O   . LEU C  418 ? 0.3179 0.3164 0.3018 -0.1333 0.1377  -0.0870 418 LEU C O   
11572 C CB  . LEU C  418 ? 0.3715 0.3813 0.3565 -0.1109 0.1244  -0.0751 418 LEU C CB  
11573 C CG  . LEU C  418 ? 0.3466 0.3455 0.3270 -0.1012 0.1216  -0.0687 418 LEU C CG  
11574 C CD1 . LEU C  418 ? 0.3025 0.3096 0.2868 -0.0927 0.1177  -0.0621 418 LEU C CD1 
11575 C CD2 . LEU C  418 ? 0.2527 0.2323 0.2280 -0.1003 0.1258  -0.0665 418 LEU C CD2 
11576 N N   . ALA C  419 ? 0.5375 0.5675 0.5287 -0.1357 0.1299  -0.0930 419 ALA C N   
11577 C CA  . ALA C  419 ? 0.5995 0.6405 0.5969 -0.1456 0.1326  -0.0982 419 ALA C CA  
11578 C C   . ALA C  419 ? 0.6351 0.6615 0.6257 -0.1551 0.1382  -0.1044 419 ALA C C   
11579 O O   . ALA C  419 ? 0.6831 0.7084 0.6765 -0.1620 0.1423  -0.1059 419 ALA C O   
11580 C CB  . ALA C  419 ? 0.5702 0.6378 0.5756 -0.1496 0.1281  -0.1037 419 ALA C CB  
11581 N N   . ALA C  420 ? 0.5051 0.5198 0.4865 -0.1554 0.1387  -0.1078 420 ALA C N   
11582 C CA  . ALA C  420 ? 0.5138 0.5142 0.4873 -0.1641 0.1446  -0.1145 420 ALA C CA  
11583 C C   . ALA C  420 ? 0.4970 0.4727 0.4645 -0.1609 0.1510  -0.1102 420 ALA C C   
11584 O O   . ALA C  420 ? 0.5529 0.5177 0.5165 -0.1683 0.1571  -0.1143 420 ALA C O   
11585 C CB  . ALA C  420 ? 0.6390 0.6373 0.6043 -0.1661 0.1436  -0.1203 420 ALA C CB  
11586 N N   . GLN C  421 ? 0.4301 0.3975 0.3970 -0.1498 0.1494  -0.1018 421 GLN C N   
11587 C CA  . GLN C  421 ? 0.4857 0.4327 0.4484 -0.1457 0.1549  -0.0968 421 GLN C CA  
11588 C C   . GLN C  421 ? 0.5054 0.4581 0.4750 -0.1453 0.1555  -0.0912 421 GLN C C   
11589 O O   . GLN C  421 ? 0.4980 0.4376 0.4654 -0.1405 0.1587  -0.0849 421 GLN C O   
11590 C CB  . GLN C  421 ? 0.6830 0.6190 0.6418 -0.1344 0.1530  -0.0906 421 GLN C CB  
11591 C CG  . GLN C  421 ? 0.7463 0.6635 0.6956 -0.1349 0.1581  -0.0946 421 GLN C CG  
11592 C CD  . GLN C  421 ? 0.8026 0.7258 0.7485 -0.1386 0.1555  -0.1012 421 GLN C CD  
11593 O OE1 . GLN C  421 ? 0.8359 0.7712 0.7826 -0.1474 0.1549  -0.1081 421 GLN C OE1 
11594 N NE2 . GLN C  421 ? 0.8192 0.7350 0.7615 -0.1320 0.1538  -0.0986 421 GLN C NE2 
11595 N N   . GLY C  422 ? 0.7409 0.7143 0.7189 -0.1501 0.1523  -0.0932 422 GLY C N   
11596 C CA  . GLY C  422 ? 0.7736 0.7546 0.7586 -0.1528 0.1541  -0.0898 422 GLY C CA  
11597 C C   . GLY C  422 ? 0.7320 0.7183 0.7212 -0.1432 0.1514  -0.0805 422 GLY C C   
11598 O O   . GLY C  422 ? 0.7676 0.7469 0.7568 -0.1425 0.1553  -0.0751 422 GLY C O   
11599 N N   . ALA C  423 ? 0.4897 0.4883 0.4820 -0.1360 0.1451  -0.0785 423 ALA C N   
11600 C CA  . ALA C  423 ? 0.4061 0.4139 0.4032 -0.1278 0.1423  -0.0710 423 ALA C CA  
11601 C C   . ALA C  423 ? 0.4454 0.4782 0.4527 -0.1305 0.1395  -0.0736 423 ALA C C   
11602 O O   . ALA C  423 ? 0.4602 0.5048 0.4705 -0.1356 0.1372  -0.0805 423 ALA C O   
11603 C CB  . ALA C  423 ? 0.2971 0.3000 0.2903 -0.1171 0.1377  -0.0664 423 ALA C CB  
11604 N N   . ARG C  424 ? 0.4097 0.4518 0.4224 -0.1274 0.1402  -0.0684 424 ARG C N   
11605 C CA  . ARG C  424 ? 0.4298 0.4963 0.4528 -0.1288 0.1381  -0.0707 424 ARG C CA  
11606 C C   . ARG C  424 ? 0.3911 0.4648 0.4139 -0.1196 0.1320  -0.0697 424 ARG C C   
11607 O O   . ARG C  424 ? 0.4370 0.5036 0.4558 -0.1102 0.1304  -0.0633 424 ARG C O   
11608 C CB  . ARG C  424 ? 0.7078 0.7812 0.7357 -0.1276 0.1414  -0.0651 424 ARG C CB  
11609 C CG  . ARG C  424 ? 0.8029 0.9008 0.8429 -0.1335 0.1421  -0.0691 424 ARG C CG  
11610 C CD  . ARG C  424 ? 0.9086 1.0083 0.9522 -0.1370 0.1480  -0.0646 424 ARG C CD  
11611 N NE  . ARG C  424 ? 1.0086 1.0958 1.0496 -0.1479 0.1533  -0.0666 424 ARG C NE  
11612 C CZ  . ARG C  424 ? 1.0242 1.0918 1.0577 -0.1482 0.1582  -0.0612 424 ARG C CZ  
11613 N NH1 . ARG C  424 ? 1.0145 1.0739 1.0424 -0.1384 0.1580  -0.0534 424 ARG C NH1 
11614 N NH2 . ARG C  424 ? 1.0066 1.0630 1.0379 -0.1585 0.1632  -0.0638 424 ARG C NH2 
11615 N N   . VAL C  425 ? 0.3590 0.4471 0.3859 -0.1224 0.1285  -0.0761 425 VAL C N   
11616 C CA  . VAL C  425 ? 0.3254 0.4203 0.3518 -0.1138 0.1232  -0.0750 425 VAL C CA  
11617 C C   . VAL C  425 ? 0.3194 0.4406 0.3564 -0.1127 0.1209  -0.0779 425 VAL C C   
11618 O O   . VAL C  425 ? 0.3807 0.5175 0.4248 -0.1209 0.1210  -0.0845 425 VAL C O   
11619 C CB  . VAL C  425 ? 0.2424 0.3314 0.2628 -0.1159 0.1206  -0.0795 425 VAL C CB  
11620 C CG1 . VAL C  425 ? 0.2292 0.3290 0.2502 -0.1081 0.1153  -0.0791 425 VAL C CG1 
11621 C CG2 . VAL C  425 ? 0.2704 0.3337 0.2804 -0.1144 0.1225  -0.0763 425 VAL C CG2 
11622 N N   . TYR C  426 ? 0.2278 0.3551 0.2662 -0.1026 0.1188  -0.0735 426 TYR C N   
11623 C CA  . TYR C  426 ? 0.2222 0.3746 0.2700 -0.0994 0.1160  -0.0769 426 TYR C CA  
11624 C C   . TYR C  426 ? 0.2601 0.4125 0.3032 -0.0921 0.1112  -0.0774 426 TYR C C   
11625 O O   . TYR C  426 ? 0.2879 0.4220 0.3218 -0.0861 0.1104  -0.0722 426 TYR C O   
11626 C CB  . TYR C  426 ? 0.2705 0.4321 0.3240 -0.0935 0.1182  -0.0727 426 TYR C CB  
11627 C CG  . TYR C  426 ? 0.2972 0.4577 0.3542 -0.1009 0.1237  -0.0714 426 TYR C CG  
11628 C CD1 . TYR C  426 ? 0.3336 0.4727 0.3824 -0.1010 0.1271  -0.0655 426 TYR C CD1 
11629 C CD2 . TYR C  426 ? 0.3080 0.4894 0.3766 -0.1080 0.1253  -0.0761 426 TYR C CD2 
11630 C CE1 . TYR C  426 ? 0.4063 0.5435 0.4574 -0.1079 0.1325  -0.0640 426 TYR C CE1 
11631 C CE2 . TYR C  426 ? 0.3478 0.5272 0.4192 -0.1156 0.1308  -0.0747 426 TYR C CE2 
11632 C CZ  . TYR C  426 ? 0.4042 0.5607 0.4663 -0.1154 0.1347  -0.0684 426 TYR C CZ  
11633 O OH  . TYR C  426 ? 0.4130 0.5663 0.4768 -0.1227 0.1405  -0.0664 426 TYR C OH  
11634 N N   . ALA C  427 ? 0.3185 0.4921 0.3680 -0.0929 0.1079  -0.0835 427 ALA C N   
11635 C CA  . ALA C  427 ? 0.2856 0.4605 0.3300 -0.0865 0.1036  -0.0845 427 ALA C CA  
11636 C C   . ALA C  427 ? 0.2731 0.4731 0.3259 -0.0784 0.1003  -0.0871 427 ALA C C   
11637 O O   . ALA C  427 ? 0.2716 0.4957 0.3367 -0.0810 0.0997  -0.0917 427 ALA C O   
11638 C CB  . ALA C  427 ? 0.2152 0.3893 0.2556 -0.0947 0.1022  -0.0898 427 ALA C CB  
11639 N N   . TYR C  428 ? 0.2065 0.4008 0.2526 -0.0680 0.0980  -0.0844 428 TYR C N   
11640 C CA  . TYR C  428 ? 0.2246 0.4397 0.2772 -0.0576 0.0951  -0.0866 428 TYR C CA  
11641 C C   . TYR C  428 ? 0.2415 0.4576 0.2864 -0.0507 0.0909  -0.0884 428 TYR C C   
11642 O O   . TYR C  428 ? 0.2297 0.4247 0.2619 -0.0523 0.0910  -0.0857 428 TYR C O   
11643 C CB  . TYR C  428 ? 0.2418 0.4494 0.2936 -0.0487 0.0973  -0.0814 428 TYR C CB  
11644 C CG  . TYR C  428 ? 0.2288 0.4113 0.2669 -0.0424 0.0971  -0.0759 428 TYR C CG  
11645 C CD1 . TYR C  428 ? 0.2356 0.4187 0.2680 -0.0330 0.0937  -0.0770 428 TYR C CD1 
11646 C CD2 . TYR C  428 ? 0.1895 0.3490 0.2205 -0.0455 0.0999  -0.0698 428 TYR C CD2 
11647 C CE1 . TYR C  428 ? 0.2510 0.4118 0.2712 -0.0284 0.0935  -0.0725 428 TYR C CE1 
11648 C CE2 . TYR C  428 ? 0.1878 0.3276 0.2079 -0.0401 0.0990  -0.0651 428 TYR C CE2 
11649 C CZ  . TYR C  428 ? 0.2408 0.3808 0.2556 -0.0322 0.0960  -0.0666 428 TYR C CZ  
11650 O OH  . TYR C  428 ? 0.2185 0.3393 0.2223 -0.0275 0.0950  -0.0625 428 TYR C OH  
11651 N N   . ILE C  429 ? 0.4051 0.6440 0.4567 -0.0416 0.0864  -0.0921 429 ILE C N   
11652 C CA  . ILE C  429 ? 0.4562 0.6847 0.4967 -0.0307 0.0771  -0.0895 429 ILE C CA  
11653 C C   . ILE C  429 ? 0.4584 0.6939 0.5021 -0.0159 0.0745  -0.0887 429 ILE C C   
11654 O O   . ILE C  429 ? 0.4632 0.7238 0.5206 -0.0119 0.0734  -0.0923 429 ILE C O   
11655 C CB  . ILE C  429 ? 0.3166 0.5555 0.3569 -0.0329 0.0683  -0.0923 429 ILE C CB  
11656 C CG1 . ILE C  429 ? 0.3063 0.5315 0.3329 -0.0219 0.0592  -0.0885 429 ILE C CG1 
11657 C CG2 . ILE C  429 ? 0.3362 0.6082 0.3938 -0.0320 0.0650  -0.0977 429 ILE C CG2 
11658 C CD1 . ILE C  429 ? 0.3219 0.5639 0.3502 -0.0196 0.0491  -0.0912 429 ILE C CD1 
11659 N N   . PHE C  430 ? 0.3954 0.6085 0.4266 -0.0081 0.0738  -0.0843 430 PHE C N   
11660 C CA  . PHE C  430 ? 0.3579 0.5723 0.3898 0.0053  0.0729  -0.0838 430 PHE C CA  
11661 C C   . PHE C  430 ? 0.3680 0.5821 0.3949 0.0174  0.0621  -0.0830 430 PHE C C   
11662 O O   . PHE C  430 ? 0.4143 0.6070 0.4270 0.0191  0.0575  -0.0791 430 PHE C O   
11663 C CB  . PHE C  430 ? 0.2392 0.4282 0.2596 0.0063  0.0777  -0.0798 430 PHE C CB  
11664 C CG  . PHE C  430 ? 0.2514 0.4397 0.2713 0.0187  0.0780  -0.0800 430 PHE C CG  
11665 C CD1 . PHE C  430 ? 0.2100 0.3846 0.2200 0.0306  0.0707  -0.0782 430 PHE C CD1 
11666 C CD2 . PHE C  430 ? 0.1968 0.3963 0.2248 0.0182  0.0858  -0.0820 430 PHE C CD2 
11667 C CE1 . PHE C  430 ? 0.2151 0.3873 0.2237 0.0422  0.0711  -0.0792 430 PHE C CE1 
11668 C CE2 . PHE C  430 ? 0.2021 0.3988 0.2283 0.0296  0.0857  -0.0821 430 PHE C CE2 
11669 C CZ  . PHE C  430 ? 0.2106 0.3953 0.2274 0.0420  0.0790  -0.0819 430 PHE C CZ  
11670 N N   . GLU C  431 ? 0.2311 0.4700 0.2702 0.0255  0.0583  -0.0865 431 GLU C N   
11671 C CA  . GLU C  431 ? 0.2708 0.5127 0.3066 0.0381  0.0476  -0.0858 431 GLU C CA  
11672 C C   . GLU C  431 ? 0.2965 0.5334 0.3296 0.0550  0.0450  -0.0851 431 GLU C C   
11673 O O   . GLU C  431 ? 0.3687 0.6071 0.3988 0.0667  0.0360  -0.0842 431 GLU C O   
11674 C CB  . GLU C  431 ? 0.4573 0.7305 0.5073 0.0367  0.0425  -0.0902 431 GLU C CB  
11675 C CG  . GLU C  431 ? 0.5351 0.8039 0.5777 0.0281  0.0368  -0.0893 431 GLU C CG  
11676 C CD  . GLU C  431 ? 0.5627 0.8619 0.6207 0.0193  0.0353  -0.0948 431 GLU C CD  
11677 O OE1 . GLU C  431 ? 0.5619 0.8829 0.6366 0.0152  0.0416  -0.0989 431 GLU C OE1 
11678 O OE2 . GLU C  431 ? 0.5671 0.8685 0.6199 0.0160  0.0279  -0.0951 431 GLU C OE2 
11679 N N   . HIS C  432 ? 0.2935 0.5246 0.3271 0.0570  0.0525  -0.0857 432 HIS C N   
11680 C CA  . HIS C  432 ? 0.2710 0.4993 0.3028 0.0735  0.0502  -0.0864 432 HIS C CA  
11681 C C   . HIS C  432 ? 0.2535 0.4473 0.2660 0.0798  0.0469  -0.0819 432 HIS C C   
11682 O O   . HIS C  432 ? 0.2406 0.4144 0.2442 0.0728  0.0522  -0.0798 432 HIS C O   
11683 C CB  . HIS C  432 ? 0.3304 0.5723 0.3723 0.0752  0.0593  -0.0901 432 HIS C CB  
11684 C CG  . HIS C  432 ? 0.4015 0.6415 0.4416 0.0928  0.0572  -0.0919 432 HIS C CG  
11685 N ND1 . HIS C  432 ? 0.4359 0.6997 0.4876 0.1055  0.0527  -0.0952 432 HIS C ND1 
11686 C CD2 . HIS C  432 ? 0.4112 0.6275 0.4386 0.1001  0.0587  -0.0910 432 HIS C CD2 
11687 C CE1 . HIS C  432 ? 0.4341 0.6881 0.4802 0.1204  0.0520  -0.0964 432 HIS C CE1 
11688 N NE2 . HIS C  432 ? 0.4173 0.6420 0.4481 0.1171  0.0555  -0.0941 432 HIS C NE2 
11689 N N   . ARG C  433 ? 0.3261 0.5132 0.3322 0.0931  0.0381  -0.0805 433 ARG C N   
11690 C CA  . ARG C  433 ? 0.3545 0.5087 0.3426 0.0998  0.0351  -0.0767 433 ARG C CA  
11691 C C   . ARG C  433 ? 0.3501 0.5010 0.3386 0.1111  0.0385  -0.0799 433 ARG C C   
11692 O O   . ARG C  433 ? 0.3767 0.5469 0.3751 0.1232  0.0370  -0.0837 433 ARG C O   
11693 C CB  . ARG C  433 ? 0.3939 0.5380 0.3725 0.1089  0.0245  -0.0729 433 ARG C CB  
11694 C CG  . ARG C  433 ? 0.4400 0.5484 0.3995 0.1147  0.0215  -0.0687 433 ARG C CG  
11695 C CD  . ARG C  433 ? 0.4866 0.5850 0.4362 0.1250  0.0111  -0.0644 433 ARG C CD  
11696 N NE  . ARG C  433 ? 0.5312 0.5963 0.4638 0.1331  0.0083  -0.0610 433 ARG C NE  
11697 C CZ  . ARG C  433 ? 0.5493 0.5865 0.4652 0.1277  0.0056  -0.0549 433 ARG C CZ  
11698 N NH1 . ARG C  433 ? 0.5063 0.5448 0.4196 0.1151  0.0056  -0.0515 433 ARG C NH1 
11699 N NH2 . ARG C  433 ? 0.5923 0.5999 0.4937 0.1348  0.0033  -0.0524 433 ARG C NH2 
11700 N N   . ALA C  434 ? 0.3237 0.4511 0.3013 0.1073  0.0429  -0.0788 434 ALA C N   
11701 C CA  . ALA C  434 ? 0.3430 0.4655 0.3189 0.1167  0.0466  -0.0824 434 ALA C CA  
11702 C C   . ALA C  434 ? 0.3865 0.4977 0.3553 0.1342  0.0392  -0.0828 434 ALA C C   
11703 O O   . ALA C  434 ? 0.4420 0.5343 0.3996 0.1365  0.0318  -0.0782 434 ALA C O   
11704 C CB  . ALA C  434 ? 0.3402 0.4381 0.3042 0.1085  0.0513  -0.0808 434 ALA C CB  
11705 N N   . SER C  435 ? 0.3213 0.4435 0.2959 0.1467  0.0414  -0.0880 435 SER C N   
11706 C CA  . SER C  435 ? 0.3850 0.4952 0.3527 0.1649  0.0350  -0.0890 435 SER C CA  
11707 C C   . SER C  435 ? 0.4694 0.5399 0.4166 0.1663  0.0334  -0.0871 435 SER C C   
11708 O O   . SER C  435 ? 0.5247 0.5743 0.4607 0.1774  0.0265  -0.0853 435 SER C O   
11709 C CB  . SER C  435 ? 0.4669 0.6013 0.4472 0.1784  0.0387  -0.0958 435 SER C CB  
11710 O OG  . SER C  435 ? 0.4628 0.5935 0.4409 0.1762  0.0473  -0.0998 435 SER C OG  
11711 N N   . THR C  436 ? 0.5761 0.6362 0.5184 0.1544  0.0398  -0.0874 436 THR C N   
11712 C CA  . THR C  436 ? 0.6617 0.6872 0.5864 0.1534  0.0389  -0.0864 436 THR C CA  
11713 C C   . THR C  436 ? 0.7029 0.7067 0.6171 0.1415  0.0351  -0.0794 436 THR C C   
11714 O O   . THR C  436 ? 0.7524 0.7300 0.6537 0.1362  0.0352  -0.0780 436 THR C O   
11715 C CB  . THR C  436 ? 0.7777 0.8032 0.7017 0.1475  0.0471  -0.0904 436 THR C CB  
11716 O OG1 . THR C  436 ? 0.7816 0.8300 0.7176 0.1345  0.0534  -0.0896 436 THR C OG1 
11717 C CG2 . THR C  436 ? 0.7961 0.8306 0.7230 0.1619  0.0500  -0.0975 436 THR C CG2 
11718 N N   . LEU C  437 ? 0.6807 0.6970 0.6008 0.1364  0.0322  -0.0754 437 LEU C N   
11719 C CA  . LEU C  437 ? 0.6390 0.6376 0.5497 0.1248  0.0295  -0.0689 437 LEU C CA  
11720 C C   . LEU C  437 ? 0.6743 0.6403 0.5677 0.1307  0.0228  -0.0649 437 LEU C C   
11721 O O   . LEU C  437 ? 0.7093 0.6714 0.5994 0.1446  0.0168  -0.0646 437 LEU C O   
11722 C CB  . LEU C  437 ? 0.4985 0.5172 0.4178 0.1189  0.0276  -0.0660 437 LEU C CB  
11723 C CG  . LEU C  437 ? 0.4636 0.4775 0.3808 0.1015  0.0311  -0.0623 437 LEU C CG  
11724 C CD1 . LEU C  437 ? 0.4595 0.5013 0.3922 0.0926  0.0378  -0.0653 437 LEU C CD1 
11725 C CD2 . LEU C  437 ? 0.4576 0.4624 0.3667 0.0985  0.0251  -0.0564 437 LEU C CD2 
11726 N N   . THR C  438 ? 0.6752 0.6178 0.5578 0.1201  0.0241  -0.0618 438 THR C N   
11727 C CA  . THR C  438 ? 0.6930 0.6023 0.5584 0.1219  0.0189  -0.0576 438 THR C CA  
11728 C C   . THR C  438 ? 0.7035 0.6066 0.5629 0.1179  0.0140  -0.0501 438 THR C C   
11729 O O   . THR C  438 ? 0.7405 0.6204 0.5867 0.1241  0.0082  -0.0460 438 THR C O   
11730 C CB  . THR C  438 ? 0.7093 0.5985 0.5670 0.1107  0.0225  -0.0575 438 THR C CB  
11731 O OG1 . THR C  438 ? 0.6809 0.5893 0.5494 0.1040  0.0296  -0.0619 438 THR C OG1 
11732 C CG2 . THR C  438 ? 0.7602 0.6221 0.6051 0.1193  0.0197  -0.0601 438 THR C CG2 
11733 N N   . TRP C  439 ? 0.6299 0.5525 0.4978 0.1074  0.0165  -0.0484 439 TRP C N   
11734 C CA  . TRP C  439 ? 0.5915 0.5102 0.4533 0.1019  0.0128  -0.0418 439 TRP C CA  
11735 C C   . TRP C  439 ? 0.6265 0.5537 0.4880 0.1146  0.0054  -0.0401 439 TRP C C   
11736 O O   . TRP C  439 ? 0.6508 0.5964 0.5223 0.1259  0.0042  -0.0449 439 TRP C O   
11737 C CB  . TRP C  439 ? 0.4849 0.4228 0.3561 0.0877  0.0181  -0.0417 439 TRP C CB  
11738 C CG  . TRP C  439 ? 0.4654 0.3937 0.3354 0.0747  0.0245  -0.0415 439 TRP C CG  
11739 C CD1 . TRP C  439 ? 0.4339 0.3735 0.3134 0.0702  0.0309  -0.0461 439 TRP C CD1 
11740 C CD2 . TRP C  439 ? 0.4857 0.3924 0.3445 0.0647  0.0250  -0.0361 439 TRP C CD2 
11741 N NE1 . TRP C  439 ? 0.4225 0.3492 0.2977 0.0586  0.0348  -0.0439 439 TRP C NE1 
11742 C CE2 . TRP C  439 ? 0.4540 0.3614 0.3174 0.0549  0.0314  -0.0380 439 TRP C CE2 
11743 C CE3 . TRP C  439 ? 0.5303 0.4176 0.3755 0.0630  0.0209  -0.0295 439 TRP C CE3 
11744 C CZ2 . TRP C  439 ? 0.4819 0.3732 0.3385 0.0438  0.0336  -0.0341 439 TRP C CZ2 
11745 C CZ3 . TRP C  439 ? 0.5264 0.3971 0.3644 0.0512  0.0238  -0.0255 439 TRP C CZ3 
11746 C CH2 . TRP C  439 ? 0.5041 0.3779 0.3487 0.0419  0.0300  -0.0280 439 TRP C CH2 
11747 N N   . PRO C  440 ? 0.6076 0.5227 0.4576 0.1130  0.0004  -0.0333 440 PRO C N   
11748 C CA  . PRO C  440 ? 0.5952 0.5169 0.4432 0.1263  -0.0077 -0.0311 440 PRO C CA  
11749 C C   . PRO C  440 ? 0.5566 0.5157 0.4214 0.1271  -0.0082 -0.0351 440 PRO C C   
11750 O O   . PRO C  440 ? 0.5217 0.5000 0.3989 0.1165  -0.0019 -0.0391 440 PRO C O   
11751 C CB  . PRO C  440 ? 0.6870 0.5882 0.5181 0.1208  -0.0116 -0.0225 440 PRO C CB  
11752 C CG  . PRO C  440 ? 0.6888 0.5868 0.5199 0.1024  -0.0043 -0.0216 440 PRO C CG  
11753 C CD  . PRO C  440 ? 0.6708 0.5664 0.5089 0.0997  0.0019  -0.0271 440 PRO C CD  
11754 N N   . LEU C  441 ? 0.5707 0.5399 0.4358 0.1395  -0.0160 -0.0337 441 LEU C N   
11755 C CA  . LEU C  441 ? 0.5433 0.5499 0.4260 0.1414  -0.0172 -0.0384 441 LEU C CA  
11756 C C   . LEU C  441 ? 0.5198 0.5386 0.4030 0.1277  -0.0171 -0.0364 441 LEU C C   
11757 O O   . LEU C  441 ? 0.4722 0.5204 0.3711 0.1219  -0.0147 -0.0414 441 LEU C O   
11758 C CB  . LEU C  441 ? 0.5933 0.6099 0.4779 0.1605  -0.0260 -0.0384 441 LEU C CB  
11759 C CG  . LEU C  441 ? 0.6173 0.6759 0.5227 0.1634  -0.0276 -0.0440 441 LEU C CG  
11760 C CD1 . LEU C  441 ? 0.6277 0.7058 0.5509 0.1591  -0.0185 -0.0518 441 LEU C CD1 
11761 C CD2 . LEU C  441 ? 0.6442 0.7135 0.5517 0.1834  -0.0372 -0.0435 441 LEU C CD2 
11762 N N   . TRP C  442 ? 0.6762 0.6717 0.5418 0.1219  -0.0193 -0.0294 442 TRP C N   
11763 C CA  . TRP C  442 ? 0.6809 0.6862 0.5443 0.1105  -0.0199 -0.0275 442 TRP C CA  
11764 C C   . TRP C  442 ? 0.6523 0.6657 0.5244 0.0936  -0.0104 -0.0312 442 TRP C C   
11765 O O   . TRP C  442 ? 0.6816 0.7103 0.5572 0.0842  -0.0096 -0.0324 442 TRP C O   
11766 C CB  . TRP C  442 ? 0.5718 0.5506 0.4131 0.1093  -0.0243 -0.0186 442 TRP C CB  
11767 C CG  . TRP C  442 ? 0.6213 0.5698 0.4506 0.1003  -0.0184 -0.0146 442 TRP C CG  
11768 C CD1 . TRP C  442 ? 0.7021 0.6215 0.5196 0.1064  -0.0194 -0.0107 442 TRP C CD1 
11769 C CD2 . TRP C  442 ? 0.5919 0.5364 0.4199 0.0834  -0.0108 -0.0141 442 TRP C CD2 
11770 N NE1 . TRP C  442 ? 0.6894 0.5883 0.4992 0.0936  -0.0130 -0.0079 442 TRP C NE1 
11771 C CE2 . TRP C  442 ? 0.6343 0.5488 0.4508 0.0800  -0.0076 -0.0098 442 TRP C CE2 
11772 C CE3 . TRP C  442 ? 0.5615 0.5244 0.3971 0.0712  -0.0063 -0.0172 442 TRP C CE3 
11773 C CZ2 . TRP C  442 ? 0.6275 0.5327 0.4412 0.0652  -0.0003 -0.0084 442 TRP C CZ2 
11774 C CZ3 . TRP C  442 ? 0.5784 0.5301 0.4103 0.0574  0.0012  -0.0157 442 TRP C CZ3 
11775 C CH2 . TRP C  442 ? 0.6072 0.5315 0.4288 0.0547  0.0041  -0.0112 442 TRP C CH2 
11776 N N   . MET C  443 ? 0.4093 0.4119 0.2843 0.0902  -0.0034 -0.0331 443 MET C N   
11777 C CA  . MET C  443 ? 0.3373 0.3453 0.2198 0.0755  0.0057  -0.0361 443 MET C CA  
11778 C C   . MET C  443 ? 0.3187 0.3570 0.2211 0.0742  0.0096  -0.0434 443 MET C C   
11779 O O   . MET C  443 ? 0.3022 0.3473 0.2117 0.0624  0.0169  -0.0459 443 MET C O   
11780 C CB  . MET C  443 ? 0.4268 0.4106 0.3030 0.0718  0.0111  -0.0346 443 MET C CB  
11781 C CG  . MET C  443 ? 0.4724 0.4278 0.3305 0.0670  0.0098  -0.0273 443 MET C CG  
11782 S SD  . MET C  443 ? 0.4629 0.3901 0.3138 0.0635  0.0144  -0.0259 443 MET C SD  
11783 C CE  . MET C  443 ? 0.3513 0.2955 0.2174 0.0518  0.0240  -0.0314 443 MET C CE  
11784 N N   . GLY C  444 ? 0.4751 0.5316 0.3867 0.0863  0.0049  -0.0466 444 GLY C N   
11785 C CA  . GLY C  444 ? 0.4446 0.5333 0.3756 0.0845  0.0079  -0.0532 444 GLY C CA  
11786 C C   . GLY C  444 ? 0.4051 0.4976 0.3460 0.0797  0.0173  -0.0574 444 GLY C C   
11787 O O   . GLY C  444 ? 0.4003 0.4831 0.3398 0.0879  0.0187  -0.0582 444 GLY C O   
11788 N N   . VAL C  445 ? 0.2781 0.3835 0.2277 0.0664  0.0237  -0.0600 445 VAL C N   
11789 C CA  . VAL C  445 ? 0.2824 0.3907 0.2399 0.0603  0.0330  -0.0630 445 VAL C CA  
11790 C C   . VAL C  445 ? 0.3024 0.3911 0.2506 0.0477  0.0377  -0.0596 445 VAL C C   
11791 O O   . VAL C  445 ? 0.3064 0.4032 0.2592 0.0362  0.0418  -0.0607 445 VAL C O   
11792 C CB  . VAL C  445 ? 0.2492 0.3878 0.2246 0.0544  0.0374  -0.0684 445 VAL C CB  
11793 C CG1 . VAL C  445 ? 0.2391 0.3806 0.2217 0.0512  0.0467  -0.0710 445 VAL C CG1 
11794 C CG2 . VAL C  445 ? 0.3023 0.4649 0.2882 0.0652  0.0314  -0.0715 445 VAL C CG2 
11795 N N   . PRO C  446 ? 0.2657 0.3283 0.2010 0.0500  0.0372  -0.0557 446 PRO C N   
11796 C CA  . PRO C  446 ? 0.2637 0.3069 0.1893 0.0395  0.0405  -0.0518 446 PRO C CA  
11797 C C   . PRO C  446 ? 0.2483 0.2963 0.1815 0.0296  0.0494  -0.0539 446 PRO C C   
11798 O O   . PRO C  446 ? 0.2412 0.3030 0.1847 0.0317  0.0533  -0.0578 446 PRO C O   
11799 C CB  . PRO C  446 ? 0.2767 0.2946 0.1900 0.0458  0.0380  -0.0485 446 PRO C CB  
11800 C CG  . PRO C  446 ? 0.2884 0.3103 0.2025 0.0604  0.0321  -0.0501 446 PRO C CG  
11801 C CD  . PRO C  446 ? 0.3524 0.4032 0.2828 0.0624  0.0344  -0.0557 446 PRO C CD  
11802 N N   . HIS C  447 ? 0.2484 0.2847 0.1758 0.0194  0.0528  -0.0510 447 HIS C N   
11803 C CA  . HIS C  447 ? 0.2409 0.2767 0.1727 0.0102  0.0609  -0.0515 447 HIS C CA  
11804 C C   . HIS C  447 ? 0.2315 0.2614 0.1641 0.0144  0.0637  -0.0524 447 HIS C C   
11805 O O   . HIS C  447 ? 0.2415 0.2566 0.1660 0.0208  0.0600  -0.0508 447 HIS C O   
11806 C CB  . HIS C  447 ? 0.3177 0.3370 0.2399 0.0023  0.0621  -0.0473 447 HIS C CB  
11807 C CG  . HIS C  447 ? 0.3609 0.3786 0.2867 -0.0069 0.0699  -0.0472 447 HIS C CG  
11808 N ND1 . HIS C  447 ? 0.4002 0.4314 0.3347 -0.0136 0.0750  -0.0499 447 HIS C ND1 
11809 C CD2 . HIS C  447 ? 0.3681 0.3720 0.2898 -0.0105 0.0731  -0.0444 447 HIS C CD2 
11810 C CE1 . HIS C  447 ? 0.4076 0.4322 0.3425 -0.0199 0.0811  -0.0486 447 HIS C CE1 
11811 N NE2 . HIS C  447 ? 0.3910 0.4003 0.3188 -0.0179 0.0799  -0.0453 447 HIS C NE2 
11812 N N   . GLY C  448 ? 0.3108 0.3515 0.2521 0.0107  0.0702  -0.0549 448 GLY C N   
11813 C CA  . GLY C  448 ? 0.3129 0.3479 0.2534 0.0138  0.0732  -0.0556 448 GLY C CA  
11814 C C   . GLY C  448 ? 0.3255 0.3709 0.2706 0.0241  0.0722  -0.0595 448 GLY C C   
11815 O O   . GLY C  448 ? 0.3269 0.3694 0.2711 0.0266  0.0753  -0.0608 448 GLY C O   
11816 N N   . TYR C  449 ? 0.3026 0.3608 0.2523 0.0303  0.0678  -0.0615 449 TYR C N   
11817 C CA  . TYR C  449 ? 0.2507 0.3194 0.2050 0.0419  0.0664  -0.0653 449 TYR C CA  
11818 C C   . TYR C  449 ? 0.2477 0.3425 0.2164 0.0409  0.0717  -0.0693 449 TYR C C   
11819 O O   . TYR C  449 ? 0.2754 0.3829 0.2498 0.0504  0.0710  -0.0728 449 TYR C O   
11820 C CB  . TYR C  449 ? 0.2869 0.3503 0.2359 0.0528  0.0577  -0.0648 449 TYR C CB  
11821 C CG  . TYR C  449 ? 0.3673 0.4023 0.3014 0.0543  0.0544  -0.0613 449 TYR C CG  
11822 C CD1 . TYR C  449 ? 0.3984 0.4188 0.3244 0.0462  0.0528  -0.0565 449 TYR C CD1 
11823 C CD2 . TYR C  449 ? 0.3962 0.4188 0.3244 0.0624  0.0539  -0.0631 449 TYR C CD2 
11824 C CE1 . TYR C  449 ? 0.4225 0.4180 0.3360 0.0458  0.0505  -0.0533 449 TYR C CE1 
11825 C CE2 . TYR C  449 ? 0.4149 0.4110 0.3297 0.0619  0.0511  -0.0602 449 TYR C CE2 
11826 C CZ  . TYR C  449 ? 0.4388 0.4219 0.3468 0.0533  0.0495  -0.0551 449 TYR C CZ  
11827 O OH  . TYR C  449 ? 0.4776 0.4355 0.3734 0.0514  0.0471  -0.0520 449 TYR C OH  
11828 N N   . GLU C  450 ? 0.2145 0.3172 0.1891 0.0292  0.0773  -0.0689 450 GLU C N   
11829 C CA  . GLU C  450 ? 0.2583 0.3820 0.2451 0.0264  0.0842  -0.0721 450 GLU C CA  
11830 C C   . GLU C  450 ? 0.2522 0.3657 0.2352 0.0264  0.0892  -0.0702 450 GLU C C   
11831 O O   . GLU C  450 ? 0.2434 0.3661 0.2331 0.0287  0.0917  -0.0702 450 GLU C O   
11832 C CB  . GLU C  450 ? 0.3507 0.4850 0.3450 0.0138  0.0879  -0.0721 450 GLU C CB  
11833 C CG  . GLU C  450 ? 0.4472 0.5640 0.4377 0.0039  0.0912  -0.0659 450 GLU C CG  
11834 C CD  . GLU C  450 ? 0.5522 0.6510 0.5320 -0.0003 0.0898  -0.0636 450 GLU C CD  
11835 O OE1 . GLU C  450 ? 0.5384 0.6231 0.5082 0.0049  0.0881  -0.0632 450 GLU C OE1 
11836 O OE2 . GLU C  450 ? 0.6119 0.7096 0.5932 -0.0090 0.0902  -0.0622 450 GLU C OE2 
11837 N N   . ILE C  451 ? 0.3006 0.3931 0.2725 0.0239  0.0891  -0.0673 451 ILE C N   
11838 C CA  . ILE C  451 ? 0.2635 0.3438 0.2309 0.0222  0.0916  -0.0631 451 ILE C CA  
11839 C C   . ILE C  451 ? 0.2774 0.3605 0.2443 0.0312  0.0927  -0.0653 451 ILE C C   
11840 O O   . ILE C  451 ? 0.2716 0.3571 0.2410 0.0293  0.0961  -0.0623 451 ILE C O   
11841 C CB  . ILE C  451 ? 0.2540 0.3136 0.2100 0.0197  0.0901  -0.0608 451 ILE C CB  
11842 C CG1 . ILE C  451 ? 0.2029 0.2583 0.1602 0.0095  0.0900  -0.0566 451 ILE C CG1 
11843 C CG2 . ILE C  451 ? 0.2117 0.2630 0.1630 0.0207  0.0909  -0.0580 451 ILE C CG2 
11844 C CD1 . ILE C  451 ? 0.2038 0.2408 0.1521 0.0062  0.0886  -0.0537 451 ILE C CD1 
11845 N N   . GLU C  452 ? 0.3217 0.4039 0.2846 0.0416  0.0893  -0.0706 452 GLU C N   
11846 C CA  . GLU C  452 ? 0.3305 0.4126 0.2918 0.0506  0.0897  -0.0731 452 GLU C CA  
11847 C C   . GLU C  452 ? 0.3283 0.4309 0.3023 0.0511  0.0931  -0.0735 452 GLU C C   
11848 O O   . GLU C  452 ? 0.3316 0.4343 0.3053 0.0536  0.0963  -0.0735 452 GLU C O   
11849 C CB  . GLU C  452 ? 0.2455 0.3197 0.1989 0.0636  0.0839  -0.0779 452 GLU C CB  
11850 C CG  . GLU C  452 ? 0.3932 0.4762 0.3514 0.0691  0.0783  -0.0788 452 GLU C CG  
11851 C CD  . GLU C  452 ? 0.3998 0.4599 0.3459 0.0768  0.0699  -0.0775 452 GLU C CD  
11852 O OE1 . GLU C  452 ? 0.3934 0.4332 0.3301 0.0700  0.0674  -0.0735 452 GLU C OE1 
11853 O OE2 . GLU C  452 ? 0.4038 0.4662 0.3500 0.0895  0.0660  -0.0804 452 GLU C OE2 
11854 N N   . PHE C  453 ? 0.3474 0.4675 0.3324 0.0480  0.0927  -0.0740 453 PHE C N   
11855 C CA  . PHE C  453 ? 0.3790 0.5204 0.3774 0.0475  0.0957  -0.0747 453 PHE C CA  
11856 C C   . PHE C  453 ? 0.3825 0.5237 0.3840 0.0367  0.1014  -0.0694 453 PHE C C   
11857 O O   . PHE C  453 ? 0.3785 0.5282 0.3850 0.0373  0.1055  -0.0689 453 PHE C O   
11858 C CB  . PHE C  453 ? 0.3569 0.5197 0.3666 0.0490  0.0924  -0.0782 453 PHE C CB  
11859 C CG  . PHE C  453 ? 0.3883 0.5549 0.3961 0.0635  0.0864  -0.0830 453 PHE C CG  
11860 C CD1 . PHE C  453 ? 0.3954 0.5454 0.3909 0.0685  0.0815  -0.0835 453 PHE C CD1 
11861 C CD2 . PHE C  453 ? 0.3915 0.5768 0.4091 0.0732  0.0853  -0.0864 453 PHE C CD2 
11862 C CE1 . PHE C  453 ? 0.3994 0.5457 0.3910 0.0822  0.0743  -0.0853 453 PHE C CE1 
11863 C CE2 . PHE C  453 ? 0.3822 0.5687 0.3973 0.0887  0.0790  -0.0900 453 PHE C CE2 
11864 C CZ  . PHE C  453 ? 0.3898 0.5566 0.3912 0.0942  0.0737  -0.0898 453 PHE C CZ  
11865 N N   . ILE C  454 ? 0.2129 0.3439 0.2109 0.0275  0.1014  -0.0652 454 ILE C N   
11866 C CA  . ILE C  454 ? 0.2100 0.3382 0.2092 0.0191  0.1053  -0.0596 454 ILE C CA  
11867 C C   . ILE C  454 ? 0.2159 0.3329 0.2061 0.0230  0.1078  -0.0568 454 ILE C C   
11868 O O   . ILE C  454 ? 0.2183 0.3395 0.2108 0.0210  0.1120  -0.0538 454 ILE C O   
11869 C CB  . ILE C  454 ? 0.3755 0.4926 0.3713 0.0106  0.1034  -0.0561 454 ILE C CB  
11870 C CG1 . ILE C  454 ? 0.1991 0.3259 0.2013 0.0069  0.1009  -0.0597 454 ILE C CG1 
11871 C CG2 . ILE C  454 ? 0.2013 0.3160 0.1988 0.0029  0.1064  -0.0507 454 ILE C CG2 
11872 C CD1 . ILE C  454 ? 0.1979 0.3433 0.2127 0.0014  0.1030  -0.0613 454 ILE C CD1 
11873 N N   . PHE C  455 ? 0.3838 0.4866 0.3632 0.0287  0.1053  -0.0580 455 PHE C N   
11874 C CA  . PHE C  455 ? 0.3946 0.4865 0.3643 0.0322  0.1071  -0.0561 455 PHE C CA  
11875 C C   . PHE C  455 ? 0.4138 0.5109 0.3839 0.0396  0.1101  -0.0604 455 PHE C C   
11876 O O   . PHE C  455 ? 0.4688 0.5577 0.4307 0.0421  0.1124  -0.0597 455 PHE C O   
11877 C CB  . PHE C  455 ? 0.3393 0.4138 0.2970 0.0339  0.1029  -0.0563 455 PHE C CB  
11878 C CG  . PHE C  455 ? 0.3119 0.3805 0.2673 0.0267  0.1010  -0.0509 455 PHE C CG  
11879 C CD1 . PHE C  455 ? 0.3002 0.3652 0.2501 0.0264  0.1015  -0.0476 455 PHE C CD1 
11880 C CD2 . PHE C  455 ? 0.3051 0.3721 0.2642 0.0201  0.0986  -0.0496 455 PHE C CD2 
11881 C CE1 . PHE C  455 ? 0.2900 0.3503 0.2397 0.0194  0.0996  -0.0435 455 PHE C CE1 
11882 C CE2 . PHE C  455 ? 0.3043 0.3645 0.2624 0.0131  0.0972  -0.0451 455 PHE C CE2 
11883 C CZ  . PHE C  455 ? 0.2797 0.3367 0.2337 0.0129  0.0976  -0.0422 455 PHE C CZ  
11884 N N   . GLY C  456 ? 0.2950 0.4072 0.2749 0.0434  0.1094  -0.0651 456 GLY C N   
11885 C CA  . GLY C  456 ? 0.2857 0.4082 0.2694 0.0505  0.1119  -0.0692 456 GLY C CA  
11886 C C   . GLY C  456 ? 0.3071 0.4197 0.2822 0.0603  0.1089  -0.0745 456 GLY C C   
11887 O O   . GLY C  456 ? 0.3464 0.4607 0.3198 0.0650  0.1119  -0.0768 456 GLY C O   
11888 N N   . LEU C  457 ? 0.2595 0.3613 0.2286 0.0634  0.1030  -0.0767 457 LEU C N   
11889 C CA  . LEU C  457 ? 0.2690 0.3593 0.2292 0.0733  0.0989  -0.0817 457 LEU C CA  
11890 C C   . LEU C  457 ? 0.3172 0.4200 0.2836 0.0852  0.0971  -0.0866 457 LEU C C   
11891 O O   . LEU C  457 ? 0.2912 0.3860 0.2508 0.0927  0.0964  -0.0901 457 LEU C O   
11892 C CB  . LEU C  457 ? 0.2689 0.3426 0.2199 0.0742  0.0928  -0.0823 457 LEU C CB  
11893 C CG  . LEU C  457 ? 0.2705 0.3242 0.2090 0.0685  0.0928  -0.0809 457 LEU C CG  
11894 C CD1 . LEU C  457 ? 0.2591 0.3137 0.1994 0.0569  0.0975  -0.0746 457 LEU C CD1 
11895 C CD2 . LEU C  457 ? 0.2739 0.3120 0.2036 0.0713  0.0864  -0.0822 457 LEU C CD2 
11896 N N   . PRO C  458 ? 0.4756 0.5981 0.4547 0.0874  0.0960  -0.0870 458 PRO C N   
11897 C CA  . PRO C  458 ? 0.4620 0.5997 0.4489 0.0993  0.0946  -0.0913 458 PRO C CA  
11898 C C   . PRO C  458 ? 0.4442 0.5884 0.4331 0.1011  0.1006  -0.0927 458 PRO C C   
11899 O O   . PRO C  458 ? 0.4741 0.6240 0.4650 0.1127  0.0992  -0.0968 458 PRO C O   
11900 C CB  . PRO C  458 ? 0.3848 0.5465 0.3870 0.0965  0.0941  -0.0906 458 PRO C CB  
11901 C CG  . PRO C  458 ? 0.3972 0.5495 0.3950 0.0895  0.0911  -0.0880 458 PRO C CG  
11902 C CD  . PRO C  458 ? 0.4070 0.5374 0.3926 0.0808  0.0942  -0.0846 458 PRO C CD  
11903 N N   . LEU C  459 ? 0.2861 0.4286 0.2737 0.0907  0.1071  -0.0891 459 LEU C N   
11904 C CA  . LEU C  459 ? 0.2996 0.4465 0.2869 0.0917  0.1134  -0.0900 459 LEU C CA  
11905 C C   . LEU C  459 ? 0.3699 0.4996 0.3437 0.0993  0.1119  -0.0941 459 LEU C C   
11906 O O   . LEU C  459 ? 0.3933 0.5281 0.3669 0.1047  0.1156  -0.0971 459 LEU C O   
11907 C CB  . LEU C  459 ? 0.2890 0.4344 0.2753 0.0794  0.1201  -0.0843 459 LEU C CB  
11908 C CG  . LEU C  459 ? 0.2825 0.4487 0.2830 0.0731  0.1250  -0.0812 459 LEU C CG  
11909 C CD1 . LEU C  459 ? 0.2732 0.4538 0.2856 0.0732  0.1201  -0.0821 459 LEU C CD1 
11910 C CD2 . LEU C  459 ? 0.4692 0.6267 0.4653 0.0616  0.1294  -0.0743 459 LEU C CD2 
11911 N N   . ASP C  460 ? 0.5744 0.6836 0.5366 0.0994  0.1065  -0.0945 460 ASP C N   
11912 C CA  . ASP C  460 ? 0.5951 0.6873 0.5446 0.1072  0.1035  -0.0990 460 ASP C CA  
11913 C C   . ASP C  460 ? 0.6677 0.7639 0.6205 0.1215  0.0988  -0.1036 460 ASP C C   
11914 O O   . ASP C  460 ? 0.7403 0.8365 0.6961 0.1255  0.0933  -0.1032 460 ASP C O   
11915 C CB  . ASP C  460 ? 0.4360 0.5061 0.3736 0.1028  0.0984  -0.0980 460 ASP C CB  
11916 C CG  . ASP C  460 ? 0.4621 0.5128 0.3856 0.1084  0.0952  -0.1025 460 ASP C CG  
11917 O OD1 . ASP C  460 ? 0.4841 0.5346 0.4064 0.1195  0.0939  -0.1071 460 ASP C OD1 
11918 O OD2 . ASP C  460 ? 0.4664 0.5021 0.3799 0.1016  0.0938  -0.1015 460 ASP C OD2 
11919 N N   . PRO C  461 ? 0.4641 0.5627 0.4154 0.1299  0.1010  -0.1079 461 PRO C N   
11920 C CA  . PRO C  461 ? 0.4648 0.5660 0.4186 0.1448  0.0969  -0.1122 461 PRO C CA  
11921 C C   . PRO C  461 ? 0.4977 0.5731 0.4382 0.1517  0.0888  -0.1142 461 PRO C C   
11922 O O   . PRO C  461 ? 0.5315 0.6061 0.4741 0.1616  0.0830  -0.1150 461 PRO C O   
11923 C CB  . PRO C  461 ? 0.6942 0.8002 0.6465 0.1500  0.1023  -0.1163 461 PRO C CB  
11924 C CG  . PRO C  461 ? 0.7226 0.8362 0.6764 0.1375  0.1102  -0.1132 461 PRO C CG  
11925 C CD  . PRO C  461 ? 0.6901 0.7895 0.6371 0.1262  0.1079  -0.1089 461 PRO C CD  
11926 N N   . SER C  462 ? 0.6199 0.6739 0.5464 0.1460  0.0880  -0.1146 462 SER C N   
11927 C CA  . SER C  462 ? 0.6465 0.6733 0.5591 0.1513  0.0807  -0.1166 462 SER C CA  
11928 C C   . SER C  462 ? 0.6077 0.6271 0.5199 0.1487  0.0752  -0.1128 462 SER C C   
11929 O O   . SER C  462 ? 0.6387 0.6344 0.5393 0.1518  0.0691  -0.1133 462 SER C O   
11930 C CB  . SER C  462 ? 0.7585 0.7667 0.6572 0.1446  0.0812  -0.1183 462 SER C CB  
11931 O OG  . SER C  462 ? 0.7859 0.7963 0.6851 0.1309  0.0835  -0.1139 462 SER C OG  
11932 N N   . LEU C  463 ? 0.5102 0.5486 0.4342 0.1422  0.0777  -0.1088 463 LEU C N   
11933 C CA  . LEU C  463 ? 0.4958 0.5284 0.4190 0.1397  0.0730  -0.1054 463 LEU C CA  
11934 C C   . LEU C  463 ? 0.5629 0.6035 0.4924 0.1515  0.0680  -0.1057 463 LEU C C   
11935 O O   . LEU C  463 ? 0.6073 0.6439 0.5357 0.1504  0.0641  -0.1030 463 LEU C O   
11936 C CB  . LEU C  463 ? 0.4854 0.5298 0.4153 0.1253  0.0775  -0.1010 463 LEU C CB  
11937 C CG  . LEU C  463 ? 0.5005 0.5270 0.4192 0.1150  0.0783  -0.0996 463 LEU C CG  
11938 C CD1 . LEU C  463 ? 0.5115 0.5462 0.4356 0.1016  0.0818  -0.0946 463 LEU C CD1 
11939 C CD2 . LEU C  463 ? 0.4926 0.4912 0.3965 0.1191  0.0712  -0.1008 463 LEU C CD2 
11940 N N   . ASN C  464 ? 0.4699 0.5219 0.4056 0.1630  0.0682  -0.1089 464 ASN C N   
11941 C CA  . ASN C  464 ? 0.4913 0.5495 0.4318 0.1767  0.0625  -0.1095 464 ASN C CA  
11942 C C   . ASN C  464 ? 0.4113 0.4930 0.3652 0.1742  0.0616  -0.1067 464 ASN C C   
11943 O O   . ASN C  464 ? 0.3714 0.4514 0.3248 0.1836  0.0550  -0.1060 464 ASN C O   
11944 C CB  . ASN C  464 ? 0.8845 0.9105 0.8085 0.1854  0.0546  -0.1096 464 ASN C CB  
11945 C CG  . ASN C  464 ? 1.0340 1.0368 0.9450 0.1887  0.0547  -0.1132 464 ASN C CG  
11946 O OD1 . ASN C  464 ? 1.0947 1.1084 1.0101 0.1908  0.0595  -0.1167 464 ASN C OD1 
11947 N ND2 . ASN C  464 ? 1.0659 1.0363 0.9605 0.1886  0.0495  -0.1126 464 ASN C ND2 
11948 N N   . TYR C  465 ? 0.4096 0.5119 0.3746 0.1615  0.0679  -0.1050 465 TYR C N   
11949 C CA  . TYR C  465 ? 0.3946 0.5228 0.3744 0.1574  0.0680  -0.1032 465 TYR C CA  
11950 C C   . TYR C  465 ? 0.4442 0.6009 0.4399 0.1658  0.0688  -0.1057 465 TYR C C   
11951 O O   . TYR C  465 ? 0.4367 0.5974 0.4344 0.1691  0.0730  -0.1081 465 TYR C O   
11952 C CB  . TYR C  465 ? 0.4285 0.5654 0.4135 0.1396  0.0749  -0.1002 465 TYR C CB  
11953 C CG  . TYR C  465 ? 0.4258 0.5430 0.3998 0.1295  0.0741  -0.0970 465 TYR C CG  
11954 C CD1 . TYR C  465 ? 0.4233 0.5440 0.3988 0.1265  0.0707  -0.0952 465 TYR C CD1 
11955 C CD2 . TYR C  465 ? 0.4405 0.5373 0.4029 0.1225  0.0769  -0.0960 465 TYR C CD2 
11956 C CE1 . TYR C  465 ? 0.4142 0.5175 0.3797 0.1171  0.0706  -0.0923 465 TYR C CE1 
11957 C CE2 . TYR C  465 ? 0.4418 0.5223 0.3952 0.1133  0.0762  -0.0931 465 TYR C CE2 
11958 C CZ  . TYR C  465 ? 0.4442 0.5276 0.3991 0.1106  0.0733  -0.0911 465 TYR C CZ  
11959 O OH  . TYR C  465 ? 0.4675 0.5349 0.4132 0.1015  0.0731  -0.0882 465 TYR C OH  
11960 N N   . THR C  466 ? 0.5187 0.6962 0.5260 0.1690  0.0649  -0.1054 466 THR C N   
11961 C CA  . THR C  466 ? 0.5540 0.7625 0.5788 0.1753  0.0653  -0.1077 466 THR C CA  
11962 C C   . THR C  466 ? 0.5447 0.7728 0.5813 0.1618  0.0744  -0.1072 466 THR C C   
11963 O O   . THR C  466 ? 0.5018 0.7258 0.5367 0.1470  0.0787  -0.1044 466 THR C O   
11964 C CB  . THR C  466 ? 0.7450 0.9737 0.7803 0.1794  0.0586  -0.1073 466 THR C CB  
11965 O OG1 . THR C  466 ? 0.7389 0.9862 0.7849 0.1634  0.0625  -0.1057 466 THR C OG1 
11966 C CG2 . THR C  466 ? 0.7924 0.9973 0.8132 0.1873  0.0506  -0.1057 466 THR C CG2 
11967 N N   . THR C  467 ? 0.7226 0.9714 0.7709 0.1673  0.0773  -0.1097 467 THR C N   
11968 C CA  . THR C  467 ? 0.7627 1.0271 0.8203 0.1558  0.0864  -0.1091 467 THR C CA  
11969 C C   . THR C  467 ? 0.8044 1.0902 0.8756 0.1418  0.0883  -0.1068 467 THR C C   
11970 O O   . THR C  467 ? 0.8355 1.1230 0.9087 0.1282  0.0957  -0.1044 467 THR C O   
11971 C CB  . THR C  467 ? 0.6397 0.9212 0.7063 0.1659  0.0892  -0.1126 467 THR C CB  
11972 O OG1 . THR C  467 ? 0.6775 0.9792 0.7557 0.1773  0.0822  -0.1147 467 THR C OG1 
11973 C CG2 . THR C  467 ? 0.6133 0.8710 0.6650 0.1764  0.0894  -0.1150 467 THR C CG2 
11974 N N   . GLU C  468 ? 0.7726 1.0735 0.8522 0.1450  0.0814  -0.1075 468 GLU C N   
11975 C CA  . GLU C  468 ? 0.7609 1.0801 0.8520 0.1308  0.0823  -0.1060 468 GLU C CA  
11976 C C   . GLU C  468 ? 0.6829 0.9798 0.7619 0.1191  0.0830  -0.1025 468 GLU C C   
11977 O O   . GLU C  468 ? 0.6732 0.9759 0.7572 0.1039  0.0868  -0.1003 468 GLU C O   
11978 C CB  . GLU C  468 ? 0.9192 1.2637 1.0234 0.1375  0.0744  -0.1084 468 GLU C CB  
11979 C CG  . GLU C  468 ? 1.0037 1.3540 1.1095 0.1576  0.0682  -0.1112 468 GLU C CG  
11980 C CD  . GLU C  468 ? 1.0728 1.3978 1.1626 0.1702  0.0603  -0.1106 468 GLU C CD  
11981 O OE1 . GLU C  468 ? 1.0845 1.4067 1.1713 0.1673  0.0552  -0.1092 468 GLU C OE1 
11982 O OE2 . GLU C  468 ? 1.0970 1.4037 1.1764 0.1827  0.0594  -0.1115 468 GLU C OE2 
11983 N N   . GLU C  469 ? 0.5947 0.8649 0.6572 0.1261  0.0792  -0.1020 469 GLU C N   
11984 C CA  . GLU C  469 ? 0.5491 0.7958 0.5988 0.1155  0.0806  -0.0987 469 GLU C CA  
11985 C C   . GLU C  469 ? 0.5799 0.8159 0.6252 0.1051  0.0891  -0.0960 469 GLU C C   
11986 O O   . GLU C  469 ? 0.5979 0.8240 0.6391 0.0918  0.0925  -0.0924 469 GLU C O   
11987 C CB  . GLU C  469 ? 0.4797 0.6996 0.5125 0.1259  0.0748  -0.0989 469 GLU C CB  
11988 C CG  . GLU C  469 ? 0.4823 0.7056 0.5146 0.1333  0.0666  -0.0997 469 GLU C CG  
11989 C CD  . GLU C  469 ? 0.4901 0.6823 0.5033 0.1429  0.0613  -0.0991 469 GLU C CD  
11990 O OE1 . GLU C  469 ? 0.4803 0.6547 0.4844 0.1505  0.0615  -0.1000 469 GLU C OE1 
11991 O OE2 . GLU C  469 ? 0.5024 0.6833 0.5087 0.1398  0.0559  -0.0960 469 GLU C OE2 
11992 N N   . ARG C  470 ? 0.4711 0.7087 0.5168 0.1117  0.0925  -0.0978 470 ARG C N   
11993 C CA  . ARG C  470 ? 0.4172 0.6463 0.4584 0.1036  0.1006  -0.0954 470 ARG C CA  
11994 C C   . ARG C  470 ? 0.3778 0.6256 0.4316 0.0908  0.1065  -0.0928 470 ARG C C   
11995 O O   . ARG C  470 ? 0.3770 0.6141 0.4262 0.0787  0.1105  -0.0884 470 ARG C O   
11996 C CB  . ARG C  470 ? 0.5344 0.7617 0.5724 0.1144  0.1029  -0.0986 470 ARG C CB  
11997 C CG  . ARG C  470 ? 0.6122 0.8239 0.6398 0.1086  0.1098  -0.0968 470 ARG C CG  
11998 C CD  . ARG C  470 ? 0.7026 0.9328 0.7401 0.1054  0.1178  -0.0966 470 ARG C CD  
11999 N NE  . ARG C  470 ? 0.7694 1.0140 0.8135 0.1185  0.1175  -0.1015 470 ARG C NE  
12000 C CZ  . ARG C  470 ? 0.7724 1.0415 0.8305 0.1186  0.1225  -0.1025 470 ARG C CZ  
12001 N NH1 . ARG C  470 ? 0.7463 1.0273 0.8129 0.1059  0.1281  -0.0988 470 ARG C NH1 
12002 N NH2 . ARG C  470 ? 0.7839 1.0649 0.8473 0.1316  0.1219  -0.1072 470 ARG C NH2 
12003 N N   . ILE C  471 ? 0.6442 0.9194 0.7141 0.0935  0.1065  -0.0953 471 ILE C N   
12004 C CA  . ILE C  471 ? 0.6731 0.9650 0.7548 0.0806  0.1119  -0.0931 471 ILE C CA  
12005 C C   . ILE C  471 ? 0.6552 0.9439 0.7373 0.0685  0.1095  -0.0905 471 ILE C C   
12006 O O   . ILE C  471 ? 0.6950 0.9837 0.7795 0.0554  0.1145  -0.0869 471 ILE C O   
12007 C CB  . ILE C  471 ? 0.3820 0.7058 0.4819 0.0849  0.1127  -0.0966 471 ILE C CB  
12008 C CG1 . ILE C  471 ? 0.3763 0.7216 0.4893 0.0832  0.1062  -0.0988 471 ILE C CG1 
12009 C CG2 . ILE C  471 ? 0.2808 0.6066 0.3793 0.1012  0.1117  -0.1005 471 ILE C CG2 
12010 C CD1 . ILE C  471 ? 0.3863 0.7448 0.5097 0.0665  0.1099  -0.0969 471 ILE C CD1 
12011 N N   . PHE C  472 ? 0.4115 0.6961 0.4902 0.0733  0.1020  -0.0922 472 PHE C N   
12012 C CA  . PHE C  472 ? 0.3481 0.6276 0.4252 0.0627  0.0997  -0.0903 472 PHE C CA  
12013 C C   . PHE C  472 ? 0.3365 0.5886 0.3997 0.0534  0.1040  -0.0850 472 PHE C C   
12014 O O   . PHE C  472 ? 0.3054 0.5555 0.3703 0.0404  0.1071  -0.0816 472 PHE C O   
12015 C CB  . PHE C  472 ? 0.2426 0.5213 0.3164 0.0716  0.0911  -0.0930 472 PHE C CB  
12016 C CG  . PHE C  472 ? 0.2329 0.5080 0.3049 0.0611  0.0889  -0.0919 472 PHE C CG  
12017 C CD1 . PHE C  472 ? 0.2607 0.5486 0.3425 0.0470  0.0916  -0.0912 472 PHE C CD1 
12018 C CD2 . PHE C  472 ? 0.2224 0.4808 0.2822 0.0656  0.0841  -0.0918 472 PHE C CD2 
12019 C CE1 . PHE C  472 ? 0.2091 0.4927 0.2885 0.0373  0.0898  -0.0906 472 PHE C CE1 
12020 C CE2 . PHE C  472 ? 0.2322 0.4877 0.2898 0.0560  0.0827  -0.0910 472 PHE C CE2 
12021 C CZ  . PHE C  472 ? 0.2588 0.5270 0.3263 0.0418  0.0856  -0.0906 472 PHE C CZ  
12022 N N   . ALA C  473 ? 0.3254 0.5564 0.3749 0.0606  0.1037  -0.0844 473 ALA C N   
12023 C CA  . ALA C  473 ? 0.2859 0.4921 0.3221 0.0540  0.1072  -0.0795 473 ALA C CA  
12024 C C   . ALA C  473 ? 0.3073 0.5169 0.3472 0.0449  0.1145  -0.0755 473 ALA C C   
12025 O O   . ALA C  473 ? 0.2738 0.4736 0.3104 0.0346  0.1166  -0.0706 473 ALA C O   
12026 C CB  . ALA C  473 ? 0.2452 0.4334 0.2684 0.0638  0.1063  -0.0809 473 ALA C CB  
12027 N N   . GLN C  474 ? 0.4763 0.6999 0.5230 0.0493  0.1184  -0.0773 474 GLN C N   
12028 C CA  . GLN C  474 ? 0.5393 0.7679 0.5898 0.0416  0.1258  -0.0736 474 GLN C CA  
12029 C C   . GLN C  474 ? 0.5368 0.7748 0.5965 0.0292  0.1264  -0.0713 474 GLN C C   
12030 O O   . GLN C  474 ? 0.5711 0.7980 0.6260 0.0205  0.1301  -0.0658 474 GLN C O   
12031 C CB  . GLN C  474 ? 0.5593 0.8067 0.6187 0.0482  0.1296  -0.0769 474 GLN C CB  
12032 C CG  . GLN C  474 ? 0.5844 0.8237 0.6355 0.0608  0.1286  -0.0804 474 GLN C CG  
12033 C CD  . GLN C  474 ? 0.6168 0.8686 0.6727 0.0650  0.1350  -0.0821 474 GLN C CD  
12034 O OE1 . GLN C  474 ? 0.6430 0.9109 0.7071 0.0747  0.1334  -0.0871 474 GLN C OE1 
12035 N NE2 . GLN C  474 ? 0.6156 0.8606 0.6664 0.0584  0.1425  -0.0776 474 GLN C NE2 
12036 N N   . ARG C  475 ? 0.3537 0.6122 0.4263 0.0288  0.1224  -0.0756 475 ARG C N   
12037 C CA  . ARG C  475 ? 0.3123 0.5813 0.3943 0.0164  0.1228  -0.0748 475 ARG C CA  
12038 C C   . ARG C  475 ? 0.3364 0.5847 0.4087 0.0081  0.1210  -0.0711 475 ARG C C   
12039 O O   . ARG C  475 ? 0.3036 0.5482 0.3770 -0.0029 0.1239  -0.0678 475 ARG C O   
12040 C CB  . ARG C  475 ? 0.3119 0.6076 0.4088 0.0180  0.1178  -0.0809 475 ARG C CB  
12041 C CG  . ARG C  475 ? 0.3510 0.6600 0.4587 0.0042  0.1191  -0.0811 475 ARG C CG  
12042 C CD  . ARG C  475 ? 0.3857 0.7260 0.5102 0.0055  0.1146  -0.0874 475 ARG C CD  
12043 N NE  . ARG C  475 ? 0.4230 0.7659 0.5475 0.0047  0.1072  -0.0906 475 ARG C NE  
12044 C CZ  . ARG C  475 ? 0.4306 0.7795 0.5545 0.0171  0.1005  -0.0939 475 ARG C CZ  
12045 N NH1 . ARG C  475 ? 0.4738 0.8254 0.5970 0.0314  0.1000  -0.0949 475 ARG C NH1 
12046 N NH2 . ARG C  475 ? 0.3571 0.7090 0.4805 0.0157  0.0943  -0.0964 475 ARG C NH2 
12047 N N   . LEU C  476 ? 0.4268 0.6611 0.4895 0.0138  0.1161  -0.0718 476 LEU C N   
12048 C CA  . LEU C  476 ? 0.4071 0.6212 0.4600 0.0072  0.1143  -0.0683 476 LEU C CA  
12049 C C   . LEU C  476 ? 0.4236 0.6181 0.4665 0.0033  0.1186  -0.0616 476 LEU C C   
12050 O O   . LEU C  476 ? 0.4575 0.6445 0.4993 -0.0061 0.1195  -0.0582 476 LEU C O   
12051 C CB  . LEU C  476 ? 0.2929 0.4960 0.3370 0.0147  0.1087  -0.0703 476 LEU C CB  
12052 C CG  . LEU C  476 ? 0.2461 0.4644 0.2968 0.0177  0.1029  -0.0758 476 LEU C CG  
12053 C CD1 . LEU C  476 ? 0.2057 0.4068 0.2442 0.0226  0.0985  -0.0760 476 LEU C CD1 
12054 C CD2 . LEU C  476 ? 0.2091 0.4399 0.2692 0.0060  0.1028  -0.0769 476 LEU C CD2 
12055 N N   . MET C  477 ? 0.3331 0.5195 0.3683 0.0110  0.1210  -0.0601 477 MET C N   
12056 C CA  . MET C  477 ? 0.3349 0.5057 0.3605 0.0085  0.1246  -0.0537 477 MET C CA  
12057 C C   . MET C  477 ? 0.3366 0.5163 0.3695 0.0003  0.1297  -0.0507 477 MET C C   
12058 O O   . MET C  477 ? 0.3100 0.4785 0.3374 -0.0053 0.1311  -0.0454 477 MET C O   
12059 C CB  . MET C  477 ? 0.2318 0.3956 0.2487 0.0176  0.1270  -0.0535 477 MET C CB  
12060 C CG  . MET C  477 ? 0.2320 0.3857 0.2410 0.0257  0.1224  -0.0570 477 MET C CG  
12061 S SD  . MET C  477 ? 0.2863 0.4403 0.2906 0.0366  0.1253  -0.0610 477 MET C SD  
12062 C CE  . MET C  477 ? 0.2510 0.3915 0.2438 0.0344  0.1308  -0.0546 477 MET C CE  
12063 N N   . LYS C  478 ? 0.3378 0.5385 0.3832 -0.0001 0.1322  -0.0544 478 LYS C N   
12064 C CA  . LYS C  478 ? 0.3515 0.5627 0.4053 -0.0089 0.1373  -0.0524 478 LYS C CA  
12065 C C   . LYS C  478 ? 0.2988 0.5055 0.3547 -0.0202 0.1351  -0.0515 478 LYS C C   
12066 O O   . LYS C  478 ? 0.2683 0.4659 0.3206 -0.0268 0.1382  -0.0466 478 LYS C O   
12067 C CB  . LYS C  478 ? 0.6547 0.8917 0.7231 -0.0075 0.1395  -0.0574 478 LYS C CB  
12068 C CG  . LYS C  478 ? 0.7511 0.9934 0.8193 -0.0030 0.1465  -0.0556 478 LYS C CG  
12069 C CD  . LYS C  478 ? 0.8046 1.0484 0.8751 -0.0125 0.1530  -0.0507 478 LYS C CD  
12070 C CE  . LYS C  478 ? 0.8406 1.0891 0.9095 -0.0079 0.1607  -0.0484 478 LYS C CE  
12071 N NZ  . LYS C  478 ? 0.8471 1.1200 0.9294 -0.0036 0.1629  -0.0541 478 LYS C NZ  
12072 N N   . TYR C  479 ? 0.3408 0.5535 0.4018 -0.0218 0.1299  -0.0563 479 TYR C N   
12073 C CA  . TYR C  479 ? 0.2957 0.5020 0.3570 -0.0321 0.1276  -0.0564 479 TYR C CA  
12074 C C   . TYR C  479 ? 0.2677 0.4489 0.3159 -0.0337 0.1272  -0.0506 479 TYR C C   
12075 O O   . TYR C  479 ? 0.2611 0.4347 0.3082 -0.0419 0.1295  -0.0477 479 TYR C O   
12076 C CB  . TYR C  479 ? 0.2436 0.4571 0.3085 -0.0313 0.1216  -0.0622 479 TYR C CB  
12077 C CG  . TYR C  479 ? 0.2502 0.4917 0.3298 -0.0312 0.1202  -0.0688 479 TYR C CG  
12078 C CD1 . TYR C  479 ? 0.2563 0.5135 0.3472 -0.0398 0.1236  -0.0702 479 TYR C CD1 
12079 C CD2 . TYR C  479 ? 0.2651 0.5182 0.3475 -0.0221 0.1151  -0.0735 479 TYR C CD2 
12080 C CE1 . TYR C  479 ? 0.3004 0.5860 0.4060 -0.0395 0.1216  -0.0764 479 TYR C CE1 
12081 C CE2 . TYR C  479 ? 0.2909 0.5722 0.3876 -0.0205 0.1128  -0.0795 479 TYR C CE2 
12082 C CZ  . TYR C  479 ? 0.3177 0.6160 0.4265 -0.0294 0.1159  -0.0810 479 TYR C CZ  
12083 O OH  . TYR C  479 ? 0.3062 0.6347 0.4303 -0.0278 0.1129  -0.0869 479 TYR C OH  
12084 N N   . TRP C  480 ? 0.2136 0.3823 0.2520 -0.0256 0.1242  -0.0491 480 TRP C N   
12085 C CA  . TRP C  480 ? 0.2761 0.4236 0.3033 -0.0264 0.1226  -0.0443 480 TRP C CA  
12086 C C   . TRP C  480 ? 0.2998 0.4401 0.3222 -0.0279 0.1267  -0.0383 480 TRP C C   
12087 O O   . TRP C  480 ? 0.3004 0.4291 0.3192 -0.0337 0.1266  -0.0352 480 TRP C O   
12088 C CB  . TRP C  480 ? 0.2076 0.3454 0.2259 -0.0176 0.1187  -0.0443 480 TRP C CB  
12089 C CG  . TRP C  480 ? 0.2013 0.3321 0.2174 -0.0193 0.1138  -0.0465 480 TRP C CG  
12090 C CD1 . TRP C  480 ? 0.1978 0.3119 0.2050 -0.0189 0.1108  -0.0437 480 TRP C CD1 
12091 C CD2 . TRP C  480 ? 0.1985 0.3405 0.2216 -0.0217 0.1115  -0.0520 480 TRP C CD2 
12092 N NE1 . TRP C  480 ? 0.1937 0.3062 0.2012 -0.0209 0.1073  -0.0468 480 TRP C NE1 
12093 C CE2 . TRP C  480 ? 0.1942 0.3237 0.2108 -0.0226 0.1077  -0.0519 480 TRP C CE2 
12094 C CE3 . TRP C  480 ? 0.1996 0.3627 0.2343 -0.0232 0.1121  -0.0572 480 TRP C CE3 
12095 C CZ2 . TRP C  480 ? 0.1916 0.3281 0.2115 -0.0248 0.1048  -0.0566 480 TRP C CZ2 
12096 C CZ3 . TRP C  480 ? 0.1962 0.3680 0.2349 -0.0252 0.1084  -0.0622 480 TRP C CZ3 
12097 C CH2 . TRP C  480 ? 0.1926 0.3507 0.2233 -0.0260 0.1050  -0.0618 480 TRP C CH2 
12098 N N   . THR C  481 ? 0.3459 0.4931 0.3679 -0.0223 0.1305  -0.0370 481 THR C N   
12099 C CA  . THR C  481 ? 0.3444 0.4857 0.3604 -0.0227 0.1345  -0.0312 481 THR C CA  
12100 C C   . THR C  481 ? 0.3612 0.5095 0.3847 -0.0321 0.1393  -0.0301 481 THR C C   
12101 O O   . THR C  481 ? 0.3504 0.4910 0.3693 -0.0358 0.1419  -0.0252 481 THR C O   
12102 C CB  . THR C  481 ? 0.3214 0.4675 0.3333 -0.0138 0.1379  -0.0303 481 THR C CB  
12103 O OG1 . THR C  481 ? 0.3614 0.5251 0.3838 -0.0135 0.1417  -0.0340 481 THR C OG1 
12104 C CG2 . THR C  481 ? 0.3019 0.4397 0.3053 -0.0046 0.1336  -0.0321 481 THR C CG2 
12105 N N   . ASN C  482 ? 0.3425 0.5060 0.3776 -0.0362 0.1404  -0.0349 482 ASN C N   
12106 C CA  . ASN C  482 ? 0.3951 0.5648 0.4379 -0.0469 0.1443  -0.0350 482 ASN C CA  
12107 C C   . ASN C  482 ? 0.4071 0.5619 0.4464 -0.0549 0.1419  -0.0344 482 ASN C C   
12108 O O   . ASN C  482 ? 0.3828 0.5321 0.4216 -0.0623 0.1456  -0.0317 482 ASN C O   
12109 C CB  . ASN C  482 ? 0.5608 0.7522 0.6176 -0.0500 0.1450  -0.0412 482 ASN C CB  
12110 C CG  . ASN C  482 ? 0.6448 0.8522 0.7074 -0.0460 0.1505  -0.0408 482 ASN C CG  
12111 O OD1 . ASN C  482 ? 0.6768 0.8989 0.7459 -0.0399 0.1495  -0.0452 482 ASN C OD1 
12112 N ND2 . ASN C  482 ? 0.6686 0.8733 0.7286 -0.0492 0.1567  -0.0355 482 ASN C ND2 
12113 N N   . PHE C  483 ? 0.5850 0.7327 0.6216 -0.0531 0.1360  -0.0371 483 PHE C N   
12114 C CA  . PHE C  483 ? 0.5572 0.6889 0.5890 -0.0592 0.1338  -0.0367 483 PHE C CA  
12115 C C   . PHE C  483 ? 0.5547 0.6695 0.5762 -0.0570 0.1346  -0.0303 483 PHE C C   
12116 O O   . PHE C  483 ? 0.5708 0.6754 0.5901 -0.0634 0.1368  -0.0284 483 PHE C O   
12117 C CB  . PHE C  483 ? 0.3358 0.4635 0.3659 -0.0569 0.1279  -0.0404 483 PHE C CB  
12118 C CG  . PHE C  483 ? 0.2952 0.4073 0.3208 -0.0629 0.1262  -0.0406 483 PHE C CG  
12119 C CD1 . PHE C  483 ? 0.3392 0.4520 0.3693 -0.0732 0.1286  -0.0437 483 PHE C CD1 
12120 C CD2 . PHE C  483 ? 0.2655 0.3621 0.2825 -0.0586 0.1226  -0.0381 483 PHE C CD2 
12121 C CE1 . PHE C  483 ? 0.3580 0.4553 0.3831 -0.0784 0.1278  -0.0446 483 PHE C CE1 
12122 C CE2 . PHE C  483 ? 0.3180 0.4006 0.3312 -0.0636 0.1217  -0.0385 483 PHE C CE2 
12123 C CZ  . PHE C  483 ? 0.3595 0.4418 0.3763 -0.0732 0.1244  -0.0419 483 PHE C CZ  
12124 N N   . ALA C  484 ? 0.4175 0.5299 0.4327 -0.0478 0.1328  -0.0276 484 ALA C N   
12125 C CA  . ALA C  484 ? 0.4191 0.5188 0.4249 -0.0452 0.1330  -0.0220 484 ALA C CA  
12126 C C   . ALA C  484 ? 0.4521 0.5528 0.4575 -0.0494 0.1392  -0.0178 484 ALA C C   
12127 O O   . ALA C  484 ? 0.4566 0.5450 0.4558 -0.0516 0.1402  -0.0140 484 ALA C O   
12128 C CB  . ALA C  484 ? 0.3480 0.4484 0.3477 -0.0351 0.1305  -0.0209 484 ALA C CB  
12129 N N   . ARG C  485 ? 0.4315 0.5472 0.4436 -0.0506 0.1437  -0.0187 485 ARG C N   
12130 C CA  . ARG C  485 ? 0.4028 0.5219 0.4150 -0.0544 0.1505  -0.0146 485 ARG C CA  
12131 C C   . ARG C  485 ? 0.3151 0.4307 0.3320 -0.0660 0.1538  -0.0153 485 ARG C C   
12132 O O   . ARG C  485 ? 0.3175 0.4210 0.3287 -0.0699 0.1564  -0.0113 485 ARG C O   
12133 C CB  . ARG C  485 ? 0.5570 0.6947 0.5755 -0.0511 0.1545  -0.0157 485 ARG C CB  
12134 C CG  . ARG C  485 ? 0.6191 0.7593 0.6305 -0.0444 0.1582  -0.0109 485 ARG C CG  
12135 C CD  . ARG C  485 ? 0.6810 0.8394 0.6996 -0.0409 0.1628  -0.0129 485 ARG C CD  
12136 N NE  . ARG C  485 ? 0.7187 0.8845 0.7428 -0.0354 0.1589  -0.0191 485 ARG C NE  
12137 C CZ  . ARG C  485 ? 0.7469 0.9137 0.7661 -0.0249 0.1575  -0.0204 485 ARG C CZ  
12138 N NH1 . ARG C  485 ? 0.7733 0.9350 0.7818 -0.0185 0.1596  -0.0164 485 ARG C NH1 
12139 N NH2 . ARG C  485 ? 0.7245 0.8974 0.7491 -0.0207 0.1541  -0.0263 485 ARG C NH2 
12140 N N   . THR C  486 ? 0.2677 0.3944 0.2950 -0.0715 0.1541  -0.0208 486 THR C N   
12141 C CA  . THR C  486 ? 0.2769 0.4021 0.3093 -0.0832 0.1576  -0.0227 486 THR C CA  
12142 C C   . THR C  486 ? 0.2733 0.3868 0.3048 -0.0884 0.1536  -0.0271 486 THR C C   
12143 O O   . THR C  486 ? 0.2930 0.3997 0.3255 -0.0978 0.1566  -0.0283 486 THR C O   
12144 C CB  . THR C  486 ? 0.6567 0.8035 0.7020 -0.0881 0.1609  -0.0267 486 THR C CB  
12145 O OG1 . THR C  486 ? 0.6865 0.8413 0.7390 -0.0899 0.1562  -0.0340 486 THR C OG1 
12146 C CG2 . THR C  486 ? 0.7211 0.8825 0.7684 -0.0796 0.1632  -0.0245 486 THR C CG2 
12147 N N   . GLY C  487 ? 0.2610 0.3711 0.2899 -0.0823 0.1473  -0.0294 487 GLY C N   
12148 C CA  . GLY C  487 ? 0.2577 0.3591 0.2861 -0.0868 0.1438  -0.0341 487 GLY C CA  
12149 C C   . GLY C  487 ? 0.2912 0.4090 0.3298 -0.0917 0.1423  -0.0415 487 GLY C C   
12150 O O   . GLY C  487 ? 0.2836 0.3970 0.3222 -0.0966 0.1398  -0.0464 487 GLY C O   
12151 N N   . ASP C  488 ? 0.3679 0.5056 0.4150 -0.0903 0.1441  -0.0426 488 ASP C N   
12152 C CA  . ASP C  488 ? 0.4103 0.5685 0.4692 -0.0952 0.1432  -0.0496 488 ASP C CA  
12153 C C   . ASP C  488 ? 0.4022 0.5790 0.4669 -0.0859 0.1412  -0.0508 488 ASP C C   
12154 O O   . ASP C  488 ? 0.4540 0.6416 0.5229 -0.0832 0.1453  -0.0484 488 ASP C O   
12155 C CB  . ASP C  488 ? 0.6257 0.7920 0.6922 -0.1062 0.1489  -0.0507 488 ASP C CB  
12156 C CG  . ASP C  488 ? 0.7173 0.9077 0.7973 -0.1119 0.1478  -0.0583 488 ASP C CG  
12157 O OD1 . ASP C  488 ? 0.7568 0.9570 0.8399 -0.1078 0.1423  -0.0630 488 ASP C OD1 
12158 O OD2 . ASP C  488 ? 0.7407 0.9414 0.8287 -0.1207 0.1523  -0.0595 488 ASP C OD2 
12159 N N   . PRO C  489 ? 0.3758 0.5556 0.4402 -0.0806 0.1355  -0.0545 489 PRO C N   
12160 C CA  . PRO C  489 ? 0.3788 0.5712 0.4460 -0.0699 0.1331  -0.0555 489 PRO C CA  
12161 C C   . PRO C  489 ? 0.4375 0.6550 0.5174 -0.0694 0.1360  -0.0583 489 PRO C C   
12162 O O   . PRO C  489 ? 0.4498 0.6763 0.5311 -0.0595 0.1355  -0.0585 489 PRO C O   
12163 C CB  . PRO C  489 ? 0.2750 0.4700 0.3426 -0.0689 0.1269  -0.0609 489 PRO C CB  
12164 C CG  . PRO C  489 ? 0.2850 0.4802 0.3559 -0.0810 0.1268  -0.0650 489 PRO C CG  
12165 C CD  . PRO C  489 ? 0.3058 0.4825 0.3703 -0.0867 0.1315  -0.0598 489 PRO C CD  
12166 N N   . ASN C  490 ? 0.2973 0.5261 0.3863 -0.0799 0.1390  -0.0609 490 ASN C N   
12167 C CA  . ASN C  490 ? 0.3383 0.5931 0.4413 -0.0808 0.1418  -0.0639 490 ASN C CA  
12168 C C   . ASN C  490 ? 0.4901 0.7479 0.5931 -0.0759 0.1482  -0.0587 490 ASN C C   
12169 O O   . ASN C  490 ? 0.4601 0.7017 0.5546 -0.0778 0.1526  -0.0524 490 ASN C O   
12170 C CB  . ASN C  490 ? 0.3840 0.6482 0.4960 -0.0947 0.1436  -0.0677 490 ASN C CB  
12171 C CG  . ASN C  490 ? 0.3470 0.6154 0.4616 -0.0999 0.1375  -0.0745 490 ASN C CG  
12172 O OD1 . ASN C  490 ? 0.3283 0.6180 0.4519 -0.0964 0.1329  -0.0801 490 ASN C OD1 
12173 N ND2 . ASN C  490 ? 0.2530 0.5020 0.3596 -0.1082 0.1375  -0.0744 490 ASN C ND2 
12174 N N   . ASP C  491 ? 1.0971 1.3765 1.2095 -0.0692 0.1487  -0.0614 491 ASP C N   
12175 C CA  . ASP C  491 ? 1.2689 1.5569 1.3847 -0.0668 0.1559  -0.0580 491 ASP C CA  
12176 C C   . ASP C  491 ? 1.3510 1.6470 1.4754 -0.0805 0.1605  -0.0582 491 ASP C C   
12177 O O   . ASP C  491 ? 1.3806 1.6919 1.5160 -0.0878 0.1576  -0.0643 491 ASP C O   
12178 C CB  . ASP C  491 ? 1.1744 1.4857 1.3002 -0.0571 0.1553  -0.0623 491 ASP C CB  
12179 C CG  . ASP C  491 ? 1.1946 1.4962 1.3108 -0.0433 0.1513  -0.0623 491 ASP C CG  
12180 O OD1 . ASP C  491 ? 1.1974 1.4884 1.3045 -0.0362 0.1553  -0.0579 491 ASP C OD1 
12181 O OD2 . ASP C  491 ? 1.1849 1.4896 1.3024 -0.0397 0.1442  -0.0669 491 ASP C OD2 
12182 N N   . PRO C  492 ? 1.4451 1.7311 1.5642 -0.0842 0.1676  -0.0518 492 PRO C N   
12183 C CA  . PRO C  492 ? 1.5170 1.7981 1.6382 -0.0985 0.1704  -0.0512 492 PRO C CA  
12184 C C   . PRO C  492 ? 1.6638 1.9688 1.8019 -0.1092 0.1714  -0.0573 492 PRO C C   
12185 O O   . PRO C  492 ? 1.7051 2.0073 1.8448 -0.1176 0.1674  -0.0619 492 PRO C O   
12186 C CB  . PRO C  492 ? 0.7520 1.0224 0.8657 -0.0990 0.1783  -0.0430 492 PRO C CB  
12187 C CG  . PRO C  492 ? 0.7039 0.9613 0.8048 -0.0856 0.1766  -0.0388 492 PRO C CG  
12188 C CD  . PRO C  492 ? 0.7096 0.9823 0.8169 -0.0761 0.1719  -0.0446 492 PRO C CD  
12189 N N   . ARG C  493 ? 1.5613 1.8895 1.7117 -0.1091 0.1763  -0.0580 493 ARG C N   
12190 C CA  . ARG C  493 ? 1.5793 1.9327 1.7469 -0.1186 0.1753  -0.0649 493 ARG C CA  
12191 C C   . ARG C  493 ? 1.6203 2.0043 1.8030 -0.1120 0.1709  -0.0718 493 ARG C C   
12192 O O   . ARG C  493 ? 1.6417 2.0474 1.8388 -0.1204 0.1692  -0.0776 493 ARG C O   
12193 C CB  . ARG C  493 ? 1.3059 1.6639 1.4799 -0.1319 0.1833  -0.0626 493 ARG C CB  
12194 C CG  . ARG C  493 ? 1.2603 1.6226 1.4415 -0.1467 0.1803  -0.0688 493 ARG C CG  
12195 C CD  . ARG C  493 ? 1.2390 1.6270 1.4375 -0.1572 0.1853  -0.0713 493 ARG C CD  
12196 N NE  . ARG C  493 ? 1.2365 1.6155 1.4315 -0.1624 0.1952  -0.0638 493 ARG C NE  
12197 C CZ  . ARG C  493 ? 1.2280 1.5888 1.4170 -0.1748 0.1991  -0.0612 493 ARG C CZ  
12198 N NH1 . ARG C  493 ? 1.2217 1.5710 1.4073 -0.1832 0.1941  -0.0660 493 ARG C NH1 
12199 N NH2 . ARG C  493 ? 1.2266 1.5804 1.4122 -0.1785 0.2082  -0.0538 493 ARG C NH2 
12200 N N   . ASP C  494 ? 1.6068 1.9932 1.7864 -0.0973 0.1689  -0.0714 494 ASP C N   
12201 C CA  . ASP C  494 ? 1.6153 2.0317 1.8097 -0.0899 0.1652  -0.0776 494 ASP C CA  
12202 C C   . ASP C  494 ? 1.6352 2.0629 1.8365 -0.0939 0.1561  -0.0850 494 ASP C C   
12203 O O   . ASP C  494 ? 1.6446 2.0553 1.8354 -0.0920 0.1502  -0.0856 494 ASP C O   
12204 C CB  . ASP C  494 ? 1.3659 1.7794 1.5539 -0.0729 0.1641  -0.0765 494 ASP C CB  
12205 C CG  . ASP C  494 ? 1.3305 1.7737 1.5330 -0.0638 0.1595  -0.0831 494 ASP C CG  
12206 O OD1 . ASP C  494 ? 1.3102 1.7801 1.5296 -0.0703 0.1589  -0.0877 494 ASP C OD1 
12207 O OD2 . ASP C  494 ? 1.3191 1.7589 1.5160 -0.0498 0.1560  -0.0839 494 ASP C OD2 
12208 N N   . SER C  495 ? 1.6185 2.0755 1.8376 -0.1000 0.1551  -0.0905 495 SER C N   
12209 C CA  . SER C  495 ? 1.5899 2.0595 1.8162 -0.1065 0.1470  -0.0976 495 SER C CA  
12210 C C   . SER C  495 ? 1.5718 2.0675 1.8084 -0.0956 0.1381  -0.1040 495 SER C C   
12211 O O   . SER C  495 ? 1.5785 2.0836 1.8192 -0.1001 0.1306  -0.1096 495 SER C O   
12212 C CB  . SER C  495 ? 1.3446 1.8262 1.5819 -0.1234 0.1502  -0.1000 495 SER C CB  
12213 O OG  . SER C  495 ? 1.3238 1.7785 1.5498 -0.1333 0.1572  -0.0943 495 SER C OG  
12214 N N   . LYS C  496 ? 1.4690 1.9757 1.7090 -0.0809 0.1387  -0.1032 496 LYS C N   
12215 C CA  . LYS C  496 ? 1.3989 1.9288 1.6478 -0.0690 0.1298  -0.1089 496 LYS C CA  
12216 C C   . LYS C  496 ? 1.3603 1.8677 1.5935 -0.0627 0.1234  -0.1083 496 LYS C C   
12217 O O   . LYS C  496 ? 1.3517 1.8623 1.5853 -0.0672 0.1162  -0.1124 496 LYS C O   
12218 C CB  . LYS C  496 ? 1.1812 1.7262 1.4366 -0.0544 0.1327  -0.1082 496 LYS C CB  
12219 C CG  . LYS C  496 ? 1.1227 1.6865 1.3841 -0.0383 0.1236  -0.1129 496 LYS C CG  
12220 C CD  . LYS C  496 ? 1.0654 1.6603 1.3433 -0.0423 0.1155  -0.1195 496 LYS C CD  
12221 C CE  . LYS C  496 ? 1.0170 1.6348 1.3034 -0.0241 0.1077  -0.1233 496 LYS C CE  
12222 N NZ  . LYS C  496 ? 0.9778 1.5735 1.2484 -0.0087 0.1050  -0.1209 496 LYS C NZ  
12223 N N   . SER C  497 ? 1.3023 1.7884 1.5223 -0.0520 0.1260  -0.1037 497 SER C N   
12224 C CA  . SER C  497 ? 1.2541 1.7046 1.4551 -0.0553 0.1281  -0.0985 497 SER C CA  
12225 C C   . SER C  497 ? 1.2083 1.6480 1.4047 -0.0677 0.1243  -0.1003 497 SER C C   
12226 O O   . SER C  497 ? 1.1992 1.6234 1.3907 -0.0801 0.1294  -0.0974 497 SER C O   
12227 C CB  . SER C  497 ? 1.1686 1.6035 1.3637 -0.0597 0.1383  -0.0920 497 SER C CB  
12228 O OG  . SER C  497 ? 1.1637 1.5657 1.3402 -0.0578 0.1400  -0.0863 497 SER C OG  
12229 N N   . PRO C  498 ? 1.0891 1.5375 1.2869 -0.0644 0.1154  -0.1052 498 PRO C N   
12230 C CA  . PRO C  498 ? 1.0033 1.4468 1.1988 -0.0771 0.1118  -0.1084 498 PRO C CA  
12231 C C   . PRO C  498 ? 0.8914 1.2989 1.0699 -0.0844 0.1162  -0.1033 498 PRO C C   
12232 O O   . PRO C  498 ? 0.8419 1.2275 1.0078 -0.0763 0.1183  -0.0980 498 PRO C O   
12233 C CB  . PRO C  498 ? 1.0871 1.5416 1.2830 -0.0681 0.1020  -0.1129 498 PRO C CB  
12234 C CG  . PRO C  498 ? 1.1135 1.5637 1.3046 -0.0507 0.1015  -0.1100 498 PRO C CG  
12235 C CD  . PRO C  498 ? 1.1453 1.6028 1.3432 -0.0481 0.1086  -0.1074 498 PRO C CD  
12236 N N   . GLN C  499 ? 0.8638 1.2652 1.0418 -0.0992 0.1177  -0.1049 499 GLN C N   
12237 C CA  . GLN C  499 ? 0.7961 1.1640 0.9588 -0.1059 0.1221  -0.1001 499 GLN C CA  
12238 C C   . GLN C  499 ? 0.7109 1.0633 0.8624 -0.1052 0.1166  -0.1017 499 GLN C C   
12239 O O   . GLN C  499 ? 0.7079 1.0747 0.8643 -0.1090 0.1107  -0.1081 499 GLN C O   
12240 C CB  . GLN C  499 ? 0.7009 1.0658 0.8668 -0.1217 0.1272  -0.1005 499 GLN C CB  
12241 C CG  . GLN C  499 ? 0.7001 1.0376 0.8551 -0.1245 0.1353  -0.0927 499 GLN C CG  
12242 C CD  . GLN C  499 ? 0.7419 1.0849 0.8999 -0.1163 0.1408  -0.0871 499 GLN C CD  
12243 O OE1 . GLN C  499 ? 0.7561 1.1178 0.9213 -0.1059 0.1387  -0.0884 499 GLN C OE1 
12244 N NE2 . GLN C  499 ? 0.7583 1.0850 0.9103 -0.1208 0.1481  -0.0809 499 GLN C NE2 
12245 N N   . TRP C  500 ? 0.3383 0.6627 0.4751 -0.0999 0.1186  -0.0957 500 TRP C N   
12246 C CA  . TRP C  500 ? 0.2348 0.5385 0.3587 -0.0996 0.1153  -0.0955 500 TRP C CA  
12247 C C   . TRP C  500 ? 0.2371 0.5194 0.3534 -0.1123 0.1189  -0.0948 500 TRP C C   
12248 O O   . TRP C  500 ? 0.2419 0.5046 0.3513 -0.1135 0.1243  -0.0888 500 TRP C O   
12249 C CB  . TRP C  500 ? 0.3839 0.6689 0.4966 -0.0873 0.1159  -0.0891 500 TRP C CB  
12250 C CG  . TRP C  500 ? 0.3668 0.6285 0.4656 -0.0854 0.1134  -0.0873 500 TRP C CG  
12251 C CD1 . TRP C  500 ? 0.3859 0.6382 0.4794 -0.0936 0.1116  -0.0903 500 TRP C CD1 
12252 C CD2 . TRP C  500 ? 0.3367 0.5814 0.4248 -0.0745 0.1128  -0.0821 500 TRP C CD2 
12253 N NE1 . TRP C  500 ? 0.3680 0.5988 0.4487 -0.0883 0.1100  -0.0869 500 TRP C NE1 
12254 C CE2 . TRP C  500 ? 0.3355 0.5614 0.4128 -0.0769 0.1105  -0.0818 500 TRP C CE2 
12255 C CE3 . TRP C  500 ? 0.3108 0.5541 0.3970 -0.0633 0.1140  -0.0781 500 TRP C CE3 
12256 C CZ2 . TRP C  500 ? 0.3075 0.5145 0.3734 -0.0687 0.1092  -0.0773 500 TRP C CZ2 
12257 C CZ3 . TRP C  500 ? 0.3103 0.5342 0.3844 -0.0554 0.1125  -0.0741 500 TRP C CZ3 
12258 C CH2 . TRP C  500 ? 0.3067 0.5130 0.3711 -0.0583 0.1100  -0.0735 500 TRP C CH2 
12259 N N   . PRO C  501 ? 0.2398 0.5267 0.3572 -0.1215 0.1157  -0.1012 501 PRO C N   
12260 C CA  . PRO C  501 ? 0.2495 0.5182 0.3602 -0.1340 0.1186  -0.1026 501 PRO C CA  
12261 C C   . PRO C  501 ? 0.2848 0.5232 0.3792 -0.1316 0.1187  -0.0992 501 PRO C C   
12262 O O   . PRO C  501 ? 0.2575 0.4936 0.3470 -0.1229 0.1148  -0.0983 501 PRO C O   
12263 C CB  . PRO C  501 ? 0.2522 0.5415 0.3703 -0.1423 0.1135  -0.1118 501 PRO C CB  
12264 C CG  . PRO C  501 ? 0.2451 0.5663 0.3759 -0.1336 0.1079  -0.1146 501 PRO C CG  
12265 C CD  . PRO C  501 ? 0.2496 0.5620 0.3751 -0.1194 0.1085  -0.1080 501 PRO C CD  
12266 N N   . PRO C  502 ? 0.4560 0.6714 0.5423 -0.1392 0.1233  -0.0975 502 PRO C N   
12267 C CA  . PRO C  502 ? 0.4780 0.6661 0.5498 -0.1370 0.1232  -0.0950 502 PRO C CA  
12268 C C   . PRO C  502 ? 0.4998 0.6911 0.5686 -0.1415 0.1189  -0.1021 502 PRO C C   
12269 O O   . PRO C  502 ? 0.5254 0.7337 0.6013 -0.1505 0.1174  -0.1094 502 PRO C O   
12270 C CB  . PRO C  502 ? 0.4237 0.5910 0.4899 -0.1443 0.1293  -0.0925 502 PRO C CB  
12271 C CG  . PRO C  502 ? 0.4429 0.6278 0.5198 -0.1553 0.1312  -0.0978 502 PRO C CG  
12272 C CD  . PRO C  502 ? 0.4218 0.6358 0.5119 -0.1501 0.1286  -0.0983 502 PRO C CD  
12273 N N   . TYR C  503 ? 0.3868 0.5630 0.4453 -0.1352 0.1168  -0.0999 503 TYR C N   
12274 C CA  . TYR C  503 ? 0.3538 0.5295 0.4069 -0.1390 0.1136  -0.1056 503 TYR C CA  
12275 C C   . TYR C  503 ? 0.3623 0.5173 0.4070 -0.1489 0.1177  -0.1083 503 TYR C C   
12276 O O   . TYR C  503 ? 0.3650 0.4956 0.4016 -0.1466 0.1216  -0.1030 503 TYR C O   
12277 C CB  . TYR C  503 ? 0.2361 0.4007 0.2804 -0.1286 0.1110  -0.1011 503 TYR C CB  
12278 C CG  . TYR C  503 ? 0.2466 0.4097 0.2838 -0.1320 0.1084  -0.1060 503 TYR C CG  
12279 C CD1 . TYR C  503 ? 0.2648 0.4525 0.3070 -0.1312 0.1034  -0.1109 503 TYR C CD1 
12280 C CD2 . TYR C  503 ? 0.2690 0.4069 0.2941 -0.1354 0.1111  -0.1057 503 TYR C CD2 
12281 C CE1 . TYR C  503 ? 0.2945 0.4818 0.3289 -0.1346 0.1013  -0.1152 503 TYR C CE1 
12282 C CE2 . TYR C  503 ? 0.2964 0.4325 0.3137 -0.1387 0.1094  -0.1102 503 TYR C CE2 
12283 C CZ  . TYR C  503 ? 0.2817 0.4425 0.3031 -0.1388 0.1046  -0.1147 503 TYR C CZ  
12284 O OH  . TYR C  503 ? 0.2433 0.4035 0.2557 -0.1423 0.1034  -0.1189 503 TYR C OH  
12285 N N   . THR C  504 ? 0.4471 0.6130 0.4941 -0.1595 0.1166  -0.1168 504 THR C N   
12286 C CA  . THR C  504 ? 0.5047 0.6520 0.5433 -0.1694 0.1207  -0.1209 504 THR C CA  
12287 C C   . THR C  504 ? 0.5769 0.7247 0.6083 -0.1731 0.1177  -0.1272 504 THR C C   
12288 O O   . THR C  504 ? 0.6005 0.7696 0.6365 -0.1708 0.1119  -0.1298 504 THR C O   
12289 C CB  . THR C  504 ? 0.5308 0.6900 0.5780 -0.1807 0.1226  -0.1259 504 THR C CB  
12290 O OG1 . THR C  504 ? 0.5140 0.7034 0.5712 -0.1850 0.1166  -0.1329 504 THR C OG1 
12291 C CG2 . THR C  504 ? 0.5656 0.7281 0.6209 -0.1776 0.1258  -0.1197 504 THR C CG2 
12292 N N   . THR C  505 ? 0.5902 0.7154 0.6100 -0.1786 0.1218  -0.1298 505 THR C N   
12293 C CA  . THR C  505 ? 0.5674 0.6907 0.5783 -0.1822 0.1198  -0.1356 505 THR C CA  
12294 C C   . THR C  505 ? 0.5430 0.6920 0.5607 -0.1919 0.1147  -0.1446 505 THR C C   
12295 O O   . THR C  505 ? 0.5263 0.6901 0.5435 -0.1916 0.1088  -0.1480 505 THR C O   
12296 C CB  . THR C  505 ? 0.5581 0.6519 0.5552 -0.1860 0.1261  -0.1371 505 THR C CB  
12297 O OG1 . THR C  505 ? 0.5775 0.6617 0.5766 -0.1915 0.1314  -0.1372 505 THR C OG1 
12298 C CG2 . THR C  505 ? 0.5466 0.6184 0.5351 -0.1751 0.1280  -0.1294 505 THR C CG2 
12299 N N   . ALA C  506 ? 0.5045 0.6588 0.5287 -0.2003 0.1163  -0.1481 506 ALA C N   
12300 C CA  . ALA C  506 ? 0.5063 0.6861 0.5389 -0.2093 0.1105  -0.1563 506 ALA C CA  
12301 C C   . ALA C  506 ? 0.4337 0.6476 0.4800 -0.2039 0.1022  -0.1564 506 ALA C C   
12302 O O   . ALA C  506 ? 0.4192 0.6484 0.4648 -0.2034 0.0947  -0.1605 506 ALA C O   
12303 C CB  . ALA C  506 ? 0.7141 0.8930 0.7525 -0.2185 0.1145  -0.1585 506 ALA C CB  
12304 N N   . ALA C  507 ? 0.4215 0.6470 0.4798 -0.1995 0.1032  -0.1519 507 ALA C N   
12305 C CA  . ALA C  507 ? 0.4102 0.6702 0.4838 -0.1942 0.0961  -0.1525 507 ALA C CA  
12306 C C   . ALA C  507 ? 0.3939 0.6604 0.4678 -0.1808 0.0929  -0.1473 507 ALA C C   
12307 O O   . ALA C  507 ? 0.3749 0.6708 0.4590 -0.1760 0.0852  -0.1494 507 ALA C O   
12308 C CB  . ALA C  507 ? 0.4820 0.7532 0.5688 -0.1955 0.0991  -0.1504 507 ALA C CB  
12309 N N   . GLN C  508 ? 0.3484 0.5877 0.4113 -0.1741 0.0984  -0.1402 508 GLN C N   
12310 C CA  . GLN C  508 ? 0.2917 0.5296 0.3509 -0.1616 0.0967  -0.1345 508 GLN C CA  
12311 C C   . GLN C  508 ? 0.2551 0.5166 0.3266 -0.1503 0.0931  -0.1312 508 GLN C C   
12312 O O   . GLN C  508 ? 0.2401 0.5190 0.3139 -0.1435 0.0876  -0.1321 508 GLN C O   
12313 C CB  . GLN C  508 ? 0.4028 0.6454 0.4550 -0.1632 0.0920  -0.1387 508 GLN C CB  
12314 C CG  . GLN C  508 ? 0.4869 0.7071 0.5256 -0.1732 0.0950  -0.1427 508 GLN C CG  
12315 C CD  . GLN C  508 ? 0.5429 0.7563 0.5667 -0.1676 0.0880  -0.1429 508 GLN C CD  
12316 O OE1 . GLN C  508 ? 0.5281 0.7374 0.5459 -0.1538 0.0846  -0.1362 508 GLN C OE1 
12317 N NE2 . GLN C  508 ? 0.5702 0.7798 0.5858 -0.1769 0.0851  -0.1502 508 GLN C NE2 
12318 N N   . GLN C  509 ? 0.3177 0.5798 0.3965 -0.1475 0.0964  -0.1273 509 GLN C N   
12319 C CA  . GLN C  509 ? 0.3251 0.6103 0.4157 -0.1369 0.0934  -0.1250 509 GLN C CA  
12320 C C   . GLN C  509 ? 0.3541 0.6232 0.4379 -0.1236 0.0956  -0.1167 509 GLN C C   
12321 O O   . GLN C  509 ? 0.4283 0.6712 0.5041 -0.1230 0.1009  -0.1108 509 GLN C O   
12322 C CB  . GLN C  509 ? 0.4010 0.6996 0.5042 -0.1413 0.0957  -0.1258 509 GLN C CB  
12323 C CG  . GLN C  509 ? 0.4441 0.7628 0.5561 -0.1534 0.0924  -0.1342 509 GLN C CG  
12324 C CD  . GLN C  509 ? 0.4760 0.8042 0.5991 -0.1591 0.0962  -0.1343 509 GLN C CD  
12325 O OE1 . GLN C  509 ? 0.5050 0.8118 0.6232 -0.1619 0.1035  -0.1295 509 GLN C OE1 
12326 N NE2 . GLN C  509 ? 0.4669 0.8282 0.6053 -0.1607 0.0909  -0.1395 509 GLN C NE2 
12327 N N   . TYR C  510 ? 0.2448 0.5296 0.3315 -0.1123 0.0910  -0.1163 510 TYR C N   
12328 C CA  . TYR C  510 ? 0.2062 0.4798 0.2885 -0.0990 0.0925  -0.1092 510 TYR C CA  
12329 C C   . TYR C  510 ? 0.2133 0.5159 0.3096 -0.0896 0.0893  -0.1105 510 TYR C C   
12330 O O   . TYR C  510 ? 0.2090 0.5401 0.3184 -0.0931 0.0853  -0.1165 510 TYR C O   
12331 C CB  . TYR C  510 ? 0.2548 0.5140 0.3237 -0.0920 0.0909  -0.1068 510 TYR C CB  
12332 C CG  . TYR C  510 ? 0.2686 0.5446 0.3371 -0.0867 0.0817  -0.1104 510 TYR C CG  
12333 C CD1 . TYR C  510 ? 0.2938 0.5754 0.3608 -0.0955 0.0766  -0.1155 510 TYR C CD1 
12334 C CD2 . TYR C  510 ? 0.2844 0.5623 0.3497 -0.0708 0.0750  -0.1070 510 TYR C CD2 
12335 C CE1 . TYR C  510 ? 0.3391 0.6293 0.4016 -0.0886 0.0649  -0.1167 510 TYR C CE1 
12336 C CE2 . TYR C  510 ? 0.3160 0.6010 0.3769 -0.0636 0.0635  -0.1077 510 TYR C CE2 
12337 C CZ  . TYR C  510 ? 0.3659 0.6576 0.4253 -0.0724 0.0584  -0.1123 510 TYR C CZ  
12338 O OH  . TYR C  510 ? 0.4169 0.7160 0.4708 -0.0650 0.0467  -0.1127 510 TYR C OH  
12339 N N   . VAL C  511 ? 0.2738 0.5696 0.3676 -0.0775 0.0905  -0.1053 511 VAL C N   
12340 C CA  . VAL C  511 ? 0.2636 0.5851 0.3699 -0.0669 0.0878  -0.1066 511 VAL C CA  
12341 C C   . VAL C  511 ? 0.2670 0.5879 0.3673 -0.0516 0.0842  -0.1052 511 VAL C C   
12342 O O   . VAL C  511 ? 0.2726 0.5679 0.3582 -0.0492 0.0857  -0.1012 511 VAL C O   
12343 C CB  . VAL C  511 ? 0.1993 0.5164 0.3097 -0.0659 0.0934  -0.1024 511 VAL C CB  
12344 C CG1 . VAL C  511 ? 0.2067 0.5237 0.3221 -0.0803 0.0974  -0.1035 511 VAL C CG1 
12345 C CG2 . VAL C  511 ? 0.1979 0.4848 0.2945 -0.0603 0.0974  -0.0950 511 VAL C CG2 
12346 N N   . SER C  512 ? 0.1894 0.5379 0.3007 -0.0407 0.0790  -0.1086 512 SER C N   
12347 C CA  . SER C  512 ? 0.1934 0.5338 0.2963 -0.0236 0.0739  -0.1057 512 SER C CA  
12348 C C   . SER C  512 ? 0.1893 0.5248 0.2933 -0.0155 0.0799  -0.1029 512 SER C C   
12349 O O   . SER C  512 ? 0.1921 0.5427 0.3078 -0.0155 0.0815  -0.1035 512 SER C O   
12350 C CB  . SER C  512 ? 0.5695 0.9310 0.6785 -0.0129 0.0621  -0.1081 512 SER C CB  
12351 O OG  . SER C  512 ? 0.6398 1.0374 0.7701 -0.0115 0.0629  -0.1130 512 SER C OG  
12352 N N   . LEU C  513 ? 0.4162 0.7253 0.5054 -0.0091 0.0817  -0.0985 513 LEU C N   
12353 C CA  . LEU C  513 ? 0.3830 0.6834 0.4702 0.0002  0.0845  -0.0952 513 LEU C CA  
12354 C C   . LEU C  513 ? 0.3864 0.6938 0.4715 0.0180  0.0787  -0.0975 513 LEU C C   
12355 O O   . LEU C  513 ? 0.4191 0.7014 0.4885 0.0230  0.0739  -0.0939 513 LEU C O   
12356 C CB  . LEU C  513 ? 0.2308 0.4975 0.3032 -0.0039 0.0895  -0.0890 513 LEU C CB  
12357 C CG  . LEU C  513 ? 0.2460 0.5012 0.3181 -0.0192 0.0945  -0.0858 513 LEU C CG  
12358 C CD1 . LEU C  513 ? 0.2547 0.4781 0.3122 -0.0207 0.0975  -0.0793 513 LEU C CD1 
12359 C CD2 . LEU C  513 ? 0.2611 0.5302 0.3446 -0.0225 0.0984  -0.0858 513 LEU C CD2 
12360 N N   . ASN C  514 ? 0.2861 0.6178 0.3842 0.0270  0.0762  -0.1004 514 ASN C N   
12361 C CA  . ASN C  514 ? 0.2999 0.6364 0.3967 0.0455  0.0684  -0.1014 514 ASN C CA  
12362 C C   . ASN C  514 ? 0.2821 0.6345 0.3898 0.0540  0.0713  -0.1031 514 ASN C C   
12363 O O   . ASN C  514 ? 0.2541 0.6022 0.3643 0.0449  0.0783  -0.1009 514 ASN C O   
12364 C CB  . ASN C  514 ? 0.4356 0.7846 0.5357 0.0480  0.0571  -0.1024 514 ASN C CB  
12365 C CG  . ASN C  514 ? 0.5180 0.9028 0.6384 0.0386  0.0577  -0.1074 514 ASN C CG  
12366 O OD1 . ASN C  514 ? 0.5287 0.9363 0.6645 0.0384  0.0634  -0.1105 514 ASN C OD1 
12367 N ND2 . ASN C  514 ? 0.5717 0.9593 0.6910 0.0301  0.0513  -0.1079 514 ASN C ND2 
12368 N N   . LEU C  515 ? 0.3497 0.7150 0.4615 0.0714  0.0650  -0.1055 515 LEU C N   
12369 C CA  . LEU C  515 ? 0.3518 0.7284 0.4724 0.0790  0.0670  -0.1062 515 LEU C CA  
12370 C C   . LEU C  515 ? 0.3854 0.7924 0.5251 0.0699  0.0685  -0.1086 515 LEU C C   
12371 O O   . LEU C  515 ? 0.3696 0.7779 0.5138 0.0643  0.0755  -0.1075 515 LEU C O   
12372 C CB  . LEU C  515 ? 0.2655 0.6433 0.3836 0.1008  0.0602  -0.1077 515 LEU C CB  
12373 C CG  . LEU C  515 ? 0.2699 0.6135 0.3680 0.1101  0.0605  -0.1053 515 LEU C CG  
12374 C CD1 . LEU C  515 ? 0.2869 0.6288 0.3836 0.1293  0.0572  -0.1066 515 LEU C CD1 
12375 C CD2 . LEU C  515 ? 0.2731 0.5933 0.3616 0.0971  0.0695  -0.1020 515 LEU C CD2 
12376 N N   . LYS C  516 ? 0.5577 0.9884 0.7080 0.0678  0.0618  -0.1118 516 LYS C N   
12377 C CA  . LYS C  516 ? 0.5906 1.0503 0.7590 0.0576  0.0624  -0.1145 516 LYS C CA  
12378 C C   . LYS C  516 ? 0.6100 1.0579 0.7765 0.0367  0.0711  -0.1125 516 LYS C C   
12379 O O   . LYS C  516 ? 0.6398 1.0600 0.7920 0.0307  0.0750  -0.1091 516 LYS C O   
12380 C CB  . LYS C  516 ? 0.4593 0.9445 0.6374 0.0587  0.0523  -0.1183 516 LYS C CB  
12381 C CG  . LYS C  516 ? 0.4745 0.9762 0.6576 0.0800  0.0424  -0.1199 516 LYS C CG  
12382 C CD  . LYS C  516 ? 0.4972 1.0229 0.6884 0.0809  0.0310  -0.1227 516 LYS C CD  
12383 C CE  . LYS C  516 ? 0.4855 0.9842 0.6579 0.0769  0.0259  -0.1194 516 LYS C CE  
12384 N NZ  . LYS C  516 ? 0.4749 0.9871 0.6487 0.0744  0.0136  -0.1202 516 LYS C NZ  
12385 N N   . PRO C  517 ? 0.5040 0.9714 0.6845 0.0262  0.0743  -0.1141 517 PRO C N   
12386 C CA  . PRO C  517 ? 0.4975 0.9490 0.6741 0.0084  0.0828  -0.1113 517 PRO C CA  
12387 C C   . PRO C  517 ? 0.5284 0.9715 0.6999 -0.0051 0.0809  -0.1120 517 PRO C C   
12388 O O   . PRO C  517 ? 0.5355 0.9880 0.7075 -0.0013 0.0731  -0.1151 517 PRO C O   
12389 C CB  . PRO C  517 ? 0.2289 0.7053 0.4222 0.0018  0.0860  -0.1133 517 PRO C CB  
12390 C CG  . PRO C  517 ? 0.2263 0.7266 0.4300 0.0184  0.0811  -0.1161 517 PRO C CG  
12391 C CD  . PRO C  517 ? 0.2299 0.7307 0.4286 0.0302  0.0713  -0.1179 517 PRO C CD  
12392 N N   . LEU C  518 ? 0.5104 0.9356 0.6767 -0.0200 0.0879  -0.1091 518 LEU C N   
