data_6016 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignments of the 45.3 kDa catalytic domain of human BACE1 ; _BMRB_accession_number 6016 _BMRB_flat_file_name bmr6016.str _Entry_type original _Submission_date 2003-11-19 _Accession_date 2003-11-21 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Dingjiang . . 2 Wang Yu-sen . . 3 Gesell Jennifer J. . 4 Wilson Eileen . . 5 Beyer Brian M. . 6 Wyss Daniel . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 319 "13C chemical shifts" 917 "15N chemical shifts" 324 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-07-08 original author . stop_ _Original_release_date 2004-07-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone resonance assignments of the 45.3 kDa catalytic domain of human BACE1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Dingjiang . . 2 Wang Yu-sen . . 3 Gesell Jennifer J. . 4 Wilson Eileen . . 5 Beyer Brian M. . 6 Wyss Daniel F. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 29 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 425 _Page_last 426 _Year 2004 _Details . loop_ _Keyword 'NMR assignments' 'Alzheimer's disease' BACE stop_ save_ ################################## # Molecular system description # ################################## save_system_BACE1 _Saveframe_category molecular_system _Mol_system_name 'beta-site APP Cleaving Enzyme 1' _Abbreviation_common BACE1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'BACE1 monomer' $BACE1_monomer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'membrane-associated aspartic protease' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_BACE1_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'beta-site APP Cleaving Enzyme 1' _Abbreviation_common BACE1 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 407 _Mol_residue_sequence ; DEEPEEPGRRGSFVEMVDNL RGKSGQGYYVEMTVGSPPQT LNILVDTGSSNFAVGAAPHP FLHRYYQRQLSSTYRDLRKG VYVPYTQGKWEGELGTDLVS IPHGPNVTVRANIAAITESD KFFINGSNWEGILGLAYAEI ARPDDSLEPFFDSLVKQTHV PNLFSLQLCGAGFPLNQSEV LASVGGSMIIGGIDHSLYTG SLWYTPIRREWYYEVIIVRV EINGQDLKMDCKEYNYDKSI VDSGTTNLRLPKKVFEAAVK SIKAASSTEKFPDGFWLGEQ LVCWQAGTTPWNIFPVISLY LMGEVTNQSFRITILPQQYL RPVEDVATSQDDCYKFAISQ SSTGTVMGAVIMEGFYVVFD RARKRIGFAVSACHVHDEFR TAAVEGPFVTLDMEDCGYNI PQTDEST ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 48 ASP 2 49 GLU 3 50 GLU 4 51 PRO 5 52 GLU 6 53 GLU 7 54 PRO 8 55 GLY 9 56 ARG 10 57 ARG 11 58 GLY 12 59 SER 13 60 PHE 14 61 VAL 15 62 GLU 16 63 MET 17 64 VAL 18 65 ASP 19 66 ASN 20 67 LEU 21 68 ARG 22 69 GLY 23 70 LYS 24 71 SER 25 72 GLY 26 73 GLN 27 74 GLY 28 75 TYR 29 76 TYR 30 77 VAL 31 78 GLU 32 79 MET 33 80 THR 34 81 VAL 35 82 GLY 36 83 SER 37 84 PRO 38 85 PRO 39 86 GLN 40 87 THR 41 88 LEU 42 89 ASN 43 90 ILE 44 91 LEU 45 92 VAL 46 93 ASP 47 94 THR 48 95 GLY 49 96 SER 50 97 SER 51 98 ASN 52 99 PHE 53 100 ALA 54 101 VAL 55 102 GLY 56 103 ALA 57 104 ALA 58 105 PRO 59 106 HIS 60 107 PRO 61 108 PHE 62 109 LEU 63 110 HIS 64 111 ARG 65 112 TYR 66 113 TYR 67 114 GLN 68 115 ARG 69 116 GLN 70 117 LEU 71 118 SER 72 119 SER 73 120 THR 74 121 TYR 75 122 ARG 76 123 ASP 77 124 LEU 78 125 ARG 79 126 LYS 80 127 GLY 81 128 VAL 82 129 TYR 83 130 VAL 84 131 PRO 85 132 TYR 86 133 THR 87 134 GLN 88 135 GLY 89 136 LYS 90 137 TRP 91 138 GLU 92 139 GLY 93 140 GLU 94 141 LEU 95 142 GLY 96 143 THR 97 144 ASP 98 145 LEU 99 146 VAL 100 147 SER 101 148 ILE 102 149 PRO 103 150 HIS 104 151 GLY 105 152 PRO 106 153 ASN 107 154 VAL 108 155 THR 109 156 VAL 110 157 ARG 111 158 ALA 112 159 ASN 113 160 ILE 114 161 ALA 115 162 ALA 116 163 ILE 117 164 THR 118 165 GLU 119 166 SER 120 167 ASP 121 168 LYS 122 169 PHE 123 170 PHE 124 171 ILE 125 172 ASN 126 173 GLY 127 174 SER 128 175 ASN 129 176 TRP 130 177 GLU 131 178 GLY 132 179 ILE 133 180 LEU 134 181 GLY 135 182 LEU 136 183 ALA 137 184 TYR 138 185 ALA 139 186 GLU 140 187 ILE 141 188 ALA 142 189 ARG 143 190 PRO 144 191 ASP 145 192 ASP 146 193 SER 147 194 LEU 148 195 GLU 149 196 PRO 150 197 PHE 151 198 PHE 152 199 ASP 153 200 SER 154 201 LEU 155 202 VAL 156 203 LYS 157 204 GLN 158 205 THR 159 206 HIS 160 207 VAL 161 208 PRO 162 209 ASN 163 210 LEU 164 211 PHE 165 212 SER 166 213 LEU 167 214 GLN 168 215 LEU 169 216 CYS 170 217 GLY 171 218 ALA 172 219 GLY 173 220 PHE 174 221 PRO 175 222 LEU 176 223 ASN 177 224 GLN 178 225 SER 179 226 GLU 180 227 VAL 181 228 LEU 182 229 ALA 183 230 SER 184 231 VAL 185 232 GLY 186 233 GLY 187 234 SER 188 235 MET 189 236 ILE 190 237 ILE 191 238 GLY 192 239 GLY 193 240 ILE 194 241 ASP 195 242 HIS 196 243 SER 197 244 LEU 198 245 TYR 199 246 THR 200 247 GLY 201 248 SER 202 249 LEU 203 250 TRP 204 251 TYR 205 252 THR 206 253 PRO 207 254 ILE 208 255 ARG 209 256 ARG 210 257 GLU 211 258 TRP 212 259 TYR 213 260 TYR 214 261 GLU 215 262 VAL 216 263 ILE 217 264 ILE 218 265 VAL 219 266 ARG 220 267 VAL 221 268 GLU 222 269 ILE 223 270 ASN 224 271 GLY 225 272 GLN 226 273 ASP 227 274 LEU 228 275 LYS 229 276 MET 230 277 ASP 231 278 CYS 232 279 LYS 233 280 GLU 234 281 TYR 235 282 ASN 236 283 TYR 237 284 ASP 238 285 LYS 239 286 SER 240 287 ILE 241 288 VAL 242 289 ASP 243 290 SER 244 291 GLY 245 292 THR 246 293 THR 247 294 ASN 248 295 LEU 249 296 ARG 250 297 LEU 251 298 PRO 252 299 LYS 253 300 LYS 254 301 VAL 255 302 PHE 256 303 GLU 257 304 ALA 258 305 ALA 259 306 VAL 260 307 LYS 261 308 SER 262 309 ILE 263 310 LYS 264 311 ALA 265 312 ALA 266 313 SER 267 314 SER 268 315 THR 269 316 GLU 270 317 LYS 271 318 PHE 272 319 PRO 273 320 ASP 274 321 GLY 275 322 PHE 276 323 TRP 277 324 LEU 278 325 GLY 279 326 GLU 280 327 GLN 281 328 LEU 282 329 VAL 283 330 CYS 284 331 TRP 285 332 GLN 286 333 ALA 287 334 GLY 288 335 THR 289 336 THR 290 337 PRO 291 338 TRP 292 339 ASN 293 340 ILE 294 341 PHE 295 342 PRO 296 343 VAL 297 344 ILE 298 345 SER 299 346 LEU 300 347 TYR 301 348 LEU 302 349 MET 303 350 GLY 304 351 GLU 305 352 VAL 306 353 THR 307 354 ASN 308 355 GLN 309 356 SER 310 357 PHE 311 358 ARG 312 359 ILE 313 360 THR 314 361 ILE 315 362 LEU 316 363 PRO 317 364 GLN 318 365 GLN 319 366 TYR 320 367 LEU 321 368 ARG 322 369 PRO 323 370 VAL 324 371 GLU 325 372 ASP 326 373 VAL 327 374 ALA 328 375 THR 329 376 SER 330 377 GLN 331 378 ASP 332 379 ASP 333 380 CYS 334 381 TYR 335 382 LYS 336 383 PHE 337 384 ALA 338 385 ILE 339 386 SER 340 387 GLN 341 388 SER 342 389 SER 343 390 THR 344 391 GLY 345 392 THR 346 393 VAL 347 394 MET 348 395 GLY 349 396 ALA 350 397 VAL 351 398 ILE 352 399 MET 353 400 GLU 354 401 GLY 355 402 PHE 356 403 TYR 357 404 VAL 358 405 VAL 359 406 PHE 360 407 ASP 361 408 ARG 362 409 ALA 363 410 ARG 364 411 LYS 365 412 ARG 366 413 ILE 367 414 GLY 368 415 PHE 369 416 ALA 370 417 VAL 371 418 SER 372 419 ALA 373 420 CYS 374 421 HIS 375 422 VAL 376 423 HIS 377 424 ASP 378 425 GLU 379 426 PHE 380 427 ARG 381 428 THR 382 429 ALA 383 430 ALA 384 431 VAL 385 432 GLU 386 433 GLY 387 434 PRO 388 435 PHE 389 436 VAL 390 437 THR 391 438 LEU 392 439 ASP 393 440 MET 394 441 GLU 395 442 ASP 396 443 CYS 397 444 GLY 398 445 TYR 399 446 ASN 400 447 ILE 401 448 PRO 402 449 GLN 403 450 THR 404 451 ASP 405 452 GLU 406 453 SER 407 454 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1FKN "Structure Of Beta-Secretase Complexed With Inhibitor" 96.07 391 100.00 100.00 0.00e+00 PDB 1M4H "Crystal Structure Of Beta-Secretase Complexed With Inhibitor Om00-3" 96.07 391 100.00 100.00 0.00e+00 PDB 1SGZ "Crystal Structure Of Unbound Beta-Secretase Catalytic Domain." 95.58 389 100.00 100.00 0.00e+00 PDB 1TQF "Crystal Structure Of Human Beta Secretase Complexed With Inhibitor" 98.03 405 99.50 99.50 0.00e+00 PDB 1W50 "Apo Structure Of Bace (beta Secretase)" 99.75 411 99.51 100.00 0.00e+00 PDB 1W51 "Bace (Beta Secretase) In Complex With A Nanomolar Non- Peptidic Inhibitor" 99.75 411 99.51 100.00 0.00e+00 PDB 1XN2 "New Substrate Binding Pockets For Beta-Secretase." 95.58 389 100.00 100.00 0.00e+00 PDB 1XN3 "Crystal Structure Of Beta-Secretase Bound To A Long Inhibitor With Additional Upstream Residues." 95.58 389 100.00 100.00 0.00e+00 PDB 1XS7 "Crystal Structure Of A Cycloamide-Urethane-Derived Novel Inhibitor Bound To Human Brain Memapsin 2 (Beta-Secretase)." 95.58 389 100.00 100.00 0.00e+00 PDB 1YM2 "Crystal Structure Of Human Beta Secretase Complexed With Nvp-Aur200" 98.28 402 100.00 100.00 0.00e+00 PDB 1YM4 "Crystal Structure Of Human Beta Secretase Complexed With Nvp-Amk640" 99.75 408 100.00 100.00 0.00e+00 PDB 2B8L "Crystal Structure Of Human Beta Secretase Complexed With Inhibitor" 98.03 405 99.50 99.50 0.00e+00 PDB 2B8V "Crystal Structure Of Human Beta-Secretase Complexed With L- L000430,469" 98.03 405 99.50 99.50 0.00e+00 PDB 2F3E "Crystal Structure Of The Bace Complex With Axq093, A Macrocyclic Inhibitor" 98.28 402 100.00 100.00 0.00e+00 PDB 2F3F "Crystal Structure Of The Bace Complex With Bdf488, A Macrocyclic Inhibitor" 98.28 402 100.00 100.00 0.00e+00 PDB 2FDP "Crystal Structure Of Beta-Secretase Complexed With An Amino- Ethylene Inhibitor" 95.33 388 100.00 100.00 0.00e+00 PDB 2G94 "Crystal Structure Of Beta-secretase Bound To A Potent And Highly Selective Inhibitor." 95.58 389 100.00 100.00 0.00e+00 PDB 2HIZ "Crystal Structure Of Human Beta-Secretase (Bace) In The Presence Of An Inhibitor" 99.75 455 100.00 100.00 0.00e+00 PDB 2HM1 "Crystal Structure Of Human Beta-Secretase (Bace) In The Presence Of An Inhibitor (2)" 97.54 406 100.00 100.00 0.00e+00 PDB 2IQG "Crystal Structure Of Hydroxyethyl Secondary Amine-Based Peptidomimetic Inhibitor Of Human Beta-Secretase (Bace)" 97.54 406 100.00 100.00 0.00e+00 PDB 2IRZ "Crystal Structure Of Human Beta-Secretase Complexed With Inhibitor" 98.03 405 99.50 99.50 0.00e+00 PDB 2IS0 "Crystal Structure Of Human Beta-Secretase Complexed With Inhibitor" 98.03 405 99.50 99.50 0.00e+00 PDB 2NTR "Crystal Structure Of Human Bace-1 Bound To Inhibitor" 98.03 405 99.50 99.50 0.00e+00 PDB 2OAH "Crystal Structure Of Human Beta Secretase Complexed With Inhibitor" 98.03 405 99.50 99.50 0.00e+00 PDB 2OF0 "X-Ray Crystal Structure Of Beta Secretase Complexed With Compound 5" 98.03 402 99.50 100.00 0.00e+00 PDB 2OHK "X-Ray Crystal Structure Of Beta Secretase Complexed With 1- Amino-Isoquinoline" 98.03 402 99.50 100.00 0.00e+00 PDB 2OHL "X-Ray Crystal Structure Of Beta Secretase Complexed With 2- Aminoquinoline" 98.03 402 99.50 100.00 0.00e+00 PDB 2OHM "X-Ray Crystal Structure Of Beta Secretase Complexed With N~3~-Benzylpyridine-2,3-Diamine" 98.03 402 99.50 100.00 0.00e+00 PDB 2OHN "X-Ray Crystal Structure Of Beta Secretase Complexed With 4- (4-Fluorobenzyl)piperidine" 98.03 402 99.50 100.00 0.00e+00 PDB 2OHP "X-ray Crystal Structure Of Beta Secretase Complexed With Compound 3" 98.03 402 99.50 100.00 0.00e+00 PDB 2OHQ "X-Ray Crystal Structure Of Beta Secretase Complexed With Compound 4" 98.03 402 99.50 100.00 0.00e+00 PDB 2OHR "X-Ray Crystal Structure Of Beta Secretase Complexed With Compound 6a" 98.03 402 99.50 100.00 0.00e+00 PDB 2OHS "X-Ray Crystal Structure Of Beta Secretase Complexed With Compound 6b" 98.03 402 99.50 100.00 0.00e+00 PDB 2OHT "X-Ray Crystal Structure Of Beta Secretase Complexed With Compound 7" 98.03 402 99.50 100.00 0.00e+00 PDB 2OHU "X-Ray Crystal Structure Of Beta Secretase Complexed With Compound 8b" 98.03 402 99.50 100.00 0.00e+00 PDB 2P4J "Crystal Structure Of Beta-Secretase Bond To An Inhibitor With Isophthalamide Derivatives At P2-P3" 95.58 389 100.00 100.00 0.00e+00 PDB 2P83 "Potent And Selective Isophthalamide S2 Hydroxyethylamine Inhibitor Of Bace1" 99.75 455 100.00 100.00 0.00e+00 PDB 2P8H "Crystal Structure Of Human Beta Secretase Complexed With Inhibitor" 98.03 405 99.50 99.50 0.00e+00 PDB 2PH6 "Crystal Structure Of Human Beta Secretase Complexed With Inhibitor" 98.03 405 99.50 99.50 0.00e+00 PDB 2PH8 "Crystal Structure Of Human Beta Secretase Complexed With Inhibitor" 98.03 405 99.50 99.50 0.00e+00 PDB 2Q11 "Structure Of Bace Complexed To Compound 1" 95.33 388 98.97 98.97 0.00e+00 PDB 2Q15 "Structure Of Bace Complexed To Compound 3a" 94.59 385 98.96 98.96 0.00e+00 PDB 2QK5 "Structure Of Bace1 Bound To Sch626485" 96.56 395 100.00 100.00 0.00e+00 PDB 2QMD "Structure Of Bace Bound To Sch722924" 96.56 395 100.00 100.00 0.00e+00 PDB 2QMF "Structure Of Bace Bound To Sch735310" 96.56 395 100.00 100.00 0.00e+00 PDB 2QMG "Structure Of Bace Bound To Sch745966" 96.56 395 100.00 100.00 0.00e+00 PDB 2QP8 "Structure Of Bace Bound To Sch734723" 96.56 395 100.00 100.00 0.00e+00 PDB 2QU2 "Bace1 With Compound 1" 100.00 415 100.00 100.00 0.00e+00 PDB 2QU3 "Bace1 With Compound 2" 100.00 415 100.00 100.00 0.00e+00 PDB 2QZK "Crystal Structure Of Human Beta Secretase Complexed With I21" 98.03 405 99.50 99.50 0.00e+00 PDB 2QZL "Crystal Structure Of Human Beta Secretase Complexed With Ixs" 98.03 411 99.50 99.50 0.00e+00 PDB 2VA5 "X-Ray Crystal Structure Of Beta Secretase Complexed With Compound 8c" 99.75 455 99.51 100.00 0.00e+00 PDB 2VA6 "X-Ray Crystal Structure Of Beta Secretase Complexed With Compound 24" 99.75 455 99.51 100.00 0.00e+00 PDB 2VA7 "X-Ray Crystal Structure Of Beta Secretase Complexed With Compound 27" 99.75 455 99.51 100.00 0.00e+00 PDB 2VIE "Human Bace-1 In Complex With N-((1s,2r)-1-Benzyl-2-Hydroxy- 3-((1,1,5-Trimethylhexyl)amino)propyl)-3-(Ethylamino)-5-(2- Oxopyrr" 96.31 392 98.98 98.98 0.00e+00 PDB 2VIJ "Human Bace-1 In Complex With 3-(1,1-Dioxidotetrahydro-2h-1, 2-Thiazin-2-Yl)-5-(Ethylamino)-N-((1s,2r)-2-Hydroxy-1-( Phenylmethy" 96.31 392 98.98 98.98 0.00e+00 PDB 2VIY "Human Bace-1 In Complex With N-((1s,2r)-3-(((1s)-2-( Cyclohexylamino)-1-Methyl-2-Oxoethyl)amino)-2-Hydroxy-1-( Phenylmethyl)pro" 