12393 C CA  . LEU C  518 ? 0.4804 0.8916 0.6391 -0.0326 0.0872  -0.1095 518 LEU C CA  
12394 C C   . LEU C  518 ? 0.4937 0.9312 0.6639 -0.0390 0.0806  -0.1158 518 LEU C C   
12395 O O   . LEU C  518 ? 0.5134 0.9750 0.6981 -0.0429 0.0802  -0.1189 518 LEU C O   
12396 C CB  . LEU C  518 ? 0.3011 0.6902 0.4535 -0.0466 0.0955  -0.1054 518 LEU C CB  
12397 C CG  . LEU C  518 ? 0.2767 0.6341 0.4139 -0.0429 0.1009  -0.0984 518 LEU C CG  
12398 C CD1 . LEU C  518 ? 0.2658 0.6035 0.3975 -0.0566 0.1073  -0.0946 518 LEU C CD1 
12399 C CD2 . LEU C  518 ? 0.2835 0.6240 0.4078 -0.0361 0.0969  -0.0975 518 LEU C CD2 
12400 N N   . GLU C  519 ? 0.3817 0.8145 0.5449 -0.0399 0.0755  -0.1176 519 GLU C N   
12401 C CA  . GLU C  519 ? 0.3798 0.8337 0.5508 -0.0474 0.0687  -0.1235 519 GLU C CA  
12402 C C   . GLU C  519 ? 0.3176 0.7477 0.4772 -0.0631 0.0725  -0.1231 519 GLU C C   
12403 O O   . GLU C  519 ? 0.3385 0.7410 0.4832 -0.0614 0.0759  -0.1189 519 GLU C O   
12404 C CB  . GLU C  519 ? 0.5246 0.9928 0.6957 -0.0335 0.0589  -0.1255 519 GLU C CB  
12405 C CG  . GLU C  519 ? 0.6519 1.1393 0.8281 -0.0406 0.0504  -0.1309 519 GLU C CG  
12406 C CD  . GLU C  519 ? 0.7880 1.2680 0.9521 -0.0246 0.0375  -0.1281 519 GLU C CD  
12407 O OE1 . GLU C  519 ? 0.8153 1.3001 0.9813 -0.0071 0.0349  -0.1258 519 GLU C OE1 
12408 O OE2 . GLU C  519 ? 0.8477 1.3154 0.9992 -0.0293 0.0305  -0.1280 519 GLU C OE2 
12409 N N   . VAL C  520 ? 0.2083 0.6465 0.3737 -0.0780 0.0723  -0.1273 520 VAL C N   
12410 C CA  . VAL C  520 ? 0.2333 0.6470 0.3864 -0.0919 0.0755  -0.1275 520 VAL C CA  
12411 C C   . VAL C  520 ? 0.2774 0.7011 0.4285 -0.0947 0.0676  -0.1326 520 VAL C C   
12412 O O   . VAL C  520 ? 0.2934 0.7457 0.4559 -0.0962 0.0597  -0.1382 520 VAL C O   
12413 C CB  . VAL C  520 ? 0.2208 0.6282 0.3766 -0.1075 0.0813  -0.1286 520 VAL C CB  
12414 C CG1 . VAL C  520 ? 0.2251 0.6080 0.3679 -0.1201 0.0834  -0.1298 520 VAL C CG1 
12415 C CG2 . VAL C  520 ? 0.2227 0.6149 0.3771 -0.1053 0.0896  -0.1222 520 VAL C CG2 
12416 N N   . ARG C  521 ? 0.4180 0.8177 0.5539 -0.0953 0.0695  -0.1303 521 ARG C N   
12417 C CA  . ARG C  521 ? 0.4304 0.8239 0.5547 -0.0955 0.0601  -0.1320 521 ARG C CA  
12418 C C   . ARG C  521 ? 0.4550 0.8257 0.5684 -0.1113 0.0652  -0.1338 521 ARG C C   
12419 O O   . ARG C  521 ? 0.4628 0.8135 0.5723 -0.1175 0.0761  -0.1311 521 ARG C O   
12420 C CB  . ARG C  521 ? 0.3234 0.6968 0.4313 -0.0787 0.0545  -0.1254 521 ARG C CB  
12421 C CG  . ARG C  521 ? 0.3073 0.6994 0.4246 -0.0621 0.0500  -0.1237 521 ARG C CG  
12422 C CD  . ARG C  521 ? 0.3479 0.7191 0.4481 -0.0462 0.0435  -0.1175 521 ARG C CD  
12423 N NE  . ARG C  521 ? 0.3954 0.7836 0.5044 -0.0298 0.0393  -0.1164 521 ARG C NE  
12424 C CZ  . ARG C  521 ? 0.4407 0.8110 0.5383 -0.0147 0.0368  -0.1109 521 ARG C CZ  
12425 N NH1 . ARG C  521 ? 0.4949 0.8314 0.5728 -0.0149 0.0381  -0.1058 521 ARG C NH1 
12426 N NH2 . ARG C  521 ? 0.4195 0.8059 0.5257 0.0004  0.0332  -0.1107 521 ARG C NH2 
12427 N N   . ARG C  522 ? 0.3679 0.7419 0.4761 -0.1173 0.0573  -0.1385 522 ARG C N   
12428 C CA  . ARG C  522 ? 0.4178 0.7703 0.5145 -0.1316 0.0614  -0.1413 522 ARG C CA  
12429 C C   . ARG C  522 ? 0.4194 0.7479 0.4943 -0.1236 0.0557  -0.1375 522 ARG C C   
12430 O O   . ARG C  522 ? 0.4269 0.7641 0.4983 -0.1113 0.0455  -0.1356 522 ARG C O   
12431 C CB  . ARG C  522 ? 0.6861 1.0608 0.7927 -0.1461 0.0570  -0.1507 522 ARG C CB  
12432 C CG  . ARG C  522 ? 0.7799 1.1654 0.9013 -0.1553 0.0638  -0.1530 522 ARG C CG  
12433 C CD  . ARG C  522 ? 0.8783 1.3010 1.0169 -0.1542 0.0553  -0.1578 522 ARG C CD  
12434 N NE  . ARG C  522 ? 0.9614 1.4070 1.1117 -0.1383 0.0515  -0.1544 522 ARG C NE  
12435 C CZ  . ARG C  522 ? 1.0135 1.4870 1.1708 -0.1285 0.0394  -0.1567 522 ARG C CZ  
12436 N NH1 . ARG C  522 ? 1.0470 1.5265 1.1980 -0.1324 0.0290  -0.1615 522 ARG C NH1 
12437 N NH2 . ARG C  522 ? 1.0017 1.4922 1.1684 -0.1125 0.0370  -0.1532 522 ARG C NH2 
12438 N N   . GLY C  523 ? 0.5545 0.8532 0.6148 -0.1303 0.0623  -0.1362 523 GLY C N   
12439 C CA  . GLY C  523 ? 0.5796 0.8563 0.6193 -0.1245 0.0578  -0.1331 523 GLY C CA  
12440 C C   . GLY C  523 ? 0.5928 0.8539 0.6222 -0.1088 0.0566  -0.1243 523 GLY C C   
12441 O O   . GLY C  523 ? 0.6326 0.8983 0.6555 -0.0983 0.0468  -0.1221 523 GLY C O   
12442 N N   . LEU C  524 ? 0.4922 0.7350 0.5200 -0.1070 0.0659  -0.1192 524 LEU C N   
12443 C CA  . LEU C  524 ? 0.4811 0.7094 0.5000 -0.0932 0.0648  -0.1114 524 LEU C CA  
12444 C C   . LEU C  524 ? 0.5181 0.7259 0.5173 -0.0912 0.0610  -0.1089 524 LEU C C   
12445 O O   . LEU C  524 ? 0.5084 0.6955 0.4983 -0.0979 0.0676  -0.1085 524 LEU C O   
12446 C CB  . LEU C  524 ? 0.2984 0.5106 0.3188 -0.0944 0.0760  -0.1073 524 LEU C CB  
12447 C CG  . LEU C  524 ? 0.2635 0.4609 0.2788 -0.0832 0.0785  -0.1000 524 LEU C CG  
12448 C CD1 . LEU C  524 ? 0.2130 0.3815 0.2142 -0.0855 0.0842  -0.0959 524 LEU C CD1 
12449 C CD2 . LEU C  524 ? 0.2634 0.4671 0.2754 -0.0693 0.0687  -0.0972 524 LEU C CD2 
12450 N N   . ARG C  525 ? 0.5791 0.7922 0.5718 -0.0809 0.0508  -0.1067 525 ARG C N   
12451 C CA  . ARG C  525 ? 0.6319 0.8291 0.6054 -0.0789 0.0460  -0.1043 525 ARG C CA  
12452 C C   . ARG C  525 ? 0.6195 0.8082 0.5850 -0.0920 0.0494  -0.1095 525 ARG C C   
12453 O O   . ARG C  525 ? 0.6208 0.7863 0.5743 -0.0944 0.0555  -0.1069 525 ARG C O   
12454 C CB  . ARG C  525 ? 0.7980 0.9712 0.7595 -0.0701 0.0484  -0.0960 525 ARG C CB  
12455 C CG  . ARG C  525 ? 0.8724 1.0497 0.8337 -0.0553 0.0411  -0.0907 525 ARG C CG  
12456 C CD  . ARG C  525 ? 0.9712 1.1563 0.9236 -0.0496 0.0295  -0.0905 525 ARG C CD  
12457 N NE  . ARG C  525 ? 1.0607 1.2249 0.9955 -0.0414 0.0265  -0.0830 525 ARG C NE  
12458 C CZ  . ARG C  525 ? 1.1369 1.2992 1.0576 -0.0380 0.0183  -0.0811 525 ARG C CZ  
12459 N NH1 . ARG C  525 ? 1.1639 1.3445 1.0857 -0.0418 0.0116  -0.0866 525 ARG C NH1 
12460 N NH2 . ARG C  525 ? 1.1567 1.2985 1.0614 -0.0314 0.0166  -0.0737 525 ARG C NH2 
12461 N N   . ALA C  526 ? 0.5040 0.7117 0.4761 -0.1002 0.0454  -0.1173 526 ALA C N   
12462 C CA  . ALA C  526 ? 0.4171 0.6184 0.3856 -0.1146 0.0503  -0.1241 526 ALA C CA  
12463 C C   . ALA C  526 ? 0.3934 0.5797 0.3415 -0.1167 0.0476  -0.1251 526 ALA C C   
12464 O O   . ALA C  526 ? 0.3732 0.5388 0.3123 -0.1232 0.0557  -0.1260 526 ALA C O   
12465 C CB  . ALA C  526 ? 0.2931 0.5203 0.2767 -0.1240 0.0472  -0.1326 526 ALA C CB  
12466 N N   . GLN C  527 ? 0.4145 0.6115 0.3549 -0.1107 0.0364  -0.1249 527 GLN C N   
12467 C CA  . GLN C  527 ? 0.4566 0.6436 0.3772 -0.1129 0.0327  -0.1266 527 GLN C CA  
12468 C C   . GLN C  527 ? 0.4397 0.6019 0.3448 -0.1053 0.0366  -0.1179 527 GLN C C   
12469 O O   . GLN C  527 ? 0.4764 0.6203 0.3669 -0.1100 0.0417  -0.1186 527 GLN C O   
12470 C CB  . GLN C  527 ? 0.7352 0.9427 0.6524 -0.1077 0.0188  -0.1280 527 GLN C CB  
12471 C CG  . GLN C  527 ? 0.8045 1.0430 0.7425 -0.1097 0.0130  -0.1335 527 GLN C CG  
12472 C CD  . GLN C  527 ? 0.8602 1.1092 0.8039 -0.1256 0.0141  -0.1446 527 GLN C CD  
12473 O OE1 . GLN C  527 ? 0.8784 1.1140 0.8071 -0.1335 0.0156  -0.1490 527 GLN C OE1 
12474 N NE2 . GLN C  527 ? 0.8788 1.1514 0.8441 -0.1306 0.0136  -0.1495 527 GLN C NE2 
12475 N N   . THR C  528 ? 0.4041 0.5662 0.3129 -0.0937 0.0344  -0.1101 528 THR C N   
12476 C CA  . THR C  528 ? 0.3800 0.5201 0.2757 -0.0862 0.0373  -0.1014 528 THR C CA  
12477 C C   . THR C  528 ? 0.3681 0.4887 0.2639 -0.0922 0.0499  -0.1007 528 THR C C   
12478 O O   . THR C  528 ? 0.3860 0.4877 0.2676 -0.0926 0.0542  -0.0975 528 THR C O   
12479 C CB  . THR C  528 ? 0.3636 0.5072 0.2647 -0.0733 0.0327  -0.0942 528 THR C CB  
12480 O OG1 . THR C  528 ? 0.3577 0.5125 0.2518 -0.0656 0.0207  -0.0928 528 THR C OG1 
12481 C CG2 . THR C  528 ? 0.3939 0.5136 0.2857 -0.0682 0.0382  -0.0860 528 THR C CG2 
12482 N N   . CYS C  529 ? 0.2827 0.4086 0.1945 -0.0970 0.0560  -0.1038 529 CYS C N   
12483 C CA  . CYS C  529 ? 0.2866 0.3950 0.1992 -0.1024 0.0677  -0.1032 529 CYS C CA  
12484 C C   . CYS C  529 ? 0.2990 0.3995 0.2039 -0.1133 0.0723  -0.1101 529 CYS C C   
12485 O O   . CYS C  529 ? 0.2873 0.3696 0.1867 -0.1158 0.0810  -0.1088 529 CYS C O   
12486 C CB  . CYS C  529 ? 0.2633 0.3777 0.1934 -0.1032 0.0731  -0.1031 529 CYS C CB  
12487 S SG  . CYS C  529 ? 0.7979 0.9092 0.7318 -0.0901 0.0721  -0.0939 529 CYS C SG  
12488 N N   . ALA C  530 ? 0.3851 0.4995 0.2896 -0.1196 0.0665  -0.1176 530 ALA C N   
12489 C CA  . ALA C  530 ? 0.3750 0.4798 0.2690 -0.1293 0.0702  -0.1246 530 ALA C CA  
12490 C C   . ALA C  530 ? 0.3759 0.4643 0.2504 -0.1245 0.0707  -0.1202 530 ALA C C   
12491 O O   . ALA C  530 ? 0.3875 0.4576 0.2593 -0.1264 0.0774  -0.1181 530 ALA C O   
12492 C CB  . ALA C  530 ? 0.3215 0.4445 0.2164 -0.1365 0.0624  -0.1336 530 ALA C CB  
12493 N N   . PHE C  531 ? 0.4006 0.4945 0.2678 -0.1157 0.0622  -0.1147 531 PHE C N   
12494 C CA  . PHE C  531 ? 0.4249 0.5033 0.2739 -0.1106 0.0628  -0.1087 531 PHE C CA  
12495 C C   . PHE C  531 ? 0.4110 0.4702 0.2650 -0.1070 0.0718  -0.1007 531 PHE C C   
12496 O O   . PHE C  531 ? 0.4052 0.4491 0.2568 -0.1089 0.0773  -0.0990 531 PHE C O   
12497 C CB  . PHE C  531 ? 0.3319 0.4180 0.1751 -0.1006 0.0522  -0.1023 531 PHE C CB  
12498 C CG  . PHE C  531 ? 0.3698 0.4393 0.1953 -0.0951 0.0533  -0.0944 531 PHE C CG  
12499 C CD1 . PHE C  531 ? 0.3979 0.4613 0.2054 -0.0974 0.0519  -0.0955 531 PHE C CD1 
12500 C CD2 . PHE C  531 ? 0.3308 0.3910 0.1586 -0.0874 0.0552  -0.0854 531 PHE C CD2 
12501 C CE1 . PHE C  531 ? 0.3647 0.4133 0.1579 -0.0923 0.0530  -0.0871 531 PHE C CE1 
12502 C CE2 . PHE C  531 ? 0.3391 0.3845 0.1513 -0.0836 0.0563  -0.0780 531 PHE C CE2 
12503 C CZ  . PHE C  531 ? 0.3561 0.3962 0.1504 -0.0864 0.0557  -0.0790 531 PHE C CZ  
12504 N N   . TRP C  532 ? 0.3910 0.4523 0.2527 -0.1014 0.0726  -0.0960 532 TRP C N   
12505 C CA  . TRP C  532 ? 0.3588 0.4041 0.2258 -0.0967 0.0787  -0.0876 532 TRP C CA  
12506 C C   . TRP C  532 ? 0.3466 0.3808 0.2242 -0.1013 0.0862  -0.0881 532 TRP C C   
12507 O O   . TRP C  532 ? 0.3598 0.3793 0.2357 -0.0991 0.0896  -0.0830 532 TRP C O   
12508 C CB  . TRP C  532 ? 0.2831 0.3343 0.1577 -0.0905 0.0778  -0.0839 532 TRP C CB  
12509 C CG  . TRP C  532 ? 0.2879 0.3400 0.1539 -0.0819 0.0697  -0.0779 532 TRP C CG  
12510 C CD1 . TRP C  532 ? 0.3249 0.3913 0.1941 -0.0762 0.0599  -0.0778 532 TRP C CD1 
12511 C CD2 . TRP C  532 ? 0.2929 0.3299 0.1465 -0.0776 0.0706  -0.0705 532 TRP C CD2 
12512 N NE1 . TRP C  532 ? 0.2968 0.3561 0.1550 -0.0681 0.0546  -0.0706 532 TRP C NE1 
12513 C CE2 . TRP C  532 ? 0.2989 0.3399 0.1474 -0.0695 0.0611  -0.0660 532 TRP C CE2 
12514 C CE3 . TRP C  532 ? 0.2927 0.3134 0.1428 -0.0786 0.0770  -0.0660 532 TRP C CE3 
12515 C CZ2 . TRP C  532 ? 0.3067 0.3342 0.1425 -0.0645 0.0597  -0.0581 532 TRP C CZ2 
12516 C CZ3 . TRP C  532 ? 0.2993 0.3094 0.1375 -0.0744 0.0761  -0.0588 532 TRP C CZ3 
12517 C CH2 . TRP C  532 ? 0.3071 0.3197 0.1367 -0.0682 0.0680  -0.0552 532 TRP C CH2 
12518 N N   . ASN C  533 ? 0.2932 0.3349 0.1815 -0.1074 0.0886  -0.0941 533 ASN C N   
12519 C CA  . ASN C  533 ? 0.3318 0.3624 0.2293 -0.1116 0.0954  -0.0946 533 ASN C CA  
12520 C C   . ASN C  533 ? 0.3628 0.3853 0.2540 -0.1185 0.0984  -0.1000 533 ASN C C   
12521 O O   . ASN C  533 ? 0.3827 0.3903 0.2759 -0.1186 0.1035  -0.0978 533 ASN C O   
12522 C CB  . ASN C  533 ? 0.4394 0.4797 0.3503 -0.1159 0.0977  -0.0984 533 ASN C CB  
12523 C CG  . ASN C  533 ? 0.4575 0.5062 0.3759 -0.1087 0.0954  -0.0934 533 ASN C CG  
12524 O OD1 . ASN C  533 ? 0.4723 0.5137 0.3879 -0.1005 0.0937  -0.0859 533 ASN C OD1 
12525 N ND2 . ASN C  533 ? 0.4487 0.5130 0.3770 -0.1120 0.0957  -0.0979 533 ASN C ND2 
12526 N N   . ARG C  534 ? 0.3353 0.3681 0.2189 -0.1241 0.0946  -0.1074 534 ARG C N   
12527 C CA  . ARG C  534 ? 0.3833 0.4090 0.2606 -0.1310 0.0971  -0.1133 534 ARG C CA  
12528 C C   . ARG C  534 ? 0.3609 0.3797 0.2231 -0.1271 0.0946  -0.1109 534 ARG C C   
12529 O O   . ARG C  534 ? 0.3587 0.3632 0.2180 -0.1267 0.0996  -0.1093 534 ARG C O   
12530 C CB  . ARG C  534 ? 0.7320 0.7718 0.6110 -0.1408 0.0947  -0.1239 534 ARG C CB  
12531 C CG  . ARG C  534 ? 0.8394 0.8822 0.7326 -0.1472 0.1001  -0.1274 534 ARG C CG  
12532 C CD  . ARG C  534 ? 0.9530 1.0191 0.8512 -0.1529 0.0942  -0.1353 534 ARG C CD  
12533 N NE  . ARG C  534 ? 1.0384 1.1066 0.9418 -0.1653 0.0973  -0.1444 534 ARG C NE  
12534 C CZ  . ARG C  534 ? 1.0701 1.1416 0.9857 -0.1720 0.1028  -0.1476 534 ARG C CZ  
12535 N NH1 . ARG C  534 ? 1.0469 1.1210 0.9706 -0.1667 0.1061  -0.1424 534 ARG C NH1 
12536 N NH2 . ARG C  534 ? 1.0968 1.1690 1.0166 -0.1835 0.1053  -0.1551 534 ARG C NH2 
12537 N N   . PHE C  535 ? 0.3702 0.3995 0.2224 -0.1242 0.0868  -0.1108 535 PHE C N   
12538 C CA  . PHE C  535 ? 0.3566 0.3800 0.1927 -0.1216 0.0843  -0.1091 535 PHE C CA  
12539 C C   . PHE C  535 ? 0.3495 0.3610 0.1817 -0.1136 0.0869  -0.0993 535 PHE C C   
12540 O O   . PHE C  535 ? 0.3552 0.3547 0.1836 -0.1131 0.0917  -0.0977 535 PHE C O   
12541 C CB  . PHE C  535 ? 0.4060 0.4440 0.2309 -0.1211 0.0743  -0.1120 535 PHE C CB  
12542 C CG  . PHE C  535 ? 0.4452 0.4769 0.2519 -0.1178 0.0716  -0.1094 535 PHE C CG  
12543 C CD1 . PHE C  535 ? 0.4711 0.4983 0.2697 -0.1227 0.0727  -0.1151 535 PHE C CD1 
12544 C CD2 . PHE C  535 ? 0.4566 0.4860 0.2536 -0.1100 0.0684  -0.1012 535 PHE C CD2 
12545 C CE1 . PHE C  535 ? 0.4680 0.4897 0.2491 -0.1195 0.0707  -0.1127 535 PHE C CE1 
12546 C CE2 . PHE C  535 ? 0.4762 0.4994 0.2556 -0.1074 0.0666  -0.0984 535 PHE C CE2 
12547 C CZ  . PHE C  535 ? 0.4702 0.4903 0.2419 -0.1120 0.0677  -0.1042 535 PHE C CZ  
12548 N N   . LEU C  536 ? 0.3404 0.3561 0.1734 -0.1075 0.0835  -0.0932 536 LEU C N   
12549 C CA  . LEU C  536 ? 0.3376 0.3437 0.1660 -0.1005 0.0848  -0.0840 536 LEU C CA  
12550 C C   . LEU C  536 ? 0.4875 0.4799 0.3232 -0.0995 0.0923  -0.0803 536 LEU C C   
12551 O O   . LEU C  536 ? 0.3376 0.3224 0.1659 -0.0964 0.0939  -0.0756 536 LEU C O   
12552 C CB  . LEU C  536 ? 0.4265 0.4378 0.2585 -0.0951 0.0814  -0.0789 536 LEU C CB  
12553 C CG  . LEU C  536 ? 0.4867 0.4914 0.3079 -0.0886 0.0796  -0.0703 536 LEU C CG  
12554 C CD1 . LEU C  536 ? 0.4957 0.4893 0.3263 -0.0854 0.0850  -0.0633 536 LEU C CD1 
12555 C CD2 . LEU C  536 ? 0.5339 0.5349 0.3372 -0.0890 0.0775  -0.0697 536 LEU C CD2 
12556 N N   . PRO C  537 ? 0.5857 0.5755 0.4356 -0.1020 0.0967  -0.0824 537 PRO C N   
12557 C CA  . PRO C  537 ? 0.5802 0.5581 0.4357 -0.1011 0.1028  -0.0803 537 PRO C CA  
12558 C C   . PRO C  537 ? 0.6227 0.5945 0.4680 -0.1036 0.1056  -0.0839 537 PRO C C   
12559 O O   . PRO C  537 ? 0.6816 0.6463 0.5250 -0.0999 0.1085  -0.0796 537 PRO C O   
12560 C CB  . PRO C  537 ? 0.4470 0.4240 0.3155 -0.1049 0.1060  -0.0840 537 PRO C CB  
12561 C CG  . PRO C  537 ? 0.4565 0.4465 0.3263 -0.1089 0.1021  -0.0889 537 PRO C CG  
12562 C CD  . PRO C  537 ? 0.4522 0.4498 0.3142 -0.1042 0.0962  -0.0851 537 PRO C CD  
12563 N N   . LYS C  538 ? 0.5378 0.5133 0.3769 -0.1098 0.1048  -0.0918 538 LYS C N   
12564 C CA  . LYS C  538 ? 0.5557 0.5251 0.3840 -0.1121 0.1074  -0.0959 538 LYS C CA  
12565 C C   . LYS C  538 ? 0.6032 0.5729 0.4171 -0.1079 0.1048  -0.0917 538 LYS C C   
12566 O O   . LYS C  538 ? 0.6107 0.5742 0.4162 -0.1075 0.1081  -0.0926 538 LYS C O   
12567 C CB  . LYS C  538 ? 0.5173 0.4914 0.3414 -0.1201 0.1060  -0.1058 538 LYS C CB  
12568 C CG  . LYS C  538 ? 0.5345 0.5083 0.3719 -0.1258 0.1093  -0.1103 538 LYS C CG  
12569 C CD  . LYS C  538 ? 0.6032 0.5777 0.4360 -0.1345 0.1100  -0.1204 538 LYS C CD  
12570 C CE  . LYS C  538 ? 0.6990 0.6595 0.5254 -0.1350 0.1162  -0.1228 538 LYS C CE  
12571 N NZ  . LYS C  538 ? 0.7588 0.7209 0.5713 -0.1398 0.1136  -0.1308 538 LYS C NZ  
12572 N N   . LEU C  539 ? 0.6849 0.6615 0.4950 -0.1046 0.0991  -0.0872 539 LEU C N   
12573 C CA  . LEU C  539 ? 0.7114 0.6880 0.5063 -0.1010 0.0961  -0.0827 539 LEU C CA  
12574 C C   . LEU C  539 ? 0.8357 0.8046 0.6325 -0.0959 0.1003  -0.0744 539 LEU C C   
12575 O O   . LEU C  539 ? 0.9044 0.8694 0.6905 -0.0947 0.1022  -0.0725 539 LEU C O   
12576 C CB  . LEU C  539 ? 0.4292 0.4151 0.2177 -0.0993 0.0882  -0.0809 539 LEU C CB  
12577 C CG  . LEU C  539 ? 0.4223 0.4077 0.1912 -0.0965 0.0841  -0.0774 539 LEU C CG  
12578 C CD1 . LEU C  539 ? 0.4177 0.4043 0.1749 -0.1004 0.0831  -0.0846 539 LEU C CD1 
12579 C CD2 . LEU C  539 ? 0.4331 0.4264 0.1956 -0.0935 0.0760  -0.0746 539 LEU C CD2 
12580 N N   . LEU C  540 ? 0.9516 0.9194 0.7620 -0.0931 0.1014  -0.0695 540 LEU C N   
12581 C CA  . LEU C  540 ? 1.0190 0.9810 0.8336 -0.0890 0.1049  -0.0624 540 LEU C CA  
12582 C C   . LEU C  540 ? 1.1079 1.0643 0.9324 -0.0894 0.1111  -0.0646 540 LEU C C   
12583 O O   . LEU C  540 ? 1.1438 1.0968 0.9743 -0.0861 0.1142  -0.0600 540 LEU C O   
12584 C CB  . LEU C  540 ? 0.8602 0.8233 0.6829 -0.0855 0.1025  -0.0560 540 LEU C CB  
12585 C CG  . LEU C  540 ? 0.8051 0.7723 0.6404 -0.0858 0.1005  -0.0580 540 LEU C CG  
12586 C CD1 . LEU C  540 ? 0.8071 0.7703 0.6572 -0.0860 0.1050  -0.0594 540 LEU C CD1 
12587 C CD2 . LEU C  540 ? 0.7370 0.7061 0.5741 -0.0821 0.0970  -0.0522 540 LEU C CD2 
12588 N N   . SER C  541 ? 1.0821 1.0379 0.9078 -0.0935 0.1127  -0.0721 541 SER C N   
12589 C CA  . SER C  541 ? 1.1068 1.0557 0.9367 -0.0943 0.1188  -0.0755 541 SER C CA  
12590 C C   . SER C  541 ? 1.1890 1.1354 1.0049 -0.0951 0.1215  -0.0783 541 SER C C   
12591 O O   . SER C  541 ? 1.2237 1.1642 1.0406 -0.0952 0.1271  -0.0814 541 SER C O   
12592 C CB  . SER C  541 ? 0.9619 0.9092 0.7986 -0.0991 0.1201  -0.0822 541 SER C CB  
12593 O OG  . SER C  541 ? 0.9512 0.8925 0.7820 -0.1023 0.1248  -0.0886 541 SER C OG  
12594 N N   . ALA C  542 ? 1.1602 1.1107 0.9619 -0.0953 0.1176  -0.0773 542 ALA C N   
12595 C CA  . ALA C  542 ? 1.1753 1.1237 0.9631 -0.0944 0.1202  -0.0773 542 ALA C CA  
12596 C C   . ALA C  542 ? 1.2528 1.2028 1.0365 -0.0904 0.1191  -0.0685 542 ALA C C   
12597 O O   . ALA C  542 ? 1.2214 1.1748 0.9958 -0.0902 0.1137  -0.0655 542 ALA C O   
12598 C CB  . ALA C  542 ? 0.9437 0.8947 0.7157 -0.0983 0.1166  -0.0839 542 ALA C CB  
12599 N N   . THR C  543 ? 1.5730 1.5204 1.3628 -0.0874 0.1244  -0.0644 543 THR C N   
12600 C CA  . THR C  543 ? 1.6398 1.5883 1.4282 -0.0846 0.1244  -0.0559 543 THR C CA  
12601 C C   . THR C  543 ? 1.6636 1.6110 1.4548 -0.0824 0.1313  -0.0540 543 THR C C   
12602 O O   . THR C  543 ? 1.6784 1.6253 1.4573 -0.0827 0.1346  -0.0554 543 THR C O   
12603 C CB  . THR C  543 ? 1.8393 1.7890 1.6408 -0.0829 0.1212  -0.0505 543 THR C CB  
12604 O OG1 . THR C  543 ? 1.8261 1.7780 1.6270 -0.0845 0.1155  -0.0530 543 THR C OG1 
12605 C CG2 . THR C  543 ? 1.8366 1.7865 1.6337 -0.0812 0.1204  -0.0422 543 THR C CG2 
12606 O OXT . THR C  543 ? 1.4322 1.3800 1.2377 -0.0800 0.1337  -0.0511 543 THR C OXT 
12607 N N   . GLU D  4   ? 1.2658 1.5482 1.4614 0.1082  -0.2847 -0.1503 4   GLU D N   
12608 C CA  . GLU D  4   ? 1.2551 1.5593 1.4682 0.0991  -0.2761 -0.1536 4   GLU D CA  
12609 C C   . GLU D  4   ? 1.2037 1.5226 1.4343 0.1097  -0.2704 -0.1589 4   GLU D C   
12610 O O   . GLU D  4   ? 1.2219 1.5716 1.4772 0.1108  -0.2718 -0.1639 4   GLU D O   
12611 C CB  . GLU D  4   ? 1.2262 1.5115 1.4223 0.0892  -0.2669 -0.1505 4   GLU D CB  
12612 C CG  . GLU D  4   ? 1.2407 1.4987 1.4103 0.0850  -0.2707 -0.1453 4   GLU D CG  
12613 C CD  . GLU D  4   ? 1.2263 1.4552 1.3741 0.0904  -0.2638 -0.1421 4   GLU D CD  
12614 O OE1 . GLU D  4   ? 1.2019 1.4309 1.3531 0.0913  -0.2543 -0.1435 4   GLU D OE1 
12615 O OE2 . GLU D  4   ? 1.2308 1.4377 1.3578 0.0933  -0.2680 -0.1383 4   GLU D OE2 
12616 N N   . ASP D  5   ? 1.0330 1.3300 1.2500 0.1175  -0.2643 -0.1582 5   ASP D N   
12617 C CA  . ASP D  5   ? 0.9324 1.2367 1.1605 0.1287  -0.2591 -0.1633 5   ASP D CA  
12618 C C   . ASP D  5   ? 0.9399 1.2121 1.1454 0.1342  -0.2543 -0.1602 5   ASP D C   
12619 O O   . ASP D  5   ? 0.9539 1.2117 1.1456 0.1258  -0.2475 -0.1567 5   ASP D O   
12620 C CB  . ASP D  5   ? 0.7002 1.0309 0.9475 0.1204  -0.2493 -0.1678 5   ASP D CB  
12621 C CG  . ASP D  5   ? 0.6188 0.9559 0.8751 0.1307  -0.2420 -0.1736 5   ASP D CG  
12622 O OD1 . ASP D  5   ? 0.6050 0.9313 0.8576 0.1452  -0.2464 -0.1754 5   ASP D OD1 
12623 O OD2 . ASP D  5   ? 0.5803 0.9330 0.8467 0.1240  -0.2323 -0.1766 5   ASP D OD2 
12624 N N   . PRO D  6   ? 1.0084 1.2698 1.2106 0.1484  -0.2582 -0.1617 6   PRO D N   
12625 C CA  . PRO D  6   ? 1.0316 1.2625 1.2125 0.1537  -0.2553 -0.1586 6   PRO D CA  
12626 C C   . PRO D  6   ? 1.0470 1.2790 1.2305 0.1528  -0.2436 -0.1616 6   PRO D C   
12627 O O   . PRO D  6   ? 1.0842 1.2924 1.2496 0.1532  -0.2396 -0.1581 6   PRO D O   
12628 C CB  . PRO D  6   ? 0.9038 1.1265 1.0836 0.1687  -0.2650 -0.1601 6   PRO D CB  
12629 C CG  . PRO D  6   ? 0.9083 1.1487 1.1000 0.1692  -0.2749 -0.1609 6   PRO D CG  
12630 C CD  . PRO D  6   ? 0.8877 1.1601 1.1012 0.1592  -0.2690 -0.1647 6   PRO D CD  
12631 N N   . GLN D  7   ? 0.9376 1.1980 1.1433 0.1515  -0.2383 -0.1680 7   GLN D N   
12632 C CA  . GLN D  7   ? 0.8741 1.1375 1.0826 0.1502  -0.2272 -0.1713 7   GLN D CA  
12633 C C   . GLN D  7   ? 0.7852 1.0379 0.9809 0.1370  -0.2201 -0.1660 7   GLN D C   
12634 O O   . GLN D  7   ? 0.8012 1.0367 0.9839 0.1368  -0.2137 -0.1643 7   GLN D O   
12635 C CB  . GLN D  7   ? 0.9666 1.2654 1.2016 0.1502  -0.2227 -0.1792 7   GLN D CB  
12636 C CG  . GLN D  7   ? 1.0232 1.3348 1.2722 0.1646  -0.2291 -0.1856 7   GLN D CG  
12637 C CD  . GLN D  7   ? 1.0534 1.3415 1.2899 0.1780  -0.2305 -0.1873 7   GLN D CD  
12638 O OE1 . GLN D  7   ? 1.0426 1.3165 1.2684 0.1766  -0.2232 -0.1869 7   GLN D OE1 
12639 N NE2 . GLN D  7   ? 1.0836 1.3669 1.3211 0.1908  -0.2409 -0.1892 7   GLN D NE2 
12640 N N   . LEU D  8   ? 0.5860 0.8483 0.7848 0.1260  -0.2221 -0.1634 8   LEU D N   
12641 C CA  . LEU D  8   ? 0.4613 0.7142 0.6485 0.1132  -0.2165 -0.1590 8   LEU D CA  
12642 C C   . LEU D  8   ? 0.4780 0.6999 0.6394 0.1125  -0.2193 -0.1520 8   LEU D C   
12643 O O   . LEU D  8   ? 0.5198 0.7302 0.6689 0.1042  -0.2141 -0.1486 8   LEU D O   
12644 C CB  . LEU D  8   ? 0.3520 0.6270 0.5523 0.1004  -0.2176 -0.1594 8   LEU D CB  
12645 C CG  . LEU D  8   ? 0.3645 0.6741 0.5909 0.0968  -0.2136 -0.1656 8   LEU D CG  
12646 C CD1 . LEU D  8   ? 0.3433 0.6658 0.5747 0.0794  -0.2124 -0.1639 8   LEU D CD1 
12647 C CD2 . LEU D  8   ? 0.3353 0.6495 0.5666 0.1020  -0.2038 -0.1701 8   LEU D CD2 
12648 N N   . LEU D  9   ? 0.4126 0.6213 0.5651 0.1209  -0.2275 -0.1499 9   LEU D N   
12649 C CA  . LEU D  9   ? 0.3790 0.5604 0.5069 0.1198  -0.2296 -0.1434 9   LEU D CA  
12650 C C   . LEU D  9   ? 0.3816 0.5424 0.4963 0.1288  -0.2284 -0.1417 9   LEU D C   
12651 O O   . LEU D  9   ? 0.3932 0.5519 0.5105 0.1389  -0.2345 -0.1433 9   LEU D O   
12652 C CB  . LEU D  9   ? 0.4231 0.6023 0.5461 0.1194  -0.2403 -0.1409 9   LEU D CB  
12653 C CG  . LEU D  9   ? 0.4442 0.6009 0.5430 0.1142  -0.2413 -0.1348 9   LEU D CG  
12654 C CD1 . LEU D  9   ? 0.4133 0.5757 0.5117 0.1085  -0.2496 -0.1339 9   LEU D CD1 
12655 C CD2 . LEU D  9   ? 0.4113 0.5444 0.4911 0.1221  -0.2437 -0.1306 9   LEU D CD2 
12656 N N   . VAL D  10  ? 0.4270 0.5724 0.5270 0.1246  -0.2210 -0.1384 10  VAL D N   
12657 C CA  . VAL D  10  ? 0.3732 0.4998 0.4605 0.1308  -0.2188 -0.1364 10  VAL D CA  
12658 C C   . VAL D  10  ? 0.4301 0.5347 0.4938 0.1275  -0.2193 -0.1293 10  VAL D C   
12659 O O   . VAL D  10  ? 0.4570 0.5614 0.5149 0.1196  -0.2173 -0.1272 10  VAL D O   
12660 C CB  . VAL D  10  ? 0.4054 0.5366 0.4976 0.1284  -0.2085 -0.1390 10  VAL D CB  
12661 C CG1 . VAL D  10  ? 0.4192 0.5305 0.4967 0.1327  -0.2062 -0.1363 10  VAL D CG1 
12662 C CG2 . VAL D  10  ? 0.4084 0.5623 0.5232 0.1323  -0.2074 -0.1464 10  VAL D CG2 
12663 N N   . ARG D  11  ? 0.3893 0.4755 0.4388 0.1332  -0.2224 -0.1258 11  ARG D N   
12664 C CA  . ARG D  11  ? 0.4176 0.4852 0.4448 0.1292  -0.2207 -0.1192 11  ARG D CA  
12665 C C   . ARG D  11  ? 0.3841 0.4416 0.4033 0.1290  -0.2134 -0.1175 11  ARG D C   
12666 O O   . ARG D  11  ? 0.3881 0.4404 0.4088 0.1354  -0.2152 -0.1187 11  ARG D O   
12667 C CB  . ARG D  11  ? 0.7742 0.8274 0.7867 0.1333  -0.2306 -0.1145 11  ARG D CB  
12668 C CG  . ARG D  11  ? 0.8473 0.8814 0.8364 0.1303  -0.2282 -0.1077 11  ARG D CG  
12669 C CD  . ARG D  11  ? 0.9335 0.9542 0.9058 0.1322  -0.2376 -0.1024 11  ARG D CD  
12670 N NE  . ARG D  11  ? 1.0021 1.0207 0.9610 0.1253  -0.2357 -0.0991 11  ARG D NE  
12671 C CZ  . ARG D  11  ? 1.0317 1.0566 0.9922 0.1234  -0.2406 -0.1003 11  ARG D CZ  
12672 N NH1 . ARG D  11  ? 1.0617 1.0969 1.0377 0.1276  -0.2477 -0.1041 11  ARG D NH1 
12673 N NH2 . ARG D  11  ? 0.9932 1.0145 0.9398 0.1175  -0.2387 -0.0980 11  ARG D NH2 
12674 N N   . VAL D  12  ? 0.4622 0.5165 0.4724 0.1220  -0.2057 -0.1149 12  VAL D N   
12675 C CA  . VAL D  12  ? 0.4969 0.5422 0.4983 0.1212  -0.1992 -0.1125 12  VAL D CA  
12676 C C   . VAL D  12  ? 0.5187 0.5493 0.4982 0.1181  -0.1992 -0.1057 12  VAL D C   
12677 O O   . VAL D  12  ? 0.5310 0.5575 0.5014 0.1172  -0.2044 -0.1030 12  VAL D O   
12678 C CB  . VAL D  12  ? 0.3727 0.4285 0.3831 0.1164  -0.1893 -0.1156 12  VAL D CB  
12679 C CG1 . VAL D  12  ? 0.3397 0.4122 0.3713 0.1187  -0.1893 -0.1224 12  VAL D CG1 
12680 C CG2 . VAL D  12  ? 0.3558 0.4129 0.3603 0.1092  -0.1856 -0.1140 12  VAL D CG2 
12681 N N   . ARG D  13  ? 0.4817 0.5060 0.4529 0.1162  -0.1934 -0.1031 13  ARG D N   
12682 C CA  . ARG D  13  ? 0.5543 0.5670 0.5050 0.1130  -0.1930 -0.0966 13  ARG D CA  
12683 C C   . ARG D  13  ? 0.5460 0.5616 0.4891 0.1079  -0.1901 -0.0955 13  ARG D C   
12684 O O   . ARG D  13  ? 0.5851 0.5935 0.5110 0.1056  -0.1912 -0.0908 13  ARG D O   
12685 C CB  . ARG D  13  ? 0.7711 0.7802 0.7168 0.1110  -0.1867 -0.0946 13  ARG D CB  
12686 C CG  . ARG D  13  ? 0.8416 0.8407 0.7663 0.1071  -0.1865 -0.0876 13  ARG D CG  
12687 C CD  . ARG D  13  ? 0.9132 0.8977 0.8273 0.1101  -0.1952 -0.0832 13  ARG D CD  
12688 N NE  . ARG D  13  ? 0.9931 0.9741 0.9155 0.1139  -0.1961 -0.0857 13  ARG D NE  
12689 C CZ  . ARG D  13  ? 1.0271 1.0049 0.9444 0.1108  -0.1920 -0.0839 13  ARG D CZ  
12690 N NH1 . ARG D  13  ? 1.0750 1.0548 0.9799 0.1036  -0.1861 -0.0794 13  ARG D NH1 
12691 N NH2 . ARG D  13  ? 0.9729 0.9465 0.8976 0.1150  -0.1939 -0.0870 13  ARG D NH2 
12692 N N   . GLY D  14  ? 0.5039 0.5297 0.4586 0.1059  -0.1868 -0.0999 14  GLY D N   
12693 C CA  . GLY D  14  ? 0.4862 0.5128 0.4338 0.1018  -0.1854 -0.0998 14  GLY D CA  
12694 C C   . GLY D  14  ? 0.4948 0.5248 0.4470 0.1022  -0.1929 -0.1019 14  GLY D C   
12695 O O   . GLY D  14  ? 0.5087 0.5396 0.4568 0.0987  -0.1926 -0.1030 14  GLY D O   
12696 N N   . GLY D  15  ? 0.4850 0.5166 0.4453 0.1066  -0.2002 -0.1027 15  GLY D N   
12697 C CA  . GLY D  15  ? 0.5000 0.5379 0.4675 0.1069  -0.2077 -0.1051 15  GLY D CA  
12698 C C   . GLY D  15  ? 0.4810 0.5340 0.4707 0.1074  -0.2083 -0.1106 15  GLY D C   
12699 O O   . GLY D  15  ? 0.4549 0.5135 0.4555 0.1091  -0.2037 -0.1130 15  GLY D O   
12700 N N   . GLN D  16  ? 0.3914 0.4524 0.3876 0.1056  -0.2143 -0.1128 16  GLN D N   
12701 C CA  . GLN D  16  ? 0.4227 0.5008 0.4406 0.1064  -0.2171 -0.1176 16  GLN D CA  
12702 C C   . GLN D  16  ? 0.3815 0.4714 0.4110 0.0998  -0.2105 -0.1211 16  GLN D C   
12703 O O   . GLN D  16  ? 0.3682 0.4527 0.3888 0.0939  -0.2062 -0.1200 16  GLN D O   
12704 C CB  . GLN D  16  ? 0.6940 0.7778 0.7150 0.1065  -0.2272 -0.1183 16  GLN D CB  
12705 C CG  . GLN D  16  ? 0.7803 0.8507 0.7860 0.1113  -0.2348 -0.1142 16  GLN D CG  
12706 C CD  . GLN D  16  ? 0.8614 0.9392 0.8786 0.1182  -0.2442 -0.1159 16  GLN D CD  
12707 O OE1 . GLN D  16  ? 0.8949 0.9713 0.9173 0.1253  -0.2448 -0.1166 16  GLN D OE1 
12708 N NE2 . GLN D  16  ? 0.8881 0.9738 0.9092 0.1166  -0.2522 -0.1170 16  GLN D NE2 
12709 N N   . LEU D  17  ? 0.5784 0.6849 0.6277 0.1011  -0.2103 -0.1253 17  LEU D N   
12710 C CA  . LEU D  17  ? 0.5514 0.6718 0.6136 0.0944  -0.2048 -0.1286 17  LEU D CA  
12711 C C   . LEU D  17  ? 0.5440 0.6868 0.6275 0.0938  -0.2099 -0.1330 17  LEU D C   
12712 O O   . LEU D  17  ? 0.5682 0.7185 0.6620 0.1017  -0.2133 -0.1354 17  LEU D O   
12713 C CB  . LEU D  17  ? 0.3378 0.4583 0.4031 0.0964  -0.1962 -0.1297 17  LEU D CB  
12714 C CG  . LEU D  17  ? 0.3330 0.4358 0.3808 0.0966  -0.1898 -0.1259 17  LEU D CG  
12715 C CD1 . LEU D  17  ? 0.3217 0.4269 0.3752 0.0999  -0.1834 -0.1277 17  LEU D CD1 
12716 C CD2 . LEU D  17  ? 0.3296 0.4283 0.3695 0.0885  -0.1860 -0.1246 17  LEU D CD2 
12717 N N   . ARG D  18  ? 0.3536 0.5070 0.4435 0.0843  -0.2107 -0.1343 18  ARG D N   
12718 C CA  . ARG D  18  ? 0.3536 0.5322 0.4656 0.0814  -0.2139 -0.1385 18  ARG D CA  
12719 C C   . ARG D  18  ? 0.3389 0.5296 0.4622 0.0777  -0.2053 -0.1414 18  ARG D C   
12720 O O   . ARG D  18  ? 0.3318 0.5130 0.4456 0.0716  -0.1994 -0.1396 18  ARG D O   
12721 C CB  . ARG D  18  ? 0.6349 0.8188 0.7470 0.0708  -0.2196 -0.1381 18  ARG D CB  
12722 C CG  . ARG D  18  ? 0.7233 0.9355 0.8589 0.0665  -0.2240 -0.1419 18  ARG D CG  
12723 C CD  . ARG D  18  ? 0.7962 1.0118 0.9300 0.0555  -0.2315 -0.1411 18  ARG D CD  
12724 N NE  . ARG D  18  ? 0.8612 1.0523 0.9716 0.0563  -0.2353 -0.1375 18  ARG D NE  
12725 C CZ  . ARG D  18  ? 0.9064 1.0898 1.0096 0.0644  -0.2419 -0.1361 18  ARG D CZ  
12726 N NH1 . ARG D  18  ? 0.8999 1.0964 1.0170 0.0731  -0.2461 -0.1378 18  ARG D NH1 
12727 N NH2 . ARG D  18  ? 0.9409 1.1033 1.0224 0.0642  -0.2444 -0.1332 18  ARG D NH2 
12728 N N   . GLY D  19  ? 0.3666 0.5785 0.5101 0.0819  -0.2047 -0.1460 19  GLY D N   
12729 C CA  . GLY D  19  ? 0.3446 0.5716 0.5005 0.0789  -0.1965 -0.1497 19  GLY D CA  
12730 C C   . GLY D  19  ? 0.3449 0.5992 0.5202 0.0690  -0.1977 -0.1527 19  GLY D C   
12731 O O   . GLY D  19  ? 0.3330 0.5913 0.5095 0.0627  -0.2048 -0.1514 19  GLY D O   
12732 N N   . ILE D  20  ? 0.3982 0.6720 0.5883 0.0666  -0.1908 -0.1569 20  ILE D N   
12733 C CA  . ILE D  20  ? 0.4600 0.7636 0.6707 0.0566  -0.1912 -0.1601 20  ILE D CA  
12734 C C   . ILE D  20  ? 0.5043 0.8342 0.7361 0.0637  -0.1860 -0.1669 20  ILE D C   
12735 O O   . ILE D  20  ? 0.5199 0.8452 0.7487 0.0699  -0.1787 -0.1691 20  ILE D O   
12736 C CB  . ILE D  20  ? 0.3859 0.6884 0.5915 0.0399  -0.1877 -0.1577 20  ILE D CB  
12737 C CG1 . ILE D  20  ? 0.4374 0.7729 0.6654 0.0280  -0.1875 -0.1609 20  ILE D CG1 
12738 C CG2 . ILE D  20  ? 0.3412 0.6333 0.5380 0.0408  -0.1785 -0.1577 20  ILE D CG2 
12739 C CD1 . ILE D  20  ? 0.4572 0.7923 0.6807 0.0104  -0.1841 -0.1589 20  ILE D CD1 
12740 N N   . ARG D  21  ? 0.4094 0.7669 0.6619 0.0634  -0.1899 -0.1706 21  ARG D N   
12741 C CA  . ARG D  21  ? 0.4210 0.8080 0.6954 0.0695  -0.1846 -0.1780 21  ARG D CA  
12742 C C   . ARG D  21  ? 0.3902 0.8018 0.6773 0.0548  -0.1764 -0.1801 21  ARG D C   
12743 O O   . ARG D  21  ? 0.3953 0.8144 0.6850 0.0393  -0.1791 -0.1770 21  ARG D O   
12744 C CB  . ARG D  21  ? 0.6683 1.0754 0.9599 0.0765  -0.1924 -0.1813 21  ARG D CB  
12745 C CG  . ARG D  21  ? 0.7305 1.1769 1.0488 0.0770  -0.1873 -0.1889 21  ARG D CG  
12746 C CD  . ARG D  21  ? 0.8114 1.2839 1.1479 0.0706  -0.1946 -0.1894 21  ARG D CD  
12747 N NE  . ARG D  21  ? 0.8991 1.4079 1.2611 0.0774  -0.1915 -0.1975 21  ARG D NE  
12748 C CZ  . ARG D  21  ? 0.9763 1.4885 1.3449 0.0952  -0.1961 -0.2024 21  ARG D CZ  
12749 N NH1 . ARG D  21  ? 0.9947 1.4756 1.3459 0.1069  -0.2040 -0.1992 21  ARG D NH1 
12750 N NH2 . ARG D  21  ? 1.0044 1.5510 1.3963 0.1013  -0.1928 -0.2104 21  ARG D NH2 
12751 N N   . LEU D  22  ? 0.3536 0.7767 0.6470 0.0589  -0.1667 -0.1852 22  LEU D N   
12752 C CA  . LEU D  22  ? 0.3562 0.7981 0.6567 0.0447  -0.1574 -0.1866 22  LEU D CA  
12753 C C   . LEU D  22  ? 0.3623 0.8399 0.6851 0.0493  -0.1497 -0.1952 22  LEU D C   
12754 O O   . LEU D  22  ? 0.3317 0.8121 0.6599 0.0661  -0.1507 -0.2005 22  LEU D O   
12755 C CB  . LEU D  22  ? 0.4474 0.8645 0.7281 0.0428  -0.1513 -0.1838 22  LEU D CB  
12756 C CG  . LEU D  22  ? 0.4720 0.8583 0.7306 0.0334  -0.1557 -0.1757 22  LEU D CG  
12757 C CD1 . LEU D  22  ? 0.4440 0.8101 0.6860 0.0343  -0.1491 -0.1742 22  LEU D CD1 
12758 C CD2 . LEU D  22  ? 0.5095 0.9071 0.7727 0.0134  -0.1581 -0.1728 22  LEU D CD2 
12759 N N   . LYS D  23  ? 0.4306 0.9344 0.7649 0.0343  -0.1421 -0.1967 23  LYS D N   
12760 C CA  . LYS D  23  ? 0.4979 1.0382 0.8528 0.0376  -0.1333 -0.2052 23  LYS D CA  
12761 C C   . LYS D  23  ? 0.5291 1.0723 0.8789 0.0361  -0.1210 -0.2084 23  LYS D C   
12762 O O   . LYS D  23  ? 0.5269 1.0742 0.8728 0.0190  -0.1150 -0.2054 23  LYS D O   
12763 C CB  . LYS D  23  ? 0.7124 1.2891 1.0882 0.0226  -0.1325 -0.2060 23  LYS D CB  
12764 C CG  . LYS D  23  ? 0.7959 1.3788 1.1822 0.0265  -0.1441 -0.2052 23  LYS D CG  
12765 C CD  . LYS D  23  ? 0.8546 1.4300 1.2422 0.0503  -0.1492 -0.2099 23  LYS D CD  
12766 C CE  . LYS D  23  ? 0.8999 1.4707 1.2906 0.0538  -0.1628 -0.2068 23  LYS D CE  
12767 N NZ  . LYS D  23  ? 0.8977 1.4372 1.2686 0.0434  -0.1706 -0.1975 23  LYS D NZ  
12768 N N   . ALA D  24  ? 0.7165 1.2561 1.0653 0.0537  -0.1180 -0.2146 24  ALA D N   
12769 C CA  . ALA D  24  ? 0.7429 1.2958 1.0929 0.0545  -0.1060 -0.2205 24  ALA D CA  
12770 C C   . ALA D  24  ? 0.7839 1.3811 1.1582 0.0518  -0.1001 -0.2276 24  ALA D C   
12771 O O   . ALA D  24  ? 0.7994 1.4102 1.1876 0.0562  -0.1068 -0.2290 24  ALA D O   
12772 C CB  . ALA D  24  ? 0.5879 1.1203 0.9283 0.0747  -0.1067 -0.2250 24  ALA D CB  
12773 N N   . PRO D  25  ? 0.7395 1.3602 1.1187 0.0441  -0.0874 -0.2319 25  PRO D N   
12774 C CA  . PRO D  25  ? 0.7130 1.3777 1.1149 0.0410  -0.0809 -0.2387 25  PRO D CA  
12775 C C   . PRO D  25  ? 0.6695 1.3428 1.0827 0.0632  -0.0850 -0.2473 25  PRO D C   
12776 O O   . PRO D  25  ? 0.6969 1.4015 1.1302 0.0637  -0.0857 -0.2515 25  PRO D O   
12777 C CB  . PRO D  25  ? 0.8177 1.4986 1.2168 0.0324  -0.0662 -0.2422 25  PRO D CB  
12778 C CG  . PRO D  25  ? 0.8336 1.4832 1.2111 0.0217  -0.0663 -0.2341 25  PRO D CG  
12779 C CD  . PRO D  25  ? 0.8228 1.4331 1.1872 0.0363  -0.0785 -0.2305 25  PRO D CD  
12780 N N   . GLY D  26  ? 0.5521 1.1966 0.9520 0.0810  -0.0886 -0.2497 26  GLY D N   
12781 C CA  . GLY D  26  ? 0.5407 1.1880 0.9479 0.1025  -0.0934 -0.2578 26  GLY D CA  
12782 C C   . GLY D  26  ? 0.5312 1.1507 0.9325 0.1151  -0.1081 -0.2542 26  GLY D C   
12783 O O   . GLY D  26  ? 0.5156 1.1254 0.9158 0.1338  -0.1132 -0.2598 26  GLY D O   
12784 N N   . GLY D  27  ? 0.6021 1.2073 0.9983 0.1049  -0.1154 -0.2449 27  GLY D N   
12785 C CA  . GLY D  27  ? 0.6241 1.2039 1.0136 0.1155  -0.1290 -0.2411 27  GLY D CA  
12786 C C   . GLY D  27  ? 0.6305 1.1830 1.0049 0.1044  -0.1356 -0.2300 27  GLY D C   
12787 O O   . GLY D  27  ? 0.6405 1.1907 1.0084 0.0884  -0.1303 -0.2251 27  GLY D O   
12788 N N   . PRO D  28  ? 0.5992 1.1313 0.9675 0.1125  -0.1477 -0.2263 28  PRO D N   
12789 C CA  . PRO D  28  ? 0.5999 1.1005 0.9499 0.1056  -0.1549 -0.2163 28  PRO D CA  
12790 C C   . PRO D  28  ? 0.6057 1.0672 0.9311 0.1127  -0.1546 -0.2132 28  PRO D C   
12791 O O   . PRO D  28  ? 0.6190 1.0735 0.9416 0.1268  -0.1534 -0.2186 28  PRO D O   
12792 C CB  . PRO D  28  ? 0.6256 1.1253 0.9809 0.1134  -0.1673 -0.2153 28  PRO D CB  
12793 C CG  . PRO D  28  ? 0.6410 1.1513 1.0064 0.1318  -0.1682 -0.2241 28  PRO D CG  
12794 C CD  . PRO D  28  ? 0.6259 1.1637 1.0037 0.1299  -0.1555 -0.2318 28  PRO D CD  
12795 N N   . VAL D  29  ? 0.6074 1.0442 0.9152 0.1027  -0.1559 -0.2049 29  VAL D N   
12796 C CA  . VAL D  29  ? 0.5509 0.9513 0.8352 0.1079  -0.1558 -0.2009 29  VAL D CA  
12797 C C   . VAL D  29  ? 0.5258 0.8978 0.7921 0.1028  -0.1633 -0.1917 29  VAL D C   
12798 O O   . VAL D  29  ? 0.5523 0.9299 0.8202 0.0898  -0.1651 -0.1875 29  VAL D O   
12799 C CB  . VAL D  29  ? 0.3885 0.7883 0.6667 0.1004  -0.1451 -0.2014 29  VAL D CB  
12800 C CG1 . VAL D  29  ? 0.2818 0.7104 0.5759 0.1044  -0.1365 -0.2108 29  VAL D CG1 
12801 C CG2 . VAL D  29  ? 0.2756 0.6789 0.5514 0.0817  -0.1428 -0.1956 29  VAL D CG2 
12802 N N   . SER D  30  ? 0.4912 0.8324 0.7395 0.1124  -0.1676 -0.1886 30  SER D N   
12803 C CA  . SER D  30  ? 0.5026 0.8165 0.7317 0.1078  -0.1730 -0.1801 30  SER D CA  
12804 C C   . SER D  30  ? 0.4832 0.7808 0.6968 0.0994  -0.1663 -0.1758 30  SER D C   
12805 O O   . SER D  30  ? 0.5067 0.7972 0.7150 0.1039  -0.1605 -0.1779 30  SER D O   
12806 C CB  . SER D  30  ? 0.5250 0.8138 0.7407 0.1204  -0.1807 -0.1779 30  SER D CB  
12807 O OG  . SER D  30  ? 0.5339 0.8342 0.7612 0.1278  -0.1890 -0.1806 30  SER D OG  
12808 N N   . ALA D  31  ? 0.3715 0.6625 0.5774 0.0873  -0.1675 -0.1702 31  ALA D N   
12809 C CA  . ALA D  31  ? 0.3370 0.6085 0.5256 0.0806  -0.1627 -0.1656 31  ALA D CA  
12810 C C   . ALA D  31  ? 0.3571 0.6024 0.5264 0.0790  -0.1685 -0.1585 31  ALA D C   
12811 O O   . ALA D  31  ? 0.3935 0.6413 0.5644 0.0747  -0.1751 -0.1566 31  ALA D O   
12812 C CB  . ALA D  31  ? 0.2733 0.5610 0.4689 0.0665  -0.1573 -0.1662 31  ALA D CB  
12813 N N   . PHE D  32  ? 0.3799 0.6011 0.5309 0.0824  -0.1659 -0.1548 32  PHE D N   
12814 C CA  . PHE D  32  ? 0.3919 0.5892 0.5234 0.0806  -0.1693 -0.1485 32  PHE D CA  
12815 C C   . PHE D  32  ? 0.4189 0.6052 0.5383 0.0734  -0.1632 -0.1455 32  PHE D C   
12816 O O   . PHE D  32  ? 0.4148 0.5926 0.5275 0.0772  -0.1577 -0.1452 32  PHE D O   
12817 C CB  . PHE D  32  ? 0.3962 0.5760 0.5168 0.0918  -0.1723 -0.1466 32  PHE D CB  
12818 C CG  . PHE D  32  ? 0.4505 0.6398 0.5823 0.0997  -0.1792 -0.1497 32  PHE D CG  
12819 C CD1 . PHE D  32  ? 0.5009 0.7040 0.6468 0.1072  -0.1778 -0.1557 32  PHE D CD1 
12820 C CD2 . PHE D  32  ? 0.4771 0.6624 0.6055 0.0997  -0.1873 -0.1472 32  PHE D CD2 
12821 C CE1 . PHE D  32  ? 0.5398 0.7520 0.6962 0.1153  -0.1847 -0.1590 32  PHE D CE1 
12822 C CE2 . PHE D  32  ? 0.5193 0.7138 0.6581 0.1072  -0.1944 -0.1500 32  PHE D CE2 
12823 C CZ  . PHE D  32  ? 0.5417 0.7496 0.6948 0.1153  -0.1932 -0.1559 32  PHE D CZ  
12824 N N   . LEU D  33  ? 0.3951 0.5804 0.5108 0.0628  -0.1648 -0.1435 33  LEU D N   
12825 C CA  . LEU D  33  ? 0.3552 0.5345 0.4630 0.0546  -0.1597 -0.1419 33  LEU D CA  
12826 C C   . LEU D  33  ? 0.3765 0.5319 0.4636 0.0524  -0.1615 -0.1368 33  LEU D C   
12827 O O   . LEU D  33  ? 0.3758 0.5268 0.4587 0.0493  -0.1677 -0.1356 33  LEU D O   
12828 C CB  . LEU D  33  ? 0.2790 0.4782 0.4001 0.0423  -0.1598 -0.1445 33  LEU D CB  
12829 C CG  . LEU D  33  ? 0.2746 0.5033 0.4190 0.0431  -0.1577 -0.1504 33  LEU D CG  
12830 C CD1 . LEU D  33  ? 0.2760 0.5234 0.4310 0.0285  -0.1565 -0.1521 33  LEU D CD1 
12831 C CD2 . LEU D  33  ? 0.2646 0.4963 0.4119 0.0520  -0.1508 -0.1534 33  LEU D CD2 
12832 N N   . GLY D  34  ? 0.4231 0.5639 0.4972 0.0545  -0.1560 -0.1344 34  GLY D N   
12833 C CA  . GLY D  34  ? 0.3777 0.4978 0.4328 0.0534  -0.1566 -0.1304 34  GLY D CA  
12834 C C   . GLY D  34  ? 0.3358 0.4441 0.3813 0.0616  -0.1591 -0.1280 34  GLY D C   
12835 O O   . GLY D  34  ? 0.3077 0.4045 0.3417 0.0606  -0.1626 -0.1261 34  GLY D O   
12836 N N   . ILE D  35  ? 0.2850 0.3959 0.3346 0.0695  -0.1577 -0.1284 35  ILE D N   
12837 C CA  . ILE D  35  ? 0.2898 0.3883 0.3283 0.0765  -0.1592 -0.1255 35  ILE D CA  
12838 C C   . ILE D  35  ? 0.2924 0.3774 0.3161 0.0768  -0.1537 -0.1222 35  ILE D C   
12839 O O   . ILE D  35  ? 0.2774 0.3640 0.3026 0.0766  -0.1479 -0.1225 35  ILE D O   
12840 C CB  . ILE D  35  ? 0.3429 0.4458 0.3885 0.0840  -0.1592 -0.1268 35  ILE D CB  
12841 C CG1 . ILE D  35  ? 0.3547 0.4734 0.4170 0.0852  -0.1645 -0.1309 35  ILE D CG1 
12842 C CG2 . ILE D  35  ? 0.3377 0.4262 0.3697 0.0898  -0.1610 -0.1231 35  ILE D CG2 
12843 C CD1 . ILE D  35  ? 0.3526 0.4774 0.4240 0.0929  -0.1642 -0.1340 35  ILE D CD1 
12844 N N   . PRO D  36  ? 0.2951 0.3681 0.3047 0.0771  -0.1555 -0.1196 36  PRO D N   
12845 C CA  . PRO D  36  ? 0.2933 0.3557 0.2895 0.0781  -0.1503 -0.1170 36  PRO D CA  
12846 C C   . PRO D  36  ? 0.2886 0.3486 0.2812 0.0832  -0.1469 -0.1147 36  PRO D C   
12847 O O   . PRO D  36  ? 0.3085 0.3662 0.2984 0.0866  -0.1507 -0.1134 36  PRO D O   
12848 C CB  . PRO D  36  ? 0.3060 0.3592 0.2898 0.0782  -0.1543 -0.1160 36  PRO D CB  
12849 C CG  . PRO D  36  ? 0.3136 0.3705 0.3019 0.0796  -0.1611 -0.1164 36  PRO D CG  
12850 C CD  . PRO D  36  ? 0.3076 0.3778 0.3133 0.0776  -0.1625 -0.1193 36  PRO D CD  
12851 N N   . PHE D  37  ? 0.2795 0.3395 0.2712 0.0833  -0.1406 -0.1140 37  PHE D N   
12852 C CA  . PHE D  37  ? 0.2773 0.3344 0.2642 0.0869  -0.1382 -0.1115 37  PHE D CA  
12853 C C   . PHE D  37  ? 0.3044 0.3551 0.2779 0.0874  -0.1344 -0.1083 37  PHE D C   
12854 O O   . PHE D  37  ? 0.3055 0.3545 0.2739 0.0890  -0.1329 -0.1058 37  PHE D O   
12855 C CB  . PHE D  37  ? 0.2677 0.3311 0.2641 0.0876  -0.1350 -0.1132 37  PHE D CB  
12856 C CG  . PHE D  37  ? 0.2589 0.3246 0.2562 0.0847  -0.1291 -0.1136 37  PHE D CG  
12857 C CD1 . PHE D  37  ? 0.2558 0.3276 0.2610 0.0808  -0.1288 -0.1164 37  PHE D CD1 
12858 C CD2 . PHE D  37  ? 0.2550 0.3173 0.2449 0.0853  -0.1243 -0.1110 37  PHE D CD2 
12859 C CE1 . PHE D  37  ? 0.2893 0.3619 0.2936 0.0780  -0.1241 -0.1164 37  PHE D CE1 
12860 C CE2 . PHE D  37  ? 0.2482 0.3123 0.2386 0.0831  -0.1194 -0.1113 37  PHE D CE2 
12861 C CZ  . PHE D  37  ? 0.2878 0.3561 0.2847 0.0796  -0.1195 -0.1138 37  PHE D CZ  
12862 N N   . ALA D  38  ? 0.4062 0.4537 0.3739 0.0861  -0.1335 -0.1088 38  ALA D N   
12863 C CA  . ALA D  38  ? 0.3805 0.4243 0.3367 0.0875  -0.1299 -0.1071 38  ALA D CA  
12864 C C   . ALA D  38  ? 0.4328 0.4711 0.3816 0.0877  -0.1324 -0.1087 38  ALA D C   
12865 O O   . ALA D  38  ? 0.4578 0.4947 0.4110 0.0852  -0.1354 -0.1109 38  ALA D O   
12866 C CB  . ALA D  38  ? 0.2738 0.3203 0.2324 0.0871  -0.1240 -0.1070 38  ALA D CB  
12867 N N   . GLU D  39  ? 0.4760 0.5115 0.4131 0.0904  -0.1315 -0.1078 39  GLU D N   
12868 C CA  . GLU D  39  ? 0.4722 0.5018 0.4011 0.0919  -0.1334 -0.1102 39  GLU D CA  
12869 C C   . GLU D  39  ? 0.3973 0.4247 0.3289 0.0918  -0.1312 -0.1121 39  GLU D C   
12870 O O   . GLU D  39  ? 0.3618 0.3934 0.2964 0.0924  -0.1263 -0.1110 39  GLU D O   
12871 C CB  . GLU D  39  ? 0.5167 0.5465 0.4328 0.0956  -0.1317 -0.1095 39  GLU D CB  
12872 C CG  . GLU D  39  ? 0.5683 0.5972 0.4778 0.0950  -0.1357 -0.1077 39  GLU D CG  
12873 C CD  . GLU D  39  ? 0.6639 0.6864 0.5702 0.0945  -0.1422 -0.1101 39  GLU D CD  
12874 O OE1 . GLU D  39  ? 0.7275 0.7448 0.6276 0.0964  -0.1430 -0.1133 39  GLU D OE1 
12875 O OE2 . GLU D  39  ? 0.6711 0.6935 0.5812 0.0924  -0.1471 -0.1090 39  GLU D OE2 
12876 N N   . PRO D  40  ? 0.3164 0.3366 0.2461 0.0903  -0.1355 -0.1147 40  PRO D N   
12877 C CA  . PRO D  40  ? 0.3165 0.3319 0.2470 0.0891  -0.1352 -0.1162 40  PRO D CA  
12878 C C   . PRO D  40  ? 0.3158 0.3305 0.2401 0.0949  -0.1308 -0.1164 40  PRO D C   
12879 O O   . PRO D  40  ? 0.3251 0.3373 0.2400 0.1002  -0.1311 -0.1179 40  PRO D O   
12880 C CB  . PRO D  40  ? 0.3328 0.3377 0.2566 0.0876  -0.1417 -0.1191 40  PRO D CB  
12881 C CG  . PRO D  40  ? 0.4148 0.4231 0.3419 0.0847  -0.1456 -0.1187 40  PRO D CG  
12882 C CD  . PRO D  40  ? 0.3285 0.3441 0.2553 0.0884  -0.1420 -0.1162 40  PRO D CD  
12883 N N   . PRO D  41  ? 0.3700 0.3876 0.2994 0.0941  -0.1272 -0.1154 41  PRO D N   
12884 C CA  . PRO D  41  ? 0.3745 0.3945 0.3003 0.0997  -0.1230 -0.1154 41  PRO D CA  
12885 C C   . PRO D  41  ? 0.4327 0.4417 0.3502 0.1039  -0.1263 -0.1184 41  PRO D C   
12886 O O   . PRO D  41  ? 0.4585 0.4657 0.3760 0.1055  -0.1252 -0.1184 41  PRO D O   
12887 C CB  . PRO D  41  ? 0.2907 0.3161 0.2252 0.0959  -0.1195 -0.1134 41  PRO D CB  
12888 C CG  . PRO D  41  ? 0.2921 0.3134 0.2315 0.0891  -0.1233 -0.1138 41  PRO D CG  
12889 C CD  . PRO D  41  ? 0.2982 0.3183 0.2373 0.0876  -0.1273 -0.1145 41  PRO D CD  
12890 N N   . VAL D  42  ? 0.3319 0.3326 0.2413 0.1061  -0.1309 -0.1210 42  VAL D N   
12891 C CA  . VAL D  42  ? 0.4054 0.3920 0.3054 0.1100  -0.1357 -0.1243 42  VAL D CA  
12892 C C   . VAL D  42  ? 0.3881 0.3762 0.2798 0.1208  -0.1345 -0.1273 42  VAL D C   
12893 O O   . VAL D  42  ? 0.3592 0.3603 0.2522 0.1236  -0.1299 -0.1266 42  VAL D O   
12894 C CB  . VAL D  42  ? 0.3628 0.3377 0.2585 0.1050  -0.1426 -0.1259 42  VAL D CB  
12895 C CG1 . VAL D  42  ? 0.3535 0.3325 0.2594 0.0946  -0.1433 -0.1235 42  VAL D CG1 
12896 C CG2 . VAL D  42  ? 0.4766 0.4536 0.3671 0.1080  -0.1436 -0.1274 42  VAL D CG2 
12897 N N   . GLY D  43  ? 0.4169 0.3919 0.2993 0.1269  -0.1392 -0.1308 43  GLY D N   
12898 C CA  . GLY D  43  ? 0.4670 0.4433 0.3409 0.1382  -0.1393 -0.1349 43  GLY D CA  
12899 C C   . GLY D  43  ? 0.4997 0.4926 0.3779 0.1450  -0.1332 -0.1347 43  GLY D C   
12900 O O   . GLY D  43  ? 0.5334 0.5268 0.4154 0.1463  -0.1323 -0.1338 43  GLY D O   
12901 N N   . SER D  44  ? 0.5287 0.5357 0.4058 0.1484  -0.1291 -0.1356 44  SER D N   
12902 C CA  . SER D  44  ? 0.5043 0.5305 0.3854 0.1536  -0.1229 -0.1356 44  SER D CA  
12903 C C   . SER D  44  ? 0.4283 0.4656 0.3198 0.1444  -0.1174 -0.1301 44  SER D C   
12904 O O   . SER D  44  ? 0.4158 0.4700 0.3109 0.1456  -0.1120 -0.1293 44  SER D O   
12905 C CB  . SER D  44  ? 0.6042 0.6416 0.4783 0.1594  -0.1208 -0.1386 44  SER D CB  
12906 O OG  . SER D  44  ? 0.6237 0.6620 0.4963 0.1513  -0.1199 -0.1359 44  SER D OG  
12907 N N   . ARG D  45  ? 0.3387 0.3674 0.2345 0.1350  -0.1191 -0.1268 45  ARG D N   
12908 C CA  . ARG D  45  ? 0.3465 0.3829 0.2520 0.1269  -0.1151 -0.1221 45  ARG D CA  
12909 C C   . ARG D  45  ? 0.3425 0.3749 0.2541 0.1244  -0.1150 -0.1207 45  ARG D C   
12910 O O   . ARG D  45  ? 0.3530 0.3912 0.2723 0.1182  -0.1119 -0.1174 45  ARG D O   
12911 C CB  . ARG D  45  ? 0.5792 0.6116 0.4866 0.1189  -0.1169 -0.1196 45  ARG D CB  
12912 C CG  . ARG D  45  ? 0.7103 0.7467 0.6110 0.1196  -0.1170 -0.1198 45  ARG D CG  
12913 C CD  . ARG D  45  ? 0.8570 0.9089 0.7562 0.1218  -0.1115 -0.1187 45  ARG D CD  
12914 N NE  . ARG D  45  ? 0.9555 1.0149 0.8628 0.1160  -0.1078 -0.1146 45  ARG D NE  
12915 C CZ  . ARG D  45  ? 0.9860 1.0587 0.8929 0.1153  -0.1033 -0.1128 45  ARG D CZ  
12916 N NH1 . ARG D  45  ? 0.9893 1.0719 0.8887 0.1200  -0.1013 -0.1149 45  ARG D NH1 
12917 N NH2 . ARG D  45  ? 0.9712 1.0481 0.8849 0.1096  -0.1010 -0.1092 45  ARG D NH2 
12918 N N   . ARG D  46  ? 0.3222 0.3436 0.2292 0.1290  -0.1191 -0.1233 46  ARG D N   
12919 C CA  . ARG D  46  ? 0.3239 0.3401 0.2343 0.1259  -0.1197 -0.1217 46  ARG D CA  
12920 C C   . ARG D  46  ? 0.3083 0.3385 0.2240 0.1284  -0.1143 -0.1206 46  ARG D C   
12921 O O   . ARG D  46  ? 0.3096 0.3487 0.2230 0.1368  -0.1128 -0.1231 46  ARG D O   
12922 C CB  . ARG D  46  ? 0.3362 0.3347 0.2375 0.1304  -0.1264 -0.1245 46  ARG D CB  
12923 C CG  . ARG D  46  ? 0.3357 0.3272 0.2376 0.1271  -0.1278 -0.1228 46  ARG D CG  
12924 C CD  . ARG D  46  ? 0.3577 0.3298 0.2477 0.1332  -0.1354 -0.1256 46  ARG D CD  
12925 N NE  . ARG D  46  ? 0.3709 0.3252 0.2549 0.1255  -0.1415 -0.1255 46  ARG D NE  
12926 C CZ  . ARG D  46  ? 0.3947 0.3283 0.2659 0.1295  -0.1494 -0.1282 46  ARG D CZ  
12927 N NH1 . ARG D  46  ? 0.4075 0.3360 0.2712 0.1427  -0.1523 -0.1315 46  ARG D NH1 
12928 N NH2 . ARG D  46  ? 0.4072 0.3254 0.2731 0.1205  -0.1549 -0.1278 46  ARG D NH2 
12929 N N   . PHE D  47  ? 0.3485 0.3818 0.2713 0.1209  -0.1117 -0.1172 47  PHE D N   
12930 C CA  . PHE D  47  ? 0.3541 0.4001 0.2823 0.1210  -0.1068 -0.1156 47  PHE D CA  
12931 C C   . PHE D  47  ? 0.3766 0.4379 0.3092 0.1188  -0.1016 -0.1140 47  PHE D C   
12932 O O   . PHE D  47  ? 0.3616 0.4343 0.2983 0.1179  -0.0977 -0.1127 47  PHE D O   
12933 C CB  . PHE D  47  ? 0.2899 0.3382 0.2144 0.1307  -0.1077 -0.1185 47  PHE D CB  
12934 C CG  . PHE D  47  ? 0.3119 0.3425 0.2285 0.1350  -0.1144 -0.1206 47  PHE D CG  
12935 C CD1 . PHE D  47  ? 0.3335 0.3530 0.2492 0.1285  -0.1167 -0.1182 47  PHE D CD1 
12936 C CD2 . PHE D  47  ? 0.3214 0.3462 0.2301 0.1459  -0.1187 -0.1250 47  PHE D CD2 
12937 C CE1 . PHE D  47  ? 0.3637 0.3646 0.2696 0.1316  -0.1237 -0.1197 47  PHE D CE1 
12938 C CE2 . PHE D  47  ? 0.3393 0.3447 0.2387 0.1503  -0.1261 -0.1269 47  PHE D CE2 
12939 C CZ  . PHE D  47  ? 0.3737 0.3661 0.2710 0.1427  -0.1288 -0.1240 47  PHE D CZ  
12940 N N   . MET D  48  ? 0.3288 0.3899 0.2590 0.1180  -0.1022 -0.1141 48  MET D N   
12941 C CA  . MET D  48  ? 0.2702 0.3431 0.2015 0.1152  -0.0986 -0.1122 48  MET D CA  
12942 C C   . MET D  48  ? 0.3473 0.4179 0.2839 0.1066  -0.0982 -0.1086 48  MET D C   
12943 O O   . MET D  48  ? 0.2618 0.3230 0.2010 0.1035  -0.1010 -0.1085 48  MET D O   
12944 C CB  . MET D  48  ? 0.3590 0.4325 0.2828 0.1190  -0.1000 -0.1141 48  MET D CB  
12945 C CG  . MET D  48  ? 0.3670 0.4460 0.2853 0.1290  -0.1001 -0.1186 48  MET D CG  
12946 S SD  . MET D  48  ? 0.7300 0.8327 0.6501 0.1311  -0.0943 -0.1187 48  MET D SD  
12947 C CE  . MET D  48  ? 1.4155 1.5235 1.3330 0.1216  -0.0921 -0.1141 48  MET D CE  
12948 N N   . PRO D  49  ? 0.3802 0.4599 0.3180 0.1029  -0.0954 -0.1061 49  PRO D N   
12949 C CA  . PRO D  49  ? 0.3497 0.4267 0.2912 0.0965  -0.0961 -0.1033 49  PRO D CA  
12950 C C   . PRO D  49  ? 0.3497 0.4191 0.2884 0.0962  -0.1001 -0.1036 49  PRO D C   
12951 O O   . PRO D  49  ? 0.3577 0.4262 0.2893 0.0999  -0.1014 -0.1052 49  PRO D O   
12952 C CB  . PRO D  49  ? 0.2504 0.3373 0.1895 0.0936  -0.0936 -0.1008 49  PRO D CB  
12953 C CG  . PRO D  49  ? 0.2494 0.3468 0.1879 0.0972  -0.0904 -0.1023 49  PRO D CG  
12954 C CD  . PRO D  49  ? 0.2561 0.3497 0.1916 0.1045  -0.0919 -0.1059 49  PRO D CD  
12955 N N   . PRO D  50  ? 0.3619 0.4265 0.3059 0.0924  -0.1024 -0.1027 50  PRO D N   
12956 C CA  . PRO D  50  ? 0.4178 0.4761 0.3601 0.0923  -0.1070 -0.1033 50  PRO D CA  
12957 C C   . PRO D  50  ? 0.4655 0.5252 0.4008 0.0917  -0.1084 -0.1011 50  PRO D C   
12958 O O   . PRO D  50  ? 0.4957 0.5591 0.4306 0.0892  -0.1073 -0.0985 50  PRO D O   
12959 C CB  . PRO D  50  ? 0.2569 0.3131 0.2087 0.0891  -0.1087 -0.1035 50  PRO D CB  
12960 C CG  . PRO D  50  ? 0.2483 0.3095 0.2044 0.0873  -0.1052 -0.1022 50  PRO D CG  
12961 C CD  . PRO D  50  ? 0.3541 0.4197 0.3063 0.0889  -0.1012 -0.1019 50  PRO D CD  
12962 N N   . GLU D  51  ? 0.4484 0.5044 0.3766 0.0937  -0.1114 -0.1020 51  GLU D N   
12963 C CA  . GLU D  51  ? 0.4967 0.5519 0.4174 0.0923  -0.1144 -0.0997 51  GLU D CA  
12964 C C   . GLU D  51  ? 0.4448 0.4936 0.3715 0.0911  -0.1196 -0.0999 51  GLU D C   
12965 O O   . GLU D  51  ? 0.4633 0.5091 0.3960 0.0916  -0.1210 -0.1026 51  GLU D O   
12966 C CB  . GLU D  51  ? 0.8341 0.8892 0.7433 0.0953  -0.1151 -0.1010 51  GLU D CB  
12967 C CG  . GLU D  51  ? 0.9228 0.9854 0.8280 0.0990  -0.1103 -0.1031 51  GLU D CG  
12968 C CD  . GLU D  51  ? 1.0135 1.0732 0.9101 0.1041  -0.1119 -0.1068 51  GLU D CD  
12969 O OE1 . GLU D  51  ? 1.0095 1.0617 0.9088 0.1070  -0.1141 -0.1101 51  GLU D OE1 
12970 O OE2 . GLU D  51  ? 1.0646 1.1290 0.9504 0.1048  -0.1114 -0.1065 51  GLU D OE2 
12971 N N   . PRO D  52  ? 0.4493 0.4964 0.3741 0.0895  -0.1231 -0.0972 52  PRO D N   
12972 C CA  . PRO D  52  ? 0.4468 0.4897 0.3787 0.0895  -0.1286 -0.0979 52  PRO D CA  
12973 C C   . PRO D  52  ? 0.4440 0.4826 0.3714 0.0905  -0.1338 -0.0991 52  PRO D C   
12974 O O   . PRO D  52  ? 0.4472 0.4845 0.3628 0.0911  -0.1340 -0.0984 52  PRO D O   
12975 C CB  . PRO D  52  ? 0.3591 0.4003 0.2880 0.0886  -0.1314 -0.0945 52  PRO D CB  
12976 C CG  . PRO D  52  ? 0.3079 0.3506 0.2226 0.0869  -0.1295 -0.0912 52  PRO D CG  
12977 C CD  . PRO D  52  ? 0.3608 0.4099 0.2763 0.0874  -0.1228 -0.0933 52  PRO D CD  
12978 N N   . LYS D  53  ? 0.3681 0.4058 0.3050 0.0905  -0.1381 -0.1012 53  LYS D N   
12979 C CA  . LYS D  53  ? 0.3688 0.4032 0.3035 0.0907  -0.1436 -0.1028 53  LYS D CA  
12980 C C   . LYS D  53  ? 0.3889 0.4191 0.3120 0.0915  -0.1486 -0.1001 53  LYS D C   
12981 O O   . LYS D  53  ? 0.3592 0.3881 0.2826 0.0921  -0.1523 -0.0977 53  LYS D O   
12982 C CB  . LYS D  53  ? 0.3129 0.3503 0.2617 0.0898  -0.1474 -0.1055 53  LYS D CB  
12983 C CG  . LYS D  53  ? 0.3235 0.3590 0.2716 0.0888  -0.1537 -0.1074 53  LYS D CG  
12984 C CD  . LYS D  53  ? 0.3480 0.3816 0.2949 0.0865  -0.1524 -0.1101 53  LYS D CD  
12985 C CE  . LYS D  53  ? 0.3622 0.3914 0.3033 0.0854  -0.1589 -0.1117 53  LYS D CE  
12986 N NZ  . LYS D  53  ? 0.3507 0.3733 0.2752 0.0878  -0.1592 -0.1109 53  LYS D NZ  
12987 N N   . ARG D  54  ? 0.4045 0.4318 0.3165 0.0917  -0.1494 -0.1009 54  ARG D N   
12988 C CA  . ARG D  54  ? 0.4032 0.4267 0.3026 0.0920  -0.1545 -0.0987 54  ARG D CA  
12989 C C   . ARG D  54  ? 0.3626 0.3845 0.2696 0.0920  -0.1620 -0.0998 54  ARG D C   
12990 O O   . ARG D  54  ? 0.3569 0.3809 0.2748 0.0913  -0.1628 -0.1032 54  ARG D O   
12991 C CB  . ARG D  54  ? 0.5201 0.5415 0.4067 0.0928  -0.1533 -0.1008 54  ARG D CB  
12992 C CG  . ARG D  54  ? 0.6121 0.6375 0.4905 0.0937  -0.1459 -0.1004 54  ARG D CG  
12993 C CD  . ARG D  54  ? 0.6317 0.6555 0.4991 0.0963  -0.1449 -0.1041 54  ARG D CD  
12994 N NE  . ARG D  54  ? 0.6690 0.6883 0.5436 0.0975  -0.1465 -0.1086 54  ARG D NE  
12995 C CZ  . ARG D  54  ? 0.6981 0.7113 0.5708 0.0969  -0.1528 -0.1110 54  ARG D CZ  
12996 N NH1 . ARG D  54  ? 0.7425 0.7536 0.6065 0.0960  -0.1579 -0.1094 54  ARG D NH1 
12997 N NH2 . ARG D  54  ? 0.6675 0.6762 0.5459 0.0967  -0.1545 -0.1146 54  ARG D NH2 
12998 N N   . PRO D  55  ? 0.4434 0.4622 0.3446 0.0927  -0.1680 -0.0967 55  PRO D N   
12999 C CA  . PRO D  55  ? 0.4223 0.4410 0.3322 0.0938  -0.1759 -0.0976 55  PRO D CA  
13000 C C   . PRO D  55  ? 0.4207 0.4393 0.3304 0.0926  -0.1800 -0.1010 55  PRO D C   
13001 O O   . PRO D  55  ? 0.4182 0.4336 0.3160 0.0917  -0.1780 -0.1018 55  PRO D O   
13002 C CB  . PRO D  55  ? 0.4031 0.4160 0.3016 0.0951  -0.1816 -0.0928 55  PRO D CB  
13003 C CG  . PRO D  55  ? 0.4171 0.4274 0.2970 0.0931  -0.1777 -0.0901 55  PRO D CG  
13004 C CD  . PRO D  55  ? 0.3866 0.4017 0.2707 0.0922  -0.1684 -0.0921 55  PRO D CD  
13005 N N   . TRP D  56  ? 0.3876 0.4102 0.3098 0.0926  -0.1859 -0.1032 56  TRP D N   
13006 C CA  . TRP D  56  ? 0.4515 0.4750 0.3751 0.0900  -0.1903 -0.1066 56  TRP D CA  
13007 C C   . TRP D  56  ? 0.4540 0.4782 0.3782 0.0907  -0.2002 -0.1065 56  TRP D C   
13008 O O   . TRP D  56  ? 0.4542 0.4806 0.3846 0.0937  -0.2044 -0.1048 56  TRP D O   
13009 C CB  . TRP D  56  ? 0.3975 0.4281 0.3370 0.0870  -0.1880 -0.1104 56  TRP D CB  
13010 C CG  . TRP D  56  ? 0.3733 0.4132 0.3303 0.0881  -0.1895 -0.1111 56  TRP D CG  
13011 C CD1 . TRP D  56  ? 0.3782 0.4258 0.3464 0.0880  -0.1968 -0.1128 56  TRP D CD1 
13012 C CD2 . TRP D  56  ? 0.3638 0.4075 0.3294 0.0900  -0.1838 -0.1107 56  TRP D CD2 
13013 N NE1 . TRP D  56  ? 0.3727 0.4292 0.3563 0.0904  -0.1957 -0.1139 56  TRP D NE1 
13014 C CE2 . TRP D  56  ? 0.3565 0.4099 0.3381 0.0916  -0.1878 -0.1127 56  TRP D CE2 
13015 C CE3 . TRP D  56  ? 0.3489 0.3895 0.3101 0.0906  -0.1760 -0.1091 56  TRP D CE3 
13016 C CZ2 . TRP D  56  ? 0.4307 0.4896 0.4232 0.0941  -0.1842 -0.1137 56  TRP D CZ2 
13017 C CZ3 . TRP D  56  ? 0.3375 0.3831 0.3092 0.0923  -0.1726 -0.1096 56  TRP D CZ3 
13018 C CH2 . TRP D  56  ? 0.4330 0.4871 0.4198 0.0942  -0.1767 -0.1121 56  TRP D CH2 
13019 N N   . SER D  57  ? 0.5478 0.5695 0.4652 0.0881  -0.2044 -0.1086 57  SER D N   
13020 C CA  . SER D  57  ? 0.5621 0.5843 0.4778 0.0882  -0.2143 -0.1086 57  SER D CA  
13021 C C   . SER D  57  ? 0.5619 0.5952 0.4972 0.0861  -0.2192 -0.1118 57  SER D C   
13022 O O   . SER D  57  ? 0.5701 0.6088 0.5158 0.0823  -0.2155 -0.1147 57  SER D O   
13023 C CB  . SER D  57  ? 0.4538 0.4686 0.3526 0.0862  -0.2169 -0.1100 57  SER D CB  
13024 O OG  . SER D  57  ? 0.4521 0.4677 0.3552 0.0819  -0.2165 -0.1144 57  SER D OG  
13025 N N   . GLY D  58  ? 0.5117 0.5492 0.4517 0.0883  -0.2277 -0.1111 58  GLY D N   
13026 C CA  . GLY D  58  ? 0.5099 0.5608 0.4684 0.0862  -0.2336 -0.1143 58  GLY D CA  
13027 C C   . GLY D  58  ? 0.4935 0.5557 0.4716 0.0875  -0.2292 -0.1157 58  GLY D C   
13028 O O   . GLY D  58  ? 0.4951 0.5537 0.4726 0.0919  -0.2241 -0.1138 58  GLY D O   
13029 N N   . VAL D  59  ? 0.4203 0.4970 0.4157 0.0832  -0.2315 -0.1193 59  VAL D N   
13030 C CA  . VAL D  59  ? 0.4046 0.4943 0.4190 0.0837  -0.2271 -0.1214 59  VAL D CA  
13031 C C   . VAL D  59  ? 0.3933 0.4842 0.4095 0.0764  -0.2200 -0.1231 59  VAL D C   
13032 O O   . VAL D  59  ? 0.4063 0.4991 0.4220 0.0689  -0.2227 -0.1247 59  VAL D O   
13033 C CB  . VAL D  59  ? 0.6017 0.7105 0.6359 0.0834  -0.2342 -0.1244 59  VAL D CB  
13034 C CG1 . VAL D  59  ? 0.5889 0.7142 0.6430 0.0811  -0.2286 -0.1277 59  VAL D CG1 
13035 C CG2 . VAL D  59  ? 0.6186 0.7265 0.6535 0.0925  -0.2408 -0.1231 59  VAL D CG2 
13036 N N   . LEU D  60  ? 0.5015 0.5904 0.5190 0.0784  -0.2116 -0.1226 60  LEU D N   
13037 C CA  . LEU D  60  ? 0.4796 0.5677 0.4970 0.0722  -0.2047 -0.1236 60  LEU D CA  
13038 C C   . LEU D  60  ? 0.4677 0.5746 0.5059 0.0678  -0.2040 -0.1269 60  LEU D C   
13039 O O   . LEU D  60  ? 0.3545 0.4731 0.4066 0.0727  -0.2040 -0.1282 60  LEU D O   
13040 C CB  . LEU D  60  ? 0.3592 0.4369 0.3674 0.0764  -0.1962 -0.1214 60  LEU D CB  
13041 C CG  . LEU D  60  ? 0.3489 0.4234 0.3548 0.0724  -0.1885 -0.1217 60  LEU D CG  
13042 C CD1 . LEU D  60  ? 0.3584 0.4199 0.3481 0.0693  -0.1889 -0.1213 60  LEU D CD1 
13043 C CD2 . LEU D  60  ? 0.3388 0.4089 0.3415 0.0780  -0.1817 -0.1197 60  LEU D CD2 
13044 N N   . ASP D  61  ? 0.5255 0.6353 0.5654 0.0584  -0.2036 -0.1283 61  ASP D N   
13045 C CA  . ASP D  61  ? 0.5833 0.7129 0.6426 0.0521  -0.2034 -0.1312 61  ASP D CA  
13046 C C   . ASP D  61  ? 0.5735 0.7056 0.6375 0.0534  -0.1944 -0.1316 61  ASP D C   
13047 O O   . ASP D  61  ? 0.6080 0.7276 0.6604 0.0506  -0.1895 -0.1302 61  ASP D O   
13048 C CB  . ASP D  61  ? 0.8146 0.9445 0.8717 0.0396  -0.2069 -0.1322 61  ASP D CB  
13049 C CG  . ASP D  61  ? 0.8785 1.0297 0.9548 0.0304  -0.2064 -0.1348 61  ASP D CG  
13050 O OD1 . ASP D  61  ? 0.8851 1.0555 0.9795 0.0346  -0.2055 -0.1366 61  ASP D OD1 
13051 O OD2 . ASP D  61  ? 0.9077 1.0565 0.9804 0.0188  -0.2069 -0.1351 61  ASP D OD2 
13052 N N   . ALA D  62  ? 0.4972 0.6448 0.5774 0.0581  -0.1924 -0.1338 62  ALA D N   
13053 C CA  . ALA D  62  ? 0.4638 0.6199 0.5521 0.0553  -0.1850 -0.1356 62  ALA D CA  
13054 C C   . ALA D  62  ? 0.4200 0.6026 0.5306 0.0499  -0.1863 -0.1396 62  ALA D C   
13055 O O   . ALA D  62  ? 0.3869 0.5839 0.5117 0.0568  -0.1849 -0.1427 62  ALA D O   
13056 C CB  . ALA D  62  ? 0.5202 0.6714 0.6070 0.0656  -0.1794 -0.1354 62  ALA D CB  
13057 N N   . THR D  63  ? 0.5739 0.7631 0.6874 0.0372  -0.1885 -0.1399 63  THR D N   
13058 C CA  . THR D  63  ? 0.6418 0.8583 0.7767 0.0295  -0.1880 -0.1435 63  THR D CA  
13059 C C   . THR D  63  ? 0.7144 0.9342 0.8498 0.0190  -0.1821 -0.1440 63  THR D C   
13060 O O   . THR D  63  ? 0.7829 1.0268 0.9360 0.0114  -0.1805 -0.1470 63  THR D O   
13061 C CB  . THR D  63  ? 0.6201 0.8487 0.7631 0.0210  -0.1966 -0.1440 63  THR D CB  
13062 O OG1 . THR D  63  ? 0.6294 0.8383 0.7542 0.0118  -0.2006 -0.1411 63  THR D OG1 
13063 C CG2 . THR D  63  ? 0.6504 0.8818 0.7975 0.0319  -0.2027 -0.1444 63  THR D CG2 
13064 N N   . THR D  64  ? 0.6243 0.8209 0.7403 0.0179  -0.1790 -0.1410 64  THR D N   
13065 C CA  . THR D  64  ? 0.5688 0.7634 0.6807 0.0058  -0.1759 -0.1407 64  THR D CA  
13066 C C   . THR D  64  ? 0.5556 0.7292 0.6506 0.0114  -0.1701 -0.1384 64  THR D C   
13067 O O   . THR D  64  ? 0.6220 0.7764 0.7027 0.0200  -0.1707 -0.1359 64  THR D O   
13068 C CB  . THR D  64  ? 0.5091 0.6912 0.6093 -0.0064 -0.1828 -0.1388 64  THR D CB  
13069 O OG1 . THR D  64  ? 0.4894 0.6518 0.5745 0.0014  -0.1869 -0.1367 64  THR D OG1 
13070 C CG2 . THR D  64  ? 0.5279 0.7330 0.6452 -0.0184 -0.1884 -0.1407 64  THR D CG2 
13071 N N   . PHE D  65  ? 0.3495 0.5270 0.4456 0.0054  -0.1647 -0.1392 65  PHE D N   
13072 C CA  . PHE D  65  ? 0.3115 0.4706 0.3922 0.0102  -0.1593 -0.1370 65  PHE D CA  
13073 C C   . PHE D  65  ? 0.3173 0.4490 0.3759 0.0090  -0.1628 -0.1335 65  PHE D C   
13074 O O   . PHE D  65  ? 0.3213 0.4476 0.3750 -0.0003 -0.1689 -0.1333 65  PHE D O   
13075 C CB  . PHE D  65  ? 0.4346 0.6025 0.5190 0.0018  -0.1542 -0.1385 65  PHE D CB  
13076 C CG  . PHE D  65  ? 0.4342 0.6292 0.5390 0.0049  -0.1487 -0.1429 65  PHE D CG  
13077 C CD1 . PHE D  65  ? 0.4135 0.6084 0.5198 0.0184  -0.1437 -0.1439 65  PHE D CD1 
13078 C CD2 . PHE D  65  ? 0.4494 0.6701 0.5715 -0.0060 -0.1482 -0.1464 65  PHE D CD2 
13079 C CE1 . PHE D  65  ? 0.4064 0.6248 0.5301 0.0222  -0.1388 -0.1490 65  PHE D CE1 
13080 C CE2 . PHE D  65  ? 0.4441 0.6916 0.5852 -0.0021 -0.1420 -0.1514 65  PHE D CE2 
13081 C CZ  . PHE D  65  ? 0.4222 0.6677 0.5636 0.0127  -0.1376 -0.1531 65  PHE D CZ  
13082 N N   . GLN D  66  ? 0.4271 0.5426 0.4729 0.0187  -0.1586 -0.1312 66  GLN D N   
13083 C CA  . GLN D  66  ? 0.4168 0.5082 0.4424 0.0202  -0.1603 -0.1287 66  GLN D CA  
13084 C C   . GLN D  66  ? 0.3956 0.4759 0.4107 0.0141  -0.1582 -0.1279 66  GLN D C   
13085 O O   . GLN D  66  ? 0.4358 0.5272 0.4585 0.0068  -0.1562 -0.1291 66  GLN D O   
13086 C CB  . GLN D  66  ? 0.4009 0.4831 0.4192 0.0334  -0.1567 -0.1266 66  GLN D CB  
13087 C CG  . GLN D  66  ? 0.4168 0.4937 0.4308 0.0378  -0.1616 -0.1261 66  GLN D CG  
13088 C CD  . GLN D  66  ? 0.4488 0.5107 0.4495 0.0326  -0.1670 -0.1263 66  GLN D CD  
13089 O OE1 . GLN D  66  ? 0.4060 0.4546 0.3953 0.0302  -0.1659 -0.1258 66  GLN D OE1 
13090 N NE2 . GLN D  66  ? 0.5180 0.5812 0.5194 0.0311  -0.1733 -0.1272 66  GLN D NE2 
13091 N N   . ASN D  67  ? 0.3251 0.3841 0.3226 0.0176  -0.1588 -0.1261 67  ASN D N   
13092 C CA  . ASN D  67  ? 0.3478 0.3932 0.3332 0.0134  -0.1577 -0.1253 67  ASN D CA  
13093 C C   . ASN D  67  ? 0.3185 0.3684 0.3058 0.0177  -0.1505 -0.1242 67  ASN D C   
13094 O O   . ASN D  67  ? 0.3051 0.3598 0.2960 0.0278  -0.1455 -0.1232 67  ASN D O   
13095 C CB  . ASN D  67  ? 0.5030 0.5250 0.4700 0.0182  -0.1604 -0.1244 67  ASN D CB  
13096 C CG  . ASN D  67  ? 0.5393 0.5534 0.5014 0.0116  -0.1682 -0.1261 67  ASN D CG  
13097 O OD1 . ASN D  67  ? 0.5463 0.5726 0.5185 0.0012  -0.1720 -0.1275 67  ASN D OD1 
13098 N ND2 . ASN D  67  ? 0.5435 0.5385 0.4906 0.0176  -0.1708 -0.1263 67  ASN D ND2 
13099 N N   . VAL D  68  ? 0.3299 0.3774 0.3135 0.0090  -0.1505 -0.1244 68  VAL D N   
13100 C CA  . VAL D  68  ? 0.3463 0.3947 0.3279 0.0121  -0.1446 -0.1233 68  VAL D CA  
13101 C C   . VAL D  68  ? 0.3593 0.3886 0.3255 0.0221  -0.1432 -0.1207 68  VAL D C   
13102 O O   . VAL D  68  ? 0.3551 0.3677 0.3097 0.0230  -0.1478 -0.1205 68  VAL D O   
13103 C CB  . VAL D  68  ? 0.3246 0.3731 0.3033 -0.0011 -0.1461 -0.1242 68  VAL D CB  
13104 C CG1 . VAL D  68  ? 0.3338 0.3804 0.3072 0.0023  -0.1408 -0.1230 68  VAL D CG1 
13105 C CG2 . VAL D  68  ? 0.3199 0.3926 0.3167 -0.0110 -0.1464 -0.1274 68  VAL D CG2 
13106 N N   . CYS D  69  ? 0.3057 0.3385 0.2728 0.0298  -0.1370 -0.1193 69  CYS D N   
13107 C CA  . CYS D  69  ? 0.3144 0.3331 0.2693 0.0387  -0.1355 -0.1171 69  CYS D CA  
13108 C C   . CYS D  69  ? 0.3430 0.3446 0.2834 0.0345  -0.1391 -0.1165 69  CYS D C   
13109 O O   . CYS D  69  ? 0.3534 0.3561 0.2931 0.0246  -0.1403 -0.1169 69  CYS D O   
13110 C CB  . CYS D  69  ? 0.3936 0.4219 0.3538 0.0461  -0.1283 -0.1157 69  CYS D CB  
13111 S SG  . CYS D  69  ? 0.7978 0.8386 0.7694 0.0533  -0.1252 -0.1158 69  CYS D SG  
13112 N N   . TYR D  70  ? 0.3351 0.3206 0.2635 0.0424  -0.1411 -0.1159 70  TYR D N   
13113 C CA  . TYR D  70  ? 0.3890 0.3543 0.3018 0.0408  -0.1458 -0.1154 70  TYR D CA  
13114 C C   . TYR D  70  ? 0.3735 0.3397 0.2833 0.0393  -0.1431 -0.1136 70  TYR D C   
13115 O O   . TYR D  70  ? 0.3475 0.3226 0.2614 0.0469  -0.1373 -0.1123 70  TYR D O   
13116 C CB  . TYR D  70  ? 0.3656 0.3158 0.2678 0.0523  -0.1485 -0.1160 70  TYR D CB  
13117 C CG  . TYR D  70  ? 0.3986 0.3260 0.2869 0.0478  -0.1571 -0.1172 70  TYR D CG  
13118 C CD1 . TYR D  70  ? 0.4139 0.3382 0.3026 0.0429  -0.1614 -0.1191 70  TYR D CD1 
13119 C CD2 . TYR D  70  ? 0.4651 0.3728 0.3389 0.0472  -0.1617 -0.1162 70  TYR D CD2 
13120 C CE1 . TYR D  70  ? 0.4915 0.3933 0.3668 0.0374  -0.1698 -0.1202 70  TYR D CE1 
13121 C CE2 . TYR D  70  ? 0.5450 0.4280 0.4042 0.0423  -0.1705 -0.1169 70  TYR D CE2 
13122 C CZ  . TYR D  70  ? 0.5665 0.4468 0.4268 0.0370  -0.1744 -0.1190 70  TYR D CZ  
13123 O OH  . TYR D  70  ? 0.6339 0.4883 0.4792 0.0311  -0.1835 -0.1196 70  TYR D OH  
13124 N N   . GLN D  71  ? 0.4435 0.3997 0.3450 0.0284  -0.1476 -0.1133 71  GLN D N   
13125 C CA  . GLN D  71  ? 0.4965 0.4550 0.3948 0.0249  -0.1452 -0.1117 71  GLN D CA  
13126 C C   . GLN D  71  ? 0.5909 0.5285 0.4724 0.0145  -0.1524 -0.1104 71  GLN D C   
13127 O O   . GLN D  71  ? 0.6620 0.5863 0.5371 0.0062  -0.1589 -0.1110 71  GLN D O   
13128 C CB  . GLN D  71  ? 0.4018 0.3857 0.3164 0.0188  -0.1392 -0.1130 71  GLN D CB  
13129 C CG  . GLN D  71  ? 0.3592 0.3521 0.2823 0.0066  -0.1421 -0.1157 71  GLN D CG  
13130 C CD  . GLN D  71  ? 0.3310 0.3506 0.2715 0.0026  -0.1363 -0.1181 71  GLN D CD  
13131 O OE1 . GLN D  71  ? 0.3344 0.3612 0.2752 -0.0075 -0.1360 -0.1196 71  GLN D OE1 
13132 N NE2 . GLN D  71  ? 0.3131 0.3473 0.2679 0.0107  -0.1321 -0.1190 71  GLN D NE2 
13133 N N   . TYR D  72  ? 0.4968 0.4302 0.3698 0.0141  -0.1515 -0.1082 72  TYR D N   
13134 C CA  . TYR D  72  ? 0.5692 0.4831 0.4250 0.0018  -0.1580 -0.1058 72  TYR D CA  
13135 C C   . TYR D  72  ? 0.5732 0.4988 0.4363 -0.0162 -0.1587 -0.1075 72  TYR D C   
13136 O O   . TYR D  72  ? 0.5399 0.4936 0.4225 -0.0171 -0.1526 -0.1109 72  TYR D O   
13137 C CB  . TYR D  72  ? 0.8506 0.7628 0.6977 0.0038  -0.1560 -0.1030 72  TYR D CB  
13138 C CG  . TYR D  72  ? 0.9980 0.8915 0.8261 -0.0116 -0.1619 -0.0993 72  TYR D CG  
13139 C CD1 . TYR D  72  ? 1.0792 0.9381 0.8845 -0.0127 -0.1711 -0.0953 72  TYR D CD1 
13140 C CD2 . TYR D  72  ? 1.0505 0.9629 0.8864 -0.0256 -0.1543 -0.0973 72  TYR D CD2 
13141 C CE1 . TYR D  72  ? 1.1400 0.9801 0.9271 -0.0290 -0.1749 -0.0892 72  TYR D CE1 
13142 C CE2 . TYR D  72  ? 1.1068 1.0059 0.9284 -0.0418 -0.1545 -0.0904 72  TYR D CE2 
13143 C CZ  . TYR D  72  ? 1.1395 1.0016 0.9361 -0.0442 -0.1649 -0.0858 72  TYR D CZ  
13144 O OH  . TYR D  72  ? 1.1429 0.9899 0.9232 -0.0616 -0.1655 -0.0779 72  TYR D OH  
13145 N N   . VAL D  73  ? 0.7786 0.6831 0.6271 -0.0305 -0.1664 -0.1051 73  VAL D N   
13146 C CA  . VAL D  73  ? 0.7831 0.7025 0.6412 -0.0499 -0.1639 -0.1043 73  VAL D CA  
13147 C C   . VAL D  73  ? 0.8386 0.7472 0.6826 -0.0650 -0.1616 -0.0967 73  VAL D C   
13148 O O   . VAL D  73  ? 0.8957 0.7706 0.7159 -0.0668 -0.1697 -0.0923 73  VAL D O   
13149 C CB  . VAL D  73  ? 0.5921 0.5011 0.4493 -0.0583 -0.1721 -0.1062 73  VAL D CB  
13150 C CG1 . VAL D  73  ? 0.5695 0.5048 0.4444 -0.0764 -0.1664 -0.1057 73  VAL D CG1 
13151 C CG2 . VAL D  73  ? 0.5978 0.5141 0.4664 -0.0416 -0.1710 -0.1105 73  VAL D CG2 
13152 N N   . ASP D  74  ? 0.6906 0.6268 0.5480 -0.0756 -0.1510 -0.0952 74  ASP D N   
13153 C CA  . ASP D  74  ? 0.7215 0.6513 0.5650 -0.0866 -0.1467 -0.0881 74  ASP D CA  
13154 C C   . ASP D  74  ? 0.7786 0.6922 0.6079 -0.1094 -0.1500 -0.0814 74  ASP D C   
13155 O O   . ASP D  74  ? 0.7850 0.7173 0.6275 -0.1244 -0.1468 -0.0822 74  ASP D O   
13156 C CB  . ASP D  74  ? 0.7979 0.7618 0.6576 -0.0868 -0.1336 -0.0896 74  ASP D CB  
13157 C CG  . ASP D  74  ? 0.8692 0.8246 0.7116 -0.0958 -0.1296 -0.0825 74  ASP D CG  
13158 O OD1 . ASP D  74  ? 0.8724 0.7975 0.6925 -0.0898 -0.1367 -0.0782 74  ASP D OD1 
13159 O OD2 . ASP D  74  ? 0.9040 0.8831 0.7545 -0.1086 -0.1197 -0.0815 74  ASP D OD2 
13160 N N   . THR D  75  ? 0.9673 0.8451 0.7688 -0.1117 -0.1570 -0.0747 75  THR D N   
13161 C CA  . THR D  75  ? 0.9607 0.8138 0.7425 -0.1331 -0.1626 -0.0671 75  THR D CA  
13162 C C   . THR D  75  ? 0.9791 0.8340 0.7487 -0.1503 -0.1555 -0.0586 75  THR D C   
13163 O O   . THR D  75  ? 1.0096 0.8435 0.7611 -0.1703 -0.1598 -0.0511 75  THR D O   
13164 C CB  . THR D  75  ? 0.7558 0.5610 0.5113 -0.1259 -0.1780 -0.0652 75  THR D CB  
13165 O OG1 . THR D  75  ? 0.7054 0.5042 0.4584 -0.1009 -0.1804 -0.0691 75  THR D OG1 
13166 C CG2 . THR D  75  ? 0.7337 0.5311 0.4941 -0.1287 -0.1862 -0.0699 75  THR D CG2 
13167 N N   . LEU D  76  ? 0.7895 0.6682 0.5674 -0.1431 -0.1452 -0.0596 76  LEU D N   
13168 C CA  . LEU D  76  ? 0.7579 0.6339 0.5196 -0.1551 -0.1395 -0.0517 76  LEU D CA  
13169 C C   . LEU D  76  ? 0.8151 0.7012 0.5745 -0.1830 -0.1338 -0.0459 76  LEU D C   
13170 O O   . LEU D  76  ? 0.8685 0.7281 0.6014 -0.1980 -0.1375 -0.0363 76  LEU D O   
13171 C CB  . LEU D  76  ? 0.6652 0.5711 0.4402 -0.1435 -0.1283 -0.0557 76  LEU D CB  
13172 C CG  . LEU D  76  ? 0.6136 0.5266 0.3763 -0.1576 -0.1196 -0.0491 76  LEU D CG  
13173 C CD1 . LEU D  76  ? 0.6364 0.5067 0.3641 -0.1598 -0.1294 -0.0395 76  LEU D CD1 
13174 C CD2 . LEU D  76  ? 0.5419 0.4883 0.3211 -0.1466 -0.1079 -0.0551 76  LEU D CD2 
13175 N N   . TYR D  77  ? 0.9765 0.9021 0.7637 -0.1900 -0.1246 -0.0517 77  TYR D N   
13176 C CA  . TYR D  77  ? 1.0061 0.9485 0.7962 -0.2168 -0.1185 -0.0476 77  TYR D CA  
13177 C C   . TYR D  77  ? 0.9786 0.9356 0.7900 -0.2212 -0.1217 -0.0533 77  TYR D C   
13178 O O   . TYR D  77  ? 0.9620 0.9617 0.8028 -0.2205 -0.1124 -0.0605 77  TYR D O   
13179 C CB  . TYR D  77  ? 0.8114 0.7970 0.6172 -0.2219 -0.1018 -0.0499 77  TYR D CB  
13180 C CG  . TYR D  77  ? 0.7787 0.7542 0.5635 -0.2203 -0.0975 -0.0443 77  TYR D CG  
13181 C CD1 . TYR D  77  ? 0.8177 0.7529 0.5680 -0.2314 -0.1052 -0.0331 77  TYR D CD1 
13182 C CD2 . TYR D  77  ? 0.7234 0.7282 0.5220 -0.2077 -0.0866 -0.0504 77  TYR D CD2 
13183 C CE1 . TYR D  77  ? 0.8365 0.7624 0.5667 -0.2299 -0.1021 -0.0278 77  TYR D CE1 
13184 C CE2 . TYR D  77  ? 0.7425 0.7385 0.5215 -0.2066 -0.0832 -0.0456 77  TYR D CE2 
13185 C CZ  . TYR D  77  ? 0.7950 0.7521 0.5399 -0.2176 -0.0909 -0.0343 77  TYR D CZ  
13186 O OH  . TYR D  77  ? 0.7963 0.7443 0.5207 -0.2164 -0.0884 -0.0293 77  TYR D OH  
13187 N N   . PRO D  78  ? 0.8184 0.7393 0.6146 -0.2249 -0.1355 -0.0506 78  PRO D N   
13188 C CA  . PRO D  78  ? 0.7742 0.7021 0.5875 -0.2253 -0.1416 -0.0566 78  PRO D CA  
13189 C C   . PRO D  78  ? 0.7774 0.7423 0.6111 -0.2480 -0.1341 -0.0573 78  PRO D C   
13190 O O   . PRO D  78  ? 0.7960 0.7578 0.6169 -0.2723 -0.1313 -0.0492 78  PRO D O   
13191 C CB  . PRO D  78  ? 0.6811 0.5561 0.4651 -0.2295 -0.1579 -0.0514 78  PRO D CB  
13192 C CG  . PRO D  78  ? 0.7196 0.5666 0.4733 -0.2422 -0.1585 -0.0404 78  PRO D CG  
13193 C CD  . PRO D  78  ? 0.7111 0.5801 0.4705 -0.2300 -0.1470 -0.0412 78  PRO D CD  
13194 N N   . GLY D  79  ? 0.7691 0.7694 0.6341 -0.2400 -0.1310 -0.0666 79  GLY D N   
13195 C CA  . GLY D  79  ? 0.8114 0.8528 0.7005 -0.2585 -0.1239 -0.0689 79  GLY D CA  
13196 C C   . GLY D  79  ? 0.8319 0.9186 0.7389 -0.2617 -0.1070 -0.0709 79  GLY D C   
13197 O O   . GLY D  79  ? 0.8246 0.9542 0.7580 -0.2708 -0.0997 -0.0756 79  GLY D O   
13198 N N   . PHE D  80  ? 0.9682 1.0461 0.8607 -0.2538 -0.1011 -0.0678 80  PHE D N   
13199 C CA  . PHE D  80  ? 0.9694 1.0876 0.8767 -0.2530 -0.0852 -0.0711 80  PHE D CA  
13200 C C   . PHE D  80  ? 0.9080 1.0538 0.8435 -0.2278 -0.0819 -0.0827 80  PHE D C   
13201 O O   . PHE D  80  ? 0.9137 1.0380 0.8435 -0.2065 -0.0880 -0.0849 80  PHE D O   
13202 C CB  . PHE D  80  ? 0.9321 1.0278 0.8119 -0.2525 -0.0817 -0.0639 80  PHE D CB  
13203 C CG  . PHE D  80  ? 0.9153 1.0458 0.8077 -0.2444 -0.0672 -0.0690 80  PHE D CG  
13204 C CD1 . PHE D  80  ? 0.9459 1.1136 0.8480 -0.2619 -0.0539 -0.0691 80  PHE D CD1 
13205 C CD2 . PHE D  80  ? 0.8986 1.0247 0.7924 -0.2197 -0.0668 -0.0739 80  PHE D CD2 
13206 C CE1 . PHE D  80  ? 0.9425 1.1409 0.8547 -0.2535 -0.0407 -0.0748 80  PHE D CE1 
13207 C CE2 . PHE D  80  ? 0.8956 1.0509 0.7993 -0.2124 -0.0543 -0.0790 80  PHE D CE2 
13208 C CZ  . PHE D  80  ? 0.9086 1.0993 0.8211 -0.2286 -0.0413 -0.0799 80  PHE D CZ  
13209 N N   . GLU D  81  ? 0.6436 0.8370 0.6090 -0.2302 -0.0727 -0.0900 81  GLU D N   
13210 C CA  . GLU D  81  ? 0.6411 0.8580 0.6337 -0.2081 -0.0725 -0.1007 81  GLU D CA  
13211 C C   . GLU D  81  ? 0.6418 0.8637 0.6359 -0.1867 -0.0658 -0.1053 81  GLU D C   
13212 O O   . GLU D  81  ? 0.6479 0.8780 0.6580 -0.1664 -0.0679 -0.1128 81  GLU D O   
13213 C CB  . GLU D  81  ? 0.9016 1.1669 0.9264 -0.2158 -0.0666 -0.1077 81  GLU D CB  
13214 C CG  . GLU D  81  ? 0.9844 1.2919 1.0257 -0.2145 -0.0511 -0.1132 81  GLU D CG  
13215 C CD  . GLU D  81  ? 1.0424 1.3886 1.1179 -0.1977 -0.0485 -0.1253 81  GLU D CD  
13216 O OE1 . GLU D  81  ? 1.0571 1.4096 1.1483 -0.1966 -0.0570 -0.1284 81  GLU D OE1 
13217 O OE2 . GLU D  81  ? 1.0626 1.4313 1.1484 -0.1850 -0.0388 -0.1317 81  GLU D OE2 
13218 N N   . GLY D  82  ? 0.8092 1.0247 0.7854 -0.1916 -0.0584 -0.1006 82  GLY D N   
13219 C CA  . GLY D  82  ? 0.7707 0.9867 0.7452 -0.1727 -0.0534 -0.1044 82  GLY D CA  
13220 C C   . GLY D  82  ? 0.7409 0.9216 0.7035 -0.1537 -0.0643 -0.1036 82  GLY D C   
13221 O O   . GLY D  82  ? 0.7370 0.9247 0.7104 -0.1340 -0.0634 -0.1101 82  GLY D O   
13222 N N   . THR D  83  ? 0.5912 0.7336 0.5304 -0.1598 -0.0746 -0.0957 83  THR D N   
13223 C CA  . THR D  83  ? 0.5577 0.6675 0.4857 -0.1427 -0.0856 -0.0952 83  THR D CA  
13224 C C   . THR D  83  ? 0.5248 0.6367 0.4685 -0.1359 -0.0936 -0.1003 83  THR D C   
13225 O O   . THR D  83  ? 0.5144 0.6212 0.4637 -0.1169 -0.0979 -0.1049 83  THR D O   
13226 C CB  . THR D  83  ? 0.6321 0.6984 0.5279 -0.1502 -0.0945 -0.0856 83  THR D CB  
13227 O OG1 . THR D  83  ? 0.6359 0.6934 0.5265 -0.1700 -0.0995 -0.0811 83  THR D OG1 
13228 C CG2 . THR D  83  ? 0.6630 0.7232 0.5399 -0.1561 -0.0882 -0.0797 83  THR D CG2 
13229 N N   . GLU D  84  ? 0.4497 0.5693 0.3996 -0.1528 -0.0957 -0.0992 84  GLU D N   
13230 C CA  . GLU D  84  ? 0.4567 0.5753 0.4182 -0.1500 -0.1048 -0.1031 84  GLU D CA  
13231 C C   . GLU D  84  ? 0.3920 0.5413 0.3817 -0.1333 -0.1021 -0.1126 84  GLU D C   
13232 O O   . GLU D  84  ? 0.3814 0.5213 0.3750 -0.1214 -0.1105 -0.1160 84  GLU D O   
13233 C CB  . GLU D  84  ? 0.7568 0.8831 0.7213 -0.1741 -0.1065 -0.1001 84  GLU D CB  
13234 C CG  . GLU D  84  ? 0.8409 0.9366 0.7939 -0.1785 -0.1207 -0.0981 84  GLU D CG  
13235 C CD  . GLU D  84  ? 0.9043 0.9509 0.8243 -0.1757 -0.1292 -0.0914 84  GLU D CD  
13236 O OE1 . GLU D  84  ? 0.9193 0.9487 0.8189 -0.1916 -0.1283 -0.0833 84  GLU D OE1 
13237 O OE2 . GLU D  84  ? 0.9290 0.9545 0.8430 -0.1574 -0.1371 -0.0943 84  GLU D OE2 
13238 N N   . MET D  85  ? 0.5035 0.6878 0.5110 -0.1319 -0.0906 -0.1170 85  MET D N   
13239 C CA  . MET D  85  ? 0.5190 0.7316 0.5527 -0.1160 -0.0884 -0.1262 85  MET D CA  
13240 C C   . MET D  85  ? 0.5488 0.7430 0.5779 -0.0935 -0.0935 -0.1285 85  MET D C   
13241 O O   . MET D  85  ? 0.5128 0.7194 0.5587 -0.0806 -0.0963 -0.1346 85  MET D O   
13242 C CB  . MET D  85  ? 0.5181 0.7679 0.5681 -0.1170 -0.0750 -0.1309 85  MET D CB  
13243 C CG  . MET D  85  ? 0.4912 0.7368 0.5346 -0.1023 -0.0690 -0.1325 85  MET D CG  
13244 S SD  . MET D  85  ? 0.4390 0.7201 0.4917 -0.1074 -0.0530 -0.1367 85  MET D SD  
13245 C CE  . MET D  85  ? 0.6308 0.9583 0.7203 -0.1041 -0.0498 -0.1472 85  MET D CE  
13246 N N   . TRP D  86  ? 0.6971 0.8626 0.7034 -0.0892 -0.0946 -0.1235 86  TRP D N   
13247 C CA  . TRP D  86  ? 0.6962 0.8466 0.6976 -0.0696 -0.0983 -0.1253 86  TRP D CA  
13248 C C   . TRP D  86  ? 0.7438 0.8646 0.7322 -0.0650 -0.1102 -0.1231 86  TRP D C   
13249 O O   . TRP D  86  ? 0.7917 0.9023 0.7777 -0.0492 -0.1140 -0.1250 86  TRP D O   
13250 C CB  . TRP D  86  ? 0.5553 0.6949 0.5411 -0.0659 -0.0930 -0.1221 86  TRP D CB  
13251 C CG  . TRP D  86  ? 0.5385 0.7053 0.5340 -0.0700 -0.0812 -0.1248 86  TRP D CG  
13252 C CD1 . TRP D  86  ? 0.5427 0.7122 0.5277 -0.0842 -0.0743 -0.1206 86  TRP D CD1 
13253 C CD2 . TRP D  86  ? 0.5112 0.7051 0.5271 -0.0593 -0.0750 -0.1326 86  TRP D CD2 
13254 N NE1 . TRP D  86  ? 0.5256 0.7240 0.5238 -0.0827 -0.0636 -0.1260 86  TRP D NE1 
13255 C CE2 . TRP D  86  ? 0.5296 0.7427 0.5471 -0.0670 -0.0642 -0.1337 86  TRP D CE2 
13256 C CE3 . TRP D  86  ? 0.4924 0.6948 0.5240 -0.0440 -0.0780 -0.1388 86  TRP D CE3 
13257 C CZ2 . TRP D  86  ? 0.5503 0.7906 0.5850 -0.0587 -0.0565 -0.1416 86  TRP D CZ2 
13258 C CZ3 . TRP D  86  ? 0.4837 0.7112 0.5320 -0.0362 -0.0711 -0.1458 86  TRP D CZ3 
13259 C CH2 . TRP D  86  ? 0.5169 0.7630 0.5670 -0.0429 -0.0605 -0.1477 86  TRP D CH2 
13260 N N   . ASN D  87  ? 0.5534 0.6606 0.5328 -0.0793 -0.1159 -0.1193 87  ASN D N   
13261 C CA  . ASN D  87  ? 0.5228 0.5997 0.4876 -0.0763 -0.1277 -0.1177 87  ASN D CA  
13262 C C   . ASN D  87  ? 0.4528 0.5395 0.4330 -0.0688 -0.1338 -0.1236 87  ASN D C   
13263 O O   . ASN D  87  ? 0.4048 0.5216 0.4074 -0.0715 -0.1302 -0.1278 87  ASN D O   
13264 C CB  . ASN D  87  ? 0.6970 0.7528 0.6447 -0.0951 -0.1326 -0.1116 87  ASN D CB  
13265 C CG  . ASN D  87  ? 0.7628 0.7843 0.6826 -0.0939 -0.1356 -0.1054 87  ASN D CG  
13266 O OD1 . ASN D  87  ? 0.7848 0.7942 0.6972 -0.0772 -0.1372 -0.1063 87  ASN D OD1 
13267 N ND2 . ASN D  87  ? 0.7864 0.7924 0.6905 -0.1118 -0.1370 -0.0988 87  ASN D ND2 
13268 N N   . PRO D  88  ? 0.5906 0.6525 0.5586 -0.0588 -0.1431 -0.1242 88  PRO D N   
13269 C CA  . PRO D  88  ? 0.5654 0.6339 0.5446 -0.0510 -0.1495 -0.1294 88  PRO D CA  
13270 C C   . PRO D  88  ? 0.5276 0.6108 0.5197 -0.0656 -0.1528 -0.1310 88  PRO D C   
13271 O O   . PRO D  88  ? 0.5617 0.6294 0.5423 -0.0806 -0.1570 -0.1274 88  PRO D O   
13272 C CB  . PRO D  88  ? 0.4123 0.4460 0.3697 -0.0436 -0.1551 -0.1253 88  PRO D CB  
13273 C CG  . PRO D  88  ? 0.4070 0.4245 0.3484 -0.0384 -0.1531 -0.1226 88  PRO D CG  
13274 C CD  . PRO D  88  ? 0.4240 0.4528 0.3675 -0.0519 -0.1476 -0.1207 88  PRO D CD  
13275 N N   . ASN D  89  ? 0.3435 0.4542 0.3582 -0.0612 -0.1498 -0.1342 89  ASN D N   
13276 C CA  . ASN D  89  ? 0.3721 0.4992 0.4012 -0.0730 -0.1537 -0.1357 89  ASN D CA  
13277 C C   . ASN D  89  ? 0.4147 0.5290 0.4409 -0.0665 -0.1606 -0.1342 89  ASN D C   
13278 O O   . ASN D  89  ? 0.4001 0.5307 0.4406 -0.0729 -0.1637 -0.1354 89  ASN D O   
13279 C CB  . ASN D  89  ? 0.4402 0.6090 0.4967 -0.0770 -0.1458 -0.1396 89  ASN D CB  
13280 C CG  . ASN D  89  ? 0.4389 0.6220 0.5104 -0.0586 -0.1421 -0.1415 89  ASN D CG  
13281 O OD1 . ASN D  89  ? 0.4766 0.6415 0.5380 -0.0434 -0.1423 -0.1395 89  ASN D OD1 
13282 N ND2 . ASN D  89  ? 0.4108 0.6272 0.5066 -0.0602 -0.1383 -0.1452 89  ASN D ND2 
13283 N N   . ARG D  90  ? 0.6440 0.7329 0.6533 -0.0530 -0.1615 -0.1316 90  ARG D N   
13284 C CA  . ARG D  90  ? 0.6537 0.7271 0.6551 -0.0479 -0.1670 -0.1304 90  ARG D CA  
13285 C C   . ARG D  90  ? 0.7438 0.7829 0.7199 -0.0448 -0.1701 -0.1281 90  ARG D C   
13286 O O   . ARG D  90  ? 0.7967 0.8222 0.7604 -0.0477 -0.1694 -0.1268 90  ARG D O   
13287 C CB  . ARG D  90  ? 0.3871 0.4693 0.3975 -0.0309 -0.1633 -0.1304 90  ARG D CB  
13288 C CG  . ARG D  90  ? 0.3389 0.4515 0.3736 -0.0311 -0.1617 -0.1329 90  ARG D CG  
13289 C CD  . ARG D  90  ? 0.3545 0.4742 0.3958 -0.0422 -0.1691 -0.1339 90  ARG D CD  
13290 N NE  . ARG D  90  ? 0.3643 0.5155 0.4307 -0.0415 -0.1675 -0.1365 90  ARG D NE  
13291 C CZ  . ARG D  90  ? 0.3771 0.5543 0.4609 -0.0501 -0.1636 -0.1391 90  ARG D CZ  
13292 N NH1 . ARG D  90  ? 0.3344 0.5092 0.4124 -0.0619 -0.1613 -0.1391 90  ARG D NH1 
13293 N NH2 . ARG D  90  ? 0.3746 0.5811 0.4817 -0.0468 -0.1617 -0.1421 90  ARG D NH2 
13294 N N   . GLU D  91  ? 0.5541 0.5797 0.5226 -0.0380 -0.1738 -0.1279 91  GLU D N   
13295 C CA  . GLU D  91  ? 0.5639 0.5587 0.5107 -0.0319 -0.1766 -0.1266 91  GLU D CA  
13296 C C   . GLU D  91  ? 0.4423 0.4320 0.3842 -0.0154 -0.1703 -0.1248 91  GLU D C   
13297 O O   . GLU D  91  ? 0.3922 0.3968 0.3449 -0.0054 -0.1653 -0.1247 91  GLU D O   
13298 C CB  . GLU D  91  ? 0.9703 0.9561 0.9126 -0.0293 -0.1820 -0.1279 91  GLU D CB  
13299 C CG  . GLU D  91  ? 1.1273 1.1097 1.0684 -0.0461 -0.1897 -0.1295 91  GLU D CG  
13300 C CD  . GLU D  91  ? 1.2823 1.2354 1.2038 -0.0536 -0.1944 -0.1286 91  GLU D CD  
13301 O OE1 . GLU D  91  ? 1.3264 1.2625 1.2353 -0.0446 -0.1921 -0.1266 91  GLU D OE1 
13302 O OE2 . GLU D  91  ? 1.3409 1.2871 1.2594 -0.0683 -0.2008 -0.1294 91  GLU D OE2 
13303 N N   . LEU D  92  ? 0.4125 0.3810 0.3381 -0.0126 -0.1708 -0.1233 92  LEU D N   
13304 C CA  . LEU D  92  ? 0.3914 0.3567 0.3131 0.0024  -0.1650 -0.1217 92  LEU D CA  
13305 C C   . LEU D  92  ? 0.3909 0.3504 0.3095 0.0148  -0.1653 -0.1222 92  LEU D C   
13306 O O   . LEU D  92  ? 0.4085 0.3547 0.3191 0.0128  -0.1714 -0.1237 92  LEU D O   
13307 C CB  . LEU D  92  ? 0.4075 0.3502 0.3118 0.0033  -0.1671 -0.1200 92  LEU D CB  
13308 C CG  . LEU D  92  ? 0.4103 0.3550 0.3132 -0.0078 -0.1665 -0.1187 92  LEU D CG  
13309 C CD1 . LEU D  92  ? 0.4193 0.3447 0.3064 -0.0002 -0.1666 -0.1162 92  LEU D CD1 
13310 C CD2 . LEU D  92  ? 0.4110 0.3856 0.3329 -0.0096 -0.1596 -0.1196 92  LEU D CD2 
13311 N N   . SER D  93  ? 0.4479 0.4175 0.3723 0.0268  -0.1589 -0.1213 93  SER D N   
13312 C CA  . SER D  93  ? 0.4091 0.3727 0.3284 0.0388  -0.1586 -0.1218 93  SER D CA  
13313 C C   . SER D  93  ? 0.4195 0.3914 0.3420 0.0502  -0.1512 -0.1201 93  SER D C   
13314 O O   . SER D  93  ? 0.4221 0.4078 0.3542 0.0490  -0.1460 -0.1187 93  SER D O   
13315 C CB  . SER D  93  ? 0.4039 0.3766 0.3307 0.0374  -0.1608 -0.1231 93  SER D CB  
13316 O OG  . SER D  93  ? 0.4123 0.3843 0.3361 0.0491  -0.1586 -0.1232 93  SER D OG  
13317 N N   . GLU D  94  ? 0.3600 0.3242 0.2747 0.0610  -0.1509 -0.1207 94  GLU D N   
13318 C CA  . GLU D  94  ? 0.3445 0.3188 0.2630 0.0705  -0.1442 -0.1194 94  GLU D CA  
13319 C C   . GLU D  94  ? 0.3332 0.3208 0.2607 0.0716  -0.1419 -0.1191 94  GLU D C   
13320 O O   . GLU D  94  ? 0.3198 0.3175 0.2521 0.0768  -0.1364 -0.1176 94  GLU D O   
13321 C CB  . GLU D  94  ? 0.4074 0.3715 0.3148 0.0815  -0.1448 -0.1208 94  GLU D CB  
13322 C CG  . GLU D  94  ? 0.4120 0.3671 0.3122 0.0854  -0.1451 -0.1205 94  GLU D CG  
13323 C CD  . GLU D  94  ? 0.4198 0.3709 0.3124 0.0987  -0.1448 -0.1226 94  GLU D CD  
13324 O OE1 . GLU D  94  ? 0.4550 0.3927 0.3375 0.1031  -0.1503 -0.1256 94  GLU D OE1 
13325 O OE2 . GLU D  94  ? 0.3800 0.3424 0.2769 0.1047  -0.1393 -0.1216 94  GLU D OE2 
13326 N N   . ASP D  95  ? 0.3404 0.3272 0.2695 0.0663  -0.1468 -0.1204 95  ASP D N   
13327 C CA  . ASP D  95  ? 0.3581 0.3562 0.2950 0.0675  -0.1458 -0.1200 95  ASP D CA  
13328 C C   . ASP D  95  ? 0.3253 0.3359 0.2756 0.0596  -0.1453 -0.1195 95  ASP D C   
13329 O O   . ASP D  95  ? 0.3276 0.3412 0.2828 0.0525  -0.1502 -0.1209 95  ASP D O   
13330 C CB  . ASP D  95  ? 0.5740 0.5639 0.5042 0.0666  -0.1523 -0.1221 95  ASP D CB  
13331 C CG  . ASP D  95  ? 0.6456 0.6454 0.5825 0.0668  -0.1533 -0.1218 95  ASP D CG  
13332 O OD1 . ASP D  95  ? 0.7057 0.7166 0.6505 0.0694  -0.1488 -0.1199 95  ASP D OD1 
13333 O OD2 . ASP D  95  ? 0.6293 0.6244 0.5624 0.0643  -0.1592 -0.1236 95  ASP D OD2 
13334 N N   . CYS D  96  ? 0.3569 0.3766 0.3138 0.0613  -0.1394 -0.1179 96  CYS D N   
13335 C CA  . CYS D  96  ? 0.3528 0.3859 0.3227 0.0556  -0.1379 -0.1182 96  CYS D CA  
13336 C C   . CYS D  96  ? 0.2832 0.3293 0.2638 0.0598  -0.1342 -0.1177 96  CYS D C   
13337 O O   . CYS D  96  ? 0.2762 0.3340 0.2681 0.0563  -0.1332 -0.1190 96  CYS D O   
13338 C CB  . CYS D  96  ? 0.4540 0.4859 0.4224 0.0513  -0.1356 -0.1179 96  CYS D CB  
13339 S SG  . CYS D  96  ? 0.6823 0.7081 0.6424 0.0594  -0.1300 -0.1156 96  CYS D SG  
13340 N N   . LEU D  97  ? 0.3148 0.3589 0.2914 0.0669  -0.1324 -0.1162 97  LEU D N   
13341 C CA  . LEU D  97  ? 0.2757 0.3285 0.2595 0.0705  -0.1288 -0.1154 97  LEU D CA  
13342 C C   . LEU D  97  ? 0.3074 0.3667 0.2992 0.0706  -0.1329 -0.1166 97  LEU D C   
13343 O O   . LEU D  97  ? 0.3504 0.4057 0.3373 0.0738  -0.1356 -0.1158 97  LEU D O   
13344 C CB  . LEU D  97  ? 0.2684 0.3168 0.2436 0.0766  -0.1254 -0.1130 97  LEU D CB  
13345 C CG  . LEU D  97  ? 0.2658 0.3108 0.2353 0.0777  -0.1212 -0.1120 97  LEU D CG  
13346 C CD1 . LEU D  97  ? 0.2641 0.3088 0.2271 0.0829  -0.1177 -0.1100 97  LEU D CD1 
13347 C CD2 . LEU D  97  ? 0.2568 0.3083 0.2338 0.0746  -0.1180 -0.1122 97  LEU D CD2 
13348 N N   . TYR D  98  ? 0.3490 0.4195 0.3534 0.0677  -0.1331 -0.1189 98  TYR D N   
13349 C CA  . TYR D  98  ? 0.3847 0.4641 0.3996 0.0675  -0.1377 -0.1211 98  TYR D CA  
13350 C C   . TYR D  98  ? 0.4428 0.5353 0.4707 0.0683  -0.1349 -0.1238 98  TYR D C   
13351 O O   . TYR D  98  ? 0.4577 0.5522 0.4859 0.0663  -0.1302 -0.1241 98  TYR D O   
13352 C CB  . TYR D  98  ? 0.3082 0.3904 0.3263 0.0602  -0.1429 -0.1229 98  TYR D CB  
13353 C CG  . TYR D  98  ? 0.3218 0.3903 0.3266 0.0593  -0.1467 -0.1214 98  TYR D CG  
13354 C CD1 . TYR D  98  ? 0.3276 0.3934 0.3297 0.0620  -0.1515 -0.1212 98  TYR D CD1 
13355 C CD2 . TYR D  98  ? 0.3318 0.3894 0.3260 0.0561  -0.1458 -0.1208 98  TYR D CD2 
13356 C CE1 . TYR D  98  ? 0.3086 0.3623 0.2980 0.0615  -0.1549 -0.1207 98  TYR D CE1 
13357 C CE2 . TYR D  98  ? 0.3262 0.3707 0.3078 0.0565  -0.1495 -0.1206 98  TYR D CE2 
13358 C CZ  . TYR D  98  ? 0.3192 0.3624 0.2987 0.0591  -0.1538 -0.1207 98  TYR D CZ  
13359 O OH  . TYR D  98  ? 0.3278 0.3585 0.2945 0.0597  -0.1574 -0.1212 98  TYR D OH  
13360 N N   . LEU D  99  ? 0.3669 0.4678 0.4048 0.0719  -0.1379 -0.1261 99  LEU D N   
13361 C CA  . LEU D  99  ? 0.3174 0.4322 0.3688 0.0737  -0.1357 -0.1302 99  LEU D CA  
13362 C C   . LEU D  99  ? 0.3134 0.4436 0.3799 0.0726  -0.1404 -0.1342 99  LEU D C   
13363 O O   . LEU D  99  ? 0.3311 0.4595 0.3966 0.0709  -0.1458 -0.1332 99  LEU D O   
13364 C CB  . LEU D  99  ? 0.2497 0.3592 0.2981 0.0815  -0.1339 -0.1297 99  LEU D CB  
13365 C CG  . LEU D  99  ? 0.2574 0.3566 0.2987 0.0874  -0.1384 -0.1272 99  LEU D CG  
13366 C CD1 . LEU D  99  ? 0.2624 0.3705 0.3155 0.0918  -0.1439 -0.1310 99  LEU D CD1 
13367 C CD2 . LEU D  99  ? 0.2561 0.3450 0.2876 0.0912  -0.1358 -0.1244 99  LEU D CD2 
13368 N N   . ASN D  100 ? 0.2805 0.4273 0.3612 0.0734  -0.1381 -0.1392 100 ASN D N   
13369 C CA  . ASN D  100 ? 0.3082 0.4749 0.4065 0.0728  -0.1413 -0.1441 100 ASN D CA  
13370 C C   . ASN D  100 ? 0.3348 0.5095 0.4427 0.0825  -0.1410 -0.1489 100 ASN D C   
13371 O O   . ASN D  100 ? 0.3923 0.5630 0.4967 0.0865  -0.1367 -0.1500 100 ASN D O   
13372 C CB  . ASN D  100 ? 0.2563 0.4404 0.3646 0.0631  -0.1380 -0.1471 100 ASN D CB  
13373 C CG  . ASN D  100 ? 0.2649 0.4382 0.3616 0.0530  -0.1383 -0.1429 100 ASN D CG  
13374 O OD1 . ASN D  100 ? 0.2601 0.4232 0.3495 0.0506  -0.1435 -0.1398 100 ASN D OD1 
13375 N ND2 . ASN D  100 ? 0.2479 0.4227 0.3418 0.0471  -0.1334 -0.1432 100 ASN D ND2 
13376 N N   . VAL D  101 ? 0.3320 0.5182 0.4520 0.0865  -0.1460 -0.1520 101 VAL D N   
13377 C CA  . VAL D  101 ? 0.3412 0.5335 0.4698 0.0969  -0.1472 -0.1572 101 VAL D CA  
13378 C C   . VAL D  101 ? 0.3776 0.5969 0.5275 0.0969  -0.1483 -0.1635 101 VAL D C   
13379 O O   . VAL D  101 ? 0.4359 0.6624 0.5915 0.0931  -0.1530 -0.1624 101 VAL D O   
13380 C CB  . VAL D  101 ? 0.2703 0.4449 0.3893 0.1050  -0.1542 -0.1541 101 VAL D CB  
13381 C CG1 . VAL D  101 ? 0.2765 0.4553 0.4034 0.1160  -0.1570 -0.1597 101 VAL D CG1 
13382 C CG2 . VAL D  101 ? 0.2696 0.4202 0.3683 0.1047  -0.1528 -0.1478 101 VAL D CG2 
13383 N N   . TRP D  102 ? 0.2632 0.4987 0.4250 0.1011  -0.1439 -0.1704 102 TRP D N   
13384 C CA  . TRP D  102 ? 0.2887 0.5513 0.4714 0.1036  -0.1446 -0.1772 102 TRP D CA  
13385 C C   . TRP D  102 ? 0.3507 0.6102 0.5363 0.1182  -0.1483 -0.1822 102 TRP D C   
13386 O O   . TRP D  102 ? 0.3582 0.6054 0.5355 0.1243  -0.1462 -0.1839 102 TRP D O   
13387 C CB  . TRP D  102 ? 0.2542 0.5421 0.4497 0.0966  -0.1361 -0.1824 102 TRP D CB  
13388 C CG  . TRP D  102 ? 0.2745 0.5708 0.4712 0.0811  -0.1339 -0.1787 102 TRP D CG  
13389 C CD1 . TRP D  102 ? 0.2902 0.6077 0.5009 0.0727  -0.1356 -0.1795 102 TRP D CD1 
13390 C CD2 . TRP D  102 ? 0.2612 0.5440 0.4438 0.0717  -0.1303 -0.1738 102 TRP D CD2 
13391 N NE1 . TRP D  102 ? 0.2751 0.5916 0.4804 0.0578  -0.1338 -0.1753 102 TRP D NE1 
13392 C CE2 . TRP D  102 ? 0.2684 0.5631 0.4561 0.0574  -0.1306 -0.1719 102 TRP D CE2 
13393 C CE3 . TRP D  102 ? 0.2732 0.5347 0.4390 0.0736  -0.1274 -0.1708 102 TRP D CE3 
13394 C CZ2 . TRP D  102 ? 0.2928 0.5763 0.4678 0.0458  -0.1287 -0.1672 102 TRP D CZ2 
13395 C CZ3 . TRP D  102 ? 0.2822 0.5349 0.4367 0.0627  -0.1249 -0.1662 102 TRP D CZ3 
13396 C CH2 . TRP D  102 ? 0.3000 0.5625 0.4585 0.0493  -0.1258 -0.1645 102 TRP D CH2 
13397 N N   . THR D  103 ? 0.4383 0.7078 0.6347 0.1238  -0.1546 -0.1846 103 THR D N   
13398 C CA  . THR D  103 ? 0.4536 0.7220 0.6540 0.1380  -0.1590 -0.1903 103 THR D CA  
13399 C C   . THR D  103 ? 0.5027 0.8021 0.7259 0.1408  -0.1599 -0.1971 103 THR D C   
13400 O O   . THR D  103 ? 0.5017 0.8205 0.7359 0.1311  -0.1588 -0.1960 103 THR D O   
13401 C CB  . THR D  103 ? 0.3686 0.6095 0.5542 0.1453  -0.1688 -0.1851 103 THR D CB  
13402 O OG1 . THR D  103 ? 0.3802 0.6272 0.5709 0.1427  -0.1752 -0.1822 103 THR D OG1 
13403 C CG2 . THR D  103 ? 0.3687 0.5816 0.5324 0.1411  -0.1678 -0.1776 103 THR D CG2 
13404 N N   . PRO D  104 ? 0.7273 1.0320 0.9575 0.1537  -0.1622 -0.2043 104 PRO D N   
13405 C CA  . PRO D  104 ? 0.7899 1.1244 1.0419 0.1584  -0.1637 -0.2112 104 PRO D CA  
13406 C C   . PRO D  104 ? 0.8470 1.1830 1.1032 0.1586  -0.1733 -0.2074 104 PRO D C   
13407 O O   . PRO D  104 ? 0.9078 1.2168 1.1481 0.1605  -0.1807 -0.2009 104 PRO D O   
13408 C CB  . PRO D  104 ? 0.6021 0.9304 0.8536 0.1743  -0.1665 -0.2184 104 PRO D CB  
13409 C CG  . PRO D  104 ? 0.5735 0.8804 0.8086 0.1740  -0.1619 -0.2173 104 PRO D CG  
13410 C CD  . PRO D  104 ? 0.5401 0.8254 0.7590 0.1637  -0.1624 -0.2072 104 PRO D CD  
13411 N N   . TYR D  105 ? 0.6177 0.9860 0.8951 0.1560  -0.1730 -0.2114 105 TYR D N   
13412 C CA  . TYR D  105 ? 0.6539 1.0269 0.9377 0.1574  -0.1830 -0.2089 105 TYR D CA  
13413 C C   . TYR D  105 ? 0.7109 1.1048 1.0123 0.1709  -0.1869 -0.2175 105 TYR D C   
13414 O O   . TYR D  105 ? 0.7520 1.1797 1.0736 0.1691  -0.1808 -0.2242 105 TYR D O   
13415 C CB  . TYR D  105 ? 0.6794 1.0727 0.9731 0.1411  -0.1810 -0.2053 105 TYR D CB  
13416 C CG  . TYR D  105 ? 0.6723 1.0702 0.9714 0.1401  -0.1915 -0.2020 105 TYR D CG  
13417 C CD1 . TYR D  105 ? 0.6873 1.1117 1.0069 0.1474  -0.1962 -0.2079 105 TYR D CD1 
13418 C CD2 . TYR D  105 ? 0.6682 1.0453 0.9520 0.1316  -0.1967 -0.1934 105 TYR D CD2 
13419 C CE1 . TYR D  105 ? 0.7137 1.1434 1.0385 0.1462  -0.2064 -0.2049 105 TYR D CE1 
13420 C CE2 . TYR D  105 ? 0.6919 1.0734 0.9798 0.1302  -0.2067 -0.1906 105 TYR D CE2 
13421 C CZ  . TYR D  105 ? 0.7105 1.1185 1.0191 0.1374  -0.2117 -0.1962 105 TYR D CZ  
13422 O OH  . TYR D  105 ? 0.7041 1.1177 1.0174 0.1360  -0.2222 -0.1936 105 TYR D OH  
13423 N N   . PRO D  106 ? 0.7648 1.1396 1.0586 0.1841  -0.1974 -0.2173 106 PRO D N   
13424 C CA  . PRO D  106 ? 0.7881 1.1258 1.0592 0.1864  -0.2059 -0.2093 106 PRO D CA  
13425 C C   . PRO D  106 ? 0.8147 1.1216 1.0646 0.1881  -0.2024 -0.2070 106 PRO D C   
13426 O O   . PRO D  106 ? 0.8038 1.1160 1.0565 0.1912  -0.1953 -0.2129 106 PRO D O   
13427 C CB  . PRO D  106 ? 0.6474 0.9825 0.9223 0.2017  -0.2174 -0.2127 106 PRO D CB  
13428 C CG  . PRO D  106 ? 0.6322 0.9887 0.9228 0.2116  -0.2131 -0.2234 106 PRO D CG  
13429 C CD  . PRO D  106 ? 0.6186 1.0090 0.9267 0.1994  -0.2014 -0.2263 106 PRO D CD  
13430 N N   . ARG D  107 ? 0.5743 0.8505 0.8034 0.1858  -0.2077 -0.1985 107 ARG D N   
13431 C CA  . ARG D  107 ? 0.5765 0.8221 0.7841 0.1863  -0.2058 -0.1947 107 ARG D CA  
13432 C C   . ARG D  107 ? 0.5316 0.7700 0.7385 0.2001  -0.2079 -0.2016 107 ARG D C   
13433 O O   . ARG D  107 ? 0.4502 0.6951 0.6659 0.2113  -0.2153 -0.2064 107 ARG D O   
13434 C CB  . ARG D  107 ? 1.0455 1.2622 1.2328 0.1847  -0.2137 -0.1854 107 ARG D CB  
13435 C CG  . ARG D  107 ? 1.1241 1.3133 1.2894 0.1793  -0.2100 -0.1789 107 ARG D CG  
13436 C CD  . ARG D  107 ? 1.2323 1.3903 1.3784 0.1874  -0.2192 -0.1748 107 ARG D CD  
13437 N NE  . ARG D  107 ? 1.3117 1.4579 1.4476 0.1851  -0.2271 -0.1675 107 ARG D NE  
13438 C CZ  . ARG D  107 ? 1.3473 1.4665 1.4646 0.1896  -0.2355 -0.1621 107 ARG D CZ  
13439 N NH1 . ARG D  107 ? 1.3510 1.4507 1.4579 0.1966  -0.2378 -0.1629 107 ARG D NH1 
13440 N NH2 . ARG D  107 ? 1.3503 1.4615 1.4586 0.1868  -0.2419 -0.1558 107 ARG D NH2 
13441 N N   . PRO D  108 ? 0.9068 1.1328 1.1038 0.1993  -0.2017 -0.2024 108 PRO D N   
13442 C CA  . PRO D  108 ? 0.9534 1.1705 1.1478 0.2113  -0.2037 -0.2089 108 PRO D CA  
13443 C C   . PRO D  108 ? 0.9900 1.1806 1.1719 0.2226  -0.2168 -0.2069 108 PRO D C   
13444 O O   . PRO D  108 ? 0.9908 1.1564 1.1552 0.2192  -0.2223 -0.1982 108 PRO D O   
13445 C CB  . PRO D  108 ? 0.8943 1.0954 1.0746 0.2051  -0.1965 -0.2064 108 PRO D CB  
13446 C CG  . PRO D  108 ? 0.8787 1.0966 1.0647 0.1911  -0.1870 -0.2033 108 PRO D CG  
13447 C CD  . PRO D  108 ? 0.8715 1.0945 1.0611 0.1867  -0.1921 -0.1980 108 PRO D CD  
13448 N N   . ALA D  109 ? 0.9710 1.1675 1.1614 0.2360  -0.2218 -0.2151 109 ALA D N   
13449 C CA  . ALA D  109 ? 0.9809 1.1518 1.1595 0.2483  -0.2350 -0.2144 109 ALA D CA  
13450 C C   . ALA D  109 ? 0.9843 1.1186 1.1385 0.2478  -0.2376 -0.2092 109 ALA D C   
13451 O O   . ALA D  109 ? 0.9907 1.0970 1.1272 0.2487  -0.2469 -0.2018 109 ALA D O   
13452 C CB  . ALA D  109 ? 0.9001 1.0857 1.0929 0.2630  -0.2384 -0.2254 109 ALA D CB  
13453 N N   . SER D  110 ? 1.0582 1.1938 1.2114 0.2457  -0.2294 -0.2129 110 SER D N   
13454 C CA  . SER D  110 ? 1.0297 1.1334 1.1618 0.2456  -0.2318 -0.2093 110 SER D CA  
13455 C C   . SER D  110 ? 0.9692 1.0741 1.0960 0.2319  -0.2208 -0.2047 110 SER D C   
13456 O O   . SER D  110 ? 0.9583 1.0903 1.0994 0.2245  -0.2105 -0.2070 110 SER D O   
13457 C CB  . SER D  110 ? 0.8692 0.9705 1.0033 0.2574  -0.2337 -0.2186 110 SER D CB  
13458 O OG  . SER D  110 ? 0.8687 0.9858 1.0174 0.2694  -0.2393 -0.2259 110 SER D OG  
13459 N N   . PRO D  111 ? 0.8779 0.9537 0.9843 0.2284  -0.2233 -0.1981 111 PRO D N   
13460 C CA  . PRO D  111 ? 0.8460 0.9207 0.9456 0.2158  -0.2143 -0.1925 111 PRO D CA  
13461 C C   . PRO D  111 ? 0.8181 0.9130 0.9281 0.2122  -0.2026 -0.1990 111 PRO D C   
13462 O O   . PRO D  111 ? 0.8389 0.9221 0.9407 0.2130  -0.2013 -0.2006 111 PRO D O   
13463 C CB  . PRO D  111 ? 0.7266 0.7653 0.8024 0.2155  -0.2214 -0.1852 111 PRO D CB  
13464 C CG  . PRO D  111 ? 0.7611 0.7815 0.8313 0.2283  -0.2336 -0.1883 111 PRO D CG  
13465 C CD  . PRO D  111 ? 0.7631 0.8046 0.8502 0.2348  -0.2361 -0.1933 111 PRO D CD  
13466 N N   . THR D  112 ? 0.6974 0.8231 0.8255 0.2079  -0.1947 -0.2027 112 THR D N   
13467 C CA  . THR D  112 ? 0.6349 0.7837 0.7738 0.2023  -0.1828 -0.2079 112 THR D CA  
13468 C C   . THR D  112 ? 0.5955 0.7332 0.7221 0.1929  -0.1767 -0.2028 112 THR D C   
13469 O O   . THR D  112 ? 0.6109 0.7341 0.7259 0.1860  -0.1780 -0.1940 112 THR D O   
13470 C CB  . THR D  112 ? 0.6075 0.7866 0.7640 0.1955  -0.1767 -0.2087 112 THR D CB  
13471 O OG1 . THR D  112 ? 0.6346 0.8335 0.8076 0.2044  -0.1794 -0.2164 112 THR D OG1 
13472 C CG2 . THR D  112 ? 0.5653 0.7637 0.7283 0.1856  -0.1644 -0.2104 112 THR D CG2 
13473 N N   . PRO D  113 ? 0.5309 0.6756 0.6596 0.1931  -0.1702 -0.2086 113 PRO D N   
13474 C CA  . PRO D  113 ? 0.4771 0.6184 0.5981 0.1843  -0.1630 -0.2056 113 PRO D CA  
13475 C C   . PRO D  113 ? 0.4568 0.6135 0.5826 0.1721  -0.1552 -0.2009 113 PRO D C   
13476 O O   . PRO D  113 ? 0.4327 0.6141 0.5736 0.1693  -0.1506 -0.2040 113 PRO D O   
13477 C CB  . PRO D  113 ? 0.3572 0.5130 0.4859 0.1879  -0.1569 -0.2148 113 PRO D CB  
13478 C CG  . PRO D  113 ? 0.3958 0.5440 0.5255 0.2006  -0.1648 -0.2202 113 PRO D CG  
13479 C CD  . PRO D  113 ? 0.4356 0.5880 0.5719 0.2035  -0.1709 -0.2183 113 PRO D CD  
13480 N N   . VAL D  114 ? 0.3616 0.5030 0.4738 0.1649  -0.1538 -0.1933 114 VAL D N   
13481 C CA  . VAL D  114 ? 0.3215 0.4703 0.4334 0.1534  -0.1478 -0.1870 114 VAL D CA  
13482 C C   . VAL D  114 ? 0.3137 0.4710 0.4251 0.1466  -0.1389 -0.1881 114 VAL D C   
13483 O O   . VAL D  114 ? 0.2717 0.4172 0.3739 0.1483  -0.1390 -0.1886 114 VAL D O   
13484 C CB  . VAL D  114 ? 0.2878 0.4136 0.3837 0.1500  -0.1525 -0.1767 114 VAL D CB  
13485 C CG1 . VAL D  114 ? 0.3358 0.4634 0.4264 0.1385  -0.1454 -0.1699 114 VAL D CG1 
13486 C CG2 . VAL D  114 ? 0.2987 0.4217 0.3968 0.1536  -0.1597 -0.1746 114 VAL D CG2 
13487 N N   . LEU D  115 ? 0.3571 0.5352 0.4783 0.1386  -0.1321 -0.1885 115 LEU D N   
13488 C CA  . LEU D  115 ? 0.3243 0.5123 0.4452 0.1307  -0.1238 -0.1889 115 LEU D CA  
13489 C C   . LEU D  115 ? 0.3222 0.5051 0.4358 0.1198  -0.1216 -0.1797 115 LEU D C   
13490 O O   . LEU D  115 ? 0.3141 0.5084 0.4355 0.1149  -0.1212 -0.1784 115 LEU D O   
13491 C CB  . LEU D  115 ? 0.2420 0.4600 0.3802 0.1294  -0.1175 -0.1974 115 LEU D CB  
13492 C CG  . LEU D  115 ? 0.2698 0.4956 0.4142 0.1389  -0.1163 -0.2073 115 LEU D CG  
13493 C CD1 . LEU D  115 ? 0.2484 0.5063 0.4110 0.1381  -0.1094 -0.2154 115 LEU D CD1 
13494 C CD2 . LEU D  115 ? 0.2830 0.4992 0.4167 0.1379  -0.1134 -0.2075 115 LEU D CD2 
13495 N N   . ILE D  116 ? 0.2440 0.4099 0.3425 0.1160  -0.1202 -0.1734 116 ILE D N   
13496 C CA  . ILE D  116 ? 0.2291 0.3874 0.3184 0.1067  -0.1177 -0.1645 116 ILE D CA  
13497 C C   . ILE D  116 ? 0.2208 0.3886 0.3095 0.0985  -0.1107 -0.1649 116 ILE D C   
13498 O O   . ILE D  116 ? 0.2192 0.3854 0.3033 0.0991  -0.1077 -0.1669 116 ILE D O   
13499 C CB  . ILE D  116 ? 0.2322 0.3673 0.3051 0.1071  -0.1199 -0.1565 116 ILE D CB  
13500 C CG1 . ILE D  116 ? 0.2430 0.3674 0.3144 0.1143  -0.1277 -0.1558 116 ILE D CG1 
13501 C CG2 . ILE D  116 ? 0.2277 0.3565 0.2918 0.0988  -0.1171 -0.1485 116 ILE D CG2 
13502 C CD1 . ILE D  116 ? 0.2483 0.3517 0.3036 0.1144  -0.1303 -0.1485 116 ILE D CD1 
13503 N N   . TRP D  117 ? 0.2176 0.3945 0.3098 0.0904  -0.1088 -0.1630 117 TRP D N   
13504 C CA  . TRP D  117 ? 0.2129 0.3985 0.3037 0.0814  -0.1031 -0.1633 117 TRP D CA  
13505 C C   . TRP D  117 ? 0.2223 0.3906 0.2976 0.0746  -0.1022 -0.1541 117 TRP D C   
13506 O O   . TRP D  117 ? 0.2151 0.3737 0.2863 0.0735  -0.1057 -0.1489 117 TRP D O   
13507 C CB  . TRP D  117 ? 0.2123 0.4218 0.3182 0.0757  -0.1020 -0.1682 117 TRP D CB  
13508 C CG  . TRP D  117 ? 0.2111 0.4261 0.3125 0.0634  -0.0979 -0.1664 117 TRP D CG  
13509 C CD1 . TRP D  117 ? 0.2285 0.4369 0.3239 0.0542  -0.0997 -0.1607 117 TRP D CD1 
13510 C CD2 . TRP D  117 ? 0.2094 0.4364 0.3103 0.0585  -0.0921 -0.1709 117 TRP D CD2 
13511 N NE1 . TRP D  117 ? 0.2154 0.4292 0.3059 0.0437  -0.0958 -0.1608 117 TRP D NE1 
13512 C CE2 . TRP D  117 ? 0.2222 0.4481 0.3157 0.0458  -0.0907 -0.1669 117 TRP D CE2 
13513 C CE3 . TRP D  117 ? 0.2078 0.4451 0.3121 0.0635  -0.0883 -0.1783 117 TRP D CE3 
13514 C CZ2 . TRP D  117 ? 0.2191 0.4518 0.3070 0.0374  -0.0843 -0.1682 117 TRP D CZ2 
13515 C CZ3 . TRP D  117 ? 0.2103 0.4532 0.3088 0.0554  -0.0799 -0.1786 117 TRP D CZ3 
13516 C CH2 . TRP D  117 ? 0.2139 0.4543 0.3039 0.0423  -0.0777 -0.1730 117 TRP D CH2 
13517 N N   . ILE D  118 ? 0.2805 0.4451 0.3468 0.0704  -0.0977 -0.1525 118 ILE D N   
13518 C CA  . ILE D  118 ? 0.2623 0.4112 0.3142 0.0652  -0.0968 -0.1445 118 ILE D CA  
13519 C C   . ILE D  118 ? 0.2533 0.4092 0.3026 0.0559  -0.0938 -0.1453 118 ILE D C   
13520 O O   . ILE D  118 ? 0.2503 0.4142 0.2997 0.0544  -0.0897 -0.1492 118 ILE D O   
13521 C CB  . ILE D  118 ? 0.2101 0.3453 0.2514 0.0690  -0.0950 -0.1402 118 ILE D CB  
13522 C CG1 . ILE D  118 ? 0.2111 0.3394 0.2536 0.0767  -0.0986 -0.1396 118 ILE D CG1 
13523 C CG2 . ILE D  118 ? 0.2114 0.3331 0.2399 0.0653  -0.0943 -0.1328 118 ILE D CG2 
13524 C CD1 . ILE D  118 ? 0.3538 0.4716 0.3877 0.0790  -0.0972 -0.1364 118 ILE D CD1 
13525 N N   . TYR D  119 ? 0.2178 0.3696 0.2633 0.0491  -0.0963 -0.1421 119 TYR D N   
13526 C CA  . TYR D  119 ? 0.2408 0.3972 0.2818 0.0386  -0.0947 -0.1427 119 TYR D CA  
13527 C C   . TYR D  119 ? 0.2261 0.3683 0.2508 0.0368  -0.0923 -0.1382 119 TYR D C   
13528 O O   . TYR D  119 ? 0.2244 0.3520 0.2410 0.0426  -0.0925 -0.1330 119 TYR D O   
13529 C CB  . TYR D  119 ? 0.2585 0.4126 0.2991 0.0310  -0.0995 -0.1409 119 TYR D CB  
13530 C CG  . TYR D  119 ? 0.2846 0.4177 0.3148 0.0344  -0.1039 -0.1345 119 TYR D CG  
13531 C CD1 . TYR D  119 ? 0.3256 0.4405 0.3394 0.0326  -0.1047 -0.1294 119 TYR D CD1 
13532 C CD2 . TYR D  119 ? 0.2875 0.4196 0.3239 0.0399  -0.1072 -0.1341 119 TYR D CD2 
13533 C CE1 . TYR D  119 ? 0.3333 0.4314 0.3382 0.0366  -0.1081 -0.1249 119 TYR D CE1 
13534 C CE2 . TYR D  119 ? 0.3238 0.4386 0.3500 0.0428  -0.1105 -0.1291 119 TYR D CE2 
13535 C CZ  . TYR D  119 ? 0.3421 0.4409 0.3532 0.0413  -0.1106 -0.1249 119 TYR D CZ  
13536 O OH  . TYR D  119 ? 0.3580 0.4423 0.3603 0.0452  -0.1134 -0.1213 119 TYR D OH  
13537 N N   . GLY D  120 ? 0.3645 0.5129 0.3847 0.0282  -0.0899 -0.1402 120 GLY D N   
13538 C CA  . GLY D  120 ? 0.2375 0.3728 0.2412 0.0255  -0.0885 -0.1359 120 GLY D CA  
13539 C C   . GLY D  120 ? 0.4749 0.5950 0.4663 0.0191  -0.0938 -0.1314 120 GLY D C   
13540 O O   . GLY D  120 ? 0.2510 0.3645 0.2444 0.0204  -0.0984 -0.1296 120 GLY D O   
13541 N N   . GLY D  121 ? 0.2602 0.3737 0.2376 0.0122  -0.0938 -0.1299 121 GLY D N   
13542 C CA  . GLY D  121 ? 0.2749 0.3685 0.2371 0.0081  -0.1003 -0.1254 121 GLY D CA  
13543 C C   . GLY D  121 ? 0.2785 0.3527 0.2266 0.0153  -0.1017 -0.1194 121 GLY D C   
13544 O O   . GLY D  121 ? 0.2971 0.3537 0.2351 0.0166  -0.1073 -0.1159 121 GLY D O   
13545 N N   . GLY D  122 ? 0.2703 0.3487 0.2190 0.0205  -0.0967 -0.1187 122 GLY D N   
13546 C CA  . GLY D  122 ? 0.2747 0.3396 0.2111 0.0253  -0.0977 -0.1137 122 GLY D CA  
13547 C C   . GLY D  122 ? 0.2701 0.3261 0.2080 0.0347  -0.0995 -0.1102 122 GLY D C   
13548 O O   . GLY D  122 ? 0.2759 0.3211 0.2045 0.0391  -0.1016 -0.1067 122 GLY D O   
13549 N N   . PHE D  123 ? 0.3122 0.3743 0.2619 0.0381  -0.0988 -0.1117 123 PHE D N   
13550 C CA  . PHE D  123 ? 0.3135 0.3693 0.2647 0.0459  -0.1003 -0.1095 123 PHE D CA  
13551 C C   . PHE D  123 ? 0.3051 0.3448 0.2447 0.0458  -0.1064 -0.1078 123 PHE D C   
13552 O O   . PHE D  123 ? 0.2846 0.3180 0.2227 0.0531  -0.1078 -0.1065 123 PHE D O   
13553 C CB  . PHE D  123 ? 0.2500 0.3068 0.2010 0.0530  -0.0971 -0.1069 123 PHE D CB  
13554 C CG  . PHE D  123 ? 0.2384 0.3073 0.1978 0.0533  -0.0920 -0.1082 123 PHE D CG  
13555 C CD1 . PHE D  123 ? 0.2290 0.3047 0.1987 0.0564  -0.0902 -0.1096 123 PHE D CD1 
13556 C CD2 . PHE D  123 ? 0.2392 0.3107 0.1947 0.0509  -0.0896 -0.1079 123 PHE D CD2 
13557 C CE1 . PHE D  123 ? 0.2216 0.3053 0.1972 0.0571  -0.0867 -0.1111 123 PHE D CE1 
13558 C CE2 . PHE D  123 ? 0.2309 0.3115 0.1929 0.0513  -0.0854 -0.1096 123 PHE D CE2 
13559 C CZ  . PHE D  123 ? 0.2225 0.3086 0.1945 0.0546  -0.0842 -0.1113 123 PHE D CZ  
13560 N N   . TYR D  124 ? 0.2866 0.3190 0.2173 0.0375  -0.1104 -0.1085 124 TYR D N   
13561 C CA  . TYR D  124 ? 0.3039 0.3184 0.2233 0.0367  -0.1175 -0.1076 124 TYR D CA  
13562 C C   . TYR D  124 ? 0.3097 0.3244 0.2326 0.0287  -0.1211 -0.1101 124 TYR D C   
13563 O O   . TYR D  124 ? 0.3257 0.3244 0.2392 0.0270  -0.1274 -0.1097 124 TYR D O   
13564 C CB  . TYR D  124 ? 0.4058 0.4041 0.3076 0.0341  -0.1221 -0.1053 124 TYR D CB  
13565 C CG  . TYR D  124 ? 0.4138 0.4143 0.3099 0.0218  -0.1227 -0.1063 124 TYR D CG  
13566 C CD1 . TYR D  124 ? 0.4120 0.4242 0.3095 0.0204  -0.1175 -0.1065 124 TYR D CD1 
13567 C CD2 . TYR D  124 ? 0.4464 0.4375 0.3350 0.0105  -0.1287 -0.1074 124 TYR D CD2 
13568 C CE1 . TYR D  124 ? 0.4741 0.4904 0.3655 0.0092  -0.1175 -0.1083 124 TYR D CE1 
13569 C CE2 . TYR D  124 ? 0.4903 0.4854 0.3748 -0.0027 -0.1271 -0.1069 124 TYR D CE2 
13570 C CZ  . TYR D  124 ? 0.5399 0.5486 0.4269 -0.0032 -0.1196 -0.1063 124 TYR D CZ  
13571 O OH  . TYR D  124 ? 0.6198 0.6352 0.5046 -0.0167 -0.1134 -0.1034 124 TYR D OH  
13572 N N   . SER D  125 ? 0.3319 0.3649 0.2686 0.0240  -0.1175 -0.1132 125 SER D N   
13573 C CA  . SER D  125 ? 0.3044 0.3416 0.2459 0.0143  -0.1212 -0.1161 125 SER D CA  
13574 C C   . SER D  125 ? 0.2879 0.3482 0.2490 0.0143  -0.1168 -0.1198 125 SER D C   
13575 O O   . SER D  125 ? 0.2732 0.3434 0.2424 0.0218  -0.1112 -0.1201 125 SER D O   
13576 C CB  . SER D  125 ? 0.3205 0.3538 0.2520 0.0013  -0.1245 -0.1171 125 SER D CB  
13577 O OG  . SER D  125 ? 0.3116 0.3624 0.2485 -0.0016 -0.1184 -0.1195 125 SER D OG  
13578 N N   . GLY D  126 ? 0.2921 0.3607 0.2609 0.0057  -0.1198 -0.1229 126 GLY D N   
13579 C CA  . GLY D  126 ? 0.2784 0.3706 0.2671 0.0062  -0.1164 -0.1270 126 GLY D CA  
13580 C C   . GLY D  126 ? 0.2757 0.3673 0.2719 0.0111  -0.1196 -0.1267 126 GLY D C   
13581 O O   . GLY D  126 ? 0.2830 0.3567 0.2689 0.0147  -0.1235 -0.1235 126 GLY D O   
13582 N N   . ALA D  127 ? 0.2663 0.3786 0.2804 0.0115  -0.1180 -0.1306 127 ALA D N   
13583 C CA  . ALA D  127 ? 0.2639 0.3784 0.2864 0.0162  -0.1212 -0.1307 127 ALA D CA  
13584 C C   . ALA D  127 ? 0.2843 0.4244 0.3271 0.0169  -0.1186 -0.1359 127 ALA D C   
13585 O O   . ALA D  127 ? 0.2534 0.4109 0.3043 0.0095  -0.1157 -0.1399 127 ALA D O   
13586 C CB  . ALA D  127 ? 0.4039 0.5100 0.4215 0.0073  -0.1281 -0.1299 127 ALA D CB  
13587 N N   . ALA D  128 ? 0.4226 0.5657 0.4734 0.0252  -0.1201 -0.1363 128 ALA D N   
13588 C CA  . ALA D  128 ? 0.4288 0.5940 0.4982 0.0295  -0.1181 -0.1415 128 ALA D CA  
13589 C C   . ALA D  128 ? 0.4199 0.6038 0.5038 0.0210  -0.1213 -0.1448 128 ALA D C   
13590 O O   . ALA D  128 ? 0.4438 0.6500 0.5454 0.0237  -0.1197 -0.1499 128 ALA D O   
13591 C CB  . ALA D  128 ? 0.2369 0.3952 0.3067 0.0420  -0.1191 -0.1404 128 ALA D CB  
13592 N N   . SER D  129 ? 0.2569 0.4320 0.3334 0.0106  -0.1261 -0.1422 129 SER D N   
13593 C CA  . SER D  129 ? 0.2632 0.4543 0.3526 0.0013  -0.1301 -0.1443 129 SER D CA  
13594 C C   . SER D  129 ? 0.2662 0.4776 0.3642 -0.0133 -0.1270 -0.1476 129 SER D C   
13595 O O   . SER D  129 ? 0.2718 0.5002 0.3822 -0.0233 -0.1293 -0.1493 129 SER D O   
13596 C CB  . SER D  129 ? 0.3350 0.5060 0.4122 -0.0028 -0.1380 -0.1402 129 SER D CB  
13597 O OG  . SER D  129 ? 0.3337 0.4810 0.3905 -0.0079 -0.1395 -0.1367 129 SER D OG  
13598 N N   . LEU D  130 ? 0.3857 0.5967 0.4771 -0.0153 -0.1213 -0.1483 130 LEU D N   
13599 C CA  . LEU D  130 ? 0.4010 0.6318 0.4980 -0.0302 -0.1166 -0.1512 130 LEU D CA  
13600 C C   . LEU D  130 ? 0.4367 0.7051 0.5598 -0.0312 -0.1116 -0.1573 130 LEU D C   
13601 O O   . LEU D  130 ? 0.4698 0.7472 0.6045 -0.0168 -0.1103 -0.1605 130 LEU D O   
13602 C CB  . LEU D  130 ? 0.3223 0.5468 0.4072 -0.0290 -0.1105 -0.1512 130 LEU D CB  
13603 C CG  . LEU D  130 ? 0.2728 0.4620 0.3319 -0.0277 -0.1145 -0.1452 130 LEU D CG  
13604 C CD1 . LEU D  130 ? 0.3500 0.5342 0.3993 -0.0245 -0.1067 -0.1434 130 LEU D CD1 
13605 C CD2 . LEU D  130 ? 0.3023 0.4765 0.3488 -0.0436 -0.1185 -0.1404 130 LEU D CD2 
13606 N N   . ASP D  131 ? 0.3930 0.6830 0.5247 -0.0484 -0.1086 -0.1588 131 ASP D N   
13607 C CA  . ASP D  131 ? 0.3972 0.7261 0.5549 -0.0499 -0.1030 -0.1645 131 ASP D CA  
13608 C C   . ASP D  131 ? 0.4080 0.7569 0.5756 -0.0388 -0.0939 -0.1709 131 ASP D C   
13609 O O   . ASP D  131 ? 0.4226 0.7951 0.6100 -0.0292 -0.0911 -0.1764 131 ASP D O   
13610 C CB  . ASP D  131 ? 0.3971 0.7459 0.5607 -0.0728 -0.1001 -0.1636 131 ASP D CB  
13611 C CG  . ASP D  131 ? 0.4341 0.7718 0.5962 -0.0821 -0.1097 -0.1593 131 ASP D CG  
13612 O OD1 . ASP D  131 ? 0.4224 0.7548 0.5907 -0.0698 -0.1163 -0.1595 131 ASP D OD1 
13613 O OD2 . ASP D  131 ? 0.4666 0.7995 0.6197 -0.1025 -0.1109 -0.1555 131 ASP D OD2 
13614 N N   . VAL D  132 ? 0.3575 0.6899 0.5075 -0.0385 -0.0880 -0.1680 132 VAL D N   
13615 C CA  . VAL D  132 ? 0.3395 0.6854 0.4946 -0.0288 -0.0787 -0.1729 132 VAL D CA  
13616 C C   . VAL D  132 ? 0.3667 0.7080 0.5279 -0.0077 -0.0834 -0.1778 132 VAL D C   
13617 O O   . VAL D  132 ? 0.3757 0.7329 0.5470 0.0024  -0.0778 -0.1843 132 VAL D O   
13618 C CB  . VAL D  132 ? 0.2482 0.5733 0.3800 -0.0336 -0.0722 -0.1675 132 VAL D CB  
13619 C CG1 . VAL D  132 ? 0.2466 0.5955 0.3855 -0.0329 -0.0601 -0.1727 132 VAL D CG1 
13620 C CG2 . VAL D  132 ? 0.2643 0.5748 0.3801 -0.0528 -0.0731 -0.1593 132 VAL D CG2 
13621 N N   . TYR D  133 ? 0.4408 0.7568 0.5931 -0.0011 -0.0930 -0.1737 133 TYR D N   
13622 C CA  . TYR D  133 ? 0.4221 0.7237 0.5732 0.0173  -0.0961 -0.1740 133 TYR D CA  
13623 C C   . TYR D  133 ? 0.4354 0.7469 0.6022 0.0250  -0.1003 -0.1760 133 TYR D C   
13624 O O   . TYR D  133 ? 0.4407 0.7371 0.6042 0.0384  -0.1042 -0.1751 133 TYR D O   
13625 C CB  . TYR D  133 ? 0.2606 0.5254 0.3892 0.0212  -0.1010 -0.1662 133 TYR D CB  
13626 C CG  . TYR D  133 ? 0.2677 0.5181 0.3780 0.0150  -0.0980 -0.1633 133 TYR D CG  
13627 C CD1 . TYR D  133 ? 0.2641 0.5285 0.3753 0.0110  -0.0898 -0.1669 133 TYR D CD1 
13628 C CD2 . TYR D  133 ? 0.2324 0.4532 0.3229 0.0137  -0.1021 -0.1557 133 TYR D CD2 
13629 C CE1 . TYR D  133 ? 0.2313 0.4774 0.3226 0.0056  -0.0859 -0.1615 133 TYR D CE1 
13630 C CE2 . TYR D  133 ? 0.2982 0.5048 0.3717 0.0093  -0.1000 -0.1527 133 TYR D CE2 
13631 C CZ  . TYR D  133 ? 0.3047 0.5230 0.3780 0.0050  -0.0922 -0.1553 133 TYR D CZ  
13632 O OH  . TYR D  133 ? 0.2424 0.4423 0.2961 0.0011  -0.0897 -0.1500 133 TYR D OH  
13633 N N   . ASP D  134 ? 0.4101 0.7461 0.5925 0.0156  -0.0997 -0.1781 134 ASP D N   
13634 C CA  . ASP D  134 ? 0.4171 0.7648 0.6149 0.0220  -0.1040 -0.1801 134 ASP D CA  
13635 C C   . ASP D  134 ? 0.3637 0.7173 0.5694 0.0397  -0.1021 -0.1865 134 ASP D C   
13636 O O   . ASP D  134 ? 0.3765 0.7502 0.5911 0.0421  -0.0946 -0.1932 134 ASP D O   
13637 C CB  . ASP D  134 ? 0.4968 0.8778 0.7129 0.0085  -0.1007 -0.1830 134 ASP D CB  
13638 C CG  . ASP D  134 ? 0.5158 0.9039 0.7434 0.0092  -0.1078 -0.1822 134 ASP D CG  
13639 O OD1 . ASP D  134 ? 0.5205 0.9055 0.7531 0.0245  -0.1118 -0.1843 134 ASP D OD1 
13640 O OD2 . ASP D  134 ? 0.5095 0.9057 0.7405 -0.0065 -0.1100 -0.1793 134 ASP D OD2 
13641 N N   . GLY D  135 ? 0.2305 0.5657 0.4318 0.0519  -0.1090 -0.1846 135 GLY D N   
13642 C CA  . GLY D  135 ? 0.2300 0.5640 0.4347 0.0681  -0.1090 -0.1899 135 GLY D CA  
13643 C C   . GLY D  135 ? 0.2365 0.5923 0.4601 0.0749  -0.1109 -0.1957 135 GLY D C   
13644 O O   . GLY D  135 ? 0.2408 0.5926 0.4661 0.0891  -0.1129 -0.2001 135 GLY D O   
13645 N N   . ARG D  136 ? 0.3294 0.7076 0.5664 0.0646  -0.1108 -0.1957 136 ARG D N   
13646 C CA  . ARG D  136 ? 0.3059 0.7052 0.5610 0.0703  -0.1138 -0.2003 136 ARG D CA  
13647 C C   . ARG D  136 ? 0.3176 0.7395 0.5861 0.0805  -0.1076 -0.2103 136 ARG D C   
13648 O O   . ARG D  136 ? 0.3305 0.7528 0.6049 0.0941  -0.1123 -0.2144 136 ARG D O   
13649 C CB  . ARG D  136 ? 0.3235 0.7438 0.5904 0.0550  -0.1146 -0.1981 136 ARG D CB  
13650 C CG  . ARG D  136 ? 0.3723 0.8277 0.6544 0.0438  -0.1047 -0.2030 136 ARG D CG  
13651 C CD  . ARG D  136 ? 0.4587 0.9223 0.7424 0.0231  -0.1055 -0.1975 136 ARG D CD  
13652 N NE  . ARG D  136 ? 0.5092 0.9578 0.7896 0.0215  -0.1167 -0.1918 136 ARG D NE  
13653 C CZ  . ARG D  136 ? 0.5224 0.9706 0.8010 0.0045  -0.1205 -0.1864 136 ARG D CZ  
13654 N NH1 . ARG D  136 ? 0.5032 0.9642 0.7826 -0.0133 -0.1142 -0.1854 136 ARG D NH1 
13655 N NH2 . ARG D  136 ? 0.5584 0.9922 0.8330 0.0046  -0.1310 -0.1819 136 ARG D NH2 
13656 N N   . PHE D  137 ? 0.3131 0.7520 0.5845 0.0742  -0.0974 -0.2142 137 PHE D N   
13657 C CA  . PHE D  137 ? 0.3234 0.7842 0.6060 0.0834  -0.0906 -0.2242 137 PHE D CA  
13658 C C   . PHE D  137 ? 0.3416 0.7786 0.6132 0.1007  -0.0937 -0.2275 137 PHE D C   
13659 O O   . PHE D  137 ? 0.3582 0.8003 0.6373 0.1137  -0.0966 -0.2335 137 PHE D O   
13660 C CB  . PHE D  137 ? 0.3432 0.8273 0.6293 0.0713  -0.0784 -0.2272 137 PHE D CB  
13661 C CG  . PHE D  137 ? 0.4413 0.9396 0.7313 0.0508  -0.0761 -0.2216 137 PHE D CG  
13662 C CD1 . PHE D  137 ? 0.4971 1.0275 0.8056 0.0432  -0.0737 -0.2239 137 PHE D CD1 
13663 C CD2 . PHE D  137 ? 0.5058 0.9841 0.7800 0.0386  -0.0771 -0.2138 137 PHE D CD2 
13664 C CE1 . PHE D  137 ? 0.5421 1.0837 0.8529 0.0224  -0.0724 -0.2182 137 PHE D CE1 
13665 C CE2 . PHE D  137 ? 0.5471 1.0344 0.8223 0.0186  -0.0763 -0.2084 137 PHE D CE2 
13666 C CZ  . PHE D  137 ? 0.5594 1.0780 0.8528 0.0098  -0.0739 -0.2104 137 PHE D CZ  
13667 N N   . LEU D  138 ? 0.3414 0.7519 0.5950 0.1006  -0.0939 -0.2234 138 LEU D N   
13668 C CA  . LEU D  138 ? 0.3465 0.7334 0.5887 0.1152  -0.0973 -0.2260 138 LEU D CA  
13669 C C   . LEU D  138 ? 0.3859 0.7573 0.6276 0.1274  -0.1080 -0.2253 138 LEU D C   
13670 O O   . LEU D  138 ? 0.3990 0.7666 0.6415 0.1408  -0.1108 -0.2313 138 LEU D O   
13671 C CB  . LEU D  138 ? 0.2406 0.6001 0.4633 0.1118  -0.0975 -0.2199 138 LEU D CB  
13672 C CG  . LEU D  138 ? 0.2330 0.6063 0.4549 0.1040  -0.0872 -0.2228 138 LEU D CG  
13673 C CD1 . LEU D  138 ? 0.2255 0.5732 0.4288 0.1004  -0.0884 -0.2165 138 LEU D CD1 
13674 C CD2 . LEU D  138 ? 0.2404 0.6258 0.4678 0.1143  -0.0821 -0.2329 138 LEU D CD2 
13675 N N   . ALA D  139 ? 0.4502 0.8130 0.6900 0.1223  -0.1144 -0.2179 139 ALA D N   
13676 C CA  . ALA D  139 ? 0.4796 0.8316 0.7201 0.1317  -0.1246 -0.2167 139 ALA D CA  
13677 C C   . ALA D  139 ? 0.4786 0.8580 0.7385 0.1392  -0.1246 -0.2252 139 ALA D C   
13678 O O   . ALA D  139 ? 0.4996 0.8727 0.7591 0.1530  -0.1284 -0.2305 139 ALA D O   
13679 C CB  . ALA D  139 ? 0.4428 0.7872 0.6801 0.1229  -0.1301 -0.2081 139 ALA D CB  
13680 N N   . GLN D  140 ? 0.4259 0.8359 0.7026 0.1296  -0.1206 -0.2263 140 GLN D N   
13681 C CA  . GLN D  140 ? 0.4688 0.9079 0.7656 0.1358  -0.1212 -0.2337 140 GLN D CA  
13682 C C   . GLN D  140 ? 0.4634 0.9146 0.7658 0.1474  -0.1161 -0.2441 140 GLN D C   
13683 O O   . GLN D  140 ? 0.4987 0.9487 0.8054 0.1617  -0.1223 -0.2491 140 GLN D O   
13684 C CB  . GLN D  140 ? 0.5606 1.0330 0.8745 0.1210  -0.1164 -0.2330 140 GLN D CB  
13685 C CG  . GLN D  140 ? 0.6320 1.1355 0.9678 0.1266  -0.1183 -0.2394 140 GLN D CG  
13686 C CD  . GLN D  140 ? 0.7095 1.2430 1.0582 0.1305  -0.1084 -0.2497 140 GLN D CD  
13687 O OE1 . GLN D  140 ? 0.7520 1.3072 1.1058 0.1176  -0.0978 -0.2507 140 GLN D OE1 
13688 N NE2 . GLN D  140 ? 0.7158 1.2496 1.0684 0.1481  -0.1119 -0.2574 140 GLN D NE2 
13689 N N   . VAL D  141 ? 0.3500 0.8127 0.6516 0.1412  -0.1052 -0.2473 141 VAL D N   
13690 C CA  . VAL D  141 ? 0.3122 0.7890 0.6190 0.1507  -0.0993 -0.2575 141 VAL D CA  
13691 C C   . VAL D  141 ? 0.3041 0.7504 0.5942 0.1635  -0.1029 -0.2596 141 VAL D C   
13692 O O   . VAL D  141 ? 0.3184 0.7691 0.6125 0.1764  -0.1040 -0.2677 141 VAL D O   
13693 C CB  . VAL D  141 ? 0.2919 0.8016 0.6079 0.1389  -0.0853 -0.2617 141 VAL D CB  
13694 C CG1 . VAL D  141 ? 0.5138 1.0626 0.8523 0.1342  -0.0824 -0.2653 141 VAL D CG1 
13695 C CG2 . VAL D  141 ? 0.2760 0.7784 0.5820 0.1223  -0.0802 -0.2539 141 VAL D CG2 
13696 N N   . GLU D  142 ? 0.3477 0.7633 0.6191 0.1599  -0.1050 -0.2526 142 GLU D N   
13697 C CA  . GLU D  142 ? 0.4015 0.7883 0.6576 0.1714  -0.1095 -0.2543 142 GLU D CA  
13698 C C   . GLU D  142 ? 0.4002 0.7564 0.6462 0.1800  -0.1227 -0.2492 142 GLU D C   
13699 O O   . GLU D  142 ? 0.4162 0.7451 0.6480 0.1885  -0.1283 -0.2491 142 GLU D O   
13700 C CB  . GLU D  142 ? 0.5933 0.9664 0.8349 0.1645  -0.1034 -0.2516 142 GLU D CB  
13701 C CG  . GLU D  142 ? 0.6664 1.0667 0.9152 0.1594  -0.0907 -0.2585 142 GLU D CG  
13702 C CD  . GLU D  142 ? 0.7344 1.1456 0.9895 0.1722  -0.0896 -0.2688 142 GLU D CD  
13703 O OE1 . GLU D  142 ? 0.7598 1.1463 1.0058 0.1849  -0.0981 -0.2702 142 GLU D OE1 
13704 O OE2 . GLU D  142 ? 0.7478 1.1924 1.0167 0.1692  -0.0803 -0.2754 142 GLU D OE2 
13705 N N   . GLY D  143 ? 0.3733 0.7345 0.6262 0.1769  -0.1279 -0.2447 143 GLY D N   
13706 C CA  . GLY D  143 ? 0.3823 0.7187 0.6271 0.1845  -0.1402 -0.2400 143 GLY D CA  
13707 C C   . GLY D  143 ? 0.3621 0.6633 0.5852 0.1806  -0.1442 -0.2309 143 GLY D C   
13708 O O   . GLY D  143 ? 0.3640 0.6386 0.5750 0.1886  -0.1537 -0.2280 143 GLY D O   
13709 N N   . ALA D  144 ? 0.4091 0.7110 0.6273 0.1680  -0.1371 -0.2260 144 ALA D N   
13710 C CA  . ALA D  144 ? 0.4390 0.7110 0.6369 0.1645  -0.1385 -0.2188 144 ALA D CA  
13711 C C   . ALA D  144 ? 0.4605 0.7213 0.6512 0.1553  -0.1414 -0.2088 144 ALA D C   
13712 O O   . ALA D  144 ? 0.4401 0.7191 0.6417 0.1482  -0.1401 -0.2074 144 ALA D O   
13713 C CB  . ALA D  144 ? 0.2830 0.5606 0.4780 0.1586  -0.1289 -0.2210 144 ALA D CB  
13714 N N   . VAL D  145 ? 0.5482 0.7789 0.7200 0.1555  -0.1459 -0.2019 145 VAL D N   
13715 C CA  . VAL D  145 ? 0.5169 0.7346 0.6786 0.1467  -0.1476 -0.1921 145 VAL D CA  
13716 C C   . VAL D  145 ? 0.5071 0.7204 0.6598 0.1370  -0.1403 -0.1882 145 VAL D C   
13717 O O   . VAL D  145 ? 0.5027 0.7020 0.6447 0.1391  -0.1388 -0.1881 145 VAL D O   
13718 C CB  . VAL D  145 ? 0.3683 0.5567 0.5138 0.1520  -0.1566 -0.1860 145 VAL D CB  
13719 C CG1 . VAL D  145 ? 0.3343 0.5096 0.4673 0.1425  -0.1563 -0.1763 145 VAL D CG1 
13720 C CG2 . VAL D  145 ? 0.3695 0.5601 0.5220 0.1609  -0.1653 -0.1884 145 VAL D CG2 
13721 N N   . LEU D  146 ? 0.4190 0.6430 0.5754 0.1262  -0.1367 -0.1846 146 LEU D N   
13722 C CA  . LEU D  146 ? 0.4040 0.6285 0.5546 0.1163  -0.1297 -0.1817 146 LEU D CA  
13723 C C   . LEU D  146 ? 0.3988 0.6053 0.5349 0.1083  -0.1311 -0.1720 146 LEU D C   
13724 O O   . LEU D  146 ? 0.4106 0.6219 0.5501 0.1027  -0.1336 -0.1691 146 LEU D O   
13725 C CB  . LEU D  146 ? 0.3739 0.6285 0.5410 0.1091  -0.1234 -0.1868 146 LEU D CB  
13726 C CG  . LEU D  146 ? 0.4134 0.6717 0.5758 0.1009  -0.1158 -0.1866 146 LEU D CG  
13727 C CD1 . LEU D  146 ? 0.4547 0.7362 0.6297 0.1041  -0.1096 -0.1961 146 LEU D CD1 
13728 C CD2 . LEU D  146 ? 0.4167 0.6819 0.5796 0.0871  -0.1141 -0.1818 146 LEU D CD2 
13729 N N   . VAL D  147 ? 0.3818 0.5684 0.5018 0.1078  -0.1297 -0.1672 147 VAL D N   
13730 C CA  . VAL D  147 ? 0.3178 0.4883 0.4235 0.1008  -0.1298 -0.1586 147 VAL D CA  
13731 C C   . VAL D  147 ? 0.2833 0.4572 0.3854 0.0919  -0.1233 -0.1570 147 VAL D C   
13732 O O   . VAL D  147 ? 0.2863 0.4663 0.3899 0.0922  -0.1187 -0.1607 147 VAL D O   
13733 C CB  . VAL D  147 ? 0.2443 0.3906 0.3333 0.1052  -0.1324 -0.1530 147 VAL D CB  
13734 C CG1 . VAL D  147 ? 0.2462 0.3799 0.3237 0.1002  -0.1340 -0.1453 147 VAL D CG1 
13735 C CG2 . VAL D  147 ? 0.2548 0.3956 0.3455 0.1151  -0.1389 -0.1557 147 VAL D CG2 
13736 N N   . SER D  148 ? 0.2979 0.4670 0.3940 0.0839  -0.1236 -0.1517 148 SER D N   
13737 C CA  . SER D  148 ? 0.3046 0.4705 0.3927 0.0756  -0.1190 -0.1488 148 SER D CA  
13738 C C   . SER D  148 ? 0.3127 0.4596 0.3858 0.0726  -0.1211 -0.1414 148 SER D C   
13739 O O   . SER D  148 ? 0.3146 0.4592 0.3883 0.0724  -0.1260 -0.1399 148 SER D O   
13740 C CB  . SER D  148 ? 0.2324 0.4187 0.3320 0.0667  -0.1170 -0.1527 148 SER D CB  
13741 O OG  . SER D  148 ? 0.2307 0.4223 0.3362 0.0621  -0.1217 -0.1519 148 SER D OG  
13742 N N   . MET D  149 ? 0.2281 0.3622 0.2881 0.0710  -0.1177 -0.1371 149 MET D N   
13743 C CA  . MET D  149 ? 0.2324 0.3501 0.2786 0.0697  -0.1192 -0.1311 149 MET D CA  
13744 C C   . MET D  149 ? 0.2332 0.3456 0.2711 0.0629  -0.1170 -0.1287 149 MET D C   
13745 O O   . MET D  149 ? 0.2297 0.3483 0.2694 0.0594  -0.1134 -0.1304 149 MET D O   
13746 C CB  . MET D  149 ? 0.2320 0.3370 0.2684 0.0760  -0.1183 -0.1274 149 MET D CB  
13747 C CG  . MET D  149 ? 0.2273 0.3266 0.2552 0.0753  -0.1130 -0.1248 149 MET D CG  
13748 S SD  . MET D  149 ? 0.2210 0.3307 0.2565 0.0764  -0.1091 -0.1295 149 MET D SD  
13749 C CE  . MET D  149 ? 0.2236 0.3304 0.2614 0.0846  -0.1122 -0.1311 149 MET D CE  
13750 N N   . ASN D  150 ? 0.2621 0.3627 0.2902 0.0610  -0.1197 -0.1252 150 ASN D N   
13751 C CA  . ASN D  150 ? 0.2965 0.3873 0.3134 0.0567  -0.1185 -0.1227 150 ASN D CA  
13752 C C   . ASN D  150 ? 0.2915 0.3724 0.2984 0.0625  -0.1150 -0.1191 150 ASN D C   
13753 O O   . ASN D  150 ? 0.2999 0.3779 0.3053 0.0680  -0.1152 -0.1177 150 ASN D O   
13754 C CB  . ASN D  150 ? 0.2753 0.3577 0.2862 0.0525  -0.1238 -0.1218 150 ASN D CB  
13755 C CG  . ASN D  150 ? 0.2903 0.3826 0.3096 0.0435  -0.1274 -0.1249 150 ASN D CG  
13756 O OD1 . ASN D  150 ? 0.2957 0.4040 0.3272 0.0410  -0.1254 -0.1282 150 ASN D OD1 
13757 N ND2 . ASN D  150 ? 0.2972 0.3812 0.3104 0.0381  -0.1327 -0.1243 150 ASN D ND2 
13758 N N   . TYR D  151 ? 0.2586 0.3353 0.2588 0.0607  -0.1121 -0.1176 151 TYR D N   
13759 C CA  . TYR D  151 ? 0.2768 0.3455 0.2678 0.0656  -0.1092 -0.1143 151 TYR D CA  
13760 C C   . TYR D  151 ? 0.2966 0.3557 0.2776 0.0634  -0.1103 -0.1130 151 TYR D C   
13761 O O   . TYR D  151 ? 0.3096 0.3685 0.2900 0.0572  -0.1119 -0.1142 151 TYR D O   
13762 C CB  . TYR D  151 ? 0.2299 0.3042 0.2235 0.0675  -0.1044 -0.1140 151 TYR D CB  
13763 C CG  . TYR D  151 ? 0.2281 0.3082 0.2245 0.0628  -0.1024 -0.1159 151 TYR D CG  
13764 C CD1 . TYR D  151 ? 0.6721 0.7639 0.6792 0.0605  -0.1024 -0.1201 151 TYR D CD1 
13765 C CD2 . TYR D  151 ? 0.2444 0.3196 0.2327 0.0609  -0.1008 -0.1140 151 TYR D CD2 
13766 C CE1 . TYR D  151 ? 0.2245 0.3237 0.2337 0.0557  -0.1001 -0.1227 151 TYR D CE1 
13767 C CE2 . TYR D  151 ? 0.2566 0.3368 0.2456 0.0558  -0.0991 -0.1157 151 TYR D CE2 
13768 C CZ  . TYR D  151 ? 0.2276 0.3203 0.2269 0.0528  -0.0985 -0.1202 151 TYR D CZ  
13769 O OH  . TYR D  151 ? 0.2818 0.3815 0.2813 0.0474  -0.0963 -0.1228 151 TYR D OH  
13770 N N   . ARG D  152 ? 0.2566 0.3081 0.2294 0.0686  -0.1099 -0.1110 152 ARG D N   
13771 C CA  . ARG D  152 ? 0.2981 0.3389 0.2605 0.0690  -0.1119 -0.1103 152 ARG D CA  
13772 C C   . ARG D  152 ? 0.2967 0.3383 0.2570 0.0669  -0.1095 -0.1095 152 ARG D C   
13773 O O   . ARG D  152 ? 0.2872 0.3349 0.2497 0.0695  -0.1052 -0.1083 152 ARG D O   
13774 C CB  . ARG D  152 ? 0.2619 0.2981 0.2178 0.0767  -0.1116 -0.1095 152 ARG D CB  
13775 C CG  . ARG D  152 ? 0.3040 0.3348 0.2570 0.0784  -0.1156 -0.1108 152 ARG D CG  
13776 C CD  . ARG D  152 ? 0.2860 0.3165 0.2338 0.0860  -0.1142 -0.1106 152 ARG D CD  
13777 N NE  . ARG D  152 ? 0.2606 0.3015 0.2139 0.0870  -0.1100 -0.1091 152 ARG D NE  
13778 C CZ  . ARG D  152 ? 0.2655 0.3104 0.2154 0.0918  -0.1074 -0.1085 152 ARG D CZ  
13779 N NH1 . ARG D  152 ? 0.2936 0.3352 0.2361 0.0975  -0.1081 -0.1099 152 ARG D NH1 
13780 N NH2 . ARG D  152 ? 0.2522 0.3048 0.2055 0.0910  -0.1046 -0.1068 152 ARG D NH2 
13781 N N   . VAL D  153 ? 0.2674 0.3020 0.2221 0.0611  -0.1128 -0.1100 153 VAL D N   
13782 C CA  . VAL D  153 ? 0.2690 0.3026 0.2192 0.0584  -0.1115 -0.1091 153 VAL D CA  
13783 C C   . VAL D  153 ? 0.3055 0.3242 0.2428 0.0625  -0.1152 -0.1080 153 VAL D C   
13784 O O   . VAL D  153 ? 0.3219 0.3325 0.2549 0.0675  -0.1183 -0.1086 153 VAL D O   
13785 C CB  . VAL D  153 ? 0.2737 0.3101 0.2252 0.0482  -0.1132 -0.1109 153 VAL D CB  
13786 C CG1 . VAL D  153 ? 0.2618 0.3141 0.2278 0.0463  -0.1105 -0.1134 153 VAL D CG1 
13787 C CG2 . VAL D  153 ? 0.3245 0.3480 0.2681 0.0430  -0.1200 -0.1117 153 VAL D CG2 
13788 N N   . GLY D  154 ? 0.3330 0.3476 0.2632 0.0612  -0.1153 -0.1068 154 GLY D N   
13789 C CA  . GLY D  154 ? 0.3507 0.3497 0.2679 0.0661  -0.1200 -0.1060 154 GLY D CA  
13790 C C   . GLY D  154 ? 0.3428 0.3427 0.2603 0.0780  -0.1190 -0.1063 154 GLY D C   
13791 O O   . GLY D  154 ? 0.2852 0.2989 0.2118 0.0813  -0.1136 -0.1060 154 GLY D O   
13792 N N   . THR D  155 ? 0.3789 0.3637 0.2856 0.0843  -0.1247 -0.1073 155 THR D N   
13793 C CA  . THR D  155 ? 0.3641 0.3507 0.2702 0.0966  -0.1244 -0.1089 155 THR D CA  
13794 C C   . THR D  155 ? 0.3637 0.3621 0.2789 0.0987  -0.1204 -0.1100 155 THR D C   
13795 O O   . THR D  155 ? 0.3356 0.3466 0.2561 0.1045  -0.1160 -0.1103 155 THR D O   
13796 C CB  . THR D  155 ? 0.3410 0.3071 0.2332 0.1037  -0.1325 -0.1110 155 THR D CB  
13797 O OG1 . THR D  155 ? 0.3511 0.3060 0.2396 0.0991  -0.1367 -0.1122 155 THR D OG1 
13798 C CG2 . THR D  155 ? 0.3563 0.3079 0.2371 0.1015  -0.1376 -0.1094 155 THR D CG2 
13799 N N   . PHE D  156 ? 0.5299 0.5246 0.4463 0.0931  -0.1222 -0.1105 156 PHE D N   
13800 C CA  . PHE D  156 ? 0.5511 0.5538 0.4736 0.0950  -0.1199 -0.1115 156 PHE D CA  
13801 C C   . PHE D  156 ? 0.5429 0.5626 0.4762 0.0932  -0.1132 -0.1097 156 PHE D C   
13802 O O   . PHE D  156 ? 0.5806 0.6086 0.5165 0.0981  -0.1102 -0.1101 156 PHE D O   
13803 C CB  . PHE D  156 ? 0.3681 0.3635 0.2899 0.0884  -0.1240 -0.1123 156 PHE D CB  
13804 C CG  . PHE D  156 ? 0.3281 0.3042 0.2379 0.0877  -0.1314 -0.1137 156 PHE D CG  
13805 C CD1 . PHE D  156 ? 0.3595 0.3245 0.2602 0.0966  -0.1355 -0.1163 156 PHE D CD1 
13806 C CD2 . PHE D  156 ? 0.3360 0.3041 0.2420 0.0782  -0.1346 -0.1128 156 PHE D CD2 
13807 C CE1 . PHE D  156 ? 0.3688 0.3125 0.2566 0.0964  -0.1433 -0.1177 156 PHE D CE1 
13808 C CE2 . PHE D  156 ? 0.3591 0.3062 0.2518 0.0765  -0.1423 -0.1138 156 PHE D CE2 
13809 C CZ  . PHE D  156 ? 0.3744 0.3080 0.2577 0.0859  -0.1469 -0.1161 156 PHE D CZ  
13810 N N   . GLY D  157 ? 0.4158 0.4403 0.3544 0.0859  -0.1111 -0.1082 157 GLY D N   
13811 C CA  . GLY D  157 ? 0.4083 0.4464 0.3560 0.0843  -0.1055 -0.1069 157 GLY D CA  
13812 C C   . GLY D  157 ? 0.3980 0.4432 0.3460 0.0879  -0.1018 -0.1057 157 GLY D C   
13813 O O   . GLY D  157 ? 0.4019 0.4565 0.3541 0.0896  -0.0981 -0.1051 157 GLY D O   
13814 N N   . PHE D  158 ? 0.3209 0.3614 0.2639 0.0879  -0.1031 -0.1053 158 PHE D N   
13815 C CA  . PHE D  158 ? 0.2800 0.3282 0.2239 0.0904  -0.1000 -0.1042 158 PHE D CA  
13816 C C   . PHE D  158 ? 0.2630 0.3104 0.2015 0.0988  -0.1017 -0.1053 158 PHE D C   
13817 O O   . PHE D  158 ? 0.2551 0.3111 0.1955 0.0999  -0.0991 -0.1045 158 PHE D O   
13818 C CB  . PHE D  158 ? 0.2975 0.3483 0.2435 0.0834  -0.0982 -0.1028 158 PHE D CB  
13819 C CG  . PHE D  158 ? 0.3057 0.3621 0.2594 0.0777  -0.0958 -0.1031 158 PHE D CG  
13820 C CD1 . PHE D  158 ? 0.3070 0.3590 0.2614 0.0731  -0.0982 -0.1043 158 PHE D CD1 
13821 C CD2 . PHE D  158 ? 0.3030 0.3691 0.2632 0.0773  -0.0918 -0.1026 158 PHE D CD2 
13822 C CE1 . PHE D  158 ? 0.3182 0.3769 0.2808 0.0696  -0.0966 -0.1056 158 PHE D CE1 
13823 C CE2 . PHE D  158 ? 0.2925 0.3624 0.2592 0.0739  -0.0907 -0.1036 158 PHE D CE2 
13824 C CZ  . PHE D  158 ? 0.3120 0.3790 0.2806 0.0708  -0.0930 -0.1053 158 PHE D CZ  
13825 N N   . LEU D  159 ? 0.3172 0.3545 0.2488 0.1051  -0.1063 -0.1075 159 LEU D N   
13826 C CA  . LEU D  159 ? 0.3343 0.3711 0.2606 0.1154  -0.1086 -0.1097 159 LEU D CA  
13827 C C   . LEU D  159 ? 0.3316 0.3860 0.2641 0.1202  -0.1038 -0.1111 159 LEU D C   
13828 O O   . LEU D  159 ? 0.3532 0.4122 0.2884 0.1200  -0.1020 -0.1117 159 LEU D O   
13829 C CB  . LEU D  159 ? 0.2999 0.3205 0.2165 0.1223  -0.1153 -0.1126 159 LEU D CB  
13830 C CG  . LEU D  159 ? 0.3314 0.3486 0.2411 0.1350  -0.1194 -0.1161 159 LEU D CG  
13831 C CD1 . LEU D  159 ? 0.3361 0.3290 0.2328 0.1384  -0.1282 -0.1176 159 LEU D CD1 
13832 C CD2 . LEU D  159 ? 0.3103 0.3432 0.2241 0.1450  -0.1165 -0.1200 159 LEU D CD2 
13833 N N   . ALA D  160 ? 0.2704 0.3351 0.2045 0.1238  -0.1022 -0.1114 160 ALA D N   
13834 C CA  . ALA D  160 ? 0.2611 0.3455 0.2019 0.1245  -0.0969 -0.1119 160 ALA D CA  
13835 C C   . ALA D  160 ? 0.2752 0.3700 0.2149 0.1345  -0.0976 -0.1154 160 ALA D C   
13836 O O   . ALA D  160 ? 0.2814 0.3725 0.2183 0.1370  -0.1002 -0.1155 160 ALA D O   
13837 C CB  . ALA D  160 ? 0.2478 0.3392 0.1946 0.1143  -0.0928 -0.1080 160 ALA D CB  
13838 N N   . LEU D  161 ? 0.3589 0.4684 0.3006 0.1401  -0.0953 -0.1184 161 LEU D N   
13839 C CA  . LEU D  161 ? 0.3908 0.5171 0.3337 0.1494  -0.0947 -0.1225 161 LEU D CA  
13840 C C   . LEU D  161 ? 0.4151 0.5638 0.3652 0.1427  -0.0887 -0.1208 161 LEU D C   
13841 O O   . LEU D  161 ? 0.4544 0.6168 0.4055 0.1451  -0.0863 -0.1228 161 LEU D O   
13842 C CB  . LEU D  161 ? 0.3036 0.4310 0.2418 0.1630  -0.0976 -0.1288 161 LEU D CB  
13843 C CG  . LEU D  161 ? 0.3085 0.4149 0.2378 0.1727  -0.1053 -0.1318 161 LEU D CG  
13844 C CD1 . LEU D  161 ? 0.3291 0.4401 0.2544 0.1883  -0.1083 -0.1391 161 LEU D CD1 
13845 C CD2 . LEU D  161 ? 0.3028 0.4077 0.2309 0.1741  -0.1073 -0.1315 161 LEU D CD2 
13846 N N   . PRO D  162 ? 0.3526 0.5048 0.3066 0.1339  -0.0869 -0.1169 162 PRO D N   
13847 C CA  . PRO D  162 ? 0.3566 0.5235 0.3160 0.1240  -0.0824 -0.1137 162 PRO D CA  
13848 C C   . PRO D  162 ? 0.4053 0.5969 0.3671 0.1280  -0.0796 -0.1167 162 PRO D C   
13849 O O   . PRO D  162 ? 0.4130 0.6176 0.3756 0.1374  -0.0802 -0.1212 162 PRO D O   
13850 C CB  . PRO D  162 ? 0.3840 0.5527 0.3459 0.1194  -0.0827 -0.1115 162 PRO D CB  
13851 C CG  . PRO D  162 ? 0.3840 0.5316 0.3411 0.1215  -0.0867 -0.1110 162 PRO D CG  
13852 C CD  . PRO D  162 ? 0.3959 0.5362 0.3478 0.1329  -0.0899 -0.1153 162 PRO D CD  
13853 N N   . GLY D  163 ? 0.4429 0.6416 0.4053 0.1210  -0.0769 -0.1145 163 GLY D N   
13854 C CA  . GLY D  163 ? 0.4845 0.7089 0.4483 0.1229  -0.0739 -0.1168 163 GLY D CA  
13855 C C   . GLY D  163 ? 0.5329 0.7580 0.4922 0.1306  -0.0741 -0.1202 163 GLY D C   
13856 O O   . GLY D  163 ? 0.5224 0.7663 0.4811 0.1293  -0.0713 -0.1208 163 GLY D O   
13857 N N   . SER D  164 ? 0.6927 0.8972 0.6481 0.1380  -0.0777 -0.1222 164 SER D N   
13858 C CA  . SER D  164 ? 0.7471 0.9485 0.6974 0.1455  -0.0790 -0.1255 164 SER D CA  
13859 C C   . SER D  164 ? 0.7687 0.9586 0.7153 0.1358  -0.0786 -0.1210 164 SER D C   
13860 O O   . SER D  164 ? 0.7446 0.9198 0.6922 0.1264  -0.0791 -0.1163 164 SER D O   
13861 C CB  . SER D  164 ? 0.6881 0.8690 0.6342 0.1557  -0.0844 -0.1290 164 SER D CB  
13862 O OG  . SER D  164 ? 0.6756 0.8316 0.6196 0.1480  -0.0867 -0.1247 164 SER D OG  
13863 N N   . ARG D  165 ? 0.6409 0.8383 0.5829 0.1388  -0.0778 -0.1228 165 ARG D N   
13864 C CA  . ARG D  165 ? 0.6557 0.8407 0.5920 0.1317  -0.0783 -0.1194 165 ARG D CA  
13865 C C   . ARG D  165 ? 0.5255 0.6861 0.4585 0.1360  -0.0830 -0.1206 165 ARG D C   
13866 O O   . ARG D  165 ? 0.4644 0.6100 0.3948 0.1294  -0.0845 -0.1173 165 ARG D O   
13867 C CB  . ARG D  165 ? 1.1726 1.3755 1.1034 0.1326  -0.0757 -0.1207 165 ARG D CB  
13868 C CG  . ARG D  165 ? 1.3113 1.5302 1.2417 0.1465  -0.0755 -0.1278 165 ARG D CG  
13869 C CD  . ARG D  165 ? 1.4330 1.6649 1.3556 0.1470  -0.0732 -0.1290 165 ARG D CD  
13870 N NE  . ARG D  165 ? 1.5145 1.7678 1.4365 0.1365  -0.0683 -0.1253 165 ARG D NE  
13871 C CZ  . ARG D  165 ? 1.5619 1.8235 1.4747 0.1314  -0.0659 -0.1236 165 ARG D CZ  
13872 N NH1 . ARG D  165 ? 1.5770 1.8271 1.4810 0.1361  -0.0677 -0.1257 165 ARG D NH1 
13873 N NH2 . ARG D  165 ? 1.5650 1.8455 1.4762 0.1205  -0.0619 -0.1196 165 ARG D NH2 
13874 N N   . GLU D  166 ? 0.5302 0.6873 0.4629 0.1471  -0.0859 -0.1254 166 GLU D N   
13875 C CA  . GLU D  166 ? 0.5675 0.7027 0.4951 0.1522  -0.0913 -0.1273 166 GLU D CA  
13876 C C   . GLU D  166 ? 0.5005 0.6148 0.4298 0.1463  -0.0941 -0.1242 166 GLU D C   
13877 O O   . GLU D  166 ? 0.5041 0.6005 0.4294 0.1449  -0.0980 -0.1238 166 GLU D O   
13878 C CB  . GLU D  166 ? 0.9678 1.1064 0.8926 0.1672  -0.0946 -0.1339 166 GLU D CB  
13879 C CG  . GLU D  166 ? 1.1082 1.2697 1.0313 0.1743  -0.0921 -0.1379 166 GLU D CG  
13880 C CD  . GLU D  166 ? 1.2397 1.3955 1.1553 0.1716  -0.0923 -0.1375 166 GLU D CD  
13881 O OE1 . GLU D  166 ? 1.2522 1.4111 1.1673 0.1605  -0.0887 -0.1328 166 GLU D OE1 
13882 O OE2 . GLU D  166 ? 1.3161 1.4630 1.2250 0.1808  -0.0967 -0.1418 166 GLU D OE2 
13883 N N   . ALA D  167 ? 0.4256 0.5432 0.3603 0.1429  -0.0925 -0.1222 167 ALA D N   
13884 C CA  . ALA D  167 ? 0.3421 0.4438 0.2785 0.1359  -0.0942 -0.1188 167 ALA D CA  
13885 C C   . ALA D  167 ? 0.3125 0.4240 0.2553 0.1277  -0.0901 -0.1151 167 ALA D C   
13886 O O   . ALA D  167 ? 0.3066 0.4197 0.2512 0.1290  -0.0903 -0.1152 167 ALA D O   
13887 C CB  . ALA D  167 ? 0.3861 0.4759 0.3186 0.1431  -0.0991 -0.1213 167 ALA D CB  
13888 N N   . PRO D  168 ? 0.3382 0.4550 0.2832 0.1196  -0.0872 -0.1119 168 PRO D N   
13889 C CA  . PRO D  168 ? 0.3193 0.4471 0.2690 0.1125  -0.0838 -0.1089 168 PRO D CA  
13890 C C   . PRO D  168 ? 0.3311 0.4493 0.2842 0.1067  -0.0843 -0.1065 168 PRO D C   
13891 O O   . PRO D  168 ? 0.3318 0.4576 0.2880 0.1024  -0.0824 -0.1048 168 PRO D O   
13892 C CB  . PRO D  168 ? 0.4035 0.5337 0.3517 0.1059  -0.0826 -0.1063 168 PRO D CB  
13893 C CG  . PRO D  168 ? 0.4510 0.5777 0.3939 0.1112  -0.0843 -0.1085 168 PRO D CG  
13894 C CD  . PRO D  168 ? 0.4745 0.5867 0.4166 0.1167  -0.0878 -0.1109 168 PRO D CD  
13895 N N   . GLY D  169 ? 0.3793 0.4820 0.3312 0.1062  -0.0871 -0.1064 169 GLY D N   
13896 C CA  . GLY D  169 ? 0.3605 0.4558 0.3148 0.1009  -0.0875 -0.1045 169 GLY D CA  
13897 C C   . GLY D  169 ? 0.3226 0.4159 0.2807 0.0931  -0.0863 -0.1022 169 GLY D C   
13898 O O   . GLY D  169 ? 0.3199 0.4182 0.2785 0.0909  -0.0852 -0.1013 169 GLY D O   
13899 N N   . ASN D  170 ? 0.2905 0.3765 0.2504 0.0894  -0.0872 -0.1017 170 ASN D N   
13900 C CA  . ASN D  170 ? 0.2984 0.3820 0.2624 0.0838  -0.0869 -0.1010 170 ASN D CA  
13901 C C   . ASN D  170 ? 0.3240 0.4036 0.2883 0.0843  -0.0888 -0.1016 170 ASN D C   
13902 O O   . ASN D  170 ? 0.2188 0.2987 0.1865 0.0813  -0.0889 -0.1013 170 ASN D O   
13903 C CB  . ASN D  170 ? 0.2780 0.3686 0.2447 0.0799  -0.0845 -0.0997 170 ASN D CB  
13904 C CG  . ASN D  170 ? 0.2441 0.3394 0.2105 0.0786  -0.0829 -0.0992 170 ASN D CG  
13905 O OD1 . ASN D  170 ? 0.2268 0.3184 0.1922 0.0786  -0.0836 -0.0996 170 ASN D OD1 
13906 N ND2 . ASN D  170 ? 0.2113 0.3151 0.1777 0.0768  -0.0815 -0.0981 170 ASN D ND2 
13907 N N   . VAL D  171 ? 0.2279 0.3032 0.1883 0.0884  -0.0909 -0.1027 171 VAL D N   
13908 C CA  . VAL D  171 ? 0.2310 0.3027 0.1909 0.0886  -0.0931 -0.1031 171 VAL D CA  
13909 C C   . VAL D  171 ? 0.2299 0.2968 0.1946 0.0847  -0.0952 -0.1039 171 VAL D C   
13910 O O   . VAL D  171 ? 0.2304 0.2967 0.1972 0.0839  -0.0969 -0.1041 171 VAL D O   
13911 C CB  . VAL D  171 ? 0.2397 0.3080 0.1934 0.0941  -0.0952 -0.1047 171 VAL D CB  
13912 C CG1 . VAL D  171 ? 0.2404 0.3181 0.1909 0.0981  -0.0927 -0.1048 171 VAL D CG1 
13913 C CG2 . VAL D  171 ? 0.3268 0.3867 0.2774 0.0962  -0.0980 -0.1063 171 VAL D CG2 
13914 N N   . GLY D  172 ? 0.2293 0.2942 0.1955 0.0822  -0.0954 -0.1044 172 GLY D N   
13915 C CA  . GLY D  172 ? 0.2282 0.2927 0.1999 0.0779  -0.0969 -0.1058 172 GLY D CA  
13916 C C   . GLY D  172 ? 0.2225 0.2932 0.2008 0.0766  -0.0952 -0.1062 172 GLY D C   
13917 O O   . GLY D  172 ? 0.2514 0.3232 0.2349 0.0760  -0.0973 -0.1079 172 GLY D O   
13918 N N   . LEU D  173 ? 0.2924 0.3669 0.2703 0.0764  -0.0922 -0.1050 173 LEU D N   
13919 C CA  . LEU D  173 ? 0.2967 0.3748 0.2788 0.0756  -0.0915 -0.1055 173 LEU D CA  
13920 C C   . LEU D  173 ? 0.3243 0.4005 0.3048 0.0776  -0.0937 -0.1046 173 LEU D C   
13921 O O   . LEU D  173 ? 0.3601 0.4360 0.3443 0.0780  -0.0958 -0.1059 173 LEU D O   
13922 C CB  . LEU D  173 ? 0.2474 0.3288 0.2275 0.0742  -0.0885 -0.1042 173 LEU D CB  
13923 C CG  . LEU D  173 ? 0.2551 0.3379 0.2358 0.0718  -0.0868 -0.1052 173 LEU D CG  
13924 C CD1 . LEU D  173 ? 0.2076 0.2938 0.1866 0.0701  -0.0844 -0.1041 173 LEU D CD1 
13925 C CD2 . LEU D  173 ? 0.2091 0.2937 0.1959 0.0701  -0.0876 -0.1088 173 LEU D CD2 
13926 N N   . LEU D  174 ? 0.2582 0.3332 0.2324 0.0794  -0.0937 -0.1026 174 LEU D N   
13927 C CA  . LEU D  174 ? 0.2251 0.2985 0.1957 0.0805  -0.0960 -0.1014 174 LEU D CA  
13928 C C   . LEU D  174 ? 0.2524 0.3216 0.2256 0.0817  -0.0999 -0.1030 174 LEU D C   
13929 O O   . LEU D  174 ? 0.2348 0.3018 0.2070 0.0823  -0.1031 -0.1025 174 LEU D O   
13930 C CB  . LEU D  174 ? 0.5565 0.6321 0.5196 0.0823  -0.0947 -0.0999 174 LEU D CB  
13931 C CG  . LEU D  174 ? 0.2261 0.3087 0.1871 0.0809  -0.0915 -0.0984 174 LEU D CG  
13932 C CD1 . LEU D  174 ? 0.2311 0.3188 0.1854 0.0831  -0.0908 -0.0977 174 LEU D CD1 
13933 C CD2 . LEU D  174 ? 0.2256 0.3089 0.1873 0.0770  -0.0921 -0.0970 174 LEU D CD2 
13934 N N   . ASP D  175 ? 0.3343 0.4021 0.3102 0.0815  -0.1006 -0.1049 175 ASP D N   
13935 C CA  . ASP D  175 ? 0.2320 0.2980 0.2123 0.0813  -0.1045 -0.1069 175 ASP D CA  
13936 C C   . ASP D  175 ? 0.2290 0.2991 0.2180 0.0809  -0.1056 -0.1092 175 ASP D C   
13937 O O   . ASP D  175 ? 0.2410 0.3103 0.2322 0.0827  -0.1094 -0.1099 175 ASP D O   
13938 C CB  . ASP D  175 ? 0.2947 0.3591 0.2759 0.0792  -0.1053 -0.1085 175 ASP D CB  
13939 C CG  . ASP D  175 ? 0.3348 0.3932 0.3071 0.0811  -0.1057 -0.1075 175 ASP D CG  
13940 O OD1 . ASP D  175 ? 0.3620 0.4194 0.3288 0.0843  -0.1057 -0.1063 175 ASP D OD1 
13941 O OD2 . ASP D  175 ? 0.3352 0.3897 0.3054 0.0796  -0.1067 -0.1083 175 ASP D OD2 
13942 N N   . GLN D  176 ? 0.2955 0.3702 0.2892 0.0791  -0.1029 -0.1108 176 GLN D N   
13943 C CA  . GLN D  176 ? 0.2214 0.3014 0.2238 0.0800  -0.1038 -0.1144 176 GLN D CA  
13944 C C   . GLN D  176 ? 0.3230 0.3993 0.3233 0.0832  -0.1064 -0.1135 176 GLN D C   
13945 O O   . GLN D  176 ? 0.2291 0.3057 0.2344 0.0861  -0.1106 -0.1160 176 GLN D O   
13946 C CB  . GLN D  176 ? 0.2163 0.3010 0.2209 0.0779  -0.1000 -0.1159 176 GLN D CB  
13947 C CG  . GLN D  176 ? 0.2153 0.3014 0.2185 0.0739  -0.0980 -0.1157 176 GLN D CG  
13948 C CD  . GLN D  176 ? 0.2120 0.3028 0.2161 0.0714  -0.0945 -0.1172 176 GLN D CD  
13949 O OE1 . GLN D  176 ? 0.2099 0.3025 0.2153 0.0728  -0.0930 -0.1182 176 GLN D OE1 
13950 N NE2 . GLN D  176 ? 0.2135 0.3052 0.2157 0.0672  -0.0937 -0.1174 176 GLN D NE2 
13951 N N   . ARG D  177 ? 0.2589 0.3317 0.2514 0.0824  -0.1045 -0.1100 177 ARG D N   
13952 C CA  . ARG D  177 ? 0.2612 0.3291 0.2490 0.0837  -0.1076 -0.1084 177 ARG D CA  
13953 C C   . ARG D  177 ? 0.2850 0.3484 0.2703 0.0859  -0.1126 -0.1074 177 ARG D C   
13954 O O   . ARG D  177 ? 0.3198 0.3799 0.3072 0.0889  -0.1177 -0.1089 177 ARG D O   
13955 C CB  . ARG D  177 ? 0.3092 0.3762 0.2880 0.0807  -0.1050 -0.1043 177 ARG D CB  
13956 C CG  . ARG D  177 ? 0.3581 0.4191 0.3296 0.0804  -0.1094 -0.1018 177 ARG D CG  
13957 C CD  . ARG D  177 ? 0.2432 0.3059 0.2063 0.0760  -0.1072 -0.0981 177 ARG D CD  
13958 N NE  . ARG D  177 ? 0.3502 0.4155 0.3162 0.0738  -0.1044 -0.0995 177 ARG D NE  
13959 C CZ  . ARG D  177 ? 0.3874 0.4584 0.3500 0.0700  -0.1005 -0.0975 177 ARG D CZ  
13960 N NH1 . ARG D  177 ? 0.3733 0.4492 0.3303 0.0688  -0.0988 -0.0946 177 ARG D NH1 
13961 N NH2 . ARG D  177 ? 0.4133 0.4861 0.3783 0.0677  -0.0985 -0.0989 177 ARG D NH2 
13962 N N   . LEU D  178 ? 0.3472 0.4099 0.3276 0.0851  -0.1120 -0.1052 178 LEU D N   
13963 C CA  . LEU D  178 ? 0.2492 0.3076 0.2261 0.0869  -0.1169 -0.1043 178 LEU D CA  
13964 C C   . LEU D  178 ? 0.2509 0.3107 0.2376 0.0895  -0.1213 -0.1081 178 LEU D C   
13965 O O   . LEU D  178 ? 0.2595 0.3152 0.2450 0.0920  -0.1270 -0.1079 178 LEU D O   
13966 C CB  . LEU D  178 ? 0.2507 0.3087 0.2218 0.0861  -0.1154 -0.1030 178 LEU D CB  
13967 C CG  . LEU D  178 ? 0.2614 0.3147 0.2258 0.0874  -0.1204 -0.1014 178 LEU D CG  
13968 C CD1 . LEU D  178 ? 0.2685 0.3188 0.2233 0.0867  -0.1219 -0.0977 178 LEU D CD1 
13969 C CD2 . LEU D  178 ? 0.2643 0.3169 0.2232 0.0874  -0.1195 -0.1015 178 LEU D CD2 
13970 N N   . ALA D  179 ? 0.2440 0.3104 0.2403 0.0886  -0.1192 -0.1118 179 ALA D N   
13971 C CA  . ALA D  179 ? 0.2454 0.3171 0.2527 0.0907  -0.1231 -0.1163 179 ALA D CA  
13972 C C   . ALA D  179 ? 0.2542 0.3253 0.2654 0.0952  -0.1261 -0.1188 179 ALA D C   
13973 O O   . ALA D  179 ? 0.2546 0.3269 0.2720 0.0993  -0.1315 -0.1217 179 ALA D O   
13974 C CB  . ALA D  179 ? 0.3507 0.4316 0.3667 0.0876  -0.1200 -0.1197 179 ALA D CB  
13975 N N   . LEU D  180 ? 0.3339 0.4026 0.3413 0.0948  -0.1232 -0.1179 180 LEU D N   
13976 C CA  . LEU D  180 ? 0.3489 0.4139 0.3577 0.0991  -0.1270 -0.1205 180 LEU D CA  
13977 C C   . LEU D  180 ? 0.3870 0.4401 0.3864 0.1016  -0.1339 -0.1168 180 LEU D C   
13978 O O   . LEU D  180 ? 0.4491 0.4982 0.4517 0.1073  -0.1404 -0.1198 180 LEU D O   
13979 C CB  . LEU D  180 ? 0.2466 0.3119 0.2530 0.0969  -0.1226 -0.1206 180 LEU D CB  
13980 C CG  . LEU D  180 ? 0.2402 0.3155 0.2573 0.0981  -0.1197 -0.1272 180 LEU D CG  
13981 C CD1 . LEU D  180 ? 0.2342 0.3212 0.2613 0.0970  -0.1177 -0.1304 180 LEU D CD1 
13982 C CD2 . LEU D  180 ? 0.2344 0.3101 0.2467 0.0936  -0.1139 -0.1254 180 LEU D CD2 
13983 N N   . GLN D  181 ? 0.3361 0.3838 0.3234 0.0976  -0.1328 -0.1106 181 GLN D N   
13984 C CA  . GLN D  181 ? 0.3686 0.4059 0.3453 0.0985  -0.1393 -0.1064 181 GLN D CA  
13985 C C   . GLN D  181 ? 0.3554 0.3926 0.3367 0.1025  -0.1447 -0.1080 181 GLN D C   
13986 O O   . GLN D  181 ? 0.4051 0.4339 0.3833 0.1066  -0.1525 -0.1076 181 GLN D O   
13987 C CB  . GLN D  181 ? 0.5551 0.5909 0.5188 0.0931  -0.1363 -0.1004 181 GLN D CB  
13988 C CG  . GLN D  181 ? 0.6713 0.7009 0.6232 0.0895  -0.1373 -0.0962 181 GLN D CG  
13989 C CD  . GLN D  181 ? 0.7724 0.8099 0.7215 0.0841  -0.1293 -0.0945 181 GLN D CD  
13990 O OE1 . GLN D  181 ? 0.7788 0.8236 0.7303 0.0834  -0.1242 -0.0948 181 GLN D OE1 
13991 N NE2 . GLN D  181 ? 0.8198 0.8554 0.7638 0.0804  -0.1290 -0.0929 181 GLN D NE2 
13992 N N   . TRP D  182 ? 0.3602 0.4059 0.3480 0.1009  -0.1414 -0.1097 182 TRP D N   
13993 C CA  . TRP D  182 ? 0.3515 0.3995 0.3452 0.1036  -0.1465 -0.1118 182 TRP D CA  
13994 C C   . TRP D  182 ? 0.3526 0.4029 0.3573 0.1097  -0.1513 -0.1171 182 TRP D C   
13995 O O   . TRP D  182 ? 0.3660 0.4112 0.3701 0.1142  -0.1589 -0.1172 182 TRP D O   
13996 C CB  . TRP D  182 ? 0.2765 0.3340 0.2775 0.1003  -0.1426 -0.1140 182 TRP D CB  
13997 C CG  . TRP D  182 ? 0.2837 0.3432 0.2883 0.1013  -0.1483 -0.1150 182 TRP D CG  
13998 C CD1 . TRP D  182 ? 0.3791 0.4335 0.3742 0.0995  -0.1506 -0.1117 182 TRP D CD1 
13999 C CD2 . TRP D  182 ? 0.2851 0.3538 0.3038 0.1041  -0.1524 -0.1200 182 TRP D CD2 
14000 N NE1 . TRP D  182 ? 0.3496 0.4082 0.3516 0.1006  -0.1564 -0.1139 182 TRP D NE1 
14001 C CE2 . TRP D  182 ? 0.3276 0.3957 0.3446 0.1033  -0.1575 -0.1188 182 TRP D CE2 
14002 C CE3 . TRP D  182 ? 0.2811 0.3598 0.3139 0.1073  -0.1523 -0.1257 182 TRP D CE3 
14003 C CZ2 . TRP D  182 ? 0.2973 0.3751 0.3268 0.1052  -0.1626 -0.1227 182 TRP D CZ2 
14004 C CZ3 . TRP D  182 ? 0.2848 0.3743 0.3305 0.1096  -0.1569 -0.1300 182 TRP D CZ3 
14005 C CH2 . TRP D  182 ? 0.2947 0.3839 0.3390 0.1083  -0.1621 -0.1282 182 TRP D CH2 
14006 N N   . VAL D  183 ? 0.2798 0.3380 0.2941 0.1104  -0.1472 -0.1219 183 VAL D N   
14007 C CA  . VAL D  183 ? 0.3510 0.4139 0.3769 0.1172  -0.1513 -0.1286 183 VAL D CA  
14008 C C   . VAL D  183 ? 0.3308 0.3785 0.3484 0.1230  -0.1593 -0.1272 183 VAL D C   
14009 O O   . VAL D  183 ? 0.3397 0.3856 0.3621 0.1299  -0.1666 -0.1304 183 VAL D O   
14010 C CB  . VAL D  183 ? 0.4385 0.5123 0.4738 0.1168  -0.1453 -0.1343 183 VAL D CB  
14011 C CG1 . VAL D  183 ? 0.4429 0.5118 0.4797 0.1239  -0.1493 -0.1389 183 VAL D CG1 
14012 C CG2 . VAL D  183 ? 0.4508 0.5424 0.5014 0.1159  -0.1431 -0.1397 183 VAL D CG2 
14013 N N   . GLN D  184 ? 0.3056 0.3420 0.3095 0.1197  -0.1584 -0.1218 184 GLN D N   
14014 C CA  . GLN D  184 ? 0.3317 0.3514 0.3251 0.1235  -0.1665 -0.1196 184 GLN D CA  
14015 C C   . GLN D  184 ? 0.3352 0.3449 0.3208 0.1258  -0.1747 -0.1154 184 GLN D C   
14016 O O   . GLN D  184 ? 0.3521 0.3502 0.3353 0.1325  -0.1839 -0.1165 184 GLN D O   
14017 C CB  . GLN D  184 ? 0.4336 0.4456 0.4136 0.1170  -0.1633 -0.1140 184 GLN D CB  
14018 C CG  . GLN D  184 ? 0.4398 0.4350 0.4104 0.1198  -0.1709 -0.1135 184 GLN D CG  
14019 C CD  . GLN D  184 ? 0.4468 0.4445 0.4285 0.1266  -0.1721 -0.1223 184 GLN D CD  
14020 O OE1 . GLN D  184 ? 0.3767 0.3895 0.3744 0.1309  -0.1688 -0.1294 184 GLN D OE1 
14021 N NE2 . GLN D  184 ? 0.5196 0.5026 0.4919 0.1272  -0.1771 -0.1222 184 GLN D NE2 
14022 N N   . GLU D  185 ? 0.3552 0.3684 0.3361 0.1206  -0.1720 -0.1109 185 GLU D N   
14023 C CA  . GLU D  185 ? 0.4451 0.4495 0.4173 0.1221  -0.1797 -0.1067 185 GLU D CA  
14024 C C   . GLU D  185 ? 0.4424 0.4542 0.4276 0.1278  -0.1843 -0.1117 185 GLU D C   
14025 O O   . GLU D  185 ? 0.4709 0.4734 0.4521 0.1329  -0.1936 -0.1106 185 GLU D O   
14026 C CB  . GLU D  185 ? 0.6178 0.6231 0.5784 0.1147  -0.1755 -0.1006 185 GLU D CB  
14027 C CG  . GLU D  185 ? 0.7461 0.7446 0.6915 0.1088  -0.1726 -0.0948 185 GLU D CG  
14028 C CD  . GLU D  185 ? 0.8648 0.8718 0.8051 0.1021  -0.1647 -0.0921 185 GLU D CD  
14029 O OE1 . GLU D  185 ? 0.8833 0.8956 0.8264 0.1022  -0.1642 -0.0931 185 GLU D OE1 
14030 O OE2 . GLU D  185 ? 0.9051 0.9133 0.8384 0.0971  -0.1594 -0.0894 185 GLU D OE2 
14031 N N   . ASN D  186 ? 0.3353 0.3639 0.3348 0.1261  -0.1782 -0.1165 186 ASN D N   
14032 C CA  . ASN D  186 ? 0.3404 0.3791 0.3522 0.1294  -0.1821 -0.1206 186 ASN D CA  
14033 C C   . ASN D  186 ? 0.3495 0.4020 0.3803 0.1351  -0.1826 -0.1292 186 ASN D C   
14034 O O   . ASN D  186 ? 0.3391 0.4004 0.3799 0.1381  -0.1871 -0.1322 186 ASN D O   
14035 C CB  . ASN D  186 ? 0.5104 0.5573 0.5223 0.1224  -0.1776 -0.1187 186 ASN D CB  