96.31 392 98.98 98.98 0.00e+00 PDB 2VIZ "Human Bace-1 In Complex With N-((1s,2r)-3-(((1s)-2-( Cyclohexylamino)-1-methyl-2-oxoethyl)amino)-2-hydroxy-1-( Phenylmethyl)pro" 96.31 392 98.98 98.98 0.00e+00 PDB 2VJ6 "Human Bace-1 In Complex With N-((1s,2r)-3-(((1s)-2-( Cyclohexylamino)-1-Methyl-2-Oxoethyl)amino)-2-Hydroxy-1-( Phenylmethyl)pro" 96.31 392 98.98 98.98 0.00e+00 PDB 2VJ7 "Human Bace-1 In Complex With 3-(Ethylamino)-N-((1s,2r)-2- Hydroxy-1-(Phenylmethyl)-3-(((3-(Trifluoromethyl)phenyl) Methyl)amino" 96.31 392 98.98 98.98 0.00e+00 PDB 2VJ9 "Human Bace-1 In Complex With N-((1s,2r)-3-(Cyclohexylamino)- 2-Hydroxy-1-(Phenylmethyl)propyl)-3-(Ethylamino)-5-(2-Oxo- 1-Pyrro" 96.31 392 98.98 98.98 0.00e+00 PDB 2VKM "Crystal Structure Of Grl-8234 Bound To Bace (Beta-Secretase)" 95.58 389 100.00 100.00 0.00e+00 PDB 2VNM "Human Bace-1 In Complex With 3-(1,1-Dioxidotetrahydro-2h-1, 2-Thiazin-2-Yl)-5-(Ethylamino)-N-((1s,2r)-2-Hydroxy-1-( Phenylmethy" 96.31 392 98.98 98.98 0.00e+00 PDB 2VNN "Human Bace-1 In Complex With 7-Ethyl-N-((1s,2r)-2-Hydroxy-1- (Phenylmethyl)-3-(((3-(Trifluoromethyl)phenyl)methyl)amino) Propyl" 96.31 392 98.98 98.98 0.00e+00 PDB 2WEZ "Human Bace-1 In Complex With 1-Ethyl-N-((1s,2r)-2-Hydroxy-3- (((3-(Methyloxy)phenyl)methyl)amino)-1-(Phenylmethyl) Propyl)-4-(2" 96.31 392 98.98 98.98 0.00e+00 PDB 2WF0 "Human Bace-1 In Complex With 4-Ethyl-N-((1s,2r)-2-Hydroxy-1- (Phenylmethyl)-3-(((3-(Trifluoromethyl)phenyl)methyl)amino) Propyl" 96.31 392 98.98 98.98 0.00e+00 PDB 2WF1 "Human Bace-1 In Complex With 7-Ethyl-N-((1s,2r)-2-Hydroxy-3- (((3-(Methyloxy)phenyl(Methyl)amino)-1-(Phenylmethyl) Propyl)-1-Me" 96.31 392 98.98 98.98 0.00e+00 PDB 2WF2 "Human Bace-1 In Complex With 8-Ethyl-N-((1s,2r)-2-Hydroxy-3- (((3-(Methyloxy)phenyl)methyl)amino)-1-(Phenylmethyl) Propyl)-1-Me" 96.31 392 98.98 98.98 0.00e+00 PDB 2WF3 "Human Bace-1 In Complex With 6-(Ethylamino)-N-((1s,2r)-2- Hydroxy-3-(((3-(Methyloxy)phenyl)methyl)amino)-1-( Phenylmethyl)propy" 96.31 392 98.98 98.98 0.00e+00 PDB 2WF4 "Human Bace-1 In Complex With 6-Ethyl-1-Methyl-N-((1s)-2-Oxo- 1-(Phenylmethyl)-3-(Tetrahydro-2h-Pyran-4-Ylamino)propyl)- 1,3,4,6" 96.31 392 98.98 98.98 0.00e+00 PDB 2WJO "Human Bace (Beta Secretase) In Complex With Cyclohexanecarboxylic Acid (2-(2-Am Ino-6-Phenoxy-4h- Quinazolin-3-Yl)-2-Cyclohexyl" 97.54 412 100.00 100.00 0.00e+00 PDB 2XFI "Human Bace-1 In Complex With N-((1s,2r)-3-(((1s)-2-( Cyclohexylamino)-1-Methyl-2-Oxoethyl)amino)-2-Hydroxy-1-( Phenylmethyl)pro" 96.31 392 98.98 98.98 0.00e+00 PDB 2XFJ "Human Bace-1 In Complex With N-((1s,2r)-3-(((1s)-2-( Cyclohexylamino)-1-Methyl-2-Oxoethyl)amino)-2-Hydroxy-1-( Phenylmethyl)pro" 96.31 392 98.98 98.98 0.00e+00 PDB 2XFK "Human Bace-1 In Complex With N-((1s,2r)-3-(((1s)-2-( Cyclohexylamino)-1-Methyl-2-Oxoethyl)amino)-2-Hydroxy-1-( Phenylmethyl)pro" 96.31 392 98.98 98.98 0.00e+00 PDB 2ZDZ "X-Ray Structure Of Bace-1 In Complex With Compound 3.B.10" 100.00 415 100.00 100.00 0.00e+00 PDB 2ZE1 "X-Ray Structure Of Bace-1 In Complex With Compound 6g" 100.00 415 100.00 100.00 0.00e+00 PDB 2ZHR "Crystal Structure Of Bace1 In Complex With Om99-2 At Ph 5.0" 100.00 411 100.00 100.00 0.00e+00 PDB 2ZHS "Crystal Structure Of Bace1 At Ph 4.0" 100.00 411 100.00 100.00 0.00e+00 PDB 2ZHT "Crystal Structure Of Bace1 At Ph 4.5" 100.00 411 100.00 100.00 0.00e+00 PDB 2ZHU "Crystal Structure Of Bace1 At Ph 5.0" 100.00 411 100.00 100.00 0.00e+00 PDB 2ZHV "Crystal Structure Of Bace1 At Ph 7.0" 100.00 411 100.00 100.00 0.00e+00 PDB 2ZJH "Crystal Structure Of The Human Bace1 Catalytic Domain In Complex With N-(1-Benzyl-Piperidin-4-Yl)-4-Mercapto-Butyramide" 98.03 405 99.75 99.75 0.00e+00 PDB 2ZJI "Crystal Structure Of The Human Bace1 Catalytic Domain In Complex With N-[1-(2,6-Dimethoxy-Benzyl)-Piperidin-4-Yl]-4-Mercapto-Bu" 98.03 405 99.75 99.75 0.00e+00 PDB 2ZJJ "Crystal Structure Of The Human Bace1 Catalytic Domain In Complex With 4-(4-Fluoro-Benzyl)-Piperazine-2-Carboxylic Acid (2-Merca" 98.03 405 99.25 99.25 0.00e+00 PDB 2ZJK "Crystal Structure Of The Human Bace1 Catalytic Domain In Complex With 4-(4-Fluoro-Benzyl)-Piperazine-2-Carboxylic Acid(3-Mercap" 98.03 405 99.75 99.75 0.00e+00 PDB 2ZJL "Crystal Structure Of The Human Bace1 Catalytic Domain In Complex With N-[1-(5-Bromo-2,3-Dimethoxy-Benzyl)-Piperidin- 4-Yl]-4-Me" 98.03 405 99.75 99.75 0.00e+00 PDB 2ZJM "Crystal Structure Of The Human Bace1 Catalytic Domain In Complex With N-[1-(5-Chloro-2-Isopropoxy-3-Methoxy-Benzyl)- Piperidin-" 98.03 405 99.50 99.50 0.00e+00 PDB 2ZJN "Crystal Structure Of The Human Bace1 Catalytic Domain In Complex With N-[1-(5-Chloro-2-Isopropoxy-3-Methoxy-Benzyl)- Piperidin-" 98.03 405 100.00 100.00 0.00e+00 PDB 3BRA "Bace-1 Complexed With Compound 1" 100.00 409 99.75 99.75 0.00e+00 PDB 3BUF "Bace-1 Complexed With Compound 2" 100.00 409 99.75 99.75 0.00e+00 PDB 3BUG "Bace-1 Complexed With Compound 3" 100.00 409 99.75 99.75 0.00e+00 PDB 3BUH "Bace-1 Complexed With Compound 4" 100.00 409 99.75 99.75 0.00e+00 PDB 3CIB "Structure Of Bace Bound To Sch727596" 95.82 390 100.00 100.00 0.00e+00 PDB 3CIC "Structure Of Bace Bound To Sch709583" 95.82 390 100.00 100.00 0.00e+00 PDB 3CID "Structure Of Bace Bound To Sch726222" 95.82 390 100.00 100.00 0.00e+00 PDB 3CKP "Crystal Structure Of Bace-1 In Complex With Inhibitor" 100.00 412 99.51 100.00 0.00e+00 PDB 3CKR "Crystal Structure Of Bace-1 In Complex With Inhibitor" 100.00 412 99.51 100.00 0.00e+00 PDB 3DM6 "Beta-Secretase 1 Complexed With Statine-Based Inhibitor" 98.03 406 100.00 100.00 0.00e+00 PDB 3DUY "Crystal Structure Of Human Beta-Secretase In Complex With Nvp-Afj144" 98.28 402 100.00 100.00 0.00e+00 PDB 3DV1 "Crystal Structure Of Human Beta-Secretase In Complex With Nvp-Arv999" 98.28 402 100.00 100.00 0.00e+00 PDB 3DV5 "Crystal Structure Of Human Beta-Secretase In Complex With Nvp-Bav544" 98.28 402 100.00 100.00 0.00e+00 PDB 3EXO "Crystal Structure Of Bace1 Bound To Inhibitor" 100.00 413 99.51 99.51 0.00e+00 PDB 3FKT "Crystal Structure Of Human Beta Secretase Complexed With Spiropiperdine Iminohydantoin Inhibitor" 98.03 405 99.50 99.50 0.00e+00 PDB 3H0B "Discovery Of Aminoheterocycles As A Novel Beta-Secretase Inhibitor Class" 98.03 405 100.00 100.00 0.00e+00 PDB 3HVG "Structure Of Bace (Beta Secretase) In Complex With Ev0" 99.75 411 99.51 99.75 0.00e+00 PDB 3HW1 "Structure Of Bace (Beta Secretase) In Complex With Ligand Ev2" 99.75 411 99.51 99.75 0.00e+00 PDB 3I25 "Potent Beta-Secretase 1 Hydroxyethylene Inhibitor" 98.03 406 100.00 100.00 0.00e+00 PDB 3IGB "Bace-1 With Compound 3" 100.00 415 100.00 100.00 0.00e+00 PDB 3IN3 "Bace1 With Compound 30" 100.00 415 100.00 100.00 0.00e+00 PDB 3IN4 "Bace1 With Compound 38" 100.00 415 