14036 C CG  . ASN D  186 ? 0.5793 0.6147 0.5728 0.1177  -0.1770 -0.1114 186 ASN D CG  
14037 O OD1 . ASN D  186 ? 0.6114 0.6375 0.5949 0.1193  -0.1839 -0.1076 186 ASN D OD1 
14038 N ND2 . ASN D  186 ? 0.5907 0.6273 0.5792 0.1122  -0.1689 -0.1095 186 ASN D ND2 
14039 N N   . ILE D  187 ? 0.4915 0.5474 0.5277 0.1367  -0.1783 -0.1334 187 ILE D N   
14040 C CA  . ILE D  187 ? 0.5151 0.5896 0.5704 0.1403  -0.1763 -0.1421 187 ILE D CA  
14041 C C   . ILE D  187 ? 0.5107 0.5843 0.5723 0.1502  -0.1854 -0.1465 187 ILE D C   
14042 O O   . ILE D  187 ? 0.5087 0.6002 0.5868 0.1534  -0.1854 -0.1530 187 ILE D O   
14043 C CB  . ILE D  187 ? 0.5238 0.6047 0.5839 0.1397  -0.1693 -0.1467 187 ILE D CB  
14044 C CG1 . ILE D  187 ? 0.4812 0.5862 0.5611 0.1405  -0.1653 -0.1549 187 ILE D CG1 
14045 C CG2 . ILE D  187 ? 0.5487 0.6146 0.6020 0.1471  -0.1743 -0.1484 187 ILE D CG2 
14046 C CD1 . ILE D  187 ? 0.4237 0.5433 0.5118 0.1341  -0.1634 -0.1538 187 ILE D CD1 
14047 N N   . ALA D  188 ? 0.5536 0.6061 0.6013 0.1548  -0.1934 -0.1424 188 ALA D N   
14048 C CA  . ALA D  188 ? 0.5722 0.6187 0.6225 0.1652  -0.2035 -0.1458 188 ALA D CA  
14049 C C   . ALA D  188 ? 0.5512 0.6109 0.6121 0.1668  -0.2076 -0.1472 188 ALA D C   
14050 O O   . ALA D  188 ? 0.5477 0.6180 0.6221 0.1748  -0.2116 -0.1539 188 ALA D O   
14051 C CB  . ALA D  188 ? 0.6031 0.6215 0.6329 0.1677  -0.2119 -0.1391 188 ALA D CB  
14052 N N   . ALA D  189 ? 0.5405 0.6005 0.5957 0.1593  -0.2065 -0.1411 189 ALA D N   
14053 C CA  . ALA D  189 ? 0.5082 0.5790 0.5715 0.1601  -0.2116 -0.1416 189 ALA D CA  
14054 C C   . ALA D  189 ? 0.4964 0.5949 0.5824 0.1597  -0.2073 -0.1491 189 ALA D C   
14055 O O   . ALA D  189 ? 0.5824 0.6929 0.6790 0.1622  -0.2125 -0.1512 189 ALA D O   
14056 C CB  . ALA D  189 ? 0.3922 0.4580 0.4440 0.1516  -0.2108 -0.1343 189 ALA D CB  
14057 N N   . PHE D  190 ? 0.3513 0.4610 0.4448 0.1559  -0.1980 -0.1527 190 PHE D N   
14058 C CA  . PHE D  190 ? 0.3420 0.4793 0.4569 0.1551  -0.1937 -0.1599 190 PHE D CA  
14059 C C   . PHE D  190 ? 0.3474 0.4920 0.4728 0.1650  -0.1943 -0.1682 190 PHE D C   
14060 O O   . PHE D  190 ? 0.4336 0.6027 0.5770 0.1649  -0.1896 -0.1750 190 PHE D O   
14061 C CB  . PHE D  190 ? 0.3582 0.5060 0.4759 0.1446  -0.1833 -0.1595 190 PHE D CB  
14062 C CG  . PHE D  190 ? 0.3448 0.4832 0.4501 0.1352  -0.1820 -0.1519 190 PHE D CG  
14063 C CD1 . PHE D  190 ? 0.3581 0.4746 0.4440 0.1334  -0.1808 -0.1456 190 PHE D CD1 
14064 C CD2 . PHE D  190 ? 0.3311 0.4832 0.4441 0.1281  -0.1821 -0.1513 190 PHE D CD2 
14065 C CE1 . PHE D  190 ? 0.3674 0.4762 0.4417 0.1256  -0.1792 -0.1394 190 PHE D CE1 
14066 C CE2 . PHE D  190 ? 0.3654 0.5075 0.4659 0.1202  -0.1814 -0.1451 190 PHE D CE2 
14067 C CZ  . PHE D  190 ? 0.3774 0.4980 0.4585 0.1195  -0.1796 -0.1394 190 PHE D CZ  
14068 N N   . GLY D  191 ? 0.3611 0.4845 0.4748 0.1730  -0.1999 -0.1677 191 GLY D N   
14069 C CA  . GLY D  191 ? 0.4171 0.5435 0.5379 0.1832  -0.2013 -0.1758 191 GLY D CA  
14070 C C   . GLY D  191 ? 0.4021 0.5260 0.5196 0.1813  -0.1937 -0.1784 191 GLY D C   
14071 O O   . GLY D  191 ? 0.4101 0.5456 0.5378 0.1871  -0.1913 -0.1867 191 GLY D O   
14072 N N   . GLY D  192 ? 0.4868 0.5968 0.5901 0.1731  -0.1897 -0.1715 192 GLY D N   
14073 C CA  . GLY D  192 ? 0.5130 0.6182 0.6111 0.1714  -0.1838 -0.1731 192 GLY D CA  
14074 C C   . GLY D  192 ? 0.5538 0.6320 0.6363 0.1780  -0.1913 -0.1715 192 GLY D C   
14075 O O   . GLY D  192 ? 0.6216 0.6820 0.6940 0.1818  -0.2005 -0.1668 192 GLY D O   
14076 N N   . ASP D  193 ? 0.3554 0.4301 0.4355 0.1793  -0.1880 -0.1751 193 ASP D N   
14077 C CA  . ASP D  193 ? 0.3763 0.4236 0.4399 0.1836  -0.1951 -0.1725 193 ASP D CA  
14078 C C   . ASP D  193 ? 0.3590 0.3975 0.4103 0.1740  -0.1899 -0.1655 193 ASP D C   
14079 O O   . ASP D  193 ? 0.3449 0.3941 0.4007 0.1704  -0.1820 -0.1689 193 ASP D O   
14080 C CB  . ASP D  193 ? 0.6497 0.6975 0.7182 0.1927  -0.1966 -0.1819 193 ASP D CB  
14081 C CG  . ASP D  193 ? 0.7539 0.7697 0.8043 0.1981  -0.2065 -0.1794 193 ASP D CG  
14082 O OD1 . ASP D  193 ? 0.7509 0.7483 0.7856 0.1918  -0.2080 -0.1710 193 ASP D OD1 
14083 O OD2 . ASP D  193 ? 0.8091 0.8179 0.8606 0.2084  -0.2128 -0.1856 193 ASP D OD2 
14084 N N   . PRO D  194 ? 0.4385 0.4587 0.4739 0.1695  -0.1941 -0.1556 194 PRO D N   
14085 C CA  . PRO D  194 ? 0.4707 0.4817 0.4927 0.1605  -0.1900 -0.1480 194 PRO D CA  
14086 C C   . PRO D  194 ? 0.5288 0.5304 0.5455 0.1623  -0.1907 -0.1509 194 PRO D C   
14087 O O   . PRO D  194 ? 0.4983 0.5017 0.5096 0.1539  -0.1841 -0.1471 194 PRO D O   
14088 C CB  . PRO D  194 ? 0.6246 0.6142 0.6292 0.1589  -0.1982 -0.1385 194 PRO D CB  
14089 C CG  . PRO D  194 ? 0.6530 0.6503 0.6656 0.1625  -0.2014 -0.1397 194 PRO D CG  
14090 C CD  . PRO D  194 ? 0.6299 0.6419 0.6606 0.1714  -0.2017 -0.1508 194 PRO D CD  
14091 N N   . MET D  195 ? 0.7604 0.7515 0.7778 0.1728  -0.1987 -0.1573 195 MET D N   
14092 C CA  . MET D  195 ? 0.7827 0.7626 0.7943 0.1756  -0.2009 -0.1608 195 MET D CA  
14093 C C   . MET D  195 ? 0.7506 0.7506 0.7781 0.1799  -0.1939 -0.1723 195 MET D C   
14094 O O   . MET D  195 ? 0.7693 0.7611 0.7927 0.1823  -0.1947 -0.1758 195 MET D O   
14095 C CB  . MET D  195 ? 0.7554 0.7042 0.7525 0.1836  -0.2149 -0.1594 195 MET D CB  
14096 C CG  . MET D  195 ? 0.7459 0.6706 0.7211 0.1761  -0.2217 -0.1467 195 MET D CG  
14097 S SD  . MET D  195 ? 1.6306 1.5188 1.5894 0.1857  -0.2389 -0.1441 195 MET D SD  
14098 C CE  . MET D  195 ? 0.5504 0.4570 0.5275 0.1949  -0.2387 -0.1510 195 MET D CE  
14099 N N   . SER D  196 ? 0.5685 0.5942 0.6131 0.1805  -0.1871 -0.1779 196 SER D N   
14100 C CA  . SER D  196 ? 0.5610 0.6093 0.6186 0.1798  -0.1776 -0.1862 196 SER D CA  
14101 C C   . SER D  196 ? 0.5396 0.6107 0.6058 0.1696  -0.1670 -0.1839 196 SER D C   
14102 O O   . SER D  196 ? 0.5693 0.6581 0.6476 0.1688  -0.1640 -0.1858 196 SER D O   
14103 C CB  . SER D  196 ? 0.6973 0.7578 0.7677 0.1890  -0.1782 -0.1958 196 SER D CB  
14104 O OG  . SER D  196 ? 0.6994 0.7860 0.7830 0.1864  -0.1675 -0.2027 196 SER D OG  
14105 N N   . VAL D  197 ? 0.4816 0.5526 0.5416 0.1616  -0.1614 -0.1801 197 VAL D N   
14106 C CA  . VAL D  197 ? 0.4091 0.4959 0.4731 0.1510  -0.1519 -0.1759 197 VAL D CA  
14107 C C   . VAL D  197 ? 0.3855 0.4833 0.4512 0.1464  -0.1441 -0.1793 197 VAL D C   
14108 O O   . VAL D  197 ? 0.4098 0.4945 0.4633 0.1429  -0.1443 -0.1763 197 VAL D O   
14109 C CB  . VAL D  197 ? 0.3265 0.3989 0.3767 0.1430  -0.1522 -0.1639 197 VAL D CB  
14110 C CG1 . VAL D  197 ? 0.2714 0.3555 0.3224 0.1323  -0.1422 -0.1594 197 VAL D CG1 
14111 C CG2 . VAL D  197 ? 0.3369 0.4035 0.3868 0.1459  -0.1585 -0.1606 197 VAL D CG2 
14112 N N   . THR D  198 ? 0.3769 0.4985 0.4564 0.1446  -0.1371 -0.1851 198 THR D N   
14113 C CA  . THR D  198 ? 0.3194 0.4534 0.4003 0.1396  -0.1297 -0.1888 198 THR D CA  
14114 C C   . THR D  198 ? 0.3031 0.4452 0.3828 0.1275  -0.1217 -0.1819 198 THR D C   
14115 O O   . THR D  198 ? 0.2984 0.4541 0.3880 0.1251  -0.1198 -0.1820 198 THR D O   
14116 C CB  . THR D  198 ? 0.2580 0.4137 0.3551 0.1463  -0.1257 -0.2004 198 THR D CB  
14117 O OG1 . THR D  198 ? 0.2759 0.4187 0.3710 0.1568  -0.1308 -0.2053 198 THR D OG1 
14118 C CG2 . THR D  198 ? 0.2525 0.4144 0.3445 0.1380  -0.1147 -0.2019 198 THR D CG2 
14119 N N   . LEU D  199 ? 0.3132 0.4454 0.3801 0.1193  -0.1169 -0.1750 199 LEU D N   
14120 C CA  . LEU D  199 ? 0.2991 0.4370 0.3637 0.1090  -0.1099 -0.1686 199 LEU D CA  
14121 C C   . LEU D  199 ? 0.2988 0.4555 0.3702 0.1058  -0.1038 -0.1760 199 LEU D C   
14122 O O   . LEU D  199 ? 0.2951 0.4529 0.3650 0.1087  -0.1022 -0.1824 199 LEU D O   
14123 C CB  . LEU D  199 ? 0.2273 0.3488 0.2765 0.1024  -0.1070 -0.1586 199 LEU D CB  
14124 C CG  . LEU D  199 ? 0.2329 0.3365 0.2725 0.1036  -0.1119 -0.1513 199 LEU D CG  
14125 C CD1 . LEU D  199 ? 0.2296 0.3244 0.2570 0.0963  -0.1075 -0.1429 199 LEU D CD1 
14126 C CD2 . LEU D  199 ? 0.2326 0.3365 0.2751 0.1042  -0.1148 -0.1482 199 LEU D CD2 
14127 N N   . PHE D  200 ? 0.2182 0.3890 0.2958 0.0993  -0.1003 -0.1753 200 PHE D N   
14128 C CA  . PHE D  200 ? 0.2153 0.4031 0.2958 0.0933  -0.0938 -0.1808 200 PHE D CA  
14129 C C   . PHE D  200 ? 0.2109 0.3996 0.2868 0.0822  -0.0903 -0.1737 200 PHE D C   
14130 O O   . PHE D  200 ? 0.2097 0.3976 0.2890 0.0801  -0.0932 -0.1694 200 PHE D O   
14131 C CB  . PHE D  200 ? 0.2175 0.4287 0.3154 0.0986  -0.0917 -0.1916 200 PHE D CB  
14132 C CG  . PHE D  200 ? 0.2139 0.4451 0.3282 0.0968  -0.0933 -0.1932 200 PHE D CG  
14133 C CD1 . PHE D  200 ? 0.3073 0.5315 0.4256 0.1016  -0.1002 -0.1901 200 PHE D CD1 
14134 C CD2 . PHE D  200 ? 0.2126 0.4667 0.3362 0.0893  -0.0855 -0.1964 200 PHE D CD2 
14135 C CE1 . PHE D  200 ? 0.3003 0.5402 0.4317 0.0989  -0.1004 -0.1906 200 PHE D CE1 
14136 C CE2 . PHE D  200 ? 0.2102 0.4851 0.3502 0.0863  -0.0871 -0.1982 200 PHE D CE2 
14137 C CZ  . PHE D  200 ? 0.2120 0.4788 0.3555 0.0912  -0.0946 -0.1951 200 PHE D CZ  
14138 N N   . GLY D  201 ? 0.2382 0.4257 0.3044 0.0750  -0.0847 -0.1721 201 GLY D N   
14139 C CA  . GLY D  201 ? 0.2350 0.4199 0.2944 0.0650  -0.0829 -0.1655 201 GLY D CA  
14140 C C   . GLY D  201 ? 0.2885 0.4808 0.3411 0.0570  -0.0767 -0.1677 201 GLY D C   
14141 O O   . GLY D  201 ? 0.3471 0.5435 0.3981 0.0592  -0.0724 -0.1729 201 GLY D O   
14142 N N   . GLU D  202 ? 0.3327 0.5238 0.3792 0.0474  -0.0763 -0.1632 202 GLU D N   
14143 C CA  . GLU D  202 ? 0.3674 0.5622 0.4053 0.0382  -0.0697 -0.1624 202 GLU D CA  
14144 C C   . GLU D  202 ? 0.3506 0.5264 0.3705 0.0331  -0.0724 -0.1544 202 GLU D C   
14145 O O   . GLU D  202 ? 0.3488 0.5117 0.3661 0.0336  -0.0772 -0.1480 202 GLU D O   
14146 C CB  . GLU D  202 ? 0.4420 0.6569 0.4910 0.0298  -0.0651 -0.1647 202 GLU D CB  
14147 C CG  . GLU D  202 ? 0.4904 0.7110 0.5307 0.0191  -0.0571 -0.1635 202 GLU D CG  
14148 C CD  . GLU D  202 ? 0.5620 0.7690 0.5887 0.0080  -0.0598 -0.1551 202 GLU D CD  
14149 O OE1 . GLU D  202 ? 0.5682 0.7664 0.5962 0.0082  -0.0670 -0.1520 202 GLU D OE1 
14150 O OE2 . GLU D  202 ? 0.6096 0.8131 0.6230 -0.0005 -0.0552 -0.1518 202 GLU D OE2 
14151 N N   . SER D  203 ? 0.2929 0.4646 0.3003 0.0291  -0.0680 -0.1529 203 SER D N   
14152 C CA  . SER D  203 ? 0.3191 0.4724 0.3094 0.0255  -0.0702 -0.1447 203 SER D CA  
14153 C C   . SER D  203 ? 0.3075 0.4433 0.2955 0.0334  -0.0739 -0.1373 203 SER D C   
14154 O O   . SER D  203 ? 0.2937 0.4274 0.2841 0.0397  -0.0725 -0.1373 203 SER D O   
14155 C CB  . SER D  203 ? 0.4691 0.6192 0.4535 0.0156  -0.0723 -0.1410 203 SER D CB  
14156 O OG  . SER D  203 ? 0.5180 0.6534 0.4840 0.0111  -0.0734 -0.1352 203 SER D OG  
14157 N N   . ALA D  204 ? 0.3445 0.4682 0.3272 0.0326  -0.0786 -0.1317 204 ALA D N   
14158 C CA  . ALA D  204 ? 0.2863 0.3975 0.2680 0.0396  -0.0812 -0.1259 204 ALA D CA  
14159 C C   . ALA D  204 ? 0.2597 0.3763 0.2542 0.0460  -0.0816 -0.1284 204 ALA D C   
14160 O O   . ALA D  204 ? 0.2408 0.3512 0.2354 0.0517  -0.0820 -0.1252 204 ALA D O   
14161 C CB  . ALA D  204 ? 0.2369 0.3358 0.2109 0.0381  -0.0860 -0.1213 204 ALA D CB  
14162 N N   . GLY D  205 ? 0.2208 0.3498 0.2259 0.0448  -0.0820 -0.1342 205 GLY D N   
14163 C CA  . GLY D  205 ? 0.2149 0.3488 0.2318 0.0516  -0.0835 -0.1371 205 GLY D CA  
14164 C C   . GLY D  205 ? 0.2333 0.3695 0.2522 0.0567  -0.0809 -0.1402 205 GLY D C   
14165 O O   . GLY D  205 ? 0.2097 0.3397 0.2302 0.0628  -0.0829 -0.1386 205 GLY D O   
14166 N N   . ALA D  206 ? 0.2148 0.3589 0.2321 0.0536  -0.0768 -0.1446 206 ALA D N   
14167 C CA  . ALA D  206 ? 0.2149 0.3596 0.2327 0.0580  -0.0746 -0.1481 206 ALA D CA  
14168 C C   . ALA D  206 ? 0.2147 0.3446 0.2219 0.0583  -0.0746 -0.1405 206 ALA D C   
14169 O O   . ALA D  206 ? 0.2146 0.3395 0.2221 0.0625  -0.0754 -0.1406 206 ALA D O   
14170 C CB  . ALA D  206 ? 0.2887 0.4461 0.3062 0.0543  -0.0694 -0.1552 206 ALA D CB  
14171 N N   . ALA D  207 ? 0.2328 0.3559 0.2308 0.0537  -0.0745 -0.1342 207 ALA D N   
14172 C CA  . ALA D  207 ? 0.2696 0.3819 0.2597 0.0544  -0.0750 -0.1275 207 ALA D CA  
14173 C C   . ALA D  207 ? 0.2985 0.4058 0.2926 0.0594  -0.0779 -0.1249 207 ALA D C   
14174 O O   . ALA D  207 ? 0.3219 0.4250 0.3139 0.0610  -0.0781 -0.1231 207 ALA D O   
14175 C CB  . ALA D  207 ? 0.2251 0.3313 0.2059 0.0507  -0.0758 -0.1222 207 ALA D CB  
14176 N N   . SER D  208 ? 0.2097 0.3175 0.2085 0.0610  -0.0805 -0.1250 208 SER D N   
14177 C CA  . SER D  208 ? 0.2077 0.3104 0.2084 0.0653  -0.0833 -0.1226 208 SER D CA  
14178 C C   . SER D  208 ? 0.2570 0.3608 0.2629 0.0693  -0.0847 -0.1264 208 SER D C   
14179 O O   . SER D  208 ? 0.2846 0.3819 0.2872 0.0710  -0.0863 -0.1234 208 SER D O   
14180 C CB  . SER D  208 ? 0.2080 0.3109 0.2122 0.0657  -0.0860 -0.1225 208 SER D CB  
14181 O OG  . SER D  208 ? 0.2106 0.3099 0.2084 0.0620  -0.0859 -0.1195 208 SER D OG  
14182 N N   . VAL D  209 ? 0.2400 0.3521 0.2534 0.0708  -0.0847 -0.1335 209 VAL D N   
14183 C CA  . VAL D  209 ? 0.2540 0.3658 0.2718 0.0762  -0.0872 -0.1385 209 VAL D CA  
14184 C C   . VAL D  209 ? 0.2853 0.3895 0.2953 0.0748  -0.0860 -0.1365 209 VAL D C   
14185 O O   . VAL D  209 ? 0.3017 0.3972 0.3087 0.0771  -0.0895 -0.1351 209 VAL D O   
14186 C CB  . VAL D  209 ? 0.2779 0.4030 0.3055 0.0786  -0.0865 -0.1482 209 VAL D CB  
14187 C CG1 . VAL D  209 ? 0.2772 0.4001 0.3087 0.0860  -0.0902 -0.1544 209 VAL D CG1 
14188 C CG2 . VAL D  209 ? 0.3043 0.4392 0.3406 0.0785  -0.0880 -0.1504 209 VAL D CG2 
14189 N N   . GLY D  210 ? 0.2991 0.4057 0.3043 0.0702  -0.0817 -0.1360 210 GLY D N   
14190 C CA  . GLY D  210 ? 0.3376 0.4374 0.3349 0.0675  -0.0807 -0.1334 210 GLY D CA  
14191 C C   . GLY D  210 ? 0.3509 0.4436 0.3426 0.0659  -0.0824 -0.1261 210 GLY D C   
14192 O O   . GLY D  210 ? 0.2222 0.3088 0.2089 0.0644  -0.0839 -0.1246 210 GLY D O   
14193 N N   . MET D  211 ? 0.2129 0.3066 0.2050 0.0658  -0.0824 -0.1220 211 MET D N   
14194 C CA  . MET D  211 ? 0.2116 0.3016 0.1988 0.0647  -0.0832 -0.1160 211 MET D CA  
14195 C C   . MET D  211 ? 0.2235 0.3083 0.2107 0.0671  -0.0871 -0.1155 211 MET D C   
14196 O O   . MET D  211 ? 0.2172 0.2993 0.1989 0.0649  -0.0879 -0.1118 211 MET D O   
14197 C CB  . MET D  211 ? 0.2080 0.2995 0.1946 0.0648  -0.0822 -0.1129 211 MET D CB  
14198 C CG  . MET D  211 ? 0.2072 0.2984 0.1881 0.0635  -0.0813 -0.1081 211 MET D CG  
14199 S SD  . MET D  211 ? 0.3487 0.4417 0.3253 0.0609  -0.0791 -0.1072 211 MET D SD  
14200 C CE  . MET D  211 ? 0.2416 0.3349 0.2211 0.0604  -0.0792 -0.1107 211 MET D CE  
14201 N N   . HIS D  212 ? 0.2628 0.3469 0.2555 0.0714  -0.0900 -0.1192 212 HIS D N   
14202 C CA  . HIS D  212 ? 0.3075 0.3846 0.2986 0.0739  -0.0950 -0.1189 212 HIS D CA  
14203 C C   . HIS D  212 ? 0.3392 0.4097 0.3269 0.0737  -0.0977 -0.1218 212 HIS D C   
14204 O O   . HIS D  212 ? 0.3824 0.4444 0.3636 0.0727  -0.1019 -0.1196 212 HIS D O   
14205 C CB  . HIS D  212 ? 0.2240 0.3020 0.2221 0.0794  -0.0985 -0.1222 212 HIS D CB  
14206 C CG  . HIS D  212 ? 0.2186 0.3002 0.2185 0.0790  -0.0971 -0.1194 212 HIS D CG  
14207 N ND1 . HIS D  212 ? 0.2986 0.3769 0.2920 0.0773  -0.0969 -0.1138 212 HIS D ND1 
14208 C CD2 . HIS D  212 ? 0.2730 0.3610 0.2796 0.0797  -0.0963 -0.1221 212 HIS D CD2 
14209 C CE1 . HIS D  212 ? 0.2157 0.2963 0.2112 0.0777  -0.0962 -0.1133 212 HIS D CE1 
14210 N NE2 . HIS D  212 ? 0.2697 0.3557 0.2729 0.0785  -0.0961 -0.1179 212 HIS D NE2 
14211 N N   . ILE D  213 ? 0.3985 0.4720 0.3891 0.0742  -0.0956 -0.1270 213 ILE D N   
14212 C CA  . ILE D  213 ? 0.4179 0.4833 0.4035 0.0734  -0.0978 -0.1301 213 ILE D CA  
14213 C C   . ILE D  213 ? 0.4116 0.4727 0.3876 0.0660  -0.0973 -0.1242 213 ILE D C   
14214 O O   . ILE D  213 ? 0.4477 0.4983 0.4165 0.0638  -0.1016 -0.1241 213 ILE D O   
14215 C CB  . ILE D  213 ? 0.3601 0.4308 0.3490 0.0741  -0.0940 -0.1363 213 ILE D CB  
14216 C CG1 . ILE D  213 ? 0.2429 0.3206 0.2421 0.0814  -0.0950 -0.1437 213 ILE D CG1 
14217 C CG2 . ILE D  213 ? 0.2556 0.3159 0.2370 0.0723  -0.0958 -0.1389 213 ILE D CG2 
14218 C CD1 . ILE D  213 ? 0.2441 0.3298 0.2464 0.0819  -0.0906 -0.1504 213 ILE D CD1 
14219 N N   . LEU D  214 ? 0.3687 0.4378 0.3442 0.0621  -0.0927 -0.1196 214 LEU D N   
14220 C CA  . LEU D  214 ? 0.3804 0.4501 0.3490 0.0554  -0.0918 -0.1152 214 LEU D CA  
14221 C C   . LEU D  214 ? 0.4285 0.4996 0.3935 0.0533  -0.0933 -0.1096 214 LEU D C   
14222 O O   . LEU D  214 ? 0.4853 0.5601 0.4456 0.0476  -0.0928 -0.1063 214 LEU D O   
14223 C CB  . LEU D  214 ? 0.3001 0.3780 0.2696 0.0533  -0.0868 -0.1141 214 LEU D CB  
14224 C CG  . LEU D  214 ? 0.2326 0.3105 0.2032 0.0537  -0.0847 -0.1191 214 LEU D CG  
14225 C CD1 . LEU D  214 ? 0.3882 0.4735 0.3596 0.0529  -0.0807 -0.1175 214 LEU D CD1 
14226 C CD2 . LEU D  214 ? 0.2420 0.3144 0.2059 0.0490  -0.0861 -0.1204 214 LEU D CD2 
14227 N N   . SER D  215 ? 0.3212 0.3908 0.2886 0.0576  -0.0951 -0.1090 215 SER D N   
14228 C CA  . SER D  215 ? 0.3254 0.3974 0.2887 0.0559  -0.0960 -0.1041 215 SER D CA  
14229 C C   . SER D  215 ? 0.3160 0.3781 0.2738 0.0559  -0.1023 -0.1037 215 SER D C   
14230 O O   . SER D  215 ? 0.3219 0.3777 0.2830 0.0615  -0.1055 -0.1065 215 SER D O   
14231 C CB  . SER D  215 ? 0.4836 0.5605 0.4518 0.0606  -0.0935 -0.1031 215 SER D CB  
14232 O OG  . SER D  215 ? 0.5195 0.5993 0.4830 0.0595  -0.0939 -0.0991 215 SER D OG  
14233 N N   . LEU D  216 ? 0.3671 0.4278 0.3160 0.0494  -0.1049 -0.1004 216 LEU D N   
14234 C CA  . LEU D  216 ? 0.4075 0.4549 0.3478 0.0480  -0.1125 -0.0999 216 LEU D CA  
14235 C C   . LEU D  216 ? 0.4110 0.4532 0.3511 0.0537  -0.1163 -0.0988 216 LEU D C   
14236 O O   . LEU D  216 ? 0.4418 0.4716 0.3819 0.0588  -0.1221 -0.1018 216 LEU D O   
14237 C CB  . LEU D  216 ? 0.4300 0.4773 0.3590 0.0380  -0.1153 -0.0961 216 LEU D CB  
14238 C CG  . LEU D  216 ? 0.4585 0.4870 0.3787 0.0348  -0.1231 -0.0982 216 LEU D CG  
14239 C CD1 . LEU D  216 ? 0.4539 0.4650 0.3669 0.0388  -0.1316 -0.0975 216 LEU D CD1 
14240 C CD2 . LEU D  216 ? 0.4461 0.4705 0.3733 0.0389  -0.1211 -0.1045 216 LEU D CD2 
14241 N N   . PRO D  217 ? 0.3345 0.3857 0.2741 0.0537  -0.1134 -0.0951 217 PRO D N   
14242 C CA  . PRO D  217 ? 0.3118 0.3577 0.2508 0.0589  -0.1170 -0.0943 217 PRO D CA  
14243 C C   . PRO D  217 ? 0.3188 0.3613 0.2685 0.0671  -0.1179 -0.0994 217 PRO D C   
14244 O O   . PRO D  217 ? 0.4131 0.4464 0.3615 0.0715  -0.1242 -0.1000 217 PRO D O   
14245 C CB  . PRO D  217 ? 0.4613 0.5191 0.4004 0.0585  -0.1119 -0.0913 217 PRO D CB  
14246 C CG  . PRO D  217 ? 0.4962 0.5655 0.4387 0.0554  -0.1055 -0.0915 217 PRO D CG  
14247 C CD  . PRO D  217 ? 0.5096 0.5752 0.4483 0.0497  -0.1078 -0.0919 217 PRO D CD  
14248 N N   . SER D  218 ? 0.2695 0.3195 0.2291 0.0691  -0.1125 -0.1029 218 SER D N   
14249 C CA  . SER D  218 ? 0.3100 0.3598 0.2798 0.0760  -0.1134 -0.1083 218 SER D CA  
14250 C C   . SER D  218 ? 0.3666 0.4066 0.3370 0.0800  -0.1198 -0.1132 218 SER D C   
14251 O O   . SER D  218 ? 0.2662 0.3047 0.2434 0.0871  -0.1237 -0.1175 218 SER D O   
14252 C CB  . SER D  218 ? 0.2411 0.3015 0.2194 0.0760  -0.1066 -0.1107 218 SER D CB  
14253 O OG  . SER D  218 ? 0.2324 0.2985 0.2119 0.0758  -0.1032 -0.1080 218 SER D OG  
14254 N N   . ARG D  219 ? 0.4585 0.4913 0.4215 0.0758  -0.1214 -0.1131 219 ARG D N   
14255 C CA  . ARG D  219 ? 0.5035 0.5258 0.4665 0.0797  -0.1265 -0.1192 219 ARG D CA  
14256 C C   . ARG D  219 ? 0.5124 0.5223 0.4747 0.0878  -0.1361 -0.1220 219 ARG D C   
14257 O O   . ARG D  219 ? 0.5334 0.5397 0.5013 0.0952  -0.1396 -0.1296 219 ARG D O   
14258 C CB  . ARG D  219 ? 0.5923 0.6051 0.5439 0.0722  -0.1279 -0.1176 219 ARG D CB  
14259 C CG  . ARG D  219 ? 0.6511 0.6717 0.6064 0.0689  -0.1211 -0.1205 219 ARG D CG  
14260 C CD  . ARG D  219 ? 0.6900 0.7166 0.6568 0.0767  -0.1186 -0.1281 219 ARG D CD  
14261 N NE  . ARG D  219 ? 0.7569 0.7703 0.7232 0.0840  -0.1256 -0.1351 219 ARG D NE  
14262 C CZ  . ARG D  219 ? 0.8032 0.8075 0.7653 0.0838  -0.1263 -0.1400 219 ARG D CZ  
14263 N NH1 . ARG D  219 ? 0.7786 0.7865 0.7367 0.0757  -0.1207 -0.1383 219 ARG D NH1 
14264 N NH2 . ARG D  219 ? 0.8332 0.8242 0.7947 0.0922  -0.1331 -0.1469 219 ARG D NH2 
14265 N N   . SER D  220 ? 0.5100 0.5138 0.4651 0.0868  -0.1408 -0.1163 220 SER D N   
14266 C CA  . SER D  220 ? 0.5077 0.4966 0.4591 0.0940  -0.1516 -0.1175 220 SER D CA  
14267 C C   . SER D  220 ? 0.5009 0.4995 0.4644 0.1018  -0.1518 -0.1198 220 SER D C   
14268 O O   . SER D  220 ? 0.5195 0.5084 0.4810 0.1079  -0.1605 -0.1197 220 SER D O   
14269 C CB  . SER D  220 ? 0.4046 0.3797 0.3389 0.0879  -0.1576 -0.1093 220 SER D CB  
14270 O OG  . SER D  220 ? 0.3752 0.3615 0.3100 0.0853  -0.1532 -0.1039 220 SER D OG  
14271 N N   . LEU D  221 ? 0.4195 0.4361 0.3943 0.1007  -0.1428 -0.1212 221 LEU D N   
14272 C CA  . LEU D  221 ? 0.4310 0.4568 0.4167 0.1060  -0.1427 -0.1235 221 LEU D CA  
14273 C C   . LEU D  221 ? 0.4350 0.4702 0.4353 0.1134  -0.1428 -0.1332 221 LEU D C   
14274 O O   . LEU D  221 ? 0.4263 0.4709 0.4373 0.1178  -0.1433 -0.1366 221 LEU D O   
14275 C CB  . LEU D  221 ? 0.3704 0.4078 0.3575 0.0999  -0.1343 -0.1191 221 LEU D CB  
14276 C CG  . LEU D  221 ? 0.3483 0.3803 0.3215 0.0928  -0.1331 -0.1110 221 LEU D CG  
14277 C CD1 . LEU D  221 ? 0.2642 0.3066 0.2383 0.0885  -0.1255 -0.1079 221 LEU D CD1 
14278 C CD2 . LEU D  221 ? 0.3634 0.3836 0.3278 0.0949  -0.1416 -0.1075 221 LEU D CD2 
14279 N N   . PHE D  222 ? 0.2866 0.3201 0.2869 0.1143  -0.1424 -0.1381 222 PHE D N   
14280 C CA  . PHE D  222 ? 0.2840 0.3287 0.2977 0.1216  -0.1422 -0.1485 222 PHE D CA  
14281 C C   . PHE D  222 ? 0.3409 0.3744 0.3500 0.1259  -0.1466 -0.1548 222 PHE D C   
14282 O O   . PHE D  222 ? 0.3530 0.3678 0.3477 0.1221  -0.1504 -0.1503 222 PHE D O   
14283 C CB  . PHE D  222 ? 0.2660 0.3297 0.2884 0.1163  -0.1316 -0.1498 222 PHE D CB  
14284 C CG  . PHE D  222 ? 0.2609 0.3232 0.2756 0.1082  -0.1247 -0.1462 222 PHE D CG  
14285 C CD1 . PHE D  222 ? 0.2573 0.3143 0.2619 0.1001  -0.1215 -0.1369 222 PHE D CD1 
14286 C CD2 . PHE D  222 ? 0.2605 0.3279 0.2780 0.1085  -0.1210 -0.1526 222 PHE D CD2 
14287 C CE1 . PHE D  222 ? 0.3709 0.4283 0.3695 0.0929  -0.1156 -0.1338 222 PHE D CE1 
14288 C CE2 . PHE D  222 ? 0.2569 0.3227 0.2669 0.1006  -0.1148 -0.1486 222 PHE D CE2 
14289 C CZ  . PHE D  222 ? 0.2528 0.3140 0.2539 0.0930  -0.1124 -0.1392 222 PHE D CZ  
14290 N N   . HIS D  223 ? 0.4836 0.5281 0.5043 0.1333  -0.1462 -0.1657 223 HIS D N   
14291 C CA  . HIS D  223 ? 0.4872 0.5191 0.5039 0.1401  -0.1504 -0.1739 223 HIS D CA  
14292 C C   . HIS D  223 ? 0.5076 0.5531 0.5310 0.1388  -0.1402 -0.1801 223 HIS D C   
14293 O O   . HIS D  223 ? 0.5483 0.5831 0.5625 0.1343  -0.1369 -0.1788 223 HIS D O   
14294 C CB  . HIS D  223 ? 0.4189 0.4453 0.4426 0.1537  -0.1599 -0.1791 223 HIS D CB  
14295 C CG  . HIS D  223 ? 0.4652 0.4769 0.4806 0.1541  -0.1698 -0.1708 223 HIS D CG  
14296 N ND1 . HIS D  223 ? 0.4646 0.4888 0.4892 0.1564  -0.1723 -0.1686 223 HIS D ND1 
14297 C CD2 . HIS D  223 ? 0.5036 0.4886 0.5005 0.1507  -0.1769 -0.1633 223 HIS D CD2 
14298 C CE1 . HIS D  223 ? 0.4883 0.4934 0.5001 0.1548  -0.1791 -0.1600 223 HIS D CE1 
14299 N NE2 . HIS D  223 ? 0.5103 0.4928 0.5052 0.1521  -0.1842 -0.1573 223 HIS D NE2 
14300 N N   . ARG D  224 ? 0.3986 0.4682 0.4378 0.1421  -0.1357 -0.1868 224 ARG D N   
14301 C CA  . ARG D  224 ? 0.4157 0.5015 0.4608 0.1389  -0.1251 -0.1912 224 ARG D CA  
14302 C C   . ARG D  224 ? 0.3978 0.4999 0.4451 0.1280  -0.1170 -0.1861 224 ARG D C   
14303 O O   . ARG D  224 ? 0.3635 0.4702 0.4135 0.1253  -0.1189 -0.1810 224 ARG D O   
14304 C CB  . ARG D  224 ? 0.4979 0.5996 0.5586 0.1496  -0.1247 -0.2021 224 ARG D CB  
14305 C CG  . ARG D  224 ? 0.5433 0.6273 0.5994 0.1585  -0.1306 -0.2053 224 ARG D CG  
14306 C CD  . ARG D  224 ? 0.5693 0.6650 0.6395 0.1701  -0.1347 -0.2128 224 ARG D CD  
14307 N NE  . ARG D  224 ? 0.6185 0.7033 0.6890 0.1767  -0.1462 -0.2102 224 ARG D NE  
14308 C CZ  . ARG D  224 ? 0.6879 0.7429 0.7443 0.1805  -0.1563 -0.2061 224 ARG D CZ  
14309 N NH1 . ARG D  224 ? 0.7224 0.7553 0.7636 0.1774  -0.1561 -0.2040 224 ARG D NH1 
14310 N NH2 . ARG D  224 ? 0.7009 0.7469 0.7568 0.1859  -0.1664 -0.2032 224 ARG D NH2 
14311 N N   . ALA D  225 ? 0.4623 0.5706 0.5069 0.1213  -0.1080 -0.1859 225 ALA D N   
14312 C CA  . ALA D  225 ? 0.4106 0.5322 0.4562 0.1117  -0.1008 -0.1814 225 ALA D CA  
14313 C C   . ALA D  225 ? 0.4019 0.5438 0.4547 0.1101  -0.0926 -0.1891 225 ALA D C   
14314 O O   . ALA D  225 ? 0.4038 0.5464 0.4564 0.1134  -0.0896 -0.1950 225 ALA D O   
14315 C CB  . ALA D  225 ? 0.2467 0.3552 0.2785 0.1024  -0.0980 -0.1705 225 ALA D CB  
14316 N N   . VAL D  226 ? 0.3118 0.4694 0.3699 0.1044  -0.0891 -0.1887 226 VAL D N   
14317 C CA  . VAL D  226 ? 0.2348 0.4119 0.2969 0.0999  -0.0808 -0.1950 226 VAL D CA  
14318 C C   . VAL D  226 ? 0.2275 0.4049 0.2815 0.0878  -0.0766 -0.1865 226 VAL D C   
14319 O O   . VAL D  226 ? 0.2532 0.4331 0.3099 0.0839  -0.0791 -0.1817 226 VAL D O   
14320 C CB  . VAL D  226 ? 0.2335 0.4339 0.3146 0.1046  -0.0798 -0.2027 226 VAL D CB  
14321 C CG1 . VAL D  226 ? 0.2312 0.4531 0.3166 0.0962  -0.0700 -0.2051 226 VAL D CG1 
14322 C CG2 . VAL D  226 ? 0.2435 0.4448 0.3325 0.1178  -0.0824 -0.2119 226 VAL D CG2 
14323 N N   . LEU D  227 ? 0.2306 0.4042 0.2743 0.0823  -0.0706 -0.1841 227 LEU D N   
14324 C CA  . LEU D  227 ? 0.2543 0.4251 0.2878 0.0720  -0.0672 -0.1762 227 LEU D CA  
14325 C C   . LEU D  227 ? 0.2548 0.4437 0.2885 0.0659  -0.0600 -0.1825 227 LEU D C   
14326 O O   . LEU D  227 ? 0.2377 0.4303 0.2671 0.0655  -0.0542 -0.1870 227 LEU D O   
14327 C CB  . LEU D  227 ? 0.2298 0.3829 0.2500 0.0695  -0.0668 -0.1683 227 LEU D CB  
14328 C CG  . LEU D  227 ? 0.2271 0.3635 0.2439 0.0719  -0.0725 -0.1604 227 LEU D CG  
14329 C CD1 . LEU D  227 ? 0.2328 0.3623 0.2529 0.0797  -0.0768 -0.1645 227 LEU D CD1 
14330 C CD2 . LEU D  227 ? 0.2277 0.3534 0.2322 0.0663  -0.0709 -0.1525 227 LEU D CD2 
14331 N N   . GLN D  228 ? 0.4020 0.6013 0.4403 0.0599  -0.0599 -0.1813 228 GLN D N   
14332 C CA  . GLN D  228 ? 0.4417 0.6580 0.4819 0.0516  -0.0518 -0.1831 228 GLN D CA  
14333 C C   . GLN D  228 ? 0.5381 0.7449 0.5623 0.0407  -0.0508 -0.1748 228 GLN D C   
14334 O O   . GLN D  228 ? 0.5986 0.7981 0.6208 0.0366  -0.0555 -0.1683 228 GLN D O   
14335 C CB  . GLN D  228 ? 0.2815 0.5162 0.3391 0.0503  -0.0518 -0.1852 228 GLN D CB  
14336 C CG  . GLN D  228 ? 0.2556 0.4970 0.3292 0.0627  -0.0559 -0.1921 228 GLN D CG  
14337 C CD  . GLN D  228 ? 0.2981 0.5619 0.3907 0.0615  -0.0558 -0.1951 228 GLN D CD  
14338 O OE1 . GLN D  228 ? 0.3178 0.5862 0.4238 0.0712  -0.0612 -0.1992 228 GLN D OE1 
14339 N NE2 . GLN D  228 ? 0.3239 0.6015 0.4174 0.0491  -0.0501 -0.1929 228 GLN D NE2 
14340 N N   . SER D  229 ? 0.3446 0.5503 0.3565 0.0365  -0.0453 -0.1754 229 SER D N   
14341 C CA  . SER D  229 ? 0.3114 0.5087 0.3067 0.0262  -0.0442 -0.1679 229 SER D CA  
14342 C C   . SER D  229 ? 0.2458 0.4228 0.2315 0.0274  -0.0524 -0.1601 229 SER D C   
14343 O O   . SER D  229 ? 0.2497 0.4195 0.2278 0.0206  -0.0547 -0.1534 229 SER D O   
14344 C CB  . SER D  229 ? 0.4798 0.6892 0.4779 0.0152  -0.0401 -0.1654 229 SER D CB  
14345 O OG  . SER D  229 ? 0.5146 0.7481 0.5262 0.0149  -0.0325 -0.1734 229 SER D OG  
14346 N N   . GLY D  230 ? 0.2402 0.4056 0.2281 0.0356  -0.0552 -0.1574 230 GLY D N   
14347 C CA  . GLY D  230 ? 0.2988 0.4459 0.2800 0.0370  -0.0602 -0.1474 230 GLY D CA  
14348 C C   . GLY D  230 ? 0.2761 0.4145 0.2597 0.0439  -0.0618 -0.1455 230 GLY D C   
14349 O O   . GLY D  230 ? 0.2314 0.3748 0.2236 0.0493  -0.0612 -0.1516 230 GLY D O   
14350 N N   . THR D  231 ? 0.2464 0.3721 0.2221 0.0436  -0.0642 -0.1376 231 THR D N   
14351 C CA  . THR D  231 ? 0.2406 0.3590 0.2166 0.0475  -0.0656 -0.1354 231 THR D CA  
14352 C C   . THR D  231 ? 0.2253 0.3347 0.1984 0.0484  -0.0690 -0.1274 231 THR D C   
14353 O O   . THR D  231 ? 0.2736 0.3799 0.2410 0.0461  -0.0701 -0.1230 231 THR D O   
14354 C CB  . THR D  231 ? 0.2593 0.3760 0.2266 0.0445  -0.0629 -0.1361 231 THR D CB  
14355 O OG1 . THR D  231 ? 0.2722 0.3887 0.2292 0.0388  -0.0617 -0.1334 231 THR D OG1 
14356 C CG2 . THR D  231 ? 0.2415 0.3654 0.2128 0.0464  -0.0595 -0.1449 231 THR D CG2 
14357 N N   . PRO D  232 ? 0.2232 0.3284 0.1992 0.0517  -0.0709 -0.1258 232 PRO D N   
14358 C CA  . PRO D  232 ? 0.2189 0.3188 0.1920 0.0522  -0.0730 -0.1192 232 PRO D CA  
14359 C C   . PRO D  232 ? 0.2225 0.3207 0.1872 0.0489  -0.0725 -0.1159 232 PRO D C   
14360 O O   . PRO D  232 ? 0.2212 0.3176 0.1831 0.0494  -0.0739 -0.1112 232 PRO D O   
14361 C CB  . PRO D  232 ? 0.2176 0.3149 0.1943 0.0547  -0.0748 -0.1197 232 PRO D CB  
14362 C CG  . PRO D  232 ? 0.2436 0.3413 0.2209 0.0547  -0.0738 -0.1255 232 PRO D CG  
14363 C CD  . PRO D  232 ? 0.2656 0.3704 0.2462 0.0549  -0.0715 -0.1305 232 PRO D CD  
14364 N N   . ASN D  233 ? 0.3013 0.4002 0.2618 0.0460  -0.0706 -0.1188 233 ASN D N   
14365 C CA  . ASN D  233 ? 0.3810 0.4783 0.3329 0.0427  -0.0708 -0.1156 233 ASN D CA  
14366 C C   . ASN D  233 ? 0.4109 0.5081 0.3554 0.0400  -0.0701 -0.1150 233 ASN D C   
14367 O O   . ASN D  233 ? 0.4354 0.5346 0.3813 0.0396  -0.0690 -0.1174 233 ASN D O   
14368 C CB  . ASN D  233 ? 0.4185 0.5147 0.3672 0.0403  -0.0698 -0.1187 233 ASN D CB  
14369 C CG  . ASN D  233 ? 0.4468 0.5452 0.3965 0.0403  -0.0668 -0.1256 233 ASN D CG  
14370 O OD1 . ASN D  233 ? 0.4462 0.5479 0.4031 0.0434  -0.0661 -0.1289 233 ASN D OD1 
14371 N ND2 . ASN D  233 ? 0.4776 0.5750 0.4198 0.0372  -0.0650 -0.1283 233 ASN D ND2 
14372 N N   . GLY D  234 ? 0.4979 0.5928 0.4334 0.0375  -0.0712 -0.1120 234 GLY D N   
14373 C CA  . GLY D  234 ? 0.5159 0.6085 0.4410 0.0342  -0.0715 -0.1110 234 GLY D CA  
14374 C C   . GLY D  234 ? 0.5047 0.5924 0.4249 0.0360  -0.0758 -0.1056 234 GLY D C   
14375 O O   . GLY D  234 ? 0.5695 0.6575 0.4954 0.0403  -0.0778 -0.1030 234 GLY D O   
14376 N N   . PRO D  235 ? 0.3240 0.4068 0.2323 0.0326  -0.0774 -0.1045 235 PRO D N   
14377 C CA  . PRO D  235 ? 0.3460 0.4213 0.2467 0.0347  -0.0827 -0.0998 235 PRO D CA  
14378 C C   . PRO D  235 ? 0.3769 0.4493 0.2838 0.0391  -0.0848 -0.0989 235 PRO D C   
14379 O O   . PRO D  235 ? 0.4264 0.4962 0.3343 0.0447  -0.0882 -0.0960 235 PRO D O   
14380 C CB  . PRO D  235 ? 0.3604 0.4298 0.2453 0.0284  -0.0837 -0.0998 235 PRO D CB  
14381 C CG  . PRO D  235 ? 0.2894 0.3661 0.1779 0.0238  -0.0779 -0.1054 235 PRO D CG  
14382 C CD  . PRO D  235 ? 0.2972 0.3815 0.1981 0.0267  -0.0742 -0.1082 235 PRO D CD  
14383 N N   . TRP D  236 ? 0.4658 0.5393 0.3766 0.0369  -0.0829 -0.1019 236 TRP D N   
14384 C CA  . TRP D  236 ? 0.4568 0.5246 0.3689 0.0393  -0.0862 -0.1011 236 TRP D CA  
14385 C C   . TRP D  236 ? 0.4825 0.5539 0.4081 0.0443  -0.0852 -0.1020 236 TRP D C   
14386 O O   . TRP D  236 ? 0.5092 0.5745 0.4342 0.0467  -0.0884 -0.1011 236 TRP D O   
14387 C CB  . TRP D  236 ? 0.2892 0.3547 0.1946 0.0324  -0.0865 -0.1034 236 TRP D CB  
14388 C CG  . TRP D  236 ? 0.3069 0.3843 0.2210 0.0291  -0.0810 -0.1088 236 TRP D CG  
14389 C CD1 . TRP D  236 ? 0.3684 0.4526 0.2787 0.0243  -0.0768 -0.1121 236 TRP D CD1 
14390 C CD2 . TRP D  236 ? 0.3683 0.4531 0.2968 0.0313  -0.0791 -0.1124 236 TRP D CD2 
14391 N NE1 . TRP D  236 ? 0.4186 0.5149 0.3409 0.0240  -0.0721 -0.1181 236 TRP D NE1 
14392 C CE2 . TRP D  236 ? 0.4169 0.5137 0.3507 0.0283  -0.0740 -0.1182 236 TRP D CE2 
14393 C CE3 . TRP D  236 ? 0.3882 0.4708 0.3250 0.0358  -0.0815 -0.1114 236 TRP D CE3 
14394 C CZ2 . TRP D  236 ? 0.4224 0.5292 0.3704 0.0304  -0.0719 -0.1233 236 TRP D CZ2 
14395 C CZ3 . TRP D  236 ? 0.3995 0.4911 0.3493 0.0369  -0.0795 -0.1157 236 TRP D CZ3 
14396 C CH2 . TRP D  236 ? 0.4069 0.5106 0.3626 0.0346  -0.0751 -0.1216 236 TRP D CH2 
14397 N N   . ALA D  237 ? 0.3063 0.3860 0.2422 0.0458  -0.0815 -0.1039 237 ALA D N   
14398 C CA  . ALA D  237 ? 0.2602 0.3428 0.2070 0.0493  -0.0809 -0.1052 237 ALA D CA  
14399 C C   . ALA D  237 ? 0.2299 0.3122 0.1800 0.0550  -0.0820 -0.1024 237 ALA D C   
14400 O O   . ALA D  237 ? 0.2249 0.3076 0.1810 0.0579  -0.0822 -0.1029 237 ALA D O   
14401 C CB  . ALA D  237 ? 0.2999 0.3899 0.2548 0.0482  -0.0774 -0.1093 237 ALA D CB  
14402 N N   . THR D  238 ? 0.3093 0.3920 0.2554 0.0565  -0.0827 -0.1001 238 THR D N   
14403 C CA  . THR D  238 ? 0.2815 0.3671 0.2309 0.0619  -0.0834 -0.0984 238 THR D CA  
14404 C C   . THR D  238 ? 0.2788 0.3626 0.2215 0.0649  -0.0863 -0.0965 238 THR D C   
14405 O O   . THR D  238 ? 0.2988 0.3808 0.2350 0.0617  -0.0872 -0.0958 238 THR D O   
14406 C CB  . THR D  238 ? 0.2771 0.3706 0.2322 0.0608  -0.0809 -0.0987 238 THR D CB  
14407 O OG1 . THR D  238 ? 0.2815 0.3778 0.2329 0.0579  -0.0808 -0.0981 238 THR D OG1 
14408 C CG2 . THR D  238 ? 0.2883 0.3823 0.2488 0.0583  -0.0789 -0.1012 238 THR D CG2 
14409 N N   . VAL D  239 ? 0.3052 0.3898 0.2488 0.0715  -0.0881 -0.0961 239 VAL D N   
14410 C CA  . VAL D  239 ? 0.3338 0.4214 0.2741 0.0762  -0.0906 -0.0952 239 VAL D CA  
14411 C C   . VAL D  239 ? 0.3311 0.4317 0.2785 0.0787  -0.0884 -0.0958 239 VAL D C   
14412 O O   . VAL D  239 ? 0.3013 0.4063 0.2545 0.0766  -0.0855 -0.0963 239 VAL D O   
14413 C CB  . VAL D  239 ? 0.3751 0.4537 0.3088 0.0837  -0.0955 -0.0955 239 VAL D CB  
14414 C CG1 . VAL D  239 ? 0.4048 0.4689 0.3292 0.0801  -0.0987 -0.0947 239 VAL D CG1 
14415 C CG2 . VAL D  239 ? 0.3880 0.4688 0.3262 0.0897  -0.0950 -0.0974 239 VAL D CG2 
14416 N N   . SER D  240 ? 0.4207 0.5279 0.3670 0.0832  -0.0904 -0.0957 240 SER D N   
14417 C CA  . SER D  240 ? 0.3997 0.5223 0.3523 0.0848  -0.0885 -0.0966 240 SER D CA  
14418 C C   . SER D  240 ? 0.4354 0.5614 0.3896 0.0932  -0.0888 -0.0989 240 SER D C   
14419 O O   . SER D  240 ? 0.4699 0.5844 0.4199 0.0980  -0.0911 -0.0998 240 SER D O   
14420 C CB  . SER D  240 ? 0.2394 0.3699 0.1909 0.0863  -0.0908 -0.0962 240 SER D CB  
14421 O OG  . SER D  240 ? 0.2495 0.3757 0.1962 0.0955  -0.0951 -0.0973 240 SER D OG  
14422 N N   . ALA D  241 ? 0.3646 0.5068 0.3241 0.0946  -0.0868 -0.1001 241 ALA D N   
14423 C CA  . ALA D  241 ? 0.3522 0.5012 0.3127 0.1033  -0.0867 -0.1032 241 ALA D CA  
14424 C C   . ALA D  241 ? 0.3318 0.4767 0.2874 0.1138  -0.0912 -0.1057 241 ALA D C   
14425 O O   . ALA D  241 ? 0.3414 0.4777 0.2929 0.1218  -0.0934 -0.1083 241 ALA D O   
14426 C CB  . ALA D  241 ? 0.3843 0.5550 0.3506 0.1018  -0.0839 -0.1040 241 ALA D CB  
14427 N N   . GLY D  242 ? 0.2495 0.3989 0.2045 0.1140  -0.0933 -0.1050 242 GLY D N   
14428 C CA  . GLY D  242 ? 0.2627 0.4083 0.2124 0.1245  -0.0985 -0.1073 242 GLY D CA  
14429 C C   . GLY D  242 ? 0.2733 0.3949 0.2133 0.1278  -0.1032 -0.1069 242 GLY D C   
14430 O O   . GLY D  242 ? 0.2842 0.3987 0.2193 0.1383  -0.1069 -0.1104 242 GLY D O   
14431 N N   . GLU D  243 ? 0.2922 0.4012 0.2284 0.1185  -0.1036 -0.1028 243 GLU D N   
14432 C CA  . GLU D  243 ? 0.3450 0.4320 0.2710 0.1188  -0.1082 -0.1016 243 GLU D CA  
14433 C C   . GLU D  243 ? 0.3715 0.4507 0.2974 0.1212  -0.1077 -0.1036 243 GLU D C   
14434 O O   . GLU D  243 ? 0.2965 0.3596 0.2136 0.1270  -0.1132 -0.1048 243 GLU D O   
14435 C CB  . GLU D  243 ? 0.4580 0.5380 0.3808 0.1070  -0.1072 -0.0974 243 GLU D CB  
14436 C CG  . GLU D  243 ? 0.5029 0.5620 0.4126 0.1054  -0.1127 -0.0955 243 GLU D CG  
14437 C CD  . GLU D  243 ? 0.5525 0.6023 0.4517 0.1132  -0.1203 -0.0952 243 GLU D CD  
14438 O OE1 . GLU D  243 ? 0.5665 0.6282 0.4696 0.1197  -0.1210 -0.0966 243 GLU D OE1 
14439 O OE2 . GLU D  243 ? 0.5809 0.6108 0.4670 0.1126  -0.1260 -0.0935 243 GLU D OE2 
14440 N N   . ALA D  244 ? 0.3304 0.4199 0.2648 0.1165  -0.1020 -0.1037 244 ALA D N   
14441 C CA  . ALA D  244 ? 0.2677 0.3521 0.2026 0.1188  -0.1015 -0.1056 244 ALA D CA  
14442 C C   . ALA D  244 ? 0.3014 0.3845 0.2321 0.1322  -0.1054 -0.1102 244 ALA D C   
14443 O O   . ALA D  244 ? 0.2920 0.3583 0.2150 0.1367  -0.1103 -0.1117 244 ALA D O   
14444 C CB  . ALA D  244 ? 0.4554 0.5534 0.3992 0.1138  -0.0955 -0.1053 244 ALA D CB  
14445 N N   . ARG D  245 ? 0.3414 0.4423 0.2765 0.1386  -0.1037 -0.1131 245 ARG D N   
14446 C CA  . ARG D  245 ? 0.3545 0.4579 0.2862 0.1530  -0.1069 -0.1191 245 ARG D CA  
14447 C C   . ARG D  245 ? 0.3105 0.3939 0.2307 0.1609  -0.1151 -0.1203 245 ARG D C   
14448 O O   . ARG D  245 ? 0.3246 0.3944 0.2373 0.1700  -0.1200 -0.1241 245 ARG D O   
14449 C CB  . ARG D  245 ? 0.5281 0.6580 0.4669 0.1576  -0.1033 -0.1223 245 ARG D CB  
14450 C CG  . ARG D  245 ? 0.6397 0.7727 0.5736 0.1730  -0.1079 -0.1287 245 ARG D CG  
14451 C CD  . ARG D  245 ? 0.7019 0.8643 0.6427 0.1789  -0.1033 -0.1339 245 ARG D CD  
14452 N NE  . ARG D  245 ? 0.7439 0.9118 0.6865 0.1800  -0.0998 -0.1361 245 ARG D NE  
14453 C CZ  . ARG D  245 ? 0.8039 0.9731 0.7419 0.1935  -0.1017 -0.1434 245 ARG D CZ  
14454 N NH1 . ARG D  245 ? 0.8016 0.9660 0.7318 0.2080  -0.1072 -0.1501 245 ARG D NH1 
14455 N NH2 . ARG D  245 ? 0.8284 1.0029 0.7684 0.1929  -0.0987 -0.1441 245 ARG D NH2 
14456 N N   . ARG D  246 ? 0.3734 0.4534 0.2911 0.1569  -0.1173 -0.1169 246 ARG D N   
14457 C CA  . ARG D  246 ? 0.3832 0.4426 0.2881 0.1631  -0.1260 -0.1168 246 ARG D CA  
14458 C C   . ARG D  246 ? 0.3613 0.3945 0.2558 0.1615  -0.1310 -0.1157 246 ARG D C   
14459 O O   . ARG D  246 ? 0.3891 0.4051 0.2730 0.1722  -0.1383 -0.1194 246 ARG D O   
14460 C CB  . ARG D  246 ? 0.5068 0.5657 0.4102 0.1547  -0.1268 -0.1113 246 ARG D CB  
14461 C CG  . ARG D  246 ? 0.6022 0.6524 0.4961 0.1637  -0.1347 -0.1120 246 ARG D CG  
14462 C CD  . ARG D  246 ? 0.6976 0.7163 0.5742 0.1638  -0.1435 -0.1092 246 ARG D CD  
14463 N NE  . ARG D  246 ? 0.7613 0.7722 0.6347 0.1482  -0.1418 -0.1027 246 ARG D NE  
14464 C CZ  . ARG D  246 ? 0.8360 0.8217 0.6944 0.1434  -0.1479 -0.0992 246 ARG D CZ  
14465 N NH1 . ARG D  246 ? 0.8880 0.8501 0.7321 0.1528  -0.1572 -0.1009 246 ARG D NH1 
14466 N NH2 . ARG D  246 ? 0.8401 0.8236 0.6963 0.1290  -0.1449 -0.0944 246 ARG D NH2 
14467 N N   . ARG D  247 ? 0.3344 0.3649 0.2317 0.1482  -0.1272 -0.1113 247 ARG D N   
14468 C CA  . ARG D  247 ? 0.3451 0.3528 0.2327 0.1432  -0.1317 -0.1094 247 ARG D CA  
14469 C C   . ARG D  247 ? 0.3830 0.3860 0.2705 0.1498  -0.1328 -0.1136 247 ARG D C   
14470 O O   . ARG D  247 ? 0.4081 0.3886 0.2836 0.1530  -0.1401 -0.1146 247 ARG D O   
14471 C CB  . ARG D  247 ? 0.3306 0.3415 0.2229 0.1275  -0.1265 -0.1047 247 ARG D CB  
14472 C CG  . ARG D  247 ? 0.3305 0.3427 0.2199 0.1203  -0.1263 -0.1007 247 ARG D CG  
14473 C CD  . ARG D  247 ? 0.3518 0.3701 0.2465 0.1066  -0.1205 -0.0978 247 ARG D CD  
14474 N NE  . ARG D  247 ? 0.3171 0.3378 0.2083 0.1003  -0.1201 -0.0947 247 ARG D NE  
14475 C CZ  . ARG D  247 ? 0.3724 0.3966 0.2649 0.0890  -0.1161 -0.0929 247 ARG D CZ  
14476 N NH1 . ARG D  247 ? 0.3816 0.4078 0.2799 0.0832  -0.1124 -0.0939 247 ARG D NH1 
14477 N NH2 . ARG D  247 ? 0.3829 0.4091 0.2707 0.0841  -0.1160 -0.0906 247 ARG D NH2 
14478 N N   . ALA D  248 ? 0.3324 0.3556 0.2318 0.1512  -0.1259 -0.1159 248 ALA D N   
14479 C CA  . ALA D  248 ? 0.4208 0.4420 0.3204 0.1566  -0.1263 -0.1196 248 ALA D CA  
14480 C C   . ALA D  248 ? 0.4524 0.4652 0.3432 0.1733  -0.1331 -0.1258 248 ALA D C   
14481 O O   . ALA D  248 ? 0.3728 0.3657 0.2538 0.1781  -0.1397 -0.1279 248 ALA D O   
14482 C CB  . ALA D  248 ? 0.3151 0.3601 0.2274 0.1543  -0.1179 -0.1203 248 ALA D CB  
14483 N N   . THR D  249 ? 0.3557 0.3838 0.2495 0.1822  -0.1319 -0.1292 249 THR D N   
14484 C CA  . THR D  249 ? 0.3767 0.3993 0.2622 0.1996  -0.1382 -0.1365 249 THR D CA  
14485 C C   . THR D  249 ? 0.4039 0.3928 0.2722 0.2038  -0.1495 -0.1360 249 THR D C   
14486 O O   . THR D  249 ? 0.4247 0.3967 0.2829 0.2155  -0.1566 -0.1413 249 THR D O   
14487 C CB  . THR D  249 ? 0.5728 0.6175 0.4639 0.2050  -0.1352 -0.1392 249 THR D CB  
14488 O OG1 . THR D  249 ? 0.5501 0.6250 0.4538 0.2048  -0.1265 -0.1417 249 THR D OG1 
14489 C CG2 . THR D  249 ? 0.6416 0.6767 0.5211 0.2226  -0.1431 -0.1470 249 THR D CG2 
14490 N N   . LEU D  250 ? 0.4059 0.3842 0.2697 0.1941  -0.1517 -0.1297 250 LEU D N   
14491 C CA  . LEU D  250 ? 0.4340 0.3789 0.2792 0.1957  -0.1628 -0.1278 250 LEU D CA  
14492 C C   . LEU D  250 ? 0.4454 0.3660 0.2813 0.1900  -0.1676 -0.1261 250 LEU D C   
14493 O O   . LEU D  250 ? 0.4742 0.3670 0.2940 0.1985  -0.1780 -0.1287 250 LEU D O   
14494 C CB  . LEU D  250 ? 0.4703 0.4126 0.3130 0.1842  -0.1629 -0.1204 250 LEU D CB  
14495 C CG  . LEU D  250 ? 0.4568 0.3655 0.2802 0.1777  -0.1725 -0.1153 250 LEU D CG  
14496 C CD1 . LEU D  250 ? 0.4900 0.3747 0.2967 0.1931  -0.1840 -0.1192 250 LEU D CD1 
14497 C CD2 . LEU D  250 ? 0.4481 0.3620 0.2721 0.1638  -0.1695 -0.1079 250 LEU D CD2 
14498 N N   . LEU D  251 ? 0.4248 0.3550 0.2701 0.1753  -0.1606 -0.1219 251 LEU D N   
14499 C CA  . LEU D  251 ? 0.4334 0.3449 0.2719 0.1679  -0.1640 -0.1205 251 LEU D CA  
14500 C C   . LEU D  251 ? 0.4444 0.3509 0.2804 0.1809  -0.1675 -0.1268 251 LEU D C   
14501 O O   . LEU D  251 ? 0.4803 0.3604 0.3025 0.1822  -0.1761 -0.1275 251 LEU D O   
14502 C CB  . LEU D  251 ? 0.4665 0.3942 0.3179 0.1522  -0.1549 -0.1168 251 LEU D CB  
14503 C CG  . LEU D  251 ? 0.4606 0.3694 0.3046 0.1453  -0.1592 -0.1164 251 LEU D CG  
14504 C CD1 . LEU D  251 ? 0.4919 0.3924 0.3318 0.1282  -0.1594 -0.1111 251 LEU D CD1 
14505 C CD2 . LEU D  251 ? 0.4351 0.3597 0.2910 0.1453  -0.1532 -0.1187 251 LEU D CD2 
14506 N N   . ALA D  252 ? 0.4747 0.4073 0.3235 0.1898  -0.1610 -0.1312 252 ALA D N   
14507 C CA  . ALA D  252 ? 0.5037 0.4365 0.3504 0.2048  -0.1642 -0.1380 252 ALA D CA  
14508 C C   . ALA D  252 ? 0.5414 0.4490 0.3711 0.2210  -0.1764 -0.1427 252 ALA D C   
14509 O O   . ALA D  252 ? 0.5658 0.4539 0.3847 0.2284  -0.1847 -0.1452 252 ALA D O   
14510 C CB  . ALA D  252 ? 0.4193 0.3859 0.2808 0.2116  -0.1553 -0.1419 252 ALA D CB  
14511 N N   . ARG D  253 ? 0.4789 0.3861 0.3053 0.2261  -0.1780 -0.1437 253 ARG D N   
14512 C CA  . ARG D  253 ? 0.5126 0.3957 0.3219 0.2422  -0.1894 -0.1492 253 ARG D CA  
14513 C C   . ARG D  253 ? 0.5419 0.3832 0.3313 0.2380  -0.2017 -0.1451 253 ARG D C   
14514 O O   . ARG D  253 ? 0.6669 0.4873 0.4418 0.2477  -0.2113 -0.1482 253 ARG D O   
14515 C CB  . ARG D  253 ? 0.5957 0.4846 0.4037 0.2443  -0.1888 -0.1500 253 ARG D CB  
14516 C CG  . ARG D  253 ? 0.6398 0.5190 0.4337 0.2591  -0.1967 -0.1569 253 ARG D CG  
14517 C CD  . ARG D  253 ? 0.6128 0.5290 0.4184 0.2659  -0.1890 -0.1628 253 ARG D CD  
14518 N NE  . ARG D  253 ? 0.5876 0.5303 0.4113 0.2566  -0.1780 -0.1593 253 ARG D NE  
14519 C CZ  . ARG D  253 ? 0.5975 0.5394 0.4235 0.2450  -0.1776 -0.1503 253 ARG D CZ  
14520 N NH1 . ARG D  253 ? 0.6566 0.5688 0.4657 0.2466  -0.1882 -0.1475 253 ARG D NH1 
14521 N NH2 . ARG D  253 ? 0.5527 0.5215 0.3958 0.2318  -0.1673 -0.1442 253 ARG D NH2 
14522 N N   . LEU D  254 ? 0.6555 0.4892 0.4438 0.2176  -0.1996 -0.1364 254 LEU D N   
14523 C CA  . LEU D  254 ? 0.6817 0.4767 0.4498 0.2092  -0.2103 -0.1318 254 LEU D CA  
14524 C C   . LEU D  254 ? 0.6997 0.4817 0.4632 0.2082  -0.2141 -0.1332 254 LEU D C   
14525 O O   . LEU D  254 ? 0.7479 0.4939 0.4910 0.2083  -0.2260 -0.1322 254 LEU D O   
14526 C CB  . LEU D  254 ? 0.5523 0.3466 0.3205 0.1874  -0.2064 -0.1231 254 LEU D CB  
14527 C CG  . LEU D  254 ? 0.5524 0.3512 0.3190 0.1890  -0.2064 -0.1206 254 LEU D CG  
14528 C CD1 . LEU D  254 ? 0.5309 0.3438 0.3049 0.1690  -0.1986 -0.1129 254 LEU D CD1 
14529 C CD2 . LEU D  254 ? 0.5949 0.3537 0.3358 0.1959  -0.2212 -0.1201 254 LEU D CD2 
14530 N N   . VAL D  255 ? 0.6641 0.4737 0.4448 0.2065  -0.2045 -0.1352 255 VAL D N   
14531 C CA  . VAL D  255 ? 0.6457 0.4453 0.4224 0.2049  -0.2074 -0.1367 255 VAL D CA  
14532 C C   . VAL D  255 ? 0.6773 0.4769 0.4496 0.2262  -0.2138 -0.1436 255 VAL D C   
14533 O O   . VAL D  255 ? 0.6254 0.4210 0.3949 0.2270  -0.2157 -0.1457 255 VAL D O   
14534 C CB  . VAL D  255 ? 0.5350 0.3597 0.3293 0.1908  -0.1956 -0.1347 255 VAL D CB  
14535 C CG1 . VAL D  255 ? 0.5232 0.3401 0.3166 0.1697  -0.1936 -0.1282 255 VAL D CG1 
14536 C CG2 . VAL D  255 ? 0.4916 0.3549 0.3061 0.1952  -0.1839 -0.1363 255 VAL D CG2 
14537 N N   . GLY D  256 ? 0.9327 0.7389 0.7044 0.2435  -0.2171 -0.1475 256 GLY D N   
14538 C CA  . GLY D  256 ? 1.0367 0.8496 0.8031 0.2576  -0.2207 -0.1536 256 GLY D CA  
14539 C C   . GLY D  256 ? 1.0568 0.9112 0.8420 0.2612  -0.2092 -0.1575 256 GLY D C   
14540 O O   . GLY D  256 ? 1.0708 0.9342 0.8523 0.2721  -0.2118 -0.1629 256 GLY D O   
14541 N N   . CYS D  257 ? 1.0059 0.8850 0.8096 0.2520  -0.1972 -0.1548 257 CYS D N   
14542 C CA  . CYS D  257 ? 0.9683 0.8858 0.7887 0.2535  -0.1861 -0.1575 257 CYS D CA  
14543 C C   . CYS D  257 ? 1.0434 0.9843 0.8675 0.2629  -0.1830 -0.1618 257 CYS D C   
14544 O O   . CYS D  257 ? 1.1276 1.0542 0.9418 0.2686  -0.1892 -0.1630 257 CYS D O   
14545 C CB  . CYS D  257 ? 0.7172 0.6516 0.5538 0.2410  -0.1758 -0.1534 257 CYS D CB  
14546 S SG  . CYS D  257 ? 1.2867 1.2057 1.1191 0.2302  -0.1771 -0.1511 257 CYS D SG  
14547 N N   . PRO D  258 ? 1.1005 1.0774 0.9389 0.2635  -0.1732 -0.1638 258 PRO D N   
14548 C CA  . PRO D  258 ? 1.1419 1.1326 0.9754 0.2761  -0.1769 -0.1699 258 PRO D CA  
14549 C C   . PRO D  258 ? 1.2032 1.1769 1.0191 0.2883  -0.1890 -0.1746 258 PRO D C   
14550 O O   . PRO D  258 ? 1.2247 1.1996 1.0389 0.2894  -0.1902 -0.1747 258 PRO D O   
14551 C CB  . PRO D  258 ? 0.7839 0.8157 0.6335 0.2753  -0.1659 -0.1712 258 PRO D CB  
14552 C CG  . PRO D  258 ? 0.7442 0.7758 0.6020 0.2666  -0.1593 -0.1674 258 PRO D CG  
14553 C CD  . PRO D  258 ? 0.7394 0.7447 0.5942 0.2563  -0.1612 -0.1621 258 PRO D CD  
14554 N N   . PRO D  259 ? 1.0624 1.0197 0.8634 0.2979  -0.1986 -0.1793 259 PRO D N   
14555 C CA  . PRO D  259 ? 1.1157 1.0429 0.8944 0.3085  -0.2128 -0.1835 259 PRO D CA  
14556 C C   . PRO D  259 ? 1.1744 1.1138 0.9459 0.3211  -0.2164 -0.1915 259 PRO D C   
14557 O O   . PRO D  259 ? 1.1138 1.0827 0.8897 0.3309  -0.2134 -0.1985 259 PRO D O   
14558 C CB  . PRO D  259 ? 0.9063 0.8185 0.6738 0.3160  -0.2202 -0.1873 259 PRO D CB  
14559 C CG  . PRO D  259 ? 0.8590 0.8029 0.6432 0.3126  -0.2091 -0.1873 259 PRO D CG  
14560 C CD  . PRO D  259 ? 0.8227 0.7825 0.6255 0.2976  -0.1971 -0.1801 259 PRO D CD  
14561 N N   . GLY D  260 ? 1.3854 1.3007 1.1449 0.3208  -0.2231 -0.1909 260 GLY D N   
14562 C CA  . GLY D  260 ? 1.4698 1.3813 1.2163 0.3344  -0.2304 -0.1992 260 GLY D CA  
14563 C C   . GLY D  260 ? 1.4855 1.4322 1.2461 0.3347  -0.2202 -0.2022 260 GLY D C   
14564 O O   . GLY D  260 ? 1.4857 1.4260 1.2404 0.3400  -0.2236 -0.2052 260 GLY D O   
14565 N N   . GLY D  261 ? 1.3843 1.3677 1.1636 0.3293  -0.2082 -0.2011 261 GLY D N   
14566 C CA  . GLY D  261 ? 1.3084 1.3238 1.1052 0.3215  -0.1953 -0.1997 261 GLY D CA  
14567 C C   . GLY D  261 ? 1.2316 1.2821 1.0425 0.3198  -0.1869 -0.1999 261 GLY D C   
14568 O O   . GLY D  261 ? 1.1882 1.2455 0.9941 0.3314  -0.1916 -0.2053 261 GLY D O   
14569 N N   . ALA D  262 ? 1.2337 1.3057 1.0610 0.3061  -0.1746 -0.1945 262 ALA D N   
14570 C CA  . ALA D  262 ? 1.1955 1.3042 1.0369 0.3039  -0.1661 -0.1944 262 ALA D CA  
14571 C C   . ALA D  262 ? 1.1742 1.3087 1.0283 0.2956  -0.1548 -0.1935 262 ALA D C   
14572 O O   . ALA D  262 ? 1.1885 1.3556 1.0484 0.3017  -0.1515 -0.1986 262 ALA D O   
14573 C CB  . ALA D  262 ? 0.9997 1.1028 0.8494 0.2950  -0.1633 -0.1868 262 ALA D CB  
14574 N N   . GLY D  263 ? 0.9943 1.1138 0.8540 0.2826  -0.1486 -0.1873 263 GLY D N   
14575 C CA  . GLY D  263 ? 0.9487 1.0907 0.8245 0.2740  -0.1376 -0.1841 263 GLY D CA  
14576 C C   . GLY D  263 ? 0.9325 1.1045 0.8191 0.2684  -0.1287 -0.1832 263 GLY D C   
14577 O O   . GLY D  263 ? 0.9036 1.0683 0.7872 0.2668  -0.1292 -0.1822 263 GLY D O   
14578 N N   . GLY D  264 ? 1.0853 1.2911 0.9830 0.2654  -0.1215 -0.1838 264 GLY D N   
14579 C CA  . GLY D  264 ? 1.0861 1.3238 0.9907 0.2624  -0.1152 -0.1843 264 GLY D CA  
14580 C C   . GLY D  264 ? 1.0498 1.2817 0.9680 0.2531  -0.1079 -0.1767 264 GLY D C   
14581 O O   . GLY D  264 ? 1.0179 1.2489 0.9438 0.2418  -0.1038 -0.1708 264 GLY D O   
14582 N N   . ASN D  265 ? 1.0014 1.2366 0.9221 0.2576  -0.1143 -0.1741 265 ASN D N   
14583 C CA  . ASN D  265 ? 1.0123 1.2395 0.9352 0.2489  -0.1103 -0.1700 265 ASN D CA  
14584 C C   . ASN D  265 ? 0.9397 1.1320 0.8592 0.2414  -0.1118 -0.1654 265 ASN D C   
14585 O O   . ASN D  265 ? 0.9667 1.1301 0.8764 0.2466  -0.1199 -0.1659 265 ASN D O   
14586 C CB  . ASN D  265 ? 1.2190 1.4439 1.1340 0.2571  -0.1157 -0.1734 265 ASN D CB  
14587 C CG  . ASN D  265 ? 1.2945 1.5526 1.2159 0.2553  -0.1091 -0.1746 265 ASN D CG  
14588 O OD1 . ASN D  265 ? 1.3068 1.5853 1.2384 0.2451  -0.1008 -0.1712 265 ASN D OD1 
14589 N ND2 . ASN D  265 ? 1.3338 1.5975 1.2483 0.2653  -0.1130 -0.1796 265 ASN D ND2 
14590 N N   . ASP D  266 ? 0.6734 0.8702 0.6007 0.2291  -0.1051 -0.1606 266 ASP D N   
14591 C CA  . ASP D  266 ? 0.5823 0.7519 0.5081 0.2211  -0.1068 -0.1559 266 ASP D CA  
14592 C C   . ASP D  266 ? 0.5583 0.7189 0.4809 0.2214  -0.1088 -0.1554 266 ASP D C   
14593 O O   . ASP D  266 ? 0.5708 0.7047 0.4883 0.2193  -0.1135 -0.1534 266 ASP D O   
14594 C CB  . ASP D  266 ? 0.7122 0.8930 0.6476 0.2089  -0.0995 -0.1517 266 ASP D CB  
14595 C CG  . ASP D  266 ? 0.7464 0.9332 0.6844 0.2074  -0.0980 -0.1518 266 ASP D CG  
14596 O OD1 . ASP D  266 ? 0.7868 0.9772 0.7203 0.2163  -0.1010 -0.1561 266 ASP D OD1 
14597 O OD2 . ASP D  266 ? 0.7292 0.9145 0.6715 0.1934  -0.0946 -0.1454 266 ASP D OD2 
14598 N N   . THR D  267 ? 0.7021 0.8868 0.6276 0.2238  -0.1054 -0.1575 267 THR D N   
14599 C CA  . THR D  267 ? 0.6692 0.8462 0.5903 0.2227  -0.1065 -0.1571 267 THR D CA  
14600 C C   . THR D  267 ? 0.6991 0.8514 0.6095 0.2337  -0.1165 -0.1605 267 THR D C   
14601 O O   . THR D  267 ? 0.7068 0.8342 0.6101 0.2272  -0.1188 -0.1579 267 THR D O   
14602 C CB  . THR D  267 ? 0.3934 0.6001 0.3163 0.2231  -0.1011 -0.1590 267 THR D CB  
14603 O OG1 . THR D  267 ? 0.3277 0.5548 0.2584 0.2109  -0.0926 -0.1550 267 THR D OG1 
14604 C CG2 . THR D  267 ? 0.3754 0.5673 0.2890 0.2180  -0.1012 -0.1577 267 THR D CG2 
14605 N N   . GLU D  268 ? 0.5295 0.6838 0.4347 0.2437  -0.1209 -0.1646 268 GLU D N   
14606 C CA  . GLU D  268 ? 0.5971 0.7261 0.4891 0.2536  -0.1313 -0.1679 268 GLU D CA  
14607 C C   . GLU D  268 ? 0.5684 0.6635 0.4550 0.2491  -0.1366 -0.1643 268 GLU D C   
14608 O O   . GLU D  268 ? 0.5639 0.6319 0.4406 0.2511  -0.1442 -0.1645 268 GLU D O   
14609 C CB  . GLU D  268 ? 1.0740 1.2166 0.9611 0.2665  -0.1353 -0.1740 268 GLU D CB  
14610 C CG  . GLU D  268 ? 1.2305 1.3521 1.1021 0.2791  -0.1464 -0.1791 268 GLU D CG  
14611 C CD  . GLU D  268 ? 1.3548 1.4900 1.2201 0.2927  -0.1513 -0.1862 268 GLU D CD  
14612 O OE1 . GLU D  268 ? 1.3748 1.4989 1.2354 0.2950  -0.1557 -0.1865 268 GLU D OE1 
14613 O OE2 . GLU D  268 ? 1.4059 1.5635 1.2701 0.3017  -0.1510 -0.1920 268 GLU D OE2 
14614 N N   . LEU D  269 ? 0.6478 0.7449 0.5401 0.2432  -0.1330 -0.1615 269 LEU D N   
14615 C CA  . LEU D  269 ? 0.5814 0.6497 0.4693 0.2377  -0.1371 -0.1579 269 LEU D CA  
14616 C C   . LEU D  269 ? 0.5183 0.5721 0.4077 0.2284  -0.1369 -0.1540 269 LEU D C   
14617 O O   . LEU D  269 ? 0.5293 0.5563 0.4083 0.2282  -0.1443 -0.1535 269 LEU D O   
14618 C CB  . LEU D  269 ? 0.4306 0.5070 0.3246 0.2331  -0.1325 -0.1562 269 LEU D CB  
14619 C CG  . LEU D  269 ? 0.4174 0.4764 0.3124 0.2236  -0.1327 -0.1515 269 LEU D CG  
14620 C CD1 . LEU D  269 ? 0.3939 0.4182 0.2770 0.2242  -0.1422 -0.1502 269 LEU D CD1 
14621 C CD2 . LEU D  269 ? 0.3756 0.4403 0.2715 0.2245  -0.1314 -0.1521 269 LEU D CD2 
14622 N N   . ILE D  270 ? 0.4532 0.5230 0.3526 0.2157  -0.1276 -0.1500 270 ILE D N   
14623 C CA  . ILE D  270 ? 0.4628 0.5209 0.3620 0.2004  -0.1251 -0.1446 270 ILE D CA  
14624 C C   . ILE D  270 ? 0.4640 0.5111 0.3552 0.2032  -0.1292 -0.1468 270 ILE D C   
14625 O O   . ILE D  270 ? 0.4052 0.4333 0.2921 0.1939  -0.1313 -0.1439 270 ILE D O   
14626 C CB  . ILE D  270 ? 0.4334 0.5129 0.3429 0.1890  -0.1154 -0.1408 270 ILE D CB  
14627 C CG1 . ILE D  270 ? 0.4630 0.5563 0.3801 0.1863  -0.1111 -0.1392 270 ILE D CG1 
14628 C CG2 . ILE D  270 ? 0.3724 0.4388 0.2822 0.1744  -0.1142 -0.1353 270 ILE D CG2 
14629 C CD1 . ILE D  270 ? 0.4934 0.5681 0.4093 0.1782  -0.1133 -0.1349 270 ILE D CD1 
14630 N N   . ALA D  271 ? 0.4495 0.5104 0.3385 0.2158  -0.1303 -0.1522 271 ALA D N   
14631 C CA  . ALA D  271 ? 0.4609 0.5102 0.3398 0.2205  -0.1351 -0.1553 271 ALA D CA  
14632 C C   . ALA D  271 ? 0.4926 0.5090 0.3597 0.2231  -0.1453 -0.1558 271 ALA D C   
14633 O O   . ALA D  271 ? 0.4231 0.4201 0.2851 0.2135  -0.1473 -0.1534 271 ALA D O   
14634 C CB  . ALA D  271 ? 0.4884 0.5580 0.3658 0.2349  -0.1358 -0.1614 271 ALA D CB  
14635 N N   . CYS D  272 ? 0.5668 0.5774 0.4290 0.2356  -0.1523 -0.1589 272 CYS D N   
14636 C CA  . CYS D  272 ? 0.5825 0.5594 0.4307 0.2387  -0.1633 -0.1593 272 CYS D CA  
14637 C C   . CYS D  272 ? 0.5518 0.5084 0.3995 0.2216  -0.1626 -0.1532 272 CYS D C   
14638 O O   . CYS D  272 ? 0.5439 0.4754 0.3812 0.2164  -0.1685 -0.1525 272 CYS D O   
14639 C CB  . CYS D  272 ? 0.5662 0.5410 0.4100 0.2527  -0.1704 -0.1621 272 CYS D CB  
14640 S SG  . CYS D  272 ? 1.2687 1.2008 1.0967 0.2510  -0.1822 -0.1594 272 CYS D SG  
14641 N N   . LEU D  273 ? 0.4896 0.4591 0.3484 0.2124  -0.1553 -0.1489 273 LEU D N   
14642 C CA  . LEU D  273 ? 0.4599 0.4168 0.3201 0.1959  -0.1537 -0.1430 273 LEU D CA  
14643 C C   . LEU D  273 ? 0.4604 0.4125 0.3210 0.1844  -0.1521 -0.1410 273 LEU D C   
14644 O O   . LEU D  273 ? 0.4638 0.3955 0.3183 0.1748  -0.1565 -0.1386 273 LEU D O   
14645 C CB  . LEU D  273 ? 0.3949 0.3727 0.2682 0.1886  -0.1449 -0.1394 273 LEU D CB  
14646 C CG  . LEU D  273 ? 0.4551 0.4237 0.3259 0.1869  -0.1473 -0.1371 273 LEU D CG  
14647 C CD1 . LEU D  273 ? 0.4174 0.4099 0.3012 0.1810  -0.1382 -0.1343 273 LEU D CD1 
14648 C CD2 . LEU D  273 ? 0.4585 0.4025 0.3214 0.1743  -0.1520 -0.1329 273 LEU D CD2 
14649 N N   . ARG D  274 ? 0.5221 0.4931 0.3890 0.1854  -0.1463 -0.1423 274 ARG D N   
14650 C CA  . ARG D  274 ? 0.5194 0.4890 0.3876 0.1750  -0.1443 -0.1405 274 ARG D CA  
14651 C C   . ARG D  274 ? 0.5525 0.4983 0.4078 0.1763  -0.1527 -0.1432 274 ARG D C   
14652 O O   . ARG D  274 ? 0.5505 0.4915 0.4056 0.1672  -0.1528 -0.1419 274 ARG D O   
14653 C CB  . ARG D  274 ? 0.4805 0.4738 0.3552 0.1770  -0.1372 -0.1415 274 ARG D CB  
14654 C CG  . ARG D  274 ? 0.4991 0.5080 0.3854 0.1653  -0.1293 -0.1364 274 ARG D CG  
14655 C CD  . ARG D  274 ? 0.5479 0.5750 0.4364 0.1659  -0.1238 -0.1371 274 ARG D CD  
14656 N NE  . ARG D  274 ? 0.5775 0.6276 0.4714 0.1715  -0.1182 -0.1381 274 ARG D NE  
14657 C CZ  . ARG D  274 ? 0.5974 0.6639 0.4994 0.1641  -0.1115 -0.1344 274 ARG D CZ  
14658 N NH1 . ARG D  274 ? 0.5753 0.6375 0.4811 0.1522  -0.1097 -0.1296 274 ARG D NH1 
14659 N NH2 . ARG D  274 ? 0.6239 0.7117 0.5300 0.1689  -0.1070 -0.1358 274 ARG D NH2 
14660 N N   . THR D  275 ? 0.5105 0.4415 0.3547 0.1881  -0.1604 -0.1470 275 THR D N   
14661 C CA  . THR D  275 ? 0.5359 0.4420 0.3654 0.1913  -0.1696 -0.1502 275 THR D CA  
14662 C C   . THR D  275 ? 0.5877 0.4646 0.4072 0.1842  -0.1777 -0.1479 275 THR D C   
14663 O O   . THR D  275 ? 0.6564 0.5094 0.4624 0.1848  -0.1860 -0.1500 275 THR D O   
14664 C CB  . THR D  275 ? 0.4959 0.4020 0.3168 0.2099  -0.1745 -0.1565 275 THR D CB  
14665 O OG1 . THR D  275 ? 0.5079 0.4026 0.3231 0.2179  -0.1807 -0.1568 275 THR D OG1 
14666 C CG2 . THR D  275 ? 0.5527 0.4916 0.3840 0.2169  -0.1661 -0.1586 275 THR D CG2 
14667 N N   . ARG D  276 ? 0.5089 0.3868 0.3336 0.1770  -0.1755 -0.1435 276 ARG D N   
14668 C CA  . ARG D  276 ? 0.4992 0.3505 0.3137 0.1681  -0.1827 -0.1407 276 ARG D CA  
14669 C C   . ARG D  276 ? 0.4891 0.3407 0.3091 0.1496  -0.1800 -0.1370 276 ARG D C   
14670 O O   . ARG D  276 ? 0.4620 0.3367 0.2968 0.1427  -0.1713 -0.1346 276 ARG D O   
14671 C CB  . ARG D  276 ? 0.5570 0.4096 0.3730 0.1688  -0.1819 -0.1379 276 ARG D CB  
14672 C CG  . ARG D  276 ? 0.5957 0.4488 0.4066 0.1875  -0.1856 -0.1418 276 ARG D CG  
14673 C CD  . ARG D  276 ? 0.6665 0.4849 0.4568 0.1941  -0.1988 -0.1433 276 ARG D CD  
14674 N NE  . ARG D  276 ? 0.7362 0.5568 0.5217 0.2143  -0.2037 -0.1477 276 ARG D NE  
14675 C CZ  . ARG D  276 ? 0.8072 0.6339 0.5899 0.2289  -0.2066 -0.1534 276 ARG D CZ  
14676 N NH1 . ARG D  276 ? 0.8135 0.6422 0.5968 0.2249  -0.2045 -0.1551 276 ARG D NH1 
14677 N NH2 . ARG D  276 ? 0.8435 0.6753 0.6220 0.2474  -0.2120 -0.1576 276 ARG D NH2 
14678 N N   . PRO D  277 ? 0.5744 0.4004 0.3825 0.1414  -0.1881 -0.1365 277 PRO D N   
14679 C CA  . PRO D  277 ? 0.5725 0.3998 0.3862 0.1230  -0.1867 -0.1332 277 PRO D CA  
14680 C C   . PRO D  277 ? 0.5651 0.4064 0.3891 0.1136  -0.1806 -0.1287 277 PRO D C   
14681 O O   . PRO D  277 ? 0.6095 0.4473 0.4299 0.1188  -0.1811 -0.1275 277 PRO D O   
14682 C CB  . PRO D  277 ? 0.5390 0.3331 0.3350 0.1167  -0.1978 -0.1334 277 PRO D CB  
14683 C CG  . PRO D  277 ? 0.5633 0.3369 0.3442 0.1314  -0.2050 -0.1355 277 PRO D CG  
14684 C CD  . PRO D  277 ? 0.5486 0.3432 0.3371 0.1485  -0.1996 -0.1390 277 PRO D CD  
14685 N N   . ALA D  278 ? 0.4683 0.3259 0.3048 0.1010  -0.1753 -0.1265 278 ALA D N   
14686 C CA  . ALA D  278 ? 0.4506 0.3256 0.2984 0.0938  -0.1686 -0.1228 278 ALA D CA  
14687 C C   . ALA D  278 ? 0.4783 0.3365 0.3160 0.0867  -0.1734 -0.1203 278 ALA D C   
14688 O O   . ALA D  278 ? 0.4784 0.3431 0.3180 0.0885  -0.1701 -0.1181 278 ALA D O   
14689 C CB  . ALA D  278 ? 0.4277 0.3209 0.2895 0.0820  -0.1639 -0.1216 278 ALA D CB  
14690 N N   . GLN D  279 ? 0.5684 0.4036 0.3938 0.0781  -0.1816 -0.1203 279 GLN D N   
14691 C CA  . GLN D  279 ? 0.6288 0.4459 0.4427 0.0678  -0.1868 -0.1171 279 GLN D CA  
14692 C C   . GLN D  279 ? 0.6693 0.4691 0.4696 0.0799  -0.1911 -0.1165 279 GLN D C   
14693 O O   . GLN D  279 ? 0.7082 0.5021 0.5027 0.0744  -0.1921 -0.1131 279 GLN D O   
14694 C CB  . GLN D  279 ? 0.6882 0.4829 0.4910 0.0549  -0.1953 -0.1170 279 GLN D CB  
14695 C CG  . GLN D  279 ? 0.7406 0.5209 0.5336 0.0389  -0.1994 -0.1128 279 GLN D CG  
14696 C CD  . GLN D  279 ? 0.7554 0.5628 0.5629 0.0301  -0.1910 -0.1107 279 GLN D CD  
14697 O OE1 . GLN D  279 ? 0.7566 0.5903 0.5819 0.0247  -0.1847 -0.1121 279 GLN D OE1 
14698 N NE2 . GLN D  279 ? 0.7733 0.5736 0.5722 0.0292  -0.1915 -0.1074 279 GLN D NE2 
14699 N N   . ASP D  280 ? 0.5568 0.3499 0.3522 0.0968  -0.1939 -0.1201 280 ASP D N   
14700 C CA  . ASP D  280 ? 0.5599 0.3412 0.3450 0.1114  -0.1980 -0.1207 280 ASP D CA  
14701 C C   . ASP D  280 ? 0.5211 0.3276 0.3189 0.1146  -0.1894 -0.1190 280 ASP D C   
14702 O O   . ASP D  280 ? 0.5567 0.3537 0.3462 0.1165  -0.1925 -0.1168 280 ASP D O   
14703 C CB  . ASP D  280 ? 0.7732 0.5491 0.5537 0.1298  -0.2017 -0.1260 280 ASP D CB  
14704 C CG  . ASP D  280 ? 0.9379 0.6797 0.6993 0.1295  -0.2134 -0.1275 280 ASP D CG  
14705 O OD1 . ASP D  280 ? 0.9742 0.6998 0.7286 0.1127  -0.2173 -0.1242 280 ASP D OD1 
14706 O OD2 . ASP D  280 ? 1.0087 0.7408 0.7619 0.1456  -0.2188 -0.1320 280 ASP D OD2 
14707 N N   . LEU D  281 ? 0.4785 0.3158 0.2955 0.1145  -0.1792 -0.1197 281 LEU D N   
14708 C CA  . LEU D  281 ? 0.4786 0.3399 0.3080 0.1155  -0.1708 -0.1178 281 LEU D CA  
14709 C C   . LEU D  281 ? 0.4771 0.3367 0.3049 0.1007  -0.1701 -0.1132 281 LEU D C   
14710 O O   . LEU D  281 ? 0.4548 0.3117 0.2776 0.1027  -0.1710 -0.1111 281 LEU D O   
14711 C CB  . LEU D  281 ? 0.4231 0.3139 0.2713 0.1158  -0.1608 -0.1186 281 LEU D CB  
14712 C CG  . LEU D  281 ? 0.4140 0.3197 0.2679 0.1314  -0.1571 -0.1217 281 LEU D CG  
14713 C CD1 . LEU D  281 ? 0.4403 0.3269 0.2802 0.1459  -0.1658 -0.1257 281 LEU D CD1 
14714 C CD2 . LEU D  281 ? 0.3967 0.3210 0.2622 0.1315  -0.1509 -0.1230 281 LEU D CD2 
14715 N N   . VAL D  282 ? 0.5176 0.3792 0.3491 0.0859  -0.1692 -0.1120 282 VAL D N   
14716 C CA  . VAL D  282 ? 0.5133 0.3766 0.3440 0.0706  -0.1681 -0.1085 282 VAL D CA  
14717 C C   . VAL D  282 ? 0.5373 0.3725 0.3472 0.0670  -0.1769 -0.1056 282 VAL D C   
14718 O O   . VAL D  282 ? 0.5545 0.3934 0.3621 0.0603  -0.1751 -0.1024 282 VAL D O   
14719 C CB  . VAL D  282 ? 0.5330 0.4035 0.3712 0.0558  -0.1669 -0.1089 282 VAL D CB  
14720 C CG1 . VAL D  282 ? 0.5309 0.3918 0.3605 0.0390  -0.1705 -0.1062 282 VAL D CG1 
14721 C CG2 . VAL D  282 ? 0.5581 0.4601 0.4173 0.0559  -0.1570 -0.1097 282 VAL D CG2 
14722 N N   . ASP D  283 ? 0.5297 0.3354 0.3229 0.0717  -0.1867 -0.1065 283 ASP D N   
14723 C CA  . ASP D  283 ? 0.5907 0.3643 0.3609 0.0691  -0.1966 -0.1031 283 ASP D CA  
14724 C C   . ASP D  283 ? 0.6674 0.4447 0.4350 0.0796  -0.1957 -0.1016 283 ASP D C   
14725 O O   . ASP D  283 ? 0.7298 0.5049 0.4909 0.0703  -0.1957 -0.0972 283 ASP D O   
14726 C CB  . ASP D  283 ? 0.6456 0.3856 0.3982 0.0761  -0.2079 -0.1049 283 ASP D CB  
14727 C CG  . ASP D  283 ? 0.6983 0.4264 0.4472 0.0607  -0.2114 -0.1046 283 ASP D CG  
14728 O OD1 . ASP D  283 ? 0.7132 0.4571 0.4713 0.0437  -0.2063 -0.1025 283 ASP D OD1 
14729 O OD2 . ASP D  283 ? 0.7217 0.4260 0.4590 0.0655  -0.2195 -0.1066 283 ASP D OD2 
14730 N N   . HIS D  284 ? 0.5449 0.3312 0.3188 0.0982  -0.1942 -0.1054 284 HIS D N   
14731 C CA  . HIS D  284 ? 0.5823 0.3733 0.3547 0.1086  -0.1940 -0.1045 284 HIS D CA  
14732 C C   . HIS D  284 ? 0.5325 0.3591 0.3247 0.1039  -0.1817 -0.1031 284 HIS D C   
14733 O O   . HIS D  284 ? 0.5286 0.3658 0.3239 0.1115  -0.1795 -0.1026 284 HIS D O   
14734 C CB  . HIS D  284 ? 0.9232 0.7118 0.6949 0.1304  -0.1975 -0.1099 284 HIS D CB  
14735 C CG  . HIS D  284 ? 1.0959 0.8489 0.8478 0.1373  -0.2100 -0.1120 284 HIS D CG  
14736 N ND1 . HIS D  284 ? 1.1694 0.9194 0.9233 0.1395  -0.2110 -0.1157 284 HIS D ND1 
14737 C CD2 . HIS D  284 ? 1.1961 0.9130 0.9243 0.1422  -0.2229 -0.1107 284 HIS D CD2 
14738 C CE1 . HIS D  284 ? 1.2322 0.9465 0.9651 0.1456  -0.2236 -0.1168 284 HIS D CE1 
14739 N NE2 . HIS D  284 ? 1.2688 0.9614 0.9854 0.1476  -0.2314 -0.1137 284 HIS D NE2 
14740 N N   . GLU D  285 ? 0.4685 0.3137 0.2744 0.0920  -0.1742 -0.1029 285 GLU D N   
14741 C CA  . GLU D  285 ? 0.4505 0.3266 0.2739 0.0876  -0.1634 -0.1018 285 GLU D CA  
14742 C C   . GLU D  285 ? 0.5310 0.4048 0.3464 0.0802  -0.1638 -0.0976 285 GLU D C   
14743 O O   . GLU D  285 ? 0.4248 0.3175 0.2492 0.0835  -0.1578 -0.0968 285 GLU D O   
14744 C CB  . GLU D  285 ? 0.8059 0.6993 0.6435 0.0766  -0.1568 -0.1026 285 GLU D CB  
14745 C CG  . GLU D  285 ? 0.7638 0.6863 0.6186 0.0734  -0.1464 -0.1020 285 GLU D CG  
14746 C CD  . GLU D  285 ? 0.7425 0.6777 0.6083 0.0622  -0.1422 -0.1029 285 GLU D CD  
14747 O OE1 . GLU D  285 ? 0.7526 0.6847 0.6137 0.0494  -0.1437 -0.1020 285 GLU D OE1 
14748 O OE2 . GLU D  285 ? 0.7137 0.6617 0.5921 0.0661  -0.1380 -0.1048 285 GLU D OE2 
14749 N N   . TRP D  286 ? 1.1047 0.9545 0.9018 0.0695  -0.1712 -0.0944 286 TRP D N   
14750 C CA  . TRP D  286 ? 1.1882 1.0348 0.9752 0.0641  -0.1721 -0.0900 286 TRP D CA  
14751 C C   . TRP D  286 ? 1.1917 1.0111 0.9596 0.0752  -0.1824 -0.0882 286 TRP D C   
14752 O O   . TRP D  286 ? 1.2217 1.0090 0.9671 0.0698  -0.1925 -0.0848 286 TRP D O   
14753 C CB  . TRP D  286 ? 1.1776 1.0168 0.9548 0.0439  -0.1732 -0.0869 286 TRP D CB  
14754 C CG  . TRP D  286 ? 1.2208 1.0886 1.0174 0.0342  -0.1636 -0.0897 286 TRP D CG  
14755 C CD1 . TRP D  286 ? 1.2196 1.0913 1.0245 0.0272  -0.1629 -0.0926 286 TRP D CD1 
14756 C CD2 . TRP D  286 ? 1.2774 1.1733 1.0877 0.0316  -0.1541 -0.0904 286 TRP D CD2 
14757 N NE1 . TRP D  286 ? 1.2090 1.1097 1.0321 0.0212  -0.1540 -0.0951 286 TRP D NE1 
14758 C CE2 . TRP D  286 ? 1.2583 1.1731 1.0844 0.0239  -0.1485 -0.0941 286 TRP D CE2 
14759 C CE3 . TRP D  286 ? 1.3154 1.2216 1.1257 0.0352  -0.1504 -0.0886 286 TRP D CE3 
14760 C CZ2 . TRP D  286 ? 1.2763 1.2185 1.1176 0.0209  -0.1395 -0.0963 286 TRP D CZ2 
14761 C CZ3 . TRP D  286 ? 1.2907 1.2240 1.1158 0.0309  -0.1410 -0.0906 286 TRP D CZ3 
14762 C CH2 . TRP D  286 ? 1.2709 1.2210 1.1109 0.0244  -0.1358 -0.0946 286 TRP D CH2 
14763 N N   . HIS D  287 ? 0.8870 0.7206 0.6644 0.0905  -0.1798 -0.0904 287 HIS D N   
14764 C CA  . HIS D  287 ? 0.9115 0.7303 0.6768 0.1034  -0.1873 -0.0895 287 HIS D CA  
14765 C C   . HIS D  287 ? 0.8709 0.7206 0.6529 0.1086  -0.1787 -0.0900 287 HIS D C   
14766 O O   . HIS D  287 ? 0.9217 0.7719 0.6975 0.1058  -0.1793 -0.0860 287 HIS D O   
14767 C CB  . HIS D  287 ? 1.2495 1.0517 1.0097 0.1203  -0.1948 -0.0946 287 HIS D CB  
14768 C CG  . HIS D  287 ? 1.4102 1.1704 1.1449 0.1180  -0.2080 -0.0928 287 HIS D CG  
14769 N ND1 . HIS D  287 ? 1.4669 1.2097 1.1884 0.0988  -0.2108 -0.0876 287 HIS D ND1 
14770 C CD2 . HIS D  287 ? 1.4822 1.2134 1.2013 0.1321  -0.2195 -0.0958 287 HIS D CD2 
14771 C CE1 . HIS D  287 ? 1.5156 1.2188 1.2139 0.0997  -0.2236 -0.0864 287 HIS D CE1 
14772 N NE2 . HIS D  287 ? 1.5211 1.2155 1.2170 0.1205  -0.2295 -0.0915 287 HIS D NE2 
14773 N N   . VAL D  288 ? 0.8502 0.7250 0.6527 0.1151  -0.1706 -0.0946 288 VAL D N   
14774 C CA  . VAL D  288 ? 0.8454 0.7483 0.6643 0.1223  -0.1632 -0.0963 288 VAL D CA  
14775 C C   . VAL D  288 ? 0.9327 0.8513 0.7560 0.1130  -0.1576 -0.0922 288 VAL D C   
14776 O O   . VAL D  288 ? 0.9378 0.8727 0.7692 0.1194  -0.1547 -0.0928 288 VAL D O   
14777 C CB  . VAL D  288 ? 0.6981 0.6242 0.5366 0.1240  -0.1543 -0.1002 288 VAL D CB  
14778 C CG1 . VAL D  288 ? 0.7098 0.6233 0.5445 0.1342  -0.1592 -0.1049 288 VAL D CG1 
14779 C CG2 . VAL D  288 ? 0.6485 0.5841 0.4947 0.1085  -0.1476 -0.0981 288 VAL D CG2 
14780 N N   . LEU D  289 ? 0.9847 0.8997 0.8027 0.0978  -0.1559 -0.0887 289 LEU D N   
14781 C CA  . LEU D  289 ? 0.9941 0.9213 0.8130 0.0884  -0.1512 -0.0854 289 LEU D CA  
14782 C C   . LEU D  289 ? 1.0752 0.9938 0.8824 0.0943  -0.1572 -0.0824 289 LEU D C   
14783 O O   . LEU D  289 ? 1.1025 0.9940 0.8897 0.0953  -0.1670 -0.0796 289 LEU D O   
14784 C CB  . LEU D  289 ? 1.0362 0.9537 0.8441 0.0724  -0.1516 -0.0828 289 LEU D CB  
14785 C CG  . LEU D  289 ? 1.0289 0.9671 0.8513 0.0620  -0.1421 -0.0851 289 LEU D CG  
14786 C CD1 . LEU D  289 ? 1.0436 0.9725 0.8522 0.0464  -0.1435 -0.0832 289 LEU D CD1 
14787 C CD2 . LEU D  289 ? 1.0072 0.9704 0.8445 0.0635  -0.1338 -0.0858 289 LEU D CD2 
14788 N N   . PRO D  290 ? 1.2168 1.1569 1.0356 0.0974  -0.1521 -0.0827 290 PRO D N   
14789 C CA  . PRO D  290 ? 1.2342 1.1735 1.0478 0.1054  -0.1567 -0.0811 290 PRO D CA  
14790 C C   . PRO D  290 ? 1.2888 1.2058 1.0797 0.0998  -0.1645 -0.0753 290 PRO D C   
14791 O O   . PRO D  290 ? 1.2896 1.1900 1.0686 0.1091  -0.1735 -0.0739 290 PRO D O   
14792 C CB  . PRO D  290 ? 1.0500 1.0182 0.8803 0.1021  -0.1477 -0.0817 290 PRO D CB  
14793 C CG  . PRO D  290 ? 1.0284 1.0070 0.8674 0.0904  -0.1394 -0.0825 290 PRO D CG  
14794 C CD  . PRO D  290 ? 1.0538 1.0208 0.8919 0.0920  -0.1412 -0.0847 290 PRO D CD  
14795 N N   . GLN D  291 ? 1.4258 1.3423 1.2099 0.0847  -0.1611 -0.0722 291 GLN D N   
14796 C CA  . GLN D  291 ? 1.4851 1.3801 1.2452 0.0767  -0.1676 -0.0661 291 GLN D CA  
14797 C C   . GLN D  291 ? 1.5223 1.4088 1.2723 0.0605  -0.1655 -0.0646 291 GLN D C   
14798 O O   . GLN D  291 ? 1.4897 1.3920 1.2545 0.0557  -0.1579 -0.0688 291 GLN D O   
14799 C CB  . GLN D  291 ? 1.2568 1.1647 1.0162 0.0747  -0.1656 -0.0635 291 GLN D CB  
14800 C CG  . GLN D  291 ? 1.1896 1.1221 0.9601 0.0635  -0.1546 -0.0653 291 GLN D CG  
14801 C CD  . GLN D  291 ? 1.1189 1.0777 0.9158 0.0686  -0.1462 -0.0708 291 GLN D CD  
14802 O OE1 . GLN D  291 ? 1.1082 1.0730 0.9157 0.0662  -0.1412 -0.0742 291 GLN D OE1 
14803 N NE2 . GLN D  291 ? 1.0726 1.0466 0.8795 0.0748  -0.1450 -0.0715 291 GLN D NE2 
14804 N N   . GLU D  292 ? 1.5150 1.3759 1.2393 0.0519  -0.1725 -0.0584 292 GLU D N   
14805 C CA  . GLU D  292 ? 1.4914 1.3430 1.2028 0.0343  -0.1710 -0.0563 292 GLU D CA  
14806 C C   . GLU D  292 ? 1.3896 1.2708 1.1141 0.0250  -0.1591 -0.0598 292 GLU D C   
14807 O O   . GLU D  292 ? 1.3704 1.2629 1.0931 0.0233  -0.1557 -0.0585 292 GLU D O   
14808 C CB  . GLU D  292 ? 1.5031 1.3243 1.1829 0.0251  -0.1794 -0.0474 292 GLU D CB  
14809 C CG  . GLU D  292 ? 1.5545 1.3606 1.2163 0.0046  -0.1793 -0.0437 292 GLU D CG  
14810 C CD  . GLU D  292 ? 1.6260 1.4011 1.2548 -0.0062 -0.1871 -0.0333 292 GLU D CD  
14811 O OE1 . GLU D  292 ? 1.6400 1.4114 1.2618 0.0015  -0.1905 -0.0296 292 GLU D OE1 
14812 O OE2 . GLU D  292 ? 1.6561 1.4143 1.2727 -0.0230 -0.1864 -0.0277 292 GLU D OE2 
14813 N N   . SER D  293 ? 1.0262 0.9188 0.7629 0.0190  -0.1534 -0.0647 293 SER D N   
14814 C CA  . SER D  293 ? 0.9148 0.8358 0.6666 0.0132  -0.1425 -0.0699 293 SER D CA  
14815 C C   . SER D  293 ? 0.8492 0.7772 0.6085 -0.0004 -0.1351 -0.0714 293 SER D C   
14816 O O   . SER D  293 ? 0.7932 0.7063 0.5490 -0.0048 -0.1387 -0.0696 293 SER D O   
14817 C CB  . SER D  293 ? 1.0378 0.9833 0.8171 0.0257  -0.1363 -0.0750 293 SER D CB  
14818 O OG  . SER D  293 ? 1.0303 0.9741 0.8219 0.0334  -0.1377 -0.0775 293 SER D OG  
14819 N N   . ILE D  294 ? 1.1644 1.1162 0.9350 -0.0072 -0.1241 -0.0745 294 ILE D N   
14820 C CA  . ILE D  294 ? 1.1569 1.1254 0.9431 -0.0166 -0.1149 -0.0780 294 ILE D CA  
14821 C C   . ILE D  294 ? 1.0606 1.0568 0.8687 -0.0097 -0.1072 -0.0861 294 ILE D C   
14822 O O   . ILE D  294 ? 1.0127 1.0168 0.8198 -0.0049 -0.1057 -0.0876 294 ILE D O   
14823 C CB  . ILE D  294 ? 1.1707 1.1394 0.9459 -0.0353 -0.1084 -0.0734 294 ILE D CB  
14824 C CG1 . ILE D  294 ? 1.1599 1.1406 0.9290 -0.0382 -0.1020 -0.0736 294 ILE D CG1 
14825 C CG2 . ILE D  294 ? 1.1747 1.1125 0.9263 -0.0439 -0.1170 -0.0645 294 ILE D CG2 
14826 C CD1 . ILE D  294 ? 1.1388 1.1354 0.9085 -0.0543 -0.0906 -0.0738 294 ILE D CD1 
14827 N N   . PHE D  295 ? 0.8647 0.8740 0.6916 -0.0096 -0.1032 -0.0910 295 PHE D N   
14828 C CA  . PHE D  295 ? 0.8715 0.9023 0.7186 -0.0017 -0.0980 -0.0983 295 PHE D CA  
14829 C C   . PHE D  295 ? 0.9205 0.9481 0.7702 0.0122  -0.1032 -0.0987 295 PHE D C   
14830 O O   . PHE D  295 ? 0.9347 0.9737 0.7943 0.0161  -0.0977 -0.0995 295 PHE D O   
14831 C CB  . PHE D  295 ? 0.9043 0.9539 0.7560 -0.0073 -0.0882 -0.1018 295 PHE D CB  
14832 C CG  . PHE D  295 ? 0.8733 0.9442 0.7474 -0.0050 -0.0814 -0.1094 295 PHE D CG  
14833 C CD1 . PHE D  295 ? 0.8412 0.9144 0.7293 0.0039  -0.0849 -0.1125 295 PHE D CD1 
14834 C CD2 . PHE D  295 ? 0.8401 0.9283 0.7200 -0.0113 -0.0721 -0.1135 295 PHE D CD2 
14835 C CE1 . PHE D  295 ? 0.7704 0.8606 0.6773 0.0065  -0.0801 -0.1189 295 PHE D CE1 
14836 C CE2 . PHE D  295 ? 0.7927 0.8989 0.6926 -0.0075 -0.0672 -0.1207 295 PHE D CE2 
14837 C CZ  . PHE D  295 ? 0.7634 0.8696 0.6764 0.0014  -0.0717 -0.1230 295 PHE D CZ  
14838 N N   . ARG D  296 ? 1.2843 1.2952 1.1287 0.0178  -0.1103 -0.0948 296 ARG D N   
14839 C CA  . ARG D  296 ? 1.2969 1.3091 1.1533 0.0296  -0.1103 -0.0932 296 ARG D CA  
14840 C C   . ARG D  296 ? 1.3562 1.3602 1.2165 0.0328  -0.1141 -0.0938 296 ARG D C   
14841 O O   . ARG D  296 ? 1.4637 1.4538 1.3123 0.0267  -0.1195 -0.0935 296 ARG D O   
14842 C CB  . ARG D  296 ? 0.9122 0.9145 0.7580 0.0359  -0.1152 -0.0887 296 ARG D CB  
14843 C CG  . ARG D  296 ? 0.9086 0.9182 0.7495 0.0327  -0.1123 -0.0876 296 ARG D CG  
14844 C CD  . ARG D  296 ? 0.8942 0.9230 0.7535 0.0351  -0.1045 -0.0904 296 ARG D CD  
14845 N NE  . ARG D  296 ? 0.8902 0.9253 0.7444 0.0307  -0.1014 -0.0904 296 ARG D NE  
14846 C CZ  . ARG D  296 ? 0.9063 0.9442 0.7523 0.0217  -0.0981 -0.0927 296 ARG D CZ  
14847 N NH1 . ARG D  296 ? 0.9268 0.9637 0.7694 0.0154  -0.0974 -0.0953 296 ARG D NH1 
14848 N NH2 . ARG D  296 ? 0.9114 0.9541 0.7520 0.0185  -0.0954 -0.0928 296 ARG D NH2 
14849 N N   . PHE D  297 ? 0.9762 0.9875 0.8516 0.0414  -0.1115 -0.0948 297 PHE D N   
14850 C CA  . PHE D  297 ? 0.8991 0.9044 0.7786 0.0441  -0.1143 -0.0960 297 PHE D CA  
14851 C C   . PHE D  297 ? 0.8342 0.8366 0.7171 0.0563  -0.1160 -0.0950 297 PHE D C   
14852 O O   . PHE D  297 ? 0.8690 0.8826 0.7597 0.0616  -0.1122 -0.0946 297 PHE D O   
14853 C CB  . PHE D  297 ? 0.9869 1.0072 0.8824 0.0413  -0.1086 -0.0995 297 PHE D CB  
14854 C CG  . PHE D  297 ? 1.0090 1.0401 0.9060 0.0317  -0.1046 -0.1022 297 PHE D CG  
14855 C CD1 . PHE D  297 ? 1.0303 1.0589 0.9221 0.0221  -0.1072 -0.1045 297 PHE D CD1 
14856 C CD2 . PHE D  297 ? 0.9906 1.0351 0.8944 0.0321  -0.0984 -0.1033 297 PHE D CD2 
14857 C CE1 . PHE D  297 ? 1.0024 1.0454 0.8971 0.0136  -0.1028 -0.1086 297 PHE D CE1 
14858 C CE2 . PHE D  297 ? 0.9717 1.0273 0.8770 0.0245  -0.0943 -0.1071 297 PHE D CE2 
14859 C CZ  . PHE D  297 ? 0.9612 1.0179 0.8628 0.0156  -0.0959 -0.1102 297 PHE D CZ  
14860 N N   . SER D  298 ? 0.6536 0.6415 0.5306 0.0605  -0.1219 -0.0953 298 SER D N   
14861 C CA  . SER D  298 ? 0.5418 0.5260 0.4198 0.0733  -0.1244 -0.0956 298 SER D CA  
14862 C C   . SER D  298 ? 0.3847 0.3873 0.2792 0.0796  -0.1178 -0.0973 298 SER D C   
14863 O O   . SER D  298 ? 0.3138 0.3254 0.2122 0.0856  -0.1159 -0.0971 298 SER D O   
14864 C CB  . SER D  298 ? 0.7466 0.7110 0.6149 0.0764  -0.1317 -0.0967 298 SER D CB  
14865 O OG  . SER D  298 ? 0.8035 0.7467 0.6532 0.0718  -0.1394 -0.0944 298 SER D OG  
14866 N N   . PHE D  299 ? 0.4367 0.4446 0.3400 0.0776  -0.1151 -0.0990 299 PHE D N   
14867 C CA  . PHE D  299 ? 0.3631 0.3854 0.2792 0.0826  -0.1098 -0.1002 299 PHE D CA  
14868 C C   . PHE D  299 ? 0.3318 0.3667 0.2585 0.0755  -0.1039 -0.1003 299 PHE D C   
14869 O O   . PHE D  299 ? 0.3434 0.3768 0.2720 0.0696  -0.1042 -0.1012 299 PHE D O   
14870 C CB  . PHE D  299 ? 0.3191 0.3355 0.2350 0.0884  -0.1124 -0.1023 299 PHE D CB  
14871 C CG  . PHE D  299 ? 0.3663 0.3694 0.2715 0.0977  -0.1187 -0.1035 299 PHE D CG  
14872 C CD1 . PHE D  299 ? 0.3755 0.3864 0.2829 0.1082  -0.1178 -0.1051 299 PHE D CD1 
14873 C CD2 . PHE D  299 ? 0.4240 0.4066 0.3164 0.0960  -0.1260 -0.1036 299 PHE D CD2 
14874 C CE1 . PHE D  299 ? 0.4068 0.4060 0.3046 0.1189  -0.1242 -0.1075 299 PHE D CE1 
14875 C CE2 . PHE D  299 ? 0.4664 0.4337 0.3475 0.1061  -0.1330 -0.1052 299 PHE D CE2 
14876 C CZ  . PHE D  299 ? 0.4442 0.4202 0.3284 0.1185  -0.1321 -0.1075 299 PHE D CZ  
14877 N N   . VAL D  300 ? 0.2939 0.3412 0.2275 0.0762  -0.0992 -0.0996 300 VAL D N   
14878 C CA  . VAL D  300 ? 0.2911 0.3483 0.2334 0.0706  -0.0944 -0.1001 300 VAL D CA  
14879 C C   . VAL D  300 ? 0.2938 0.3611 0.2439 0.0743  -0.0908 -0.1000 300 VAL D C   
14880 O O   . VAL D  300 ? 0.2852 0.3540 0.2343 0.0804  -0.0915 -0.0999 300 VAL D O   
14881 C CB  . VAL D  300 ? 0.2471 0.3067 0.1863 0.0654  -0.0930 -0.0995 300 VAL D CB  
14882 C CG1 . VAL D  300 ? 0.2597 0.3100 0.1894 0.0597  -0.0964 -0.0997 300 VAL D CG1 
14883 C CG2 . VAL D  300 ? 0.2482 0.3104 0.1845 0.0694  -0.0931 -0.0978 300 VAL D CG2 
14884 N N   . PRO D  301 ? 0.3001 0.3745 0.2572 0.0706  -0.0874 -0.1006 301 PRO D N   
14885 C CA  . PRO D  301 ? 0.2761 0.3583 0.2377 0.0726  -0.0850 -0.1001 301 PRO D CA  
14886 C C   . PRO D  301 ? 0.2437 0.3311 0.2029 0.0749  -0.0845 -0.0989 301 PRO D C   
14887 O O   . PRO D  301 ? 0.2356 0.3222 0.1911 0.0734  -0.0851 -0.0982 301 PRO D O   
14888 C CB  . PRO D  301 ? 0.2139 0.2997 0.1805 0.0680  -0.0828 -0.1012 301 PRO D CB  
14889 C CG  . PRO D  301 ? 0.2155 0.2978 0.1838 0.0660  -0.0839 -0.1033 301 PRO D CG  
14890 C CD  . PRO D  301 ? 0.2237 0.2992 0.1850 0.0657  -0.0865 -0.1026 301 PRO D CD  
14891 N N   . VAL D  302 ? 0.2181 0.3118 0.1790 0.0784  -0.0838 -0.0987 302 VAL D N   
14892 C CA  . VAL D  302 ? 0.2190 0.3213 0.1792 0.0808  -0.0834 -0.0983 302 VAL D CA  
14893 C C   . VAL D  302 ? 0.2635 0.3746 0.2272 0.0757  -0.0810 -0.0975 302 VAL D C   
14894 O O   . VAL D  302 ? 0.2108 0.3217 0.1766 0.0732  -0.0801 -0.0974 302 VAL D O   
14895 C CB  . VAL D  302 ? 0.2226 0.3289 0.1816 0.0885  -0.0844 -0.0997 302 VAL D CB  
14896 C CG1 . VAL D  302 ? 0.2193 0.3292 0.1807 0.0882  -0.0829 -0.1000 302 VAL D CG1 
14897 C CG2 . VAL D  302 ? 0.2244 0.3425 0.1836 0.0919  -0.0842 -0.1003 302 VAL D CG2 
14898 N N   . VAL D  303 ? 0.2942 0.4120 0.2575 0.0739  -0.0808 -0.0969 303 VAL D N   
14899 C CA  . VAL D  303 ? 0.2590 0.3851 0.2246 0.0684  -0.0795 -0.0961 303 VAL D CA  
14900 C C   . VAL D  303 ? 0.2744 0.4134 0.2412 0.0719  -0.0792 -0.0963 303 VAL D C   
14901 O O   . VAL D  303 ? 0.2397 0.3883 0.2070 0.0749  -0.0797 -0.0968 303 VAL D O   
14902 C CB  . VAL D  303 ? 0.2738 0.4013 0.2379 0.0642  -0.0799 -0.0956 303 VAL D CB  
14903 C CG1 . VAL D  303 ? 0.3026 0.4400 0.2681 0.0586  -0.0797 -0.0949 303 VAL D CG1 
14904 C CG2 . VAL D  303 ? 0.2624 0.3793 0.2249 0.0607  -0.0796 -0.0963 303 VAL D CG2 
14905 N N   . ASP D  304 ? 0.3144 0.4543 0.2815 0.0715  -0.0785 -0.0962 304 ASP D N   
14906 C CA  . ASP D  304 ? 0.3149 0.4668 0.2822 0.0757  -0.0779 -0.0971 304 ASP D CA  
14907 C C   . ASP D  304 ? 0.2845 0.4497 0.2523 0.0694  -0.0771 -0.0958 304 ASP D C   
14908 O O   . ASP D  304 ? 0.3037 0.4823 0.2714 0.0718  -0.0762 -0.0966 304 ASP D O   
14909 C CB  . ASP D  304 ? 0.4213 0.5651 0.3868 0.0801  -0.0782 -0.0980 304 ASP D CB  
14910 C CG  . ASP D  304 ? 0.4369 0.5705 0.4017 0.0745  -0.0787 -0.0964 304 ASP D CG  
14911 O OD1 . ASP D  304 ? 0.4478 0.5791 0.4132 0.0681  -0.0790 -0.0953 304 ASP D OD1 
14912 O OD2 . ASP D  304 ? 0.4113 0.5390 0.3746 0.0771  -0.0795 -0.0969 304 ASP D OD2 
14913 N N   . GLY D  305 ? 0.2834 0.4445 0.2506 0.0610  -0.0780 -0.0940 305 GLY D N   
14914 C CA  . GLY D  305 ? 0.3137 0.4831 0.2791 0.0530  -0.0786 -0.0923 305 GLY D CA  
14915 C C   . GLY D  305 ? 0.3471 0.5091 0.3082 0.0508  -0.0798 -0.0912 305 GLY D C   
14916 O O   . GLY D  305 ? 0.3684 0.5330 0.3255 0.0430  -0.0817 -0.0893 305 GLY D O   
14917 N N   . ASP D  306 ? 0.3623 0.5143 0.3232 0.0571  -0.0796 -0.0921 306 ASP D N   
14918 C CA  . ASP D  306 ? 0.4154 0.5605 0.3719 0.0563  -0.0812 -0.0911 306 ASP D CA  
14919 C C   . ASP D  306 ? 0.3522 0.4801 0.3088 0.0549  -0.0835 -0.0913 306 ASP D C   
14920 O O   . ASP D  306 ? 0.2715 0.3941 0.2246 0.0488  -0.0863 -0.0903 306 ASP D O   
14921 C CB  . ASP D  306 ? 0.5877 0.7340 0.5441 0.0646  -0.0800 -0.0926 306 ASP D CB  
14922 C CG  . ASP D  306 ? 0.6066 0.7487 0.5572 0.0640  -0.0817 -0.0914 306 ASP D CG  
14923 O OD1 . ASP D  306 ? 0.6035 0.7343 0.5515 0.0599  -0.0846 -0.0899 306 ASP D OD1 
14924 O OD2 . ASP D  306 ? 0.6106 0.7608 0.5588 0.0684  -0.0805 -0.0924 306 ASP D OD2 
14925 N N   . PHE D  307 ? 0.4107 0.5307 0.3710 0.0605  -0.0827 -0.0930 307 PHE D N   
14926 C CA  . PHE D  307 ? 0.3911 0.4987 0.3533 0.0608  -0.0843 -0.0943 307 PHE D CA  
14927 C C   . PHE D  307 ? 0.4273 0.5329 0.3912 0.0571  -0.0841 -0.0953 307 PHE D C   
14928 O O   . PHE D  307 ? 0.4518 0.5505 0.4149 0.0544  -0.0864 -0.0963 307 PHE D O   
14929 C CB  . PHE D  307 ? 0.2134 0.3164 0.1790 0.0665  -0.0835 -0.0959 307 PHE D CB  
14930 C CG  . PHE D  307 ? 0.2133 0.3073 0.1819 0.0673  -0.0853 -0.0976 307 PHE D CG  
14931 C CD1 . PHE D  307 ? 0.2116 0.3030 0.1836 0.0657  -0.0851 -0.0997 307 PHE D CD1 
14932 C CD2 . PHE D  307 ? 0.2157 0.3052 0.1841 0.0699  -0.0875 -0.0978 307 PHE D CD2 
14933 C CE1 . PHE D  307 ? 0.2118 0.2983 0.1880 0.0673  -0.0868 -0.1024 307 PHE D CE1 
14934 C CE2 . PHE D  307 ? 0.2159 0.2997 0.1884 0.0711  -0.0896 -0.1000 307 PHE D CE2 
14935 C CZ  . PHE D  307 ? 0.2137 0.2969 0.1907 0.0701  -0.0892 -0.1026 307 PHE D CZ  
14936 N N   . LEU D  308 ? 0.4404 0.5515 0.4060 0.0577  -0.0819 -0.0955 308 LEU D N   
14937 C CA  . LEU D  308 ? 0.4318 0.5431 0.3973 0.0535  -0.0817 -0.0961 308 LEU D CA  
14938 C C   . LEU D  308 ? 0.4042 0.5260 0.3674 0.0488  -0.0820 -0.0943 308 LEU D C   
14939 O O   . LEU D  308 ? 0.3438 0.4760 0.3080 0.0513  -0.0806 -0.0936 308 LEU D O   
14940 C CB  . LEU D  308 ? 0.2886 0.3991 0.2560 0.0563  -0.0800 -0.0972 308 LEU D CB  
14941 C CG  . LEU D  308 ? 0.2648 0.3672 0.2346 0.0592  -0.0800 -0.0992 308 LEU D CG  
14942 C CD1 . LEU D  308 ? 0.2715 0.3728 0.2409 0.0602  -0.0790 -0.0999 308 LEU D CD1 
14943 C CD2 . LEU D  308 ? 0.2110 0.3077 0.1819 0.0571  -0.0813 -0.1016 308 LEU D CD2 
14944 N N   . SER D  309 ? 0.3859 0.5049 0.3456 0.0421  -0.0843 -0.0941 309 SER D N   
14945 C CA  . SER D  309 ? 0.4085 0.5377 0.3654 0.0353  -0.0856 -0.0923 309 SER D CA  
14946 C C   . SER D  309 ? 0.3954 0.5327 0.3543 0.0333  -0.0846 -0.0925 309 SER D C   
14947 O O   . SER D  309 ? 0.3760 0.5276 0.3356 0.0303  -0.0846 -0.0912 309 SER D O   
14948 C CB  . SER D  309 ? 0.4732 0.5936 0.4239 0.0278  -0.0900 -0.0922 309 SER D CB  
14949 O OG  . SER D  309 ? 0.4810 0.5915 0.4306 0.0254  -0.0912 -0.0948 309 SER D OG  
14950 N N   . ASP D  310 ? 0.3931 0.5222 0.3526 0.0347  -0.0840 -0.0943 310 ASP D N   
14951 C CA  . ASP D  310 ? 0.4330 0.5674 0.3934 0.0341  -0.0833 -0.0945 310 ASP D CA  
14952 C C   . ASP D  310 ? 0.3972 0.5232 0.3584 0.0397  -0.0816 -0.0961 310 ASP D C   
14953 O O   . ASP D  310 ? 0.4057 0.5250 0.3683 0.0439  -0.0808 -0.0969 310 ASP D O   
14954 C CB  . ASP D  310 ? 0.6995 0.8309 0.6557 0.0256  -0.0858 -0.0953 310 ASP D CB  
14955 C CG  . ASP D  310 ? 0.7755 0.9178 0.7324 0.0230  -0.0864 -0.0945 310 ASP D CG  
14956 O OD1 . ASP D  310 ? 0.8048 0.9499 0.7636 0.0285  -0.0849 -0.0945 310 ASP D OD1 
14957 O OD2 . ASP D  310 ? 0.7859 0.9336 0.7409 0.0150  -0.0890 -0.0939 310 ASP D OD2 
14958 N N   . THR D  311 ? 0.3715 0.4981 0.3313 0.0393  -0.0814 -0.0965 311 THR D N   
14959 C CA  . THR D  311 ? 0.3407 0.4598 0.2996 0.0427  -0.0802 -0.0978 311 THR D CA  
14960 C C   . THR D  311 ? 0.3053 0.4149 0.2632 0.0406  -0.0798 -0.1007 311 THR D C   
14961 O O   . THR D  311 ? 0.2958 0.4031 0.2519 0.0360  -0.0813 -0.1018 311 THR D O   
14962 C CB  . THR D  311 ? 0.4298 0.5503 0.3849 0.0410  -0.0809 -0.0977 311 THR D CB  
14963 O OG1 . THR D  311 ? 0.4683 0.5822 0.4197 0.0361  -0.0808 -0.1002 311 THR D OG1 
14964 C CG2 . THR D  311 ? 0.4275 0.5595 0.3833 0.0392  -0.0827 -0.0959 311 THR D CG2 
14965 N N   . PRO D  312 ? 0.3066 0.4111 0.2657 0.0440  -0.0784 -0.1025 312 PRO D N   
14966 C CA  . PRO D  312 ? 0.2966 0.3947 0.2560 0.0433  -0.0779 -0.1065 312 PRO D CA  
14967 C C   . PRO D  312 ? 0.3229 0.4185 0.2772 0.0388  -0.0779 -0.1091 312 PRO D C   
14968 O O   . PRO D  312 ? 0.3150 0.4051 0.2686 0.0376  -0.0788 -0.1126 312 PRO D O   
14969 C CB  . PRO D  312 ? 0.3252 0.4222 0.2867 0.0469  -0.0763 -0.1079 312 PRO D CB  
14970 C CG  . PRO D  312 ? 0.3625 0.4621 0.3215 0.0481  -0.0765 -0.1045 312 PRO D CG  
14971 C CD  . PRO D  312 ? 0.3638 0.4683 0.3235 0.0485  -0.0777 -0.1014 312 PRO D CD  
14972 N N   . GLU D  313 ? 0.4624 0.5607 0.4122 0.0367  -0.0775 -0.1078 313 GLU D N   
14973 C CA  . GLU D  313 ? 0.4661 0.5615 0.4097 0.0322  -0.0777 -0.1104 313 GLU D CA  
14974 C C   . GLU D  313 ? 0.4256 0.5194 0.3675 0.0275  -0.0804 -0.1106 313 GLU D C   
14975 O O   . GLU D  313 ? 0.4917 0.5786 0.4293 0.0246  -0.0811 -0.1145 313 GLU D O   
14976 C CB  . GLU D  313 ? 0.4090 0.5072 0.3469 0.0306  -0.0777 -0.1085 313 GLU D CB  
14977 C CG  . GLU D  313 ? 1.3568 1.4595 1.2964 0.0345  -0.0784 -0.1042 313 GLU D CG  
14978 C CD  . GLU D  313 ? 1.3229 1.4224 1.2618 0.0376  -0.0768 -0.1048 313 GLU D CD  
14979 O OE1 . GLU D  313 ? 1.3274 1.4239 1.2631 0.0358  -0.0747 -0.1082 313 GLU D OE1 
14980 O OE2 . GLU D  313 ? 1.2782 1.3787 1.2194 0.0415  -0.0778 -0.1022 313 GLU D OE2 
14981 N N   . ALA D  314 ? 0.2447 0.3446 0.1893 0.0266  -0.0822 -0.1067 314 ALA D N   
14982 C CA  . ALA D  314 ? 0.2505 0.3498 0.1932 0.0208  -0.0853 -0.1064 314 ALA D CA  
14983 C C   . ALA D  314 ? 0.3029 0.3919 0.2451 0.0210  -0.0867 -0.1094 314 ALA D C   
14984 O O   . ALA D  314 ? 0.3451 0.4253 0.2816 0.0164  -0.0894 -0.1124 314 ALA D O   
14985 C CB  . ALA D  314 ? 0.2451 0.3559 0.1917 0.0205  -0.0862 -0.1020 314 ALA D CB  
14986 N N   . LEU D  315 ? 0.3796 0.4686 0.3268 0.0266  -0.0856 -0.1088 315 LEU D N   
14987 C CA  . LEU D  315 ? 0.3750 0.4547 0.3219 0.0278  -0.0880 -0.1112 315 LEU D CA  
14988 C C   . LEU D  315 ? 0.3827 0.4524 0.3280 0.0302  -0.0879 -0.1174 315 LEU D C   
14989 O O   . LEU D  315 ? 0.4341 0.4929 0.3758 0.0296  -0.0916 -0.1206 315 LEU D O   
14990 C CB  . LEU D  315 ? 0.2436 0.3260 0.1964 0.0339  -0.0871 -0.1095 315 LEU D CB  
14991 C CG  . LEU D  315 ? 0.2365 0.3299 0.1911 0.0334  -0.0860 -0.1044 315 LEU D CG  
14992 C CD1 . LEU D  315 ? 0.5557 0.6501 0.5149 0.0395  -0.0850 -0.1033 315 LEU D CD1 
14993 C CD2 . LEU D  315 ? 0.3067 0.4030 0.2569 0.0263  -0.0892 -0.1020 315 LEU D CD2 
14994 N N   . ILE D  316 ? 0.2750 0.3482 0.2221 0.0330  -0.0842 -0.1196 316 ILE D N   
14995 C CA  . ILE D  316 ? 0.3396 0.4058 0.2849 0.0352  -0.0835 -0.1263 316 ILE D CA  
14996 C C   . ILE D  316 ? 0.4574 0.5174 0.3938 0.0290  -0.0850 -0.1283 316 ILE D C   
14997 O O   . ILE D  316 ? 0.5095 0.5593 0.4420 0.0301  -0.0862 -0.1342 316 ILE D O   
14998 C CB  . ILE D  316 ? 0.3632 0.4359 0.3124 0.0394  -0.0789 -0.1288 316 ILE D CB  
14999 C CG1 . ILE D  316 ? 0.3593 0.4389 0.3052 0.0359  -0.0766 -0.1247 316 ILE D CG1 
15000 C CG2 . ILE D  316 ? 0.3539 0.4307 0.3118 0.0453  -0.0783 -0.1288 316 ILE D CG2 
15001 C CD1 . ILE D  316 ? 0.3661 0.4501 0.3118 0.0376  -0.0727 -0.1274 316 ILE D CD1 
15002 N N   . ASN D  317 ? 0.5436 0.6093 0.4765 0.0231  -0.0854 -0.1237 317 ASN D N   
15003 C CA  . ASN D  317 ? 0.5944 0.6548 0.5185 0.0159  -0.0878 -0.1251 317 ASN D CA  
15004 C C   . ASN D  317 ? 0.5807 0.6297 0.4996 0.0111  -0.0931 -0.1266 317 ASN D C   
15005 O O   . ASN D  317 ? 0.5633 0.6015 0.4741 0.0071  -0.0954 -0.1308 317 ASN D O   
15006 C CB  . ASN D  317 ? 0.8622 0.9331 0.7853 0.0108  -0.0883 -0.1197 317 ASN D CB  
15007 C CG  . ASN D  317 ? 0.9511 1.0246 0.8702 0.0109  -0.0859 -0.1206 317 ASN D CG  
15008 O OD1 . ASN D  317 ? 0.9549 1.0241 0.8721 0.0143  -0.0829 -0.1251 317 ASN D OD1 
15009 N ND2 . ASN D  317 ? 0.9992 1.0806 0.9167 0.0071  -0.0875 -0.1165 317 ASN D ND2 
15010 N N   . THR D  318 ? 0.5953 0.6456 0.5176 0.0110  -0.0955 -0.1232 318 THR D N   
15011 C CA  . THR D  318 ? 0.6438 0.6831 0.5591 0.0043  -0.1016 -0.1235 318 THR D CA  
15012 C C   . THR D  318 ? 0.6844 0.7097 0.5991 0.0091  -0.1051 -0.1263 318 THR D C   
15013 O O   . THR D  318 ? 0.7342 0.7423 0.6421 0.0092  -0.1087 -0.1316 318 THR D O   
15014 C CB  . THR D  318 ? 0.7659 0.8167 0.6811 -0.0041 -0.1039 -0.1170 318 THR D CB  
15015 O OG1 . THR D  318 ? 0.7950 0.8614 0.7193 0.0013  -0.0997 -0.1125 318 THR D OG1 
15016 C CG2 . THR D  318 ? 0.7648 0.8198 0.6751 -0.0126 -0.1053 -0.1164 318 THR D CG2 
15017 N N   . GLY D  319 ? 0.7486 0.7798 0.6697 0.0138  -0.1046 -0.1230 319 GLY D N   
15018 C CA  . GLY D  319 ? 0.8127 0.8304 0.7311 0.0164  -0.1100 -0.1239 319 GLY D CA  
15019 C C   . GLY D  319 ? 0.8628 0.8627 0.7794 0.0242  -0.1127 -0.1312 319 GLY D C   
15020 O O   . GLY D  319 ? 0.8463 0.8489 0.7673 0.0301  -0.1083 -0.1362 319 GLY D O   
15021 N N   . ASP D  320 ? 0.9355 0.9170 0.8451 0.0242  -0.1202 -0.1319 320 ASP D N   
15022 C CA  . ASP D  320 ? 0.9500 0.9105 0.8558 0.0318  -0.1247 -0.1390 320 ASP D CA  
15023 C C   . ASP D  320 ? 0.9210 0.8851 0.8375 0.0457  -0.1233 -0.1430 320 ASP D C   
15024 O O   . ASP D  320 ? 0.9159 0.8811 0.8357 0.0494  -0.1261 -0.1400 320 ASP D O   
15025 C CB  . ASP D  320 ? 1.0106 0.9458 0.9028 0.0265  -0.1349 -0.1375 320 ASP D CB  
15026 C CG  . ASP D  320 ? 1.0671 0.9769 0.9533 0.0343  -0.1403 -0.1449 320 ASP D CG  
15027 O OD1 . ASP D  320 ? 1.0881 1.0008 0.9776 0.0389  -0.1356 -0.1514 320 ASP D OD1 
15028 O OD2 . ASP D  320 ? 1.0911 0.9778 0.9686 0.0361  -0.1494 -0.1441 320 ASP D OD2 
15029 N N   . PHE D  321 ? 0.8210 0.7884 0.7428 0.0527  -0.1190 -0.1500 321 PHE D N   
15030 C CA  . PHE D  321 ? 0.7908 0.7654 0.7242 0.0653  -0.1173 -0.1551 321 PHE D CA  
15031 C C   . PHE D  321 ? 0.8568 0.8132 0.7882 0.0754  -0.1234 -0.1628 321 PHE D C   
15032 O O   . PHE D  321 ? 0.8512 0.8164 0.7934 0.0862  -0.1215 -0.1688 321 PHE D O   
15033 C CB  . PHE D  321 ? 0.7177 0.7145 0.6607 0.0665  -0.1078 -0.1566 321 PHE D CB  
15034 C CG  . PHE D  321 ? 0.6470 0.6595 0.5928 0.0594  -0.1033 -0.1486 321 PHE D CG  
15035 C CD1 . PHE D  321 ? 0.6089 0.6244 0.5573 0.0590  -0.1058 -0.1428 321 PHE D CD1 
15036 C CD2 . PHE D  321 ? 0.6063 0.6292 0.5508 0.0534  -0.0974 -0.1468 321 PHE D CD2 
15037 C CE1 . PHE D  321 ? 0.5660 0.5950 0.5166 0.0537  -0.1017 -0.1359 321 PHE D CE1 
15038 C CE2 . PHE D  321 ? 0.5446 0.5801 0.4913 0.0483  -0.0942 -0.1396 321 PHE D CE2 
15039 C CZ  . PHE D  321 ? 0.5309 0.5695 0.4810 0.0488  -0.0961 -0.1344 321 PHE D CZ  
15040 N N   . GLN D  322 ? 0.9684 0.8999 0.8860 0.0716  -0.1308 -0.1626 322 GLN D N   
15041 C CA  . GLN D  322 ? 1.0273 0.9360 0.9403 0.0813  -0.1384 -0.1689 322 GLN D CA  
15042 C C   . GLN D  322 ? 1.0229 0.9350 0.9456 0.0932  -0.1423 -0.1702 322 GLN D C   
15043 O O   . GLN D  322 ? 1.0140 0.9308 0.9378 0.0901  -0.1444 -0.1638 322 GLN D O   
15044 C CB  . GLN D  322 ? 1.1774 1.0557 1.0721 0.0731  -0.1481 -0.1652 322 GLN D CB  
15045 C CG  . GLN D  322 ? 1.2510 1.1188 1.1346 0.0638  -0.1470 -0.1668 322 GLN D CG  
15046 C CD  . GLN D  322 ? 1.3417 1.1996 1.2247 0.0741  -0.1466 -0.1765 322 GLN D CD  
15047 O OE1 . GLN D  322 ? 1.3869 1.2412 1.2762 0.0884  -0.1493 -0.1819 322 GLN D OE1 
15048 N NE2 . GLN D  322 ? 1.3573 1.2122 1.2329 0.0671  -0.1434 -0.1791 322 GLN D NE2 
15049 N N   . ASP D  323 ? 1.1741 1.0858 1.1041 0.1067  -0.1432 -0.1787 323 ASP D N   
15050 C CA  . ASP D  323 ? 1.1812 1.1026 1.1242 0.1191  -0.1460 -0.1816 323 ASP D CA  
15051 C C   . ASP D  323 ? 1.1035 1.0510 1.0580 0.1157  -0.1403 -0.1770 323 ASP D C   
15052 O O   . ASP D  323 ? 1.0854 1.0299 1.0383 0.1143  -0.1453 -0.1714 323 ASP D O   
15053 C CB  . ASP D  323 ? 1.9994 1.8935 1.9344 0.1269  -0.1593 -0.1813 323 ASP D CB  
15054 C CG  . ASP D  323 ? 2.0074 1.8793 1.9251 0.1153  -0.1666 -0.1719 323 ASP D CG  
15055 O OD1 . ASP D  323 ? 1.9923 1.8734 1.9120 0.1114  -0.1672 -0.1658 323 ASP D OD1 
15056 O OD2 . ASP D  323 ? 2.0252 1.8708 1.9268 0.1095  -0.1719 -0.1705 323 ASP D OD2 
15057 N N   . LEU D  324 ? 0.8637 0.8351 0.8277 0.1134  -0.1298 -0.1790 324 LEU D N   
15058 C CA  . LEU D  324 ? 0.6992 0.6959 0.6763 0.1132  -0.1241 -0.1773 324 LEU D CA  
15059 C C   . LEU D  324 ? 0.6266 0.6425 0.6163 0.1200  -0.1176 -0.1860 324 LEU D C   
15060 O O   . LEU D  324 ? 0.6583 0.6753 0.6445 0.1176  -0.1122 -0.1893 324 LEU D O   
15061 C CB  . LEU D  324 ? 0.4612 0.4675 0.4347 0.1004  -0.1174 -0.1693 324 LEU D CB  
15062 C CG  . LEU D  324 ? 0.3929 0.4240 0.3789 0.0999  -0.1108 -0.1680 324 LEU D CG  
15063 C CD1 . LEU D  324 ? 0.3949 0.4294 0.3887 0.1064  -0.1163 -0.1675 324 LEU D CD1 
15064 C CD2 . LEU D  324 ? 0.3324 0.3707 0.3142 0.0887  -0.1050 -0.1596 324 LEU D CD2 
15065 N N   . GLN D  325 ? 0.4126 0.4444 0.4164 0.1279  -0.1182 -0.1899 325 GLN D N   
15066 C CA  . GLN D  325 ? 0.4214 0.4753 0.4379 0.1328  -0.1114 -0.1981 325 GLN D CA  
15067 C C   . GLN D  325 ? 0.3684 0.4461 0.3929 0.1258  -0.1035 -0.1958 325 GLN D C   
15068 O O   . GLN D  325 ? 0.3901 0.4741 0.4199 0.1251  -0.1059 -0.1922 325 GLN D O   
15069 C CB  . GLN D  325 ? 0.7597 0.8174 0.7875 0.1464  -0.1173 -0.2056 325 GLN D CB  
15070 C CG  . GLN D  325 ? 0.8650 0.8981 0.8840 0.1541  -0.1250 -0.2086 325 GLN D CG  
15071 C CD  . GLN D  325 ? 0.9390 0.9692 0.9658 0.1670  -0.1346 -0.2124 325 GLN D CD  
15072 O OE1 . GLN D  325 ? 0.9331 0.9599 0.9613 0.1681  -0.1411 -0.2081 325 GLN D OE1 
15073 N NE2 . GLN D  325 ? 0.9914 1.0228 1.0226 0.1770  -0.1358 -0.2204 325 GLN D NE2 
15074 N N   . VAL D  326 ? 0.4912 0.5802 0.5148 0.1205  -0.0946 -0.1976 326 VAL D N   
15075 C CA  . VAL D  326 ? 0.4799 0.5871 0.5071 0.1123  -0.0874 -0.1945 326 VAL D CA  
15076 C C   . VAL D  326 ? 0.4981 0.6270 0.5335 0.1133  -0.0793 -0.2026 326 VAL D C   
15077 O O   . VAL D  326 ? 0.5365 0.6637 0.5679 0.1149  -0.0759 -0.2074 326 VAL D O   
15078 C CB  . VAL D  326 ? 0.2903 0.3883 0.3041 0.1011  -0.0843 -0.1858 326 VAL D CB  
15079 C CG1 . VAL D  326 ? 0.2668 0.3810 0.2826 0.0936  -0.0776 -0.1826 326 VAL D CG1 
15080 C CG2 . VAL D  326 ? 0.2801 0.3613 0.2867 0.0986  -0.0908 -0.1775 326 VAL D CG2 
15081 N N   . LEU D  327 ? 0.2719 0.4213 0.3179 0.1119  -0.0763 -0.2043 327 LEU D N   
15082 C CA  . LEU D  327 ? 0.2707 0.4432 0.3231 0.1097  -0.0673 -0.2111 327 LEU D CA  
15083 C C   . LEU D  327 ? 0.2599 0.4387 0.3058 0.0974  -0.0618 -0.2050 327 LEU D C   
15084 O O   . LEU D  327 ? 0.2497 0.4313 0.2985 0.0943  -0.0644 -0.2010 327 LEU D O   
15085 C CB  . LEU D  327 ? 0.2692 0.4629 0.3402 0.1178  -0.0679 -0.2197 327 LEU D CB  
15086 C CG  . LEU D  327 ? 0.2656 0.4893 0.3464 0.1140  -0.0582 -0.2265 327 LEU D CG  
15087 C CD1 . LEU D  327 ? 0.2784 0.5080 0.3562 0.1152  -0.0511 -0.2323 327 LEU D CD1 
15088 C CD2 . LEU D  327 ? 0.2613 0.5056 0.3620 0.1207  -0.0604 -0.2325 327 LEU D CD2 
15089 N N   . VAL D  328 ? 0.2646 0.4436 0.3002 0.0907  -0.0551 -0.2041 328 VAL D N   
15090 C CA  . VAL D  328 ? 0.2585 0.4407 0.2854 0.0794  -0.0508 -0.1979 328 VAL D CA  
15091 C C   . VAL D  328 ? 0.2626 0.4660 0.2905 0.0748  -0.0414 -0.2045 328 VAL D C   
15092 O O   . VAL D  328 ? 0.2714 0.4853 0.3046 0.0800  -0.0371 -0.2130 328 VAL D O   
15093 C CB  . VAL D  328 ? 0.2622 0.4256 0.2733 0.0739  -0.0513 -0.1899 328 VAL D CB  
15094 C CG1 . VAL D  328 ? 0.4424 0.5877 0.4516 0.0764  -0.0591 -0.1830 328 VAL D CG1 
15095 C CG2 . VAL D  328 ? 0.2758 0.4362 0.2814 0.0762  -0.0479 -0.1953 328 VAL D CG2 
15096 N N   . GLY D  329 ? 0.2584 0.4682 0.2804 0.0647  -0.0383 -0.2004 329 GLY D N   
15097 C CA  . GLY D  329 ? 0.2651 0.4943 0.2845 0.0581  -0.0288 -0.2059 329 GLY D CA  
15098 C C   . GLY D  329 ? 0.3169 0.5501 0.3274 0.0452  -0.0264 -0.1996 329 GLY D C   
15099 O O   . GLY D  329 ? 0.3729 0.5949 0.3821 0.0423  -0.0327 -0.1912 329 GLY D O   
15100 N N   . VAL D  330 ? 0.2883 0.5353 0.2930 0.0369  -0.0175 -0.2013 330 VAL D N   
15101 C CA  . VAL D  330 ? 0.2857 0.5314 0.2796 0.0229  -0.0157 -0.1918 330 VAL D CA  
15102 C C   . VAL D  330 ? 0.2940 0.5654 0.2950 0.0140  -0.0063 -0.1942 330 VAL D C   
15103 O O   . VAL D  330 ? 0.3135 0.6049 0.3237 0.0185  0.0008  -0.2043 330 VAL D O   
15104 C CB  . VAL D  330 ? 0.2861 0.5165 0.2570 0.0177  -0.0153 -0.1875 330 VAL D CB  
15105 C CG1 . VAL D  330 ? 0.2796 0.4856 0.2445 0.0231  -0.0249 -0.1812 330 VAL D CG1 
15106 C CG2 . VAL D  330 ? 0.2967 0.5355 0.2629 0.0208  -0.0080 -0.1965 330 VAL D CG2 
15107 N N   . VAL D  331 ? 0.2947 0.5659 0.2915 0.0013  -0.0064 -0.1854 331 VAL D N   
15108 C CA  . VAL D  331 ? 0.3571 0.6525 0.3581 -0.0106 0.0030  -0.1864 331 VAL D CA  
15109 C C   . VAL D  331 ? 0.4680 0.7639 0.4484 -0.0193 0.0108  -0.1856 331 VAL D C   
15110 O O   . VAL D  331 ? 0.5267 0.8031 0.4907 -0.0160 0.0077  -0.1837 331 VAL D O   
15111 C CB  . VAL D  331 ? 0.3807 0.6731 0.3820 -0.0231 -0.0005 -0.1767 331 VAL D CB  
15112 C CG1 . VAL D  331 ? 0.3834 0.6732 0.4022 -0.0152 -0.0091 -0.1769 331 VAL D CG1 
15113 C CG2 . VAL D  331 ? 0.3846 0.6497 0.3613 -0.0317 -0.0053 -0.1652 331 VAL D CG2 
15114 N N   . LYS D  332 ? 0.6124 0.9308 0.5930 -0.0312 0.0208  -0.1866 332 LYS D N   
15115 C CA  . LYS D  332 ? 0.6280 0.9488 0.5884 -0.0390 0.0290  -0.1868 332 LYS D CA  
15116 C C   . LYS D  332 ? 0.6677 0.9592 0.6017 -0.0478 0.0230  -0.1743 332 LYS D C   
15117 O O   . LYS D  332 ? 0.6950 0.9712 0.6133 -0.0432 0.0210  -0.1746 332 LYS D O   
15118 C CB  . LYS D  332 ? 0.4660 0.8190 0.4307 -0.0513 0.0419  -0.1901 332 LYS D CB  
15119 C CG  . LYS D  332 ? 0.4326 0.7980 0.3849 -0.0507 0.0524  -0.1982 332 LYS D CG  
15120 C CD  . LYS D  332 ? 0.4396 0.8362 0.3907 -0.0659 0.0663  -0.1997 332 LYS D CD  
15121 C CE  . LYS D  332 ? 0.4632 0.8446 0.3856 -0.0859 0.0674  -0.1861 332 LYS D CE  
15122 N NZ  . LYS D  332 ? 0.4468 0.8384 0.3731 -0.1044 0.0692  -0.1771 332 LYS D NZ  
15123 N N   . ASP D  333 ? 0.6086 0.8912 0.5374 -0.0600 0.0192  -0.1636 333 ASP D N   
15124 C CA  . ASP D  333 ? 0.6337 0.8861 0.5380 -0.0663 0.0117  -0.1518 333 ASP D CA  
15125 C C   . ASP D  333 ? 0.5673 0.7993 0.4764 -0.0628 -0.0002 -0.1450 333 ASP D C   
15126 O O   . ASP D  333 ? 0.5328 0.7657 0.4460 -0.0722 -0.0018 -0.1398 333 ASP D O   
15127 C CB  . ASP D  333 ? 0.7585 1.0129 0.6441 -0.0858 0.0175  -0.1440 333 ASP D CB  
15128 C CG  . ASP D  333 ? 0.8209 1.1109 0.7201 -0.0946 0.0303  -0.1503 333 ASP D CG  
15129 O OD1 . ASP D  333 ? 0.7961 1.1063 0.7216 -0.0878 0.0318  -0.1579 333 ASP D OD1 
15130 O OD2 . ASP D  333 ? 0.8858 1.1846 0.7692 -0.1084 0.0389  -0.1478 333 ASP D OD2 
15131 N N   . GLU D  334 ? 0.5722 0.7852 0.4787 -0.0505 -0.0087 -0.1447 334 GLU D N   
15132 C CA  . GLU D  334 ? 0.5513 0.7478 0.4640 -0.0447 -0.0193 -0.1401 334 GLU D CA  
15133 C C   . GLU D  334 ? 0.5800 0.7523 0.4727 -0.0535 -0.0263 -0.1285 334 GLU D C   
15134 O O   . GLU D  334 ? 0.6029 0.7635 0.4991 -0.0531 -0.0337 -0.1241 334 GLU D O   
15135 C CB  . GLU D  334 ? 0.5223 0.7091 0.4392 -0.0292 -0.0253 -0.1439 334 GLU D CB  
15136 C CG  . GLU D  334 ? 0.5291 0.7340 0.4644 -0.0189 -0.0207 -0.1552 334 GLU D CG  
15137 C CD  . GLU D  334 ? 0.5170 0.7242 0.4723 -0.0103 -0.0260 -0.1577 334 GLU D CD  
15138 O OE1 . GLU D  334 ? 0.5234 0.7169 0.4773 -0.0113 -0.0335 -0.1509 334 GLU D OE1 
15139 O OE2 . GLU D  334 ? 0.4890 0.7109 0.4604 -0.0019 -0.0231 -0.1666 334 GLU D OE2 
15140 N N   . GLY D  335 ? 0.5251 0.6888 0.3957 -0.0609 -0.0245 -0.1237 335 GLY D N   
15141 C CA  . GLY D  335 ? 0.5702 0.7070 0.4191 -0.0664 -0.0330 -0.1128 335 GLY D CA  
15142 C C   . GLY D  335 ? 0.6260 0.7564 0.4655 -0.0825 -0.0331 -0.1048 335 GLY D C   
15143 O O   . GLY D  335 ? 0.6715 0.7763 0.4964 -0.0849 -0.0425 -0.0963 335 GLY D O   
15144 N N   . SER D  336 ? 0.6611 0.8148 0.5087 -0.0938 -0.0229 -0.1077 336 SER D N   
15145 C CA  . SER D  336 ? 0.6706 0.8199 0.5074 -0.1124 -0.0220 -0.0996 336 SER D CA  
15146 C C   . SER D  336 ? 0.6800 0.8131 0.5220 -0.1128 -0.0318 -0.0951 336 SER D C   
15147 O O   . SER D  336 ? 0.7093 0.8167 0.5314 -0.1222 -0.0389 -0.0853 336 SER D O   
15148 C CB  . SER D  336 ? 0.7105 0.8941 0.5600 -0.1236 -0.0086 -0.1050 336 SER D CB  
15149 O OG  . SER D  336 ? 0.7116 0.9197 0.5904 -0.1116 -0.0051 -0.1161 336 SER D OG  
15150 N N   . TYR D  337 ? 0.7154 0.8615 0.5826 -0.1024 -0.0329 -0.1024 337 TYR D N   
15151 C CA  . TYR D  337 ? 0.7187 0.8533 0.5931 -0.1027 -0.0415 -0.0998 337 TYR D CA  
15152 C C   . TYR D  337 ? 0.7062 0.8035 0.5601 -0.0989 -0.0541 -0.0918 337 TYR D C   
15153 O O   . TYR D  337 ? 0.7430 0.8225 0.5884 -0.1076 -0.0607 -0.0856 337 TYR D O   
15154 C CB  . TYR D  337 ? 0.7532 0.9044 0.6551 -0.0884 -0.0422 -0.1090 337 TYR D CB  
15155 C CG  . TYR D  337 ? 0.7856 0.9251 0.6943 -0.0877 -0.0514 -0.1071 337 TYR D CG  
15156 C CD1 . TYR D  337 ? 0.8237 0.9361 0.7235 -0.0772 -0.0624 -0.1041 337 TYR D CD1 
15157 C CD2 . TYR D  337 ? 0.8150 0.9720 0.7391 -0.0974 -0.0493 -0.1089 337 TYR D CD2 
15158 C CE1 . TYR D  337 ? 0.8762 0.9771 0.7803 -0.0761 -0.0708 -0.1030 337 TYR D CE1 
15159 C CE2 . TYR D  337 ? 0.8818 1.0271 0.8107 -0.0971 -0.0583 -0.1075 337 TYR D CE2 
15160 C CZ  . TYR D  337 ? 0.9249 1.0410 0.8428 -0.0863 -0.0691 -0.1047 337 TYR D CZ  
15161 O OH  . TYR D  337 ? 0.9726 1.0761 0.8936 -0.0854 -0.0782 -0.1040 337 TYR D OH  
15162 N N   . PHE D  338 ? 0.6349 0.7208 0.4809 -0.0858 -0.0578 -0.0922 338 PHE D N   
15163 C CA  . PHE D  338 ? 0.6009 0.6553 0.4307 -0.0785 -0.0699 -0.0864 338 PHE D CA  
15164 C C   . PHE D  338 ? 0.6067 0.6367 0.4074 -0.0895 -0.0740 -0.0764 338 PHE D C   
15165 O O   . PHE D  338 ? 0.6645 0.6661 0.4509 -0.0876 -0.0848 -0.0705 338 PHE D O   
15166 C CB  . PHE D  338 ? 0.6047 0.6591 0.4390 -0.0604 -0.0727 -0.0909 338 PHE D CB  
15167 C CG  . PHE D  338 ? 0.6378 0.7131 0.4978 -0.0500 -0.0693 -0.0998 338 PHE D CG  
15168 C CD1 . PHE D  338 ? 0.6731 0.7435 0.5442 -0.0429 -0.0756 -0.1014 338 PHE D CD1 
15169 C CD2 . PHE D  338 ? 0.6704 0.7693 0.5422 -0.0477 -0.0601 -0.1068 338 PHE D CD2 
15170 C CE1 . PHE D  338 ? 0.6935 0.7817 0.5867 -0.0339 -0.0732 -0.1089 338 PHE D CE1 
15171 C CE2 . PHE D  338 ? 0.6892 0.8047 0.5832 -0.0381 -0.0580 -0.1148 338 PHE D CE2 
15172 C CZ  . PHE D  338 ? 0.7033 0.8134 0.6079 -0.0315 -0.0647 -0.1154 338 PHE D CZ  
15173 N N   . LEU D  339 ? 0.5509 0.5907 0.3414 -0.1006 -0.0656 -0.0745 339 LEU D N   
15174 C CA  . LEU D  339 ? 0.5902 0.6058 0.3504 -0.1103 -0.0699 -0.0645 339 LEU D CA  
15175 C C   . LEU D  339 ? 0.6552 0.6440 0.3999 -0.1225 -0.0781 -0.0555 339 LEU D C   
15176 O O   . LEU D  339 ? 0.6861 0.6431 0.4061 -0.1223 -0.0882 -0.0475 339 LEU D O   
15177 C CB  . LEU D  339 ? 0.6285 0.6619 0.3804 -0.1224 -0.0583 -0.0643 339 LEU D CB  
15178 C CG  . LEU D  339 ? 0.5943 0.6441 0.3529 -0.1098 -0.0532 -0.0719 339 LEU D CG  
15179 C CD1 . LEU D  339 ? 0.6223 0.6910 0.3728 -0.1217 -0.0411 -0.0729 339 LEU D CD1 
15180 C CD2 . LEU D  339 ? 0.5665 0.5924 0.3094 -0.0977 -0.0640 -0.0682 339 LEU D CD2 
15181 N N   . VAL D  340 ? 0.6595 0.6599 0.4186 -0.1321 -0.0749 -0.0572 340 VAL D N   
15182 C CA  . VAL D  340 ? 0.6966 0.6713 0.4419 -0.1450 -0.0830 -0.0493 340 VAL D CA  
15183 C C   . VAL D  340 ? 0.7257 0.6698 0.4660 -0.1308 -0.0977 -0.0483 340 VAL D C   
15184 O O   . VAL D  340 ? 0.7411 0.6558 0.4647 -0.1388 -0.1070 -0.0416 340 VAL D O   
15185 C CB  . VAL D  340 ? 0.6210 0.6187 0.3854 -0.1589 -0.0764 -0.0521 340 VAL D CB  
15186 C CG1 . VAL D  340 ? 0.6809 0.6980 0.4393 -0.1799 -0.0646 -0.0488 340 VAL D CG1 
15187 C CG2 . VAL D  340 ? 0.5379 0.5664 0.3353 -0.1448 -0.0713 -0.0639 340 VAL D CG2 
15188 N N   . TYR D  341 ? 0.7673 0.7180 0.5209 -0.1100 -0.0996 -0.0553 341 TYR D N   
15189 C CA  . TYR D  341 ? 0.7833 0.7138 0.5378 -0.0937 -0.1113 -0.0571 341 TYR D CA  
15190 C C   . TYR D  341 ? 0.8661 0.7657 0.5964 -0.0842 -0.1221 -0.0515 341 TYR D C   
15191 O O   . TYR D  341 ? 0.8867 0.7760 0.6195 -0.0669 -0.1302 -0.0546 341 TYR D O   
15192 C CB  . TYR D  341 ? 0.6871 0.6418 0.4699 -0.0780 -0.1080 -0.0673 341 TYR D CB  
15193 C CG  . TYR D  341 ? 0.7061 0.6771 0.5085 -0.0852 -0.1045 -0.0714 341 TYR D CG  
15194 C CD1 . TYR D  341 ? 0.7656 0.7653 0.5812 -0.0978 -0.0931 -0.0737 341 TYR D CD1 
15195 C CD2 . TYR D  341 ? 0.7082 0.6665 0.5152 -0.0795 -0.1130 -0.0732 341 TYR D CD2 
15196 C CE1 . TYR D  341 ? 0.7782 0.7952 0.6128 -0.1044 -0.0904 -0.0776 341 TYR D CE1 
15197 C CE2 . TYR D  341 ? 0.7184 0.6918 0.5428 -0.0867 -0.1107 -0.0769 341 TYR D CE2 
15198 C CZ  . TYR D  341 ? 0.7644 0.7679 0.6033 -0.0992 -0.0995 -0.0789 341 TYR D CZ  
15199 O OH  . TYR D  341 ? 0.7795 0.8014 0.6374 -0.1061 -0.0974 -0.0829 341 TYR D OH  
15200 N N   . GLY D  342 ? 0.9744 0.8603 0.6812 -0.0955 -0.1224 -0.0435 342 GLY D N   
15201 C CA  . GLY D  342 ? 1.0420 0.8990 0.7248 -0.0868 -0.1333 -0.0378 342 GLY D CA  
15202 C C   . GLY D  342 ? 1.0870 0.9503 0.7594 -0.0845 -0.1302 -0.0359 342 GLY D C   
15203 O O   . GLY D  342 ? 1.1388 0.9826 0.7963 -0.0729 -0.1401 -0.0330 342 GLY D O   
15204 N N   . VAL D  343 ? 1.1795 1.0703 0.8594 -0.0948 -0.1170 -0.0379 343 VAL D N   
15205 C CA  . VAL D  343 ? 1.1338 1.0215 0.7928 -0.1010 -0.1149 -0.0325 343 VAL D CA  
15206 C C   . VAL D  343 ? 1.1501 1.0175 0.7835 -0.1228 -0.1158 -0.0218 343 VAL D C   
15207 O O   . VAL D  343 ? 1.1978 1.0800 0.8387 -0.1390 -0.1068 -0.0219 343 VAL D O   
15208 C CB  . VAL D  343 ? 0.7737 0.6972 0.4472 -0.1031 -0.1006 -0.0393 343 VAL D CB  
15209 C CG1 . VAL D  343 ? 0.7435 0.6606 0.3920 -0.1091 -0.0999 -0.0336 343 VAL D CG1 
15210 C CG2 . VAL D  343 ? 0.7351 0.6782 0.4338 -0.0841 -0.0995 -0.0496 343 VAL D CG2 
15211 N N   . PRO D  344 ? 0.8915 0.7252 0.4945 -0.1234 -0.1270 -0.0124 344 PRO D N   
15212 C CA  . PRO D  344 ? 0.9091 0.7168 0.4825 -0.1443 -0.1301 -0.0004 344 PRO D CA  
15213 C C   . PRO D  344 ? 0.9096 0.7413 0.4791 -0.1652 -0.1150 0.0017  344 PRO D C   
15214 O O   . PRO D  344 ? 0.9007 0.7514 0.4702 -0.1621 -0.1080 -0.0013 344 PRO D O   
15215 C CB  . PRO D  344 ? 0.8107 0.5842 0.3543 -0.1357 -0.1442 0.0073  344 PRO D CB  
15216 C CG  . PRO D  344 ? 0.7820 0.5555 0.3417 -0.1099 -0.1524 -0.0004 344 PRO D CG  
15217 C CD  . PRO D  344 ? 0.7421 0.5585 0.3373 -0.1031 -0.1393 -0.0125 344 PRO D CD  
15218 N N   . GLY D  345 ? 0.9513 0.7825 0.5170 -0.1867 -0.1104 0.0065  345 GLY D N   
15219 C CA  . GLY D  345 ? 0.9694 0.8228 0.5290 -0.2085 -0.0962 0.0093  345 GLY D CA  
15220 C C   . GLY D  345 ? 0.9346 0.8319 0.5273 -0.2145 -0.0808 -0.0004 345 GLY D C   
15221 O O   . GLY D  345 ? 0.9639 0.8834 0.5551 -0.2338 -0.0682 0.0011  345 GLY D O   
15222 N N   . PHE D  346 ? 0.8378 0.7487 0.4604 -0.1975 -0.0820 -0.0105 346 PHE D N   
15223 C CA  . PHE D  346 ? 0.7947 0.7463 0.4505 -0.1996 -0.0694 -0.0205 346 PHE D CA  
15224 C C   . PHE D  346 ? 0.8266 0.7709 0.4931 -0.2063 -0.0744 -0.0198 346 PHE D C   
15225 O O   . PHE D  346 ? 0.8440 0.7667 0.5138 -0.1926 -0.0863 -0.0209 346 PHE D O   
15226 C CB  . PHE D  346 ? 0.6821 0.6568 0.3645 -0.1761 -0.0663 -0.0330 346 PHE D CB  
15227 C CG  . PHE D  346 ? 0.6629 0.6510 0.3390 -0.1706 -0.0596 -0.0359 346 PHE D CG  
15228 C CD1 . PHE D  346 ? 0.6560 0.6181 0.3091 -0.1622 -0.0690 -0.0307 346 PHE D CD1 
15229 C CD2 . PHE D  346 ? 0.6460 0.6729 0.3394 -0.1731 -0.0445 -0.0446 346 PHE D CD2 
15230 C CE1 . PHE D  346 ? 0.6410 0.6152 0.2877 -0.1578 -0.0635 -0.0336 346 PHE D CE1 
15231 C CE2 . PHE D  346 ? 0.6247 0.6622 0.3108 -0.1680 -0.0388 -0.0480 346 PHE D CE2 
15232 C CZ  . PHE D  346 ? 0.6260 0.6369 0.2885 -0.1610 -0.0484 -0.0423 346 PHE D CZ  
15233 N N   . SER D  347 ? 0.8383 0.8020 0.5101 -0.2276 -0.0654 -0.0182 347 SER D N   
15234 C CA  . SER D  347 ? 0.8205 0.7851 0.5064 -0.2359 -0.0684 -0.0189 347 SER D CA  
15235 C C   . SER D  347 ? 0.7202 0.7356 0.4370 -0.2425 -0.0528 -0.0279 347 SER D C   
15236 O O   . SER D  347 ? 0.7069 0.7503 0.4272 -0.2441 -0.0403 -0.0316 347 SER D O   
15237 C CB  . SER D  347 ? 1.0314 0.9638 0.6882 -0.2598 -0.0753 -0.0055 347 SER D CB  
15238 O OG  . SER D  347 ? 1.0618 0.9954 0.7315 -0.2702 -0.0784 -0.0062 347 SER D OG  
15239 N N   . LYS D  348 ? 0.6450 0.6730 0.3842 -0.2451 -0.0539 -0.0323 348 LYS D N   
15240 C CA  . LYS D  348 ? 0.6259 0.7032 0.3949 -0.2516 -0.0399 -0.0408 348 LYS D CA  
15241 C C   . LYS D  348 ? 0.6649 0.7543 0.4217 -0.2811 -0.0312 -0.0333 348 LYS D C   
15242 O O   . LYS D  348 ? 0.6549 0.7880 0.4302 -0.2887 -0.0168 -0.0393 348 LYS D O   
15243 C CB  . LYS D  348 ? 0.5773 0.6664 0.3747 -0.2454 -0.0443 -0.0479 348 LYS D CB  
15244 C CG  . LYS D  348 ? 0.6777 0.7463 0.4661 -0.2648 -0.0528 -0.0402 348 LYS D CG  
15245 C CD  . LYS D  348 ? 0.6534 0.7395 0.4716 -0.2597 -0.0560 -0.0482 348 LYS D CD  
15246 C CE  . LYS D  348 ? 0.6843 0.7443 0.4911 -0.2781 -0.0668 -0.0408 348 LYS D CE  
15247 N NZ  . LYS D  348 ? 0.7064 0.7753 0.5023 -0.3095 -0.0604 -0.0325 348 LYS D NZ  
15248 N N   . ASP D  349 ? 0.7677 0.8180 0.4929 -0.2976 -0.0402 -0.0202 349 ASP D N   
15249 C CA  . ASP D  349 ? 0.8909 0.9482 0.6026 -0.3290 -0.0338 -0.0113 349 ASP D CA  
15250 C C   . ASP D  349 ? 1.0442 1.1097 0.7331 -0.3430 -0.0227 -0.0053 349 ASP D C   
15251 O O   . ASP D  349 ? 1.0503 1.1528 0.7472 -0.3621 -0.0087 -0.0060 349 ASP D O   
15252 C CB  . ASP D  349 ? 1.0869 1.1008 0.7780 -0.3439 -0.0486 -0.0005 349 ASP D CB  
15253 C CG  . ASP D  349 ? 1.1164 1.1328 0.8334 -0.3348 -0.0565 -0.0078 349 ASP D CG  
15254 O OD1 . ASP D  349 ? 1.1138 1.1758 0.8647 -0.3346 -0.0469 -0.0175 349 ASP D OD1 
15255 O OD2 . ASP D  349 ? 1.1276 1.1010 0.8311 -0.3268 -0.0724 -0.0044 349 ASP D OD2 
15256 N N   . ASN D  350 ? 0.9456 0.9791 0.6067 -0.3333 -0.0288 0.0002  350 ASN D N   
15257 C CA  . ASN D  350 ? 0.9069 0.9505 0.5478 -0.3424 -0.0182 0.0040  350 ASN D CA  
15258 C C   . ASN D  350 ? 0.8520 0.9346 0.5163 -0.3223 -0.0063 -0.0100 350 ASN D C   
15259 O O   . ASN D  350 ? 0.8077 0.9063 0.5022 -0.3021 -0.0072 -0.0214 350 ASN D O   
15260 C CB  . ASN D  350 ? 1.0494 1.0404 0.6459 -0.3452 -0.0305 0.0178  350 ASN D CB  
15261 C CG  . ASN D  350 ? 1.0685 1.0210 0.6607 -0.3187 -0.0476 0.0167  350 ASN D CG  
15262 O OD1 . ASN D  350 ? 1.0329 0.9931 0.6525 -0.3009 -0.0514 0.0073  350 ASN D OD1 
15263 N ND2 . ASN D  350 ? 1.1580 1.0703 0.7152 -0.3161 -0.0580 0.0264  350 ASN D ND2 
15264 N N   . GLU D  351 ? 0.9102 1.0074 0.5598 -0.3281 0.0045  -0.0093 351 GLU D N   
15265 C CA  . GLU D  351 ? 0.9117 1.0411 0.5800 -0.3085 0.0146  -0.0228 351 GLU D CA  
15266 C C   . GLU D  351 ? 0.8709 0.9683 0.5244 -0.2866 0.0035  -0.0224 351 GLU D C   
15267 O O   . GLU D  351 ? 0.8155 0.9308 0.4790 -0.2698 0.0091  -0.0322 351 GLU D O   
15268 C CB  . GLU D  351 ? 1.1510 1.3141 0.8117 -0.3235 0.0321  -0.0243 351 GLU D CB  
15269 C CG  . GLU D  351 ? 1.2215 1.4291 0.9050 -0.3412 0.0459  -0.0286 351 GLU D CG  
15270 C CD  . GLU D  351 ? 1.3200 1.5495 0.9838 -0.3645 0.0608  -0.0242 351 GLU D CD  
15271 O OE1 . GLU D  351 ? 1.3438 1.5527 0.9757 -0.3658 0.0601  -0.0180 351 GLU D OE1 
15272 O OE2 . GLU D  351 ? 1.3546 1.6231 1.0349 -0.3818 0.0731  -0.0268 351 GLU D OE2 
15273 N N   . SER D  352 ? 0.9219 0.9719 0.5511 -0.2873 -0.0126 -0.0110 352 SER D N   
15274 C CA  . SER D  352 ? 0.8965 0.9151 0.5143 -0.2657 -0.0255 -0.0104 352 SER D CA  
15275 C C   . SER D  352 ? 0.8360 0.8587 0.4367 -0.2607 -0.0206 -0.0113 352 SER D C   
15276 O O   . SER D  352 ? 0.8039 0.8282 0.4138 -0.2390 -0.0236 -0.0189 352 SER D O   
15277 C CB  . SER D  352 ? 0.9945 1.0237 0.6458 -0.2411 -0.0293 -0.0224 352 SER D CB  
15278 O OG  . SER D  352 ? 1.0007 1.0280 0.6685 -0.2450 -0.0338 -0.0226 352 SER D OG  
15279 N N   . LEU D  353 ? 0.7494 0.7751 0.3251 -0.2813 -0.0128 -0.0039 353 LEU D N   
15280 C CA  . LEU D  353 ? 0.7583 0.7821 0.3120 -0.2780 -0.0101 -0.0032 353 LEU D CA  
15281 C C   . LEU D  353 ? 0.8218 0.7971 0.3499 -0.2680 -0.0291 0.0063  353 LEU D C   
15282 O O   . LEU D  353 ? 0.9016 0.8430 0.4107 -0.2783 -0.0400 0.0180  353 LEU D O   
15283 C CB  . LEU D  353 ? 0.7941 0.8282 0.3228 -0.3044 0.0014  0.0044  353 LEU D CB  
15284 C CG  . LEU D  353 ? 0.8542 0.9337 0.4042 -0.3214 0.0194  -0.0014 353 LEU D CG  
15285 C CD1 . LEU D  353 ? 0.9003 0.9880 0.4208 -0.3484 0.0304  0.0074  353 LEU D CD1 
15286 C CD2 . LEU D  353 ? 0.7913 0.9166 0.3787 -0.3042 0.0317  -0.0199 353 LEU D CD2 
15287 N N   . ILE D  354 ? 0.8141 0.7857 0.3425 -0.2475 -0.0340 0.0009  354 ILE D N   
15288 C CA  . ILE D  354 ? 0.8031 0.7331 0.3132 -0.2342 -0.0528 0.0078  354 ILE D CA  
15289 C C   . ILE D  354 ? 0.8439 0.7599 0.3220 -0.2348 -0.0559 0.0136  354 ILE D C   
15290 O O   . ILE D  354 ? 0.8468 0.7892 0.3229 -0.2396 -0.0432 0.0085  354 ILE D O   
15291 C CB  . ILE D  354 ? 0.7475 0.6814 0.2862 -0.2072 -0.0595 -0.0027 354 ILE D CB  
15292 C CG1 . ILE D  354 ? 0.7313 0.7032 0.2926 -0.1961 -0.0474 -0.0167 354 ILE D CG1 
15293 C CG2 . ILE D  354 ? 0.7219 0.6564 0.2848 -0.2049 -0.0622 -0.0055 354 ILE D CG2 
15294 C CD1 . ILE D  354 ? 0.6628 0.6383 0.2493 -0.1715 -0.0538 -0.0262 354 ILE D CD1 
15295 N N   . SER D  355 ? 0.9385 0.8129 0.3911 -0.2295 -0.0733 0.0237  355 SER D N   
15296 C CA  . SER D  355 ? 1.0056 0.8633 0.4266 -0.2284 -0.0792 0.0299  355 SER D CA  
15297 C C   . SER D  355 ? 0.9400 0.8101 0.3775 -0.2042 -0.0824 0.0192  355 SER D C   
15298 O O   . SER D  355 ? 0.8620 0.7489 0.3329 -0.1886 -0.0813 0.0085  355 SER D O   
15299 C CB  . SER D  355 ? 1.1946 1.0016 0.5817 -0.2309 -0.0982 0.0449  355 SER D CB  
15300 O OG  . SER D  355 ? 1.1878 0.9761 0.5883 -0.2089 -0.1131 0.0422  355 SER D OG  
15301 N N   . ARG D  356 ? 0.9508 0.8136 0.3751 -0.1982 -0.0856 0.0222  356 ARG D N   
15302 C CA  . ARG D  356 ? 0.9286 0.8038 0.3725 -0.1752 -0.0886 0.0126  356 ARG D CA  
15303 C C   . ARG D  356 ? 0.9186 0.7723 0.3715 -0.1563 -0.1051 0.0132  356 ARG D C   
15304 O O   . ARG D  356 ? 0.8734 0.7437 0.3532 -0.1406 -0.1052 0.0027  356 ARG D O   
15305 C CB  . ARG D  356 ? 1.0087 0.8822 0.4381 -0.1726 -0.0890 0.0152  356 ARG D CB  
15306 C CG  . ARG D  356 ? 0.9777 0.8628 0.4271 -0.1495 -0.0937 0.0058  356 ARG D CG  
15307 C CD  . ARG D  356 ? 0.9884 0.8934 0.4362 -0.1493 -0.0848 0.0003  356 ARG D CD  
15308 N NE  . ARG D  356 ? 0.9697 0.8940 0.4433 -0.1305 -0.0852 -0.0118 356 ARG D NE  
15309 C CZ  . ARG D  356 ? 0.9418 0.8945 0.4378 -0.1281 -0.0732 -0.0243 356 ARG D CZ  
15310 N NH1 . ARG D  356 ? 0.9371 0.9060 0.4346 -0.1426 -0.0593 -0.0271 356 ARG D NH1 
15311 N NH2 . ARG D  356 ? 0.9176 0.8832 0.4349 -0.1115 -0.0752 -0.0341 356 ARG D NH2 
15312 N N   . ALA D  357 ? 0.9795 0.7961 0.4103 -0.1578 -0.1189 0.0253  357 ALA D N   
15313 C CA  . ALA D  357 ? 0.9962 0.7914 0.4349 -0.1389 -0.1348 0.0259  357 ALA D CA  
15314 C C   . ALA D  357 ? 0.9677 0.7714 0.4281 -0.1356 -0.1336 0.0187  357 ALA D C   
15315 O O   . ALA D  357 ? 0.9507 0.7556 0.4315 -0.1159 -0.1409 0.0126  357 ALA D O   
15316 C CB  . ALA D  357 ? 1.1129 0.8652 0.5227 -0.1432 -0.1489 0.0398  357 ALA D CB  
15317 N N   . GLN D  358 ? 0.9826 0.7952 0.4409 -0.1550 -0.1234 0.0191  358 GLN D N   
15318 C CA  . GLN D  358 ? 0.9666 0.7939 0.4568 -0.1515 -0.1183 0.0117  358 GLN D CA  
15319 C C   . GLN D  358 ? 0.9157 0.7799 0.4404 -0.1369 -0.1094 -0.0028 358 GLN D C   
15320 O O   . GLN D  358 ? 0.8812 0.7487 0.4294 -0.1215 -0.1138 -0.0092 358 GLN D O   
15321 C CB  . GLN D  358 ? 0.9820 0.8173 0.4715 -0.1747 -0.1070 0.0151  358 GLN D CB  
15322 C CG  . GLN D  358 ? 1.0033 0.7992 0.4683 -0.1869 -0.1180 0.0278  358 GLN D CG  
15323 C CD  . GLN D  358 ? 0.9917 0.7992 0.4637 -0.2085 -0.1074 0.0294  358 GLN D CD  
15324 O OE1 . GLN D  358 ? 1.0087 0.8323 0.4709 -0.2284 -0.0952 0.0325  358 GLN D OE1 
15325 N NE2 . GLN D  358 ? 0.9699 0.7708 0.4589 -0.2048 -0.1120 0.0270  358 GLN D NE2 
15326 N N   . PHE D  359 ? 0.9873 0.8777 0.5135 -0.1419 -0.0972 -0.0080 359 PHE D N   
15327 C CA  . PHE D  359 ? 0.9610 0.8831 0.5162 -0.1285 -0.0896 -0.0215 359 PHE D CA  
15328 C C   . PHE D  359 ? 0.9522 0.8664 0.5119 -0.1075 -0.1019 -0.0244 359 PHE D C   
15329 O O   . PHE D  359 ? 0.9358 0.8647 0.5232 -0.0935 -0.1016 -0.0334 359 PHE D O   
15330 C CB  . PHE D  359 ? 0.7724 0.7198 0.3232 -0.1380 -0.0754 -0.0264 359 PHE D CB  
15331 C CG  . PHE D  359 ? 0.6379 0.6115 0.2115 -0.1240 -0.0699 -0.0395 359 PHE D CG  
15332 C CD1 . PHE D  359 ? 0.8298 0.8301 0.4350 -0.1199 -0.0598 -0.0503 359 PHE D CD1 
15333 C CD2 . PHE D  359 ? 0.6395 0.6106 0.2065 -0.1137 -0.0748 -0.0406 359 PHE D CD2 
15334 C CE1 . PHE D  359 ? 0.5786 0.5994 0.2025 -0.1076 -0.0557 -0.0619 359 PHE D CE1 
15335 C CE2 . PHE D  359 ? 0.6110 0.6036 0.2002 -0.1012 -0.0701 -0.0520 359 PHE D CE2 
15336 C CZ  . PHE D  359 ? 0.5823 0.5984 0.1965 -0.0993 -0.0610 -0.0628 359 PHE D CZ  
15337 N N   . LEU D  360 ? 0.8957 0.7886 0.4328 -0.1046 -0.1120 -0.0164 360 LEU D N   
15338 C CA  . LEU D  360 ? 0.8581 0.7476 0.4061 -0.0837 -0.1225 -0.0183 360 LEU D CA  
15339 C C   . LEU D  360 ? 0.8566 0.7349 0.4187 -0.0706 -0.1324 -0.0193 360 LEU D C   
15340 O O   . LEU D  360 ? 0.8651 0.7594 0.4519 -0.0551 -0.1334 -0.0273 360 LEU D O   
15341 C CB  . LEU D  360 ? 0.7763 0.6447 0.3009 -0.0829 -0.1314 -0.0086 360 LEU D CB  
15342 C CG  . LEU D  360 ? 0.7970 0.6760 0.3070 -0.0945 -0.1222 -0.0076 360 LEU D CG  
15343 C CD1 . LEU D  360 ? 0.8546 0.7149 0.3446 -0.0906 -0.1324 0.0009  360 LEU D CD1 
15344 C CD2 . LEU D  360 ? 0.7583 0.6709 0.2910 -0.0888 -0.1113 -0.0205 360 LEU D CD2 
15345 N N   . ALA D  361 ? 0.7440 0.5946 0.2901 -0.0770 -0.1398 -0.0112 361 ALA D N   
15346 C CA  . ALA D  361 ? 0.7191 0.5573 0.2773 -0.0648 -0.1489 -0.0126 361 ALA D CA  
15347 C C   . ALA D  361 ? 0.7148 0.5771 0.3013 -0.0632 -0.1401 -0.0229 361 ALA D C   
15348 O O   . ALA D  361 ? 0.6144 0.4818 0.2210 -0.0476 -0.1445 -0.0288 361 ALA D O   
15349 C CB  . ALA D  361 ? 0.8277 0.6293 0.3610 -0.0738 -0.1583 -0.0021 361 ALA D CB  
15350 N N   . GLY D  362 ? 0.6315 0.5121 0.2241 -0.0785 -0.1259 -0.0249 362 GLY D N   
15351 C CA  . GLY D  362 ? 0.6004 0.5067 0.2240 -0.0772 -0.1156 -0.0341 362 GLY D CA  
15352 C C   . GLY D  362 ? 0.5625 0.4939 0.2097 -0.0626 -0.1120 -0.0447 362 GLY D C   
15353 O O   . GLY D  362 ? 0.5345 0.4794 0.2071 -0.0545 -0.1096 -0.0518 362 GLY D O   
15354 N N   . VAL D  363 ? 0.5756 0.5127 0.2134 -0.0600 -0.1122 -0.0456 363 VAL D N   
15355 C CA  . VAL D  363 ? 0.5649 0.5228 0.2222 -0.0471 -0.1105 -0.0549 363 VAL D CA  
15356 C C   . VAL D  363 ? 0.5691 0.5200 0.2372 -0.0296 -0.1219 -0.0556 363 VAL D C   
15357 O O   . VAL D  363 ? 0.4956 0.4639 0.1882 -0.0200 -0.1192 -0.0631 363 VAL D O   
15358 C CB  . VAL D  363 ? 0.5441 0.5105 0.1899 -0.0493 -0.1074 -0.0560 363 VAL D CB  
15359 C CG1 . VAL D  363 ? 0.5162 0.5013 0.1842 -0.0349 -0.1074 -0.0641 363 VAL D CG1 
15360 C CG2 . VAL D  363 ? 0.5486 0.5300 0.1903 -0.0646 -0.0933 -0.0587 363 VAL D CG2 
15361 N N   . ARG D  364 ? 0.6768 0.6051 0.3318 -0.0252 -0.1325 -0.0473 364 ARG D N   
15362 C CA  . ARG D  364 ? 0.7011 0.6261 0.3717 -0.0090 -0.1404 -0.0477 364 ARG D CA  
15363 C C   . ARG D  364 ? 0.7209 0.6434 0.4039 -0.0067 -0.1403 -0.0511 364 ARG D C   
15364 O O   . ARG D  364 ? 0.7242 0.6577 0.4300 0.0054  -0.1405 -0.0557 364 ARG D O   
15365 C CB  . ARG D  364 ? 0.7114 0.6105 0.3637 -0.0041 -0.1522 -0.0387 364 ARG D CB  
15366 C CG  . ARG D  364 ? 0.7605 0.6596 0.3985 -0.0063 -0.1538 -0.0344 364 ARG D CG  
15367 C CD  . ARG D  364 ? 0.7474 0.6763 0.4048 -0.0016 -0.1476 -0.0413 364 ARG D CD  
15368 N NE  . ARG D  364 ? 0.7607 0.6988 0.4391 0.0131  -0.1520 -0.0436 364 ARG D NE  
15369 C CZ  . ARG D  364 ? 0.8219 0.7581 0.4979 0.0206  -0.1592 -0.0402 364 ARG D CZ  
15370 N NH1 . ARG D  364 ? 0.8739 0.7977 0.5268 0.0152  -0.1634 -0.0341 364 ARG D NH1 
15371 N NH2 . ARG D  364 ? 0.8047 0.7514 0.5007 0.0330  -0.1620 -0.0429 364 ARG D NH2 
15372 N N   . ILE D  365 ? 0.7330 0.6418 0.4010 -0.0202 -0.1395 -0.0485 365 ILE D N   
15373 C CA  . ILE D  365 ? 0.7139 0.6215 0.3968 -0.0195 -0.1383 -0.0510 365 ILE D CA  
15374 C C   . ILE D  365 ? 0.6473 0.5850 0.3595 -0.0174 -0.1273 -0.0606 365 ILE D C   
15375 O O   . ILE D  365 ? 0.6201 0.5611 0.3488 -0.0090 -0.1289 -0.0648 365 ILE D O   
15376 C CB  . ILE D  365 ? 0.6638 0.5519 0.3310 -0.0358 -0.1378 -0.0438 365 ILE D CB  
15377 C CG1 . ILE D  365 ? 0.7374 0.5890 0.3819 -0.0317 -0.1529 -0.0361 365 ILE D CG1 
15378 C CG2 . ILE D  365 ? 0.6120 0.5108 0.2993 -0.0399 -0.1315 -0.0484 365 ILE D CG2 
15379 C CD1 . ILE D  365 ? 0.7709 0.6073 0.3941 -0.0253 -0.1624 -0.0306 365 ILE D CD1 
15380 N N   . GLY D  366 ? 0.6081 0.5664 0.3254 -0.0243 -0.1167 -0.0642 366 GLY D N   
15381 C CA  . GLY D  366 ? 0.6129 0.5974 0.3558 -0.0225 -0.1068 -0.0731 366 GLY D CA  
15382 C C   . GLY D  366 ? 0.6262 0.6261 0.3828 -0.0100 -0.1072 -0.0797 366 GLY D C   
15383 O O   . GLY D  366 ? 0.6385 0.6549 0.4165 -0.0052 -0.1023 -0.0866 366 GLY D O   
15384 N N   . VAL D  367 ? 0.6784 0.6731 0.4236 -0.0058 -0.1127 -0.0767 367 VAL D N   
15385 C CA  . VAL D  367 ? 0.6243 0.6322 0.3884 0.0028  -0.1105 -0.0783 367 VAL D CA  
15386 C C   . VAL D  367 ? 0.7039 0.7008 0.4677 0.0125  -0.1194 -0.0726 367 VAL D C   
15387 O O   . VAL D  367 ? 0.7534 0.7465 0.5071 0.0136  -0.1236 -0.0687 367 VAL D O   
15388 C CB  . VAL D  367 ? 0.4593 0.4753 0.2167 -0.0021 -0.1063 -0.0793 367 VAL D CB  
15389 C CG1 . VAL D  367 ? 0.3999 0.4281 0.1780 0.0044  -0.1033 -0.0819 367 VAL D CG1 
15390 C CG2 . VAL D  367 ? 0.4458 0.4696 0.1962 -0.0120 -0.0981 -0.0846 367 VAL D CG2 
15391 N N   . PRO D  368 ? 0.5557 0.5481 0.3306 0.0203  -0.1225 -0.0727 368 PRO D N   
15392 C CA  . PRO D  368 ? 0.5696 0.5523 0.3455 0.0317  -0.1305 -0.0691 368 PRO D CA  
15393 C C   . PRO D  368 ? 0.5534 0.5523 0.3451 0.0388  -0.1287 -0.0704 368 PRO D C   
15394 O O   . PRO D  368 ? 0.4758 0.4710 0.2645 0.0461  -0.1350 -0.0674 368 PRO D O   
15395 C CB  . PRO D  368 ? 0.6918 0.6712 0.4790 0.0370  -0.1309 -0.0714 368 PRO D CB  
15396 C CG  . PRO D  368 ? 0.6824 0.6648 0.4689 0.0265  -0.1254 -0.0747 368 PRO D CG  
15397 C CD  . PRO D  368 ? 0.6588 0.6568 0.4471 0.0195  -0.1179 -0.0774 368 PRO D CD  
15398 N N   . GLN D  369 ? 0.7042 0.7201 0.5120 0.0360  -0.1203 -0.0750 369 GLN D N   
15399 C CA  . GLN D  369 ? 0.7149 0.7460 0.5369 0.0392  -0.1172 -0.0766 369 GLN D CA  
15400 C C   . GLN D  369 ? 0.6834 0.7134 0.4939 0.0379  -0.1216 -0.0735 369 GLN D C   
15401 O O   . GLN D  369 ? 0.6812 0.7188 0.4995 0.0440  -0.1242 -0.0729 369 GLN D O   
15402 C CB  . GLN D  369 ? 0.8114 0.8537 0.6426 0.0324  -0.1083 -0.0813 369 GLN D CB  
15403 C CG  . GLN D  369 ? 0.9009 0.9514 0.7514 0.0360  -0.1033 -0.0848 369 GLN D CG  
15404 C CD  . GLN D  369 ? 1.0002 1.0429 0.8506 0.0376  -0.1046 -0.0850 369 GLN D CD  
15405 O OE1 . GLN D  369 ? 1.0752 1.1052 0.9103 0.0350  -0.1092 -0.0827 369 GLN D OE1 
15406 N NE2 . GLN D  369 ? 0.9569 1.0061 0.8232 0.0413  -0.1012 -0.0875 369 GLN D NE2 
15407 N N   . ALA D  370 ? 0.6176 0.6387 0.4084 0.0296  -0.1225 -0.0714 370 ALA D N   
15408 C CA  . ALA D  370 ? 0.5595 0.5808 0.3377 0.0256  -0.1249 -0.0690 370 ALA D CA  
15409 C C   . ALA D  370 ? 0.5939 0.6077 0.3650 0.0332  -0.1347 -0.0640 370 ALA D C   
15410 O O   . ALA D  370 ? 0.6091 0.6079 0.3718 0.0383  -0.1410 -0.0607 370 ALA D O   
15411 C CB  . ALA D  370 ? 0.4318 0.4461 0.1894 0.0142  -0.1224 -0.0685 370 ALA D CB  
15412 N N   . SER D  371 ? 0.5704 0.5934 0.3443 0.0341  -0.1364 -0.0636 371 SER D N   
15413 C CA  . SER D  371 ? 0.6301 0.6470 0.3943 0.0397  -0.1458 -0.0590 371 SER D CA  
15414 C C   . SER D  371 ? 0.6798 0.6836 0.4181 0.0312  -0.1482 -0.0546 371 SER D C   
15415 O O   . SER D  371 ? 0.6646 0.6655 0.3938 0.0217  -0.1423 -0.0558 371 SER D O   
15416 C CB  . SER D  371 ? 0.7340 0.7669 0.5098 0.0421  -0.1468 -0.0604 371 SER D CB  
15417 O OG  . SER D  371 ? 0.7297 0.7684 0.4995 0.0315  -0.1425 -0.0618 371 SER D OG  
15418 N N   . ASP D  372 ? 0.8773 0.8741 0.6036 0.0348  -0.1568 -0.0498 372 ASP D N   
15419 C CA  . ASP D  372 ? 0.9155 0.9005 0.6161 0.0266  -0.1592 -0.0451 372 ASP D CA  
15420 C C   . ASP D  372 ? 0.8695 0.8687 0.5679 0.0148  -0.1506 -0.0490 372 ASP D C   
15421 O O   . ASP D  372 ? 0.8788 0.8747 0.5640 0.0054  -0.1447 -0.0498 372 ASP D O   
15422 C CB  . ASP D  372 ? 0.9105 0.8872 0.6007 0.0335  -0.1704 -0.0395 372 ASP D CB  
15423 C CG  . ASP D  372 ? 0.9004 0.8568 0.5864 0.0451  -0.1799 -0.0355 372 ASP D CG  
15424 O OD1 . ASP D  372 ? 0.9085 0.8608 0.6038 0.0490  -0.1778 -0.0379 372 ASP D OD1 
15425 O OD2 . ASP D  372 ? 0.8480 0.7917 0.5209 0.0506  -0.1899 -0.0303 372 ASP D OD2 
15426 N N   . LEU D  373 ? 0.7795 0.7940 0.4908 0.0157  -0.1501 -0.0519 373 LEU D N   
15427 C CA  . LEU D  373 ? 0.7325 0.7568 0.4398 0.0053  -0.1439 -0.0556 373 LEU D CA  
15428 C C   . LEU D  373 ? 0.6817 0.7095 0.3947 -0.0017 -0.1330 -0.0617 373 LEU D C   
15429 O O   . LEU D  373 ? 0.6937 0.7220 0.3941 -0.0115 -0.1271 -0.0644 373 LEU D O   
15430 C CB  . LEU D  373 ? 0.4939 0.5300 0.2138 0.0078  -0.1469 -0.0572 373 LEU D CB  
15431 C CG  . LEU D  373 ? 0.4972 0.5388 0.2108 -0.0021 -0.1432 -0.0607 373 LEU D CG  
15432 C CD1 . LEU D  373 ? 0.5236 0.5618 0.2123 -0.0092 -0.1453 -0.0576 373 LEU D CD1 
15433 C CD2 . LEU D  373 ? 0.4876 0.5398 0.2166 0.0015  -0.1471 -0.0623 373 LEU D CD2 
15434 N N   . ALA D  374 ? 0.6180 0.6479 0.3495 0.0040  -0.1303 -0.0643 374 ALA D N   
15435 C CA  . ALA D  374 ? 0.5762 0.6087 0.3149 -0.0005 -0.1208 -0.0701 374 ALA D CA  
15436 C C   . ALA D  374 ? 0.5730 0.5975 0.2940 -0.0077 -0.1174 -0.0696 374 ALA D C   
15437 O O   . ALA D  374 ? 0.5566 0.5807 0.2715 -0.0149 -0.1099 -0.0742 374 ALA D O   
15438 C CB  . ALA D  374 ? 0.5163 0.5544 0.2784 0.0077  -0.1192 -0.0724 374 ALA D CB  
15439 N N   . ALA D  375 ? 0.5033 0.5186 0.2149 -0.0046 -0.1235 -0.0642 375 ALA D N   
15440 C CA  . ALA D  375 ? 0.5222 0.5289 0.2151 -0.0109 -0.1216 -0.0627 375 ALA D CA  
15441 C C   . ALA D  375 ? 0.5696 0.5779 0.2417 -0.0178 -0.1193 -0.0624 375 ALA D C   
15442 O O   . ALA D  375 ? 0.5669 0.5734 0.2276 -0.0233 -0.1128 -0.0652 375 ALA D O   
15443 C CB  . ALA D  375 ? 0.5542 0.5410 0.2384 -0.0053 -0.1308 -0.0555 375 ALA D CB  
15444 N N   . GLU D  376 ? 0.6101 0.6188 0.2767 -0.0157 -0.1251 -0.0590 376 GLU D N   
15445 C CA  . GLU D  376 ? 0.6878 0.6977 0.3357 -0.0198 -0.1232 -0.0593 376 GLU D CA  
15446 C C   . GLU D  376 ? 0.6254 0.6505 0.2815 -0.0198 -0.1132 -0.0701 376 GLU D C   
15447 O O   . GLU D  376 ? 0.6264 0.6402 0.2623 -0.0239 -0.1089 -0.0712 376 GLU D O   
15448 C CB  . GLU D  376 ? 1.1115 1.1207 0.7550 -0.0166 -0.1320 -0.0544 376 GLU D CB  
15449 C CG  . GLU D  376 ? 1.2722 1.2761 0.8920 -0.0205 -0.1322 -0.0523 376 GLU D CG  
15450 C CD  . GLU D  376 ? 1.4044 1.3921 1.0089 -0.0179 -0.1438 -0.0422 376 GLU D CD  
15451 O OE1 . GLU D  376 ? 1.4020 1.3805 1.0139 -0.0112 -0.1517 -0.0376 376 GLU D OE1 
15452 O OE2 . GLU D  376 ? 1.4799 1.4625 1.0648 -0.0215 -0.1454 -0.0393 376 GLU D OE2 
15453 N N   . ALA D  377 ? 0.6827 0.7076 0.3570 -0.0294 -0.1094 -0.0703 377 ALA D N   
15454 C CA  . ALA D  377 ? 0.6562 0.6627 0.3256 -0.0239 -0.1058 -0.0784 377 ALA D CA  
15455 C C   . ALA D  377 ? 0.6581 0.6727 0.3305 -0.0241 -0.0962 -0.0841 377 ALA D C   
15456 O O   . ALA D  377 ? 0.6695 0.6933 0.3391 -0.0288 -0.0864 -0.0891 377 ALA D O   
15457 C CB  . ALA D  377 ? 0.4887 0.5089 0.1839 -0.0222 -0.1050 -0.0816 377 ALA D CB  
15458 N N   . VAL D  378 ? 0.5955 0.6093 0.2761 -0.0235 -0.0974 -0.0821 378 VAL D N   
15459 C CA  . VAL D  378 ? 0.5681 0.5930 0.2562 -0.0280 -0.0874 -0.0860 378 VAL D CA  
15460 C C   . VAL D  378 ? 0.5969 0.6223 0.2640 -0.0389 -0.0821 -0.0829 378 VAL D C   
15461 O O   . VAL D  378 ? 0.6121 0.6494 0.2812 -0.0471 -0.0702 -0.0873 378 VAL D O   
15462 C CB  . VAL D  378 ? 0.4778 0.5000 0.1766 -0.0253 -0.0915 -0.0839 378 VAL D CB  
15463 C CG1 . VAL D  378 ? 0.4723 0.5058 0.1770 -0.0326 -0.0817 -0.0874 378 VAL D CG1 
15464 C CG2 . VAL D  378 ? 0.4516 0.4801 0.1757 -0.0186 -0.0925 -0.0858 378 VAL D CG2 
15465 N N   . VAL D  379 ? 0.5366 0.5496 0.1844 -0.0402 -0.0903 -0.0744 379 VAL D N   
15466 C CA  . VAL D  379 ? 0.5650 0.5717 0.1891 -0.0541 -0.0858 -0.0681 379 VAL D CA  
15467 C C   . VAL D  379 ? 0.5739 0.5893 0.1911 -0.0574 -0.0781 -0.0726 379 VAL D C   
15468 O O   . VAL D  379 ? 0.6759 0.6995 0.2868 -0.0686 -0.0666 -0.0744 379 VAL D O   
15469 C CB  . VAL D  379 ? 0.5902 0.5764 0.1942 -0.0550 -0.0973 -0.0564 379 VAL D CB  
15470 C CG1 . VAL D  379 ? 0.6237 0.6016 0.2004 -0.0681 -0.0936 -0.0497 379 VAL D CG1 
15471 C CG2 . VAL D  379 ? 0.5909 0.5639 0.1954 -0.0569 -0.1021 -0.0510 379 VAL D CG2 
15472 N N   . LEU D  380 ? 0.6151 0.6301 0.2344 -0.0477 -0.0841 -0.0751 380 LEU D N   
15473 C CA  . LEU D  380 ? 0.5818 0.6023 0.1936 -0.0500 -0.0781 -0.0798 380 LEU D CA  
15474 C C   . LEU D  380 ? 0.5683 0.6037 0.1936 -0.0537 -0.0644 -0.0892 380 LEU D C   
15475 O O   . LEU D  380 ? 0.6039 0.6468 0.2193 -0.0617 -0.0546 -0.0918 380 LEU D O   
15476 C CB  . LEU D  380 ? 0.5767 0.5946 0.1935 -0.0389 -0.0870 -0.0827 380 LEU D CB  
15477 C CG  . LEU D  380 ? 0.5898 0.6134 0.2055 -0.0405 -0.0797 -0.0905 380 LEU D CG  
15478 C CD1 . LEU D  380 ? 0.6097 0.6327 0.2013 -0.0487 -0.0757 -0.0878 380 LEU D CD1 
15479 C CD2 . LEU D  380 ? 0.6014 0.6201 0.2251 -0.0322 -0.0877 -0.0936 380 LEU D CD2 
15480 N N   . HIS D  381 ? 0.5413 0.5826 0.1901 -0.0476 -0.0637 -0.0942 381 HIS D N   
15481 C CA  . HIS D  381 ? 0.5303 0.5875 0.1958 -0.0485 -0.0518 -0.1037 381 HIS D CA  
15482 C C   . HIS D  381 ? 0.5319 0.6011 0.1949 -0.0591 -0.0409 -0.1043 381 HIS D C   
15483 O O   . HIS D  381 ? 0.5381 0.6204 0.2004 -0.0637 -0.0298 -0.1105 381 HIS D O   
15484 C CB  . HIS D  381 ? 0.6476 0.7076 0.3390 -0.0397 -0.0543 -0.1078 381 HIS D CB  
15485 C CG  . HIS D  381 ? 0.6435 0.7158 0.3515 -0.0367 -0.0456 -0.1178 381 HIS D CG  
15486 N ND1 . HIS D  381 ? 0.6572 0.7257 0.3674 -0.0322 -0.0476 -0.1217 381 HIS D ND1 
15487 C CD2 . HIS D  381 ? 0.6109 0.6987 0.3338 -0.0373 -0.0357 -0.1249 381 HIS D CD2 
15488 C CE1 . HIS D  381 ? 0.6456 0.7247 0.3703 -0.0297 -0.0397 -0.1306 381 HIS D CE1 
15489 N NE2 . HIS D  381 ? 0.6225 0.7141 0.3559 -0.0319 -0.0324 -0.1329 381 HIS D NE2 
15490 N N   . TYR D  382 ? 0.5313 0.5961 0.1926 -0.0636 -0.0441 -0.0980 382 TYR D N   
15491 C CA  . TYR D  382 ? 0.5341 0.6115 0.1961 -0.0749 -0.0339 -0.0989 382 TYR D CA  
15492 C C   . TYR D  382 ? 0.7290 0.8038 0.3647 -0.0905 -0.0290 -0.0918 382 TYR D C   
15493 O O   . TYR D  382 ? 0.5701 0.6596 0.2062 -0.1018 -0.0182 -0.0935 382 TYR D O   
15494 C CB  . TYR D  382 ? 0.5190 0.5936 0.1926 -0.0740 -0.0388 -0.0964 382 TYR D CB  
15495 C CG  . TYR D  382 ? 0.4879 0.5746 0.1909 -0.0629 -0.0372 -0.1056 382 TYR D CG  
15496 C CD1 . TYR D  382 ? 0.4720 0.5496 0.1865 -0.0501 -0.0465 -0.1058 382 TYR D CD1 
15497 C CD2 . TYR D  382 ? 0.4759 0.5834 0.1954 -0.0655 -0.0264 -0.1137 382 TYR D CD2 
15498 C CE1 . TYR D  382 ? 0.4531 0.5394 0.1932 -0.0411 -0.0450 -0.1126 382 TYR D CE1 
15499 C CE2 . TYR D  382 ? 0.4497 0.5662 0.1955 -0.0548 -0.0259 -0.1213 382 TYR D CE2 
15500 C CZ  . TYR D  382 ? 0.4356 0.5401 0.1908 -0.0430 -0.0351 -0.1202 382 TYR D CZ  
15501 O OH  . TYR D  382 ? 0.4122 0.5236 0.1919 -0.0336 -0.0345 -0.1263 382 TYR D OH  
15502 N N   . THR D  383 ? 0.5881 0.6456 0.2015 -0.0915 -0.0366 -0.0839 383 THR D N   
15503 C CA  . THR D  383 ? 0.6213 0.6740 0.2079 -0.1062 -0.0324 -0.0762 383 THR D CA  
15504 C C   . THR D  383 ? 0.6298 0.7002 0.2140 -0.1099 -0.0195 -0.0838 383 THR D C   
15505 O O   . THR D  383 ? 0.7027 0.7762 0.2937 -0.0994 -0.0200 -0.0911 383 THR D O   
15506 C CB  . THR D  383 ? 0.6875 0.7154 0.2517 -0.1042 -0.0458 -0.0655 383 THR D CB  
15507 O OG1 . THR D  383 ? 0.7046 0.7145 0.2665 -0.1033 -0.0570 -0.0570 383 THR D OG1 
15508 C CG2 . THR D  383 ? 0.6799 0.7027 0.2162 -0.1183 -0.0413 -0.0582 383 THR D CG2 
15509 N N   . ASP D  384 ? 0.6472 0.7291 0.2214 -0.1251 -0.0079 -0.0823 384 ASP D N   
15510 C CA  . ASP D  384 ? 0.6632 0.7589 0.2293 -0.1293 0.0032  -0.0877 384 ASP D CA  
15511 C C   . ASP D  384 ? 0.6971 0.7727 0.2321 -0.1363 -0.0033 -0.0763 384 ASP D C   
15512 O O   . ASP D  384 ? 0.7197 0.7840 0.2358 -0.1500 -0.0048 -0.0648 384 ASP D O   
15513 C CB  . ASP D  384 ? 0.8174 0.9389 0.3891 -0.1420 0.0195  -0.0920 384 ASP D CB  
15514 C CG  . ASP D  384 ? 0.8752 1.0077 0.4308 -0.1505 0.0303  -0.0936 384 ASP D CG  
15515 O OD1 . ASP D  384 ? 0.8874 1.0144 0.4358 -0.1422 0.0280  -0.0973 384 ASP D OD1 
15516 O OD2 . ASP D  384 ? 0.9098 1.0572 0.4598 -0.1661 0.0413  -0.0912 384 ASP D OD2 
15517 N N   . TRP D  385 ? 0.7473 0.8173 0.2765 -0.1269 -0.0078 -0.0795 385 TRP D N   
15518 C CA  . TRP D  385 ? 0.7486 0.7980 0.2511 -0.1294 -0.0173 -0.0694 385 TRP D CA  
15519 C C   . TRP D  385 ? 0.7798 0.8346 0.2597 -0.1436 -0.0074 -0.0664 385 TRP D C   
15520 O O   . TRP D  385 ? 0.8057 0.8431 0.2600 -0.1497 -0.0139 -0.0560 385 TRP D O   
15521 C CB  . TRP D  385 ? 0.7223 0.7653 0.2293 -0.1137 -0.0268 -0.0743 385 TRP D CB  
15522 C CG  . TRP D  385 ? 0.6981 0.7317 0.2211 -0.1021 -0.0389 -0.0732 385 TRP D CG  
15523 C CD1 . TRP D  385 ? 0.6659 0.7081 0.2154 -0.0910 -0.0389 -0.0824 385 TRP D CD1 
15524 C CD2 . TRP D  385 ? 0.7052 0.7190 0.2194 -0.1002 -0.0529 -0.0621 385 TRP D CD2 
15525 N NE1 . TRP D  385 ? 0.6517 0.6822 0.2096 -0.0825 -0.0516 -0.0779 385 TRP D NE1 
15526 C CE2 . TRP D  385 ? 0.6751 0.6888 0.2122 -0.0872 -0.0605 -0.0659 385 TRP D CE2 
15527 C CE3 . TRP D  385 ? 0.7361 0.7313 0.2249 -0.1078 -0.0602 -0.0493 385 TRP D CE3 
15528 C CZ2 . TRP D  385 ? 0.6736 0.6722 0.2105 -0.0808 -0.0744 -0.0582 385 TRP D CZ2 
15529 C CZ3 . TRP D  385 ? 0.7356 0.7134 0.2238 -0.1010 -0.0747 -0.0414 385 TRP D CZ3 
15530 C CH2 . TRP D  385 ? 0.7072 0.6882 0.2200 -0.0873 -0.0814 -0.0463 385 TRP D CH2 
15531 N N   . LEU D  386 ? 0.8475 0.9270 0.3373 -0.1484 0.0083  -0.0757 386 LEU D N   
15532 C CA  . LEU D  386 ? 0.9401 1.0288 0.4106 -0.1635 0.0196  -0.0731 386 LEU D CA  
15533 C C   . LEU D  386 ? 0.9930 1.0754 0.4508 -0.1818 0.0208  -0.0603 386 LEU D C   
15534 O O   . LEU D  386 ? 1.0367 1.1123 0.4689 -0.1962 0.0231  -0.0511 386 LEU D O   
15535 C CB  . LEU D  386 ? 0.9932 1.1124 0.4803 -0.1619 0.0359  -0.0877 386 LEU D CB  
15536 C CG  . LEU D  386 ? 1.0799 1.2086 0.5479 -0.1693 0.0457  -0.0898 386 LEU D CG  
15537 C CD1 . LEU D  386 ? 1.1173 1.2705 0.5862 -0.1857 0.0618  -0.0900 386 LEU D CD1 
15538 C CD2 . LEU D  386 ? 1.1159 1.2194 0.5519 -0.1744 0.0355  -0.0776 386 LEU D CD2 
15539 N N   . HIS D  387 ? 0.8891 0.9716 0.3635 -0.1815 0.0183  -0.0593 387 HIS D N   
15540 C CA  . HIS D  387 ? 0.8596 0.9335 0.3236 -0.1985 0.0179  -0.0475 387 HIS D CA  
15541 C C   . HIS D  387 ? 0.7998 0.8513 0.2694 -0.1913 0.0030  -0.0415 387 HIS D C   
15542 O O   . HIS D  387 ? 0.8014 0.8630 0.2904 -0.1911 0.0054  -0.0454 387 HIS D O   
15543 C CB  . HIS D  387 ? 0.9463 1.0518 0.4276 -0.2090 0.0342  -0.0543 387 HIS D CB  
15544 C CG  . HIS D  387 ? 1.0287 1.1611 0.5091 -0.2150 0.0501  -0.0620 387 HIS D CG  
15545 N ND1 . HIS D  387 ? 1.1115 1.2386 0.5644 -0.2295 0.0537  -0.0536 387 HIS D ND1 
15546 C CD2 . HIS D  387 ? 1.0365 1.2007 0.5400 -0.2076 0.0629  -0.0774 387 HIS D CD2 
15547 C CE1 . HIS D  387 ? 1.1298 1.2857 0.5891 -0.2308 0.0685  -0.0639 387 HIS D CE1 
15548 N NE2 . HIS D  387 ? 1.1004 1.2787 0.5904 -0.2171 0.0740  -0.0786 387 HIS D NE2 
15549 N N   . PRO D  388 ? 0.7985 0.8203 0.2517 -0.1849 -0.0128 -0.0324 388 PRO D N   
15550 C CA  . PRO D  388 ? 0.7827 0.7842 0.2436 -0.1740 -0.0279 -0.0284 388 PRO D CA  
15551 C C   . PRO D  388 ? 0.8158 0.8037 0.2694 -0.1875 -0.0305 -0.0186 388 PRO D C   
15552 O O   . PRO D  388 ? 0.7737 0.7538 0.2410 -0.1796 -0.0385 -0.0191 388 PRO D O   
15553 C CB  . PRO D  388 ? 0.8798 0.8549 0.3210 -0.1667 -0.0427 -0.0199 388 PRO D CB  
15554 C CG  . PRO D  388 ? 0.9222 0.9056 0.3478 -0.1720 -0.0352 -0.0214 388 PRO D CG  
15555 C CD  . PRO D  388 ? 0.9090 0.9143 0.3340 -0.1891 -0.0175 -0.0241 388 PRO D CD  
15556 N N   . GLU D  389 ? 0.9771 0.9615 0.4086 -0.2081 -0.0241 -0.0096 389 GLU D N   
15557 C CA  . GLU D  389 ? 0.9881 0.9534 0.4061 -0.2240 -0.0282 0.0023  389 GLU D CA  
15558 C C   . GLU D  389 ? 0.8894 0.8807 0.3232 -0.2368 -0.0148 -0.0028 389 GLU D C   
15559 O O   . GLU D  389 ? 0.8697 0.8458 0.2957 -0.2489 -0.0191 0.0058  389 GLU D O   
15560 C CB  . GLU D  389 ? 1.2060 1.1496 0.5894 -0.2415 -0.0302 0.0168  389 GLU D CB  
15561 C CG  . GLU D  389 ? 1.2915 1.2053 0.6556 -0.2308 -0.0455 0.0243  389 GLU D CG  
15562 C CD  . GLU D  389 ? 1.3216 1.2089 0.6912 -0.2143 -0.0638 0.0275  389 GLU D CD  
15563 O OE1 . GLU D  389 ? 1.3227 1.1976 0.6946 -0.2192 -0.0682 0.0317  389 GLU D OE1 
15564 O OE2 . GLU D  389 ? 1.3319 1.2122 0.7044 -0.1964 -0.0738 0.0253  389 GLU D OE2 
15565 N N   . ASP D  390 ? 0.8301 0.8596 0.2861 -0.2340 0.0007  -0.0168 390 ASP D N   
15566 C CA  . ASP D  390 ? 0.8761 0.9354 0.3471 -0.2475 0.0151  -0.0219 390 ASP D CA  
15567 C C   . ASP D  390 ? 0.8926 0.9457 0.3777 -0.2447 0.0080  -0.0222 390 ASP D C   
15568 O O   . ASP D  390 ? 0.8851 0.9414 0.3918 -0.2256 0.0027  -0.0314 390 ASP D O   
15569 C CB  . ASP D  390 ? 1.0009 1.1018 0.4977 -0.2395 0.0311  -0.0389 390 ASP D CB  
15570 C CG  . ASP D  390 ? 1.0407 1.1768 0.5569 -0.2515 0.0461  -0.0454 390 ASP D CG  
15571 O OD1 . ASP D  390 ? 1.0646 1.1953 0.5693 -0.2714 0.0469  -0.0352 390 ASP D OD1 
15572 O OD2 . ASP D  390 ? 1.0412 1.2104 0.5848 -0.2410 0.0568  -0.0607 390 ASP D OD2 
15573 N N   . PRO D  391 ? 1.1058 1.1490 0.5786 -0.2644 0.0074  -0.0118 391 PRO D N   
15574 C CA  . PRO D  391 ? 1.0912 1.1238 0.5868 -0.2588 -0.0009 -0.0106 391 PRO D CA  
15575 C C   . PRO D  391 ? 1.0672 1.1379 0.6057 -0.2481 0.0096  -0.0262 391 PRO D C   
15576 O O   . PRO D  391 ? 1.0944 1.1592 0.6560 -0.2306 0.0012  -0.0312 391 PRO D O   
15577 C CB  . PRO D  391 ? 0.8692 0.8902 0.3468 -0.2847 0.0004  0.0026  391 PRO D CB  
15578 C CG  . PRO D  391 ? 0.8583 0.8640 0.2936 -0.2998 0.0010  0.0132  391 PRO D CG  
15579 C CD  . PRO D  391 ? 0.8889 0.9253 0.3349 -0.2892 0.0126  0.0007  391 PRO D CD  
15580 N N   . THR D  392 ? 0.7374 0.8468 0.2859 -0.2578 0.0274  -0.0340 392 THR D N   
15581 C CA  . THR D  392 ? 0.6975 0.8448 0.2864 -0.2477 0.0375  -0.0492 392 THR D CA  
15582 C C   . THR D  392 ? 0.6649 0.8157 0.2722 -0.2215 0.0335  -0.0615 392 THR D C   
15583 O O   . THR D  392 ? 0.6340 0.7876 0.2699 -0.2070 0.0287  -0.0678 392 THR D O   
15584 C CB  . THR D  392 ? 0.9114 1.1008 0.5043 -0.2609 0.0574  -0.0564 392 THR D CB  
15585 O OG1 . THR D  392 ? 0.9900 1.1735 0.5577 -0.2877 0.0611  -0.0430 392 THR D OG1 
15586 C CG2 . THR D  392 ? 0.8683 1.0960 0.5032 -0.2540 0.0668  -0.0697 392 THR D CG2 
15587 N N   . HIS D  393 ? 0.7058 0.8555 0.2953 -0.2165 0.0351  -0.0647 393 HIS D N   
15588 C CA  . HIS D  393 ? 0.7143 0.8638 0.3168 -0.1939 0.0302  -0.0753 393 HIS D CA  
15589 C C   . HIS D  393 ? 0.6696 0.7876 0.2762 -0.1806 0.0123  -0.0696 393 HIS D C   
15590 O O   . HIS D  393 ? 0.6265 0.7501 0.2591 -0.1637 0.0090  -0.0782 393 HIS D O   
15591 C CB  . HIS D  393 ? 0.9038 1.0505 0.4881 -0.1904 0.0322  -0.0767 393 HIS D CB  
15592 C CG  . HIS D  393 ? 0.9431 1.0851 0.5424 -0.1676 0.0255  -0.0854 393 HIS D CG  
15593 N ND1 . HIS D  393 ? 0.9457 1.1119 0.5740 -0.1542 0.0323  -0.1003 393 HIS D ND1 
15594 C CD2 . HIS D  393 ? 0.9753 1.0909 0.5652 -0.1562 0.0119  -0.0808 393 HIS D CD2 
15595 C CE1 . HIS D  393 ? 0.9505 1.1037 0.5852 -0.1371 0.0234  -0.1039 393 HIS D CE1 
15596 N NE2 . HIS D  393 ? 0.9791 1.1036 0.5916 -0.1380 0.0114  -0.0925 393 HIS D NE2 
15597 N N   . LEU D  394 ? 0.7736 0.8584 0.3538 -0.1880 0.0008  -0.0553 394 LEU D N   
15598 C CA  . LEU D  394 ? 0.7361 0.7915 0.3187 -0.1753 -0.0161 -0.0501 394 LEU D CA  
15599 C C   . LEU D  394 ? 0.7125 0.7746 0.3265 -0.1692 -0.0173 -0.0539 394 LEU D C   
15600 O O   . LEU D  394 ? 0.6997 0.7589 0.3327 -0.1516 -0.0244 -0.0594 394 LEU D O   
15601 C CB  . LEU D  394 ? 0.6903 0.7094 0.2392 -0.1862 -0.0277 -0.0339 394 LEU D CB  
15602 C CG  . LEU D  394 ? 0.7139 0.7191 0.2324 -0.1856 -0.0325 -0.0298 394 LEU D CG  
15603 C CD1 . LEU D  394 ? 0.7540 0.7221 0.2398 -0.1961 -0.0441 -0.0132 394 LEU D CD1 
15604 C CD2 . LEU D  394 ? 0.6884 0.6909 0.2226 -0.1622 -0.0411 -0.0367 394 LEU D CD2 
15605 N N   . ARG D  395 ? 0.6521 0.7242 0.2708 -0.1847 -0.0102 -0.0509 395 ARG D N   
15606 C CA  . ARG D  395 ? 0.6430 0.7222 0.2896 -0.1815 -0.0112 -0.0541 395 ARG D CA  
15607 C C   . ARG D  395 ? 0.5725 0.6808 0.2530 -0.1649 -0.0048 -0.0694 395 ARG D C   
15608 O O   . ARG D  395 ? 0.5485 0.6498 0.2468 -0.1490 -0.0131 -0.0730 395 ARG D O   
15609 C CB  . ARG D  395 ? 0.6287 0.7199 0.2737 -0.2037 -0.0025 -0.0492 395 ARG D CB  
15610 C CG  . ARG D  395 ? 0.6113 0.7090 0.2820 -0.2037 -0.0041 -0.0512 395 ARG D CG  
15611 C CD  . ARG D  395 ? 0.5919 0.7341 0.2905 -0.2064 0.0114  -0.0626 395 ARG D CD  
15612 N NE  . ARG D  395 ? 0.6166 0.7751 0.3057 -0.2306 0.0221  -0.0577 395 ARG D NE  
15613 C CZ  . ARG D  395 ? 0.6438 0.8432 0.3465 -0.2359 0.0382  -0.0667 395 ARG D CZ  
15614 N NH1 . ARG D  395 ? 0.6098 0.8332 0.3341 -0.2177 0.0440  -0.0810 395 ARG D NH1 
15615 N NH2 . ARG D  395 ? 0.6705 0.8868 0.3646 -0.2593 0.0483  -0.0618 395 ARG D NH2 
15616 N N   . ASP D  396 ? 0.5686 0.7087 0.2565 -0.1680 0.0095  -0.0784 396 ASP D N   
15617 C CA  . ASP D  396 ? 0.5603 0.7263 0.2785 -0.1523 0.0152  -0.0931 396 ASP D CA  
15618 C C   . ASP D  396 ? 0.5274 0.6795 0.2473 -0.1328 0.0062  -0.0975 396 ASP D C   
15619 O O   . ASP D  396 ? 0.4924 0.6523 0.2371 -0.1182 0.0044  -0.1059 396 ASP D O   
15620 C CB  . ASP D  396 ? 0.7464 0.9478 0.4697 -0.1580 0.0319  -0.1029 396 ASP D CB  
15621 C CG  . ASP D  396 ? 0.8493 1.0732 0.5814 -0.1750 0.0417  -0.1012 396 ASP D CG  
15622 O OD1 . ASP D  396 ? 0.9197 1.1353 0.6280 -0.1942 0.0435  -0.0905 396 ASP D OD1 
15623 O OD2 . ASP D  396 ? 0.8627 1.1120 0.6251 -0.1698 0.0468  -0.1101 396 ASP D OD2 
15624 N N   . ALA D  397 ? 0.5764 0.7076 0.2694 -0.1335 0.0000  -0.0913 397 ALA D N   
15625 C CA  . ALA D  397 ? 0.5653 0.6856 0.2580 -0.1173 -0.0083 -0.0951 397 ALA D CA  
15626 C C   . ALA D  397 ? 0.5150 0.6126 0.2143 -0.1074 -0.0225 -0.0897 397 ALA D C   
15627 O O   . ALA D  397 ? 0.5057 0.6010 0.2163 -0.0925 -0.0284 -0.0947 397 ALA D O   
15628 C CB  . ALA D  397 ? 0.5517 0.6604 0.2139 -0.1215 -0.0101 -0.0910 397 ALA D CB  
15629 N N   . MET D  398 ? 0.5282 0.6090 0.2199 -0.1159 -0.0281 -0.0796 398 MET D N   
15630 C CA  . MET D  398 ? 0.5182 0.5788 0.2169 -0.1059 -0.0409 -0.0756 398 MET D CA  
15631 C C   . MET D  398 ? 0.4876 0.5663 0.2189 -0.0979 -0.0374 -0.0843 398 MET D C   
15632 O O   . MET D  398 ? 0.4669 0.5409 0.2126 -0.0833 -0.0446 -0.0875 398 MET D O   
15633 C CB  . MET D  398 ? 0.5455 0.5806 0.2244 -0.1177 -0.0481 -0.0629 398 MET D CB  
15634 C CG  . MET D  398 ? 0.5394 0.5522 0.2236 -0.1077 -0.0614 -0.0591 398 MET D CG  
15635 S SD  . MET D  398 ? 0.6815 0.6691 0.3493 -0.0929 -0.0764 -0.0550 398 MET D SD  
15636 C CE  . MET D  398 ? 0.6566 0.6656 0.3543 -0.0737 -0.0750 -0.0676 398 MET D CE  
15637 N N   . SER D  399 ? 0.4859 0.5866 0.2287 -0.1077 -0.0262 -0.0880 399 SER D N   
15638 C CA  . SER D  399 ? 0.4584 0.5800 0.2323 -0.1002 -0.0220 -0.0972 399 SER D CA  
15639 C C   . SER D  399 ? 0.4373 0.5681 0.2234 -0.0840 -0.0215 -0.1072 399 SER D C   
15640 O O   . SER D  399 ? 0.4150 0.5463 0.2200 -0.0715 -0.0261 -0.1116 399 SER D O   
15641 C CB  . SER D  399 ? 0.4617 0.6112 0.2456 -0.1128 -0.0088 -0.1012 399 SER D CB  
15642 O OG  . SER D  399 ? 0.4362 0.6097 0.2503 -0.1040 -0.0040 -0.1119 399 SER D OG  
15643 N N   . ALA D  400 ? 0.4473 0.5833 0.2199 -0.0852 -0.0164 -0.1101 400 ALA D N   
15644 C CA  . ALA D  400 ? 0.4322 0.5769 0.2136 -0.0723 -0.0151 -0.1201 400 ALA D CA  
15645 C C   . ALA D  400 ? 0.4217 0.5475 0.2030 -0.0601 -0.0274 -0.1178 400 ALA D C   
15646 O O   . ALA D  400 ? 0.4003 0.5315 0.2005 -0.0485 -0.0292 -0.1244 400 ALA D O   
15647 C CB  . ALA D  400 ? 0.6845 0.8363 0.4481 -0.0774 -0.0079 -0.1232 400 ALA D CB  
15648 N N   . VAL D  401 ? 0.4481 0.5525 0.2079 -0.0627 -0.0360 -0.1084 401 VAL D N   
15649 C CA  . VAL D  401 ? 0.4493 0.5376 0.2086 -0.0514 -0.0481 -0.1057 401 VAL D CA  
15650 C C   . VAL D  401 ? 0.4086 0.4969 0.1900 -0.0430 -0.0521 -0.1071 401 VAL D C   
15651 O O   . VAL D  401 ? 0.3887 0.4835 0.1858 -0.0322 -0.0535 -0.1135 401 VAL D O   
15652 C CB  . VAL D  401 ? 0.4535 0.5181 0.1878 -0.0553 -0.0578 -0.0945 401 VAL D CB  
15653 C CG1 . VAL D  401 ? 0.4442 0.4970 0.1811 -0.0423 -0.0696 -0.0931 401 VAL D CG1 
15654 C CG2 . VAL D  401 ? 0.4758 0.5397 0.1868 -0.0631 -0.0546 -0.0929 401 VAL D CG2 
15655 N N   . VAL D  402 ? 0.4142 0.4953 0.1960 -0.0490 -0.0538 -0.1014 402 VAL D N   
15656 C CA  . VAL D  402 ? 0.3961 0.4763 0.1969 -0.0416 -0.0581 -0.1026 402 VAL D CA  
15657 C C   . VAL D  402 ? 0.4572 0.5583 0.2829 -0.0345 -0.0518 -0.1129 402 VAL D C   
15658 O O   . VAL D  402 ? 0.3546 0.4549 0.1926 -0.0231 -0.0566 -0.1161 402 VAL D O   
15659 C CB  . VAL D  402 ? 0.4178 0.4905 0.2163 -0.0516 -0.0588 -0.0966 402 VAL D CB  
15660 C CG1 . VAL D  402 ? 0.4033 0.4825 0.2247 -0.0456 -0.0599 -0.1006 402 VAL D CG1 
15661 C CG2 . VAL D  402 ? 0.4399 0.4846 0.2160 -0.0538 -0.0694 -0.0864 402 VAL D CG2 
15662 N N   . GLY D  403 ? 0.4792 0.5989 0.3112 -0.0412 -0.0413 -0.1181 403 GLY D N   
15663 C CA  . GLY D  403 ? 0.4838 0.6230 0.3383 -0.0343 -0.0356 -0.1281 403 GLY D CA  
15664 C C   . GLY D  403 ? 0.4958 0.6363 0.3545 -0.0230 -0.0370 -0.1347 403 GLY D C   
15665 O O   . GLY D  403 ? 0.5021 0.6461 0.3776 -0.0136 -0.0393 -0.1394 403 GLY D O   
15666 N N   . ASP D  404 ? 0.5066 0.6434 0.3489 -0.0246 -0.0363 -0.1348 404 ASP D N   
15667 C CA  . ASP D  404 ? 0.4833 0.6163 0.3320 -0.0155 -0.0364 -0.1370 404 ASP D CA  
15668 C C   . ASP D  404 ? 0.4800 0.5974 0.3334 -0.0076 -0.0458 -0.1308 404 ASP D C   
15669 O O   . ASP D  404 ? 0.4988 0.6162 0.3669 0.0002  -0.0466 -0.1329 404 ASP D O   
15670 C CB  . ASP D  404 ? 0.4757 0.6050 0.3062 -0.0200 -0.0337 -0.1359 404 ASP D CB  
15671 C CG  . ASP D  404 ? 0.5435 0.6891 0.3673 -0.0288 -0.0232 -0.1412 404 ASP D CG  
15672 O OD1 . ASP D  404 ? 0.5552 0.7185 0.3938 -0.0289 -0.0169 -0.1484 404 ASP D OD1 
15673 O OD2 . ASP D  404 ? 0.5801 0.7218 0.3840 -0.0358 -0.0211 -0.1382 404 ASP D OD2 
15674 N N   . HIS D  405 ? 0.3941 0.4985 0.2341 -0.0101 -0.0528 -0.1231 405 HIS D N   
15675 C CA  . HIS D  405 ? 0.3580 0.4499 0.2018 -0.0027 -0.0608 -0.1173 405 HIS D CA  
15676 C C   . HIS D  405 ? 0.3341 0.4276 0.1963 0.0036  -0.0629 -0.1178 405 HIS D C   
15677 O O   . HIS D  405 ? 0.3082 0.3997 0.1815 0.0103  -0.0648 -0.1166 405 HIS D O   
15678 C CB  . HIS D  405 ? 0.3814 0.4591 0.2063 -0.0054 -0.0684 -0.1097 405 HIS D CB  
15679 C CG  . HIS D  405 ? 0.3956 0.4640 0.2263 0.0022  -0.0760 -0.1043 405 HIS D CG  