100.00 100.00 0.00e+00 PDB 3IND "Bace1 With The Aminohydantoin Compound 29" 100.00 415 100.00 100.00 0.00e+00 PDB 3INE "Bace1 With The Aminohydantoin Compound S-34" 100.00 415 100.00 100.00 0.00e+00 PDB 3INF "Bace1 With The Aminohydantoin Compound 37" 100.00 415 100.00 100.00 0.00e+00 PDB 3INH "Bace1 With The Aminohydantoin Compound R-58" 100.00 415 100.00 100.00 0.00e+00 PDB 3IVH "Design And Synthesis Of Potent Bace-1 Inhibitors With Cellular Activity: Structure-Activity Relationship Of P1 Substituents" 97.54 406 100.00 100.00 0.00e+00 PDB 3IVI "Design And Synthesis Of Potent Bace-1 Inhibitors With Cellular Activity: Structure-Activity Relationship Of P1 Substituents" 97.54 406 100.00 100.00 0.00e+00 PDB 3IXJ "Crystal Structure Of Beta-Secretase 1 In Complex With Selective Beta-Secretase 1 Inhibitor" 95.33 388 100.00 100.00 0.00e+00 PDB 3IXK "Potent Beta-Secretase 1 Inhibitor" 98.03 405 100.00 100.00 0.00e+00 PDB 3K5C "Human Bace-1 Complex With Nb-216" 98.28 402 100.00 100.00 0.00e+00 PDB 3K5D "Crystal Structure Of Bace-1 In Complex With Ahm178" 99.75 408 100.00 100.00 0.00e+00 PDB 3K5F "Human Bace-1 Complex With Ayh011" 98.28 402 100.00 100.00 0.00e+00 PDB 3K5G "Human Bace-1 Complex With Bjc060" 98.28 402 100.00 100.00 0.00e+00 PDB 3KMX "Structure Of Bace Bound To Sch346572" 97.05 395 100.00 100.00 0.00e+00 PDB 3KMY "Structure Of Bace Bound To Sch12472" 97.05 395 100.00 100.00 0.00e+00 PDB 3KN0 "Structure Of Bace Bound To Sch708236" 97.05 395 100.00 100.00 0.00e+00 PDB 3KYR "Bace-1 In Complex With A Norstatine Type Inhibitor" 98.03 405 100.00 100.00 0.00e+00 PDB 3L38 "Bace1 In Complex With The Aminopyridine Compound 44" 100.00 415 100.00 100.00 0.00e+00 PDB 3L3A "Bace-1 With The Aminopyridine Compound 32" 100.00 415 100.00 100.00 0.00e+00 PDB 3L58 "Structure Of Bace Bound To Sch589432" 100.00 414 100.00 100.00 0.00e+00 PDB 3L59 "Structure Of Bace Bound To Sch710413" 100.00 414 100.00 100.00 0.00e+00 PDB 3L5B "Structure Of Bace Bound To Sch713601" 100.00 414 100.00 100.00 0.00e+00 PDB 3L5C "Structure Of Bace Bound To Sch723871" 100.00 414 100.00 100.00 0.00e+00 PDB 3L5D "Structure Of Bace Bound To Sch723873" 100.00 414 100.00 100.00 0.00e+00 PDB 3L5E "Structure Of Bace Bound To Sch736062" 100.00 414 100.00 100.00 0.00e+00 PDB 3L5F "Structure Of Bace Bound To Sch736201" 100.00 414 100.00 100.00 0.00e+00 PDB 3LHG "Bace1 In Complex With The Aminohydantoin Compound 4g" 100.00 415 100.00 100.00 0.00e+00 PDB 3LNK "Structure Of Bace Bound To Sch743813" 97.05 395 100.00 100.00 0.00e+00 PDB 3LPI "Structure Of Bace Bound To Sch745132" 100.00 455 100.00 100.00 0.00e+00 PDB 3LPJ "Structure Of Bace Bound To Sch743641" 100.00 455 100.00 100.00 0.00e+00 PDB 3LPK "Structure Of Bace Bound To Sch747123" 100.00 455 100.00 100.00 0.00e+00 PDB 3MSJ "Structure Of Bace (Beta Secretase) In Complex With Inhibitor" 99.75 411 99.51 99.75 0.00e+00 PDB 3MSK "Fragment Based Discovery And Optimisation Of Bace-1 Inhibitors" 99.75 408 100.00 100.00 0.00e+00 PDB 3MSL "Fragment Based Discovery And Optimisation Of Bace-1 Inhibitors" 99.75 408 100.00 100.00 0.00e+00 PDB 3N4L "Bace-1 In Complex With Eln380842" 97.54 406 100.00 100.00 0.00e+00 PDB 3NSH "Bace-1 In Complex With Eln475957" 97.54 406 100.00 100.00 0.00e+00 PDB 3OHF "Crystal Structure Of Beta-Site App-Cleaving Enzyme 1 (Bace-Wt) Complex With Bms-655295 Aka N~3~-((1s,2r)-1- Benzyl-2-Hydroxy-3-" 100.00 455 100.00 100.00 0.00e+00 PDB 3OHH "Crystal Structure Of Beta-Site App-Cleaving Enzyme 1 (Bace-Wt) Complex With Bms-681889 Aka N~1~-Butyl-5-Cyano- N~3~-((1s,2r)-1-" 100.00 455 100.00 100.00 0.00e+00 PDB 3OOZ "Bace1 In Complex With The Aminohydantoin Compound 102" 100.00 415 100.00 100.00 0.00e+00 PDB 3PI5 "Crystal Structure Of Human Beta Secretase In Complex With Bfg356" 98.28 402 100.00 100.00 0.00e+00 PDB 3QBH "Structure Based Design, Synthesis And Sar Of Cyclic Hydroxyethylamine (Hea) Bace-1 Inhibitors" 98.28 402 100.00 100.00 0.00e+00 PDB 3QI1 "Design And Synthesis Of Hydroxyethylamine (hea) Bace-1 Inhibitors: Prime Side Chromane-containing Inhibitors" 99.75 408 99.51 99.51 0.00e+00 PDB 3R1G "Structure Basis Of Allosteric Inhibition Of Bace1 By An Exosite- Binding Antibody" 98.03 402 99.75 99.75 0.00e+00 PDB 3R2F "Crystal Structure Of Beta-site App-cleaving Enzyme 1 (bace-wt) Complex With Bms-693391 Aka (2s)-2-((3r)-3-acetamido-3-isobutyl-" 100.00 455 100.00 100.00 0.00e+00 PDB 3RSV "Structure Of Bace-1 (Beta-Secretase) In Complex With (R)-3-(2-Amino-6- O-Tolylquinolin-3-Yl)-N-((R)-2,2-Dimethyltetrahydro-2h-P" 99.75 411 99.51 100.00 0.00e+00 PDB 3RSX "Structure Of Bace-1 (Beta-Secretase) In Complex With 6-(Thiophen-3- Yl)quinolin-2-Amine" 99.75 411 99.51 100.00 0.00e+00 PDB 3RTH "Structure Of Bace-1 (Beta-Secretase) In Complex With 6-(2-(3,3- Dimethylbut-1-Ynyl)phenyl)quinolin-2-Amine" 99.75 411 99.51 100.00 0.00e+00 PDB 3RTM "Structure Of Bace-1 (Beta-Secretase) In Complex With 3-(2- Aminoquinolin-3-Yl)-N-Cyclohexyl-N-Methylpropanamide" 99.75 411 99.51 100.00 0.00e+00 PDB 3RTN "Structure Of Bace-1 (Beta-Secretase) In Complex With 3-(2-Amino-6-O- Tolylquinolin-3-Yl)-N-Cyclohexylpropanamide" 99.75 411 99.51 100.00 0.00e+00 PDB 3RU1 "Structure Of Bace-1 (Beta-Secretase) In Complex With 3-(2- Aminoquinolin-3-Yl)-N-(Cyclohexylmethyl)propanamide" 99.75 411 99.51 100.00 0.00e+00 PDB 3RVI "Structure Of Bace-1 (Beta-Secretase) In Complex With 2-((2-Amino-6-O- Tolylquinolin-3-Yl)methyl)-N-(Cyclohexylmethyl)pentanamid" 99.75 411 99.51 100.00 0.00e+00 PDB 3S2O "Fragment Based Discovery And Optimisation Of Bace-1 Inhibitors" 99.75 408 100.00 100.00 0.00e+00 PDB 3S7L "Pyrazolyl And Thienyl Aminohydantoins As Potent Bace1 Inhibitors" 100.00 415 100.00 100.00 0.00e+00 PDB 3S7M "Pyrazolyl And Thienyl Aminohydantoins As Potent Bace1 Inhibitors" 100.00 415 100.00 100.00 0.00e+00 PDB 3SKF "Crystal Structure Of Beta-Site App-Cleaving Enzyme 1 (Bace-Wt) Complex With (2s)-2-((3s)-3-(Acetylamino)-3-(Butan-2-Yl)-2-Oxopy" 100.00 455 100.00 100.00 0.00e+00 PDB 3SKG "Crystal Structure Of Beta-Site App-Cleaving Enzyme 1 (Bace-Wt) Complex With (2s)-2-((3r)-3-Acetamido-3-Isobutyl-2-Oxo-1-Pyrroli" 100.00 455 100.00 100.00 0.00e+00 PDB 3TPJ "Apo Structure Of Bace1" 100.00 433 99.51 99.51 0.00e+00 PDB 3TPL "Apo Structure Of Bace1" 100.00 433 99.51 99.51 0.00e+00 PDB 3TPP "Crystal Structure Of Bace1 Complexed With An Inhibitor" 100.00 433 99.51 99.51 0.00e+00 PDB 3TPR "Crystal Structure Of Bace1 Complexed With An Inhibitor" 100.00 433 100.00 100.00 0.00e+00 PDB 3U6A "Rational Design And Synthesis Of Aminopiperazinones As Beta Secretase (bace) Inhibitors" 95.58 390 100.00 100.00 0.00e+00 PDB 3UDH "Crystal Structure Of Bace With Compound 1" 97.30 404 100.00 100.00 0.00e+00 PDB 3UDJ "Crystal Structure Of Bace With Compound 5" 97.30 404 100.00 100.00 0.00e+00 PDB 3UDK "Crystal Structure Of Bace With Compound 6" 97.30 404 100.00 100.00 0.00e+00 PDB 3UDM "Crystal Structure Of Bace With Compound 8" 97.30 404 100.00 100.00 0.00e+00 PDB 3UDN "Crystal Structure Of Bace With Compound 9" 97.30 404 100.00 100.00 0.00e+00 PDB 3UDP "Crystal Structure Of Bace With Compound 12" 97.30 404 100.00 100.00 0.00e+00 PDB 3UDQ "Crystal Structure Of Bace With Compound 13" 97.30 404 100.00 100.00 0.00e+00 PDB 3UDR "Crystal Structure Of Bace With Compound 14" 97.30 404 100.00 100.00 0.00e+00 PDB 3UDY "Crystal Structure Of Bace With Compound 11" 97.30 404 100.00 100.00 0.00e+00 PDB 3UFL "Discovery Of Pyrrolidine-Based B-Secretase Inhibitors: Lead Advancement Through Conformational Design For Maintenance Of Ligand" 95.58 389 100.00 100.00 0.00e+00 PDB 3UQP "Crystal Structure Of Bace1 With Its Inhibitor" 100.00 433 99.51 99.51 0.00e+00 PDB 3UQR "Crystal Structure Of Bace1 With Its Inhibitor" 100.00 433 100.00 100.00 0.00e+00 PDB 3UQU "Crystal Structure Of Bace1 With Its Inhibitor" 100.00 433 99.51 99.51 0.00e+00 PDB 3UQW "Crystal Structure Of Bace1 With Its Inhibitor" 100.00 433 99.51 99.51 0.00e+00 PDB 3UQX "Crystal Structure Of Bace1 With Its Inhibitor" 100.00 433 99.51 99.51 0.00e+00 PDB 3VEU "Crystal Structure Of Human Beta Secretase In Complex With Nvp-Avi326" 98.28 402 100.00 100.00 0.00e+00 PDB 3VF3 "Crystal Structure Of Human Beta Secretase In Complex With Nvp-Bqq711" 98.28 402 100.00 100.00 0.00e+00 PDB 3VG1 "Crystal Structure Of Human Beta Secretase In Complex With Nvp-Bur436, Derived From A Soaking Experiment" 98.28 402 100.00 100.00 0.00e+00 PDB 3VV6 "Crystal Structure Of Beta Secetase In Complex With 2-amino-3-methyl-6- ((1s, 2r)-2-phenylcyclopropyl)pyrimidin-4(3h)-one" 100.00 416 100.00 100.00 0.00e+00 PDB 3VV7 "Crystal Structure Of Beta Secetase In Complex With 2-amino-6-((1s,2r)- 2-(3'-methoxybiphenyl-3-yl)cyclopropyl)-3-methylpyrimidi" 100.00 416 100.00 100.00 0.00e+00 PDB 3VV8 "Crystal Structure Of Beta Secetase In Complex With 2-amino-3-methyl-6- ((1s,2r)-2-(3'-methylbiphenyl-4-yl)cyclopropyl)pyrimidin" 100.00 416 100.00 100.00 0.00e+00 PDB 3WB4 "Crystal Structure Of Beta Secetase In Complex With 2-amino-3,6- Dimethyl-6-(2-phenylethyl)-3,4,5,6-tetrahydropyrimidin-4-one" 100.00 416 100.00 100.00 0.00e+00 PDB 3WB5 "Crystal Structure Of Beta Secetase In Complex With (6s)-2-amino-3,6- Dimethyl-6-[(1r,2r)-2-phenylcyclopropyl]-3,4,5,6-tetrahydr" 100.00 416 100.00 100.00 0.00e+00 PDB 3ZMG "Crystal Structure Of Bace-1 In Complex With Chemical Ligand" 100.00 409 99.75 99.75 0.00e+00 PDB 3ZOV "Crystal Structure Of Bace-1 In Complex With Chemical Ligand" 100.00 409 99.75 99.75 0.00e+00 PDB 4ACU "Aminoimidazoles As Bace-1 Inhibitors. X-Ray Crystal Structure Of Beta Secretase Complexed With Compound 14" 99.75 411 99.51 100.00 0.00e+00 PDB 4ACX "Aminoimidazoles As Bace-1 Inhibitors. X-Ray Crystal Structure Of Beta Secretase Complexed With Compound 23" 99.75 411 99.51 100.00 0.00e+00 PDB 4AZY "Design And Synthesis Of Bace1 Inhibitors With In Vivo Brain Reduction Of Beta-Amyloid Peptides (Compound 10)" 99.75 411 99.51 100.00 0.00e+00 PDB 4B00 "Design And Synthesis Of Bace1 Inhibitors With In Vivo Brain Reduction Of Beta-Amyloid Peptides (Compound (R)-41)" 99.75 411 99.51 100.00 0.00e+00 PDB 4B05 "Preclinical Characterization Of Azd3839, A Novel Clinical Candidate Bace1 Inhibitor For The Treatment Of Alzheimer Disease" 99.75 411 99.51 100.00 0.00e+00 PDB 4B0Q "Lead Generation Of Bace1 Inhibitors By Coupling Non-amidine New Warheads To A Known Binding Scaffold" 94.35 384 100.00 100.00 0.00e+00 PDB 4B1D "New Aminoimidazoles As Bace-1 Inhibitors: From Rational Design To Ab-Lowering In Brain" 95.33 388 100.00 100.00 0.00e+00 PDB 4B1E "New Aminoimidazoles As Bace-1 Inhibitors: From Rational Design To Ab-Lowering In Brain" 95.33 388 100.00 100.00 0.00e+00 PDB 4B70 "Aminoimidazoles As Bace-1 Inhibitors: From De Novo Design To Ab-lowering In Brain" 94.59 385 100.00 100.00 0.00e+00 PDB 4B72 "Aminoimidazoles As Bace-1 Inhibitors: From De Novo Design To Ab-lowering In Brain" 95.33 388 100.00 100.00 0.00e+00 PDB 4B77 "Aminoimidazoles As Bace-1 Inhibitors: From De Novo Design To Ab-lowering In Brain" 95.33 388 100.00 100.00 0.00e+00 PDB 4B78 "Aminoimidazoles As Bace-1 Inhibitors: From De Novo Design To Ab-lowering In Brain" 94.35 384 100.00 100.00 0.00e+00 PDB 4BEK "Crystal Structure Of Bace-1 In Complex With Chemical Ligand" 100.00 409 99.75 99.75 0.00e+00 PDB 4BFD "Crystal Structure Of Bace-1 In Complex With Chemical Ligand" 100.00 409 99.75 99.75 0.00e+00 PDB 4D83 "Crystal Structure Of Human Beta Secretase In Complex With Nvp-Bur436, Derived From A Co-Crystallization Experiment" 98.28 402 100.00 100.00 0.00e+00 PDB 4D85 "Crystal Structure Of Human Beta Secretase In Complex With Nvp-Bvi151" 99.75 408 100.00 100.00 0.00e+00 PDB 4D88 "Crystal Structure Of Human Beta Secretase In Complex With Nvp-Bxq490" 98.28 402 100.00 100.00 0.00e+00 PDB 4D89 "Crystal Structure Of Human Beta Secretase In Complex With Nvp-Bxd552, Derived From A Soaking Experiment" 98.28 402 100.00 100.00 0.00e+00 PDB 4D8C "Crystal Structure Of Human Beta Secretase In Complex With Nvp-Bxd552, Derived From A Co-Crystallization Experiment" 98.28 402 100.00 100.00 0.00e+00 PDB 4DH6 "Structure Of Bace-1 (beta-secretase) In Complex With (2r)-n-((2s,3r)- 1-(benzo[d][1,3]dioxol-5-yl)-3-hydroxy-4-((s)-6'-neopenty" 99.75 411 99.51 100.00 0.00e+00 PDB 4DI2 "Crystal Structure Of Bace1 In Complex With Hydroxyethylamine Inhibitor 37" 99.75 411 99.51 100.00 0.00e+00 PDB 4DJU "Structure Of Bace Bound To 2-Imino-3-Methyl-5,5-Diphenylimidazolidin- 4-One" 100.00 414 100.00 100.00 0.00e+00 PDB 4DJV "Structure Of Bace Bound To 2-Imino-5-(3'-Methoxy-[1,1'-Biphenyl]-3- Yl)-3-Methyl-5-Phenylimidazolidin-4-One" 100.00 414 100.00 100.00 0.00e+00 PDB 4DJW "Structure Of Bace Bound To 2-Imino-3-Methyl-5-Phenyl-5-(3-(Pyridin-3- Yl)phenyl)imidazolidin-4-One" 100.00 414 100.00 100.00 0.00e+00 PDB 4DJX "Structure Of Bace Bound To 5-(3-(5-Chloropyridin-3-Yl)phenyl)-5- Cyclopropyl-2-Imino-3-Methylimidazolidin-4-One" 100.00 414 100.00 100.00 0.00e+00 PDB 4DJY "Structure Of Bace Bound To (R)-5-Cyclopropyl-2-Imino-3-Methyl-5-(3-(5- (Prop-1-Yn-1-Yl)pyridin-3-Yl)phenyl)imidazolidin-4-One" 100.00 414 100.00 100.00 0.00e+00 PDB 4DPF "Bace-1 In Complex With A Hea-Macrocyclic Type Inhibitor" 95.82 391 100.00 100.00 0.00e+00 PDB 4DPI "Bace-1 In Complex With Hea-Macrocyclic Inhibitor, Mv078512" 95.82 391 100.00 100.00 0.00e+00 PDB 4DUS "Structure Of Bace-1 (beta-secretase) In Complex With N-((2s,3r)-1-(4- Fluorophenyl)-3-hydroxy-4-((6'-neopentyl-3',4'- Dihydrosp" 99.75 411 99.51 100.00 0.00e+00 