15680 N ND1 . HIS D  405 ? 0.4103 0.4814 0.2529 0.0080  -0.0759 -0.1044 405 HIS D ND1 
15681 C CD2 . HIS D  405 ? 0.4251 0.4831 0.2516 0.0049  -0.0834 -0.0991 405 HIS D CD2 
15682 C CE1 . HIS D  405 ? 0.4345 0.5002 0.2811 0.0135  -0.0820 -0.0996 405 HIS D CE1 
15683 N NE2 . HIS D  405 ? 0.4428 0.5002 0.2803 0.0126  -0.0865 -0.0965 405 HIS D NE2 
15684 N N   . ASN D  406 ? 0.3417 0.4390 0.2061 0.0004  -0.0626 -0.1192 406 ASN D N   
15685 C CA  . ASN D  406 ? 0.3055 0.4038 0.1862 0.0060  -0.0649 -0.1197 406 ASN D CA  
15686 C C   . ASN D  406 ? 0.3199 0.4318 0.2195 0.0096  -0.0596 -0.1268 406 ASN D C   
15687 O O   . ASN D  406 ? 0.2832 0.3936 0.1958 0.0164  -0.0619 -0.1260 406 ASN D O   
15688 C CB  . ASN D  406 ? 0.3134 0.4066 0.1873 0.0013  -0.0692 -0.1175 406 ASN D CB  
15689 C CG  . ASN D  406 ? 0.4479 0.5233 0.3055 0.0019  -0.0772 -0.1100 406 ASN D CG  
15690 O OD1 . ASN D  406 ? 0.4770 0.5450 0.3392 0.0098  -0.0811 -0.1061 406 ASN D OD1 
15691 N ND2 . ASN D  406 ? 0.4198 0.4877 0.2592 -0.0069 -0.0787 -0.1065 406 ASN D ND2 
15692 N N   . VAL D  407 ? 0.2955 0.4213 0.1962 0.0053  -0.0526 -0.1338 407 VAL D N   
15693 C CA  . VAL D  407 ? 0.3926 0.5321 0.3112 0.0100  -0.0484 -0.1415 407 VAL D CA  
15694 C C   . VAL D  407 ? 0.3658 0.5103 0.2862 0.0130  -0.0432 -0.1470 407 VAL D C   
15695 O O   . VAL D  407 ? 0.3608 0.4998 0.2889 0.0201  -0.0453 -0.1468 407 VAL D O   
15696 C CB  . VAL D  407 ? 0.2864 0.4426 0.2105 0.0040  -0.0444 -0.1475 407 VAL D CB  
15697 C CG1 . VAL D  407 ? 0.2757 0.4462 0.2193 0.0109  -0.0413 -0.1562 407 VAL D CG1 
15698 C CG2 . VAL D  407 ? 0.2871 0.4347 0.2107 0.0000  -0.0496 -0.1402 407 VAL D CG2 
15699 N N   . VAL D  408 ? 0.3949 0.5493 0.3070 0.0071  -0.0365 -0.1516 408 VAL D N   
15700 C CA  . VAL D  408 ? 0.4128 0.5742 0.3278 0.0104  -0.0307 -0.1588 408 VAL D CA  
15701 C C   . VAL D  408 ? 0.4111 0.5578 0.3233 0.0156  -0.0345 -0.1558 408 VAL D C   
15702 O O   . VAL D  408 ? 0.4187 0.5653 0.3413 0.0225  -0.0347 -0.1602 408 VAL D O   
15703 C CB  . VAL D  408 ? 0.3181 0.4903 0.2201 0.0021  -0.0225 -0.1625 408 VAL D CB  
15704 C CG1 . VAL D  408 ? 0.3243 0.4987 0.2268 0.0068  -0.0179 -0.1688 408 VAL D CG1 
15705 C CG2 . VAL D  408 ? 0.3190 0.5124 0.2271 -0.0037 -0.0162 -0.1682 408 VAL D CG2 
15706 N N   . CYS D  409 ? 0.3350 0.4691 0.2329 0.0120  -0.0382 -0.1484 409 CYS D N   
15707 C CA  . CYS D  409 ? 0.3289 0.4516 0.2237 0.0149  -0.0417 -0.1460 409 CYS D CA  
15708 C C   . CYS D  409 ? 0.3353 0.4517 0.2425 0.0212  -0.0471 -0.1432 409 CYS D C   
15709 O O   . CYS D  409 ? 0.2946 0.4074 0.2055 0.0245  -0.0477 -0.1458 409 CYS D O   
15710 C CB  . CYS D  409 ? 0.4076 0.5209 0.2844 0.0096  -0.0446 -0.1395 409 CYS D CB  
15711 S SG  . CYS D  409 ? 0.5104 0.6289 0.3703 0.0028  -0.0377 -0.1439 409 CYS D SG  
15712 N N   . PRO D  410 ? 0.4171 0.5316 0.3295 0.0223  -0.0510 -0.1379 410 PRO D N   
15713 C CA  . PRO D  410 ? 0.3961 0.5077 0.3213 0.0282  -0.0546 -0.1365 410 PRO D CA  
15714 C C   . PRO D  410 ? 0.3738 0.4915 0.3113 0.0332  -0.0523 -0.1441 410 PRO D C   
15715 O O   . PRO D  410 ? 0.3806 0.4927 0.3226 0.0369  -0.0549 -0.1442 410 PRO D O   
15716 C CB  . PRO D  410 ? 0.3596 0.4706 0.2875 0.0283  -0.0576 -0.1317 410 PRO D CB  
15717 C CG  . PRO D  410 ? 0.3736 0.4802 0.2866 0.0229  -0.0587 -0.1273 410 PRO D CG  
15718 C CD  . PRO D  410 ? 0.3878 0.4991 0.2916 0.0182  -0.0536 -0.1321 410 PRO D CD  
15719 N N   . VAL D  411 ? 0.3497 0.4790 0.2921 0.0333  -0.0481 -0.1505 411 VAL D N   
15720 C CA  . VAL D  411 ? 0.2679 0.4045 0.2227 0.0395  -0.0465 -0.1587 411 VAL D CA  
15721 C C   . VAL D  411 ? 0.2774 0.4094 0.2285 0.0418  -0.0450 -0.1633 411 VAL D C   
15722 O O   . VAL D  411 ? 0.2770 0.4039 0.2346 0.0477  -0.0477 -0.1662 411 VAL D O   
15723 C CB  . VAL D  411 ? 0.2760 0.4302 0.2365 0.0384  -0.0411 -0.1661 411 VAL D CB  
15724 C CG1 . VAL D  411 ? 0.2701 0.4329 0.2434 0.0463  -0.0394 -0.1758 411 VAL D CG1 
15725 C CG2 . VAL D  411 ? 0.2617 0.4198 0.2266 0.0359  -0.0436 -0.1627 411 VAL D CG2 
15726 N N   . ALA D  412 ? 0.3246 0.4567 0.2634 0.0367  -0.0413 -0.1639 412 ALA D N   
15727 C CA  . ALA D  412 ? 0.3625 0.4886 0.2947 0.0377  -0.0400 -0.1681 412 ALA D CA  
15728 C C   . ALA D  412 ? 0.3928 0.5034 0.3225 0.0385  -0.0463 -0.1633 412 ALA D C   
15729 O O   . ALA D  412 ? 0.4372 0.5411 0.3689 0.0427  -0.0480 -0.1678 412 ALA D O   
15730 C CB  . ALA D  412 ? 0.3125 0.4403 0.2297 0.0310  -0.0357 -0.1677 412 ALA D CB  
15731 N N   . GLN D  413 ? 0.2937 0.3990 0.2186 0.0343  -0.0500 -0.1545 413 GLN D N   
15732 C CA  . GLN D  413 ? 0.2919 0.3865 0.2154 0.0338  -0.0554 -0.1497 413 GLN D CA  
15733 C C   . GLN D  413 ? 0.2886 0.3802 0.2232 0.0392  -0.0587 -0.1509 413 GLN D C   
15734 O O   . GLN D  413 ? 0.3124 0.3947 0.2451 0.0398  -0.0618 -0.1523 413 GLN D O   
15735 C CB  . GLN D  413 ? 0.4396 0.5331 0.3595 0.0300  -0.0585 -0.1407 413 GLN D CB  
15736 C CG  . GLN D  413 ? 0.5649 0.6512 0.4826 0.0281  -0.0632 -0.1366 413 GLN D CG  
15737 C CD  . GLN D  413 ? 0.6982 0.7859 0.6143 0.0260  -0.0662 -0.1286 413 GLN D CD  
15738 O OE1 . GLN D  413 ? 0.7353 0.8260 0.6580 0.0286  -0.0670 -0.1250 413 GLN D OE1 
15739 N NE2 . GLN D  413 ? 0.7421 0.8275 0.6491 0.0217  -0.0683 -0.1260 413 GLN D NE2 
15740 N N   . LEU D  414 ? 0.3433 0.4415 0.2879 0.0427  -0.0585 -0.1505 414 LEU D N   
15741 C CA  . LEU D  414 ? 0.3328 0.4280 0.2870 0.0483  -0.0621 -0.1516 414 LEU D CA  
15742 C C   . LEU D  414 ? 0.3815 0.4736 0.3381 0.0536  -0.0621 -0.1604 414 LEU D C   
15743 O O   . LEU D  414 ? 0.4107 0.4917 0.3667 0.0558  -0.0666 -0.1608 414 LEU D O   
15744 C CB  . LEU D  414 ? 0.2943 0.3981 0.2583 0.0511  -0.0621 -0.1506 414 LEU D CB  
15745 C CG  . LEU D  414 ? 0.3045 0.4042 0.2769 0.0566  -0.0667 -0.1506 414 LEU D CG  
15746 C CD1 . LEU D  414 ? 0.2498 0.3412 0.2185 0.0539  -0.0706 -0.1426 414 LEU D CD1 
15747 C CD2 . LEU D  414 ? 0.2458 0.3554 0.2282 0.0599  -0.0664 -0.1523 414 LEU D CD2 
15748 N N   . ALA D  415 ? 0.4402 0.5418 0.3988 0.0558  -0.0571 -0.1676 415 ALA D N   
15749 C CA  . ALA D  415 ? 0.4486 0.5483 0.4102 0.0626  -0.0568 -0.1768 415 ALA D CA  
15750 C C   . ALA D  415 ? 0.4272 0.5107 0.3775 0.0606  -0.0595 -0.1772 415 ALA D C   
15751 O O   . ALA D  415 ? 0.4692 0.5408 0.4200 0.0652  -0.0642 -0.1799 415 ALA D O   
15752 C CB  . ALA D  415 ? 0.3014 0.4164 0.2654 0.0640  -0.0497 -0.1845 415 ALA D CB  
15753 N N   . GLY D  416 ? 0.3240 0.4061 0.2632 0.0534  -0.0572 -0.1741 416 GLY D N   
15754 C CA  . GLY D  416 ? 0.3283 0.3960 0.2556 0.0498  -0.0598 -0.1745 416 GLY D CA  
15755 C C   . GLY D  416 ? 0.3333 0.3879 0.2596 0.0482  -0.0669 -0.1697 416 GLY D C   
15756 O O   . GLY D  416 ? 0.3619 0.4026 0.2835 0.0496  -0.0706 -0.1737 416 GLY D O   
15757 N N   . ARG D  417 ? 0.3410 0.3996 0.2710 0.0449  -0.0688 -0.1615 417 ARG D N   
15758 C CA  . ARG D  417 ? 0.4105 0.4594 0.3390 0.0419  -0.0748 -0.1566 417 ARG D CA  
15759 C C   . ARG D  417 ? 0.4234 0.4641 0.3575 0.0485  -0.0789 -0.1600 417 ARG D C   
15760 O O   . ARG D  417 ? 0.4416 0.4675 0.3694 0.0470  -0.0841 -0.1612 417 ARG D O   
15761 C CB  . ARG D  417 ? 0.6131 0.6702 0.5448 0.0380  -0.0752 -0.1475 417 ARG D CB  
15762 C CG  . ARG D  417 ? 0.7363 0.7999 0.6621 0.0325  -0.0727 -0.1436 417 ARG D CG  
15763 C CD  . ARG D  417 ? 0.8688 0.9275 0.7869 0.0253  -0.0765 -0.1398 417 ARG D CD  
15764 N NE  . ARG D  417 ? 0.9909 1.0366 0.9039 0.0237  -0.0802 -0.1441 417 ARG D NE  
15765 C CZ  . ARG D  417 ? 1.0575 1.0972 0.9634 0.0163  -0.0846 -0.1420 417 ARG D CZ  
15766 N NH1 . ARG D  417 ? 1.0712 1.1193 0.9761 0.0108  -0.0855 -0.1358 417 ARG D NH1 
15767 N NH2 . ARG D  417 ? 1.0694 1.0947 0.9693 0.0144  -0.0885 -0.1464 417 ARG D NH2 
15768 N N   . LEU D  418 ? 0.4597 0.5093 0.4046 0.0554  -0.0774 -0.1618 418 LEU D N   
15769 C CA  . LEU D  418 ? 0.4823 0.5247 0.4328 0.0628  -0.0821 -0.1651 418 LEU D CA  
15770 C C   . LEU D  418 ? 0.5650 0.5944 0.5107 0.0677  -0.0842 -0.1735 418 LEU D C   
15771 O O   . LEU D  418 ? 0.6369 0.6504 0.5796 0.0707  -0.0908 -0.1749 418 LEU D O   
15772 C CB  . LEU D  418 ? 0.2989 0.3556 0.2626 0.0696  -0.0800 -0.1669 418 LEU D CB  
15773 C CG  . LEU D  418 ? 0.2809 0.3482 0.2498 0.0665  -0.0789 -0.1594 418 LEU D CG  
15774 C CD1 . LEU D  418 ? 0.2730 0.3506 0.2543 0.0735  -0.0791 -0.1625 418 LEU D CD1 
15775 C CD2 . LEU D  418 ? 0.2789 0.3373 0.2428 0.0618  -0.0834 -0.1517 418 LEU D CD2 
15776 N N   . ALA D  419 ? 0.4877 0.5227 0.4312 0.0685  -0.0788 -0.1792 419 ALA D N   
15777 C CA  . ALA D  419 ? 0.4778 0.5009 0.4159 0.0736  -0.0801 -0.1877 419 ALA D CA  
15778 C C   . ALA D  419 ? 0.5080 0.5105 0.4319 0.0665  -0.0853 -0.1856 419 ALA D C   
15779 O O   . ALA D  419 ? 0.5554 0.5393 0.4747 0.0701  -0.0916 -0.1889 419 ALA D O   
15780 C CB  . ALA D  419 ? 0.5743 0.6093 0.5116 0.0745  -0.0724 -0.1938 419 ALA D CB  
15781 N N   . ALA D  420 ? 0.6006 0.6061 0.5173 0.0562  -0.0834 -0.1801 420 ALA D N   
15782 C CA  . ALA D  420 ? 0.6672 0.6568 0.5709 0.0474  -0.0882 -0.1779 420 ALA D CA  
15783 C C   . ALA D  420 ? 0.6248 0.6014 0.5271 0.0447  -0.0960 -0.1735 420 ALA D C   
15784 O O   . ALA D  420 ? 0.6391 0.5976 0.5305 0.0392  -0.1017 -0.1741 420 ALA D O   
15785 C CB  . ALA D  420 ? 0.8185 0.8182 0.7174 0.0375  -0.0852 -0.1720 420 ALA D CB  
15786 N N   . GLN D  421 ? 0.4341 0.4195 0.3464 0.0479  -0.0965 -0.1689 421 GLN D N   
15787 C CA  . GLN D  421 ? 0.4417 0.4159 0.3523 0.0458  -0.1036 -0.1645 421 GLN D CA  
15788 C C   . GLN D  421 ? 0.4388 0.3991 0.3516 0.0567  -0.1086 -0.1702 421 GLN D C   
15789 O O   . GLN D  421 ? 0.3966 0.3477 0.3089 0.0575  -0.1148 -0.1669 421 GLN D O   
15790 C CB  . GLN D  421 ? 0.6631 0.6530 0.5812 0.0426  -0.1020 -0.1562 421 GLN D CB  
15791 C CG  . GLN D  421 ? 0.6961 0.6866 0.6073 0.0303  -0.1043 -0.1491 421 GLN D CG  
15792 C CD  . GLN D  421 ? 0.7143 0.7129 0.6213 0.0234  -0.1004 -0.1482 421 GLN D CD  
15793 O OE1 . GLN D  421 ? 0.7024 0.7123 0.6136 0.0270  -0.0945 -0.1497 421 GLN D OE1 
15794 N NE2 . GLN D  421 ? 0.7374 0.7304 0.6354 0.0128  -0.1044 -0.1458 421 GLN D NE2 
15795 N N   . GLY D  422 ? 0.6968 0.6574 0.6123 0.0655  -0.1057 -0.1786 422 GLY D N   
15796 C CA  . GLY D  422 ? 0.7353 0.6808 0.6513 0.0768  -0.1111 -0.1853 422 GLY D CA  
15797 C C   . GLY D  422 ? 0.7105 0.6661 0.6402 0.0871  -0.1121 -0.1859 422 GLY D C   
15798 O O   . GLY D  422 ? 0.7391 0.6792 0.6676 0.0934  -0.1201 -0.1866 422 GLY D O   
15799 N N   . ALA D  423 ? 0.5507 0.5314 0.4924 0.0885  -0.1047 -0.1855 423 ALA D N   
15800 C CA  . ALA D  423 ? 0.4948 0.4880 0.4504 0.0976  -0.1052 -0.1870 423 ALA D CA  
15801 C C   . ALA D  423 ? 0.5011 0.5080 0.4659 0.1067  -0.1001 -0.1964 423 ALA D C   
15802 O O   . ALA D  423 ? 0.5420 0.5566 0.5039 0.1031  -0.0932 -0.1991 423 ALA D O   
15803 C CB  . ALA D  423 ? 0.3749 0.3864 0.3374 0.0917  -0.1011 -0.1798 423 ALA D CB  
15804 N N   . ARG D  424 ? 0.3925 0.4026 0.3676 0.1184  -0.1039 -0.2015 424 ARG D N   
15805 C CA  . ARG D  424 ? 0.4601 0.4889 0.4466 0.1268  -0.0985 -0.2106 424 ARG D CA  
15806 C C   . ARG D  424 ? 0.4359 0.4924 0.4332 0.1220  -0.0905 -0.2086 424 ARG D C   
15807 O O   . ARG D  424 ? 0.4113 0.4729 0.4134 0.1193  -0.0924 -0.2028 424 ARG D O   
15808 C CB  . ARG D  424 ? 0.7726 0.7984 0.7677 0.1409  -0.1055 -0.2168 424 ARG D CB  
15809 C CG  . ARG D  424 ? 0.8746 0.9104 0.8754 0.1501  -0.1016 -0.2275 424 ARG D CG  
15810 C CD  . ARG D  424 ? 0.9794 1.0177 0.9916 0.1643  -0.1085 -0.2332 424 ARG D CD  
15811 N NE  . ARG D  424 ? 1.0940 1.1024 1.0968 0.1685  -0.1209 -0.2295 424 ARG D NE  
15812 C CZ  . ARG D  424 ? 1.2080 1.1909 1.1994 0.1743  -0.1274 -0.2329 424 ARG D CZ  
15813 N NH1 . ARG D  424 ? 1.2534 1.2380 1.2420 0.1774  -0.1224 -0.2405 424 ARG D NH1 
15814 N NH2 . ARG D  424 ? 1.2314 1.1858 1.2128 0.1768  -0.1392 -0.2286 424 ARG D NH2 
15815 N N   . VAL D  425 ? 0.3841 0.4567 0.3832 0.1201  -0.0816 -0.2133 425 VAL D N   
15816 C CA  . VAL D  425 ? 0.3303 0.4247 0.3344 0.1126  -0.0738 -0.2106 425 VAL D CA  
15817 C C   . VAL D  425 ? 0.3333 0.4497 0.3463 0.1169  -0.0664 -0.2198 425 VAL D C   
15818 O O   . VAL D  425 ? 0.3493 0.4622 0.3570 0.1199  -0.0638 -0.2258 425 VAL D O   
15819 C CB  . VAL D  425 ? 0.3822 0.4697 0.3719 0.1005  -0.0699 -0.2039 425 VAL D CB  
15820 C CG1 . VAL D  425 ? 0.3671 0.4744 0.3594 0.0931  -0.0624 -0.2012 425 VAL D CG1 
15821 C CG2 . VAL D  425 ? 0.3819 0.4504 0.3630 0.0951  -0.0765 -0.1949 425 VAL D CG2 
15822 N N   . TYR D  426 ? 0.5073 0.6468 0.5334 0.1168  -0.0628 -0.2212 426 TYR D N   
15823 C CA  . TYR D  426 ? 0.4917 0.6564 0.5258 0.1177  -0.0540 -0.2291 426 TYR D CA  
15824 C C   . TYR D  426 ? 0.4827 0.6625 0.5146 0.1059  -0.0465 -0.2248 426 TYR D C   
15825 O O   . TYR D  426 ? 0.4813 0.6584 0.5129 0.1006  -0.0494 -0.2175 426 TYR D O   
15826 C CB  . TYR D  426 ? 0.3495 0.5316 0.4020 0.1279  -0.0560 -0.2363 426 TYR D CB  
15827 C CG  . TYR D  426 ? 0.3460 0.5128 0.3999 0.1405  -0.0642 -0.2408 426 TYR D CG  
15828 C CD1 . TYR D  426 ? 0.3544 0.5013 0.4070 0.1448  -0.0749 -0.2361 426 TYR D CD1 
15829 C CD2 . TYR D  426 ? 0.3755 0.5466 0.4305 0.1481  -0.0614 -0.2499 426 TYR D CD2 
15830 C CE1 . TYR D  426 ? 0.3938 0.5243 0.4456 0.1560  -0.0832 -0.2398 426 TYR D CE1 
15831 C CE2 . TYR D  426 ? 0.4106 0.5653 0.4653 0.1602  -0.0697 -0.2541 426 TYR D CE2 
15832 C CZ  . TYR D  426 ? 0.4209 0.5546 0.4735 0.1639  -0.0809 -0.2488 426 TYR D CZ  
15833 O OH  . TYR D  426 ? 0.4476 0.5625 0.4979 0.1756  -0.0901 -0.2525 426 TYR D OH  
15834 N N   . ALA D  427 ? 0.3483 0.5430 0.3773 0.1016  -0.0373 -0.2291 427 ALA D N   
15835 C CA  . ALA D  427 ? 0.3419 0.5474 0.3649 0.0895  -0.0308 -0.2246 427 ALA D CA  
15836 C C   . ALA D  427 ? 0.3536 0.5895 0.3859 0.0877  -0.0213 -0.2322 427 ALA D C   
15837 O O   . ALA D  427 ? 0.3178 0.5639 0.3531 0.0928  -0.0166 -0.2403 427 ALA D O   
15838 C CB  . ALA D  427 ? 0.3114 0.5010 0.3150 0.0818  -0.0290 -0.2192 427 ALA D CB  
15839 N N   . TYR D  428 ? 0.4281 0.6789 0.4645 0.0801  -0.0185 -0.2299 428 TYR D N   
15840 C CA  . TYR D  428 ? 0.4347 0.7171 0.4801 0.0759  -0.0088 -0.2366 428 TYR D CA  
15841 C C   . TYR D  428 ? 0.4327 0.7203 0.4635 0.0607  -0.0020 -0.2316 428 TYR D C   
15842 O O   . TYR D  428 ? 0.4239 0.6937 0.4424 0.0541  -0.0068 -0.2225 428 TYR D O   
15843 C CB  . TYR D  428 ? 0.4780 0.7798 0.5444 0.0804  -0.0109 -0.2409 428 TYR D CB  
15844 C CG  . TYR D  428 ? 0.4188 0.7154 0.4833 0.0734  -0.0154 -0.2342 428 TYR D CG  
15845 C CD1 . TYR D  428 ? 0.4115 0.7164 0.4704 0.0579  -0.0102 -0.2264 428 TYR D CD1 
15846 C CD2 . TYR D  428 ? 0.3523 0.6310 0.4209 0.0798  -0.0263 -0.2297 428 TYR D CD2 
15847 C CE1 . TYR D  428 ? 0.3940 0.6881 0.4509 0.0501  -0.0161 -0.2153 428 TYR D CE1 
15848 C CE2 . TYR D  428 ? 0.3364 0.6071 0.4038 0.0719  -0.0314 -0.2188 428 TYR D CE2 
15849 C CZ  . TYR D  428 ? 0.3586 0.6365 0.4202 0.0574  -0.0265 -0.2119 428 TYR D CZ  
15850 O OH  . TYR D  428 ? 0.3276 0.5953 0.3860 0.0498  -0.0319 -0.2016 428 TYR D OH  
15851 N N   . ILE D  429 ? 0.4588 0.7710 0.4905 0.0549  0.0088  -0.2370 429 ILE D N   
15852 C CA  . ILE D  429 ? 0.4996 0.8213 0.5188 0.0392  0.0155  -0.2327 429 ILE D CA  
15853 C C   . ILE D  429 ? 0.5254 0.8806 0.5627 0.0342  0.0226  -0.2364 429 ILE D C   
15854 O O   . ILE D  429 ? 0.5683 0.9493 0.6174 0.0393  0.0304  -0.2471 429 ILE D O   
15855 C CB  . ILE D  429 ? 0.5213 0.8359 0.5192 0.0315  0.0214  -0.2298 429 ILE D CB  
15856 C CG1 . ILE D  429 ? 0.5039 0.8108 0.4819 0.0160  0.0219  -0.2203 429 ILE D CG1 
15857 C CG2 . ILE D  429 ? 0.5347 0.8753 0.5377 0.0313  0.0327  -0.2383 429 ILE D CG2 
15858 C CD1 . ILE D  429 ? 0.5094 0.8078 0.4658 0.0088  0.0264  -0.2166 429 ILE D CD1 
15859 N N   . PHE D  430 ? 0.5494 0.9028 0.5907 0.0243  0.0187  -0.2260 430 PHE D N   
15860 C CA  . PHE D  430 ? 0.5408 0.9231 0.6018 0.0187  0.0228  -0.2273 430 PHE D CA  
15861 C C   . PHE D  430 ? 0.5969 0.9947 0.6476 0.0002  0.0331  -0.2228 430 PHE D C   
15862 O O   . PHE D  430 ? 0.6429 1.0225 0.6767 -0.0129 0.0304  -0.2108 430 PHE D O   
15863 C CB  . PHE D  430 ? 0.3649 0.7348 0.4337 0.0169  0.0124  -0.2185 430 PHE D CB  
15864 C CG  . PHE D  430 ? 0.3298 0.7284 0.4210 0.0122  0.0143  -0.2202 430 PHE D CG  
15865 C CD1 . PHE D  430 ? 0.2798 0.6962 0.3950 0.0262  0.0118  -0.2298 430 PHE D CD1 
15866 C CD2 . PHE D  430 ? 0.3331 0.7397 0.4209 -0.0064 0.0176  -0.2119 430 PHE D CD2 
15867 C CE1 . PHE D  430 ? 0.2631 0.7075 0.3998 0.0218  0.0127  -0.2315 430 PHE D CE1 
15868 C CE2 . PHE D  430 ? 0.3095 0.7431 0.4181 -0.0122 0.0188  -0.2134 430 PHE D CE2 
15869 C CZ  . PHE D  430 ? 0.2855 0.7394 0.4194 0.0021  0.0165  -0.2234 430 PHE D CZ  
15870 N N   . GLU D  431 ? 0.5168 0.9478 0.5767 -0.0004 0.0447  -0.2327 431 GLU D N   
15871 C CA  . GLU D  431 ? 0.5046 0.9532 0.5530 -0.0184 0.0562  -0.2296 431 GLU D CA  
15872 C C   . GLU D  431 ? 0.4743 0.9548 0.5382 -0.0331 0.0624  -0.2274 431 GLU D C   
15873 O O   . GLU D  431 ? 0.4939 0.9880 0.5464 -0.0500 0.0721  -0.2237 431 GLU D O   
15874 C CB  . GLU D  431 ? 0.5395 1.0020 0.5799 -0.0129 0.0668  -0.2409 431 GLU D CB  
15875 C CG  . GLU D  431 ? 0.5720 1.0010 0.5904 -0.0051 0.0614  -0.2403 431 GLU D CG  
15876 C CD  . GLU D  431 ? 0.5972 1.0311 0.6067 -0.0018 0.0688  -0.2465 431 GLU D CD  
15877 O OE1 . GLU D  431 ? 0.5989 1.0582 0.6258 0.0046  0.0745  -0.2552 431 GLU D OE1 
15878 O OE2 . GLU D  431 ? 0.5999 1.0096 0.5855 -0.0055 0.0672  -0.2408 431 GLU D OE2 
15879 N N   . HIS D  432 ? 0.3701 0.8630 0.4589 -0.0277 0.0569  -0.2295 432 HIS D N   
15880 C CA  . HIS D  432 ? 0.3241 0.8511 0.4298 -0.0416 0.0628  -0.2288 432 HIS D CA  
15881 C C   . HIS D  432 ? 0.3171 0.8261 0.4148 -0.0595 0.0558  -0.2138 432 HIS D C   
15882 O O   . HIS D  432 ? 0.3054 0.7945 0.4088 -0.0539 0.0437  -0.2094 432 HIS D O   
15883 C CB  . HIS D  432 ? 0.3301 0.8878 0.4694 -0.0273 0.0615  -0.2406 432 HIS D CB  
15884 C CG  . HIS D  432 ? 0.3618 0.9544 0.5207 -0.0419 0.0655  -0.2392 432 HIS D CG  
15885 N ND1 . HIS D  432 ? 0.3719 1.0063 0.5384 -0.0530 0.0799  -0.2447 432 HIS D ND1 
15886 C CD2 . HIS D  432 ? 0.3683 0.9605 0.5399 -0.0485 0.0568  -0.2329 432 HIS D CD2 
15887 C CE1 . HIS D  432 ? 0.3587 1.0178 0.5429 -0.0664 0.0799  -0.2416 432 HIS D CE1 
15888 N NE2 . HIS D  432 ? 0.3565 0.9898 0.5438 -0.0638 0.0656  -0.2345 432 HIS D NE2 
15889 N N   . ARG D  433 ? 0.3527 0.8679 0.4358 -0.0812 0.0634  -0.2061 433 ARG D N   
15890 C CA  . ARG D  433 ? 0.3831 0.8854 0.4597 -0.1001 0.0577  -0.1930 433 ARG D CA  
15891 C C   . ARG D  433 ? 0.4372 0.9760 0.5433 -0.1057 0.0592  -0.1971 433 ARG D C   
15892 O O   . ARG D  433 ? 0.4657 1.0466 0.5864 -0.1107 0.0711  -0.2049 433 ARG D O   
15893 C CB  . ARG D  433 ? 0.4371 0.9321 0.4862 -0.1221 0.0648  -0.1830 433 ARG D CB  
15894 C CG  . ARG D  433 ? 0.4836 0.9673 0.5244 -0.1445 0.0601  -0.1697 433 ARG D CG  
15895 C CD  . ARG D  433 ? 0.5482 1.0301 0.5626 -0.1671 0.0688  -0.1609 433 ARG D CD  
15896 N NE  . ARG D  433 ? 0.5921 1.0616 0.5963 -0.1902 0.0643  -0.1480 433 ARG D NE  
15897 C CZ  . ARG D  433 ? 0.6113 1.0366 0.5874 -0.1983 0.0547  -0.1347 433 ARG D CZ  
15898 N NH1 . ARG D  433 ? 0.5917 0.9840 0.5485 -0.1852 0.0489  -0.1327 433 ARG D NH1 
15899 N NH2 . ARG D  433 ? 0.6374 1.0512 0.6043 -0.2194 0.0503  -0.1238 433 ARG D NH2 
15900 N N   . ALA D  434 ? 0.5233 1.0478 0.6384 -0.1045 0.0470  -0.1925 434 ALA D N   
15901 C CA  . ALA D  434 ? 0.5115 1.0690 0.6546 -0.1098 0.0465  -0.1960 434 ALA D CA  
15902 C C   . ALA D  434 ? 0.5171 1.0955 0.6565 -0.1377 0.0547  -0.1894 434 ALA D C   
15903 O O   . ALA D  434 ? 0.5390 1.0897 0.6515 -0.1549 0.0534  -0.1770 434 ALA D O   
15904 C CB  . ALA D  434 ? 0.4409 0.9744 0.5902 -0.1037 0.0310  -0.1917 434 ALA D CB  
15905 N N   . SER D  435 ? 0.3437 0.9715 0.5103 -0.1420 0.0627  -0.1978 435 SER D N   
15906 C CA  . SER D  435 ? 0.3749 1.0295 0.5419 -0.1696 0.0714  -0.1925 435 SER D CA  
15907 C C   . SER D  435 ? 0.4207 1.0488 0.5786 -0.1879 0.0600  -0.1793 435 SER D C   
15908 O O   . SER D  435 ? 0.4246 1.0480 0.5652 -0.2134 0.0636  -0.1689 435 SER D O   
15909 C CB  . SER D  435 ? 0.5254 1.2408 0.7288 -0.1678 0.0801  -0.2052 435 SER D CB  
15910 O OG  . SER D  435 ? 0.5235 1.2462 0.7522 -0.1609 0.0686  -0.2079 435 SER D OG  
15911 N N   . THR D  436 ? 0.6539 1.2631 0.8221 -0.1744 0.0459  -0.1798 436 THR D N   
15912 C CA  . THR D  436 ? 0.7104 1.2963 0.8738 -0.1880 0.0337  -0.1699 436 THR D CA  
15913 C C   . THR D  436 ? 0.7386 1.2665 0.8668 -0.1904 0.0247  -0.1577 436 THR D C   
15914 O O   . THR D  436 ? 0.7803 1.2807 0.9001 -0.1986 0.0131  -0.1497 436 THR D O   
15915 C CB  . THR D  436 ? 0.7460 1.3352 0.9338 -0.1706 0.0219  -0.1763 436 THR D CB  
15916 O OG1 . THR D  436 ? 0.7368 1.2935 0.9159 -0.1464 0.0147  -0.1784 436 THR D OG1 
15917 C CG2 . THR D  436 ? 0.7455 1.3919 0.9703 -0.1635 0.0289  -0.1898 436 THR D CG2 
15918 N N   . LEU D  437 ? 0.5646 1.0742 0.6727 -0.1821 0.0294  -0.1570 437 LEU D N   
15919 C CA  . LEU D  437 ? 0.5387 0.9956 0.6151 -0.1811 0.0206  -0.1467 437 LEU D CA  
15920 C C   . LEU D  437 ? 0.5086 0.9447 0.5608 -0.2080 0.0188  -0.1331 437 LEU D C   
15921 O O   . LEU D  437 ? 0.4950 0.9582 0.5501 -0.2290 0.0277  -0.1313 437 LEU D O   
15922 C CB  . LEU D  437 ? 0.6758 1.1221 0.7368 -0.1680 0.0265  -0.1493 437 LEU D CB  
15923 C CG  . LEU D  437 ? 0.7144 1.1114 0.7516 -0.1568 0.0157  -0.1428 437 LEU D CG  
15924 C CD1 . LEU D  437 ? 0.7189 1.1164 0.7616 -0.1328 0.0171  -0.1519 437 LEU D CD1 
15925 C CD2 . LEU D  437 ? 0.7385 1.1086 0.7421 -0.1728 0.0170  -0.1313 437 LEU D CD2 
15926 N N   . THR D  438 ? 0.5822 0.9700 0.6105 -0.2070 0.0067  -0.1239 438 THR D N   
15927 C CA  . THR D  438 ? 0.5852 0.9437 0.5892 -0.2296 0.0007  -0.1108 438 THR D CA  
15928 C C   . THR D  438 ? 0.6330 0.9600 0.6019 -0.2358 0.0022  -0.1015 438 THR D C   
15929 O O   . THR D  438 ? 0.6886 1.0118 0.6393 -0.2592 0.0060  -0.0927 438 THR D O   
15930 C CB  . THR D  438 ? 0.4367 0.7624 0.4381 -0.2255 -0.0153 -0.1071 438 THR D CB  
15931 O OG1 . THR D  438 ? 0.4093 0.7572 0.4412 -0.2084 -0.0183 -0.1176 438 THR D OG1 
15932 C CG2 . THR D  438 ? 0.4638 0.7817 0.4563 -0.2524 -0.0194 -0.0982 438 THR D CG2 
15933 N N   . TRP D  439 ? 0.6085 0.9103 0.5669 -0.2153 -0.0025 -0.1028 439 TRP D N   
15934 C CA  . TRP D  439 ? 0.6031 0.8740 0.5293 -0.2165 -0.0029 -0.0950 439 TRP D CA  
15935 C C   . TRP D  439 ? 0.5945 0.8889 0.5115 -0.2308 0.0117  -0.0941 439 TRP D C   
15936 O O   . TRP D  439 ? 0.5378 0.8766 0.4771 -0.2324 0.0238  -0.1029 439 TRP D O   
15937 C CB  . TRP D  439 ? 0.4844 0.7419 0.4108 -0.1903 -0.0065 -0.1006 439 TRP D CB  
15938 C CG  . TRP D  439 ? 0.4586 0.6910 0.3892 -0.1753 -0.0199 -0.1009 439 TRP D CG  
15939 C CD1 . TRP D  439 ? 0.4433 0.6904 0.3998 -0.1588 -0.0226 -0.1100 439 TRP D CD1 
15940 C CD2 . TRP D  439 ? 0.4662 0.6539 0.3735 -0.1744 -0.0328 -0.0920 439 TRP D CD2 
15941 N NE1 . TRP D  439 ? 0.4450 0.6603 0.3953 -0.1486 -0.0357 -0.1072 439 TRP D NE1 
15942 C CE2 . TRP D  439 ? 0.4612 0.6406 0.3822 -0.1573 -0.0420 -0.0967 439 TRP D CE2 
15943 C CE3 . TRP D  439 ? 0.4877 0.6414 0.3633 -0.1858 -0.0379 -0.0808 439 TRP D CE3 
15944 C CZ2 . TRP D  439 ? 0.4318 0.5724 0.3367 -0.1511 -0.0551 -0.0913 439 TRP D CZ2 
15945 C CZ3 . TRP D  439 ? 0.5040 0.6176 0.3639 -0.1785 -0.0519 -0.0755 439 TRP D CZ3 
15946 C CH2 . TRP D  439 ? 0.4902 0.5988 0.3653 -0.1611 -0.0599 -0.0812 439 TRP D CH2 
15947 N N   . PRO D  440 ? 0.5519 0.8167 0.4352 -0.2408 0.0104  -0.0836 440 PRO D N   
15948 C CA  . PRO D  440 ? 0.5772 0.8584 0.4453 -0.2570 0.0232  -0.0807 440 PRO D CA  
15949 C C   . PRO D  440 ? 0.5099 0.8250 0.3910 -0.2434 0.0361  -0.0926 440 PRO D C   
15950 O O   . PRO D  440 ? 0.4842 0.7993 0.3785 -0.2198 0.0333  -0.1014 440 PRO D O   
15951 C CB  . PRO D  440 ? 0.6067 0.8401 0.4354 -0.2613 0.0148  -0.0681 440 PRO D CB  
15952 C CG  . PRO D  440 ? 0.5751 0.7749 0.4036 -0.2401 0.0001  -0.0685 440 PRO D CG  
15953 C CD  . PRO D  440 ? 0.5664 0.7791 0.4228 -0.2370 -0.0042 -0.0738 440 PRO D CD  
15954 N N   . LEU D  441 ? 0.5431 0.8862 0.4189 -0.2594 0.0501  -0.0927 441 LEU D N   
15955 C CA  . LEU D  441 ? 0.5673 0.9434 0.4520 -0.2489 0.0635  -0.1043 441 LEU D CA  
15956 C C   . LEU D  441 ? 0.5591 0.9074 0.4251 -0.2311 0.0591  -0.1051 441 LEU D C   
15957 O O   . LEU D  441 ? 0.4914 0.8565 0.3712 -0.2122 0.0638  -0.1171 441 LEU D O   
15958 C CB  . LEU D  441 ? 0.7990 1.2035 0.6730 -0.2727 0.0786  -0.1016 441 LEU D CB  
15959 C CG  . LEU D  441 ? 0.8072 1.2616 0.6978 -0.2676 0.0960  -0.1155 441 LEU D CG  
15960 C CD1 . LEU D  441 ? 0.8255 1.2682 0.6913 -0.2597 0.1006  -0.1171 441 LEU D CD1 
15961 C CD2 . LEU D  441 ? 0.7525 1.2366 0.6832 -0.2454 0.0964  -0.1312 441 LEU D CD2 
15962 N N   . TRP D  442 ? 0.6472 0.9521 0.4817 -0.2371 0.0493  -0.0923 442 TRP D N   
15963 C CA  . TRP D  442 ? 0.6600 0.9399 0.4737 -0.2239 0.0453  -0.0916 442 TRP D CA  
15964 C C   . TRP D  442 ? 0.6466 0.9138 0.4755 -0.1975 0.0358  -0.0988 442 TRP D C   
15965 O O   . TRP D  442 ? 0.6597 0.9159 0.4788 -0.1841 0.0343  -0.1018 442 TRP D O   
15966 C CB  . TRP D  442 ? 0.7507 0.9883 0.5264 -0.2371 0.0364  -0.0758 442 TRP D CB  
15967 C CG  . TRP D  442 ? 0.7776 0.9755 0.5472 -0.2341 0.0195  -0.0672 442 TRP D CG  
15968 C CD1 . TRP D  442 ? 0.8258 1.0071 0.5873 -0.2518 0.0134  -0.0572 442 TRP D CD1 
15969 C CD2 . TRP D  442 ? 0.7274 0.8968 0.4970 -0.2126 0.0064  -0.0682 442 TRP D CD2 
15970 N NE1 . TRP D  442 ? 0.8212 0.9649 0.5774 -0.2411 -0.0026 -0.0527 442 TRP D NE1 
15971 C CE2 . TRP D  442 ? 0.7591 0.8967 0.5208 -0.2171 -0.0067 -0.0593 442 TRP D CE2 
15972 C CE3 . TRP D  442 ? 0.6491 0.8175 0.4244 -0.1906 0.0046  -0.0759 442 TRP D CE3 
15973 C CZ2 . TRP D  442 ? 0.7163 0.8239 0.4763 -0.1995 -0.0205 -0.0585 442 TRP D CZ2 
15974 C CZ3 . TRP D  442 ? 0.6195 0.7592 0.3937 -0.1749 -0.0090 -0.0743 442 TRP D CZ3 
15975 C CH2 . TRP D  442 ? 0.6567 0.7675 0.4236 -0.1788 -0.0210 -0.0659 442 TRP D CH2 
15976 N N   . MET D  443 ? 0.6803 0.9497 0.5326 -0.1910 0.0294  -0.1016 443 MET D N   
15977 C CA  . MET D  443 ? 0.6440 0.8988 0.5089 -0.1680 0.0195  -0.1067 443 MET D CA  
15978 C C   . MET D  443 ? 0.5835 0.8696 0.4757 -0.1508 0.0265  -0.1216 443 MET D C   
15979 O O   . MET D  443 ? 0.5641 0.8423 0.4694 -0.1327 0.0193  -0.1266 443 MET D O   
15980 C CB  . MET D  443 ? 0.5270 0.7651 0.4007 -0.1683 0.0081  -0.1023 443 MET D CB  
15981 C CG  . MET D  443 ? 0.4747 0.6698 0.3208 -0.1749 -0.0040 -0.0893 443 MET D CG  
15982 S SD  . MET D  443 ? 0.6235 0.8026 0.4827 -0.1729 -0.0167 -0.0871 443 MET D SD  
15983 C CE  . MET D  443 ? 0.4923 0.6176 0.3166 -0.1737 -0.0315 -0.0743 443 MET D CE  
15984 N N   . GLY D  444 ? 0.5095 0.8307 0.4093 -0.1567 0.0404  -0.1288 444 GLY D N   
15985 C CA  . GLY D  444 ? 0.5061 0.8553 0.4285 -0.1398 0.0471  -0.1435 444 GLY D CA  
15986 C C   . GLY D  444 ? 0.4845 0.8447 0.4375 -0.1273 0.0418  -0.1502 444 GLY D C   
15987 O O   . GLY D  444 ? 0.4757 0.8524 0.4438 -0.1369 0.0424  -0.1492 444 GLY D O   
15988 N N   . VAL D  445 ? 0.4846 0.8349 0.4455 -0.1065 0.0360  -0.1568 445 VAL D N   
15989 C CA  . VAL D  445 ? 0.4539 0.8113 0.4412 -0.0925 0.0300  -0.1632 445 VAL D CA  
15990 C C   . VAL D  445 ? 0.4798 0.7991 0.4565 -0.0849 0.0163  -0.1559 445 VAL D C   
15991 O O   . VAL D  445 ? 0.5165 0.8215 0.4889 -0.0706 0.0126  -0.1590 445 VAL D O   
15992 C CB  . VAL D  445 ? 0.3383 0.7153 0.3423 -0.0739 0.0347  -0.1774 445 VAL D CB  
15993 C CG1 . VAL D  445 ? 0.3186 0.7029 0.3491 -0.0601 0.0279  -0.1835 445 VAL D CG1 
15994 C CG2 . VAL D  445 ? 0.3480 0.7622 0.3583 -0.0798 0.0494  -0.1857 445 VAL D CG2 
15995 N N   . PRO D  446 ? 0.3506 0.6532 0.3219 -0.0950 0.0089  -0.1463 446 PRO D N   
15996 C CA  . PRO D  446 ? 0.4037 0.6696 0.3616 -0.0894 -0.0038 -0.1387 446 PRO D CA  
15997 C C   . PRO D  446 ? 0.3773 0.6379 0.3506 -0.0700 -0.0111 -0.1444 446 PRO D C   
15998 O O   . PRO D  446 ? 0.3704 0.6533 0.3670 -0.0619 -0.0089 -0.1531 446 PRO D O   
15999 C CB  . PRO D  446 ? 0.3603 0.6167 0.3148 -0.1043 -0.0091 -0.1301 446 PRO D CB  
16000 C CG  . PRO D  446 ? 0.3762 0.6565 0.3299 -0.1226 0.0016  -0.1293 446 PRO D CG  
16001 C CD  . PRO D  446 ? 0.3630 0.6800 0.3379 -0.1141 0.0122  -0.1418 446 PRO D CD  
16002 N N   . HIS D  447 ? 0.3772 0.6081 0.3367 -0.0629 -0.0202 -0.1392 447 HIS D N   
16003 C CA  . HIS D  447 ? 0.3747 0.5961 0.3441 -0.0466 -0.0281 -0.1423 447 HIS D CA  
16004 C C   . HIS D  447 ? 0.4088 0.6398 0.3982 -0.0455 -0.0321 -0.1444 447 HIS D C   
16005 O O   . HIS D  447 ? 0.4069 0.6341 0.3943 -0.0569 -0.0350 -0.1390 447 HIS D O   
16006 C CB  . HIS D  447 ? 0.3477 0.5369 0.2974 -0.0439 -0.0372 -0.1343 447 HIS D CB  
16007 C CG  . HIS D  447 ? 0.3356 0.5138 0.2926 -0.0292 -0.0454 -0.1361 447 HIS D CG  
16008 N ND1 . HIS D  447 ? 0.3761 0.5593 0.3406 -0.0165 -0.0445 -0.1425 447 HIS D ND1 
16009 C CD2 . HIS D  447 ? 0.3306 0.4923 0.2868 -0.0257 -0.0547 -0.1321 447 HIS D CD2 
16010 C CE1 . HIS D  447 ? 0.3722 0.5436 0.3406 -0.0068 -0.0525 -0.1418 447 HIS D CE1 
16011 N NE2 . HIS D  447 ? 0.3559 0.5151 0.3196 -0.0117 -0.0584 -0.1359 447 HIS D NE2 
16012 N N   . GLY D  448 ? 0.5415 0.7847 0.5495 -0.0321 -0.0328 -0.1524 448 GLY D N   
16013 C CA  . GLY D  448 ? 0.5218 0.7726 0.5479 -0.0291 -0.0381 -0.1545 448 GLY D CA  
16014 C C   . GLY D  448 ? 0.5290 0.8124 0.5753 -0.0351 -0.0318 -0.1603 448 GLY D C   
16015 O O   . GLY D  448 ? 0.5673 0.8599 0.6304 -0.0319 -0.0365 -0.1629 448 GLY D O   
16016 N N   . TYR D  449 ? 0.3252 0.6279 0.3704 -0.0435 -0.0212 -0.1628 449 TYR D N   
16017 C CA  . TYR D  449 ? 0.2975 0.6349 0.3621 -0.0513 -0.0144 -0.1680 449 TYR D CA  
16018 C C   . TYR D  449 ? 0.2751 0.6418 0.3627 -0.0377 -0.0094 -0.1805 449 TYR D C   
16019 O O   . TYR D  449 ? 0.2740 0.6742 0.3784 -0.0430 -0.0021 -0.1862 449 TYR D O   
16020 C CB  . TYR D  449 ? 0.3981 0.7442 0.4511 -0.0719 -0.0062 -0.1626 449 TYR D CB  
16021 C CG  . TYR D  449 ? 0.4564 0.7789 0.4959 -0.0857 -0.0141 -0.1515 449 TYR D CG  
16022 C CD1 . TYR D  449 ? 0.5199 0.8057 0.5338 -0.0864 -0.0203 -0.1429 449 TYR D CD1 
16023 C CD2 . TYR D  449 ? 0.4402 0.7759 0.4926 -0.0968 -0.0165 -0.1503 449 TYR D CD2 
16024 C CE1 . TYR D  449 ? 0.5517 0.8129 0.5519 -0.0970 -0.0286 -0.1335 449 TYR D CE1 
16025 C CE2 . TYR D  449 ? 0.4668 0.7772 0.5051 -0.1090 -0.0248 -0.1406 449 TYR D CE2 
16026 C CZ  . TYR D  449 ? 0.5287 0.8009 0.5403 -0.1084 -0.0309 -0.1324 449 TYR D CZ  
16027 O OH  . TYR D  449 ? 0.5475 0.7914 0.5433 -0.1186 -0.0399 -0.1235 449 TYR D OH  
16028 N N   . GLU D  450 ? 0.4999 0.8537 0.5875 -0.0203 -0.0135 -0.1848 450 GLU D N   
16029 C CA  . GLU D  450 ? 0.5223 0.8964 0.6308 -0.0047 -0.0124 -0.1963 450 GLU D CA  
16030 C C   . GLU D  450 ? 0.5437 0.9172 0.6690 0.0042  -0.0227 -0.1974 450 GLU D C   
16031 O O   . GLU D  450 ? 0.5880 0.9814 0.7332 0.0159  -0.0230 -0.2066 450 GLU D O   
16032 C CB  . GLU D  450 ? 0.3723 0.7312 0.4711 0.0091  -0.0122 -0.2007 450 GLU D CB  
16033 C CG  . GLU D  450 ? 0.3717 0.7009 0.4648 0.0202  -0.0236 -0.1971 450 GLU D CG  
16034 C CD  . GLU D  450 ? 0.4207 0.7205 0.4915 0.0121  -0.0281 -0.1858 450 GLU D CD  
16035 O OE1 . GLU D  450 ? 0.4164 0.7159 0.4811 -0.0020 -0.0271 -0.1790 450 GLU D OE1 
16036 O OE2 . GLU D  450 ? 0.4557 0.7330 0.5152 0.0198  -0.0328 -0.1839 450 GLU D OE2 
16037 N N   . ILE D  451 ? 0.3858 0.7365 0.5024 -0.0009 -0.0316 -0.1884 451 ILE D N   
16038 C CA  . ILE D  451 ? 0.3188 0.6641 0.4470 0.0082  -0.0423 -0.1888 451 ILE D CA  
16039 C C   . ILE D  451 ? 0.2981 0.6756 0.4515 0.0068  -0.0422 -0.1946 451 ILE D C   
16040 O O   . ILE D  451 ? 0.2644 0.6523 0.4345 0.0208  -0.0467 -0.2015 451 ILE D O   
16041 C CB  . ILE D  451 ? 0.2336 0.5506 0.3471 0.0020  -0.0511 -0.1789 451 ILE D CB  
16042 C CG1 . ILE D  451 ? 0.2356 0.5233 0.3258 0.0040  -0.0517 -0.1733 451 ILE D CG1 
16043 C CG2 . ILE D  451 ? 0.2256 0.5375 0.3496 0.0120  -0.0618 -0.1799 451 ILE D CG2 
16044 C CD1 . ILE D  451 ? 0.2372 0.4979 0.3135 0.0011  -0.0605 -0.1650 451 ILE D CD1 
16045 N N   . GLU D  452 ? 0.3786 0.7720 0.5343 -0.0105 -0.0376 -0.1916 452 GLU D N   
16046 C CA  . GLU D  452 ? 0.3949 0.8215 0.5749 -0.0153 -0.0375 -0.1963 452 GLU D CA  
16047 C C   . GLU D  452 ? 0.4248 0.8844 0.6272 -0.0020 -0.0320 -0.2087 452 GLU D C   
16048 O O   . GLU D  452 ? 0.4666 0.9498 0.6922 0.0038  -0.0361 -0.2146 452 GLU D O   
16049 C CB  . GLU D  452 ? 0.2929 0.7322 0.4691 -0.0383 -0.0312 -0.1910 452 GLU D CB  
16050 C CG  . GLU D  452 ? 0.3319 0.7773 0.4954 -0.0463 -0.0185 -0.1908 452 GLU D CG  
16051 C CD  . GLU D  452 ? 0.3976 0.8326 0.5428 -0.0694 -0.0159 -0.1804 452 GLU D CD  
16052 O OE1 . GLU D  452 ? 0.4246 0.8228 0.5452 -0.0718 -0.0206 -0.1719 452 GLU D OE1 
16053 O OE2 . GLU D  452 ? 0.4331 0.8966 0.5882 -0.0853 -0.0094 -0.1808 452 GLU D OE2 
16054 N N   . PHE D  453 ? 0.3015 0.7620 0.4964 0.0039  -0.0236 -0.2131 453 PHE D N   
16055 C CA  . PHE D  453 ? 0.2810 0.7694 0.4945 0.0184  -0.0184 -0.2259 453 PHE D CA  
16056 C C   . PHE D  453 ? 0.2961 0.7679 0.5137 0.0401  -0.0282 -0.2304 453 PHE D C   
16057 O O   . PHE D  453 ? 0.3090 0.8030 0.5485 0.0530  -0.0308 -0.2397 453 PHE D O   
16058 C CB  . PHE D  453 ? 0.3005 0.7955 0.5029 0.0163  -0.0058 -0.2297 453 PHE D CB  
16059 C CG  . PHE D  453 ? 0.3338 0.8551 0.5368 -0.0036 0.0055  -0.2279 453 PHE D CG  
16060 C CD1 . PHE D  453 ? 0.3795 0.8806 0.5598 -0.0223 0.0071  -0.2161 453 PHE D CD1 
16061 C CD2 . PHE D  453 ? 0.3566 0.9234 0.5827 -0.0038 0.0141  -0.2379 453 PHE D CD2 
16062 C CE1 . PHE D  453 ? 0.4119 0.9353 0.5905 -0.0424 0.0171  -0.2134 453 PHE D CE1 
16063 C CE2 . PHE D  453 ? 0.3850 0.9781 0.6113 -0.0241 0.0251  -0.2357 453 PHE D CE2 
16064 C CZ  . PHE D  453 ? 0.4009 0.9711 0.6025 -0.0442 0.0265  -0.2230 453 PHE D CZ  
16065 N N   . ILE D  454 ? 0.2544 0.6876 0.4510 0.0440  -0.0341 -0.2238 454 ILE D N   
16066 C CA  . ILE D  454 ? 0.2213 0.6356 0.4185 0.0625  -0.0435 -0.2267 454 ILE D CA  
16067 C C   . ILE D  454 ? 0.2160 0.6349 0.4287 0.0668  -0.0543 -0.2260 454 ILE D C   
16068 O O   . ILE D  454 ? 0.2190 0.6344 0.4388 0.0819  -0.0600 -0.2307 454 ILE D O   
16069 C CB  . ILE D  454 ? 0.2398 0.6141 0.4120 0.0633  -0.0478 -0.2187 454 ILE D CB  
16070 C CG1 . ILE D  454 ? 0.2269 0.5956 0.3821 0.0574  -0.0380 -0.2184 454 ILE D CG1 
16071 C CG2 . ILE D  454 ? 0.2198 0.5762 0.3921 0.0810  -0.0565 -0.2219 454 ILE D CG2 
16072 C CD1 . ILE D  454 ? 0.2325 0.6188 0.3954 0.0677  -0.0310 -0.2301 454 ILE D CD1 
16073 N N   . PHE D  455 ? 0.2631 0.6820 0.4748 0.0523  -0.0570 -0.2186 455 PHE D N   
16074 C CA  . PHE D  455 ? 0.2940 0.7136 0.5160 0.0543  -0.0659 -0.2165 455 PHE D CA  
16075 C C   . PHE D  455 ? 0.3104 0.7628 0.5531 0.0537  -0.0615 -0.2224 455 PHE D C   
16076 O O   . PHE D  455 ? 0.3279 0.7786 0.5780 0.0598  -0.0681 -0.2218 455 PHE D O   
16077 C CB  . PHE D  455 ? 0.2716 0.6737 0.4822 0.0404  -0.0718 -0.2064 455 PHE D CB  
16078 C CG  . PHE D  455 ? 0.2946 0.6582 0.4850 0.0465  -0.0794 -0.1998 455 PHE D CG  
16079 C CD1 . PHE D  455 ? 0.3191 0.6621 0.4891 0.0424  -0.0760 -0.1953 455 PHE D CD1 
16080 C CD2 . PHE D  455 ? 0.2524 0.5957 0.4400 0.0560  -0.0877 -0.1960 455 PHE D CD2 
16081 C CE1 . PHE D  455 ? 0.2841 0.5952 0.4368 0.0480  -0.0825 -0.1897 455 PHE D CE1 
16082 C CE2 . PHE D  455 ? 0.2274 0.5377 0.3964 0.0608  -0.0930 -0.1896 455 PHE D CE2 
16083 C CZ  . PHE D  455 ? 0.2513 0.5472 0.4041 0.0570  -0.0905 -0.1868 455 PHE D CZ  
16084 N N   . GLY D  456 ? 0.3179 0.8003 0.5689 0.0462  -0.0501 -0.2278 456 GLY D N   
16085 C CA  . GLY D  456 ? 0.3359 0.8508 0.6053 0.0468  -0.0447 -0.2342 456 GLY D CA  
16086 C C   . GLY D  456 ? 0.3560 0.8923 0.6358 0.0286  -0.0435 -0.2300 456 GLY D C   
16087 O O   . GLY D  456 ? 0.3780 0.9377 0.6741 0.0303  -0.0427 -0.2338 456 GLY D O   
16088 N N   . LEU D  457 ? 0.3415 0.8691 0.6109 0.0108  -0.0441 -0.2220 457 LEU D N   
16089 C CA  . LEU D  457 ? 0.3414 0.8866 0.6173 -0.0099 -0.0427 -0.2172 457 LEU D CA  
16090 C C   . LEU D  457 ? 0.3976 0.9854 0.6901 -0.0180 -0.0308 -0.2229 457 LEU D C   
16091 O O   . LEU D  457 ? 0.4153 1.0204 0.7201 -0.0267 -0.0323 -0.2214 457 LEU D O   
16092 C CB  . LEU D  457 ? 0.2365 0.7636 0.4941 -0.0292 -0.0440 -0.2085 457 LEU D CB  
16093 C CG  . LEU D  457 ? 0.2356 0.7251 0.4788 -0.0297 -0.0573 -0.2002 457 LEU D CG  
16094 C CD1 . LEU D  457 ? 0.2281 0.6913 0.4654 -0.0072 -0.0646 -0.2014 457 LEU D CD1 
16095 C CD2 . LEU D  457 ? 0.2428 0.7051 0.4601 -0.0453 -0.0563 -0.1911 457 LEU D CD2 
16096 N N   . PRO D  458 ? 0.4793 1.0838 0.7711 -0.0157 -0.0191 -0.2294 458 PRO D N   
16097 C CA  . PRO D  458 ? 0.5165 1.1609 0.8221 -0.0229 -0.0074 -0.2348 458 PRO D CA  
16098 C C   . PRO D  458 ? 0.5622 1.2253 0.8878 -0.0109 -0.0111 -0.2406 458 PRO D C   
16099 O O   . PRO D  458 ? 0.6061 1.3028 0.9446 -0.0208 -0.0039 -0.2429 458 PRO D O   
16100 C CB  . PRO D  458 ? 0.5159 1.1663 0.8149 -0.0143 0.0032  -0.2423 458 PRO D CB  
16101 C CG  . PRO D  458 ? 0.5035 1.1243 0.7835 -0.0170 0.0006  -0.2369 458 PRO D CG  
16102 C CD  . PRO D  458 ? 0.4846 1.0739 0.7610 -0.0114 -0.0149 -0.2306 458 PRO D CD  
16103 N N   . LEU D  459 ? 0.4246 1.0665 0.7517 0.0091  -0.0222 -0.2425 459 LEU D N   
16104 C CA  . LEU D  459 ? 0.4049 1.0614 0.7496 0.0211  -0.0275 -0.2475 459 LEU D CA  
16105 C C   . LEU D  459 ? 0.4000 1.0691 0.7558 0.0064  -0.0323 -0.2414 459 LEU D C   
16106 O O   . LEU D  459 ? 0.4213 1.1152 0.7950 0.0101  -0.0333 -0.2457 459 LEU D O   
16107 C CB  . LEU D  459 ? 0.2646 0.8903 0.6043 0.0434  -0.0392 -0.2489 459 LEU D CB  
16108 C CG  . LEU D  459 ? 0.2642 0.8751 0.5930 0.0589  -0.0362 -0.2552 459 LEU D CG  
16109 C CD1 . LEU D  459 ? 0.2604 0.8321 0.5779 0.0748  -0.0486 -0.2526 459 LEU D CD1 
16110 C CD2 . LEU D  459 ? 0.2772 0.9154 0.6186 0.0697  -0.0301 -0.2662 459 LEU D CD2 
16111 N N   . ASP D  460 ? 0.3564 1.0076 0.7010 -0.0103 -0.0360 -0.2316 460 ASP D N   
16112 C CA  . ASP D  460 ? 0.4166 1.0750 0.7679 -0.0271 -0.0412 -0.2249 460 ASP D CA  
16113 C C   . ASP D  460 ? 0.4454 1.1383 0.8038 -0.0493 -0.0294 -0.2245 460 ASP D C   
16114 O O   . ASP D  460 ? 0.4739 1.1641 0.8190 -0.0642 -0.0217 -0.2210 460 ASP D O   
16115 C CB  . ASP D  460 ? 0.5993 1.2203 0.9321 -0.0361 -0.0503 -0.2149 460 ASP D CB  
16116 C CG  . ASP D  460 ? 0.6608 1.2814 0.9978 -0.0510 -0.0584 -0.2081 460 ASP D CG  
16117 O OD1 . ASP D  460 ? 0.6918 1.3302 1.0310 -0.0732 -0.0530 -0.2047 460 ASP D OD1 
16118 O OD2 . ASP D  460 ? 0.6821 1.2827 1.0184 -0.0413 -0.0705 -0.2058 460 ASP D OD2 
16119 N N   . PRO D  461 ? 0.4808 1.2065 0.8594 -0.0520 -0.0281 -0.2278 461 PRO D N   
16120 C CA  . PRO D  461 ? 0.4773 1.2405 0.8643 -0.0711 -0.0158 -0.2286 461 PRO D CA  
16121 C C   . PRO D  461 ? 0.4786 1.2362 0.8560 -0.1005 -0.0159 -0.2177 461 PRO D C   
16122 O O   . PRO D  461 ? 0.4766 1.2567 0.8528 -0.1199 -0.0047 -0.2161 461 PRO D O   
16123 C CB  . PRO D  461 ? 0.5440 1.3393 0.9560 -0.0627 -0.0179 -0.2350 461 PRO D CB  
16124 C CG  . PRO D  461 ? 0.5430 1.3181 0.9576 -0.0352 -0.0287 -0.2398 461 PRO D CG  
16125 C CD  . PRO D  461 ? 0.5308 1.2613 0.9254 -0.0357 -0.0380 -0.2316 461 PRO D CD  
16126 N N   . SER D  462 ? 0.5423 1.2678 0.9108 -0.1041 -0.0289 -0.2101 462 SER D N   
16127 C CA  . SER D  462 ? 0.6095 1.3212 0.9650 -0.1311 -0.0315 -0.1996 462 SER D CA  
16128 C C   . SER D  462 ? 0.6599 1.3478 0.9906 -0.1415 -0.0265 -0.1945 462 SER D C   
16129 O O   . SER D  462 ? 0.6792 1.3511 0.9945 -0.1645 -0.0282 -0.1855 462 SER D O   
16130 C CB  . SER D  462 ? 0.6447 1.3280 0.9974 -0.1302 -0.0481 -0.1939 462 SER D CB  
16131 O OG  . SER D  462 ? 0.6245 1.2740 0.9662 -0.1100 -0.0563 -0.1945 462 SER D OG  
16132 N N   . LEU D  463 ? 0.8710 1.5541 1.1968 -0.1244 -0.0213 -0.2003 463 LEU D N   
16133 C CA  . LEU D  463 ? 0.8751 1.5342 1.1776 -0.1313 -0.0180 -0.1961 463 LEU D CA  
16134 C C   . LEU D  463 ? 0.9282 1.6117 1.2262 -0.1445 -0.0018 -0.1974 463 LEU D C   
16135 O O   . LEU D  463 ? 0.9661 1.6318 1.2439 -0.1531 0.0015  -0.1933 463 LEU D O   
16136 C CB  . LEU D  463 ? 0.5062 1.1397 0.8022 -0.1065 -0.0236 -0.2003 463 LEU D CB  
16137 C CG  . LEU D  463 ? 0.4560 1.0583 0.7494 -0.0957 -0.0396 -0.1969 463 LEU D CG  
16138 C CD1 . LEU D  463 ? 0.4412 1.0126 0.7217 -0.0762 -0.0446 -0.1984 463 LEU D CD1 
16139 C CD2 . LEU D  463 ? 0.4534 1.0345 0.7335 -0.1178 -0.0472 -0.1867 463 LEU D CD2 
16140 N N   . ASN D  464 ? 0.5545 1.2779 0.8698 -0.1461 0.0078  -0.2030 464 ASN D N   
16141 C CA  . ASN D  464 ? 0.5802 1.3292 0.8903 -0.1617 0.0237  -0.2034 464 ASN D CA  
16142 C C   . ASN D  464 ? 0.4974 1.2445 0.7974 -0.1495 0.0329  -0.2093 464 ASN D C   
16143 O O   . ASN D  464 ? 0.4845 1.2369 0.7695 -0.1655 0.0439  -0.2060 464 ASN D O   
16144 C CB  . ASN D  464 ? 0.9805 1.7177 1.2723 -0.1944 0.0246  -0.1906 464 ASN D CB  
16145 C CG  . ASN D  464 ? 1.1257 1.8661 1.4270 -0.2082 0.0163  -0.1851 464 ASN D CG  
16146 O OD1 . ASN D  464 ? 1.1388 1.8856 1.4592 -0.1929 0.0080  -0.1899 464 ASN D OD1 
16147 N ND2 . ASN D  464 ? 1.2495 1.9838 1.5360 -0.2378 0.0181  -0.1746 464 ASN D ND2 
16148 N N   . TYR D  465 ? 0.5626 1.2999 0.8687 -0.1217 0.0279  -0.2174 465 TYR D N   
16149 C CA  . TYR D  465 ? 0.5255 1.2628 0.8239 -0.1080 0.0363  -0.2245 465 TYR D CA  
16150 C C   . TYR D  465 ? 0.4894 1.2653 0.8018 -0.1019 0.0476  -0.2342 465 TYR D C   
16151 O O   . TYR D  465 ? 0.5044 1.3021 0.8358 -0.0995 0.0451  -0.2372 465 TYR D O   
16152 C CB  . TYR D  465 ? 0.5769 1.2864 0.8748 -0.0811 0.0262  -0.2292 465 TYR D CB  
16153 C CG  . TYR D  465 ? 0.5786 1.2493 0.8592 -0.0854 0.0163  -0.2208 465 TYR D CG  
16154 C CD1 . TYR D  465 ? 0.5878 1.2366 0.8686 -0.0881 0.0024  -0.2141 465 TYR D CD1 
16155 C CD2 . TYR D  465 ? 0.5865 1.2344 0.8447 -0.0855 0.0204  -0.2182 465 TYR D CD2 
16156 C CE1 . TYR D  465 ? 0.5935 1.2005 0.8535 -0.0905 -0.0074 -0.2060 465 TYR D CE1 
16157 C CE2 . TYR D  465 ? 0.5907 1.1865 0.8222 -0.0865 0.0106  -0.2072 465 TYR D CE2 
16158 C CZ  . TYR D  465 ? 0.5834 1.1596 0.8162 -0.0886 -0.0029 -0.2014 465 TYR D CZ  
16159 O OH  . TYR D  465 ? 0.5549 1.0823 0.7621 -0.0884 -0.0121 -0.1917 465 TYR D OH  
16160 N N   . THR D  466 ? 0.3244 1.1085 0.6267 -0.0995 0.0594  -0.2391 466 THR D N   
16161 C CA  . THR D  466 ? 0.3343 1.1527 0.6472 -0.0925 0.0697  -0.2492 466 THR D CA  
16162 C C   . THR D  466 ? 0.3283 1.1447 0.6542 -0.0612 0.0635  -0.2609 466 THR D C   
16163 O O   . THR D  466 ? 0.3138 1.1006 0.6379 -0.0455 0.0523  -0.2608 466 THR D O   
16164 C CB  . THR D  466 ? 0.5798 1.4040 0.8743 -0.1006 0.0836  -0.2501 466 THR D CB  
16165 O OG1 . THR D  466 ? 0.5996 1.3998 0.8839 -0.0798 0.0818  -0.2558 466 THR D OG1 
16166 C CG2 . THR D  466 ? 0.5986 1.4117 0.8732 -0.1302 0.0876  -0.2367 466 THR D CG2 
16167 N N   . THR D  467 ? 0.4896 1.3359 0.8270 -0.0525 0.0705  -0.2709 467 THR D N   
16168 C CA  . THR D  467 ? 0.5278 1.3731 0.8785 -0.0243 0.0632  -0.2816 467 THR D CA  
16169 C C   . THR D  467 ? 0.5575 1.3767 0.8930 -0.0060 0.0630  -0.2872 467 THR D C   
16170 O O   . THR D  467 ? 0.5387 1.3367 0.8770 0.0163  0.0526  -0.2918 467 THR D O   
16171 C CB  . THR D  467 ? 0.6370 1.5246 1.0083 -0.0208 0.0686  -0.2903 467 THR D CB  
16172 O OG1 . THR D  467 ? 0.6776 1.5946 1.0463 -0.0453 0.0818  -0.2868 467 THR D OG1 
16173 C CG2 . THR D  467 ? 0.6218 1.5178 1.0142 -0.0165 0.0578  -0.2896 467 THR D CG2 
16174 N N   . GLU D  468 ? 0.7099 1.5287 1.0277 -0.0168 0.0740  -0.2858 468 GLU D N   
16175 C CA  . GLU D  468 ? 0.7245 1.5140 1.0239 -0.0041 0.0737  -0.2885 468 GLU D CA  
16176 C C   . GLU D  468 ? 0.6529 1.4048 0.9455 0.0009  0.0616  -0.2818 468 GLU D C   
16177 O O   . GLU D  468 ? 0.6480 1.3752 0.9393 0.0217  0.0524  -0.2859 468 GLU D O   
16178 C CB  . GLU D  468 ? 0.8323 1.6238 1.1108 -0.0215 0.0867  -0.2846 468 GLU D CB  
16179 C CG  . GLU D  468 ? 0.9087 1.7296 1.1874 -0.0223 0.0990  -0.2924 468 GLU D CG  
16180 C CD  . GLU D  468 ? 0.9741 1.8340 1.2632 -0.0437 0.1078  -0.2895 468 GLU D CD  
16181 O OE1 . GLU D  468 ? 0.9645 1.8285 1.2627 -0.0564 0.1031  -0.2820 468 GLU D OE1 
16182 O OE2 . GLU D  468 ? 1.0195 1.9052 1.3070 -0.0481 0.1191  -0.2945 468 GLU D OE2 
16183 N N   . GLU D  469 ? 0.5265 1.2738 0.8143 -0.0193 0.0612  -0.2710 469 GLU D N   
16184 C CA  . GLU D  469 ? 0.4596 1.1729 0.7401 -0.0176 0.0503  -0.2638 469 GLU D CA  
16185 C C   . GLU D  469 ? 0.4156 1.1144 0.7092 0.0017  0.0358  -0.2662 469 GLU D C   
16186 O O   . GLU D  469 ? 0.3973 1.0639 0.6827 0.0141  0.0267  -0.2648 469 GLU D O   
16187 C CB  . GLU D  469 ? 0.3076 1.0217 0.5833 -0.0440 0.0510  -0.2519 469 GLU D CB  
16188 C CG  . GLU D  469 ? 0.2989 1.0190 0.5562 -0.0638 0.0641  -0.2475 469 GLU D CG  
16189 C CD  . GLU D  469 ? 0.3052 1.0174 0.5538 -0.0900 0.0622  -0.2346 469 GLU D CD  
16190 O OE1 . GLU D  469 ? 0.3166 1.0401 0.5761 -0.1024 0.0583  -0.2300 469 GLU D OE1 
16191 O OE2 . GLU D  469 ? 0.3055 0.9784 0.5234 -0.0962 0.0613  -0.2250 469 GLU D OE2 
16192 N N   . ARG D  470 ? 0.3237 1.0460 0.6364 0.0038  0.0337  -0.2694 470 ARG D N   
16193 C CA  . ARG D  470 ? 0.3425 1.0523 0.6666 0.0219  0.0203  -0.2717 470 ARG D CA  
16194 C C   . ARG D  470 ? 0.3355 1.0297 0.6556 0.0464  0.0172  -0.2806 470 ARG D C   
16195 O O   . ARG D  470 ? 0.3123 0.9738 0.6257 0.0601  0.0062  -0.2792 470 ARG D O   
16196 C CB  . ARG D  470 ? 0.6232 1.3651 0.9690 0.0187  0.0198  -0.2738 470 ARG D CB  
16197 C CG  . ARG D  470 ? 0.7009 1.4292 1.0572 0.0328  0.0052  -0.2734 470 ARG D CG  
16198 C CD  . ARG D  470 ? 0.7866 1.5375 1.1605 0.0493  0.0039  -0.2837 470 ARG D CD  
16199 N NE  . ARG D  470 ? 0.8708 1.6653 1.2613 0.0363  0.0125  -0.2859 470 ARG D NE  
16200 C CZ  . ARG D  470 ? 0.9369 1.7607 1.3432 0.0470  0.0154  -0.2958 470 ARG D CZ  
16201 N NH1 . ARG D  470 ? 0.9562 1.7686 1.3631 0.0710  0.0099  -0.3043 470 ARG D NH1 
16202 N NH2 . ARG D  470 ? 0.9540 1.8185 1.3752 0.0333  0.0235  -0.2971 470 ARG D NH2 
16203 N N   . ILE D  471 ? 0.5143 1.2303 0.8367 0.0509  0.0265  -0.2894 471 ILE D N   
16204 C CA  . ILE D  471 ? 0.5537 1.2558 0.8724 0.0734  0.0232  -0.2984 471 ILE D CA  
16205 C C   . ILE D  471 ? 0.5548 1.2168 0.8520 0.0790  0.0194  -0.2952 471 ILE D C   
16206 O O   . ILE D  471 ? 0.5323 1.1662 0.8248 0.0968  0.0091  -0.2973 471 ILE D O   
16207 C CB  . ILE D  471 ? 0.3919 1.1262 0.7159 0.0751  0.0348  -0.3081 471 ILE D CB  
16208 C CG1 . ILE D  471 ? 0.4236 1.1619 0.7598 0.0979  0.0281  -0.3183 471 ILE D CG1 
16209 C CG2 . ILE D  471 ? 0.3878 1.1131 0.6920 0.0711  0.0444  -0.3090 471 ILE D CG2 
16210 C CD1 . ILE D  471 ? 0.4423 1.1891 0.7970 0.1024  0.0184  -0.3174 471 ILE D CD1 
16211 N N   . PHE D  472 ? 0.5928 1.2523 0.8768 0.0624  0.0272  -0.2891 472 PHE D N   
16212 C CA  . PHE D  472 ? 0.5471 1.1738 0.8103 0.0635  0.0260  -0.2853 472 PHE D CA  
16213 C C   . PHE D  472 ? 0.5280 1.1246 0.7892 0.0679  0.0128  -0.2783 472 PHE D C   
16214 O O   . PHE D  472 ? 0.5065 1.0707 0.7557 0.0801  0.0055  -0.2780 472 PHE D O   
16215 C CB  . PHE D  472 ? 0.3749 1.0126 0.6264 0.0419  0.0384  -0.2800 472 PHE D CB  
16216 C CG  . PHE D  472 ? 0.3557 0.9621 0.5857 0.0399  0.0377  -0.2748 472 PHE D CG  
16217 C CD1 . PHE D  472 ? 0.3522 0.9315 0.5683 0.0551  0.0346  -0.2786 472 PHE D CD1 
16218 C CD2 . PHE D  472 ? 0.3476 0.9518 0.5707 0.0219  0.0400  -0.2656 472 PHE D CD2 
16219 C CE1 . PHE D  472 ? 0.3084 0.8587 0.5034 0.0528  0.0341  -0.2736 472 PHE D CE1 
16220 C CE2 . PHE D  472 ? 0.2716 0.8389 0.4692 0.0196  0.0378  -0.2584 472 PHE D CE2 
16221 C CZ  . PHE D  472 ? 0.2824 0.8284 0.4686 0.0359  0.0362  -0.2643 472 PHE D CZ  
16222 N N   . ALA D  473 ? 0.5241 1.1312 0.7965 0.0574  0.0092  -0.2724 473 ALA D N   
16223 C CA  . ALA D  473 ? 0.4955 1.0764 0.7663 0.0596  -0.0035 -0.2650 473 ALA D CA  
16224 C C   . ALA D  473 ? 0.5472 1.1072 0.8199 0.0812  -0.0150 -0.2689 473 ALA D C   
16225 O O   . ALA D  473 ? 0.5670 1.0938 0.8268 0.0902  -0.0226 -0.2663 473 ALA D O   
16226 C CB  . ALA D  473 ? 0.2541 0.8510 0.5370 0.0446  -0.0058 -0.2586 473 ALA D CB  
16227 N N   . GLN D  474 ? 0.5832 1.1628 0.8713 0.0890  -0.0162 -0.2750 474 GLN D N   
16228 C CA  . GLN D  474 ? 0.6126 1.1723 0.9018 0.1088  -0.0277 -0.2784 474 GLN D CA  
16229 C C   . GLN D  474 ? 0.6566 1.1938 0.9316 0.1218  -0.0282 -0.2831 474 GLN D C   
16230 O O   . GLN D  474 ? 0.6932 1.1997 0.9601 0.1344  -0.0390 -0.2819 474 GLN D O   
16231 C CB  . GLN D  474 ? 0.4608 1.0464 0.7696 0.1158  -0.0297 -0.2844 474 GLN D CB  
16232 C CG  . GLN D  474 ? 0.4769 1.1039 0.7981 0.1086  -0.0171 -0.2911 474 GLN D CG  
16233 C CD  . GLN D  474 ? 0.4886 1.1436 0.8313 0.1122  -0.0199 -0.2950 474 GLN D CD  
16234 O OE1 . GLN D  474 ? 0.5065 1.1980 0.8619 0.1080  -0.0107 -0.3010 474 GLN D OE1 
16235 N NE2 . GLN D  474 ? 0.4565 1.0950 0.8030 0.1197  -0.0326 -0.2913 474 GLN D NE2 
16236 N N   . ARG D  475 ? 0.6460 1.1969 0.9162 0.1176  -0.0168 -0.2878 475 ARG D N   
16237 C CA  . ARG D  475 ? 0.6477 1.1747 0.9021 0.1276  -0.0172 -0.2910 475 ARG D CA  
16238 C C   . ARG D  475 ? 0.6311 1.1208 0.8680 0.1265  -0.0236 -0.2830 475 ARG D C   
16239 O O   . ARG D  475 ? 0.6570 1.1166 0.8843 0.1389  -0.0326 -0.2829 475 ARG D O   
16240 C CB  . ARG D  475 ? 0.5886 1.1349 0.8380 0.1204  -0.0032 -0.2957 475 ARG D CB  
16241 C CG  . ARG D  475 ? 0.5991 1.1186 0.8298 0.1278  -0.0032 -0.2974 475 ARG D CG  
16242 C CD  . ARG D  475 ? 0.6416 1.1834 0.8708 0.1256  0.0092  -0.3046 475 ARG D CD  
16243 N NE  . ARG D  475 ? 0.6872 1.2077 0.8951 0.1223  0.0135  -0.3025 475 ARG D NE  
16244 C CZ  . ARG D  475 ? 0.7001 1.2328 0.8985 0.1073  0.0254  -0.3004 475 ARG D CZ  
16245 N NH1 . ARG D  475 ? 0.6792 1.2461 0.8879 0.0933  0.0345  -0.2999 475 ARG D NH1 
16246 N NH2 . ARG D  475 ? 0.7182 1.2283 0.8958 0.1055  0.0279  -0.2982 475 ARG D NH2 
16247 N N   . LEU D  476 ? 0.5229 1.0152 0.7557 0.1113  -0.0192 -0.2761 476 LEU D N   
16248 C CA  . LEU D  476 ? 0.4646 0.9251 0.6814 0.1096  -0.0242 -0.2688 476 LEU D CA  
16249 C C   . LEU D  476 ? 0.4438 0.8800 0.6613 0.1179  -0.0385 -0.2639 476 LEU D C   
16250 O O   . LEU D  476 ? 0.4293 0.8335 0.6327 0.1246  -0.0455 -0.2607 476 LEU D O   
16251 C CB  . LEU D  476 ? 0.2714 0.7420 0.4843 0.0918  -0.0164 -0.2630 476 LEU D CB  
16252 C CG  . LEU D  476 ? 0.2572 0.7349 0.4571 0.0837  -0.0034 -0.2654 476 LEU D CG  
16253 C CD1 . LEU D  476 ? 0.2515 0.7088 0.4313 0.0688  -0.0020 -0.2544 476 LEU D CD1 
16254 C CD2 . LEU D  476 ? 0.2714 0.7296 0.4589 0.0963  -0.0043 -0.2704 476 LEU D CD2 
16255 N N   . MET D  477 ? 0.4349 0.8855 0.6673 0.1167  -0.0427 -0.2627 477 MET D N   
16256 C CA  . MET D  477 ? 0.4182 0.8461 0.6500 0.1247  -0.0560 -0.2581 477 MET D CA  
16257 C C   . MET D  477 ? 0.4519 0.8593 0.6781 0.1416  -0.0634 -0.2626 477 MET D C   
16258 O O   . MET D  477 ? 0.4556 0.8314 0.6699 0.1475  -0.0729 -0.2578 477 MET D O   
16259 C CB  . MET D  477 ? 0.2873 0.7356 0.5358 0.1211  -0.0585 -0.2571 477 MET D CB  
16260 C CG  . MET D  477 ? 0.2754 0.7413 0.5289 0.1028  -0.0533 -0.2513 477 MET D CG  
16261 S SD  . MET D  477 ? 0.5489 1.0324 0.8197 0.0987  -0.0587 -0.2488 477 MET D SD  
16262 C CE  . MET D  477 ? 1.0508 1.5543 1.3354 0.1141  -0.0576 -0.2603 477 MET D CE  
16263 N N   . LYS D  478 ? 0.5111 0.9366 0.7454 0.1487  -0.0591 -0.2715 478 LYS D N   
16264 C CA  . LYS D  478 ? 0.5608 0.9678 0.7895 0.1644  -0.0658 -0.2764 478 LYS D CA  
16265 C C   . LYS D  478 ? 0.5710 0.9463 0.7796 0.1655  -0.0674 -0.2731 478 LYS D C   
16266 O O   . LYS D  478 ? 0.6056 0.9511 0.8044 0.1742  -0.0779 -0.2704 478 LYS D O   
16267 C CB  . LYS D  478 ? 0.6241 1.0572 0.8632 0.1708  -0.0591 -0.2870 478 LYS D CB  
16268 C CG  . LYS D  478 ? 0.6597 1.1174 0.9183 0.1766  -0.0619 -0.2917 478 LYS D CG  
16269 C CD  . LYS D  478 ? 0.6618 1.0962 0.9188 0.1923  -0.0760 -0.2923 478 LYS D CD  
16270 C CE  . LYS D  478 ? 0.6632 1.0815 0.9114 0.2060  -0.0787 -0.2988 478 LYS D CE  
16271 N NZ  . LYS D  478 ? 0.6763 1.0683 0.9203 0.2199  -0.0933 -0.2981 478 LYS D NZ  
16272 N N   . TYR D  479 ? 0.4266 0.8081 0.6282 0.1559  -0.0571 -0.2729 479 TYR D N   
16273 C CA  . TYR D  479 ? 0.3559 0.7084 0.5381 0.1557  -0.0578 -0.2694 479 TYR D CA  
16274 C C   . TYR D  479 ? 0.3181 0.6420 0.4905 0.1548  -0.0675 -0.2604 479 TYR D C   
16275 O O   . TYR D  479 ? 0.2979 0.5932 0.4597 0.1627  -0.0762 -0.2583 479 TYR D O   
16276 C CB  . TYR D  479 ? 0.3442 0.7075 0.5191 0.1435  -0.0453 -0.2690 479 TYR D CB  
16277 C CG  . TYR D  479 ? 0.4046 0.7875 0.5816 0.1447  -0.0356 -0.2773 479 TYR D CG  
16278 C CD1 . TYR D  479 ? 0.4589 0.8458 0.6428 0.1579  -0.0387 -0.2850 479 TYR D CD1 
16279 C CD2 . TYR D  479 ? 0.4318 0.8290 0.6027 0.1327  -0.0233 -0.2774 479 TYR D CD2 
16280 C CE1 . TYR D  479 ? 0.4873 0.8933 0.6731 0.1597  -0.0295 -0.2931 479 TYR D CE1 
16281 C CE2 . TYR D  479 ? 0.4625 0.8781 0.6340 0.1333  -0.0139 -0.2847 479 TYR D CE2 
16282 C CZ  . TYR D  479 ? 0.4838 0.9043 0.6634 0.1471  -0.0170 -0.2928 479 TYR D CZ  
16283 O OH  . TYR D  479 ? 0.5018 0.9411 0.6818 0.1483  -0.0075 -0.3006 479 TYR D OH  
16284 N N   . TRP D  480 ? 0.3364 0.6690 0.5129 0.1448  -0.0660 -0.2551 480 TRP D N   
16285 C CA  . TRP D  480 ? 0.3156 0.6243 0.4825 0.1421  -0.0735 -0.2463 480 TRP D CA  
16286 C C   . TRP D  480 ? 0.3265 0.6145 0.4921 0.1518  -0.0864 -0.2436 480 TRP D C   
16287 O O   . TRP D  480 ? 0.3109 0.5704 0.4627 0.1546  -0.0933 -0.2386 480 TRP D O   
16288 C CB  . TRP D  480 ? 0.2456 0.5710 0.4201 0.1305  -0.0704 -0.2417 480 TRP D CB  
16289 C CG  . TRP D  480 ? 0.2357 0.5577 0.3990 0.1195  -0.0638 -0.2373 480 TRP D CG  
16290 C CD1 . TRP D  480 ? 0.2287 0.5320 0.3797 0.1093  -0.0679 -0.2257 480 TRP D CD1 
16291 C CD2 . TRP D  480 ? 0.3032 0.6310 0.4572 0.1128  -0.0526 -0.2399 480 TRP D CD2 
16292 N NE1 . TRP D  480 ? 0.2893 0.5860 0.4246 0.0974  -0.0605 -0.2209 480 TRP D NE1 
16293 C CE2 . TRP D  480 ? 0.3079 0.6188 0.4441 0.0988  -0.0512 -0.2290 480 TRP D CE2 
16294 C CE3 . TRP D  480 ? 0.2496 0.5931 0.4064 0.1166  -0.0442 -0.2493 480 TRP D CE3 
16295 C CZ2 . TRP D  480 ? 0.3300 0.6403 0.4520 0.0894  -0.0421 -0.2279 480 TRP D CZ2 
16296 C CZ3 . TRP D  480 ? 0.2522 0.5977 0.3958 0.1078  -0.0340 -0.2499 480 TRP D CZ3 
16297 C CH2 . TRP D  480 ? 0.3545 0.6819 0.4799 0.0936  -0.0336 -0.2381 480 TRP D CH2 
16298 N N   . THR D  481 ? 0.3671 0.6700 0.5466 0.1562  -0.0894 -0.2466 481 THR D N   
16299 C CA  . THR D  481 ? 0.4149 0.6985 0.5922 0.1652  -0.1015 -0.2441 481 THR D CA  
16300 C C   . THR D  481 ? 0.4910 0.7553 0.6605 0.1774  -0.1073 -0.2481 481 THR D C   
16301 O O   . THR D  481 ? 0.5102 0.7485 0.6705 0.1835  -0.1178 -0.2441 481 THR D O   
16302 C CB  . THR D  481 ? 0.4096 0.7138 0.6033 0.1667  -0.1033 -0.2461 481 THR D CB  
16303 O OG1 . THR D  481 ? 0.4271 0.7568 0.6336 0.1717  -0.0975 -0.2557 481 THR D OG1 
16304 C CG2 . THR D  481 ? 0.3791 0.6985 0.5790 0.1534  -0.0990 -0.2406 481 THR D CG2 
16305 N N   . ASN D  482 ? 0.5422 0.8184 0.7144 0.1807  -0.1005 -0.2557 482 ASN D N   
16306 C CA  . ASN D  482 ? 0.5722 0.8271 0.7345 0.1912  -0.1055 -0.2589 482 ASN D CA  
16307 C C   . ASN D  482 ? 0.5667 0.7907 0.7100 0.1875  -0.1085 -0.2519 482 ASN D C   
16308 O O   . ASN D  482 ? 0.5477 0.7440 0.6801 0.1946  -0.1179 -0.2498 482 ASN D O   
16309 C CB  . ASN D  482 ? 0.6488 0.9223 0.8163 0.1945  -0.0967 -0.2682 482 ASN D CB  
16310 C CG  . ASN D  482 ? 0.7267 1.0206 0.9097 0.2048  -0.0983 -0.2765 482 ASN D CG  
16311 O OD1 . ASN D  482 ? 0.7587 1.0472 0.9463 0.2114  -0.1077 -0.2755 482 ASN D OD1 
16312 N ND2 . ASN D  482 ? 0.7480 1.0658 0.9385 0.2064  -0.0889 -0.2850 482 ASN D ND2 
16313 N N   . PHE D  483 ? 0.6975 0.9264 0.8364 0.1760  -0.1004 -0.2481 483 PHE D N   
16314 C CA  . PHE D  483 ? 0.6685 0.8704 0.7900 0.1713  -0.1025 -0.2409 483 PHE D CA  
16315 C C   . PHE D  483 ? 0.6641 0.8465 0.7805 0.1724  -0.1133 -0.2336 483 PHE D C   
16316 O O   . PHE D  483 ? 0.7023 0.8568 0.8054 0.1756  -0.1207 -0.2296 483 PHE D O   
16317 C CB  . PHE D  483 ? 0.4982 0.7097 0.6157 0.1587  -0.0922 -0.2380 483 PHE D CB  
16318 C CG  . PHE D  483 ? 0.5032 0.6881 0.6027 0.1529  -0.0943 -0.2300 483 PHE D CG  
16319 C CD1 . PHE D  483 ? 0.5299 0.6950 0.6159 0.1539  -0.0943 -0.2296 483 PHE D CD1 
16320 C CD2 . PHE D  483 ? 0.4902 0.6697 0.5857 0.1462  -0.0963 -0.2228 483 PHE D CD2 
16321 C CE1 . PHE D  483 ? 0.5357 0.6776 0.6053 0.1471  -0.0959 -0.2215 483 PHE D CE1 
16322 C CE2 . PHE D  483 ? 0.4900 0.6464 0.5684 0.1400  -0.0979 -0.2148 483 PHE D CE2 
16323 C CZ  . PHE D  483 ? 0.5132 0.6517 0.5794 0.1399  -0.0975 -0.2138 483 PHE D CZ  
16324 N N   . ALA D  484 ? 0.5426 0.7398 0.6690 0.1691  -0.1138 -0.2317 484 ALA D N   
16325 C CA  . ALA D  484 ? 0.5220 0.7030 0.6434 0.1690  -0.1230 -0.2244 484 ALA D CA  
16326 C C   . ALA D  484 ? 0.5962 0.7553 0.7119 0.1797  -0.1344 -0.2244 484 ALA D C   
16327 O O   . ALA D  484 ? 0.6103 0.7435 0.7126 0.1804  -0.1423 -0.2181 484 ALA D O   
16328 C CB  . ALA D  484 ? 0.2827 0.4840 0.4167 0.1642  -0.1213 -0.2231 484 ALA D CB  
16329 N N   . ARG D  485 ? 0.4718 0.6419 0.5972 0.1882  -0.1352 -0.2318 485 ARG D N   
16330 C CA  . ARG D  485 ? 0.4951 0.6479 0.6172 0.1997  -0.1462 -0.2332 485 ARG D CA  
16331 C C   . ARG D  485 ? 0.4944 0.6200 0.6016 0.2050  -0.1507 -0.2334 485 ARG D C   
16332 O O   . ARG D  485 ? 0.4925 0.5892 0.5856 0.2068  -0.1603 -0.2275 485 ARG D O   
16333 C CB  . ARG D  485 ? 0.7644 0.9418 0.9034 0.2072  -0.1445 -0.2419 485 ARG D CB  
16334 C CG  . ARG D  485 ? 0.8822 1.0463 1.0205 0.2201  -0.1559 -0.2444 485 ARG D CG  
16335 C CD  . ARG D  485 ? 0.9736 1.1649 1.1290 0.2285  -0.1525 -0.2548 485 ARG D CD  
16336 N NE  . ARG D  485 ? 1.0261 1.2530 1.1968 0.2202  -0.1396 -0.2585 485 ARG D NE  
16337 C CZ  . ARG D  485 ? 1.0441 1.2934 1.2278 0.2141  -0.1366 -0.2570 485 ARG D CZ  
16338 N NH1 . ARG D  485 ? 1.0396 1.2797 1.2231 0.2155  -0.1452 -0.2518 485 ARG D NH1 
16339 N NH2 . ARG D  485 ? 1.0290 1.3093 1.2250 0.2060  -0.1249 -0.2603 485 ARG D NH2 
16340 N N   . THR D  486 ? 0.5595 0.6937 0.6690 0.2072  -0.1438 -0.2402 486 THR D N   
16341 C CA  . THR D  486 ? 0.5884 0.6970 0.6838 0.2123  -0.1473 -0.2414 486 THR D CA  
16342 C C   . THR D  486 ? 0.5293 0.6248 0.6114 0.2028  -0.1417 -0.2369 486 THR D C   
16343 O O   . THR D  486 ? 0.5331 0.6014 0.6005 0.2051  -0.1462 -0.2357 486 THR D O   
16344 C CB  . THR D  486 ? 0.8633 0.9858 0.9663 0.2209  -0.1430 -0.2520 486 THR D CB  
16345 O OG1 . THR D  486 ? 0.8383 0.9805 0.9447 0.2129  -0.1296 -0.2548 486 THR D OG1 
16346 C CG2 . THR D  486 ? 0.9433 1.0890 1.0635 0.2292  -0.1449 -0.2583 486 THR D CG2 
16347 N N   . GLY D  487 ? 0.4799 0.5930 0.5659 0.1918  -0.1321 -0.2342 487 GLY D N   
16348 C CA  . GLY D  487 ? 0.4553 0.5598 0.5293 0.1822  -0.1251 -0.2307 487 GLY D CA  
16349 C C   . GLY D  487 ? 0.4660 0.5824 0.5410 0.1816  -0.1153 -0.2374 487 GLY D C   
16350 O O   . GLY D  487 ? 0.4227 0.5268 0.4850 0.1753  -0.1111 -0.2352 487 GLY D O   
16351 N N   . ASP D  488 ? 0.6474 0.7879 0.7368 0.1880  -0.1117 -0.2459 488 ASP D N   
16352 C CA  . ASP D  488 ? 0.6864 0.8422 0.7776 0.1875  -0.1015 -0.2530 488 ASP D CA  
16353 C C   . ASP D  488 ? 0.6199 0.8129 0.7296 0.1859  -0.0940 -0.2579 488 ASP D C   
16354 O O   . ASP D  488 ? 0.6537 0.8576 0.7758 0.1925  -0.0990 -0.2605 488 ASP D O   
16355 C CB  . ASP D  488 ? 0.8151 0.9578 0.9031 0.2004  -0.1069 -0.2602 488 ASP D CB  
16356 C CG  . ASP D  488 ? 0.9075 1.0628 0.9951 0.2014  -0.0971 -0.2683 488 ASP D CG  
16357 O OD1 . ASP D  488 ? 0.9340 1.1204 1.0328 0.1969  -0.0868 -0.2721 488 ASP D OD1 
16358 O OD2 . ASP D  488 ? 0.9437 1.0772 1.0191 0.2067  -0.0999 -0.2711 488 ASP D OD2 
16359 N N   . PRO D  489 ? 0.4318 0.6441 0.5426 0.1767  -0.0820 -0.2593 489 PRO D N   
16360 C CA  . PRO D  489 ? 0.4249 0.6733 0.5527 0.1734  -0.0743 -0.2637 489 PRO D CA  
16361 C C   . PRO D  489 ? 0.4861 0.7557 0.6273 0.1836  -0.0726 -0.2742 489 PRO D C   
16362 O O   . PRO D  489 ? 0.4947 0.7890 0.6521 0.1841  -0.0717 -0.2768 489 PRO D O   
16363 C CB  . PRO D  489 ? 0.3256 0.5848 0.4470 0.1605  -0.0622 -0.2621 489 PRO D CB  
16364 C CG  . PRO D  489 ? 0.3354 0.5663 0.4374 0.1593  -0.0631 -0.2590 489 PRO D CG  
16365 C CD  . PRO D  489 ? 0.3416 0.5427 0.4373 0.1660  -0.0759 -0.2543 489 PRO D CD  
16366 N N   . ASN D  490 ? 0.4879 0.7486 0.6226 0.1915  -0.0720 -0.2801 490 ASN D N   
16367 C CA  . ASN D  490 ? 0.5335 0.8180 0.6807 0.2007  -0.0685 -0.2909 490 ASN D CA  
16368 C C   . ASN D  490 ? 0.6397 0.9213 0.7963 0.2147  -0.0794 -0.2947 490 ASN D C   
16369 O O   . ASN D  490 ? 0.6165 0.8696 0.7654 0.2196  -0.0912 -0.2897 490 ASN D O   
16370 C CB  . ASN D  490 ? 0.5172 0.7991 0.6552 0.2039  -0.0618 -0.2977 490 ASN D CB  
16371 C CG  . ASN D  490 ? 0.4665 0.7133 0.5831 0.2005  -0.0645 -0.2920 490 ASN D CG  
16372 O OD1 . ASN D  490 ? 0.4106 0.6583 0.5175 0.1906  -0.0558 -0.2902 490 ASN D OD1 
16373 N ND2 . ASN D  490 ? 0.4876 0.7032 0.5960 0.2080  -0.0767 -0.2890 490 ASN D ND2 
16374 N N   . ASP D  491 ? 0.9133 1.2254 1.0860 0.2206  -0.0752 -0.3035 491 ASP D N   
16375 C CA  . ASP D  491 ? 1.0174 1.3321 1.2006 0.2349  -0.0844 -0.3089 491 ASP D CA  
16376 C C   . ASP D  491 ? 1.0569 1.3404 1.2278 0.2488  -0.0939 -0.3123 491 ASP D C   
16377 O O   . ASP D  491 ? 1.0615 1.3407 1.2245 0.2519  -0.0889 -0.3178 491 ASP D O   
16378 C CB  . ASP D  491 ? 1.1911 1.5475 1.3935 0.2379  -0.0760 -0.3187 491 ASP D CB  
16379 C CG  . ASP D  491 ? 1.2511 1.6285 1.4710 0.2375  -0.0794 -0.3177 491 ASP D CG  
16380 O OD1 . ASP D  491 ? 1.2762 1.6376 1.4969 0.2475  -0.0918 -0.3167 491 ASP D OD1 
16381 O OD2 . ASP D  491 ? 1.2624 1.6719 1.4943 0.2267  -0.0697 -0.3178 491 ASP D OD2 
16382 N N   . PRO D  492 ? 0.9929 1.2531 1.1606 0.2569  -0.1077 -0.3089 492 PRO D N   
16383 C CA  . PRO D  492 ? 1.0461 1.2731 1.2008 0.2699  -0.1186 -0.3112 492 PRO D CA  
16384 C C   . PRO D  492 ? 1.1025 1.3445 1.2658 0.2850  -0.1180 -0.3241 492 PRO D C   
16385 O O   . PRO D  492 ? 1.0945 1.3193 1.2465 0.2922  -0.1187 -0.3291 492 PRO D O   
16386 C CB  . PRO D  492 ? 1.0716 1.2793 1.2248 0.2738  -0.1326 -0.3047 492 PRO D CB  
16387 C CG  . PRO D  492 ? 1.0289 1.2541 1.1907 0.2606  -0.1284 -0.2973 492 PRO D CG  
16388 C CD  . PRO D  492 ? 1.0051 1.2703 1.1817 0.2542  -0.1139 -0.3031 492 PRO D CD  
16389 N N   . ARG D  493 ? 1.3365 1.6110 1.5196 0.2895  -0.1164 -0.3296 493 ARG D N   
16390 C CA  . ARG D  493 ? 1.4168 1.7096 1.6106 0.3049  -0.1163 -0.3423 493 ARG D CA  
16391 C C   . ARG D  493 ? 1.4826 1.8014 1.6802 0.3023  -0.1015 -0.3505 493 ARG D C   
16392 O O   . ARG D  493 ? 1.5356 1.8479 1.7280 0.3139  -0.1018 -0.3593 493 ARG D O   
16393 C CB  . ARG D  493 ? 1.2562 1.5775 1.4708 0.3102  -0.1191 -0.3456 493 ARG D CB  
16394 C CG  . ARG D  493 ? 1.2639 1.5603 1.4752 0.3178  -0.1352 -0.3406 493 ARG D CG  
16395 C CD  . ARG D  493 ? 1.2488 1.5525 1.4658 0.3047  -0.1353 -0.3307 493 ARG D CD  
16396 N NE  . ARG D  493 ? 1.2371 1.5779 1.4671 0.2910  -0.1204 -0.3310 493 ARG D NE  
16397 C CZ  . ARG D  493 ? 1.2354 1.6161 1.4864 0.2912  -0.1145 -0.3368 493 ARG D CZ  
16398 N NH1 . ARG D  493 ? 1.2434 1.6336 1.5061 0.3053  -0.1222 -0.3432 493 ARG D NH1 
16399 N NH2 . ARG D  493 ? 1.2150 1.6261 1.4750 0.2770  -0.1011 -0.3361 493 ARG D NH2 
16400 N N   . ASP D  494 ? 1.3989 1.7452 1.6037 0.2869  -0.0888 -0.3476 494 ASP D N   
16401 C CA  . ASP D  494 ? 1.3927 1.7660 1.6012 0.2845  -0.0747 -0.3557 494 ASP D CA  
16402 C C   . ASP D  494 ? 1.3977 1.7408 1.5843 0.2780  -0.0724 -0.3510 494 ASP D C   
16403 O O   . ASP D  494 ? 1.3649 1.7052 1.5449 0.2623  -0.0668 -0.3423 494 ASP D O   
16404 C CB  . ASP D  494 ? 1.2497 1.6621 1.4720 0.2689  -0.0620 -0.3535 494 ASP D CB  
16405 C CG  . ASP D  494 ? 1.2132 1.6444 1.4532 0.2679  -0.0668 -0.3509 494 ASP D CG  
16406 O OD1 . ASP D  494 ? 1.2094 1.6186 1.4481 0.2764  -0.0803 -0.3479 494 ASP D OD1 
16407 O OD2 . ASP D  494 ? 1.1825 1.6502 1.4368 0.2577  -0.0569 -0.3515 494 ASP D OD2 
16408 N N   . SER D  495 ? 1.4729 1.7941 1.6482 0.2903  -0.0767 -0.3574 495 SER D N   
16409 C CA  . SER D  495 ? 1.5068 1.7961 1.6602 0.2855  -0.0759 -0.3538 495 SER D CA  
16410 C C   . SER D  495 ? 1.5310 1.8421 1.6831 0.2822  -0.0614 -0.3614 495 SER D C   
16411 O O   . SER D  495 ? 1.5181 1.8108 1.6529 0.2755  -0.0570 -0.3592 495 SER D O   
16412 C CB  . SER D  495 ? 1.4373 1.6856 1.5762 0.2991  -0.0896 -0.3553 495 SER D CB  
16413 O OG  . SER D  495 ? 1.4096 1.6212 1.5290 0.2899  -0.0939 -0.3450 495 SER D OG  
16414 N N   . LYS D  496 ? 1.5614 1.9124 1.7315 0.2868  -0.0539 -0.3705 496 LYS D N   
16415 C CA  . LYS D  496 ? 1.5299 1.9108 1.7018 0.2768  -0.0378 -0.3741 496 LYS D CA  
16416 C C   . LYS D  496 ? 1.4714 1.8895 1.6607 0.2641  -0.0303 -0.3701 496 LYS D C   
16417 O O   . LYS D  496 ? 1.4446 1.8946 1.6535 0.2694  -0.0291 -0.3760 496 LYS D O   
16418 C CB  . LYS D  496 ? 1.4095 1.8068 1.5839 0.2898  -0.0321 -0.3886 496 LYS D CB  
16419 C CG  . LYS D  496 ? 1.3965 1.8034 1.5596 0.2803  -0.0175 -0.3913 496 LYS D CG  
16420 C CD  . LYS D  496 ? 1.3949 1.7599 1.5324 0.2740  -0.0199 -0.3845 496 LYS D CD  
16421 C CE  . LYS D  496 ? 0.8506 1.2124 0.9812 0.2532  -0.0151 -0.3713 496 LYS D CE  
16422 N NZ  . LYS D  496 ? 0.8295 1.2260 0.9632 0.2394  0.0008  -0.3718 496 LYS D NZ  
16423 N N   . SER D  497 ? 1.5235 1.9338 1.7041 0.2472  -0.0264 -0.3594 497 SER D N   
16424 C CA  . SER D  497 ? 1.4600 1.8997 1.6476 0.2299  -0.0152 -0.3547 497 SER D CA  
16425 C C   . SER D  497 ? 1.4512 1.8607 1.6160 0.2202  -0.0133 -0.3473 497 SER D C   
16426 O O   . SER D  497 ? 1.5088 1.8814 1.6602 0.2272  -0.0229 -0.3452 497 SER D O   
16427 C CB  . SER D  497 ? 1.1268 1.5720 1.3267 0.2245  -0.0213 -0.3472 497 SER D CB  
16428 O OG  . SER D  497 ? 1.0850 1.5613 1.2929 0.2082  -0.0104 -0.3438 497 SER D OG  
16429 N N   . PRO D  498 ? 1.1938 1.6174 1.3529 0.2041  -0.0015 -0.3434 498 PRO D N   
16430 C CA  . PRO D  498 ? 1.1143 1.5058 1.2504 0.1967  -0.0014 -0.3367 498 PRO D CA  
16431 C C   . PRO D  498 ? 1.0306 1.3889 1.1598 0.1944  -0.0130 -0.3259 498 PRO D C   
16432 O O   . PRO D  498 ? 0.9902 1.3563 1.1287 0.1879  -0.0155 -0.3195 498 PRO D O   
16433 C CB  . PRO D  498 ? 1.0063 1.4203 1.1383 0.1792  0.0125  -0.3335 498 PRO D CB  
16434 C CG  . PRO D  498 ? 1.0216 1.4727 1.1747 0.1740  0.0165  -0.3340 498 PRO D CG  
16435 C CD  . PRO D  498 ? 1.0673 1.5307 1.2375 0.1909  0.0108  -0.3434 498 PRO D CD  
16436 N N   . GLN D  499 ? 1.0171 1.3386 1.1295 0.1996  -0.0202 -0.3243 499 GLN D N   
16437 C CA  . GLN D  499 ? 0.9519 1.2405 1.0564 0.1984  -0.0316 -0.3147 499 GLN D CA  
16438 C C   . GLN D  499 ? 0.8736 1.1542 0.9663 0.1817  -0.0274 -0.3043 499 GLN D C   
16439 O O   . GLN D  499 ? 0.8805 1.1649 0.9622 0.1732  -0.0181 -0.3045 499 GLN D O   
16440 C CB  . GLN D  499 ? 0.9132 1.1656 1.0036 0.2094  -0.0409 -0.3171 499 GLN D CB  
16441 C CG  . GLN D  499 ? 0.9569 1.1881 1.0510 0.2197  -0.0556 -0.3147 499 GLN D CG  
16442 C CD  . GLN D  499 ? 1.0298 1.2824 1.1426 0.2334  -0.0589 -0.3233 499 GLN D CD  
16443 O OE1 . GLN D  499 ? 1.0737 1.3598 1.1986 0.2347  -0.0497 -0.3310 499 GLN D OE1 
16444 N NE2 . GLN D  499 ? 1.0396 1.2730 1.1541 0.2435  -0.0722 -0.3219 499 GLN D NE2 
16445 N N   . TRP D  500 ? 0.7349 1.0040 0.8292 0.1773  -0.0345 -0.2953 500 TRP D N   
16446 C CA  . TRP D  500 ? 0.6199 0.8786 0.7028 0.1630  -0.0323 -0.2851 500 TRP D CA  
16447 C C   . TRP D  500 ? 0.5809 0.8007 0.6455 0.1641  -0.0401 -0.2803 500 TRP D C   
16448 O O   . TRP D  500 ? 0.6121 0.8112 0.6765 0.1701  -0.0510 -0.2770 500 TRP D O   
16449 C CB  . TRP D  500 ? 0.5883 0.8557 0.6830 0.1587  -0.0362 -0.2789 500 TRP D CB  
16450 C CG  . TRP D  500 ? 0.5613 0.8235 0.6474 0.1446  -0.0338 -0.2692 500 TRP D CG  
16451 C CD1 . TRP D  500 ? 0.5896 0.8297 0.6570 0.1368  -0.0332 -0.2627 500 TRP D CD1 
16452 C CD2 . TRP D  500 ? 0.5044 0.7837 0.6003 0.1369  -0.0322 -0.2650 500 TRP D CD2 
16453 N NE1 . TRP D  500 ? 0.5814 0.8236 0.6460 0.1253  -0.0316 -0.2546 500 TRP D NE1 
16454 C CE2 . TRP D  500 ? 0.5309 0.7964 0.6124 0.1253  -0.0308 -0.2562 500 TRP D CE2 
16455 C CE3 . TRP D  500 ? 0.4572 0.7620 0.5722 0.1385  -0.0321 -0.2679 500 TRP D CE3 
16456 C CZ2 . TRP D  500 ? 0.4898 0.7648 0.5745 0.1161  -0.0294 -0.2509 500 TRP D CZ2 
16457 C CZ3 . TRP D  500 ? 0.4283 0.7431 0.5471 0.1286  -0.0304 -0.2627 500 TRP D CZ3 
16458 C CH2 . TRP D  500 ? 0.4376 0.7371 0.5410 0.1179  -0.0290 -0.2546 500 TRP D CH2 
16459 N N   . PRO D  501 ? 0.4170 0.6266 0.4651 0.1576  -0.0346 -0.2797 501 PRO D N   
16460 C CA  . PRO D  501 ? 0.4322 0.6061 0.4621 0.1573  -0.0413 -0.2758 501 PRO D CA  
16461 C C   . PRO D  501 ? 0.5135 0.6718 0.5380 0.1481  -0.0466 -0.2640 501 PRO D C   
16462 O O   . PRO D  501 ? 0.5296 0.7036 0.5582 0.1389  -0.0419 -0.2588 501 PRO D O   
16463 C CB  . PRO D  501 ? 0.4940 0.6679 0.5089 0.1501  -0.0324 -0.2779 501 PRO D CB  
16464 C CG  . PRO D  501 ? 0.4896 0.6987 0.5155 0.1504  -0.0215 -0.2852 501 PRO D CG  
16465 C CD  . PRO D  501 ? 0.4687 0.6996 0.5132 0.1494  -0.0220 -0.2826 501 PRO D CD  
16466 N N   . PRO D  502 ? 0.7763 0.9039 0.7907 0.1501  -0.0562 -0.2599 502 PRO D N   
16467 C CA  . PRO D  502 ? 0.7838 0.8974 0.7904 0.1396  -0.0596 -0.2486 502 PRO D CA  
16468 C C   . PRO D  502 ? 0.7657 0.8802 0.7592 0.1271  -0.0521 -0.2448 502 PRO D C   
16469 O O   . PRO D  502 ? 0.8399 0.9575 0.8264 0.1272  -0.0462 -0.2508 502 PRO D O   
16470 C CB  . PRO D  502 ? 0.8434 0.9241 0.8393 0.1437  -0.0702 -0.2467 502 PRO D CB  
16471 C CG  . PRO D  502 ? 0.8891 0.9624 0.8797 0.1523  -0.0698 -0.2564 502 PRO D CG  
16472 C CD  . PRO D  502 ? 0.8765 0.9800 0.8836 0.1603  -0.0637 -0.2650 502 PRO D CD  
16473 N N   . TYR D  503 ? 0.4446 0.5569 0.4343 0.1167  -0.0525 -0.2351 503 TYR D N   
16474 C CA  . TYR D  503 ? 0.4109 0.5206 0.3867 0.1050  -0.0475 -0.2301 503 TYR D CA  
16475 C C   . TYR D  503 ? 0.4635 0.5448 0.4247 0.1010  -0.0545 -0.2248 503 TYR D C   
16476 O O   . TYR D  503 ? 0.4788 0.5486 0.4414 0.1003  -0.0616 -0.2187 503 TYR D O   
16477 C CB  . TYR D  503 ? 0.4684 0.5932 0.4483 0.0962  -0.0441 -0.2227 503 TYR D CB  
16478 C CG  . TYR D  503 ? 0.4935 0.6136 0.4588 0.0842  -0.0411 -0.2156 503 TYR D CG  
16479 C CD1 . TYR D  503 ? 0.5170 0.6182 0.4728 0.0785  -0.0470 -0.2072 503 TYR D CD1 
16480 C CD2 . TYR D  503 ? 0.5299 0.6656 0.4908 0.0784  -0.0326 -0.2172 503 TYR D CD2 
16481 C CE1 . TYR D  503 ? 0.5439 0.6419 0.4872 0.0683  -0.0452 -0.2007 503 TYR D CE1 
16482 C CE2 . TYR D  503 ? 0.5781 0.7083 0.5245 0.0680  -0.0310 -0.2103 503 TYR D CE2 
16483 C CZ  . TYR D  503 ? 0.5755 0.6870 0.5138 0.0635  -0.0376 -0.2022 503 TYR D CZ  
16484 O OH  . TYR D  503 ? 0.5777 0.6848 0.5027 0.0541  -0.0369 -0.1955 503 TYR D OH  
16485 N N   . THR D  504 ? 0.5852 0.6558 0.5320 0.0978  -0.0526 -0.2275 504 THR D N   
16486 C CA  . THR D  504 ? 0.6081 0.6531 0.5402 0.0923  -0.0589 -0.2234 504 THR D CA  
16487 C C   . THR D  504 ? 0.5829 0.6276 0.5013 0.0808  -0.0549 -0.2193 504 THR D C   
16488 O O   . THR D  504 ? 0.5778 0.6380 0.4949 0.0788  -0.0472 -0.2217 504 THR D O   
16489 C CB  . THR D  504 ? 0.7951 0.8217 0.7204 0.1000  -0.0628 -0.2317 504 THR D CB  
16490 O OG1 . THR D  504 ? 0.8038 0.8414 0.7272 0.1039  -0.0553 -0.2407 504 THR D OG1 
16491 C CG2 . THR D  504 ? 0.8401 0.8613 0.7765 0.1114  -0.0695 -0.2345 504 THR D CG2 
16492 N N   . THR D  505 ? 0.6498 0.6773 0.5573 0.0730  -0.0603 -0.2132 505 THR D N   
16493 C CA  . THR D  505 ? 0.7022 0.7306 0.5976 0.0622  -0.0578 -0.2086 505 THR D CA  
16494 C C   . THR D  505 ? 0.7738 0.7987 0.6571 0.0627  -0.0537 -0.2166 505 THR D C   
16495 O O   . THR D  505 ? 0.8003 0.8339 0.6760 0.0569  -0.0485 -0.2154 505 THR D O   
16496 C CB  . THR D  505 ? 0.6847 0.6980 0.5719 0.0534  -0.0647 -0.2011 505 THR D CB  
16497 O OG1 . THR D  505 ? 0.7038 0.7049 0.5962 0.0574  -0.0716 -0.2005 505 THR D OG1 
16498 C CG2 . THR D  505 ? 0.6513 0.6768 0.5410 0.0457  -0.0636 -0.1910 505 THR D CG2 
16499 N N   . ALA D  506 ? 0.7556 0.7664 0.6358 0.0699  -0.0564 -0.2249 506 ALA D N   
16500 C CA  . ALA D  506 ? 0.7462 0.7530 0.6151 0.0720  -0.0525 -0.2339 506 ALA D CA  