PDB 4DV9 "Crystal Structure Of Bace1 With Its Inhibitor" 100.00 433 99.51 99.51 0.00e+00 PDB 4DVF "Crystal Structure Of Bace1 With Its Inhibitor" 100.00 433 99.51 99.51 0.00e+00 PDB 4EWO "Design And Synthesis Of Potent Hydroxyethylamine (Hea) Bace-1 Inhibitors" 94.84 386 100.00 100.00 0.00e+00 PDB 4EXG "Design And Synthesis Of Potent Hydroxyethylamine (Hea) Bace-1 Inhibitors" 94.84 386 100.00 100.00 0.00e+00 PDB 4FCO "Crystal Structure Of Bace1 With Its Inhibitor" 100.00 433 99.51 99.51 0.00e+00 PDB 4FGX "Crystal Structure Of Bace1 With Novel Inhibitor" 100.00 433 99.51 99.51 0.00e+00 PDB 4FM7 "Crystal Structure Of Bace With Compound 14g" 97.30 404 100.00 100.00 0.00e+00 PDB 4FM8 "Crystal Structure Of Bace With Compound 12a" 97.30 404 100.00 100.00 0.00e+00 PDB 4FRI "Crystal Structure Of Bace1 In Complex With Biarylspiro Aminooxazoline 6" 99.75 411 99.51 100.00 0.00e+00 PDB 4FRJ "Crystal Structure Of Bace1 In Complex With Aminooxazoline Xanthene 9l" 99.75 411 99.51 100.00 0.00e+00 PDB 4FRK "Crystal Structure Of Bace1 In Complex With Aminooxazoline Xanthene 11a" 99.75 411 99.51 100.00 0.00e+00 PDB 4FRS "Structure Of Bace In Complex With (s)-4-(3-chloro-5-(5-(prop-1-yn-1- Yl)pyridin-3-yl)thiophen-2-yl)-1,4-dimethyl-6-oxotetrahydr" 97.05 395 100.00 100.00 0.00e+00 PDB 4FS4 "Structure Of Bace Bound To (s)-4-(3'-methoxy-[1,1'-biphenyl]-3-yl)-1, 4-dimethyl-6-oxotetrahydropyrimidin-2(1h)-iminium" 95.82 390 100.00 100.00 0.00e+00 PDB 4FSE "Crystal Structure Of Beta-site App-cleaving Enzyme 1 (bace-wt) Complex With N-(n-(4-amino-3,5- Dichlorobenzyl)carbamimidoyl)-3-" 100.00 455 100.00 100.00 0.00e+00 PDB 4FSL "Crystal Structure Of Beta-site App-cleaving Enzyme 1 (bace-db-mut) Complex With N-(n-(4- Acetamido-3-chloro-5-methylbenzyl) Car" 100.00 412 99.51 100.00 0.00e+00 PDB 4GID "Structure Of Beta-secretase Complexed With Inhibitor" 95.33 388 100.00 100.00 0.00e+00 PDB 4GMI "Bace-1 In Complex With Hea-type Macrocyclic Inhibitor, Mv078571" 95.82 391 100.00 100.00 0.00e+00 PDB 4H1E "Structure Of Bace-1 Bound To (7ar)-6-Benzoyl-7a-(4-(3-Cyanophenyl) Thiophen-2-Yl)-3-Methyl-4-Oxohexahydro-1h-Pyrrolo[3,4-D]pyri" 100.00 414 100.00 100.00 0.00e+00 PDB 4H3F "Structure Of Bace Bound To 3-(5-((7ar)-2-Imino-6-(6-Methoxypyridin-2- Yl)-3-Methyl-4-Oxooctahydro-1h-Pyrrolo[3,4-D]pyrimidin-7a" 100.00 414 100.00 100.00 0.00e+00 PDB 4H3G "Structure Of Bace Bound To 2-((7ar)-7a-(4-(3-Cyanophenyl)thiophen-2- Yl)-2-Imino-3-Methyl-4-Oxohexahydro-1h-Pyrrolo[3,4-D]pyrim" 100.00 414 100.00 100.00 0.00e+00 PDB 4H3I "Structure Of Bace Bound To 3-(5-((7ar)-2-Imino-6-(3-Methoxypyridin-2- Yl)-3-Methyl-4-Oxooctahydro-1h-Pyrrolo[3,4-D]pyrimidin-7a" 100.00 414 100.00 100.00 0.00e+00 PDB 4H3J "Structure Of Bace Bound To 2-Fluoro-5-(5-(2-Imino-3-Methyl-4-Oxo-6- Phenyloctahydro-1h-Pyrrolo[3,4-D]pyrimidin-7a-Yl)thiophen-2" 100.00 414 100.00 100.00 0.00e+00 PDB 4HA5 "Structure Of Bace Bound To (S)-3-(5-(2-Imino-1,4-Dimethyl-6- Oxohexahydropyrimidin-4-Yl)thiophen-3-Yl)benzonitrile" 100.00 414 100.00 100.00 0.00e+00 PDB 4HZT "Structure-based Design Of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage The Catalytic Aspartates" 97.54 406 100.00 100.00 0.00e+00 PDB 4I0D "Design And Synthesis Of Thiophene Dihydroisoquinolins As Novel Bace-1 Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4I0E "Design And Synthesis Of Thiophene Dihydroisoquinolins As Novel Bace-1 Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4I0F "Design And Synthesis Of Thiophene Dihydroisoquinolins As Novel Bace-1 Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4I0G "Design And Synthesis Of Thiophene Dihydroisoquinolins As Novel Bace-1 Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4I0H "Spr And Structural Analysis Yield Insight Towards Mechanism Of Inhibition Of Bace Inhibitors." 97.54 406 100.00 100.00 0.00e+00 PDB 4I0I "Spr And Structural Analysis Yield Insight Towards Mechanism Of Inhibition Of Bace Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4I0J "Spr And Structural Analysis Yield Insight Towards Mechanism Of Inhibition Of Bace Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4I0Z "Structure-based Design Of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage The Catalytic Aspartates" 97.54 406 100.00 100.00 0.00e+00 PDB 4I10 "Structure-based Design Of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage The Catalytic Aspartates" 97.54 406 100.00 100.00 0.00e+00 PDB 4I11 "Structure-based Design Of Novel Dihydroisoquinoline Bace-1 Inhibitors That Do Not Engage The Catalytic Aspartates." 97.54 406 100.00 100.00 0.00e+00 PDB 4I12 "Design And Synthesis Of Thiophene Dihydroisoquinolins As Novel Bace-1 Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4I1C "Design And Synthesis Of Thiophene Dihydroisoquinolins As Novel Bace-1 Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4IVS "Crystal Structure Of Bace1 With Its Inhibitor" 100.00 433 99.51 99.51 0.00e+00 PDB 4IVT "Crystal Structure Of Bace1 With Its Inhibitor" 100.00 433 99.51 99.51 0.00e+00 PDB 4J0P "Crystal Structure Of Bace-1 In Complex With 5-cyano-pyridine-2- Carboxylic Acid [3-((s)-2-amino-4-methyl-5,6-dihydro-4h-[1,3]ox" 100.00 409 99.75 99.75 0.00e+00 PDB 4J0T "Crystal Structure Of Bace-1 In Complex With 5-ethoxy-pyridine-2- Carboxylic Acid [3-((r)-2-amino-5,5-difluoro-4-methyl-5,6-dihy" 100.00 409 99.75 99.75 0.00e+00 PDB 4J0V "Crystal Structure Of Bace-1 In Complex With 5-cyano-pyridine-2- Carboxylic Acid [3-((4r,5r)-2-amino-5-fluoro-4-methyl-5,6-dihyd" 100.00 409 99.75 99.75 0.00e+00 PDB 4J0Y "Crystal Structure Of Bace-1 In Complex With 5-cyano-pyridine-2- Carboxylic Acid [3-((4r,5s)-2-amino-5-fluoro-4-methyl-5,6-dihyd" 100.00 409 99.75 99.75 0.00e+00 PDB 4J0Z "Crystal Structure Of Bace-1 In Complex With 5-cyano-pyridine-2- Carboxylic Acid [3-((4s,5r)-2-amino-5-fluoro-4-fluoromethyl-5,6" 100.00 409 99.75 99.75 0.00e+00 PDB 4J17 "Crystal Structure Of Bace-1 In Complex With 5-cyano-pyridine-2- Carboxylic Acid [3-((s)-2-amino-4-difluoromethyl-5,6-dihydro-4h" 100.00 409 99.75 99.75 0.00e+00 PDB 4J1C "Crystal Structure Of Bace-1 In Complex With 5-cyano-pyridine-2- Carboxylic Acid [3-((s)-2-amino-5,5-difluoro-4-fluoromethyl-5,6" 100.00 409 99.75 99.75 0.00e+00 PDB 4J1E "Crystal Structure Of Bace-1 In Complex With 5-cyano-pyridine-2- Carboxylic Acid [3-((4s,6s)-2-amino-4-fluoromethyl-6-trifluorom" 100.00 409 99.75 99.75 0.00e+00 PDB 4J1F "Crystal Structure Of Bace-1 In Complex With 5-cyano-pyridine-2- Carboxylic Acid [3-((4s,6s)-2-amino-4-methyl-6-trifluoromethyl-" 100.00 409 99.75 99.75 0.00e+00 PDB 4J1H "Crystal Structure Of Bace-1 In Complex With 5-cyano-pyridine-2- Carboxylic Acid [3-((4s,6r)-2-amino-4-methyl-6-trifluoromethyl-" 100.00 409 99.75 99.75 0.00e+00 