16501 C C   . ALA D  506 ? 0.7049 0.7358 0.5796 0.0759  -0.0426 -0.2387 506 ALA D C   
16502 O O   . ALA D  506 ? 0.6859 0.7256 0.5521 0.0687  -0.0373 -0.2366 506 ALA D O   
16503 C CB  . ALA D  506 ? 0.8019 0.7899 0.6687 0.0813  -0.0576 -0.2424 506 ALA D CB  
16504 N N   . ALA D  507 ? 0.7064 0.7490 0.5960 0.0869  -0.0406 -0.2446 507 ALA D N   
16505 C CA  . ALA D  507 ? 0.7153 0.7819 0.6114 0.0915  -0.0311 -0.2516 507 ALA D CA  
16506 C C   . ALA D  507 ? 0.6818 0.7725 0.5867 0.0855  -0.0252 -0.2454 507 ALA D C   
16507 O O   . ALA D  507 ? 0.6697 0.7779 0.5720 0.0828  -0.0166 -0.2483 507 ALA D O   
16508 C CB  . ALA D  507 ? 0.8037 0.8746 0.7129 0.1059  -0.0319 -0.2609 507 ALA D CB  
16509 N N   . GLN D  508 ? 0.6240 0.7144 0.5382 0.0833  -0.0301 -0.2372 508 GLN D N   
16510 C CA  . GLN D  508 ? 0.5519 0.6612 0.4743 0.0774  -0.0265 -0.2306 508 GLN D CA  
16511 C C   . GLN D  508 ? 0.4986 0.6348 0.4340 0.0818  -0.0187 -0.2371 508 GLN D C   
16512 O O   . GLN D  508 ? 0.4928 0.6452 0.4251 0.0748  -0.0114 -0.2358 508 GLN D O   
16513 C CB  . GLN D  508 ? 0.6762 0.7846 0.5838 0.0654  -0.0240 -0.2235 508 GLN D CB  
16514 C CG  . GLN D  508 ? 0.7595 0.8451 0.6532 0.0598  -0.0307 -0.2180 508 GLN D CG  
16515 C CD  . GLN D  508 ? 0.8451 0.9322 0.7258 0.0491  -0.0288 -0.2110 508 GLN D CD  
16516 O OE1 . GLN D  508 ? 0.8749 0.9768 0.7589 0.0452  -0.0249 -0.2068 508 GLN D OE1 
16517 N NE2 . GLN D  508 ? 0.8708 0.9423 0.7358 0.0440  -0.0321 -0.2097 508 GLN D NE2 
16518 N N   . GLN D  509 ? 0.4940 0.6356 0.4438 0.0930  -0.0204 -0.2439 509 GLN D N   
16519 C CA  . GLN D  509 ? 0.4891 0.6592 0.4530 0.0971  -0.0131 -0.2507 509 GLN D CA  
16520 C C   . GLN D  509 ? 0.4700 0.6550 0.4516 0.0977  -0.0149 -0.2474 509 GLN D C   
16521 O O   . GLN D  509 ? 0.4797 0.6532 0.4685 0.1028  -0.0234 -0.2446 509 GLN D O   
16522 C CB  . GLN D  509 ? 0.5616 0.7340 0.5303 0.1095  -0.0122 -0.2624 509 GLN D CB  
16523 C CG  . GLN D  509 ? 0.6080 0.7518 0.5717 0.1174  -0.0220 -0.2637 509 GLN D CG  
16524 C CD  . GLN D  509 ? 0.6912 0.8339 0.6544 0.1290  -0.0208 -0.2756 509 GLN D CD  
16525 O OE1 . GLN D  509 ? 0.7070 0.8730 0.6754 0.1317  -0.0122 -0.2832 509 GLN D OE1 
16526 N NE2 . GLN D  509 ? 0.7319 0.8473 0.6882 0.1357  -0.0295 -0.2775 509 GLN D NE2 
16527 N N   . TYR D  510 ? 0.4456 0.6560 0.4327 0.0916  -0.0068 -0.2478 510 TYR D N   
16528 C CA  . TYR D  510 ? 0.4023 0.6304 0.4056 0.0907  -0.0071 -0.2460 510 TYR D CA  
16529 C C   . TYR D  510 ? 0.4087 0.6690 0.4246 0.0926  0.0019  -0.2550 510 TYR D C   
16530 O O   . TYR D  510 ? 0.3767 0.6442 0.3863 0.0928  0.0088  -0.2608 510 TYR D O   
16531 C CB  . TYR D  510 ? 0.4035 0.6301 0.3981 0.0777  -0.0062 -0.2361 510 TYR D CB  
16532 C CG  . TYR D  510 ? 0.4017 0.6403 0.3838 0.0669  0.0034  -0.2356 510 TYR D CG  
16533 C CD1 . TYR D  510 ? 0.3888 0.6119 0.3516 0.0627  0.0044  -0.2334 510 TYR D CD1 
16534 C CD2 . TYR D  510 ? 0.4087 0.6738 0.3970 0.0599  0.0112  -0.2371 510 TYR D CD2 
16535 C CE1 . TYR D  510 ? 0.4097 0.6425 0.3592 0.0526  0.0126  -0.2324 510 TYR D CE1 
16536 C CE2 . TYR D  510 ? 0.4261 0.7011 0.4006 0.0487  0.0199  -0.2359 510 TYR D CE2 
16537 C CZ  . TYR D  510 ? 0.4171 0.6755 0.3720 0.0455  0.0204  -0.2334 510 TYR D CZ  
16538 O OH  . TYR D  510 ? 0.4071 0.6745 0.3467 0.0343  0.0286  -0.2316 510 TYR D OH  
16539 N N   . VAL D  511 ? 0.3669 0.6476 0.4004 0.0937  0.0022  -0.2565 511 VAL D N   
16540 C CA  . VAL D  511 ? 0.3525 0.6669 0.3999 0.0949  0.0109  -0.2650 511 VAL D CA  
16541 C C   . VAL D  511 ? 0.3410 0.6797 0.3921 0.0817  0.0183  -0.2620 511 VAL D C   
16542 O O   . VAL D  511 ? 0.3266 0.6574 0.3755 0.0753  0.0143  -0.2546 511 VAL D O   
16543 C CB  . VAL D  511 ? 0.4390 0.7624 0.5072 0.1088  0.0052  -0.2718 511 VAL D CB  
16544 C CG1 . VAL D  511 ? 0.4821 0.7807 0.5451 0.1217  -0.0023 -0.2753 511 VAL D CG1 
16545 C CG2 . VAL D  511 ? 0.3755 0.6971 0.4545 0.1085  -0.0023 -0.2665 511 VAL D CG2 
16546 N N   . SER D  512 ? 0.3823 0.7506 0.4382 0.0771  0.0292  -0.2678 512 SER D N   
16547 C CA  . SER D  512 ? 0.4022 0.7971 0.4636 0.0638  0.0367  -0.2657 512 SER D CA  
16548 C C   . SER D  512 ? 0.3962 0.8154 0.4840 0.0695  0.0349  -0.2705 512 SER D C   
16549 O O   . SER D  512 ? 0.4125 0.8411 0.5147 0.0821  0.0329  -0.2782 512 SER D O   
16550 C CB  . SER D  512 ? 0.5275 0.9440 0.5799 0.0527  0.0500  -0.2678 512 SER D CB  
16551 O OG  . SER D  512 ? 0.5785 1.0245 0.6476 0.0587  0.0561  -0.2775 512 SER D OG  
16552 N N   . LEU D  513 ? 0.3526 0.7801 0.4456 0.0605  0.0346  -0.2657 513 LEU D N   
16553 C CA  . LEU D  513 ? 0.3407 0.7960 0.4587 0.0621  0.0344  -0.2693 513 LEU D CA  
16554 C C   . LEU D  513 ? 0.3670 0.8538 0.4861 0.0440  0.0468  -0.2680 513 LEU D C   
16555 O O   . LEU D  513 ? 0.3565 0.8362 0.4643 0.0298  0.0477  -0.2592 513 LEU D O   
16556 C CB  . LEU D  513 ? 0.2897 0.7298 0.4142 0.0659  0.0236  -0.2647 513 LEU D CB  
16557 C CG  . LEU D  513 ? 0.3441 0.7475 0.4618 0.0796  0.0109  -0.2627 513 LEU D CG  
16558 C CD1 . LEU D  513 ? 0.3066 0.6947 0.4258 0.0795  0.0018  -0.2567 513 LEU D CD1 
16559 C CD2 . LEU D  513 ? 0.2982 0.7026 0.4289 0.0958  0.0054  -0.2697 513 LEU D CD2 
16560 N N   . ASN D  514 ? 0.5433 1.0606 0.6741 0.0433  0.0547  -0.2744 514 ASN D N   
16561 C CA  . ASN D  514 ? 0.5892 1.1407 0.7238 0.0252  0.0668  -0.2730 514 ASN D CA  
16562 C C   . ASN D  514 ? 0.6070 1.1899 0.7681 0.0319  0.0671  -0.2805 514 ASN D C   
16563 O O   . ASN D  514 ? 0.6218 1.1964 0.7961 0.0491  0.0571  -0.2850 514 ASN D O   
16564 C CB  . ASN D  514 ? 0.5827 1.1368 0.6960 0.0147  0.0779  -0.2723 514 ASN D CB  
16565 C CG  . ASN D  514 ? 0.6351 1.1745 0.7415 0.0301  0.0763  -0.2790 514 ASN D CG  
16566 O OD1 . ASN D  514 ? 0.6534 1.1913 0.7746 0.0475  0.0695  -0.2861 514 ASN D OD1 
16567 N ND2 . ASN D  514 ? 0.6655 1.1927 0.7482 0.0233  0.0820  -0.2764 514 ASN D ND2 
16568 N N   . LEU D  515 ? 0.5546 1.1721 0.7224 0.0180  0.0779  -0.2811 515 LEU D N   
16569 C CA  . LEU D  515 ? 0.5496 1.1979 0.7417 0.0246  0.0782  -0.2886 515 LEU D CA  
16570 C C   . LEU D  515 ? 0.5723 1.2172 0.7665 0.0448  0.0764  -0.2991 515 LEU D C   
16571 O O   . LEU D  515 ? 0.5944 1.2358 0.8034 0.0619  0.0670  -0.3044 515 LEU D O   
16572 C CB  . LEU D  515 ? 0.4257 1.1118 0.6230 0.0042  0.0904  -0.2867 515 LEU D CB  
16573 C CG  . LEU D  515 ? 0.4192 1.1237 0.6353 -0.0065 0.0872  -0.2818 515 LEU D CG  
16574 C CD1 . LEU D  515 ? 0.3196 0.9967 0.5309 -0.0095 0.0782  -0.2732 515 LEU D CD1 
16575 C CD2 . LEU D  515 ? 0.4317 1.1683 0.6472 -0.0313 0.0996  -0.2772 515 LEU D CD2 
16576 N N   . LYS D  516 ? 0.4765 1.1200 0.6544 0.0428  0.0848  -0.3016 516 LYS D N   
16577 C CA  . LYS D  516 ? 0.5058 1.1466 0.6841 0.0606  0.0842  -0.3117 516 LYS D CA  
16578 C C   . LYS D  516 ? 0.5018 1.1031 0.6753 0.0788  0.0706  -0.3122 516 LYS D C   
16579 O O   . LYS D  516 ? 0.5049 1.0808 0.6707 0.0757  0.0637  -0.3043 516 LYS D O   
16580 C CB  . LYS D  516 ? 0.6857 1.3296 0.8444 0.0527  0.0957  -0.3127 516 LYS D CB  
16581 C CG  . LYS D  516 ? 0.7372 1.3501 0.8694 0.0426  0.0959  -0.3035 516 LYS D CG  
16582 C CD  . LYS D  516 ? 0.8034 1.4257 0.9165 0.0296  0.1086  -0.3026 516 LYS D CD  
16583 C CE  . LYS D  516 ? 0.8295 1.4797 0.9423 0.0057  0.1187  -0.2958 516 LYS D CE  
16584 N NZ  . LYS D  516 ? 0.8595 1.5129 0.9487 -0.0093 0.1300  -0.2923 516 LYS D NZ  
16585 N N   . PRO D  517 ? 0.5640 1.1599 0.7417 0.0975  0.0664  -0.3213 517 PRO D N   
16586 C CA  . PRO D  517 ? 0.5684 1.1280 0.7435 0.1140  0.0523  -0.3213 517 PRO D CA  
16587 C C   . PRO D  517 ? 0.5671 1.0867 0.7185 0.1115  0.0483  -0.3140 517 PRO D C   
16588 O O   . PRO D  517 ? 0.5607 1.0777 0.6955 0.0976  0.0561  -0.3089 517 PRO D O   
16589 C CB  . PRO D  517 ? 0.6679 1.2313 0.8476 0.1317  0.0514  -0.3328 517 PRO D CB  
16590 C CG  . PRO D  517 ? 0.6886 1.2968 0.8838 0.1274  0.0619  -0.3394 517 PRO D CG  
16591 C CD  . PRO D  517 ? 0.6659 1.2909 0.8535 0.1047  0.0735  -0.3323 517 PRO D CD  
16592 N N   . LEU D  518 ? 0.5399 1.0278 0.6891 0.1247  0.0357  -0.3131 518 LEU D N   
16593 C CA  . LEU D  518 ? 0.5478 0.9972 0.6761 0.1231  0.0304  -0.3060 518 LEU D CA  
16594 C C   . LEU D  518 ? 0.6290 1.0704 0.7385 0.1212  0.0376  -0.3086 518 LEU D C   
16595 O O   . LEU D  518 ? 0.6553 1.1056 0.7670 0.1307  0.0408  -0.3179 518 LEU D O   
16596 C CB  . LEU D  518 ? 0.5171 0.9356 0.6460 0.1379  0.0161  -0.3057 518 LEU D CB  
16597 C CG  . LEU D  518 ? 0.4586 0.8685 0.5963 0.1376  0.0065  -0.2989 518 LEU D CG  
16598 C CD1 . LEU D  518 ? 0.4305 0.8010 0.5586 0.1477  -0.0063 -0.2956 518 LEU D CD1 
16599 C CD2 . LEU D  518 ? 0.4407 0.8549 0.5727 0.1205  0.0114  -0.2903 518 LEU D CD2 
16600 N N   . GLU D  519 ? 0.8493 1.2730 0.9395 0.1093  0.0398  -0.3005 519 GLU D N   
16601 C CA  . GLU D  519 ? 0.8969 1.3097 0.9663 0.1057  0.0458  -0.3013 519 GLU D CA  
16602 C C   . GLU D  519 ? 0.7705 1.1433 0.8214 0.1045  0.0375  -0.2931 519 GLU D C   
16603 O O   . GLU D  519 ? 0.7478 1.1118 0.7937 0.0946  0.0351  -0.2838 519 GLU D O   
16604 C CB  . GLU D  519 ? 1.0903 1.5277 1.1530 0.0884  0.0588  -0.2986 519 GLU D CB  
16605 C CG  . GLU D  519 ? 1.1669 1.5937 1.2056 0.0821  0.0655  -0.2980 519 GLU D CG  
16606 C CD  . GLU D  519 ? 1.2146 1.6612 1.2438 0.0628  0.0766  -0.2925 519 GLU D CD  
16607 O OE1 . GLU D  519 ? 1.2326 1.7091 1.2767 0.0553  0.0818  -0.2923 519 GLU D OE1 
16608 O OE2 . GLU D  519 ? 1.2301 1.6614 1.2361 0.0545  0.0796  -0.2879 519 GLU D OE2 
16609 N N   . VAL D  520 ? 0.4404 0.7886 0.4809 0.1142  0.0327  -0.2966 520 VAL D N   
16610 C CA  . VAL D  520 ? 0.4217 0.7329 0.4456 0.1124  0.0244  -0.2887 520 VAL D CA  
16611 C C   . VAL D  520 ? 0.4288 0.7310 0.4297 0.0999  0.0303  -0.2838 520 VAL D C   
16612 O O   . VAL D  520 ? 0.4479 0.7570 0.4399 0.0999  0.0377  -0.2898 520 VAL D O   
16613 C CB  . VAL D  520 ? 0.4364 0.7218 0.4577 0.1267  0.0153  -0.2934 520 VAL D CB  
16614 C CG1 . VAL D  520 ? 0.4322 0.6815 0.4380 0.1231  0.0064  -0.2845 520 VAL D CG1 
16615 C CG2 . VAL D  520 ? 0.4327 0.7267 0.4751 0.1393  0.0088  -0.2981 520 VAL D CG2 
16616 N N   . ARG D  521 ? 0.4147 0.7018 0.4058 0.0897  0.0268  -0.2730 521 ARG D N   
16617 C CA  . ARG D  521 ? 0.4212 0.6973 0.3899 0.0779  0.0303  -0.2670 521 ARG D CA  
16618 C C   . ARG D  521 ? 0.4202 0.6613 0.3759 0.0784  0.0203  -0.2604 521 ARG D C   
16619 O O   . ARG D  521 ? 0.4093 0.6373 0.3738 0.0845  0.0113  -0.2579 521 ARG D O   
16620 C CB  . ARG D  521 ? 0.5600 0.8507 0.5264 0.0636  0.0352  -0.2594 521 ARG D CB  
16621 C CG  . ARG D  521 ? 0.6261 0.9531 0.6082 0.0611  0.0444  -0.2647 521 ARG D CG  
16622 C CD  . ARG D  521 ? 0.6556 0.9976 0.6248 0.0446  0.0540  -0.2600 521 ARG D CD  
16623 N NE  . ARG D  521 ? 0.6307 1.0084 0.6162 0.0398  0.0623  -0.2637 521 ARG D NE  
16624 C CZ  . ARG D  521 ? 0.6198 1.0081 0.6098 0.0294  0.0630  -0.2578 521 ARG D CZ  
16625 N NH1 . ARG D  521 ? 0.5806 0.9455 0.5590 0.0237  0.0558  -0.2481 521 ARG D NH1 
16626 N NH2 . ARG D  521 ? 0.6505 1.0730 0.6561 0.0242  0.0709  -0.2616 521 ARG D NH2 
16627 N N   . ARG D  522 ? 0.6576 0.8844 0.5920 0.0715  0.0217  -0.2574 522 ARG D N   
16628 C CA  . ARG D  522 ? 0.7019 0.8971 0.6229 0.0709  0.0127  -0.2518 522 ARG D CA  
16629 C C   . ARG D  522 ? 0.6671 0.8534 0.5727 0.0579  0.0115  -0.2407 522 ARG D C   
16630 O O   . ARG D  522 ? 0.6583 0.8516 0.5505 0.0497  0.0179  -0.2395 522 ARG D O   
16631 C CB  . ARG D  522 ? 0.9357 1.1168 0.8445 0.0768  0.0128  -0.2595 522 ARG D CB  
16632 C CG  . ARG D  522 ? 1.0178 1.1860 0.9359 0.0900  0.0059  -0.2659 522 ARG D CG  
16633 C CD  . ARG D  522 ? 1.1107 1.2758 1.0214 0.0980  0.0092  -0.2773 522 ARG D CD  
16634 N NE  . ARG D  522 ? 1.1866 1.3504 1.0771 0.0898  0.0154  -0.2777 522 ARG D NE  
16635 C CZ  . ARG D  522 ? 1.2208 1.3603 1.0916 0.0833  0.0108  -0.2732 522 ARG D CZ  
16636 N NH1 . ARG D  522 ? 1.2277 1.3434 1.0972 0.0832  0.0005  -0.2678 522 ARG D NH1 
16637 N NH2 . ARG D  522 ? 1.2179 1.3578 1.0701 0.0763  0.0164  -0.2739 522 ARG D NH2 
16638 N N   . GLY D  523 ? 0.7301 0.9016 0.6383 0.0565  0.0030  -0.2324 523 GLY D N   
16639 C CA  . GLY D  523 ? 0.7568 0.9169 0.6526 0.0464  -0.0009 -0.2213 523 GLY D CA  
16640 C C   . GLY D  523 ? 0.7587 0.9347 0.6609 0.0401  0.0017  -0.2158 523 GLY D C   
16641 O O   . GLY D  523 ? 0.7533 0.9505 0.6577 0.0370  0.0102  -0.2196 523 GLY D O   
16642 N N   . LEU D  524 ? 0.7063 0.8718 0.6092 0.0368  -0.0053 -0.2064 524 LEU D N   
16643 C CA  . LEU D  524 ? 0.6646 0.8421 0.5739 0.0319  -0.0043 -0.2016 524 LEU D CA  
16644 C C   . LEU D  524 ? 0.6904 0.8592 0.5830 0.0219  -0.0064 -0.1917 524 LEU D C   
16645 O O   . LEU D  524 ? 0.6713 0.8240 0.5611 0.0214  -0.0143 -0.1840 524 LEU D O   
16646 C CB  . LEU D  524 ? 0.5132 0.6856 0.4380 0.0379  -0.0116 -0.1990 524 LEU D CB  
16647 C CG  . LEU D  524 ? 0.4570 0.6481 0.4007 0.0422  -0.0094 -0.2039 524 LEU D CG  
16648 C CD1 . LEU D  524 ? 0.4171 0.5978 0.3715 0.0473  -0.0182 -0.1996 524 LEU D CD1 
16649 C CD2 . LEU D  524 ? 0.4384 0.6474 0.3802 0.0329  -0.0034 -0.2025 524 LEU D CD2 
16650 N N   . ARG D  525 ? 0.7585 0.9388 0.6403 0.0137  0.0006  -0.1916 525 ARG D N   
16651 C CA  . ARG D  525 ? 0.7986 0.9695 0.6611 0.0042  -0.0016 -0.1824 525 ARG D CA  
16652 C C   . ARG D  525 ? 0.7973 0.9465 0.6495 0.0058  -0.0092 -0.1780 525 ARG D C   
16653 O O   . ARG D  525 ? 0.7860 0.9230 0.6328 0.0032  -0.0164 -0.1691 525 ARG D O   
16654 C CB  . ARG D  525 ? 0.8359 1.0075 0.7009 -0.0005 -0.0053 -0.1750 525 ARG D CB  
16655 C CG  . ARG D  525 ? 0.8562 1.0503 0.7306 -0.0043 0.0019  -0.1795 525 ARG D CG  
16656 C CD  . ARG D  525 ? 0.9185 1.1254 0.7777 -0.0154 0.0109  -0.1801 525 ARG D CD  
16657 N NE  . ARG D  525 ? 1.0002 1.1952 0.8391 -0.0258 0.0070  -0.1695 525 ARG D NE  
16658 C CZ  . ARG D  525 ? 1.0832 1.2722 0.9002 -0.0332 0.0091  -0.1656 525 ARG D CZ  
16659 N NH1 . ARG D  525 ? 1.1095 1.3041 0.9222 -0.0315 0.0156  -0.1718 525 ARG D NH1 
16660 N NH2 . ARG D  525 ? 1.0962 1.2725 0.8947 -0.0419 0.0040  -0.1554 525 ARG D NH2 
16661 N N   . ALA D  526 ? 0.7801 0.9256 0.6298 0.0101  -0.0074 -0.1848 526 ALA D N   
16662 C CA  . ALA D  526 ? 0.6898 0.8165 0.5346 0.0128  -0.0145 -0.1833 526 ALA D CA  
16663 C C   . ALA D  526 ? 0.6500 0.7636 0.4768 0.0061  -0.0198 -0.1751 526 ALA D C   
16664 O O   . ALA D  526 ? 0.6423 0.7447 0.4708 0.0063  -0.0277 -0.1689 526 ALA D O   
16665 C CB  . ALA D  526 ? 0.5540 0.6793 0.3974 0.0181  -0.0111 -0.1932 526 ALA D CB  
16666 N N   . GLN D  527 ? 0.5710 0.6870 0.3806 0.0004  -0.0155 -0.1754 527 GLN D N   
16667 C CA  . GLN D  527 ? 0.5669 0.6710 0.3579 -0.0055 -0.0210 -0.1680 527 GLN D CA  
16668 C C   . GLN D  527 ? 0.5116 0.6131 0.3030 -0.0087 -0.0267 -0.1579 527 GLN D C   
16669 O O   . GLN D  527 ? 0.5041 0.5941 0.2913 -0.0093 -0.0351 -0.1511 527 GLN D O   
16670 C CB  . GLN D  527 ? 0.6611 0.7698 0.4331 -0.0111 -0.0145 -0.1701 527 GLN D CB  
16671 C CG  . GLN D  527 ? 0.7319 0.8456 0.5036 -0.0073 -0.0075 -0.1811 527 GLN D CG  
16672 C CD  . GLN D  527 ? 0.8002 0.8975 0.5665 -0.0042 -0.0135 -0.1838 527 GLN D CD  
16673 O OE1 . GLN D  527 ? 0.8158 0.9113 0.5917 0.0023  -0.0127 -0.1914 527 GLN D OE1 
16674 N NE2 . GLN D  527 ? 0.8238 0.9084 0.5738 -0.0090 -0.0202 -0.1775 527 GLN D NE2 
16675 N N   . THR D  528 ? 0.4991 0.6123 0.2959 -0.0106 -0.0221 -0.1573 528 THR D N   
16676 C CA  . THR D  528 ? 0.4890 0.5994 0.2853 -0.0135 -0.0272 -0.1487 528 THR D CA  
16677 C C   . THR D  528 ? 0.4527 0.5569 0.2653 -0.0073 -0.0344 -0.1456 528 THR D C   
16678 O O   . THR D  528 ? 0.4239 0.5189 0.2332 -0.0077 -0.0421 -0.1378 528 THR D O   
16679 C CB  . THR D  528 ? 0.5022 0.6273 0.3019 -0.0178 -0.0205 -0.1500 528 THR D CB  
16680 O OG1 . THR D  528 ? 0.5119 0.6449 0.2961 -0.0251 -0.0126 -0.1523 528 THR D OG1 
16681 C CG2 . THR D  528 ? 0.5072 0.6259 0.3033 -0.0211 -0.0269 -0.1410 528 THR D CG2 
16682 N N   . CYS D  529 ? 0.4074 0.5172 0.2374 -0.0012 -0.0321 -0.1518 529 CYS D N   
16683 C CA  . CYS D  529 ? 0.4080 0.5126 0.2524 0.0039  -0.0382 -0.1487 529 CYS D CA  
16684 C C   . CYS D  529 ? 0.3648 0.4576 0.2047 0.0042  -0.0445 -0.1456 529 CYS D C   
16685 O O   . CYS D  529 ? 0.3862 0.4747 0.2330 0.0058  -0.0504 -0.1402 529 CYS D O   
16686 C CB  . CYS D  529 ? 0.3505 0.4629 0.2132 0.0102  -0.0350 -0.1555 529 CYS D CB  
16687 S SG  . CYS D  529 ? 0.7887 0.9154 0.6604 0.0092  -0.0311 -0.1561 529 CYS D SG  
16688 N N   . ALA D  530 ? 0.4212 0.5100 0.2490 0.0020  -0.0431 -0.1493 530 ALA D N   
16689 C CA  . ALA D  530 ? 0.4135 0.4919 0.2348 0.0004  -0.0494 -0.1465 530 ALA D CA  
16690 C C   . ALA D  530 ? 0.3893 0.4639 0.2008 -0.0034 -0.0552 -0.1377 530 ALA D C   
16691 O O   . ALA D  530 ? 0.3856 0.4556 0.1987 -0.0036 -0.0618 -0.1331 530 ALA D O   
16692 C CB  . ALA D  530 ? 0.5648 0.6388 0.3737 -0.0012 -0.0468 -0.1530 530 ALA D CB  
16693 N N   . PHE D  531 ? 0.4222 0.4989 0.2228 -0.0065 -0.0528 -0.1355 531 PHE D N   
16694 C CA  . PHE D  531 ? 0.4352 0.5065 0.2259 -0.0090 -0.0593 -0.1269 531 PHE D CA  
16695 C C   . PHE D  531 ? 0.4300 0.5026 0.2357 -0.0051 -0.0637 -0.1219 531 PHE D C   
16696 O O   . PHE D  531 ? 0.3972 0.4666 0.2055 -0.0039 -0.0705 -0.1169 531 PHE D O   
16697 C CB  . PHE D  531 ? 0.4166 0.4887 0.1913 -0.0137 -0.0560 -0.1256 531 PHE D CB  
16698 C CG  . PHE D  531 ? 0.4213 0.4864 0.1863 -0.0153 -0.0631 -0.1168 531 PHE D CG  
16699 C CD1 . PHE D  531 ? 0.4339 0.4897 0.1856 -0.0166 -0.0709 -0.1116 531 PHE D CD1 
16700 C CD2 . PHE D  531 ? 0.6341 0.7013 0.4022 -0.0156 -0.0628 -0.1142 531 PHE D CD2 
16701 C CE1 . PHE D  531 ? 0.4408 0.4890 0.1828 -0.0172 -0.0783 -0.1038 531 PHE D CE1 
16702 C CE2 . PHE D  531 ? 0.4232 0.4813 0.1804 -0.0166 -0.0703 -0.1065 531 PHE D CE2 
16703 C CZ  . PHE D  531 ? 0.4361 0.4845 0.1802 -0.0170 -0.0781 -0.1013 531 PHE D CZ  
16704 N N   . TRP D  532 ? 0.5195 0.5982 0.3356 -0.0031 -0.0596 -0.1238 532 TRP D N   
16705 C CA  . TRP D  532 ? 0.4930 0.5724 0.3211 0.0006  -0.0632 -0.1193 532 TRP D CA  
16706 C C   . TRP D  532 ? 0.4985 0.5786 0.3424 0.0053  -0.0663 -0.1187 532 TRP D C   
16707 O O   . TRP D  532 ? 0.5121 0.5908 0.3599 0.0075  -0.0717 -0.1131 532 TRP D O   
16708 C CB  . TRP D  532 ? 0.3497 0.4360 0.1850 0.0010  -0.0582 -0.1225 532 TRP D CB  
16709 C CG  . TRP D  532 ? 0.3633 0.4489 0.1835 -0.0047 -0.0572 -0.1203 532 TRP D CG  
16710 C CD1 . TRP D  532 ? 0.3860 0.4795 0.1990 -0.0100 -0.0497 -0.1250 532 TRP D CD1 
16711 C CD2 . TRP D  532 ? 0.3926 0.4695 0.2021 -0.0063 -0.0639 -0.1128 532 TRP D CD2 
16712 N NE1 . TRP D  532 ? 0.3869 0.4771 0.1844 -0.0163 -0.0513 -0.1202 532 TRP D NE1 
16713 C CE2 . TRP D  532 ? 0.3858 0.4638 0.1800 -0.0136 -0.0608 -0.1128 532 TRP D CE2 
16714 C CE3 . TRP D  532 ? 0.4716 0.5406 0.2829 -0.0022 -0.0722 -0.1063 532 TRP D CE3 
16715 C CZ2 . TRP D  532 ? 0.3991 0.4671 0.1776 -0.0171 -0.0670 -0.1061 532 TRP D CZ2 
16716 C CZ3 . TRP D  532 ? 0.3781 0.4379 0.1754 -0.0042 -0.0782 -0.1004 532 TRP D CZ3 
16717 C CH2 . TRP D  532 ? 0.4051 0.4625 0.1849 -0.0116 -0.0763 -0.1001 532 TRP D CH2 
16718 N N   . ASN D  533 ? 0.4834 0.5660 0.3358 0.0070  -0.0630 -0.1245 533 ASN D N   
16719 C CA  . ASN D  533 ? 0.4763 0.5591 0.3420 0.0104  -0.0657 -0.1240 533 ASN D CA  
16720 C C   . ASN D  533 ? 0.5178 0.5970 0.3792 0.0079  -0.0700 -0.1225 533 ASN D C   
16721 O O   . ASN D  533 ? 0.5615 0.6417 0.4320 0.0093  -0.0731 -0.1207 533 ASN D O   
16722 C CB  . ASN D  533 ? 0.3935 0.4782 0.2690 0.0134  -0.0616 -0.1309 533 ASN D CB  
16723 C CG  . ASN D  533 ? 0.3997 0.4908 0.2814 0.0157  -0.0571 -0.1338 533 ASN D CG  
16724 O OD1 . ASN D  533 ? 0.3988 0.4919 0.2831 0.0163  -0.0583 -0.1297 533 ASN D OD1 
16725 N ND2 . ASN D  533 ? 0.4301 0.5246 0.3141 0.0173  -0.0521 -0.1416 533 ASN D ND2 
16726 N N   . ARG D  534 ? 0.4756 0.5511 0.3226 0.0038  -0.0703 -0.1236 534 ARG D N   
16727 C CA  . ARG D  534 ? 0.5359 0.6080 0.3782 0.0007  -0.0748 -0.1233 534 ARG D CA  
16728 C C   . ARG D  534 ? 0.5479 0.6194 0.3804 -0.0019 -0.0804 -0.1174 534 ARG D C   
16729 O O   . ARG D  534 ? 0.5904 0.6653 0.4291 -0.0013 -0.0857 -0.1131 534 ARG D O   
16730 C CB  . ARG D  534 ? 0.6824 0.7492 0.5160 -0.0017 -0.0717 -0.1306 534 ARG D CB  
16731 C CG  . ARG D  534 ? 0.7460 0.8117 0.5894 0.0014  -0.0685 -0.1368 534 ARG D CG  
16732 C CD  . ARG D  534 ? 0.8303 0.8907 0.6638 0.0005  -0.0646 -0.1450 534 ARG D CD  
16733 N NE  . ARG D  534 ? 0.8944 0.9480 0.7317 0.0013  -0.0661 -0.1499 534 ARG D NE  
16734 C CZ  . ARG D  534 ? 0.9676 1.0142 0.7996 -0.0032 -0.0718 -0.1492 534 ARG D CZ  
16735 N NH1 . ARG D  534 ? 0.9821 1.0295 0.8065 -0.0080 -0.0763 -0.1439 534 ARG D NH1 
16736 N NH2 . ARG D  534 ? 1.0022 1.0405 0.8358 -0.0033 -0.0735 -0.1539 534 ARG D NH2 
16737 N N   . PHE D  535 ? 0.4431 0.5107 0.2599 -0.0046 -0.0796 -0.1174 535 PHE D N   
16738 C CA  . PHE D  535 ? 0.4100 0.4751 0.2149 -0.0070 -0.0859 -0.1120 535 PHE D CA  
16739 C C   . PHE D  535 ? 0.3880 0.4556 0.1970 -0.0038 -0.0898 -0.1054 535 PHE D C   
16740 O O   . PHE D  535 ? 0.3892 0.4601 0.2017 -0.0024 -0.0961 -0.1009 535 PHE D O   
16741 C CB  . PHE D  535 ? 0.4095 0.4681 0.1937 -0.0111 -0.0842 -0.1136 535 PHE D CB  
16742 C CG  . PHE D  535 ? 0.4239 0.4783 0.1939 -0.0135 -0.0916 -0.1076 535 PHE D CG  
16743 C CD1 . PHE D  535 ? 0.4307 0.4850 0.1983 -0.0155 -0.0978 -0.1067 535 PHE D CD1 
16744 C CD2 . PHE D  535 ? 0.4322 0.4827 0.1909 -0.0139 -0.0931 -0.1028 535 PHE D CD2 
16745 C CE1 . PHE D  535 ? 0.4446 0.4962 0.2001 -0.0173 -0.1054 -0.1012 535 PHE D CE1 
16746 C CE2 . PHE D  535 ? 0.5674 0.6131 0.3122 -0.0159 -0.1010 -0.0970 535 PHE D CE2 
16747 C CZ  . PHE D  535 ? 0.5693 0.6163 0.3133 -0.0172 -0.1071 -0.0962 535 PHE D CZ  
16748 N N   . LEU D  536 ? 0.4139 0.4805 0.2221 -0.0024 -0.0862 -0.1051 536 LEU D N   
16749 C CA  . LEU D  536 ? 0.4333 0.4991 0.2419 0.0005  -0.0901 -0.0992 536 LEU D CA  
16750 C C   . LEU D  536 ? 0.4999 0.5722 0.3250 0.0062  -0.0944 -0.0960 536 LEU D C   
16751 O O   . LEU D  536 ? 0.5150 0.5871 0.3375 0.0089  -0.1005 -0.0910 536 LEU D O   
16752 C CB  . LEU D  536 ? 0.4131 0.4774 0.2205 0.0004  -0.0853 -0.1006 536 LEU D CB  
16753 C CG  . LEU D  536 ? 0.4193 0.4785 0.2202 0.0015  -0.0893 -0.0952 536 LEU D CG  
16754 C CD1 . LEU D  536 ? 0.3595 0.4228 0.1785 0.0083  -0.0907 -0.0938 536 LEU D CD1 
16755 C CD2 . LEU D  536 ? 0.3954 0.4485 0.1808 0.0001  -0.0970 -0.0894 536 LEU D CD2 
16756 N N   . PRO D  537 ? 0.6352 0.7134 0.4764 0.0085  -0.0913 -0.0990 537 PRO D N   
16757 C CA  . PRO D  537 ? 0.6330 0.7187 0.4881 0.0131  -0.0948 -0.0963 537 PRO D CA  
16758 C C   . PRO D  537 ? 0.6388 0.7287 0.4916 0.0117  -0.1007 -0.0942 537 PRO D C   
16759 O O   . PRO D  537 ? 0.6614 0.7568 0.5190 0.0162  -0.1053 -0.0905 537 PRO D O   
16760 C CB  . PRO D  537 ? 0.5662 0.6554 0.4340 0.0132  -0.0904 -0.1003 537 PRO D CB  
16761 C CG  . PRO D  537 ? 0.5595 0.6439 0.4243 0.0122  -0.0847 -0.1042 537 PRO D CG  
16762 C CD  . PRO D  537 ? 0.5735 0.6522 0.4211 0.0077  -0.0847 -0.1047 537 PRO D CD  
16763 N N   . LYS D  538 ? 0.5328 0.6205 0.3786 0.0060  -0.1005 -0.0971 538 LYS D N   
16764 C CA  . LYS D  538 ? 0.5713 0.6628 0.4137 0.0035  -0.1066 -0.0955 538 LYS D CA  
16765 C C   . LYS D  538 ? 0.6062 0.6966 0.4392 0.0057  -0.1124 -0.0906 538 LYS D C   
16766 O O   . LYS D  538 ? 0.5992 0.6976 0.4372 0.0087  -0.1184 -0.0876 538 LYS D O   
16767 C CB  . LYS D  538 ? 0.6416 0.7266 0.4724 -0.0033 -0.1058 -0.0997 538 LYS D CB  
16768 C CG  . LYS D  538 ? 0.6797 0.7674 0.5179 -0.0067 -0.1060 -0.1031 538 LYS D CG  
16769 C CD  . LYS D  538 ? 0.7311 0.8142 0.5739 -0.0067 -0.0993 -0.1082 538 LYS D CD  
16770 C CE  . LYS D  538 ? 0.7798 0.8614 0.6251 -0.0114 -0.1008 -0.1119 538 LYS D CE  
16771 N NZ  . LYS D  538 ? 0.7864 0.8624 0.6360 -0.0107 -0.0955 -0.1169 538 LYS D NZ  
16772 N N   . LEU D  539 ? 0.7275 0.8083 0.5466 0.0043  -0.1108 -0.0899 539 LEU D N   
16773 C CA  . LEU D  539 ? 0.7717 0.8481 0.5775 0.0052  -0.1168 -0.0850 539 LEU D CA  
16774 C C   . LEU D  539 ? 0.7695 0.8501 0.5852 0.0135  -0.1204 -0.0812 539 LEU D C   
16775 O O   . LEU D  539 ? 0.7158 0.8014 0.5330 0.0177  -0.1272 -0.0780 539 LEU D O   
16776 C CB  . LEU D  539 ? 0.6413 0.7061 0.4288 0.0005  -0.1134 -0.0853 539 LEU D CB  
16777 C CG  . LEU D  539 ? 0.5870 0.6444 0.3562 -0.0005 -0.1194 -0.0797 539 LEU D CG  
16778 C CD1 . LEU D  539 ? 0.5734 0.6335 0.3363 -0.0017 -0.1269 -0.0771 539 LEU D CD1 
16779 C CD2 . LEU D  539 ? 0.5860 0.6329 0.3353 -0.0075 -0.1150 -0.0808 539 LEU D CD2 
16780 N N   . LEU D  540 ? 0.8452 0.9239 0.6679 0.0164  -0.1156 -0.0822 540 LEU D N   
16781 C CA  . LEU D  540 ? 0.8651 0.9450 0.6960 0.0247  -0.1179 -0.0798 540 LEU D CA  
16782 C C   . LEU D  540 ? 0.9148 1.0076 0.7615 0.0311  -0.1211 -0.0795 540 LEU D C   
16783 O O   . LEU D  540 ? 0.8870 0.9815 0.7368 0.0393  -0.1258 -0.0771 540 LEU D O   
16784 C CB  . LEU D  540 ? 0.6456 0.7228 0.4831 0.0250  -0.1112 -0.0824 540 LEU D CB  
16785 C CG  . LEU D  540 ? 0.5575 0.6266 0.3920 0.0289  -0.1120 -0.0805 540 LEU D CG  
16786 C CD1 . LEU D  540 ? 0.5654 0.6233 0.3803 0.0276  -0.1179 -0.0762 540 LEU D CD1 
16787 C CD2 . LEU D  540 ? 0.4936 0.5604 0.3302 0.0249  -0.1048 -0.0841 540 LEU D CD2 
16788 N N   . SER D  541 ? 0.9333 1.0352 0.7892 0.0276  -0.1186 -0.0823 541 SER D N   
16789 C CA  . SER D  541 ? 1.0240 1.1406 0.8939 0.0314  -0.1213 -0.0824 541 SER D CA  
16790 C C   . SER D  541 ? 1.1108 1.2334 0.9764 0.0315  -0.1288 -0.0803 541 SER D C   
16791 O O   . SER D  541 ? 1.0888 1.2216 0.9623 0.0388  -0.1333 -0.0791 541 SER D O   
16792 C CB  . SER D  541 ? 1.0312 1.1543 0.9115 0.0264  -0.1164 -0.0858 541 SER D CB  
16793 O OG  . SER D  541 ? 1.0425 1.1679 0.9185 0.0194  -0.1188 -0.0869 541 SER D OG  
16794 N N   . ALA D  542 ? 1.2238 1.3407 1.0768 0.0238  -0.1304 -0.0805 542 ALA D N   
16795 C CA  . ALA D  542 ? 1.2558 1.3778 1.1035 0.0228  -0.1381 -0.0786 542 ALA D CA  
16796 C C   . ALA D  542 ? 1.3041 1.4209 1.1419 0.0291  -0.1448 -0.0742 542 ALA D C   
16797 O O   . ALA D  542 ? 1.2770 1.3996 1.1125 0.0309  -0.1523 -0.0722 542 ALA D O   
16798 C CB  . ALA D  542 ? 1.1324 1.2481 0.9678 0.0127  -0.1380 -0.0804 542 ALA D CB  
16799 N N   . THR D  543 ? 1.5197 1.6251 1.3513 0.0324  -0.1427 -0.0728 543 THR D N   
16800 C CA  . THR D  543 ? 1.5935 1.6918 1.4163 0.0398  -0.1493 -0.0687 543 THR D CA  
16801 C C   . THR D  543 ? 1.6148 1.7139 1.4490 0.0503  -0.1484 -0.0691 543 THR D C   
16802 O O   . THR D  543 ? 1.5894 1.6996 1.4404 0.0527  -0.1438 -0.0723 543 THR D O   
16803 C CB  . THR D  543 ? 1.3548 1.4356 1.1547 0.0338  -0.1497 -0.0658 543 THR D CB  
16804 O OG1 . THR D  543 ? 1.3851 1.4573 1.1754 0.0413  -0.1575 -0.0612 543 THR D OG1 
16805 C CG2 . THR D  543 ? 1.3249 1.3975 1.1233 0.0297  -0.1414 -0.0679 543 THR D CG2 
16806 O OXT . THR D  543 ? 1.5040 1.5918 1.3297 0.0566  -0.1526 -0.0664 543 THR D OXT 
16807 C C1  . 4OJ E  .   ? 1.0504 0.9835 1.0870 0.0618  -0.0055 0.0422  600 4OJ A C1  
16808 C C2  . 4OJ E  .   ? 1.0810 1.0135 1.1174 0.0686  -0.0149 0.0449  600 4OJ A C2  
16809 C C3  . 4OJ E  .   ? 1.0620 1.0056 1.1170 0.0712  -0.0167 0.0446  600 4OJ A C3  
16810 C C4  . 4OJ E  .   ? 1.0277 0.9820 1.0989 0.0666  -0.0093 0.0418  600 4OJ A C4  
16811 C C5  . 4OJ E  .   ? 0.9857 0.9408 1.0566 0.0599  -0.0012 0.0394  600 4OJ A C5  
16812 C C6  . 4OJ E  .   ? 0.9882 0.9330 1.0429 0.0576  0.0010  0.0396  600 4OJ A C6  
16813 O O12 . 4OJ E  .   ? 0.9410 0.9067 1.0272 0.0560  0.0046  0.0367  600 4OJ A O12 
16814 P P13 . 4OJ E  .   ? 0.4204 0.3977 0.5237 0.0580  0.0039  0.0356  600 4OJ A P13 
16815 O O1P . 4OJ E  .   ? 0.4102 0.4038 0.5278 0.0586  -0.0016 0.0342  600 4OJ A O1P 
16816 O O2P . 4OJ E  .   ? 0.4426 0.4116 0.5424 0.0637  0.0023  0.0380  600 4OJ A O2P 
16817 C C7  . 4OJ E  .   ? 0.9413 0.8881 0.9980 0.0511  0.0101  0.0367  600 4OJ A C7  
16818 C C1  . NAG F  .   ? 1.0927 1.4706 1.6668 0.0121  0.0987  0.0242  701 NAG A C1  
16819 C C2  . NAG F  .   ? 1.0958 1.4714 1.6738 0.0000  0.1104  0.0288  701 NAG A C2  
16820 C C3  . NAG F  .   ? 1.1075 1.4888 1.7046 -0.0098 0.1011  0.0281  701 NAG A C3  
16821 C C4  . NAG F  .   ? 1.1161 1.5207 1.7424 -0.0073 0.0941  0.0231  701 NAG A C4  
16822 C C5  . NAG F  .   ? 1.1075 1.5138 1.7273 0.0059  0.0835  0.0193  701 NAG A C5  
16823 C C6  . NAG F  .   ? 1.1007 1.5306 1.7492 0.0099  0.0766  0.0148  701 NAG A C6  
16824 C C7  . NAG F  .   ? 1.0267 1.3751 1.5600 0.0040  0.1276  0.0350  701 NAG A C7  
16825 C C8  . NAG F  .   ? 1.0235 1.3522 1.5276 0.0092  0.1233  0.0363  701 NAG A C8  
16826 N N2  . NAG F  .   ? 1.0586 1.4131 1.6091 -0.0017 0.1163  0.0335  701 NAG A N2  
16827 O O3  . NAG F  .   ? 1.1071 1.4857 1.7085 -0.0210 0.1126  0.0325  701 NAG A O3  
16828 O O4  . NAG F  .   ? 1.1156 1.5246 1.7580 -0.0156 0.0829  0.0215  701 NAG A O4  
16829 O O5  . NAG F  .   ? 1.1155 1.5151 1.7175 0.0142  0.0939  0.0203  701 NAG A O5  
16830 O O6  . NAG F  .   ? 1.0765 1.5040 1.7166 0.0211  0.0634  0.0120  701 NAG A O6  
16831 O O7  . NAG F  .   ? 0.9950 1.3537 1.5359 0.0052  0.1411  0.0351  701 NAG A O7  
16857 C C1  . 4OJ L  .   ? 1.0603 0.9705 1.0224 -0.2679 0.1602  -0.0502 600 4OJ B C1  
16858 C C2  . 4OJ L  .   ? 1.0839 1.0001 1.0605 -0.2592 0.1505  -0.0466 600 4OJ B C2  
16859 C C3  . 4OJ L  .   ? 1.0894 0.9965 1.0610 -0.2487 0.1435  -0.0412 600 4OJ B C3  
16860 C C4  . 4OJ L  .   ? 1.1225 1.0146 1.0747 -0.2468 0.1461  -0.0395 600 4OJ B C4  
16861 C C5  . 4OJ L  .   ? 1.1239 1.0095 1.0610 -0.2555 0.1554  -0.0428 600 4OJ B C5  
16862 C C6  . 4OJ L  .   ? 1.0431 0.9378 0.9850 -0.2662 0.1625  -0.0482 600 4OJ B C6  
16863 O O12 . 4OJ L  .   ? 1.1677 1.0382 1.0852 -0.2537 0.1572  -0.0407 600 4OJ B O12 
16864 P P13 . 4OJ L  .   ? 0.5602 0.4190 0.4697 -0.2419 0.1497  -0.0349 600 4OJ B P13 
16865 O O1P . 4OJ L  .   ? 0.5417 0.3837 0.4359 -0.2397 0.1448  -0.0297 600 4OJ B O1P 
16866 O O2P . 4OJ L  .   ? 0.5267 0.3982 0.4564 -0.2329 0.1438  -0.0348 600 4OJ B O2P 
16867 C C7  . 4OJ L  .   ? 1.0039 0.8919 0.9292 -0.2764 0.1727  -0.0517 600 4OJ B C7  
16868 C C1  . NAG M  .   ? 1.3330 0.9963 1.1685 -0.1264 0.0451  -0.0229 701 NAG B C1  
16869 C C2  . NAG M  .   ? 1.3369 0.9839 1.1730 -0.1219 0.0427  -0.0236 701 NAG B C2  
16870 C C3  . NAG M  .   ? 1.3647 0.9976 1.1951 -0.1274 0.0444  -0.0232 701 NAG B C3  
16871 C C4  . NAG M  .   ? 1.3868 1.0211 1.2200 -0.1338 0.0465  -0.0290 701 NAG B C4  
16872 C C5  . NAG M  .   ? 1.3596 1.0122 1.1937 -0.1381 0.0487  -0.0298 701 NAG B C5  
16873 C C6  . NAG M  .   ? 1.2955 0.9515 1.1329 -0.1437 0.0502  -0.0361 701 NAG B C6  
16874 C C7  . NAG M  .   ? 1.3247 0.9729 1.1568 -0.1121 0.0394  -0.0151 701 NAG B C7  
16875 C C8  . NAG M  .   ? 1.2720 0.9313 1.1087 -0.1056 0.0372  -0.0138 701 NAG B C8  
16876 N N2  . NAG M  .   ? 1.3374 0.9819 1.1737 -0.1142 0.0397  -0.0200 701 NAG B N2  
16877 O O3  . NAG M  .   ? 1.3821 0.9984 1.2117 -0.1233 0.0418  -0.0220 701 NAG B O3  
16878 O O4  . NAG M  .   ? 1.4169 1.0381 1.2458 -0.1394 0.0481  -0.0293 701 NAG B O4  
16879 O O5  . NAG M  .   ? 1.3646 1.0301 1.2018 -0.1328 0.0471  -0.0278 701 NAG B O5  
16880 O O6  . NAG M  .   ? 1.2601 0.9097 1.0940 -0.1513 0.0527  -0.0375 701 NAG B O6  
16881 O O7  . NAG M  .   ? 1.3373 0.9798 1.1622 -0.1154 0.0409  -0.0120 701 NAG B O7  
16882 C C1  . NAG N  .   ? 1.0380 1.2362 1.4406 -0.1962 0.0738  -0.0867 702 NAG B C1  
16883 C C2  . NAG N  .   ? 1.0427 1.2412 1.4568 -0.1873 0.0613  -0.0805 702 NAG B C2  
16884 C C3  . NAG N  .   ? 1.0456 1.2222 1.4307 -0.1867 0.0561  -0.0685 702 NAG B C3  
16885 C C4  . NAG N  .   ? 1.0636 1.2338 1.4292 -0.1950 0.0530  -0.0604 702 NAG B C4  
16886 C C5  . NAG N  .   ? 1.1643 1.3384 1.5262 -0.2033 0.0636  -0.0669 702 NAG B C5  
16887 C C6  . NAG N  .   ? 0.6189 0.7921 0.9714 -0.2109 0.0588  -0.0604 702 NAG B C6  
16888 C C7  . NAG N  .   ? 1.0289 1.2457 1.4913 -0.1708 0.0555  -0.0906 702 NAG B C7  
16889 C C8  . NAG N  .   ? 0.9932 1.1993 1.4561 -0.1610 0.0487  -0.0857 702 NAG B C8  
16890 N N2  . NAG N  .   ? 1.0544 1.2585 1.4884 -0.1787 0.0641  -0.0889 702 NAG B N2  
16891 O O3  . NAG N  .   ? 1.0236 1.1998 1.4171 -0.1793 0.0449  -0.0627 702 NAG B O3  
16892 O O4  . NAG N  .   ? 1.0492 1.1972 1.3866 -0.1939 0.0513  -0.0515 702 NAG B O4  
16893 O O5  . NAG N  .   ? 1.1275 1.3214 1.5154 -0.2035 0.0696  -0.0788 702 NAG B O5  
16894 O O6  . NAG N  .   ? 0.5914 0.7856 0.9677 -0.2136 0.0527  -0.0624 702 NAG B O6  
16895 O O7  . NAG N  .   ? 1.0129 1.2489 1.5005 -0.1708 0.0529  -0.0960 702 NAG B O7  
16911 C C1  . 4OJ R  .   ? 0.8189 0.7763 0.7251 -0.0040 0.0717  -0.0407 600 4OJ C C1  
16912 C C2  . 4OJ R  .   ? 0.8291 0.7716 0.7277 -0.0081 0.0694  -0.0368 600 4OJ C C2  
16913 C C3  . 4OJ R  .   ? 0.8085 0.7520 0.7080 -0.0160 0.0725  -0.0338 600 4OJ C C3  
16914 C C4  . 4OJ R  .   ? 0.7852 0.7427 0.6924 -0.0196 0.0776  -0.0350 600 4OJ C C4  
16915 C C5  . 4OJ R  .   ? 0.7638 0.7348 0.6784 -0.0163 0.0797  -0.0387 600 4OJ C C5  
16916 C C6  . 4OJ R  .   ? 0.7612 0.7331 0.6755 -0.0085 0.0769  -0.0415 600 4OJ C C6  
16917 O O12 . 4OJ R  .   ? 0.7400 0.7227 0.6616 -0.0209 0.0849  -0.0398 600 4OJ C O12 
16918 P P13 . 4OJ R  .   ? 0.3553 0.3380 0.2798 -0.0284 0.0865  -0.0368 600 4OJ C P13 
16919 O O1P . 4OJ R  .   ? 0.3244 0.3039 0.2546 -0.0310 0.0864  -0.0334 600 4OJ C O1P 
16920 O O2P . 4OJ R  .   ? 0.3939 0.3683 0.3084 -0.0309 0.0859  -0.0355 600 4OJ C O2P 
16921 C C7  . 4OJ R  .   ? 0.6970 0.6847 0.6194 -0.0051 0.0799  -0.0453 600 4OJ C C7  
16922 C C1  . NAG S  .   ? 1.1665 1.4102 1.3352 -0.0135 0.1476  0.0115  701 NAG C C1  
16923 C C2  . NAG S  .   ? 1.1951 1.4385 1.3707 0.0020  0.1514  0.0117  701 NAG C C2  
16924 C C3  . NAG S  .   ? 1.1723 1.4295 1.3627 0.0080  0.1473  0.0161  701 NAG C C3  
16925 C C4  . NAG S  .   ? 1.1742 1.4602 1.3866 0.0015  0.1450  0.0160  701 NAG C C4  
16926 C C5  . NAG S  .   ? 1.1601 1.4417 1.3681 -0.0164 0.1445  0.0126  701 NAG C C5  
16927 C C6  . NAG S  .   ? 1.1264 1.4310 1.3579 -0.0224 0.1440  0.0140  701 NAG C C6  
16928 C C7  . NAG S  .   ? 1.2134 1.4220 1.3646 0.0126  0.1584  0.0091  701 NAG C C7  
16929 C C8  . NAG S  .   ? 1.2059 1.4363 1.3704 0.0130  0.1628  0.0068  701 NAG C C8  
16930 N N2  . NAG S  .   ? 1.2145 1.4307 1.3713 0.0080  0.1533  0.0115  701 NAG C N2  
16931 O O3  . NAG S  .   ? 1.1475 1.4053 1.3423 0.0243  0.1492  0.0193  701 NAG C O3  
16932 O O4  . NAG S  .   ? 1.1706 1.4740 1.3948 0.0067  0.1377  0.0216  701 NAG C O4  
16933 O O5  . NAG S  .   ? 1.1734 1.4417 1.3612 -0.0207 0.1469  0.0102  701 NAG C O5  
16934 O O6  . NAG S  .   ? 1.1066 1.4254 1.3502 -0.0159 0.1499  0.0115  701 NAG C O6  
16935 O O7  . NAG S  .   ? 1.2092 1.3943 1.3453 0.0162  0.1597  0.0084  701 NAG C O7  
16951 C C1  . 4OJ AA .   ? 0.8170 0.9524 0.7867 -0.0353 -0.0800 -0.1246 600 4OJ D C1  
16952 C C2  . 4OJ AA .   ? 0.8893 0.9968 0.8375 -0.0386 -0.0864 -0.1176 600 4OJ D C2  
16953 C C3  . 4OJ AA .   ? 0.9211 1.0119 0.8562 -0.0284 -0.0894 -0.1156 600 4OJ D C3  
16954 C C4  . 4OJ AA .   ? 0.9100 1.0120 0.8533 -0.0169 -0.0857 -0.1202 600 4OJ D C4  
16955 C C5  . 4OJ AA .   ? 0.8431 0.9696 0.8060 -0.0142 -0.0797 -0.1268 600 4OJ D C5  
16956 C C6  . 4OJ AA .   ? 0.7331 0.8767 0.7096 -0.0226 -0.0769 -0.1292 600 4OJ D C6  
16957 O O12 . 4OJ AA .   ? 0.8458 0.9789 0.8140 -0.0033 -0.0772 -0.1309 600 4OJ D O12 
16958 P P13 . 4OJ AA .   ? 0.4004 0.5191 0.3563 0.0062  -0.0800 -0.1290 600 4OJ D P13 
16959 O O1P . 4OJ AA .   ? 0.4039 0.5123 0.3627 0.0155  -0.0858 -0.1271 600 4OJ D O1P 
16960 O O2P . 4OJ AA .   ? 0.3943 0.4978 0.3300 0.0009  -0.0810 -0.1230 600 4OJ D O2P 
16961 C C7  . 4OJ AA .   ? 0.5759 0.7466 0.5742 -0.0178 -0.0712 -0.1371 600 4OJ D C7  
16962 C C1  . NAG BA .   ? 1.2019 1.4932 1.1230 0.2607  -0.1058 -0.1790 701 NAG D C1  
16963 C C2  . NAG BA .   ? 1.2043 1.5402 1.1304 0.2647  -0.1018 -0.1837 701 NAG D C2  
16964 C C3  . NAG BA .   ? 1.2426 1.5984 1.1687 0.2623  -0.0960 -0.1843 701 NAG D C3  
16965 C C4  . NAG BA .   ? 1.2459 1.5731 1.1579 0.2684  -0.1001 -0.1869 701 NAG D C4  
16966 C C5  . NAG BA .   ? 1.2136 1.4971 1.1198 0.2705  -0.1089 -0.1847 701 NAG D C5  
16967 C C6  . NAG BA .   ? 1.1542 1.4231 1.0509 0.2878  -0.1211 -0.1912 701 NAG D C6  
16968 C C7  . NAG BA .   ? 1.1053 1.4614 1.0406 0.2589  -0.0988 -0.1827 701 NAG D C7  
16969 C C8  . NAG BA .   ? 1.1203 1.4631 1.0430 0.2748  -0.1088 -0.1900 701 NAG D C8  
16970 N N2  . NAG BA .   ? 1.1420 1.4976 1.0782 0.2552  -0.0957 -0.1806 701 NAG D N2  
16971 O O3  . NAG BA .   ? 1.2669 1.6647 1.1969 0.2657  -0.0921 -0.1889 701 NAG D O3  
16972 O O4  . NAG BA .   ? 1.2220 1.5492 1.1292 0.2571  -0.0916 -0.1839 701 NAG D O4  
16973 O O5  . NAG BA .   ? 1.2050 1.4813 1.1204 0.2614  -0.1074 -0.1788 701 NAG D O5  
16974 O O6  . NAG BA .   ? 1.1153 1.3709 0.9994 0.2939  -0.1231 -0.1956 701 NAG D O6  
16975 O O7  . NAG BA .   ? 1.0622 1.4286 1.0051 0.2503  -0.0944 -0.1796 701 NAG D O7  
16976 C C1  . NAG CA .   ? 1.3403 1.2008 0.8796 -0.3080 -0.0780 0.0332  702 NAG D C1  
16977 C C2  . NAG CA .   ? 1.3816 1.2113 0.9276 -0.2902 -0.0945 0.0308  702 NAG D C2  
16978 C C3  . NAG CA .   ? 1.4020 1.1832 0.9188 -0.2745 -0.1118 0.0374  702 NAG D C3  
16979 C C4  . NAG CA .   ? 1.4210 1.2031 0.9188 -0.2703 -0.1087 0.0406  702 NAG D C4  
16980 C C5  . NAG CA .   ? 1.4613 1.2591 0.9422 -0.2980 -0.0958 0.0481  702 NAG D C5  
16981 C C6  . NAG CA .   ? 1.4349 1.2679 0.9226 -0.2911 -0.0825 0.0415  702 NAG D C6  
16982 C C7  . NAG CA .   ? 1.3330 1.1179 0.8777 -0.3018 -0.1139 0.0356  702 NAG D C7  
16983 C C8  . NAG CA .   ? 1.2779 1.0754 0.8536 -0.2748 -0.1169 0.0226  702 NAG D C8  
16984 N N2  . NAG CA .   ? 1.3859 1.2027 0.9318 -0.3084 -0.0992 0.0353  702 NAG D N2  
16985 O O3  . NAG CA .   ? 1.3441 1.1200 0.8798 -0.2473 -0.1205 0.0283  702 NAG D O3  
16986 O O4  . NAG CA .   ? 1.4169 1.1512 0.8847 -0.2596 -0.1263 0.0485  702 NAG D O4  
16987 O O5  . NAG CA .   ? 1.4354 1.2572 0.9320 -0.3192 -0.0858 0.0473  702 NAG D O5  
16988 O O6  . NAG CA .   ? 1.4171 1.2249 0.8844 -0.2746 -0.0929 0.0444  702 NAG D O6  
16989 O O7  . NAG CA .   ? 1.3247 1.0702 0.8435 -0.3176 -0.1248 0.0460  702 NAG D O7  
16990 C C1  . NAG DA .   ? 1.2325 1.9424 1.5167 -0.2475 0.0036  -0.1672 703 NAG D C1  
16991 C C2  . NAG DA .   ? 1.2749 1.9390 1.5290 -0.2683 -0.0048 -0.1545 703 NAG D C2  
16992 C C3  . NAG DA .   ? 1.3169 1.9847 1.5648 -0.2988 -0.0041 -0.1452 703 NAG D C3  
16993 C C4  . NAG DA .   ? 1.3346 2.0538 1.5996 -0.3065 0.0112  -0.1495 703 NAG D C4  
16994 C C5  . NAG DA .   ? 1.2933 2.0489 1.5926 -0.2831 0.0107  -0.1615 703 NAG D C5  
16995 C C6  . NAG DA .   ? 1.2510 2.0561 1.5658 -0.2801 0.0273  -0.1698 703 NAG D C6  
16996 C C7  . NAG DA .   ? 1.2223 1.8170 1.4556 -0.2420 -0.0261 -0.1539 703 NAG D C7  
16997 C C8  . NAG DA .   ? 1.1838 1.7680 1.4282 -0.2129 -0.0358 -0.1609 703 NAG D C8  
16998 N N2  . NAG DA .   ? 1.2553 1.8821 1.5049 -0.2544 -0.0212 -0.1538 703 NAG D N2  
16999 O O3  . NAG DA .   ? 1.3272 1.9598 1.5423 -0.3208 -0.0048 -0.1338 703 NAG D O3  
17000 O O4  . NAG DA .   ? 1.3698 2.0905 1.6264 -0.3361 0.0120  -0.1400 703 NAG D O4  
17001 O O5  . NAG DA .   ? 1.2649 2.0034 1.5697 -0.2543 0.0027  -0.1682 703 NAG D O5  
17002 O O6  . NAG DA .   ? 1.2459 2.0707 1.5573 -0.3080 0.0346  -0.1635 703 NAG D O6  
17003 O O7  . NAG DA .   ? 1.2222 1.7952 1.4311 -0.2534 -0.0233 -0.1482 703 NAG D O7  
# 
_database_PDB_caveat.id     1 
_database_PDB_caveat.text   'NAG A 702   C1 IS PLANAR' 
# 
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   GLU 1   1   ?   ?   ?   A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   ARG 3   3   3   ARG ARG A . n 
A 1 4   GLU 4   4   4   GLU GLU A . n 
A 1 5   ASP 5   5   5   ASP ASP A . n 
A 1 6   PRO 6   6   6   PRO PRO A . n 
A 1 7   GLN 7   7   7   GLN GLN A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  ARG 11  11  11  ARG ARG A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  ARG 13  13  13  ARG ARG A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  GLN 16  16  16  GLN GLN A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  GLY 19  19  19  GLY GLY A . n 
A 1 20  ILE 20  20  20  ILE ILE A . n 
A 1 21  ARG 21  21  21  ARG ARG A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  ALA 24  24  24  ALA ALA A . n 
A 1 25  PRO 25  25  25  PRO PRO A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  SER 30  30  30  SER SER A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  PRO 41  41  41  PRO PRO A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  ARG 45  45  45  ARG ARG A . n 
A 1 46  ARG 46  46  46  ARG ARG A . n 
A 1 47  PHE 47  47  47  PHE PHE A . n 
A 1 48  MET 48  48  48  MET MET A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  PRO 50  50  50  PRO PRO A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  LYS 53  53  53  LYS LYS A . n 
A 1 54  ARG 54  54  54  ARG ARG A . n 
A 1 55  PRO 55  55  55  PRO PRO A . n 
A 1 56  TRP 56  56  56  TRP TRP A . n 
A 1 57  SER 57  57  57  SER SER A . n 
A 1 58  GLY 58  58  58  GLY GLY A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  PHE 65  65  65  PHE PHE A . n 
A 1 66  GLN 66  66  66  GLN GLN A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  CYS 69  69  69  CYS CYS A . n 
A 1 70  TYR 70  70  70  TYR TYR A . n 
A 1 71  GLN 71  71  71  GLN GLN A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  TYR 77  77  77  TYR TYR A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  THR 83  83  83  THR THR A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  MET 85  85  85  MET MET A . n 
A 1 86  TRP 86  86  86  TRP TRP A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  PRO 88  88  88  PRO PRO A . n 
A 1 89  ASN 89  89  89  ASN ASN A . n 
A 1 90  ARG 90  90  90  ARG ARG A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  ASP 95  95  95  ASP ASP A . n 
A 1 96  CYS 96  96  96  CYS CYS A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  TYR 98  98  98  TYR TYR A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 ASN 100 100 100 ASN ASN A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 TRP 102 102 102 TRP TRP A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 SER 110 110 110 SER SER A . n 
A 1 111 PRO 111 111 111 PRO PRO A . n 
A 1 112 THR 112 112 112 THR THR A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ILE 116 116 116 ILE ILE A . n 
A 1 117 TRP 117 117 117 TRP TRP A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 TYR 119 119 119 TYR TYR A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 PHE 123 123 123 PHE PHE A . n 
A 1 124 TYR 124 124 124 TYR TYR A . n 
A 1 125 SER 125 125 125 SER SER A . n 
A 1 126 GLY 126 126 126 GLY GLY A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 ASP 131 131 131 ASP ASP A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 TYR 133 133 133 TYR TYR A . n 
A 1 134 ASP 134 134 134 ASP ASP A . n 
A 1 135 GLY 135 135 135 GLY GLY A . n 
A 1 136 ARG 136 136 136 ARG ARG A . n 
A 1 137 PHE 137 137 137 PHE PHE A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 GLN 140 140 140 GLN GLN A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 GLU 142 142 142 GLU GLU A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 VAL 145 145 145 VAL VAL A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 MET 149 149 149 MET MET A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 TYR 151 151 151 TYR TYR A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 THR 155 155 155 THR THR A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 PHE 158 158 158 PHE PHE A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 PRO 162 162 162 PRO PRO A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 ARG 165 165 165 ARG ARG A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 ASN 170 170 170 ASN ASN A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 ASP 175 175 175 ASP ASP A . n 
A 1 176 GLN 176 176 176 GLN GLN A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 GLN 181 181 181 GLN GLN A . n 
A 1 182 TRP 182 182 182 TRP TRP A . n 
A 1 183 VAL 183 183 183 VAL VAL A . n 
A 1 184 GLN 184 184 184 GLN GLN A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 PHE 190 190 190 PHE PHE A . n 
A 1 191 GLY 191 191 191 GLY GLY A . n 
A 1 192 GLY 192 192 192 GLY GLY A . n 
A 1 193 ASP 193 193 193 ASP ASP A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 MET 195 195 195 MET MET A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 GLY 201 201 201 GLY GLY A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 GLY 205 205 205 GLY GLY A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 VAL 209 209 209 VAL VAL A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 MET 211 211 211 MET MET A . n 
A 1 212 HIS 212 212 212 HIS HIS A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 PRO 217 217 217 PRO PRO A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 ARG 219 219 219 ARG ARG A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 HIS 223 223 223 HIS HIS A . n 
A 1 224 ARG 224 224 224 ARG ARG A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 GLN 228 228 228 GLN GLN A . n 
A 1 229 SER 229 229 229 SER SER A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 THR 231 231 231 THR THR A . n 
A 1 232 PRO 232 232 232 PRO PRO A . n 
A 1 233 ASN 233 233 233 ASN ASN A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 PRO 235 235 235 PRO PRO A . n 
A 1 236 TRP 236 236 236 TRP TRP A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 THR 238 238 238 THR THR A . n 
A 1 239 VAL 239 239 239 VAL VAL A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 GLY 242 242 242 GLY GLY A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 ARG 246 246 246 ARG ARG A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 ALA 248 248 248 ALA ALA A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 ALA 252 252 252 ALA ALA A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 GLY 256 256 256 GLY GLY A . n 
A 1 257 CYS 257 257 257 CYS CYS A . n 
A 1 258 PRO 258 258 258 PRO PRO A . n 
A 1 259 PRO 259 259 259 PRO PRO A . n 
A 1 260 GLY 260 260 260 GLY GLY A . n 
A 1 261 GLY 261 261 261 GLY GLY A . n 
A 1 262 ALA 262 262 262 ALA ALA A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 ASN 265 265 265 ASN ASN A . n 
A 1 266 ASP 266 266 266 ASP ASP A . n 
A 1 267 THR 267 267 267 THR THR A . n 
A 1 268 GLU 268 268 268 GLU GLU A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 ILE 270 270 270 ILE ILE A . n 
A 1 271 ALA 271 271 271 ALA ALA A . n 
A 1 272 CYS 272 272 272 CYS CYS A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 ARG 274 274 274 ARG ARG A . n 
A 1 275 THR 275 275 275 THR THR A . n 
A 1 276 ARG 276 276 276 ARG ARG A . n 
A 1 277 PRO 277 277 277 PRO PRO A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 GLN 279 279 279 GLN GLN A . n 
A 1 280 ASP 280 280 280 ASP ASP A . n 
A 1 281 LEU 281 281 281 LEU LEU A . n 
A 1 282 VAL 282 282 282 VAL VAL A . n 
A 1 283 ASP 283 283 283 ASP ASP A . n 
A 1 284 HIS 284 284 284 HIS HIS A . n 
A 1 285 GLU 285 285 285 GLU GLU A . n 
A 1 286 TRP 286 286 286 TRP TRP A . n 
A 1 287 HIS 287 287 287 HIS HIS A . n 
A 1 288 VAL 288 288 288 VAL VAL A . n 
A 1 289 LEU 289 289 289 LEU LEU A . n 
A 1 290 PRO 290 290 290 PRO PRO A . n 
A 1 291 GLN 291 291 291 GLN GLN A . n 
A 1 292 GLU 292 292 292 GLU GLU A . n 
A 1 293 SER 293 293 293 SER SER A . n 
A 1 294 ILE 294 294 294 ILE ILE A . n 
A 1 295 PHE 295 295 295 PHE PHE A . n 
A 1 296 ARG 296 296 296 ARG ARG A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 SER 298 298 298 SER SER A . n 
A 1 299 PHE 299 299 299 PHE PHE A . n 
A 1 300 VAL 300 300 300 VAL VAL A . n 
A 1 301 PRO 301 301 301 PRO PRO A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 ASP 304 304 304 ASP ASP A . n 
A 1 305 GLY 305 305 305 GLY GLY A . n 
A 1 306 ASP 306 306 306 ASP ASP A . n 
A 1 307 PHE 307 307 307 PHE PHE A . n 
A 1 308 LEU 308 308 308 LEU LEU A . n 
A 1 309 SER 309 309 309 SER SER A . n 
A 1 310 ASP 310 310 310 ASP ASP A . n 
A 1 311 THR 311 311 311 THR THR A . n 
A 1 312 PRO 312 312 312 PRO PRO A . n 
A 1 313 GLU 313 313 313 GLU GLU A . n 
A 1 314 ALA 314 314 314 ALA ALA A . n 
A 1 315 LEU 315 315 315 LEU LEU A . n 
A 1 316 ILE 316 316 316 ILE ILE A . n 
A 1 317 ASN 317 317 317 ASN ASN A . n 
A 1 318 THR 318 318 318 THR THR A . n 
A 1 319 GLY 319 319 319 GLY GLY A . n 
A 1 320 ASP 320 320 320 ASP ASP A . n 
A 1 321 PHE 321 321 321 PHE PHE A . n 
A 1 322 GLN 322 322 322 GLN GLN A . n 
A 1 323 ASP 323 323 323 ASP ASP A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 GLN 325 325 325 GLN GLN A . n 
A 1 326 VAL 326 326 326 VAL VAL A . n 
A 1 327 LEU 327 327 327 LEU LEU A . n 
A 1 328 VAL 328 328 328 VAL VAL A . n 
A 1 329 GLY 329 329 329 GLY GLY A . n 
A 1 330 VAL 330 330 330 VAL VAL A . n 
A 1 331 VAL 331 331 331 VAL VAL A . n 
A 1 332 LYS 332 332 332 LYS LYS A . n 
A 1 333 ASP 333 333 333 ASP ASP A . n 
A 1 334 GLU 334 334 334 GLU GLU A . n 
A 1 335 GLY 335 335 335 GLY GLY A . n 
A 1 336 SER 336 336 336 SER SER A . n 
A 1 337 TYR 337 337 337 TYR TYR A . n 
A 1 338 PHE 338 338 338 PHE PHE A . n 
A 1 339 LEU 339 339 339 LEU LEU A . n 
A 1 340 VAL 340 340 340 VAL VAL A . n 
A 1 341 TYR 341 341 341 TYR TYR A . n 
A 1 342 GLY 342 342 342 GLY GLY A . n 
A 1 343 VAL 343 343 343 VAL VAL A . n 
A 1 344 PRO 344 344 344 PRO PRO A . n 
A 1 345 GLY 345 345 345 GLY GLY A . n 
A 1 346 PHE 346 346 346 PHE PHE A . n 
A 1 347 SER 347 347 347 SER SER A . n 
A 1 348 LYS 348 348 348 LYS LYS A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 ASN 350 350 350 ASN ASN A . n 
A 1 351 GLU 351 351 351 GLU GLU A . n 
A 1 352 SER 352 352 352 SER SER A . n 
A 1 353 LEU 353 353 353 LEU LEU A . n 
A 1 354 ILE 354 354 354 ILE ILE A . n 
A 1 355 SER 355 355 355 SER SER A . n 
A 1 356 ARG 356 356 356 ARG ARG A . n 
A 1 357 ALA 357 357 357 ALA ALA A . n 
A 1 358 GLN 358 358 358 GLN GLN A . n 
A 1 359 PHE 359 359 359 PHE PHE A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 GLY 362 362 362 GLY GLY A . n 
A 1 363 VAL 363 363 363 VAL VAL A . n 
A 1 364 ARG 364 364 364 ARG ARG A . n 
A 1 365 ILE 365 365 365 ILE ILE A . n 
A 1 366 GLY 366 366 366 GLY GLY A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 PRO 368 368 368 PRO PRO A . n 
A 1 369 GLN 369 369 369 GLN GLN A . n 
A 1 370 ALA 370 370 370 ALA ALA A . n 
A 1 371 SER 371 371 371 SER SER A . n 
A 1 372 ASP 372 372 372 ASP ASP A . n 
A 1 373 LEU 373 373 373 LEU LEU A . n 
A 1 374 ALA 374 374 374 ALA ALA A . n 
A 1 375 ALA 375 375 375 ALA ALA A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 ALA 377 377 377 ALA ALA A . n 
A 1 378 VAL 378 378 378 VAL VAL A . n 
A 1 379 VAL 379 379 379 VAL VAL A . n 
A 1 380 LEU 380 380 380 LEU LEU A . n 
A 1 381 HIS 381 381 381 HIS HIS A . n 
A 1 382 TYR 382 382 382 TYR TYR A . n 
A 1 383 THR 383 383 383 THR THR A . n 
A 1 384 ASP 384 384 384 ASP ASP A . n 
A 1 385 TRP 385 385 385 TRP TRP A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 HIS 387 387 387 HIS HIS A . n 
A 1 388 PRO 388 388 388 PRO PRO A . n 
A 1 389 GLU 389 389 389 GLU GLU A . n 
A 1 390 ASP 390 390 390 ASP ASP A . n 
A 1 391 PRO 391 391 391 PRO PRO A . n 
A 1 392 THR 392 392 392 THR THR A . n 
A 1 393 HIS 393 393 393 HIS HIS A . n 
A 1 394 LEU 394 394 394 LEU LEU A . n 
A 1 395 ARG 395 395 395 ARG ARG A . n 
A 1 396 ASP 396 396 396 ASP ASP A . n 
A 1 397 ALA 397 397 397 ALA ALA A . n 
A 1 398 MET 398 398 398 MET MET A . n 
A 1 399 SER 399 399 399 SER SER A . n 
A 1 400 ALA 400 400 400 ALA ALA A . n 
A 1 401 VAL 401 401 401 VAL VAL A . n 
A 1 402 VAL 402 402 402 VAL VAL A . n 
A 1 403 GLY 403 403 403 GLY GLY A . n 
A 1 404 ASP 404 404 404 ASP ASP A . n 
A 1 405 HIS 405 405 405 HIS HIS A . n 
A 1 406 ASN 406 406 406 ASN ASN A . n 
A 1 407 VAL 407 407 407 VAL VAL A . n 
A 1 408 VAL 408 408 408 VAL VAL A . n 
A 1 409 CYS 409 409 409 CYS CYS A . n 
A 1 410 PRO 410 410 410 PRO PRO A . n 
A 1 411 VAL 411 411 411 VAL VAL A . n 
A 1 412 ALA 412 412 412 ALA ALA A . n 
A 1 413 GLN 413 413 413 GLN GLN A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 ALA 415 415 415 ALA ALA A . n 
A 1 416 GLY 416 416 416 GLY GLY A . n 
A 1 417 ARG 417 417 417 ARG ARG A . n 
A 1 418 LEU 418 418 418 LEU LEU A . n 
A 1 419 ALA 419 419 419 ALA ALA A . n 
A 1 420 ALA 420 420 420 ALA ALA A . n 
A 1 421 GLN 421 421 421 GLN GLN A . n 
A 1 422 GLY 422 422 422 GLY GLY A . n 
A 1 423 ALA 423 423 423 ALA ALA A . n 
A 1 424 ARG 424 424 424 ARG ARG A . n 
A 1 425 VAL 425 425 425 VAL VAL A . n 
A 1 426 TYR 426 426 426 TYR TYR A . n 
A 1 427 ALA 427 427 427 ALA ALA A . n 
A 1 428 TYR 428 428 428 TYR TYR A . n 
A 1 429 ILE 429 429 429 ILE ILE A . n 
A 1 430 PHE 430 430 430 PHE PHE A . n 
A 1 431 GLU 431 431 431 GLU GLU A . n 
A 1 432 HIS 432 432 432 HIS HIS A . n 
A 1 433 ARG 433 433 433 ARG ARG A . n 
A 1 434 ALA 434 434 434 ALA ALA A . n 
A 1 435 SER 435 435 435 SER SER A . n 
A 1 436 THR 436 436 436 THR THR A . n 
A 1 437 LEU 437 437 437 LEU LEU A . n 
A 1 438 THR 438 438 438 THR THR A . n 
A 1 439 TRP 439 439 439 TRP TRP A . n 
A 1 440 PRO 440 440 440 PRO PRO A . n 
A 1 441 LEU 441 441 441 LEU LEU A . n 
A 1 442 TRP 442 442 442 TRP TRP A . n 
A 1 443 MET 443 443 443 MET MET A . n 
A 1 444 GLY 444 444 444 GLY GLY A . n 
A 1 445 VAL 445 445 445 VAL VAL A . n 
A 1 446 PRO 446 446 446 PRO PRO A . n 
A 1 447 HIS 447 447 447 HIS HIS A . n 
A 1 448 GLY 448 448 448 GLY GLY A . n 
A 1 449 TYR 449 449 449 TYR TYR A . n 
A 1 450 GLU 450 450 450 GLU GLU A . n 
A 1 451 ILE 451 451 451 ILE ILE A . n 
A 1 452 GLU 452 452 452 GLU GLU A . n 
A 1 453 PHE 453 453 453 PHE PHE A . n 
A 1 454 ILE 454 454 454 ILE ILE A . n 
A 1 455 PHE 455 455 455 PHE PHE A . n 
A 1 456 GLY 456 456 456 GLY GLY A . n 
A 1 457 LEU 457 457 457 LEU LEU A . n 
A 1 458 PRO 458 458 458 PRO PRO A . n 
A 1 459 LEU 459 459 459 LEU LEU A . n 
A 1 460 ASP 460 460 460 ASP ASP A . n 
A 1 461 PRO 461 461 461 PRO PRO A . n 
A 1 462 SER 462 462 462 SER SER A . n 
A 1 463 LEU 463 463 463 LEU LEU A . n 
A 1 464 ASN 464 464 464 ASN ASN A . n 
A 1 465 TYR 465 465 465 TYR TYR A . n 
A 1 466 THR 466 466 466 THR THR A . n 
A 1 467 THR 467 467 467 THR THR A . n 
A 1 468 GLU 468 468 468 GLU GLU A . n 
A 1 469 GLU 469 469 469 GLU GLU A . n 
A 1 470 ARG 470 470 470 ARG ARG A . n 
A 1 471 ILE 471 471 471 ILE ILE A . n 
A 1 472 PHE 472 472 472 PHE PHE A . n 
A 1 473 ALA 473 473 473 ALA ALA A . n 
A 1 474 GLN 474 474 474 GLN GLN A . n 
A 1 475 ARG 475 475 475 ARG ARG A . n 
A 1 476 LEU 476 476 476 LEU LEU A . n 
A 1 477 MET 477 477 477 MET MET A . n 
A 1 478 LYS 478 478 478 LYS LYS A . n 
A 1 479 TYR 479 479 479 TYR TYR A . n 
A 1 480 TRP 480 480 480 TRP TRP A . n 
A 1 481 THR 481 481 481 THR THR A . n 
A 1 482 ASN 482 482 482 ASN ASN A . n 
A 1 483 PHE 483 483 483 PHE PHE A . n 
A 1 484 ALA 484 484 484 ALA ALA A . n 
A 1 485 ARG 485 485 485 ARG ARG A . n 
A 1 486 THR 486 486 486 THR THR A . n 
A 1 487 GLY 487 487 487 GLY GLY A . n 
A 1 488 ASP 488 488 488 ASP ASP A . n 
A 1 489 PRO 489 489 489 PRO PRO A . n 
A 1 490 ASN 490 490 490 ASN ASN A . n 
A 1 491 ASP 491 491 491 ASP ASP A . n 
A 1 492 PRO 492 492 492 PRO PRO A . n 
A 1 493 ARG 493 493 493 ARG ARG A . n 
A 1 494 ASP 494 494 494 ASP ASP A . n 
A 1 495 SER 495 495 495 SER SER A . n 
A 1 496 LYS 496 496 496 LYS LYS A . n 
A 1 497 SER 497 497 497 SER SER A . n 
A 1 498 PRO 498 498 498 PRO PRO A . n 
A 1 499 GLN 499 499 499 GLN GLN A . n 
A 1 500 TRP 500 500 500 TRP TRP A . n 
A 1 501 PRO 501 501 501 PRO PRO A . n 
A 1 502 PRO 502 502 502 PRO PRO A . n 
A 1 503 TYR 503 503 503 TYR TYR A . n 
A 1 504 THR 504 504 504 THR THR A . n 
A 1 505 THR 505 505 505 THR THR A . n 
A 1 506 ALA 506 506 506 ALA ALA A . n 
A 1 507 ALA 507 507 507 ALA ALA A . n 
A 1 508 GLN 508 508 508 GLN GLN A . n 
A 1 509 GLN 509 509 509 GLN GLN A . n 
A 1 510 TYR 510 510 510 TYR TYR A . n 
A 1 511 VAL 511 511 511 VAL VAL A . n 
A 1 512 SER 512 512 512 SER SER A . n 
A 1 513 LEU 513 513 513 LEU LEU A . n 
A 1 514 ASN 514 514 514 ASN ASN A . n 
A 1 515 LEU 515 515 515 LEU LEU A . n 
A 1 516 LYS 516 516 516 LYS LYS A . n 
A 1 517 PRO 517 517 517 PRO PRO A . n 
A 1 518 LEU 518 518 518 LEU LEU A . n 
A 1 519 GLU 519 519 519 GLU GLU A . n 
A 1 520 VAL 520 520 520 VAL VAL A . n 
A 1 521 ARG 521 521 521 ARG ARG A . n 
A 1 522 ARG 522 522 522 ARG ARG A . n 
A 1 523 GLY 523 523 523 GLY GLY A . n 
A 1 524 LEU 524 524 524 LEU LEU A . n 
A 1 525 ARG 525 525 525 ARG ARG A . n 
A 1 526 ALA 526 526 526 ALA ALA A . n 
A 1 527 GLN 527 527 527 GLN GLN A . n 
A 1 528 THR 528 528 528 THR THR A . n 
A 1 529 CYS 529 529 529 CYS CYS A . n 
A 1 530 ALA 530 530 530 ALA ALA A . n 
A 1 531 PHE 531 531 531 PHE PHE A . n 
A 1 532 TRP 532 532 532 TRP TRP A . n 
A 1 533 ASN 533 533 533 ASN ASN A . n 
A 1 534 ARG 534 534 534 ARG ARG A . n 
A 1 535 PHE 535 535 535 PHE PHE A . n 
A 1 536 LEU 536 536 536 LEU LEU A . n 
A 1 537 PRO 537 537 537 PRO PRO A . n 
A 1 538 LYS 538 538 538 LYS LYS A . n 
A 1 539 LEU 539 539 539 LEU LEU A . n 
A 1 540 LEU 540 540 540 LEU LEU A . n 
A 1 541 SER 541 541 541 SER SER A . n 
A 1 542 ALA 542 542 542 ALA ALA A . n 
A 1 543 THR 543 543 543 THR THR A . n 
B 1 1   GLU 1   1   ?   ?   ?   B . n 
B 1 2   GLY 2   2   ?   ?   ?   B . n 
B 1 3   ARG 3   3   ?   ?   ?   B . n 
B 1 4   GLU 4   4   ?   ?   ?   B . n 
B 1 5   ASP 5   5   5   ASP ASP B . n 
B 1 6   PRO 6   6   6   PRO PRO B . n 
B 1 7   GLN 7   7   7   GLN GLN B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  VAL 10  10  10  VAL VAL B . n 
B 1 11  ARG 11  11  11  ARG ARG B . n 
B 1 12  VAL 12  12  12  VAL VAL B . n 
B 1 13  ARG 13  13  13  ARG ARG B . n 
B 1 14  GLY 14  14  14  GLY GLY B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  GLN 16  16  16  GLN GLN B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  ARG 18  18  18  ARG ARG B . n 
B 1 19  GLY 19  19  19  GLY GLY B . n 
B 1 20  ILE 20  20  20  ILE ILE B . n 
B 1 21  ARG 21  21  21  ARG ARG B . n 
B 1 22  LEU 22  22  22  LEU LEU B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  ALA 24  24  24  ALA ALA B . n 
B 1 25  PRO 25  25  25  PRO PRO B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  SER 30  30  30  SER SER B . n 
B 1 31  ALA 31  31  31  ALA ALA B . n 
B 1 32  PHE 32  32  32  PHE PHE B . n 
B 1 33  LEU 33  33  33  LEU LEU B . n 
B 1 34  GLY 34  34  34  GLY GLY B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  PRO 36  36  36  PRO PRO B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  PRO 40  40  40  PRO PRO B . n 
B 1 41  PRO 41  41  41  PRO PRO B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  GLY 43  43  43  GLY GLY B . n 
B 1 44  SER 44  44  44  SER SER B . n 
B 1 45  ARG 45  45  45  ARG ARG B . n 
B 1 46  ARG 46  46  46  ARG ARG B . n 
B 1 47  PHE 47  47  47  PHE PHE B . n 
B 1 48  MET 48  48  48  MET MET B . n 
B 1 49  PRO 49  49  49  PRO PRO B . n 
B 1 50  PRO 50  50  50  PRO PRO B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  PRO 52  52  52  PRO PRO B . n 
B 1 53  LYS 53  53  53  LYS LYS B . n 
B 1 54  ARG 54  54  54  ARG ARG B . n 
B 1 55  PRO 55  55  55  PRO PRO B . n 
B 1 56  TRP 56  56  56  TRP TRP B . n 
B 1 57  SER 57  57  57  SER SER B . n 
B 1 58  GLY 58  58  58  GLY GLY B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  ASP 61  61  61  ASP ASP B . n 
B 1 62  ALA 62  62  62  ALA ALA B . n 
B 1 63  THR 63  63  63  THR THR B . n 
B 1 64  THR 64  64  64  THR THR B . n 
B 1 65  PHE 65  65  65  PHE PHE B . n 
B 1 66  GLN 66  66  66  GLN GLN B . n 
B 1 67  ASN 67  67  67  ASN ASN B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  CYS 69  69  69  CYS CYS B . n 
B 1 70  TYR 70  70  70  TYR TYR B . n 
B 1 71  GLN 71  71  71  GLN GLN B . n 
B 1 72  TYR 72  72  72  TYR TYR B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  THR 75  75  75  THR THR B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  TYR 77  77  77  TYR TYR B . n 
B 1 78  PRO 78  78  78  PRO PRO B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  PHE 80  80  80  PHE PHE B . n 
B 1 81  GLU 81  81  81  GLU GLU B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  THR 83  83  83  THR THR B . n 
B 1 84  GLU 84  84  84  GLU GLU B . n 
B 1 85  MET 85  85  85  MET MET B . n 
B 1 86  TRP 86  86  86  TRP TRP B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  PRO 88  88  88  PRO PRO B . n 
B 1 89  ASN 89  89  89  ASN ASN B . n 
B 1 90  ARG 90  90  90  ARG ARG B . n 
B 1 91  GLU 91  91  91  GLU GLU B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  GLU 94  94  94  GLU GLU B . n 
B 1 95  ASP 95  95  95  ASP ASP B . n 
B 1 96  CYS 96  96  96  CYS CYS B . n 
B 1 97  LEU 97  97  97  LEU LEU B . n 
B 1 98  TYR 98  98  98  TYR TYR B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 ASN 100 100 100 ASN ASN B . n 
B 1 101 VAL 101 101 101 VAL VAL B . n 
B 1 102 TRP 102 102 102 TRP TRP B . n 
B 1 103 THR 103 103 103 THR THR B . n 
B 1 104 PRO 104 104 104 PRO PRO B . n 
B 1 105 TYR 105 105 105 TYR TYR B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 ARG 107 107 107 ARG ARG B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 SER 110 110 110 SER SER B . n 
B 1 111 PRO 111 111 111 PRO PRO B . n 
B 1 112 THR 112 112 112 THR THR B . n 
B 1 113 PRO 113 113 113 PRO PRO B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 ILE 116 116 116 ILE ILE B . n 
B 1 117 TRP 117 117 117 TRP TRP B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 TYR 119 119 119 TYR TYR B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 GLY 121 121 121 GLY GLY B . n 
B 1 122 GLY 122 122 122 GLY GLY B . n 
B 1 123 PHE 123 123 123 PHE PHE B . n 
B 1 124 TYR 124 124 124 TYR TYR B . n 
B 1 125 SER 125 125 125 SER SER B . n 
B 1 126 GLY 126 126 126 GLY GLY B . n 
B 1 127 ALA 127 127 127 ALA ALA B . n 
B 1 128 ALA 128 128 128 ALA ALA B . n 
B 1 129 SER 129 129 129 SER SER B . n 
B 1 130 LEU 130 130 130 LEU LEU B . n 
B 1 131 ASP 131 131 131 ASP ASP B . n 
B 1 132 VAL 132 132 132 VAL VAL B . n 
B 1 133 TYR 133 133 133 TYR TYR B . n 
B 1 134 ASP 134 134 134 ASP ASP B . n 
B 1 135 GLY 135 135 135 GLY GLY B . n 
B 1 136 ARG 136 136 136 ARG ARG B . n 
B 1 137 PHE 137 137 137 PHE PHE B . n 
B 1 138 LEU 138 138 138 LEU LEU B . n 
B 1 139 ALA 139 139 139 ALA ALA B . n 
B 1 140 GLN 140 140 140 GLN GLN B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 GLU 142 142 142 GLU GLU B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 ALA 144 144 144 ALA ALA B . n 
B 1 145 VAL 145 145 145 VAL VAL B . n 
B 1 146 LEU 146 146 146 LEU LEU B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 SER 148 148 148 SER SER B . n 
B 1 149 MET 149 149 149 MET MET B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 TYR 151 151 151 TYR TYR B . n 
B 1 152 ARG 152 152 152 ARG ARG B . n 
B 1 153 VAL 153 153 153 VAL VAL B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 THR 155 155 155 THR THR B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 GLY 157 157 157 GLY GLY B . n 
B 1 158 PHE 158 158 158 PHE PHE B . n 
B 1 159 LEU 159 159 159 LEU LEU B . n 
B 1 160 ALA 160 160 160 ALA ALA B . n 
B 1 161 LEU 161 161 161 LEU LEU B . n 
B 1 162 PRO 162 162 162 PRO PRO B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 SER 164 164 164 SER SER B . n 
B 1 165 ARG 165 165 165 ARG ARG B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 ALA 167 167 167 ALA ALA B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 ASN 170 170 170 ASN ASN B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 GLY 172 172 172 GLY GLY B . n 
B 1 173 LEU 173 173 173 LEU LEU B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 ASP 175 175 175 ASP ASP B . n 
B 1 176 GLN 176 176 176 GLN GLN B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 LEU 178 178 178 LEU LEU B . n 
B 1 179 ALA 179 179 179 ALA ALA B . n 
B 1 180 LEU 180 180 180 LEU LEU B . n 
B 1 181 GLN 181 181 181 GLN GLN B . n 
B 1 182 TRP 182 182 182 TRP TRP B . n 
B 1 183 VAL 183 183 183 VAL VAL B . n 
B 1 184 GLN 184 184 184 GLN GLN B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 ASN 186 186 186 ASN ASN B . n 
B 1 187 ILE 187 187 187 ILE ILE B . n 
B 1 188 ALA 188 188 188 ALA ALA B . n 
B 1 189 ALA 189 189 189 ALA ALA B . n 
B 1 190 PHE 190 190 190 PHE PHE B . n 
B 1 191 GLY 191 191 191 GLY GLY B . n 
B 1 192 GLY 192 192 192 GLY GLY B . n 
B 1 193 ASP 193 193 193 ASP ASP B . n 
B 1 194 PRO 194 194 194 PRO PRO B . n 
B 1 195 MET 195 195 195 MET MET B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 VAL 197 197 197 VAL VAL B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 LEU 199 199 199 LEU LEU B . n 
B 1 200 PHE 200 200 200 PHE PHE B . n 
B 1 201 GLY 201 201 201 GLY GLY B . n 
B 1 202 GLU 202 202 202 GLU GLU B . n 
B 1 203 SER 203 203 203 SER SER B . n 
B 1 204 ALA 204 204 204 ALA ALA B . n 
B 1 205 GLY 205 205 205 GLY GLY B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 ALA 207 207 207 ALA ALA B . n 
B 1 208 SER 208 208 208 SER SER B . n 
B 1 209 VAL 209 209 209 VAL VAL B . n 
B 1 210 GLY 210 210 210 GLY GLY B . n 
B 1 211 MET 211 211 211 MET MET B . n 
B 1 212 HIS 212 212 212 HIS HIS B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 LEU 214 214 214 LEU LEU B . n 
B 1 215 SER 215 215 215 SER SER B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 PRO 217 217 217 PRO PRO B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 ARG 219 219 219 ARG ARG B . n 
B 1 220 SER 220 220 220 SER SER B . n 
B 1 221 LEU 221 221 221 LEU LEU B . n 
B 1 222 PHE 222 222 222 PHE PHE B . n 
B 1 223 HIS 223 223 223 HIS HIS B . n 
B 1 224 ARG 224 224 224 ARG ARG B . n 
B 1 225 ALA 225 225 225 ALA ALA B . n 
B 1 226 VAL 226 226 226 VAL VAL B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 GLN 228 228 228 GLN GLN B . n 
B 1 229 SER 229 229 229 SER SER B . n 
B 1 230 GLY 230 230 230 GLY GLY B . n 
B 1 231 THR 231 231 231 THR THR B . n 
B 1 232 PRO 232 232 232 PRO PRO B . n 
B 1 233 ASN 233 233 233 ASN ASN B . n 
B 1 234 GLY 234 234 234 GLY GLY B . n 
B 1 235 PRO 235 235 235 PRO PRO B . n 
B 1 236 TRP 236 236 236 TRP TRP B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 THR 238 238 238 THR THR B . n 
B 1 239 VAL 239 239 239 VAL VAL B . n 
B 1 240 SER 240 240 240 SER SER B . n 
B 1 241 ALA 241 241 241 ALA ALA B . n 
B 1 242 GLY 242 242 242 GLY GLY B . n 
B 1 243 GLU 243 243 243 GLU GLU B . n 
B 1 244 ALA 244 244 244 ALA ALA B . n 
B 1 245 ARG 245 245 245 ARG ARG B . n 
B 1 246 ARG 246 246 246 ARG ARG B . n 
B 1 247 ARG 247 247 247 ARG ARG B . n 
B 1 248 ALA 248 248 248 ALA ALA B . n 
B 1 249 THR 249 249 249 THR THR B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 LEU 251 251 251 LEU LEU B . n 
B 1 252 ALA 252 252 252 ALA ALA B . n 
B 1 253 ARG 253 253 253 ARG ARG B . n 
B 1 254 LEU 254 254 254 LEU LEU B . n 
B 1 255 VAL 255 255 255 VAL VAL B . n 
B 1 256 GLY 256 256 256 GLY GLY B . n 
B 1 257 CYS 257 257 257 CYS CYS B . n 
B 1 258 PRO 258 258 258 PRO PRO B . n 
B 1 259 PRO 259 259 259 PRO PRO B . n 
B 1 260 GLY 260 260 260 GLY GLY B . n 
B 1 261 GLY 261 261 261 GLY GLY B . n 
B 1 262 ALA 262 262 262 ALA ALA B . n 
B 1 263 GLY 263 263 263 GLY GLY B . n 
B 1 264 GLY 264 264 264 GLY GLY B . n 
B 1 265 ASN 265 265 265 ASN ASN B . n 
B 1 266 ASP 266 266 266 ASP ASP B . n 
B 1 267 THR 267 267 267 THR THR B . n 
B 1 268 GLU 268 268 268 GLU GLU B . n 
B 1 269 LEU 269 269 269 LEU LEU B . n 
B 1 270 ILE 270 270 270 ILE ILE B . n 
B 1 271 ALA 271 271 271 ALA ALA B . n 
B 1 272 CYS 272 272 272 CYS CYS B . n 
B 1 273 LEU 273 273 273 LEU LEU B . n 
B 1 274 ARG 274 274 274 ARG ARG B . n 
B 1 275 THR 275 275 275 THR THR B . n 
B 1 276 ARG 276 276 276 ARG ARG B . n 
B 1 277 PRO 277 277 277 PRO PRO B . n 
B 1 278 ALA 278 278 278 ALA ALA B . n 
B 1 279 GLN 279 279 279 GLN GLN B . n 
B 1 280 ASP 280 280 280 ASP ASP B . n 
B 1 281 LEU 281 281 281 LEU LEU B . n 
B 1 282 VAL 282 282 282 VAL VAL B . n 
B 1 283 ASP 283 283 283 ASP ASP B . n 
B 1 284 HIS 284 284 284 HIS HIS B . n 
B 1 285 GLU 285 285 285 GLU GLU B . n 
B 1 286 TRP 286 286 286 TRP TRP B . n 
B 1 287 HIS 287 287 287 HIS HIS B . n 
B 1 288 VAL 288 288 288 VAL VAL B . n 
B 1 289 LEU 289 289 289 LEU LEU B . n 
B 1 290 PRO 290 290 290 PRO PRO B . n 
B 1 291 GLN 291 291 291 GLN GLN B . n 
B 1 292 GLU 292 292 292 GLU GLU B . n 
B 1 293 SER 293 293 293 SER SER B . n 
B 1 294 ILE 294 294 294 ILE ILE B . n 
B 1 295 PHE 295 295 295 PHE PHE B . n 
B 1 296 ARG 296 296 296 ARG ARG B . n 
B 1 297 PHE 297 297 297 PHE PHE B . n 
B 1 298 SER 298 298 298 SER SER B . n 
B 1 299 PHE 299 299 299 PHE PHE B . n 
B 1 300 VAL 300 300 300 VAL VAL B . n 
B 1 301 PRO 301 301 301 PRO PRO B . n 
B 1 302 VAL 302 302 302 VAL VAL B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 ASP 304 304 304 ASP ASP B . n 
B 1 305 GLY 305 305 305 GLY GLY B . n 
B 1 306 ASP 306 306 306 ASP ASP B . n 
B 1 307 PHE 307 307 307 PHE PHE B . n 
B 1 308 LEU 308 308 308 LEU LEU B . n 
B 1 309 SER 309 309 309 SER SER B . n 
B 1 310 ASP 310 310 310 ASP ASP B . n 
B 1 311 THR 311 311 311 THR THR B . n 
B 1 312 PRO 312 312 312 PRO PRO B . n 
B 1 313 GLU 313 313 313 GLU GLU B . n 
B 1 314 ALA 314 314 314 ALA ALA B . n 
B 1 315 LEU 315 315 315 LEU LEU B . n 
B 1 316 ILE 316 316 316 ILE ILE B . n 
B 1 317 ASN 317 317 317 ASN ASN B . n 
B 1 318 THR 318 318 318 THR THR B . n 
B 1 319 GLY 319 319 319 GLY GLY B . n 
B 1 320 ASP 320 320 320 ASP ASP B . n 
B 1 321 PHE 321 321 321 PHE PHE B . n 
B 1 322 GLN 322 322 322 GLN GLN B . n 
B 1 323 ASP 323 323 323 ASP ASP B . n 
B 1 324 LEU 324 324 324 LEU LEU B . n 
B 1 325 GLN 325 325 325 GLN GLN B . n 
B 1 326 VAL 326 326 326 VAL VAL B . n 
B 1 327 LEU 327 327 327 LEU LEU B . n 
B 1 328 VAL 328 328 328 VAL VAL B . n 
B 1 329 GLY 329 329 329 GLY GLY B . n 
B 1 330 VAL 330 330 330 VAL VAL B . n 
B 1 331 VAL 331 331 331 VAL VAL B . n 
B 1 332 LYS 332 332 332 LYS LYS B . n 
B 1 333 ASP 333 333 333 ASP ASP B . n 
B 1 334 GLU 334 334 334 GLU GLU B . n 
B 1 335 GLY 335 335 335 GLY GLY B . n 
B 1 336 SER 336 336 336 SER SER B . n 
B 1 337 TYR 337 337 337 TYR TYR B . n 
B 1 338 PHE 338 338 338 PHE PHE B . n 
B 1 339 LEU 339 339 339 LEU LEU B . n 
B 1 340 VAL 340 340 340 VAL VAL B . n 
B 1 341 TYR 341 341 341 TYR TYR B . n 
B 1 342 GLY 342 342 342 GLY GLY B . n 
B 1 343 VAL 343 343 343 VAL VAL B . n 
B 1 344 PRO 344 344 344 PRO PRO B . n 
B 1 345 GLY 345 345 345 GLY GLY B . n 
B 1 346 PHE 346 346 346 PHE PHE B . n 
B 1 347 SER 347 347 347 SER SER B . n 
B 1 348 LYS 348 348 348 LYS LYS B . n 
B 1 349 ASP 349 349 349 ASP ASP B . n 
B 1 350 ASN 350 350 350 ASN ASN B . n 
B 1 351 GLU 351 351 351 GLU GLU B . n 
B 1 352 SER 352 352 352 SER SER B . n 
B 1 353 LEU 353 353 353 LEU LEU B . n 
B 1 354 ILE 354 354 354 ILE ILE B . n 
B 1 355 SER 355 355 355 SER SER B . n 
B 1 356 ARG 356 356 356 ARG ARG B . n 
B 1 357 ALA 357 357 357 ALA ALA B . n 
B 1 358 GLN 358 358 358 GLN GLN B . n 
B 1 359 PHE 359 359 359 PHE PHE B . n 
B 1 360 LEU 360 360 360 LEU LEU B . n 
B 1 361 ALA 361 361 361 ALA ALA B . n 
B 1 362 GLY 362 362 362 GLY GLY B . n 
B 1 363 VAL 363 363 363 VAL VAL B . n 
B 1 364 ARG 364 364 364 ARG ARG B . n 
B 1 365 ILE 365 365 365 ILE ILE B . n 
B 1 366 GLY 366 366 366 GLY GLY B . n 
B 1 367 VAL 367 367 367 VAL VAL B . n 
B 1 368 PRO 368 368 368 PRO PRO B . n 
B 1 369 GLN 369 369 369 GLN GLN B . n 
B 1 370 ALA 370 370 370 ALA ALA B . n 
B 1 371 SER 371 371 371 SER SER B . n 
B 1 372 ASP 372 372 372 ASP ASP B . n 
B 1 373 LEU 373 373 373 LEU LEU B . n 
B 1 374 ALA 374 374 374 ALA ALA B . n 
B 1 375 ALA 375 375 375 ALA ALA B . n 
B 1 376 GLU 376 376 376 GLU GLU B . n 
B 1 377 ALA 377 377 377 ALA ALA B . n 
B 1 378 VAL 378 378 378 VAL VAL B . n 
B 1 379 VAL 379 379 379 VAL VAL B . n 
B 1 380 LEU 380 380 380 LEU LEU B . n 
B 1 381 HIS 381 381 381 HIS HIS B . n 
B 1 382 TYR 382 382 382 TYR TYR B . n 
B 1 383 THR 383 383 383 THR THR B . n 
B 1 384 ASP 384 384 384 ASP ASP B . n 
B 1 385 TRP 385 385 385 TRP TRP B . n 
B 1 386 LEU 386 386 386 LEU LEU B . n 
B 1 387 HIS 387 387 387 HIS HIS B . n 
B 1 388 PRO 388 388 388 PRO PRO B . n 
B 1 389 GLU 389 389 389 GLU GLU B . n 
B 1 390 ASP 390 390 390 ASP ASP B . n 
B 1 391 PRO 391 391 391 PRO PRO B . n 
B 1 392 THR 392 392 392 THR THR B . n 
B 1 393 HIS 393 393 393 HIS HIS B . n 
B 1 394 LEU 394 394 394 LEU LEU B . n 
B 1 395 ARG 395 395 395 ARG ARG B . n 
B 1 396 ASP 396 396 396 ASP ASP B . n 
B 1 397 ALA 397 397 397 ALA ALA B . n 
B 1 398 MET 398 398 398 MET MET B . n 
B 1 399 SER 399 399 399 SER SER B . n 
B 1 400 ALA 400 400 400 ALA ALA B . n 
B 1 401 VAL 401 401 401 VAL VAL B . n 
B 1 402 VAL 402 402 402 VAL VAL B . n 
B 1 403 GLY 403 403 403 GLY GLY B . n 
B 1 404 ASP 404 404 404 ASP ASP B . n 
B 1 405 HIS 405 405 405 HIS HIS B . n 
B 1 406 ASN 406 406 406 ASN ASN B . n 
B 1 407 VAL 407 407 407 VAL VAL B . n 
B 1 408 VAL 408 408 408 VAL VAL B . n 
B 1 409 CYS 409 409 409 CYS CYS B . n 
B 1 410 PRO 410 410 410 PRO PRO B . n 
B 1 411 VAL 411 411 411 VAL VAL B . n 
B 1 412 ALA 412 412 412 ALA ALA B . n 
B 1 413 GLN 413 413 413 GLN GLN B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 ALA 415 415 415 ALA ALA B . n 
B 1 416 GLY 416 416 416 GLY GLY B . n 
B 1 417 ARG 417 417 417 ARG ARG B . n 
B 1 418 LEU 418 418 418 LEU LEU B . n 
B 1 419 ALA 419 419 419 ALA ALA B . n 
B 1 420 ALA 420 420 420 ALA ALA B . n 
B 1 421 GLN 421 421 421 GLN GLN B . n 
B 1 422 GLY 422 422 422 GLY GLY B . n 
B 1 423 ALA 423 423 423 ALA ALA B . n 
B 1 424 ARG 424 424 424 ARG ARG B . n 
B 1 425 VAL 425 425 425 VAL VAL B . n 
B 1 426 TYR 426 426 426 TYR TYR B . n 
B 1 427 ALA 427 427 427 ALA ALA B . n 
B 1 428 TYR 428 428 428 TYR TYR B . n 
B 1 429 ILE 429 429 429 ILE ILE B . n 
B 1 430 PHE 430 430 430 PHE PHE B . n 
B 1 431 GLU 431 431 431 GLU GLU B . n 
B 1 432 HIS 432 432 432 HIS HIS B . n 
B 1 433 ARG 433 433 433 ARG ARG B . n 
B 1 434 ALA 434 434 434 ALA ALA B . n 
B 1 435 SER 435 435 435 SER SER B . n 
B 1 436 THR 436 436 436 THR THR B . n 
B 1 437 LEU 437 437 437 LEU LEU B . n 
B 1 438 THR 438 438 438 THR THR B . n 
B 1 439 TRP 439 439 439 TRP TRP B . n 
B 1 440 PRO 440 440 440 PRO PRO B . n 
B 1 441 LEU 441 441 441 LEU LEU B . n 
B 1 442 TRP 442 442 442 TRP TRP B . n 
B 1 443 MET 443 443 443 MET MET B . n 
B 1 444 GLY 444 444 444 GLY GLY B . n 
B 1 445 VAL 445 445 445 VAL VAL B . n 
B 1 446 PRO 446 446 446 PRO PRO B . n 
B 1 447 HIS 447 447 447 HIS HIS B . n 
B 1 448 GLY 448 448 448 GLY GLY B . n 
B 1 449 TYR 449 449 449 TYR TYR B . n 
B 1 450 GLU 450 450 450 GLU GLU B . n 
B 1 451 ILE 451 451 451 ILE ILE B . n 
B 1 452 GLU 452 452 452 GLU GLU B . n 
B 1 453 PHE 453 453 453 PHE PHE B . n 
B 1 454 ILE 454 454 454 ILE ILE B . n 
B 1 455 PHE 455 455 455 PHE PHE B . n 
B 1 456 GLY 456 456 456 GLY GLY B . n 
B 1 457 LEU 457 457 457 LEU LEU B . n 
B 1 458 PRO 458 458 458 PRO PRO B . n 
B 1 459 LEU 459 459 459 LEU LEU B . n 
B 1 460 ASP 460 460 460 ASP ASP B . n 
B 1 461 PRO 461 461 461 PRO PRO B . n 
B 1 462 SER 462 462 462 SER SER B . n 
B 1 463 LEU 463 463 463 LEU LEU B . n 
B 1 464 ASN 464 464 464 ASN ASN B . n 
B 1 465 TYR 465 465 465 TYR TYR B . n 
B 1 466 THR 466 466 466 THR THR B . n 
B 1 467 THR 467 467 467 THR THR B . n 
B 1 468 GLU 468 468 468 GLU GLU B . n 
B 1 469 GLU 469 469 469 GLU GLU B . n 
B 1 470 ARG 470 470 470 ARG ARG B . n 
B 1 471 ILE 471 471 471 ILE ILE B . n 
B 1 472 PHE 472 472 472 PHE PHE B . n 
B 1 473 ALA 473 473 473 ALA ALA B . n 
B 1 474 GLN 474 474 474 GLN GLN B . n 
B 1 475 ARG 475 475 475 ARG ARG B . n 
B 1 476 LEU 476 476 476 LEU LEU B . n 
B 1 477 MET 477 477 477 MET MET B . n 
B 1 478 LYS 478 478 478 LYS LYS B . n 
B 1 479 TYR 479 479 479 TYR TYR B . n 
B 1 480 TRP 480 480 480 TRP TRP B . n 
B 1 481 THR 481 481 481 THR THR B . n 
B 1 482 ASN 482 482 482 ASN ASN B . n 
B 1 483 PHE 483 483 483 PHE PHE B . n 
B 1 484 ALA 484 484 484 ALA ALA B . n 
B 1 485 ARG 485 485 485 ARG ARG B . n 
B 1 486 THR 486 486 486 THR THR B . n 
B 1 487 GLY 487 487 487 GLY GLY B . n 
B 1 488 ASP 488 488 488 ASP ASP B . n 
B 1 489 PRO 489 489 489 PRO PRO B . n 
B 1 490 ASN 490 490 490 ASN ASN B . n 
B 1 491 ASP 491 491 491 ASP ASP B . n 
B 1 492 PRO 492 492 492 PRO PRO B . n 
B 1 493 ARG 493 493 493 ARG ARG B . n 
B 1 494 ASP 494 494 494 ASP ASP B . n 
B 1 495 SER 495 495 495 SER SER B . n 
B 1 496 LYS 496 496 496 LYS LYS B . n 
B 1 497 SER 497 497 497 SER SER B . n 
B 1 498 PRO 498 498 498 PRO PRO B . n 
B 1 499 GLN 499 499 499 GLN GLN B . n 
B 1 500 TRP 500 500 500 TRP TRP B . n 
B 1 501 PRO 501 501 501 PRO PRO B . n 
B 1 502 PRO 502 502 502 PRO PRO B . n 
B 1 503 TYR 503 503 503 TYR TYR B . n 
B 1 504 THR 504 504 504 THR THR B . n 
B 1 505 THR 505 505 505 THR THR B . n 
B 1 506 ALA 506 506 506 ALA ALA B . n 
B 1 507 ALA 507 507 507 ALA ALA B . n 
B 1 508 GLN 508 508 508 GLN GLN B . n 
B 1 509 GLN 509 509 509 GLN GLN B . n 
B 1 510 TYR 510 510 510 TYR TYR B . n 
B 1 511 VAL 511 511 511 VAL VAL B . n 
B 1 512 SER 512 512 512 SER SER B . n 
B 1 513 LEU 513 513 513 LEU LEU B . n 
B 1 514 ASN 514 514 514 ASN ASN B . n 
B 1 515 LEU 515 515 515 LEU LEU B . n 
B 1 516 LYS 516 516 516 LYS LYS B . n 
B 1 517 PRO 517 517 517 PRO PRO B . n 
B 1 518 LEU 518 518 518 LEU LEU B . n 
B 1 519 GLU 519 519 519 GLU GLU B . n 
B 1 520 VAL 520 520 520 VAL VAL B . n 
B 1 521 ARG 521 521 521 ARG ARG B . n 
B 1 522 ARG 522 522 522 ARG ARG B . n 
B 1 523 GLY 523 523 523 GLY GLY B . n 
B 1 524 LEU 524 524 524 LEU LEU B . n 
B 1 525 ARG 525 525 525 ARG ARG B . n 
B 1 526 ALA 526 526 526 ALA ALA B . n 
B 1 527 GLN 527 527 527 GLN GLN B . n 
B 1 528 THR 528 528 528 THR THR B . n 
B 1 529 CYS 529 529 529 CYS CYS B . n 
B 1 530 ALA 530 530 530 ALA ALA B . n 
B 1 531 PHE 531 531 531 PHE PHE B . n 
B 1 532 TRP 532 532 532 TRP TRP B . n 
B 1 533 ASN 533 533 533 ASN ASN B . n 
B 1 534 ARG 534 534 534 ARG ARG B . n 
B 1 535 PHE 535 535 535 PHE PHE B . n 
B 1 536 LEU 536 536 536 LEU LEU B . n 
B 1 537 PRO 537 537 537 PRO PRO B . n 
B 1 538 LYS 538 538 538 LYS LYS B . n 
B 1 539 LEU 539 539 539 LEU LEU B . n 
B 1 540 LEU 540 540 540 LEU LEU B . n 
B 1 541 SER 541 541 541 SER SER B . n 
B 1 542 ALA 542 542 542 ALA ALA B . n 
B 1 543 THR 543 543 543 THR THR B . n 
C 1 1   GLU 1   1   ?   ?   ?   C . n 
C 1 2   GLY 2   2   ?   ?   ?   C . n 
C 1 3   ARG 3   3   ?   ?   ?   C . n 
C 1 4   GLU 4   4   4   GLU GLU C . n 
C 1 5   ASP 5   5   5   ASP ASP C . n 
C 1 6   PRO 6   6   6   PRO PRO C . n 
C 1 7   GLN 7   7   7   GLN GLN C . n 
C 1 8   LEU 8   8   8   LEU LEU C . n 
C 1 9   LEU 9   9   9   LEU LEU C . n 
C 1 10  VAL 10  10  10  VAL VAL C . n 
C 1 11  ARG 11  11  11  ARG ARG C . n 
C 1 12  VAL 12  12  12  VAL VAL C . n 
C 1 13  ARG 13  13  13  ARG ARG C . n 
C 1 14  GLY 14  14  14  GLY GLY C . n 
C 1 15  GLY 15  15  15  GLY GLY C . n 
C 1 16  GLN 16  16  16  GLN GLN C . n 
C 1 17  LEU 17  17  17  LEU LEU C . n 
C 1 18  ARG 18  18  18  ARG ARG C . n 
C 1 19  GLY 19  19  19  GLY GLY C . n 
C 1 20  ILE 20  20  20  ILE ILE C . n 
C 1 21  ARG 21  21  21  ARG ARG C . n 
C 1 22  LEU 22  22  22  LEU LEU C . n 
C 1 23  LYS 23  23  23  LYS LYS C . n 
C 1 24  ALA 24  24  24  ALA ALA C . n 
C 1 25  PRO 25  25  25  PRO PRO C . n 
C 1 26  GLY 26  26  26  GLY GLY C . n 
C 1 27  GLY 27  27  27  GLY GLY C . n 
C 1 28  PRO 28  28  28  PRO PRO C . n 
C 1 29  VAL 29  29  29  VAL VAL C . n 
C 1 30  SER 30  30  30  SER SER C . n 
C 1 31  ALA 31  31  31  ALA ALA C . n 
C 1 32  PHE 32  32  32  PHE PHE C . n 
C 1 33  LEU 33  33  33  LEU LEU C . n 
C 1 34  GLY 34  34  34  GLY GLY C . n 
C 1 35  ILE 35  35  35  ILE ILE C . n 
C 1 36  PRO 36  36  36  PRO PRO C . n 
C 1 37  PHE 37  37  37  PHE PHE C . n 
C 1 38  ALA 38  38  38  ALA ALA C . n 
C 1 39  GLU 39  39  39  GLU GLU C . n 
C 1 40  PRO 40  40  40  PRO PRO C . n 
C 1 41  PRO 41  41  41  PRO PRO C . n 
C 1 42  VAL 42  42  42  VAL VAL C . n 
C 1 43  GLY 43  43  43  GLY GLY C . n 
C 1 44  SER 44  44  44  SER SER C . n 
C 1 45  ARG 45  45  45  ARG ARG C . n 
C 1 46  ARG 46  46  46  ARG ARG C . n 
C 1 47  PHE 47  47  47  PHE PHE C . n 
C 1 48  MET 48  48  48  MET MET C . n 
C 1 49  PRO 49  49  49  PRO PRO C . n 
C 1 50  PRO 50  50  50  PRO PRO C . n 
C 1 51  GLU 51  51  51  GLU GLU C . n 
C 1 52  PRO 52  52  52  PRO PRO C . n 
C 1 53  LYS 53  53  53  LYS LYS C . n 
C 1 54  ARG 54  54  54  ARG ARG C . n 
C 1 55  PRO 55  55  55  PRO PRO C . n 
C 1 56  TRP 56  56  56  TRP TRP C . n 
C 1 57  SER 57  57  57  SER SER C . n 
C 1 58  GLY 58  58  58  GLY GLY C . n 
C 1 59  VAL 59  59  59  VAL VAL C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  ASP 61  61  61  ASP ASP C . n 
C 1 62  ALA 62  62  62  ALA ALA C . n 
C 1 63  THR 63  63  63  THR THR C . n 
C 1 64  THR 64  64  64  THR THR C . n 
C 1 65  PHE 65  65  65  PHE PHE C . n 
C 1 66  GLN 66  66  66  GLN GLN C . n 
C 1 67  ASN 67  67  67  ASN ASN C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  CYS 69  69  69  CYS CYS C . n 
C 1 70  TYR 70  70  70  TYR TYR C . n 
C 1 71  GLN 71  71  71  GLN GLN C . n 
C 1 72  TYR 72  72  72  TYR TYR C . n 
C 1 73  VAL 73  73  73  VAL VAL C . n 
C 1 74  ASP 74  74  74  ASP ASP C . n 
C 1 75  THR 75  75  75  THR THR C . n 
C 1 76  LEU 76  76  76  LEU LEU C . n 
C 1 77  TYR 77  77  77  TYR TYR C . n 
C 1 78  PRO 78  78  78  PRO PRO C . n 
C 1 79  GLY 79  79  79  GLY GLY C . n 
C 1 80  PHE 80  80  80  PHE PHE C . n 
C 1 81  GLU 81  81  81  GLU GLU C . n 
C 1 82  GLY 82  82  82  GLY GLY C . n 
C 1 83  THR 83  83  83  THR THR C . n 
C 1 84  GLU 84  84  84  GLU GLU C . n 
C 1 85  MET 85  85  85  MET MET C . n 
C 1 86  TRP 86  86  86  TRP TRP C . n 
C 1 87  ASN 87  87  87  ASN ASN C . n 
C 1 88  PRO 88  88  88  PRO PRO C . n 
C 1 89  ASN 89  89  89  ASN ASN C . n 
C 1 90  ARG 90  90  90  ARG ARG C . n 
C 1 91  GLU 91  91  91  GLU GLU C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  SER 93  93  93  SER SER C . n 
C 1 94  GLU 94  94  94  GLU GLU C . n 
C 1 95  ASP 95  95  95  ASP ASP C . n 
C 1 96  CYS 96  96  96  CYS CYS C . n 
C 1 97  LEU 97  97  97  LEU LEU C . n 
C 1 98  TYR 98  98  98  TYR TYR C . n 
C 1 99  LEU 99  99  99  LEU LEU C . n 
C 1 100 ASN 100 100 100 ASN ASN C . n 
C 1 101 VAL 101 101 101 VAL VAL C . n 
C 1 102 TRP 102 102 102 TRP TRP C . n 
C 1 103 THR 103 103 103 THR THR C . n 
C 1 104 PRO 104 104 104 PRO PRO C . n 
C 1 105 TYR 105 105 105 TYR TYR C . n 
C 1 106 PRO 106 106 106 PRO PRO C . n 
C 1 107 ARG 107 107 107 ARG ARG C . n 
C 1 108 PRO 108 108 108 PRO PRO C . n 
C 1 109 ALA 109 109 109 ALA ALA C . n 
C 1 110 SER 110 110 110 SER SER C . n 
C 1 111 PRO 111 111 111 PRO PRO C . n 
C 1 112 THR 112 112 112 THR THR C . n 
C 1 113 PRO 113 113 113 PRO PRO C . n 
C 1 114 VAL 114 114 114 VAL VAL C . n 
C 1 115 LEU 115 115 115 LEU LEU C . n 
C 1 116 ILE 116 116 116 ILE ILE C . n 
C 1 117 TRP 117 117 117 TRP TRP C . n 
C 1 118 ILE 118 118 118 ILE ILE C . n 
C 1 119 TYR 119 119 119 TYR TYR C . n 
C 1 120 GLY 120 120 120 GLY GLY C . n 
C 1 121 GLY 121 121 121 GLY GLY C . n 
C 1 122 GLY 122 122 122 GLY GLY C . n 
C 1 123 PHE 123 123 123 PHE PHE C . n 
C 1 124 TYR 124 124 124 TYR TYR C . n 
C 1 125 SER 125 125 125 SER SER C . n 
C 1 126 GLY 126 126 126 GLY GLY C . n 
C 1 127 ALA 127 127 127 ALA ALA C . n 
C 1 128 ALA 128 128 128 ALA ALA C . n 
C 1 129 SER 129 129 129 SER SER C . n 
C 1 130 LEU 130 130 130 LEU LEU C . n 
C 1 131 ASP 131 131 131 ASP ASP C . n 
C 1 132 VAL 132 132 132 VAL VAL C . n 
C 1 133 TYR 133 133 133 TYR TYR C . n 
C 1 134 ASP 134 134 134 ASP ASP C . n 
C 1 135 GLY 135 135 135 GLY GLY C . n 
C 1 136 ARG 136 136 136 ARG ARG C . n 
C 1 137 PHE 137 137 137 PHE PHE C . n 
C 1 138 LEU 138 138 138 LEU LEU C . n 
C 1 139 ALA 139 139 139 ALA ALA C . n 
C 1 140 GLN 140 140 140 GLN GLN C . n 
C 1 141 VAL 141 141 141 VAL VAL C . n 
C 1 142 GLU 142 142 142 GLU GLU C . n 
C 1 143 GLY 143 143 143 GLY GLY C . n 
C 1 144 ALA 144 144 144 ALA ALA C . n 
C 1 145 VAL 145 145 145 VAL VAL C . n 
C 1 146 LEU 146 146 146 LEU LEU C . n 
C 1 147 VAL 147 147 147 VAL VAL C . n 
C 1 148 SER 148 148 148 SER SER C . n 
C 1 149 MET 149 149 149 MET MET C . n 
C 1 150 ASN 150 150 150 ASN ASN C . n 
C 1 151 TYR 151 151 151 TYR TYR C . n 
C 1 152 ARG 152 152 152 ARG ARG C . n 
C 1 153 VAL 153 153 153 VAL VAL C . n 
C 1 154 GLY 154 154 154 GLY GLY C . n 
C 1 155 THR 155 155 155 THR THR C . n 
C 1 156 PHE 156 156 156 PHE PHE C . n 
C 1 157 GLY 157 157 157 GLY GLY C . n 
C 1 158 PHE 158 158 158 PHE PHE C . n 
C 1 159 LEU 159 159 159 LEU LEU C . n 
C 1 160 ALA 160 160 160 ALA ALA C . n 
C 1 161 LEU 161 161 161 LEU LEU C . n 
C 1 162 PRO 162 162 162 PRO PRO C . n 
C 1 163 GLY 163 163 163 GLY GLY C . n 
C 1 164 SER 164 164 164 SER SER C . n 
C 1 165 ARG 165 165 165 ARG ARG C . n 
C 1 166 GLU 166 166 166 GLU GLU C . n 
C 1 167 ALA 167 167 167 ALA ALA C . n 
C 1 168 PRO 168 168 168 PRO PRO C . n 
C 1 169 GLY 169 169 169 GLY GLY C . n 
C 1 170 ASN 170 170 170 ASN ASN C . n 
C 1 171 VAL 171 171 171 VAL VAL C . n 
C 1 172 GLY 172 172 172 GLY GLY C . n 
C 1 173 LEU 173 173 173 LEU LEU C . n 
C 1 174 LEU 174 174 174 LEU LEU C . n 
C 1 175 ASP 175 175 175 ASP ASP C . n 
C 1 176 GLN 176 176 176 GLN GLN C . n 
C 1 177 ARG 177 177 177 ARG ARG C . n 
C 1 178 LEU 178 178 178 LEU LEU C . n 
C 1 179 ALA 179 179 179 ALA ALA C . n 
C 1 180 LEU 180 180 180 LEU LEU C . n 
C 1 181 GLN 181 181 181 GLN GLN C . n 
C 1 182 TRP 182 182 182 TRP TRP C . n 
C 1 183 VAL 183 183 183 VAL VAL C . n 
C 1 184 GLN 184 184 184 GLN GLN C . n 
C 1 185 GLU 185 185 185 GLU GLU C . n 
C 1 186 ASN 186 186 186 ASN ASN C . n 
C 1 187 ILE 187 187 187 ILE ILE C . n 
C 1 188 ALA 188 188 188 ALA ALA C . n 
C 1 189 ALA 189 189 189 ALA ALA C . n 
C 1 190 PHE 190 190 190 PHE PHE C . n 
C 1 191 GLY 191 191 191 GLY GLY C . n 
C 1 192 GLY 192 192 192 GLY GLY C . n 
C 1 193 ASP 193 193 193 ASP ASP C . n 
C 1 194 PRO 194 194 194 PRO PRO C . n 
C 1 195 MET 195 195 195 MET MET C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 VAL 197 197 197 VAL VAL C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 LEU 199 199 199 LEU LEU C . n 
C 1 200 PHE 200 200 200 PHE PHE C . n 
C 1 201 GLY 201 201 201 GLY GLY C . n 
C 1 202 GLU 202 202 202 GLU GLU C . n 
C 1 203 SER 203 203 203 SER SER C . n 
C 1 204 ALA 204 204 204 ALA ALA C . n 
C 1 205 GLY 205 205 205 GLY GLY C . n 
C 1 206 ALA 206 206 206 ALA ALA C . n 
C 1 207 ALA 207 207 207 ALA ALA C . n 
C 1 208 SER 208 208 208 SER SER C . n 
C 1 209 VAL 209 209 209 VAL VAL C . n 
C 1 210 GLY 210 210 210 GLY GLY C . n 
C 1 211 MET 211 211 211 MET MET C . n 
C 1 212 HIS 212 212 212 HIS HIS C . n 
C 1 213 ILE 213 213 213 ILE ILE C . n 
C 1 214 LEU 214 214 214 LEU LEU C . n 
C 1 215 SER 215 215 215 SER SER C . n 
C 1 216 LEU 216 216 216 LEU LEU C . n 
C 1 217 PRO 217 217 217 PRO PRO C . n 
C 1 218 SER 218 218 218 SER SER C . n 
C 1 219 ARG 219 219 219 ARG ARG C . n 
C 1 220 SER 220 220 220 SER SER C . n 
C 1 221 LEU 221 221 221 LEU LEU C . n 
C 1 222 PHE 222 222 222 PHE PHE C . n 
C 1 223 HIS 223 223 223 HIS HIS C . n 
C 1 224 ARG 224 224 224 ARG ARG C . n 
C 1 225 ALA 225 225 225 ALA ALA C . n 
C 1 226 VAL 226 226 226 VAL VAL C . n 
C 1 227 LEU 227 227 227 LEU LEU C . n 
C 1 228 GLN 228 228 228 GLN GLN C . n 
C 1 229 SER 229 229 229 SER SER C . n 
C 1 230 GLY 230 230 230 GLY GLY C . n 
C 1 231 THR 231 231 231 THR THR C . n 
C 1 232 PRO 232 232 232 PRO PRO C . n 
C 1 233 ASN 233 233 233 ASN ASN C . n 
C 1 234 GLY 234 234 234 GLY GLY C . n 
C 1 235 PRO 235 235 235 PRO PRO C . n 
C 1 236 TRP 236 236 236 TRP TRP C . n 
C 1 237 ALA 237 237 237 ALA ALA C . n 
C 1 238 THR 238 238 238 THR THR C . n 
C 1 239 VAL 239 239 239 VAL VAL C . n 
C 1 240 SER 240 240 240 SER SER C . n 
C 1 241 ALA 241 241 241 ALA ALA C . n 
C 1 242 GLY 242 242 242 GLY GLY C . n 
C 1 243 GLU 243 243 243 GLU GLU C . n 
C 1 244 ALA 244 244 244 ALA ALA C . n 
C 1 245 ARG 245 245 245 ARG ARG C . n 
C 1 246 ARG 246 246 246 ARG ARG C . n 
C 1 247 ARG 247 247 247 ARG ARG C . n 
C 1 248 ALA 248 248 248 ALA ALA C . n 
C 1 249 THR 249 249 249 THR THR C . n 
C 1 250 LEU 250 250 250 LEU LEU C . n 
C 1 251 LEU 251 251 251 LEU LEU C . n 
C 1 252 ALA 252 252 252 ALA ALA C . n 
C 1 253 ARG 253 253 253 ARG ARG C . n 
C 1 254 LEU 254 254 254 LEU LEU C . n 
C 1 255 VAL 255 255 255 VAL VAL C . n 
C 1 256 GLY 256 256 256 GLY GLY C . n 
C 1 257 CYS 257 257 257 CYS CYS C . n 
C 1 258 PRO 258 258 258 PRO PRO C . n 
C 1 259 PRO 259 259 259 PRO PRO C . n 
C 1 260 GLY 260 260 260 GLY GLY C . n 
C 1 261 GLY 261 261 261 GLY GLY C . n 
C 1 262 ALA 262 262 262 ALA ALA C . n 
C 1 263 GLY 263 263 263 GLY GLY C . n 
C 1 264 GLY 264 264 264 GLY GLY C . n 
C 1 265 ASN 265 265 265 ASN ASN C . n 
C 1 266 ASP 266 266 266 ASP ASP C . n 
C 1 267 THR 267 267 267 THR THR C . n 
C 1 268 GLU 268 268 268 GLU GLU C . n 
C 1 269 LEU 269 269 269 LEU LEU C . n 
C 1 270 ILE 270 270 270 ILE ILE C . n 
C 1 271 ALA 271 271 271 ALA ALA C . n 
C 1 272 CYS 272 272 272 CYS CYS C . n 
C 1 273 LEU 273 273 273 LEU LEU C . n 
C 1 274 ARG 274 274 274 ARG ARG C . n 
C 1 275 THR 275 275 275 THR THR C . n 
C 1 276 ARG 276 276 276 ARG ARG C . n 
C 1 277 PRO 277 277 277 PRO PRO C . n 
C 1 278 ALA 278 278 278 ALA ALA C . n 
C 1 279 GLN 279 279 279 GLN GLN C . n 
C 1 280 ASP 280 280 280 ASP ASP C . n 
C 1 281 LEU 281 281 281 LEU LEU C . n 
C 1 282 VAL 282 282 282 VAL VAL C . n 
C 1 283 ASP 283 283 283 ASP ASP C . n 
C 1 284 HIS 284 284 284 HIS HIS C . n 
C 1 285 GLU 285 285 285 GLU GLU C . n 
C 1 286 TRP 286 286 286 TRP TRP C . n 
C 1 287 HIS 287 287 287 HIS HIS C . n 
C 1 288 VAL 288 288 288 VAL VAL C . n 
C 1 289 LEU 289 289 289 LEU LEU C . n 
C 1 290 PRO 290 290 290 PRO PRO C . n 
C 1 291 GLN 291 291 291 GLN GLN C . n 
C 1 292 GLU 292 292 292 GLU GLU C . n 
C 1 293 SER 293 293 293 SER SER C . n 
C 1 294 ILE 294 294 294 ILE ILE C . n 
C 1 295 PHE 295 295 295 PHE PHE C . n 
C 1 296 ARG 296 296 296 ARG ARG C . n 
C 1 297 PHE 297 297 297 PHE PHE C . n 
C 1 298 SER 298 298 298 SER SER C . n 
C 1 299 PHE 299 299 299 PHE PHE C . n 
C 1 300 VAL 300 300 300 VAL VAL C . n 
C 1 301 PRO 301 301 301 PRO PRO C . n 
C 1 302 VAL 302 302 302 VAL VAL C . n 
C 1 303 VAL 303 303 303 VAL VAL C . n 
C 1 304 ASP 304 304 304 ASP ASP C . n 
C 1 305 GLY 305 305 305 GLY GLY C . n 
C 1 306 ASP 306 306 306 ASP ASP C . n 
C 1 307 PHE 307 307 307 PHE PHE C . n 
C 1 308 LEU 308 308 308 LEU LEU C . n 
C 1 309 SER 309 309 309 SER SER C . n 
C 1 310 ASP 310 310 310 ASP ASP C . n 
C 1 311 THR 311 311 311 THR THR C . n 
C 1 312 PRO 312 312 312 PRO PRO C . n 
C 1 313 GLU 313 313 313 GLU GLU C . n 
C 1 314 ALA 314 314 314 ALA ALA C . n 
C 1 315 LEU 315 315 315 LEU LEU C . n 
C 1 316 ILE 316 316 316 ILE ILE C . n 
C 1 317 ASN 317 317 317 ASN ASN C . n 
C 1 318 THR 318 318 318 THR THR C . n 
C 1 319 GLY 319 319 319 GLY GLY C . n 
C 1 320 ASP 320 320 320 ASP ASP C . n 
C 1 321 PHE 321 321 321 PHE PHE C . n 
C 1 322 GLN 322 322 322 GLN GLN C . n 
C 1 323 ASP 323 323 323 ASP ASP C . n 
C 1 324 LEU 324 324 324 LEU LEU C . n 
C 1 325 GLN 325 325 325 GLN GLN C . n 
C 1 326 VAL 326 326 326 VAL VAL C . n 
C 1 327 LEU 327 327 327 LEU LEU C . n 
C 1 328 VAL 328 328 328 VAL VAL C . n 
C 1 329 GLY 329 329 329 GLY GLY C . n 
C 1 330 VAL 330 330 330 VAL VAL C . n 
C 1 331 VAL 331 331 331 VAL VAL C . n 
C 1 332 LYS 332 332 332 LYS LYS C . n 
C 1 333 ASP 333 333 333 ASP ASP C . n 
C 1 334 GLU 334 334 334 GLU GLU C . n 
C 1 335 GLY 335 335 335 GLY GLY C . n 
C 1 336 SER 336 336 336 SER SER C . n 
C 1 337 TYR 337 337 337 TYR TYR C . n 
C 1 338 PHE 338 338 338 PHE PHE C . n 
C 1 339 LEU 339 339 339 LEU LEU C . n 
C 1 340 VAL 340 340 340 VAL VAL C . n 
C 1 341 TYR 341 341 341 TYR TYR C . n 
C 1 342 GLY 342 342 342 GLY GLY C . n 
C 1 343 VAL 343 343 343 VAL VAL C . n 
C 1 344 PRO 344 344 344 PRO PRO C . n 
C 1 345 GLY 345 345 345 GLY GLY C . n 
C 1 346 PHE 346 346 346 PHE PHE C . n 
C 1 347 SER 347 347 347 SER SER C . n 
C 1 348 LYS 348 348 348 LYS LYS C . n 
C 1 349 ASP 349 349 349 ASP ASP C . n 
C 1 350 ASN 350 350 350 ASN ASN C . n 
C 1 351 GLU 351 351 351 GLU GLU C . n 
C 1 352 SER 352 352 352 SER SER C . n 
C 1 353 LEU 353 353 353 LEU LEU C . n 
C 1 354 ILE 354 354 354 ILE ILE C . n 
C 1 355 SER 355 355 355 SER SER C . n 
C 1 356 ARG 356 356 356 ARG ARG C . n 
C 1 357 ALA 357 357 357 ALA ALA C . n 
C 1 358 GLN 358 358 358 GLN GLN C . n 
C 1 359 PHE 359 359 359 PHE PHE C . n 
C 1 360 LEU 360 360 360 LEU LEU C . n 
C 1 361 ALA 361 361 361 ALA ALA C . n 
C 1 362 GLY 362 362 362 GLY GLY C . n 
C 1 363 VAL 363 363 363 VAL VAL C . n 
C 1 364 ARG 364 364 364 ARG ARG C . n 
C 1 365 ILE 365 365 365 ILE ILE C . n 
C 1 366 GLY 366 366 366 GLY GLY C . n 
C 1 367 VAL 367 367 367 VAL VAL C . n 
C 1 368 PRO 368 368 368 PRO PRO C . n 
C 1 369 GLN 369 369 369 GLN GLN C . n 
C 1 370 ALA 370 370 370 ALA ALA C . n 
C 1 371 SER 371 371 371 SER SER C . n 
C 1 372 ASP 372 372 372 ASP ASP C . n 
C 1 373 LEU 373 373 373 LEU LEU C . n 
C 1 374 ALA 374 374 374 ALA ALA C . n 
C 1 375 ALA 375 375 375 ALA ALA C . n 
C 1 376 GLU 376 376 376 GLU GLU C . n 
C 1 377 ALA 377 377 377 ALA ALA C . n 
C 1 378 VAL 378 378 378 VAL VAL C . n 
C 1 379 VAL 379 379 379 VAL VAL C . n 
C 1 380 LEU 380 380 380 LEU LEU C . n 
C 1 381 HIS 381 381 381 HIS HIS C . n 
C 1 382 TYR 382 382 382 TYR TYR C . n 
C 1 383 THR 383 383 383 THR THR C . n 
C 1 384 ASP 384 384 384 ASP ASP C . n 
C 1 385 TRP 385 385 385 TRP TRP C . n 
C 1 386 LEU 386 386 386 LEU LEU C . n 
C 1 387 HIS 387 387 387 HIS HIS C . n 
C 1 388 PRO 388 388 388 PRO PRO C . n 
C 1 389 GLU 389 389 389 GLU GLU C . n 
C 1 390 ASP 390 390 390 ASP ASP C . n 
C 1 391 PRO 391 391 391 PRO PRO C . n 
C 1 392 THR 392 392 392 THR THR C . n 
C 1 393 HIS 393 393 393 HIS HIS C . n 
C 1 394 LEU 394 394 394 LEU LEU C . n 
C 1 395 ARG 395 395 395 ARG ARG C . n 
C 1 396 ASP 396 396 396 ASP ASP C . n 
C 1 397 ALA 397 397 397 ALA ALA C . n 
C 1 398 MET 398 398 398 MET MET C . n 
C 1 399 SER 399 399 399 SER SER C . n 
C 1 400 ALA 400 400 400 ALA ALA C . n 
C 1 401 VAL 401 401 401 VAL VAL C . n 
C 1 402 VAL 402 402 402 VAL VAL C . n 
C 1 403 GLY 403 403 403 GLY GLY C . n 
C 1 404 ASP 404 404 404 ASP ASP C . n 
C 1 405 HIS 405 405 405 HIS HIS C . n 
C 1 406 ASN 406 406 406 ASN ASN C . n 
C 1 407 VAL 407 407 407 VAL VAL C . n 
C 1 408 VAL 408 408 408 VAL VAL C . n 
C 1 409 CYS 409 409 409 CYS CYS C . n 
C 1 410 PRO 410 410 410 PRO PRO C . n 
C 1 411 VAL 411 411 411 VAL VAL C . n 
C 1 412 ALA 412 412 412 ALA ALA C . n 
C 1 413 GLN 413 413 413 GLN GLN C . n 
C 1 414 LEU 414 414 414 LEU LEU C . n 
C 1 415 ALA 415 415 415 ALA ALA C . n 
C 1 416 GLY 416 416 416 GLY GLY C . n 
C 1 417 ARG 417 417 417 ARG ARG C . n 
C 1 418 LEU 418 418 418 LEU LEU C . n 
C 1 419 ALA 419 419 419 ALA ALA C . n 
C 1 420 ALA 420 420 420 ALA ALA C . n 
C 1 421 GLN 421 421 421 GLN GLN C . n 
C 1 422 GLY 422 422 422 GLY GLY C . n 
C 1 423 ALA 423 423 423 ALA ALA C . n 
C 1 424 ARG 424 424 424 ARG ARG C . n 
C 1 425 VAL 425 425 425 VAL VAL C . n 
C 1 426 TYR 426 426 426 TYR TYR C . n 
C 1 427 ALA 427 427 427 ALA ALA C . n 
C 1 428 TYR 428 428 428 TYR TYR C . n 
C 1 429 ILE 429 429 429 ILE ILE C . n 
C 1 430 PHE 430 430 430 PHE PHE C . n 
C 1 431 GLU 431 431 431 GLU GLU C . n 
C 1 432 HIS 432 432 432 HIS HIS C . n 
C 1 433 ARG 433 433 433 ARG ARG C . n 
C 1 434 ALA 434 434 434 ALA ALA C . n 
C 1 435 SER 435 435 435 SER SER C . n 
C 1 436 THR 436 436 436 THR THR C . n 
C 1 437 LEU 437 437 437 LEU LEU C . n 
C 1 438 THR 438 438 438 THR THR C . n 
C 1 439 TRP 439 439 439 TRP TRP C . n 
C 1 440 PRO 440 440 440 PRO PRO C . n 
C 1 441 LEU 441 441 441 LEU LEU C . n 
C 1 442 TRP 442 442 442 TRP TRP C . n 
C 1 443 MET 443 443 443 MET MET C . n 
C 1 444 GLY 444 444 444 GLY GLY C . n 
C 1 445 VAL 445 445 445 VAL VAL C . n 
C 1 446 PRO 446 446 446 PRO PRO C . n 
C 1 447 HIS 447 447 447 HIS HIS C . n 
C 1 448 GLY 448 448 448 GLY GLY C . n 
C 1 449 TYR 449 449 449 TYR TYR C . n 
C 1 450 GLU 450 450 450 GLU GLU C . n 
C 1 451 ILE 451 451 451 ILE ILE C . n 
C 1 452 GLU 452 452 452 GLU GLU C . n 
C 1 453 PHE 453 453 453 PHE PHE C . n 
C 1 454 ILE 454 454 454 ILE ILE C . n 
C 1 455 PHE 455 455 455 PHE PHE C . n 
C 1 456 GLY 456 456 456 GLY GLY C . n 
C 1 457 LEU 457 457 457 LEU LEU C . n 
C 1 458 PRO 458 458 458 PRO PRO C . n 
C 1 459 LEU 459 459 459 LEU LEU C . n 
C 1 460 ASP 460 460 460 ASP ASP C . n 
C 1 461 PRO 461 461 461 PRO PRO C . n 
C 1 462 SER 462 462 462 SER SER C . n 
C 1 463 LEU 463 463 463 LEU LEU C . n 
C 1 464 ASN 464 464 464 ASN ASN C . n 
C 1 465 TYR 465 465 465 TYR TYR C . n 
C 1 466 THR 466 466 466 THR THR C . n 
C 1 467 THR 467 467 467 THR THR C . n 
C 1 468 GLU 468 468 468 GLU GLU C . n 
C 1 469 GLU 469 469 469 GLU GLU C . n 
C 1 470 ARG 470 470 470 ARG ARG C . n 
C 1 471 ILE 471 471 471 ILE ILE C . n 
C 1 472 PHE 472 472 472 PHE PHE C . n 
C 1 473 ALA 473 473 473 ALA ALA C . n 
C 1 474 GLN 474 474 474 GLN GLN C . n 
C 1 475 ARG 475 475 475 ARG ARG C . n 
C 1 476 LEU 476 476 476 LEU LEU C . n 
C 1 477 MET 477 477 477 MET MET C . n 
C 1 478 LYS 478 478 478 LYS LYS C . n 
C 1 479 TYR 479 479 479 TYR TYR C . n 
C 1 480 TRP 480 480 480 TRP TRP C . n 
C 1 481 THR 481 481 481 THR THR C . n 
C 1 482 ASN 482 482 482 ASN ASN C . n 
C 1 483 PHE 483 483 483 PHE PHE C . n 
C 1 484 ALA 484 484 484 ALA ALA C . n 
C 1 485 ARG 485 485 485 ARG ARG C . n 
C 1 486 THR 486 486 486 THR THR C . n 
C 1 487 GLY 487 487 487 GLY GLY C . n 
C 1 488 ASP 488 488 488 ASP ASP C . n 
C 1 489 PRO 489 489 489 PRO PRO C . n 
C 1 490 ASN 490 490 490 ASN ASN C . n 
C 1 491 ASP 491 491 491 ASP ASP C . n 
C 1 492 PRO 492 492 492 PRO PRO C . n 
C 1 493 ARG 493 493 493 ARG ARG C . n 
C 1 494 ASP 494 494 494 ASP ASP C . n 
C 1 495 SER 495 495 495 SER SER C . n 
C 1 496 LYS 496 496 496 LYS LYS C . n 
C 1 497 SER 497 497 497 SER SER C . n 
C 1 498 PRO 498 498 498 PRO PRO C . n 
C 1 499 GLN 499 499 499 GLN GLN C . n 
C 1 500 TRP 500 500 500 TRP TRP C . n 
C 1 501 PRO 501 501 501 PRO PRO C . n 
C 1 502 PRO 502 502 502 PRO PRO C . n 
C 1 503 TYR 503 503 503 TYR TYR C . n 
C 1 504 THR 504 504 504 THR THR C . n 
C 1 505 THR 505 505 505 THR THR C . n 
C 1 506 ALA 506 506 506 ALA ALA C . n 
C 1 507 ALA 507 507 507 ALA ALA C . n 
C 1 508 GLN 508 508 508 GLN GLN C . n 
C 1 509 GLN 509 509 509 GLN GLN C . n 
C 1 510 TYR 510 510 510 TYR TYR C . n 
C 1 511 VAL 511 511 511 VAL VAL C . n 
C 1 512 SER 512 512 512 SER SER C . n 
C 1 513 LEU 513 513 513 LEU LEU C . n 
C 1 514 ASN 514 514 514 ASN ASN C . n 
C 1 515 LEU 515 515 515 LEU LEU C . n 
C 1 516 LYS 516 516 516 LYS LYS C . n 
C 1 517 PRO 517 517 517 PRO PRO C . n 
C 1 518 LEU 518 518 518 LEU LEU C . n 
C 1 519 GLU 519 519 519 GLU GLU C . n 
C 1 520 VAL 520 520 520 VAL VAL C . n 
C 1 521 ARG 521 521 521 ARG ARG C . n 
C 1 522 ARG 522 522 522 ARG ARG C . n 
C 1 523 GLY 523 523 523 GLY GLY C . n 
C 1 524 LEU 524 524 524 LEU LEU C . n 
C 1 525 ARG 525 525 525 ARG ARG C . n 
C 1 526 ALA 526 526 526 ALA ALA C . n 
C 1 527 GLN 527 527 527 GLN GLN C . n 
C 1 528 THR 528 528 528 THR THR C . n 
C 1 529 CYS 529 529 529 CYS CYS C . n 
C 1 530 ALA 530 530 530 ALA ALA C . n 
C 1 531 PHE 531 531 531 PHE PHE C . n 
C 1 532 TRP 532 532 532 TRP TRP C . n 
C 1 533 ASN 533 533 533 ASN ASN C . n 
C 1 534 ARG 534 534 534 ARG ARG C . n 
C 1 535 PHE 535 535 535 PHE PHE C . n 
C 1 536 LEU 536 536 536 LEU LEU C . n 
C 1 537 PRO 537 537 537 PRO PRO C . n 
C 1 538 LYS 538 538 538 LYS LYS C . n 
C 1 539 LEU 539 539 539 LEU LEU C . n 
C 1 540 LEU 540 540 540 LEU LEU C . n 
C 1 541 SER 541 541 541 SER SER C . n 
C 1 542 ALA 542 542 542 ALA ALA C . n 
C 1 543 THR 543 543 543 THR THR C . n 
D 1 1   GLU 1   1   ?   ?   ?   D . n 
D 1 2   GLY 2   2   ?   ?   ?   D . n 
D 1 3   ARG 3   3   ?   ?   ?   D . n 
D 1 4   GLU 4   4   4   GLU GLU D . n 
D 1 5   ASP 5   5   5   ASP ASP D . n 
D 1 6   PRO 6   6   6   PRO PRO D . n 
D 1 7   GLN 7   7   7   GLN GLN D . n 
D 1 8   LEU 8   8   8   LEU LEU D . n 
D 1 9   LEU 9   9   9   LEU LEU D . n 
D 1 10  VAL 10  10  10  VAL VAL D . n 
D 1 11  ARG 11  11  11  ARG ARG D . n 
D 1 12  VAL 12  12  12  VAL VAL D . n 
D 1 13  ARG 13  13  13  ARG ARG D . n 
D 1 14  GLY 14  14  14  GLY GLY D . n 
D 1 15  GLY 15  15  15  GLY GLY D . n 
D 1 16  GLN 16  16  16  GLN GLN D . n 
D 1 17  LEU 17  17  17  LEU LEU D . n 
D 1 18  ARG 18  18  18  ARG ARG D . n 
D 1 19  GLY 19  19  19  GLY GLY D . n 
D 1 20  ILE 20  20  20  ILE ILE D . n 
D 1 21  ARG 21  21  21  ARG ARG D . n 
D 1 22  LEU 22  22  22  LEU LEU D . n 
D 1 23  LYS 23  23  23  LYS LYS D . n 
D 1 24  ALA 24  24  24  ALA ALA D . n 
D 1 25  PRO 25  25  25  PRO PRO D . n 
D 1 26  GLY 26  26  26  GLY GLY D . n 
D 1 27  GLY 27  27  27  GLY GLY D . n 
D 1 28  PRO 28  28  28  PRO PRO D . n 
D 1 29  VAL 29  29  29  VAL VAL D . n 
D 1 30  SER 30  30  30  SER SER D . n 
D 1 31  ALA 31  31  31  ALA ALA D . n 
D 1 32  PHE 32  32  32  PHE PHE D . n 
D 1 33  LEU 33  33  33  LEU LEU D . n 
D 1 34  GLY 34  34  34  GLY GLY D . n 
D 1 35  ILE 35  35  35  ILE ILE D . n 
D 1 36  PRO 36  36  36  PRO PRO D . n 
D 1 37  PHE 37  37  37  PHE PHE D . n 
D 1 38  ALA 38  38  38  ALA ALA D . n 
D 1 39  GLU 39  39  39  GLU GLU D . n 
D 1 40  PRO 40  40  40  PRO PRO D . n 
D 1 41  PRO 41  41  41  PRO PRO D . n 
D 1 42  VAL 42  42  42  VAL VAL D . n 
D 1 43  GLY 43  43  43  GLY GLY D . n 
D 1 44  SER 44  44  44  SER SER D . n 
D 1 45  ARG 45  45  45  ARG ARG D . n 
D 1 46  ARG 46  46  46  ARG ARG D . n 
D 1 47  PHE 47  47  47  PHE PHE D . n 
D 1 48  MET 48  48  48  MET MET D . n 
D 1 49  PRO 49  49  49  PRO PRO D . n 
D 1 50  PRO 50  50  50  PRO PRO D . n 
D 1 51  GLU 51  51  51  GLU GLU D . n 
D 1 52  PRO 52  52  52  PRO PRO D . n 
D 1 53  LYS 53  53  53  LYS LYS D . n 
D 1 54  ARG 54  54  54  ARG ARG D . n 
D 1 55  PRO 55  55  55  PRO PRO D . n 
D 1 56  TRP 56  56  56  TRP TRP D . n 
D 1 57  SER 57  57  57  SER SER D . n 
D 1 58  GLY 58  58  58  GLY GLY D . n 
D 1 59  VAL 59  59  59  VAL VAL D . n 
D 1 60  LEU 60  60  60  LEU LEU D . n 
D 1 61  ASP 61  61  61  ASP ASP D . n 
D 1 62  ALA 62  62  62  ALA ALA D . n 
D 1 63  THR 63  63  63  THR THR D . n 
D 1 64  THR 64  64  64  THR THR D . n 
D 1 65  PHE 65  65  65  PHE PHE D . n 
D 1 66  GLN 66  66  66  GLN GLN D . n 
D 1 67  ASN 67  67  67  ASN ASN D . n 
D 1 68  VAL 68  68  68  VAL VAL D . n 
D 1 69  CYS 69  69  69  CYS CYS D . n 
D 1 70  TYR 70  70  70  TYR TYR D . n 
D 1 71  GLN 71  71  71  GLN GLN D . n 
D 1 72  TYR 72  72  72  TYR TYR D . n 
D 1 73  VAL 73  73  73  VAL VAL D . n 
D 1 74  ASP 74  74  74  ASP ASP D . n 
D 1 75  THR 75  75  75  THR THR D . n 
D 1 76  LEU 76  76  76  LEU LEU D . n 
D 1 77  TYR 77  77  77  TYR TYR D . n 
D 1 78  PRO 78  78  78  PRO PRO D . n 
D 1 79  GLY 79  79  79  GLY GLY D . n 
D 1 80  PHE 80  80  80  PHE PHE D . n 
D 1 81  GLU 81  81  81  GLU GLU D . n 
D 1 82  GLY 82  82  82  GLY GLY D . n 
D 1 83  THR 83  83  83  THR THR D . n 
D 1 84  GLU 84  84  84  GLU GLU D . n 
D 1 85  MET 85  85  85  MET MET D . n 
D 1 86  TRP 86  86  86  TRP TRP D . n 
D 1 87  ASN 87  87  87  ASN ASN D . n 
D 1 88  PRO 88  88  88  PRO PRO D . n 
D 1 89  ASN 89  89  89  ASN ASN D . n 
D 1 90  ARG 90  90  90  ARG ARG D . n 
D 1 91  GLU 91  91  91  GLU GLU D . n 
D 1 92  LEU 92  92  92  LEU LEU D . n 
D 1 93  SER 93  93  93  SER SER D . n 
D 1 94  GLU 94  94  94  GLU GLU D . n 
D 1 95  ASP 95  95  95  ASP ASP D . n 
D 1 96  CYS 96  96  96  CYS CYS D . n 
D 1 97  LEU 97  97  97  LEU LEU D . n 
D 1 98  TYR 98  98  98  TYR TYR D . n 
D 1 99  LEU 99  99  99  LEU LEU D . n 
D 1 100 ASN 100 100 100 ASN ASN D . n 
D 1 101 VAL 101 101 101 VAL VAL D . n 
D 1 102 TRP 102 102 102 TRP TRP D . n 
D 1 103 THR 103 103 103 THR THR D . n 
D 1 104 PRO 104 104 104 PRO PRO D . n 
D 1 105 TYR 105 105 105 TYR TYR D . n 
D 1 106 PRO 106 106 106 PRO PRO D . n 
D 1 107 ARG 107 107 107 ARG ARG D . n 
D 1 108 PRO 108 108 108 PRO PRO D . n 
D 1 109 ALA 109 109 109 ALA ALA D . n 
D 1 110 SER 110 110 110 SER SER D . n 
D 1 111 PRO 111 111 111 PRO PRO D . n 
D 1 112 THR 112 112 112 THR THR D . n 
D 1 113 PRO 113 113 113 PRO PRO D . n 
D 1 114 VAL 114 114 114 VAL VAL D . n 
D 1 115 LEU 115 115 115 LEU LEU D . n 
D 1 116 ILE 116 116 116 ILE ILE D . n 
D 1 117 TRP 117 117 117 TRP TRP D . n 
D 1 118 ILE 118 118 118 ILE ILE D . n 
D 1 119 TYR 119 119 119 TYR TYR D . n 
D 1 120 GLY 120 120 120 GLY GLY D . n 
D 1 121 GLY 121 121 121 GLY GLY D . n 
D 1 122 GLY 122 122 122 GLY GLY D . n 
D 1 123 PHE 123 123 123 PHE PHE D . n 
D 1 124 TYR 124 124 124 TYR TYR D . n 
D 1 125 SER 125 125 125 SER SER D . n 
D 1 126 GLY 126 126 126 GLY GLY D . n 
D 1 127 ALA 127 127 127 ALA ALA D . n 
D 1 128 ALA 128 128 128 ALA ALA D . n 
D 1 129 SER 129 129 129 SER SER D . n 
D 1 130 LEU 130 130 130 LEU LEU D . n 
D 1 131 ASP 131 131 131 ASP ASP D . n 
D 1 132 VAL 132 132 132 VAL VAL D . n 
D 1 133 TYR 133 133 133 TYR TYR D . n 
D 1 134 ASP 134 134 134 ASP ASP D . n 
D 1 135 GLY 135 135 135 GLY GLY D . n 
D 1 136 ARG 136 136 136 ARG ARG D . n 
D 1 137 PHE 137 137 137 PHE PHE D . n 
D 1 138 LEU 138 138 138 LEU LEU D . n 
D 1 139 ALA 139 139 139 ALA ALA D . n 
D 1 140 GLN 140 140 140 GLN GLN D . n 
D 1 141 VAL 141 141 141 VAL VAL D . n 
D 1 142 GLU 142 142 142 GLU GLU D . n 
D 1 143 GLY 143 143 143 GLY GLY D . n 
D 1 144 ALA 144 144 144 ALA ALA D . n 
D 1 145 VAL 145 145 145 VAL VAL D . n 
D 1 146 LEU 146 146 146 LEU LEU D . n 
D 1 147 VAL 147 147 147 VAL VAL D . n 
D 1 148 SER 148 148 148 SER SER D . n 
D 1 149 MET 149 149 149 MET MET D . n 
D 1 150 ASN 150 150 150 ASN ASN D . n 
D 1 151 TYR 151 151 151 TYR TYR D . n 
D 1 152 ARG 152 152 152 ARG ARG D . n 
D 1 153 VAL 153 153 153 VAL VAL D . n 
D 1 154 GLY 154 154 154 GLY GLY D . n 
D 1 155 THR 155 155 155 THR THR D . n 
D 1 156 PHE 156 156 156 PHE PHE D . n 
D 1 157 GLY 157 157 157 GLY GLY D . n 
D 1 158 PHE 158 158 158 PHE PHE D . n 
D 1 159 LEU 159 159 159 LEU LEU D . n 
D 1 160 ALA 160 160 160 ALA ALA D . n 
D 1 161 LEU 161 161 161 LEU LEU D . n 
D 1 162 PRO 162 162 162 PRO PRO D . n 
D 1 163 GLY 163 163 163 GLY GLY D . n 
D 1 164 SER 164 164 164 SER SER D . n 
D 1 165 ARG 165 165 165 ARG ARG D . n 
D 1 166 GLU 166 166 166 GLU GLU D . n 
D 1 167 ALA 167 167 167 ALA ALA D . n 
D 1 168 PRO 168 168 168 PRO PRO D . n 
D 1 169 GLY 169 169 169 GLY GLY D . n 
D 1 170 ASN 170 170 170 ASN ASN D . n 
D 1 171 VAL 171 171 171 VAL VAL D . n 
D 1 172 GLY 172 172 172 GLY GLY D . n 
D 1 173 LEU 173 173 173 LEU LEU D . n 
D 1 174 LEU 174 174 174 LEU LEU D . n 
D 1 175 ASP 175 175 175 ASP ASP D . n 
D 1 176 GLN 176 176 176 GLN GLN D . n 
D 1 177 ARG 177 177 177 ARG ARG D . n 
D 1 178 LEU 178 178 178 LEU LEU D . n 
D 1 179 ALA 179 179 179 ALA ALA D . n 
D 1 180 LEU 180 180 180 LEU LEU D . n 
D 1 181 GLN 181 181 181 GLN GLN D . n 
D 1 182 TRP 182 182 182 TRP TRP D . n 
D 1 183 VAL 183 183 183 VAL VAL D . n 
D 1 184 GLN 184 184 184 GLN GLN D . n 
D 1 185 GLU 185 185 185 GLU GLU D . n 
D 1 186 ASN 186 186 186 ASN ASN D . n 
D 1 187 ILE 187 187 187 ILE ILE D . n 
D 1 188 ALA 188 188 188 ALA ALA D . n 
D 1 189 ALA 189 189 189 ALA ALA D . n 
D 1 190 PHE 190 190 190 PHE PHE D . n 
D 1 191 GLY 191 191 191 GLY GLY D . n 
D 1 192 GLY 192 192 192 GLY GLY D . n 
D 1 193 ASP 193 193 193 ASP ASP D . n 
D 1 194 PRO 194 194 194 PRO PRO D . n 
D 1 195 MET 195 195 195 MET MET D . n 
D 1 196 SER 196 196 196 SER SER D . n 
D 1 197 VAL 197 197 197 VAL VAL D . n 
D 1 198 THR 198 198 198 THR THR D . n 
D 1 199 LEU 199 199 199 LEU LEU D . n 
D 1 200 PHE 200 200 200 PHE PHE D . n 
D 1 201 GLY 201 201 201 GLY GLY D . n 
D 1 202 GLU 202 202 202 GLU GLU D . n 
D 1 203 SER 203 203 203 SER SER D . n 
D 1 204 ALA 204 204 204 ALA ALA D . n 
D 1 205 GLY 205 205 205 GLY GLY D . n 
D 1 206 ALA 206 206 206 ALA ALA D . n 
D 1 207 ALA 207 207 207 ALA ALA D . n 
D 1 208 SER 208 208 208 SER SER D . n 
D 1 209 VAL 209 209 209 VAL VAL D . n 
D 1 210 GLY 210 210 210 GLY GLY D . n 
D 1 211 MET 211 211 211 MET MET D . n 
D 1 212 HIS 212 212 212 HIS HIS D . n 
D 1 213 ILE 213 213 213 ILE ILE D . n 
D 1 214 LEU 214 214 214 LEU LEU D . n 
D 1 215 SER 215 215 215 SER SER D . n 
D 1 216 LEU 216 216 216 LEU LEU D . n 
D 1 217 PRO 217 217 217 PRO PRO D . n 
D 1 218 SER 218 218 218 SER SER D . n 
D 1 219 ARG 219 219 219 ARG ARG D . n 
D 1 220 SER 220 220 220 SER SER D . n 
D 1 221 LEU 221 221 221 LEU LEU D . n 
D 1 222 PHE 222 222 222 PHE PHE D . n 
D 1 223 HIS 223 223 223 HIS HIS D . n 
D 1 224 ARG 224 224 224 ARG ARG D . n 
D 1 225 ALA 225 225 225 ALA ALA D . n 
D 1 226 VAL 226 226 226 VAL VAL D . n 
D 1 227 LEU 227 227 227 LEU LEU D . n 
D 1 228 GLN 228 228 228 GLN GLN D . n 
D 1 229 SER 229 229 229 SER SER D . n 
D 1 230 GLY 230 230 230 GLY GLY D . n 
D 1 231 THR 231 231 231 THR THR D . n 
D 1 232 PRO 232 232 232 PRO PRO D . n 
D 1 233 ASN 233 233 233 ASN ASN D . n 
D 1 234 GLY 234 234 234 GLY GLY D . n 
D 1 235 PRO 235 235 235 PRO PRO D . n 
D 1 236 TRP 236 236 236 TRP TRP D . n 
D 1 237 ALA 237 237 237 ALA ALA D . n 
D 1 238 THR 238 238 238 THR THR D . n 
D 1 239 VAL 239 239 239 VAL VAL D . n 
D 1 240 SER 240 240 240 SER SER D . n 
D 1 241 ALA 241 241 241 ALA ALA D . n 
D 1 242 GLY 242 242 242 GLY GLY D . n 
D 1 243 GLU 243 243 243 GLU GLU D . n 
D 1 244 ALA 244 244 244 ALA ALA D . n 
D 1 245 ARG 245 245 245 ARG ARG D . n 
D 1 246 ARG 246 246 246 ARG ARG D . n 
D 1 247 ARG 247 247 247 ARG ARG D . n 
D 1 248 ALA 248 248 248 ALA ALA D . n 
D 1 249 THR 249 249 249 THR THR D . n 
D 1 250 LEU 250 250 250 LEU LEU D . n 
D 1 251 LEU 251 251 251 LEU LEU D . n 
D 1 252 ALA 252 252 252 ALA ALA D . n 
D 1 253 ARG 253 253 253 ARG ARG D . n 
D 1 254 LEU 254 254 254 LEU LEU D . n 
D 1 255 VAL 255 255 255 VAL VAL D . n 
D 1 256 GLY 256 256 256 GLY GLY D . n 
D 1 257 CYS 257 257 257 CYS CYS D . n 
D 1 258 PRO 258 258 258 PRO PRO D . n 
D 1 259 PRO 259 259 259 PRO PRO D . n 
D 1 260 GLY 260 260 260 GLY GLY D . n 
D 1 261 GLY 261 261 261 GLY GLY D . n 
D 1 262 ALA 262 262 262 ALA ALA D . n 
D 1 263 GLY 263 263 263 GLY GLY D . n 
D 1 264 GLY 264 264 264 GLY GLY D . n 
D 1 265 ASN 265 265 265 ASN ASN D . n 
D 1 266 ASP 266 266 266 ASP ASP D . n 
D 1 267 THR 267 267 267 THR THR D . n 
D 1 268 GLU 268 268 268 GLU GLU D . n 
D 1 269 LEU 269 269 269 LEU LEU D . n 
D 1 270 ILE 270 270 270 ILE ILE D . n 
D 1 271 ALA 271 271 271 ALA ALA D . n 
D 1 272 CYS 272 272 272 CYS CYS D . n 
D 1 273 LEU 273 273 273 LEU LEU D . n 
D 1 274 ARG 274 274 274 ARG ARG D . n 
D 1 275 THR 275 275 275 THR THR D . n 
D 1 276 ARG 276 276 276 ARG ARG D . n 
D 1 277 PRO 277 277 277 PRO PRO D . n 
D 1 278 ALA 278 278 278 ALA ALA D . n 
D 1 279 GLN 279 279 279 GLN GLN D . n 
D 1 280 ASP 280 280 280 ASP ASP D . n 
D 1 281 LEU 281 281 281 LEU LEU D . n 
D 1 282 VAL 282 282 282 VAL VAL D . n 
D 1 283 ASP 283 283 283 ASP ASP D . n 
D 1 284 HIS 284 284 284 HIS HIS D . n 
D 1 285 GLU 285 285 285 GLU GLU D . n 
D 1 286 TRP 286 286 286 TRP TRP D . n 
D 1 287 HIS 287 287 287 HIS HIS D . n 
D 1 288 VAL 288 288 288 VAL VAL D . n 
D 1 289 LEU 289 289 289 LEU LEU D . n 
D 1 290 PRO 290 290 290 PRO PRO D . n 
D 1 291 GLN 291 291 291 GLN GLN D . n 
D 1 292 GLU 292 292 292 GLU GLU D . n 
D 1 293 SER 293 293 293 SER SER D . n 
D 1 294 ILE 294 294 294 ILE ILE D . n 
D 1 295 PHE 295 295 295 PHE PHE D . n 
D 1 296 ARG 296 296 296 ARG ARG D . n 
D 1 297 PHE 297 297 297 PHE PHE D . n 
D 1 298 SER 298 298 298 SER SER D . n 
D 1 299 PHE 299 299 299 PHE PHE D . n 
D 1 300 VAL 300 300 300 VAL VAL D . n 
D 1 301 PRO 301 301 301 PRO PRO D . n 
D 1 302 VAL 302 302 302 VAL VAL D . n 
D 1 303 VAL 303 303 303 VAL VAL D . n 
D 1 304 ASP 304 304 304 ASP ASP D . n 
D 1 305 GLY 305 305 305 GLY GLY D . n 
D 1 306 ASP 306 306 306 ASP ASP D . n 
D 1 307 PHE 307 307 307 PHE PHE D . n 
D 1 308 LEU 308 308 308 LEU LEU D . n 
D 1 309 SER 309 309 309 SER SER D . n 
D 1 310 ASP 310 310 310 ASP ASP D . n 
D 1 311 THR 311 311 311 THR THR D . n 
D 1 312 PRO 312 312 312 PRO PRO D . n 
D 1 313 GLU 313 313 313 GLU GLU D . n 
D 1 314 ALA 314 314 314 ALA ALA D . n 
D 1 315 LEU 315 315 315 LEU LEU D . n 
D 1 316 ILE 316 316 316 ILE ILE D . n 
D 1 317 ASN 317 317 317 ASN ASN D . n 
D 1 318 THR 318 318 318 THR THR D . n 
D 1 319 GLY 319 319 319 GLY GLY D . n 
D 1 320 ASP 320 320 320 ASP ASP D . n 
D 1 321 PHE 321 321 321 PHE PHE D . n 
D 1 322 GLN 322 322 322 GLN GLN D . n 
D 1 323 ASP 323 323 323 ASP ASP D . n 
D 1 324 LEU 324 324 324 LEU LEU D . n 
D 1 325 GLN 325 325 325 GLN GLN D . n 
D 1 326 VAL 326 326 326 VAL VAL D . n 
D 1 327 LEU 327 327 327 LEU LEU D . n 
D 1 328 VAL 328 328 328 VAL VAL D . n 
D 1 329 GLY 329 329 329 GLY GLY D . n 
D 1 330 VAL 330 330 330 VAL VAL D . n 
D 1 331 VAL 331 331 331 VAL VAL D . n 
D 1 332 LYS 332 332 332 LYS LYS D . n 
D 1 333 ASP 333 333 333 ASP ASP D . n 
D 1 334 GLU 334 334 334 GLU GLU D . n 
D 1 335 GLY 335 335 335 GLY GLY D . n 
D 1 336 SER 336 336 336 SER SER D . n 
D 1 337 TYR 337 337 337 TYR TYR D . n 
D 1 338 PHE 338 338 338 PHE PHE D . n 
D 1 339 LEU 339 339 339 LEU LEU D . n 
D 1 340 VAL 340 340 340 VAL VAL D . n 
D 1 341 TYR 341 341 341 TYR TYR D . n 
D 1 342 GLY 342 342 342 GLY GLY D . n 
D 1 343 VAL 343 343 343 VAL VAL D . n 
D 1 344 PRO 344 344 344 PRO PRO D . n 
D 1 345 GLY 345 345 345 GLY GLY D . n 
D 1 346 PHE 346 346 346 PHE PHE D . n 
D 1 347 SER 347 347 347 SER SER D . n 
D 1 348 LYS 348 348 348 LYS LYS D . n 
D 1 349 ASP 349 349 349 ASP ASP D . n 
D 1 350 ASN 350 350 350 ASN ASN D . n 
D 1 351 GLU 351 351 351 GLU GLU D . n 
D 1 352 SER 352 352 352 SER SER D . n 
D 1 353 LEU 353 353 353 LEU LEU D . n 
D 1 354 ILE 354 354 354 ILE ILE D . n 
D 1 355 SER 355 355 355 SER SER D . n 
D 1 356 ARG 356 356 356 ARG ARG D . n 
D 1 357 ALA 357 357 357 ALA ALA D . n 
D 1 358 GLN 358 358 358 GLN GLN D . n 
D 1 359 PHE 359 359 359 PHE PHE D . n 
D 1 360 LEU 360 360 360 LEU LEU D . n 
D 1 361 ALA 361 361 361 ALA ALA D . n 
D 1 362 GLY 362 362 362 GLY GLY D . n 
D 1 363 VAL 363 363 363 VAL VAL D . n 
D 1 364 ARG 364 364 364 ARG ARG D . n 
D 1 365 ILE 365 365 365 ILE ILE D . n 
D 1 366 GLY 366 366 366 GLY GLY D . n 
D 1 367 VAL 367 367 367 VAL VAL D . n 
D 1 368 PRO 368 368 368 PRO PRO D . n 
D 1 369 GLN 369 369 369 GLN GLN D . n 
D 1 370 ALA 370 370 370 ALA ALA D . n 
D 1 371 SER 371 371 371 SER SER D . n 
D 1 372 ASP 372 372 372 ASP ASP D . n 
D 1 373 LEU 373 373 373 LEU LEU D . n 
D 1 374 ALA 374 374 374 ALA ALA D . n 
D 1 375 ALA 375 375 375 ALA ALA D . n 
D 1 376 GLU 376 376 376 GLU GLU D . n 
D 1 377 ALA 377 377 377 ALA ALA D . n 
D 1 378 VAL 378 378 378 VAL VAL D . n 
D 1 379 VAL 379 379 379 VAL VAL D . n 
D 1 380 LEU 380 380 380 LEU LEU D . n 
D 1 381 HIS 381 381 381 HIS HIS D . n 
D 1 382 TYR 382 382 382 TYR TYR D . n 
D 1 383 THR 383 383 383 THR THR D . n 
D 1 384 ASP 384 384 384 ASP ASP D . n 
D 1 385 TRP 385 385 385 TRP TRP D . n 
D 1 386 LEU 386 386 386 LEU LEU D . n 
D 1 387 HIS 387 387 387 HIS HIS D . n 
D 1 388 PRO 388 388 388 PRO PRO D . n 
D 1 389 GLU 389 389 389 GLU GLU D . n 
D 1 390 ASP 390 390 390 ASP ASP D . n 
D 1 391 PRO 391 391 391 PRO PRO D . n 
D 1 392 THR 392 392 392 THR THR D . n 
D 1 393 HIS 393 393 393 HIS HIS D . n 
D 1 394 LEU 394 394 394 LEU LEU D . n 
D 1 395 ARG 395 395 395 ARG ARG D . n 
D 1 396 ASP 396 396 396 ASP ASP D . n 
D 1 397 ALA 397 397 397 ALA ALA D . n 
D 1 398 MET 398 398 398 MET MET D . n 
D 1 399 SER 399 399 399 SER SER D . n 
D 1 400 ALA 400 400 400 ALA ALA D . n 
D 1 401 VAL 401 401 401 VAL VAL D . n 
D 1 402 VAL 402 402 402 VAL VAL D . n 
D 1 403 GLY 403 403 403 GLY GLY D . n 
D 1 404 ASP 404 404 404 ASP ASP D . n 
D 1 405 HIS 405 405 405 HIS HIS D . n 
D 1 406 ASN 406 406 406 ASN ASN D . n 
D 1 407 VAL 407 407 407 VAL VAL D . n 
D 1 408 VAL 408 408 408 VAL VAL D . n 
D 1 409 CYS 409 409 409 CYS CYS D . n 
D 1 410 PRO 410 410 410 PRO PRO D . n 
D 1 411 VAL 411 411 411 VAL VAL D . n 
D 1 412 ALA 412 412 412 ALA ALA D . n 
D 1 413 GLN 413 413 413 GLN GLN D . n 
D 1 414 LEU 414 414 414 LEU LEU D . n 
D 1 415 ALA 415 415 415 ALA ALA D . n 
D 1 416 GLY 416 416 416 GLY GLY D . n 
D 1 417 ARG 417 417 417 ARG ARG D . n 
D 1 418 LEU 418 418 418 LEU LEU D . n 
D 1 419 ALA 419 419 419 ALA ALA D . n 
D 1 420 ALA 420 420 420 ALA ALA D . n 
D 1 421 GLN 421 421 421 GLN GLN D . n 
D 1 422 GLY 422 422 422 GLY GLY D . n 
D 1 423 ALA 423 423 423 ALA ALA D . n 
D 1 424 ARG 424 424 424 ARG ARG D . n 
D 1 425 VAL 425 425 425 VAL VAL D . n 
D 1 426 TYR 426 426 426 TYR TYR D . n 
D 1 427 ALA 427 427 427 ALA ALA D . n 
D 1 428 TYR 428 428 428 TYR TYR D . n 
D 1 429 ILE 429 429 429 ILE ILE D . n 
D 1 430 PHE 430 430 430 PHE PHE D . n 
D 1 431 GLU 431 431 431 GLU GLU D . n 
D 1 432 HIS 432 432 432 HIS HIS D . n 
D 1 433 ARG 433 433 433 ARG ARG D . n 
D 1 434 ALA 434 434 434 ALA ALA D . n 
D 1 435 SER 435 435 435 SER SER D . n 
D 1 436 THR 436 436 436 THR THR D . n 
D 1 437 LEU 437 437 437 LEU LEU D . n 
D 1 438 THR 438 438 438 THR THR D . n 
D 1 439 TRP 439 439 439 TRP TRP D . n 
D 1 440 PRO 440 440 440 PRO PRO D . n 
D 1 441 LEU 441 441 441 LEU LEU D . n 
D 1 442 TRP 442 442 442 TRP TRP D . n 
D 1 443 MET 443 443 443 MET MET D . n 
D 1 444 GLY 444 444 444 GLY GLY D . n 
D 1 445 VAL 445 445 445 VAL VAL D . n 
D 1 446 PRO 446 446 446 PRO PRO D . n 
D 1 447 HIS 447 447 447 HIS HIS D . n 
D 1 448 GLY 448 448 448 GLY GLY D . n 
D 1 449 TYR 449 449 449 TYR TYR D . n 
D 1 450 GLU 450 450 450 GLU GLU D . n 
D 1 451 ILE 451 451 451 ILE ILE D . n 
D 1 452 GLU 452 452 452 GLU GLU D . n 
D 1 453 PHE 453 453 453 PHE PHE D . n 
D 1 454 ILE 454 454 454 ILE ILE D . n 
D 1 455 PHE 455 455 455 PHE PHE D . n 
D 1 456 GLY 456 456 456 GLY GLY D . n 
D 1 457 LEU 457 457 457 LEU LEU D . n 
D 1 458 PRO 458 458 458 PRO PRO D . n 
D 1 459 LEU 459 459 459 LEU LEU D . n 
D 1 460 ASP 460 460 460 ASP ASP D . n 
D 1 461 PRO 461 461 461 PRO PRO D . n 
D 1 462 SER 462 462 462 SER SER D . n 
D 1 463 LEU 463 463 463 LEU LEU D . n 
D 1 464 ASN 464 464 464 ASN ASN D . n 
D 1 465 TYR 465 465 465 TYR TYR D . n 
D 1 466 THR 466 466 466 THR THR D . n 
D 1 467 THR 467 467 467 THR THR D . n 
D 1 468 GLU 468 468 468 GLU GLU D . n 
D 1 469 GLU 469 469 469 GLU GLU D . n 
D 1 470 ARG 470 470 470 ARG ARG D . n 
D 1 471 ILE 471 471 471 ILE ILE D . n 
D 1 472 PHE 472 472 472 PHE PHE D . n 
D 1 473 ALA 473 473 473 ALA ALA D . n 
D 1 474 GLN 474 474 474 GLN GLN D . n 
D 1 475 ARG 475 475 475 ARG ARG D . n 
D 1 476 LEU 476 476 476 LEU LEU D . n 
D 1 477 MET 477 477 477 MET MET D . n 
D 1 478 LYS 478 478 478 LYS LYS D . n 
D 1 479 TYR 479 479 479 TYR TYR D . n 
D 1 480 TRP 480 480 480 TRP TRP D . n 
D 1 481 THR 481 481 481 THR THR D . n 
D 1 482 ASN 482 482 482 ASN ASN D . n 
D 1 483 PHE 483 483 483 PHE PHE D . n 
D 1 484 ALA 484 484 484 ALA ALA D . n 
D 1 485 ARG 485 485 485 ARG ARG D . n 
D 1 486 THR 486 486 486 THR THR D . n 
D 1 487 GLY 487 487 487 GLY GLY D . n 
D 1 488 ASP 488 488 488 ASP ASP D . n 
D 1 489 PRO 489 489 489 PRO PRO D . n 
D 1 490 ASN 490 490 490 ASN ASN D . n 
D 1 491 ASP 491 491 491 ASP ASP D . n 
D 1 492 PRO 492 492 492 PRO PRO D . n 
D 1 493 ARG 493 493 493 ARG ARG D . n 
D 1 494 ASP 494 494 494 ASP ASP D . n 
D 1 495 SER 495 495 495 SER SER D . n 
D 1 496 LYS 496 496 496 LYS LYS D . n 
D 1 497 SER 497 497 497 SER SER D . n 
D 1 498 PRO 498 498 498 PRO PRO D . n 
D 1 499 GLN 499 499 499 GLN GLN D . n 
D 1 500 TRP 500 500 500 TRP TRP D . n 
D 1 501 PRO 501 501 501 PRO PRO D . n 
D 1 502 PRO 502 502 502 PRO PRO D . n 
D 1 503 TYR 503 503 503 TYR TYR D . n 
D 1 504 THR 504 504 504 THR THR D . n 
D 1 505 THR 505 505 505 THR THR D . n 
D 1 506 ALA 506 506 506 ALA ALA D . n 
D 1 507 ALA 507 507 507 ALA ALA D . n 
D 1 508 GLN 508 508 508 GLN GLN D . n 
D 1 509 GLN 509 509 509 GLN GLN D . n 
D 1 510 TYR 510 510 510 TYR TYR D . n 
D 1 511 VAL 511 511 511 VAL VAL D . n 
D 1 512 SER 512 512 512 SER SER D . n 
D 1 513 LEU 513 513 513 LEU LEU D . n 
D 1 514 ASN 514 514 514 ASN ASN D . n 
D 1 515 LEU 515 515 515 LEU LEU D . n 
D 1 516 LYS 516 516 516 LYS LYS D . n 
D 1 517 PRO 517 517 517 PRO PRO D . n 
D 1 518 LEU 518 518 518 LEU LEU D . n 
D 1 519 GLU 519 519 519 GLU GLU D . n 
D 1 520 VAL 520 520 520 VAL VAL D . n 
D 1 521 ARG 521 521 521 ARG ARG D . n 
D 1 522 ARG 522 522 522 ARG ARG D . n 
D 1 523 GLY 523 523 523 GLY GLY D . n 
D 1 524 LEU 524 524 524 LEU LEU D . n 
D 1 525 ARG 525 525 525 ARG ARG D . n 
D 1 526 ALA 526 526 526 ALA ALA D . n 
D 1 527 GLN 527 527 527 GLN GLN D . n 
D 1 528 THR 528 528 528 THR THR D . n 
D 1 529 CYS 529 529 529 CYS CYS D . n 
D 1 530 ALA 530 530 530 ALA ALA D . n 
D 1 531 PHE 531 531 531 PHE PHE D . n 
D 1 532 TRP 532 532 532 TRP TRP D . n 
D 1 533 ASN 533 533 533 ASN ASN D . n 
D 1 534 ARG 534 534 534 ARG ARG D . n 
D 1 535 PHE 535 535 535 PHE PHE D . n 
D 1 536 LEU 536 536 536 LEU LEU D . n 
D 1 537 PRO 537 537 537 PRO PRO D . n 
D 1 538 LYS 538 538 538 LYS LYS D . n 
D 1 539 LEU 539 539 539 LEU LEU D . n 
D 1 540 LEU 540 540 540 LEU LEU D . n 
D 1 541 SER 541 541 541 SER SER D . n 
D 1 542 ALA 542 542 542 ALA ALA D . n 
D 1 543 THR 543 543 543 THR THR D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E  2 4OJ 1   600  600  4OJ 4OJ A . 
F  3 NAG 1   701  701  NAG NAG A . 
G  4 SO4 1   1544 1544 SO4 SO4 A . 
H  4 SO4 1   1545 1545 SO4 SO4 A . 
I  4 SO4 1   1546 1546 SO4 SO4 A . 
J  4 SO4 1   1547 1547 SO4 SO4 A . 
K  4 SO4 1   1548 1548 SO4 SO4 A . 
L  2 4OJ 1   600  600  4OJ 4OJ B . 
M  3 NAG 1   701  701  NAG NAG B . 
N  3 NAG 1   702  702  NAG NAG B . 
O  4 SO4 1   1544 1544 SO4 SO4 B . 
P  4 SO4 1   1545 1545 SO4 SO4 B . 
Q  4 SO4 1   1546 1546 SO4 SO4 B . 
R  2 4OJ 1   600  600  4OJ 4OJ C . 
S  3 NAG 1   701  701  NAG NAG C . 
T  5 CL  1   1544 1544 CL  CL  C . 
U  5 CL  1   1545 1545 CL  CL  C . 
V  4 SO4 1   1546 1546 SO4 SO4 C . 
W  4 SO4 1   1547 1547 SO4 SO4 C . 
X  5 CL  1   3000 3000 CL  CL  C . 
Y  5 CL  1   3001 3001 CL  CL  C . 
Z  5 CL  1   3002 3002 CL  CL  C . 
AA 2 4OJ 1   600  600  4OJ 4OJ D . 
BA 3 NAG 1   701  701  NAG NAG D . 
CA 3 NAG 1   702  702  NAG NAG D . 
DA 3 NAG 1   703  703  NAG NAG D . 
EA 4 SO4 1   1544 1544 SO4 SO4 D . 
FA 4 SO4 1   1545 1545 SO4 SO4 D . 
GA 4 SO4 1   1546 1546 SO4 SO4 D . 
HA 5 CL  1   3000 3000 CL  CL  D . 
IA 5 CL  1   3001 3001 CL  CL  D . 
JA 5 CL  1   3002 3002 CL  CL  D . 
KA 6 HOH 1   2001 2001 HOH HOH A . 
KA 6 HOH 2   2002 2002 HOH HOH A . 
KA 6 HOH 3   2003 2003 HOH HOH A . 
KA 6 HOH 4   2004 2004 HOH HOH A . 
KA 6 HOH 5   2005 2005 HOH HOH A . 
KA 6 HOH 6   2006 2006 HOH HOH A . 
KA 6 HOH 7   2007 2007 HOH HOH A . 
KA 6 HOH 8   2008 2008 HOH HOH A . 
KA 6 HOH 9   2009 2009 HOH HOH A . 
KA 6 HOH 10  2010 2010 HOH HOH A . 
KA 6 HOH 11  2011 2011 HOH HOH A . 
KA 6 HOH 12  2012 2012 HOH HOH A . 
KA 6 HOH 13  2013 2013 HOH HOH A . 
KA 6 HOH 14  2014 2014 HOH HOH A . 
KA 6 HOH 15  2015 2015 HOH HOH A . 
KA 6 HOH 16  2016 2016 HOH HOH A . 
KA 6 HOH 17  2017 2017 HOH HOH A . 
KA 6 HOH 18  2018 2018 HOH HOH A . 
KA 6 HOH 19  2019 2019 HOH HOH A . 
KA 6 HOH 20  2020 2020 HOH HOH A . 
KA 6 HOH 21  2021 2021 HOH HOH A . 
KA 6 HOH 22  2022 2022 HOH HOH A . 
KA 6 HOH 23  2023 2023 HOH HOH A . 
KA 6 HOH 24  2024 2024 HOH HOH A . 
KA 6 HOH 25  2025 2025 HOH HOH A . 
KA 6 HOH 26  2026 2026 HOH HOH A . 
KA 6 HOH 27  2027 2027 HOH HOH A . 
KA 6 HOH 28  2028 2028 HOH HOH A . 
KA 6 HOH 29  2029 2029 HOH HOH A . 
KA 6 HOH 30  2030 2030 HOH HOH A . 
KA 6 HOH 31  2031 2031 HOH HOH A . 
KA 6 HOH 32  2032 2032 HOH HOH A . 
KA 6 HOH 33  2033 2033 HOH HOH A . 
KA 6 HOH 34  2034 2034 HOH HOH A . 
KA 6 HOH 35  2035 2035 HOH HOH A . 
KA 6 HOH 36  2036 2036 HOH HOH A . 
KA 6 HOH 37  2037 2037 HOH HOH A . 
KA 6 HOH 38  2038 2038 HOH HOH A . 
KA 6 HOH 39  2039 2039 HOH HOH A . 
KA 6 HOH 40  2040 2040 HOH HOH A . 
KA 6 HOH 41  2041 2041 HOH HOH A . 
KA 6 HOH 42  2042 2042 HOH HOH A . 
KA 6 HOH 43  2043 2043 HOH HOH A . 
KA 6 HOH 44  2044 2044 HOH HOH A . 
KA 6 HOH 45  2045 2045 HOH HOH A . 
KA 6 HOH 46  2046 2046 HOH HOH A . 
KA 6 HOH 47  2047 2047 HOH HOH A . 
KA 6 HOH 48  2048 2048 HOH HOH A . 
KA 6 HOH 49  2049 2049 HOH HOH A . 
KA 6 HOH 50  2050 2050 HOH HOH A . 
KA 6 HOH 51  2051 2051 HOH HOH A . 
KA 6 HOH 52  2052 2052 HOH HOH A . 
KA 6 HOH 53  2053 2053 HOH HOH A . 
KA 6 HOH 54  2054 2054 HOH HOH A . 
KA 6 HOH 55  2055 2055 HOH HOH A . 
KA 6 HOH 56  2056 2056 HOH HOH A . 
KA 6 HOH 57  2057 2057 HOH HOH A . 
KA 6 HOH 58  2058 2058 HOH HOH A . 
KA 6 HOH 59  2059 2059 HOH HOH A . 
KA 6 HOH 60  2060 2060 HOH HOH A . 
KA 6 HOH 61  2061 2061 HOH HOH A . 
KA 6 HOH 62  2062 2062 HOH HOH A . 
KA 6 HOH 63  2063 2063 HOH HOH A . 
KA 6 HOH 64  2064 2064 HOH HOH A . 
KA 6 HOH 65  2065 2065 HOH HOH A . 
KA 6 HOH 66  2066 2066 HOH HOH A . 
KA 6 HOH 67  2067 2067 HOH HOH A . 
KA 6 HOH 68  2068 2068 HOH HOH A . 
KA 6 HOH 69  2069 2069 HOH HOH A . 
KA 6 HOH 70  2070 2070 HOH HOH A . 
KA 6 HOH 71  2071 2071 HOH HOH A . 
KA 6 HOH 72  2072 2072 HOH HOH A . 
KA 6 HOH 73  2073 2073 HOH HOH A . 
KA 6 HOH 74  2074 2074 HOH HOH A . 
KA 6 HOH 75  2075 2075 HOH HOH A . 
KA 6 HOH 76  2076 2076 HOH HOH A . 
KA 6 HOH 77  2077 2077 HOH HOH A . 
KA 6 HOH 78  2078 2078 HOH HOH A . 
KA 6 HOH 79  2079 2079 HOH HOH A . 
KA 6 HOH 80  2080 2080 HOH HOH A . 
KA 6 HOH 81  2081 2081 HOH HOH A . 
KA 6 HOH 82  2082 2082 HOH HOH A . 
KA 6 HOH 83  2083 2083 HOH HOH A . 
KA 6 HOH 84  2084 2084 HOH HOH A . 
KA 6 HOH 85  2085 2085 HOH HOH A . 
KA 6 HOH 86  2086 2086 HOH HOH A . 
KA 6 HOH 87  2087 2087 HOH HOH A . 
KA 6 HOH 88  2088 2088 HOH HOH A . 
KA 6 HOH 89  2089 2089 HOH HOH A . 
KA 6 HOH 90  2090 2090 HOH HOH A . 
KA 6 HOH 91  2091 2091 HOH HOH A . 
KA 6 HOH 92  2092 2092 HOH HOH A . 
KA 6 HOH 93  2093 2093 HOH HOH A . 
KA 6 HOH 94  2094 2094 HOH HOH A . 
KA 6 HOH 95  2095 2095 HOH HOH A . 
KA 6 HOH 96  2096 2096 HOH HOH A . 
KA 6 HOH 97  2097 2097 HOH HOH A . 
KA 6 HOH 98  2098 2098 HOH HOH A . 
KA 6 HOH 99  2099 2099 HOH HOH A . 
KA 6 HOH 100 2100 2100 HOH HOH A . 
KA 6 HOH 101 2101 2101 HOH HOH A . 
KA 6 HOH 102 2102 2102 HOH HOH A . 
KA 6 HOH 103 2103 2103 HOH HOH A . 
KA 6 HOH 104 2104 2104 HOH HOH A . 
KA 6 HOH 105 2105 2105 HOH HOH A . 
KA 6 HOH 106 2106 2106 HOH HOH A . 
KA 6 HOH 107 2107 2107 HOH HOH A . 
KA 6 HOH 108 2108 2108 HOH HOH A . 
KA 6 HOH 109 2109 2109 HOH HOH A . 
KA 6 HOH 110 2110 2110 HOH HOH A . 
KA 6 HOH 111 2111 2111 HOH HOH A . 
KA 6 HOH 112 2112 2112 HOH HOH A . 
KA 6 HOH 113 2113 2113 HOH HOH A . 
KA 6 HOH 114 2114 2114 HOH HOH A . 
KA 6 HOH 115 2115 2115 HOH HOH A . 
KA 6 HOH 116 2116 2116 HOH HOH A . 
KA 6 HOH 117 2117 2117 HOH HOH A . 
LA 6 HOH 1   2001 2001 HOH HOH B . 
LA 6 HOH 2   2002 2002 HOH HOH B . 
LA 6 HOH 3   2003 2003 HOH HOH B . 
LA 6 HOH 4   2004 2004 HOH HOH B . 
LA 6 HOH 5   2005 2005 HOH HOH B . 
LA 6 HOH 6   2006 2006 HOH HOH B . 
LA 6 HOH 7   2007 2007 HOH HOH B . 
LA 6 HOH 8   2008 2008 HOH HOH B . 
LA 6 HOH 9   2009 2009 HOH HOH B . 
LA 6 HOH 10  2010 2010 HOH HOH B . 
LA 6 HOH 11  2011 2011 HOH HOH B . 
LA 6 HOH 12  2012 2012 HOH HOH B . 
LA 6 HOH 13  2013 2013 HOH HOH B . 
LA 6 HOH 14  2014 2014 HOH HOH B . 
LA 6 HOH 15  2015 2015 HOH HOH B . 
LA 6 HOH 16  2016 2016 HOH HOH B . 
LA 6 HOH 17  2017 2017 HOH HOH B . 
LA 6 HOH 18  2018 2018 HOH HOH B . 
LA 6 HOH 19  2019 2019 HOH HOH B . 
LA 6 HOH 20  2020 2020 HOH HOH B . 
LA 6 HOH 21  2021 2021 HOH HOH B . 
LA 6 HOH 22  2022 2022 HOH HOH B . 
LA 6 HOH 23  2023 2023 HOH HOH B . 
LA 6 HOH 24  2024 2024 HOH HOH B . 
LA 6 HOH 25  2025 2025 HOH HOH B . 
LA 6 HOH 26  2026 2026 HOH HOH B . 
LA 6 HOH 27  2027 2027 HOH HOH B . 
LA 6 HOH 28  2028 2028 HOH HOH B . 
LA 6 HOH 29  2029 2029 HOH HOH B . 
LA 6 HOH 30  2030 2030 HOH HOH B . 
LA 6 HOH 31  2031 2031 HOH HOH B . 
LA 6 HOH 32  2032 2032 HOH HOH B . 
LA 6 HOH 33  2033 2033 HOH HOH B . 
LA 6 HOH 34  2034 2034 HOH HOH B . 
LA 6 HOH 35  2035 2035 HOH HOH B . 
LA 6 HOH 36  2036 2036 HOH HOH B . 
LA 6 HOH 37  2037 2037 HOH HOH B . 
LA 6 HOH 38  2038 2038 HOH HOH B . 
LA 6 HOH 39  2039 2039 HOH HOH B . 
LA 6 HOH 40  2040 2040 HOH HOH B . 
LA 6 HOH 41  2041 2041 HOH HOH B . 
LA 6 HOH 42  2042 2042 HOH HOH B . 
LA 6 HOH 43  2043 2043 HOH HOH B . 
LA 6 HOH 44  2044 2044 HOH HOH B . 
LA 6 HOH 45  2045 2045 HOH HOH B . 
LA 6 HOH 46  2046 2046 HOH HOH B . 
LA 6 HOH 47  2047 2047 HOH HOH B . 
LA 6 HOH 48  2048 2048 HOH HOH B . 
LA 6 HOH 49  2049 2049 HOH HOH B . 
LA 6 HOH 50  2050 2050 HOH HOH B . 
LA 6 HOH 51  2051 2051 HOH HOH B . 
LA 6 HOH 52  2052 2052 HOH HOH B . 
LA 6 HOH 53  2053 2053 HOH HOH B . 
LA 6 HOH 54  2054 2054 HOH HOH B . 
LA 6 HOH 55  2055 2055 HOH HOH B . 
LA 6 HOH 56  2056 2056 HOH HOH B . 
LA 6 HOH 57  2057 2057 HOH HOH B . 
LA 6 HOH 58  2058 2058 HOH HOH B . 
LA 6 HOH 59  2059 2059 HOH HOH B . 
LA 6 HOH 60  2060 2060 HOH HOH B . 
LA 6 HOH 61  2061 2061 HOH HOH B . 
LA 6 HOH 62  2062 2062 HOH HOH B . 
LA 6 HOH 63  2063 2063 HOH HOH B . 
LA 6 HOH 64  2064 2064 HOH HOH B . 
LA 6 HOH 65  2065 2065 HOH HOH B . 
LA 6 HOH 66  2066 2066 HOH HOH B . 
LA 6 HOH 67  2067 2067 HOH HOH B . 
LA 6 HOH 68  2068 2068 HOH HOH B . 
LA 6 HOH 69  2069 2069 HOH HOH B . 
LA 6 HOH 70  2070 2070 HOH HOH B . 
LA 6 HOH 71  2071 2071 HOH HOH B . 
LA 6 HOH 72  2072 2072 HOH HOH B . 
LA 6 HOH 73  2073 2073 HOH HOH B . 
LA 6 HOH 74  2074 2074 HOH HOH B . 
LA 6 HOH 75  2075 2075 HOH HOH B . 
LA 6 HOH 76  2076 2076 HOH HOH B . 
LA 6 HOH 77  2077 2077 HOH HOH B . 
LA 6 HOH 78  2078 2078 HOH HOH B . 
LA 6 HOH 79  2079 2079 HOH HOH B . 
LA 6 HOH 80  2080 2080 HOH HOH B . 
LA 6 HOH 81  2081 2081 HOH HOH B . 
LA 6 HOH 82  2082 2082 HOH HOH B . 
MA 6 HOH 1   2001 2001 HOH HOH C . 
MA 6 HOH 2   2002 2002 HOH HOH C . 
MA 6 HOH 3   2003 2003 HOH HOH C . 
MA 6 HOH 4   2004 2004 HOH HOH C . 
MA 6 HOH 5   2005 2005 HOH HOH C . 
MA 6 HOH 6   2006 2006 HOH HOH C . 
MA 6 HOH 7   2007 2007 HOH HOH C . 
MA 6 HOH 8   2008 2008 HOH HOH C . 
MA 6 HOH 9   2009 2009 HOH HOH C . 
MA 6 HOH 10  2010 2010 HOH HOH C . 
MA 6 HOH 11  2011 2011 HOH HOH C . 
MA 6 HOH 12  2012 2012 HOH HOH C . 
MA 6 HOH 13  2013 2013 HOH HOH C . 
MA 6 HOH 14  2014 2014 HOH HOH C . 
MA 6 HOH 15  2015 2015 HOH HOH C . 
MA 6 HOH 16  2016 2016 HOH HOH C . 
MA 6 HOH 17  2017 2017 HOH HOH C . 
MA 6 HOH 18  2018 2018 HOH HOH C . 
MA 6 HOH 19  2019 2019 HOH HOH C . 
MA 6 HOH 20  2020 2020 HOH HOH C . 
MA 6 HOH 21  2021 2021 HOH HOH C . 
MA 6 HOH 22  2022 2022 HOH HOH C . 
MA 6 HOH 23  2023 2023 HOH HOH C . 
MA 6 HOH 24  2024 2024 HOH HOH C . 
MA 6 HOH 25  2025 2025 HOH HOH C . 
MA 6 HOH 26  2026 2026 HOH HOH C . 
MA 6 HOH 27  2027 2027 HOH HOH C . 
MA 6 HOH 28  2028 2028 HOH HOH C . 
MA 6 HOH 29  2029 2029 HOH HOH C . 
MA 6 HOH 30  2030 2030 HOH HOH C . 
MA 6 HOH 31  2031 2031 HOH HOH C . 
MA 6 HOH 32  2032 2032 HOH HOH C . 
MA 6 HOH 33  2033 2033 HOH HOH C . 
MA 6 HOH 34  2034 2034 HOH HOH C . 
MA 6 HOH 35  2035 2035 HOH HOH C . 
MA 6 HOH 36  2036 2036 HOH HOH C . 
MA 6 HOH 37  2037 2037 HOH HOH C . 
MA 6 HOH 38  2038 2038 HOH HOH C . 
MA 6 HOH 39  2039 2039 HOH HOH C . 
MA 6 HOH 40  2040 2040 HOH HOH C . 
MA 6 HOH 41  2041 2041 HOH HOH C . 
MA 6 HOH 42  2042 2042 HOH HOH C . 
MA 6 HOH 43  2043 2043 HOH HOH C . 
MA 6 HOH 44  2044 2044 HOH HOH C . 
MA 6 HOH 45  2045 2045 HOH HOH C . 
MA 6 HOH 46  2046 2046 HOH HOH C . 
MA 6 HOH 47  2047 2047 HOH HOH C . 
MA 6 HOH 48  2048 2048 HOH HOH C . 
MA 6 HOH 49  2049 2049 HOH HOH C . 
MA 6 HOH 50  2050 2050 HOH HOH C . 
MA 6 HOH 51  2051 2051 HOH HOH C . 
MA 6 HOH 52  2052 2052 HOH HOH C . 
MA 6 HOH 53  2053 2053 HOH HOH C . 
MA 6 HOH 54  2054 2054 HOH HOH C . 
MA 6 HOH 55  2055 2055 HOH HOH C . 
MA 6 HOH 56  2056 2056 HOH HOH C . 
MA 6 HOH 57  2057 2057 HOH HOH C . 
MA 6 HOH 58  2058 2058 HOH HOH C . 
MA 6 HOH 59  2059 2059 HOH HOH C . 
MA 6 HOH 60  2060 2060 HOH HOH C . 
MA 6 HOH 61  2061 2061 HOH HOH C . 
MA 6 HOH 62  2062 2062 HOH HOH C . 
MA 6 HOH 63  2063 2063 HOH HOH C . 
MA 6 HOH 64  2064 2064 HOH HOH C . 
MA 6 HOH 65  2065 2065 HOH HOH C . 
MA 6 HOH 66  2066 2066 HOH HOH C . 
MA 6 HOH 67  2067 2067 HOH HOH C . 
MA 6 HOH 68  2068 2068 HOH HOH C . 
MA 6 HOH 69  2069 2069 HOH HOH C . 
MA 6 HOH 70  2070 2070 HOH HOH C . 
MA 6 HOH 71  2071 2071 HOH HOH C . 
MA 6 HOH 72  2072 2072 HOH HOH C . 
MA 6 HOH 73  2073 2073 HOH HOH C . 
MA 6 HOH 74  2074 2074 HOH HOH C . 
MA 6 HOH 75  2075 2075 HOH HOH C . 
MA 6 HOH 76  2076 2076 HOH HOH C . 
MA 6 HOH 77  2077 2077 HOH HOH C . 
MA 6 HOH 78  2078 2078 HOH HOH C . 
MA 6 HOH 79  2079 2079 HOH HOH C . 
MA 6 HOH 80  2080 2080 HOH HOH C . 
MA 6 HOH 81  2081 2081 HOH HOH C . 
MA 6 HOH 82  2082 2082 HOH HOH C . 
MA 6 HOH 83  2083 2083 HOH HOH C . 
MA 6 HOH 84  2084 2084 HOH HOH C . 
MA 6 HOH 85  2085 2085 HOH HOH C . 
MA 6 HOH 86  2086 2086 HOH HOH C . 
MA 6 HOH 87  2087 2087 HOH HOH C . 
MA 6 HOH 88  2088 2088 HOH HOH C . 
MA 6 HOH 89  2089 2089 HOH HOH C . 
MA 6 HOH 90  2090 2090 HOH HOH C . 
MA 6 HOH 91  2091 2091 HOH HOH C . 
MA 6 HOH 92  2092 2092 HOH HOH C . 
MA 6 HOH 93  2093 2093 HOH HOH C . 
MA 6 HOH 94  2094 2094 HOH HOH C . 
MA 6 HOH 95  2095 2095 HOH HOH C . 
MA 6 HOH 96  2096 2096 HOH HOH C . 
MA 6 HOH 97  2097 2097 HOH HOH C . 
MA 6 HOH 98  2098 2098 HOH HOH C . 
MA 6 HOH 99  2099 2099 HOH HOH C . 
MA 6 HOH 100 2100 2100 HOH HOH C . 
MA 6 HOH 101 2101 2101 HOH HOH C . 
MA 6 HOH 102 2102 2102 HOH HOH C . 
MA 6 HOH 103 2103 2103 HOH HOH C . 
MA 6 HOH 104 2104 2104 HOH HOH C . 
MA 6 HOH 105 2105 2105 HOH HOH C . 
MA 6 HOH 106 2106 2106 HOH HOH C . 
MA 6 HOH 107 2107 2107 HOH HOH C . 
MA 6 HOH 108 2108 2108 HOH HOH C . 
MA 6 HOH 109 2109 2109 HOH HOH C . 
MA 6 HOH 110 2110 2110 HOH HOH C . 
MA 6 HOH 111 2111 2111 HOH HOH C . 
MA 6 HOH 112 2112 2112 HOH HOH C . 
MA 6 HOH 113 2113 2113 HOH HOH C . 
MA 6 HOH 114 2114 2114 HOH HOH C . 
MA 6 HOH 115 2115 2115 HOH HOH C . 
NA 6 HOH 1   2001 2001 HOH HOH D . 
NA 6 HOH 2   2002 2002 HOH HOH D . 
NA 6 HOH 3   2003 2003 HOH HOH D . 
NA 6 HOH 4   2004 2004 HOH HOH D . 
NA 6 HOH 5   2005 2005 HOH HOH D . 
NA 6 HOH 6   2006 2006 HOH HOH D . 
NA 6 HOH 7   2007 2007 HOH HOH D . 
NA 6 HOH 8   2008 2008 HOH HOH D . 
NA 6 HOH 9   2009 2009 HOH HOH D . 
NA 6 HOH 10  2010 2010 HOH HOH D . 
NA 6 HOH 11  2011 2011 HOH HOH D . 
NA 6 HOH 12  2012 2012 HOH HOH D . 
NA 6 HOH 13  2013 2013 HOH HOH D . 
NA 6 HOH 14  2014 2014 HOH HOH D . 
NA 6 HOH 15  2015 2015 HOH HOH D . 
NA 6 HOH 16  2016 2016 HOH HOH D . 
NA 6 HOH 17  2017 2017 HOH HOH D . 
NA 6 HOH 18  2018 2018 HOH HOH D . 
NA 6 HOH 19  2019 2019 HOH HOH D . 
NA 6 HOH 20  2020 2020 HOH HOH D . 
NA 6 HOH 21  2021 2021 HOH HOH D . 
NA 6 HOH 22  2022 2022 HOH HOH D . 
NA 6 HOH 23  2023 2023 HOH HOH D . 
NA 6 HOH 24  2024 2024 HOH HOH D . 
NA 6 HOH 25  2025 2025 HOH HOH D . 
NA 6 HOH 26  2026 2026 HOH HOH D . 
NA 6 HOH 27  2027 2027 HOH HOH D . 
NA 6 HOH 28  2028 2028 HOH HOH D . 
NA 6 HOH 29  2029 2029 HOH HOH D . 
NA 6 HOH 30  2030 2030 HOH HOH D . 
NA 6 HOH 31  2031 2031 HOH HOH D . 
NA 6 HOH 32  2032 2032 HOH HOH D . 
NA 6 HOH 33  2033 2033 HOH HOH D . 
NA 6 HOH 34  2034 2034 HOH HOH D . 
NA 6 HOH 35  2035 2035 HOH HOH D . 
NA 6 HOH 36  2036 2036 HOH HOH D . 
NA 6 HOH 37  2037 2037 HOH HOH D . 
NA 6 HOH 38  2038 2038 HOH HOH D . 
NA 6 HOH 39  2039 2039 HOH HOH D . 
NA 6 HOH 40  2040 2040 HOH HOH D . 
NA 6 HOH 41  2041 2041 HOH HOH D . 
NA 6 HOH 42  2042 2042 HOH HOH D . 
NA 6 HOH 43  2043 2043 HOH HOH D . 
NA 6 HOH 44  2044 2044 HOH HOH D . 
NA 6 HOH 45  2045 2045 HOH HOH D . 
NA 6 HOH 46  2046 2046 HOH HOH D . 
NA 6 HOH 47  2047 2047 HOH HOH D . 
NA 6 HOH 48  2048 2048 HOH HOH D . 
NA 6 HOH 49  2049 2049 HOH HOH D . 
NA 6 HOH 50  2050 2050 HOH HOH D . 
NA 6 HOH 51  2051 2051 HOH HOH D . 
NA 6 HOH 52  2052 2052 HOH HOH D . 
NA 6 HOH 53  2053 2053 HOH HOH D . 
NA 6 HOH 54  2054 2054 HOH HOH D . 
NA 6 HOH 55  2055 2055 HOH HOH D . 
NA 6 HOH 56  2056 2056 HOH HOH D . 
NA 6 HOH 57  2057 2057 HOH HOH D . 
NA 6 HOH 58  2058 2058 HOH HOH D . 
NA 6 HOH 59  2059 2059 HOH HOH D . 
NA 6 HOH 60  2060 2060 HOH HOH D . 
NA 6 HOH 61  2061 2061 HOH HOH D . 
NA 6 HOH 62  2062 2062 HOH HOH D . 
NA 6 HOH 63  2063 2063 HOH HOH D . 
NA 6 HOH 64  2064 2064 HOH HOH D . 
NA 6 HOH 65  2065 2065 HOH HOH D . 
NA 6 HOH 66  2066 2066 HOH HOH D . 
NA 6 HOH 67  2067 2067 HOH HOH D . 
NA 6 HOH 68  2068 2068 HOH HOH D . 
NA 6 HOH 69  2069 2069 HOH HOH D . 
NA 6 HOH 70  2070 2070 HOH HOH D . 
NA 6 HOH 71  2071 2071 HOH HOH D . 
NA 6 HOH 72  2072 2072 HOH HOH D . 
NA 6 HOH 73  2073 2073 HOH HOH D . 
NA 6 HOH 74  2074 2074 HOH HOH D . 
NA 6 HOH 75  2075 2075 HOH HOH D . 
NA 6 HOH 76  2076 2076 HOH HOH D . 
NA 6 HOH 77  2077 2077 HOH HOH D . 
NA 6 HOH 78  2078 2078 HOH HOH D . 
NA 6 HOH 79  2079 2079 HOH HOH D . 
NA 6 HOH 80  2080 2080 HOH HOH D . 
NA 6 HOH 81  2081 2081 HOH HOH D . 
NA 6 HOH 82  2082 2082 HOH HOH D . 
NA 6 HOH 83  2083 2083 HOH HOH D . 
NA 6 HOH 84  2084 2084 HOH HOH D . 
NA 6 HOH 85  2085 2085 HOH HOH D . 
NA 6 HOH 86  2086 2086 HOH HOH D . 
NA 6 HOH 87  2087 2087 HOH HOH D . 
NA 6 HOH 88  2088 2088 HOH HOH D . 
NA 6 HOH 89  2089 2089 HOH HOH D . 
NA 6 HOH 90  2090 2090 HOH HOH D . 
NA 6 HOH 91  2091 2091 HOH HOH D . 
NA 6 HOH 92  2092 2092 HOH HOH D . 
NA 6 HOH 93  2093 2093 HOH HOH D . 
NA 6 HOH 94  2094 2094 HOH HOH D . 
NA 6 HOH 95  2095 2095 HOH HOH D . 
NA 6 HOH 96  2096 2096 HOH HOH D . 
NA 6 HOH 97  2097 2097 HOH HOH D . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 265 A ASN 265 ? ASN 'GLYCOSYLATION SITE' 
2 B ASN 265 B ASN 265 ? ASN 'GLYCOSYLATION SITE' 
3 B ASN 350 B ASN 350 ? ASN 'GLYCOSYLATION SITE' 
4 D ASN 265 D ASN 265 ? ASN 'GLYCOSYLATION SITE' 
5 D ASN 350 D ASN 350 ? ASN 'GLYCOSYLATION SITE' 
6 D ASN 464 D ASN 464 ? ASN 'GLYCOSYLATION SITE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 software_defined_assembly            PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I,J,K,L,M,N,O,P,Q,KA,LA                       
2 1 C,D,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,MA,NA 
# 
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)' 4220   ? 
1 MORE         -106.5 ? 
1 'SSA (A^2)'  38450  ? 
2 'ABSA (A^2)' 4630   ? 
2 MORE         -124.6 ? 
2 'SSA (A^2)'  39140  ? 
# 
_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_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2013-02-06 
2 'Structure model' 1 1 2013-02-27 
# 
_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_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined -5.0300  -28.8538 26.5797 0.1486 0.1647 0.2848 0.0417  0.0116  0.0264  0.9249 1.5694 1.0605 
-0.1518 -0.1280 0.1825 0.0406  0.0347  0.0352  -0.2593 0.0125  0.0472  -0.1423 -0.0599 0.0452  
'X-RAY DIFFRACTION' 2 ? refined 8.4933   27.5493  46.2152 0.6839 0.3580 0.4524 -0.4454 0.2660  -0.0120 0.9423 0.7201 0.5802 0.3483 
0.1452  0.3100 -0.0427 0.2708  0.0568  -0.4125 0.1964  -0.3699 -0.5503 0.5101  0.1944  
'X-RAY DIFFRACTION' 3 ? refined -24.9244 12.4072  87.1263 0.1829 0.1936 0.1287 -0.0329 0.1094  -0.0422 0.8522 0.8534 1.3462 
-0.0523 -0.0856 0.0812 -0.1288 -0.0125 -0.0132 -0.0175 -0.0054 0.0822  -0.0824 -0.2288 -0.2848 
'X-RAY DIFFRACTION' 4 ? refined -47.7610 5.0806   30.9194 0.2236 0.3784 0.2353 0.0370  -0.0831 -0.1480 0.8959 0.9504 1.9068 0.1479 
0.5628  0.2230 0.1006  -0.1985 0.0207  0.0994  -0.1283 0.2801  0.1435  -0.3213 -0.0236 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? 'CHAIN A' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? 'CHAIN B' 
'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? 'CHAIN C' 
'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? 'CHAIN D' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
PHENIX refinement       '(PHENIX.REFINE: 1.8.1_1168)' ? 1 
XDS    'data reduction' .                             ? 2 
XSCALE 'data scaling'   .                             ? 3 
MOLREP phasing          .                             ? 4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 ND2 C ASN 265  ? ? C1 C NAG 701  ? ? 1.45 
2 1 O   D HOH 2009 ? ? O  D HOH 2010 ? ? 2.09 
3 1 O   D HOH 2003 ? ? O  D HOH 2010 ? ? 2.10 
4 1 OE1 A GLU 334  ? ? O  A HOH 2088 ? ? 2.10 
5 1 OE2 A GLU 202  ? ? O  A HOH 2060 ? ? 2.13 
6 1 O   B ASN 265  ? ? O  B HOH 2044 ? ? 2.17 
7 1 NE1 C TRP 286  ? ? O  C HOH 2077 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C C CYS 257 ? ? N  C PRO 258 ? ? CA C PRO 258 ? ? 104.26 119.30 -15.04 1.50 Y 
2 1 N D SER 497 ? ? CA D SER 497 ? ? C  D SER 497 ? ? 92.24  111.00 -18.76 2.70 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 ARG A 3   ? ? 72.69   -18.14  
2  1 SER A 203 ? ? 60.93   -123.38 
3  1 ALA A 262 ? ? -86.79  -155.64 
4  1 ASP A 306 ? ? -117.17 -74.82  
5  1 VAL A 367 ? ? -115.27 73.80   
6  1 LEU A 373 ? ? 72.08   -23.51  
7  1 VAL A 407 ? ? -130.43 -64.57  
8  1 PRO A 440 ? ? -61.13  -177.98 
9  1 LYS A 496 ? ? 178.15  177.70  
10 1 ALA A 506 ? ? -55.43  -70.78  
11 1 LEU A 539 ? ? -82.22  -72.38  
12 1 SER A 541 ? ? -92.43  35.90   
13 1 ALA A 542 ? ? 117.39  5.35    
14 1 VAL B 12  ? ? 59.48   97.06   
15 1 ARG B 13  ? ? -34.74  -19.81  
16 1 ARG B 107 ? ? -63.07  -173.98 
17 1 ALA B 109 ? ? -88.61  -76.99  
18 1 PHE B 123 ? ? 68.87   -9.62   
19 1 ALA B 127 ? ? 178.26  156.04  
20 1 SER B 203 ? ? 57.73   -121.22 
21 1 HIS B 223 ? ? -130.01 -57.81  
22 1 ILE B 294 ? ? -108.96 -63.74  
23 1 PHE B 295 ? ? -80.12  -155.36 
24 1 ARG B 296 ? ? 68.77   80.62   
25 1 ASP B 306 ? ? -120.71 -75.91  
26 1 ASP B 349 ? ? -87.04  -72.19  
27 1 VAL B 445 ? ? -114.76 79.06   
28 1 ASP B 488 ? ? -176.63 129.43  
29 1 ARG B 493 ? ? -109.49 -60.86  
30 1 LYS B 496 ? ? 55.05   -155.16 
31 1 ARG B 525 ? ? 55.79   -97.12  
32 1 ALA B 526 ? ? 71.36   -103.38 
33 1 THR B 528 ? ? 80.93   -28.93  
34 1 ALA B 542 ? ? 73.02   -5.32   
35 1 PRO C 41  ? ? -78.71  49.00   
36 1 SER C 110 ? ? 69.46   140.29  
37 1 PHE C 123 ? ? 67.43   -5.76   
38 1 SER C 125 ? ? -170.33 -175.99 
39 1 SER C 203 ? ? 52.92   -120.05 
40 1 THR C 231 ? ? -175.16 142.62  
41 1 ASP C 306 ? ? -108.41 -76.10  
42 1 VAL C 367 ? ? -118.28 73.38   
43 1 VAL C 407 ? ? -121.19 -65.07  
44 1 LYS C 496 ? ? -74.46  -76.27  
45 1 SER C 497 ? ? 22.22   65.59   
46 1 ALA C 506 ? ? -58.85  -70.31  
47 1 ARG C 525 ? ? 36.15   65.20   
48 1 ASP D 5   ? ? -177.03 127.77  
49 1 PHE D 47  ? ? 77.16   -2.46   
50 1 PRO D 111 ? ? -62.84  80.24   
51 1 PHE D 123 ? ? 58.82   12.59   
52 1 SER D 203 ? ? 56.61   -118.81 
53 1 HIS D 223 ? ? -131.58 -58.10  
54 1 CYS D 257 ? ? -67.45  -175.35 
55 1 PRO D 258 ? ? -37.63  126.53  
56 1 ALA D 262 ? ? -138.88 -61.83  
57 1 HIS D 287 ? ? -143.23 -60.09  
58 1 ASP D 306 ? ? -101.23 -76.68  
59 1 VAL D 407 ? ? -117.34 -73.45  
60 1 ALA D 506 ? ? -57.76  -73.94  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 CYS A 257 ? ? PRO A 258 ? ? 149.41  
2 1 ASP A 323 ? ? LEU A 324 ? ? -146.18 
3 1 SER A 497 ? ? PRO A 498 ? ? -59.06  
4 1 SER A 541 ? ? ALA A 542 ? ? -134.94 
5 1 LYS B 496 ? ? SER B 497 ? ? -35.28  
6 1 PRO C 258 ? ? PRO C 259 ? ? -34.24  
7 1 GLY C 342 ? ? VAL C 343 ? ? 147.16  
8 1 LYS C 496 ? ? SER C 497 ? ? 121.82  
9 1 CYS D 257 ? ? PRO D 258 ? ? -113.50 
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C1 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    D 
_pdbx_validate_chiral.auth_comp_id    NAG 
_pdbx_validate_chiral.auth_seq_id     702 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         PLANAR 
_pdbx_validate_chiral.omega           . 
# 
_pdbx_unobs_or_zero_occ_atoms.id               1 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag     N 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id     C 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id     NAG 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id      701 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id     O1 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id     ? 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id    S 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id    NAG 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id     1 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id    O1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 1 ? A GLU 1 
2  1 Y 1 B GLU 1 ? B GLU 1 
3  1 Y 1 B GLY 2 ? B GLY 2 
4  1 Y 1 B ARG 3 ? B ARG 3 
5  1 Y 1 B GLU 4 ? B GLU 4 
6  1 Y 1 C GLU 1 ? C GLU 1 
7  1 Y 1 C GLY 2 ? C GLY 2 
8  1 Y 1 C ARG 3 ? C ARG 3 
9  1 Y 1 D GLU 1 ? D GLU 1 
10 1 Y 1 D GLY 2 ? D GLY 2 
11 1 Y 1 D ARG 3 ? D ARG 3 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2-methylphenyl) dihydrogen phosphate' 4OJ 
3 N-ACETYL-D-GLUCOSAMINE                  NAG 
4 'SULFATE ION'                           SO4 
5 'CHLORIDE ION'                          CL  
6 water                                   HOH 
# 