PDB 4J1I "Crystal Structure Of Bace-1 In Complex With 5-cyano-pyridine-2- Carboxylic Acid [3-((4r,5r,6r)-2-amino-5-fluoro-4-methyl-6- Tri" 100.00 409 99.75 99.75 0.00e+00 PDB 4J1K "Crystal Structure Of Bace-1 In Complex With 5-cyano-pyridine-2- Carboxylic Acid [3-((4r,5r,6s)-2-amino-5-fluoro-4-methyl-6- Tri" 100.00 409 99.75 99.75 0.00e+00 PDB 4JOO "Spirocyclic Beta-site Amyloid Precursor Protein Cleaving Enzyme 1 (bace1) Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4JP9 "Spirocyclic Beta-site Amyloid Precursor Protein Cleaving Enzyme 1 (bace1) Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4JPC "Spirocyclic Beta-site Amyloid Precursor Protein Cleaving Enzyme 1 (bace1) Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4JPE "Spirocyclic Beta-site Amyloid Precursor Protein Cleaving Enzyme 1 (bace1) Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4K8S "Hydroxyethylamine-based Inhibitors Of Bace1: P1-p3 Macrocyclization Can Improve Potency, Selectivity, And Cell Activity" 95.33 388 100.00 100.00 0.00e+00 PDB 4K9H "Bace-1 Inhibitor Complex" 95.33 388 100.00 100.00 0.00e+00 PDB 4KE0 "Crystal Structure Of Bace1 In Complex With Hydroxyethylamine- Macrocyclic Inhibitor 13" 99.75 411 99.51 100.00 0.00e+00 PDB 4KE1 "Crystal Structure Of Bace1 In Complex With Hydroxyethylamine- Macrocyclic Inhibitor 19" 99.75 411 99.51 100.00 0.00e+00 PDB 4L7G "Diethylaminosulfur Trifluoride-mediated Intramolecular Cyclization Of 2-hydroxy-benzylureas To Fused Bicyclic Aminooxazoline Co" 98.03 409 99.75 99.75 0.00e+00 PDB 4L7H "Diethylaminosulfur Trifluoride-mediated Intramolecular Cyclization Of 2-hydroxy-benzylureas To Fused Bicyclic Aminooxazoline Co" 98.03 409 99.75 99.75 0.00e+00 PDB 4L7J "Diethylaminosulfur Trifluoride-mediated Intramolecular Cyclization Of 2-hydroxy-benzylureas To Fused Bicyclic Aminooxazoline Co" 98.03 409 99.75 99.75 0.00e+00 PDB 4LC7 "Aminooxazoline Inhibitor Of Bace-1" 97.54 406 100.00 100.00 0.00e+00 PDB 4LXA "Crystal Structure Of Human Beta Secretase In Complex With Compound 11a" 98.28 402 100.00 100.00 0.00e+00 PDB 4LXK "Crystal Structure Of Human Beta Secretase In Complex With Compound 11d" 98.28 402 100.00 100.00 0.00e+00 PDB 4LXM "Crystal Structure Of Human Beta Secretase In Complex With Compound 12a" 98.28 402 100.00 100.00 0.00e+00 PDB 4N00 "Discovery Of 7-thp Chromans: Bace1 Inhibitors That Reduce A-beta In The Cns" 97.54 406 100.00 100.00 0.00e+00 PDB 4PZW "Synthesis, Characterization And Pk/pd Studies Of A Series Of Spirocyclic Pyranochromene Bace1 Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4PZX "Synthesis, Characterization And Pk/pd Studies Of A Series Of Spirocyclic Pyranochromene Bace1 Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4R5N "8-tetrahydropyran-2-yl Chromans: Highly Selective Beta-site Amyloid Precursor Protein Cleaving Enzyme 1 (bace1) Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4R8Y "Bace-1 In Complex With (r)-4-(2-cyclohexylethyl)-4-(((r)-1-(2- Cyclopentylacetyl)pyrrolidin-3-yl)methyl)-1-methyl-5-oxoimidazol" 100.00 414 100.00 100.00 0.00e+00 PDB 4R91 "Bace-1 In Complex With (r)-4-(2-cyclohexylethyl)-4-(((1s,3r)-3- (cyclopentylamino)cyclohexyl)methyl)-1-methyl-5-oxoimidazolidin" 100.00 414 100.00 100.00 0.00e+00 PDB 4R92 "Bace-1 In Complex With (r)-4-(2-cyclohexylethyl)-4-(((1s,3r)-3- (isonicotinamido)cyclohexyl)methyl)-1-methyl-5-oxoimidazolidin-" 100.00 414 100.00 100.00 0.00e+00 PDB 4R93 "Bace-1 In Complex With (r)-4-(2-cyclohexylethyl)-1-methyl-5-oxo-4- (((1s,3r)-3-(3-phenylureido)cyclohexyl)methyl)imidazolidin-2" 100.00 414 100.00 100.00 0.00e+00 PDB 4R95 "Bace-1 In Complex With 2-(((1r,3s)-3-(((r)-4-(2-cyclohexylethyl)-2- Iminio-1-methyl-5-oxoimidazolidin-4-yl)methyl)cyclohexyl)am" 100.00 414 100.00 100.00 0.00e+00 PDB 4RRN "8-tetrahydropyran-2-yl Chromans: Highly Selective Beta-site Amyloid Precursor Protein Cleaving Enzyme 1 (bace1) Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4RRO "8-tetrahydropyran-2-yl Chromans: Highly Selective Beta-site Amyloid Precursor Protein Cleaving Enzyme 1 (bace1) Inhibitors" 97.54 406 100.00 100.00 0.00e+00 PDB 4RRS "8-tetrahydropyran-2-yl Chromans: Highly Selective Beta-site Amyloid Precursor Protein Cleaving Enzyme 1 (bace1) Inhibitors" 97.54 406 100.00 100.00 0.00e+00 DBJ BAA86463 "KIAA1149 protein [Homo sapiens]" 100.00 532 100.00 100.00 0.00e+00 DBJ BAB29317 "unnamed protein product [Mus musculus]" 54.05 267 99.09 99.55 1.56e-158 DBJ BAB29370 "unnamed protein product [Mus musculus]" 100.00 501 98.28 99.26 0.00e+00 DBJ BAC28156 "unnamed protein product [Mus musculus]" 100.00 501 98.28 99.26 0.00e+00 DBJ BAC30889 "unnamed protein product [Mus musculus]" 100.00 501 98.28 99.26 0.00e+00 GB AAF04142 "beta-site APP cleaving enzyme [Homo sapiens]" 100.00 501 100.00 100.00 0.00e+00 GB AAF04143 "beta-site APP cleaving enzyme [Mus musculus]" 100.00 501 98.28 99.26 0.00e+00 GB AAF04144 "beta-site APP cleaving enzyme [Rattus norvegicus]" 100.00 501 98.28 99.26 0.00e+00 GB AAF13715 "memapsin 2 [Homo sapiens]" 100.00 488 100.00 100.00 0.00e+00 GB AAF17079 "aspartyl protease 2 [Homo sapiens]" 100.00 501 100.00 100.00 0.00e+00 REF NP_001039996 "beta-secretase 1 precursor [Bos taurus]" 100.00 501 98.77 99.02 0.00e+00 REF NP_001193977 "beta-secretase 1 isoform E [Homo sapiens]" 82.80 401 100.00 100.00 0.00e+00 REF NP_001247857 "beta-secretase 1 precursor [Macaca mulatta]" 100.00 501 99.75 99.75 0.00e+00 REF NP_001276783 "beta-site APP-cleaving enzyme 1 precursor [Sus scrofa]" 100.00 506 98.77 99.26 0.00e+00 REF NP_035922 "beta-secretase 1 isoform 1 precursor [Mus musculus]" 100.00 501 98.28 99.26 0.00e+00 SP P56817 "RecName: Full=Beta-secretase 1; AltName: Full=Aspartyl protease 2; Short=ASP2; Short=Asp 2; AltName: Full=Beta-site amyloid pre" 100.00 501 100.00 100.00 0.00e+00 SP P56818 "RecName: Full=Beta-secretase 1; AltName: Full=Aspartyl protease 2; Short=ASP2; Short=Asp 2; AltName: Full=Beta-site amyloid pre" 100.00 501 98.28 99.26 0.00e+00 SP P56819 "RecName: Full=Beta-secretase 1; AltName: Full=Aspartyl protease 2; Short=ASP2; Short=Asp 2; AltName: Full=Beta-site amyloid pre" 100.00 501 98.28 99.26 0.00e+00 SP Q2HJ40 "RecName: Full=Beta-secretase 1; AltName: Full=Beta-site amyloid precursor protein cleaving enzyme 1; Short=Beta-site APP cleavi" 100.00 501 98.77 99.02 0.00e+00 TPG DAA22394 "TPA: beta-secretase 1 precursor [Bos taurus]" 100.00 501 98.77 99.02 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $BACE1_monomer Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $BACE1_monomer 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $BACE1_monomer 0.9 mM '[U-2H; U-15N; U-13C]' stop_ save_ ############################ # Computer software used # ############################ save_NMRpipe _Saveframe_category software _Name NMRpipe _Version . loop_ _Task 'data processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TROSY' _Sample_label . save_ save_3D-TROSY-HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TROSY-HNCACB _Sample_label . save_ save_3D-TROSY-HNCACO_3 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TROSY-HNCACO _Sample_label . save_ save_3D-TROSY-HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TROSY-HNCA _Sample_label . save_ save_3D-TROSY-HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TROSY-HNCO _Sample_label . save_ save_3D-TROSY-HNCOCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TROSY-HNCOCA _Sample_label . save_ save_3D-TROSY-CT-CACB(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TROSY-CT-CACB(CO)NH _Sample_label . save_ save_4D_TROSY-HNCOCA_8 _Saveframe_category NMR_applied_experiment _Experiment_name '4D TROSY-HNCOCA' _Sample_label . save_ save_4D_TROSY-HNCACO_9 _Saveframe_category NMR_applied_experiment _Experiment_name '4D TROSY-HNCACO' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TROSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TROSY-HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TROSY-HNCACO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TROSY-HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TROSY-HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TROSY-HNCOCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-TROSY-CT-CACB(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '4D TROSY-HNCOCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '4D TROSY-HNCACO' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condi-1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.1 na temperature 298 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details ; Chemical shift reference was calibrated based on the proton chemical shift of an external standard. ; loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS C 13 'methyl protons' ppm 0.0 external indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.0 external indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N TROSY' 3D-TROSY-HNCACB 3D-TROSY-HNCACO 3D-TROSY-HNCA 3D-TROSY-HNCO 3D-TROSY-HNCOCA 3D-TROSY-CT-CACB(CO)NH '4D TROSY-HNCOCA' '4D TROSY-HNCACO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condi-1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'BACE1 monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 GLU N N 121.007 0.2 1 2 . 2 GLU H H 8.117 0.02 1 3 . 2 GLU CA C 56.005 0.1 1 4 . 2 GLU CB C 30.080 0.1 1 5 . 2 GLU C C 176.294 0.1 1 6 . 3 GLU N N 124.001 0.2 1 7 . 3 GLU H H 8.334 0.02 1 8 . 3 GLU CA C 54.076 0.1 1 9 . 3 GLU CB C 29.294 0.1 1 10 . 5 GLU N N 121.573 0.2 1 11 . 6 GLU N N 124.001 0.2 1 12 . 7 PRO C C 177.936 0.1 1 13 . 8 GLY N N 109.045 0.2 1 14 . 8 GLY H H 8.457 0.02 1 15 . 8 GLY CA C 45.222 0.1 1 16 . 13 PHE C C 176.664 0.1 1 17 . 14 VAL N N 118.985 0.2 1 18 . 14 VAL H H 7.422 0.02 1 19 . 14 VAL CA C 64.490 0.1 1 20 . 14 VAL C C 176.975 0.1 1 21 . 15 GLU N N 120.363 0.2 1 22 . 15 GLU H H 9.037 0.02 1 23 . 15 GLU CA C 57.783 0.1 1 24 . 15 GLU CB C 28.610 0.1 1 25 . 15 GLU C C 177.388 0.1 1 26 . 16 MET N N 118.383 0.2 1 27 . 16 MET H H 8.085 0.02 1 28 . 16 MET CA C 55.421 0.1 1 29 . 16 MET C C 173.354 0.1 1 30 . 17 VAL N N 117.512 0.2 1 31 . 17 VAL H H 6.844 0.02 1 32 . 17 VAL CA C 62.867 0.1 1 33 . 17 VAL CB C 31.124 0.1 1 34 . 17 VAL C C 174.207 0.1 1 35 . 18 ASP N N 120.604 0.2 1 36 . 18 ASP H H 7.534 0.02 1 37 . 18 ASP CA C 53.653 0.1 1 38 . 25 GLY C C 174.506 0.1 1 39 . 26 GLN N N 117.739 0.2 1 40 . 26 GLN H H 8.067 0.02 1 41 . 26 GLN CA C 54.679 0.1 1 42 . 26 GLN CB C 28.973 0.1 1 43 . 26 GLN C C 176.123 0.1 1 44 . 27 GLY N N 110.083 0.2 1 45 . 27 GLY H H 7.764 0.02 1 46 . 27 GLY CA C 44.567 0.1 1 47 . 27 GLY C C 172.016 0.1 1 48 . 28 TYR N N 119.905 0.2 1 49 . 28 TYR H H 8.642 0.02 1 50 . 28 TYR CA C 56.400 0.1 1 51 . 28 TYR CB C 40.449 0.1 1 52 . 28 TYR C C 174.585 0.1 1 53 . 29 TYR N N 117.742 0.2 1 54 . 29 TYR H H 9.179 0.02 1 55 . 29 TYR CA C 54.168 0.1 1 56 . 29 TYR CB C 42.275 0.1 1 57 . 29 TYR C C 172.043 0.1 1 58 . 30 VAL N N 122.550 0.2 1 59 . 30 VAL H H 9.230 0.02 1 60 . 30 VAL CA C 58.370 0.1 1 61 . 30 VAL CB C 36.382 0.1 1 62 . 30 VAL C C 172.933 0.1 1 63 . 31 GLU N N 129.152 0.2 1 64 . 31 GLU H H 8.462 0.02 1 65 . 31 GLU CA C 57.043 0.1 1 66 . 31 GLU CB C 30.313 0.1 1 67 . 31 GLU C C 176.586 0.1 1 68 . 32 MET N N 124.037 0.2 1 69 . 32 MET H H 9.348 0.02 1 70 . 32 MET CA C 55.043 0.1 1 71 . 32 MET CB C 37.373 0.1 1 72 . 32 MET C C 174.157 0.1 1 73 . 33 THR N N 109.135 0.2 1 74 . 33 THR H H 8.799 0.02 1 75 . 33 THR CA C 58.729 0.1 1 76 . 33 THR CB C 70.524 0.1 1 77 . 33 THR C C 173.710 0.1 1 78 . 34 VAL N N 119.686 0.2 1 79 . 34 VAL H H 8.805 0.02 1 80 . 34 VAL CA C 59.271 0.1 1 81 . 34 VAL CB C 34.356 0.1 1 82 . 34 VAL C C 176.974 0.1 1 83 . 35 GLY N N 111.071 0.2 1 84 . 35 GLY H H 8.631 0.02 1 85 . 35 GLY CA C 43.226 0.1 1 86 . 35 GLY C C 173.736 0.1 1 87 . 36 SER N N 110.948 0.2 1 88 . 36 SER H H 7.453 0.02 1 89 . 36 SER CA C 54.987 0.1 1 90 . 36 SER CB C 64.491 0.1 1 91 . 38 PRO C C 177.791 0.1 1 92 . 39 GLN N N 126.467 0.2 1 93 . 39 GLN H H 8.663 0.02 1 94 . 39 GLN CA C 54.587 0.1 1 95 . 39 GLN CB C 28.389 0.1 1 96 . 39 GLN C C 175.448 0.1 1 97 . 40 THR N N 121.780 0.2 1 98 . 40 THR H H 8.208 0.02 1 99 . 40 THR CA C 63.488 0.1 1 100 . 40 THR CB C 68.568 0.1 1 101 . 40 THR C C 173.564 0.1 1 102 . 41 LEU N N 126.016 0.2 1 103 . 41 LEU H H 8.847 0.02 1 104 . 41 LEU CA C 53.534 0.1 1 105 . 41 LEU CB C 47.411 0.1 1 106 . 41 LEU C C 174.201 0.1 1 107 . 42 ASN N N 120.354 0.2 1 108 . 42 ASN H H 9.196 0.02 1 109 . 42 ASN CA C 51.294 0.1 1 110 . 42 ASN CB C 39.960 0.1 1 111 . 42 ASN C C 175.758 0.1 1 112 . 43 ILE N N 124.944 0.2 1 113 . 43 ILE H H 9.219 0.02 1 114 . 43 ILE CA C 57.276 0.1 1 115 . 43 ILE CB C 37.102 0.1 1 116 . 43 ILE C C 174.852 0.1 1 117 . 44 LEU N N 130.343 0.2 1 118 . 44 LEU H H 8.627 0.02 1 119 . 44 LEU CA C 55.494 0.1 1 120 . 44 LEU CB C 41.362 0.1 1 121 . 44 LEU C C 175.772 0.1 1 122 . 45 VAL N N 125.918 0.2 1 123 . 45 VAL H H 8.903 0.02 1 124 . 45 VAL CA C 62.926 0.1 1 125 . 45 VAL CB C 31.103 0.1 1 126 . 45 VAL C C 176.029 0.1 1 127 . 46 ASP N N 130.550 0.2 1 128 . 46 ASP H H 8.242 0.02 1 129 . 46 ASP CA C 52.707 0.1 1 130 . 46 ASP CB C 43.235 0.1 1 131 . 46 ASP C C 175.126 0.1 1 132 . 47 THR N N 116.119 0.2 1 133 . 47 THR H H 8.460 0.02 1 134 . 47 THR CA C 63.716 0.1 1 135 . 47 THR CB C 68.171 0.1 1 136 . 47 THR C C 173.558 0.1 1 137 . 48 GLY N N 113.704 0.2 1 138 . 48 GLY H H 9.008 0.02 1 139 . 48 GLY CA C 44.825 0.1 1 140 . 48 GLY C C 172.015 0.1 1 141 . 49 SER N N 112.246 0.2 1 142 . 49 SER H H 7.285 0.02 1 143 . 49 SER CA C 58.402 0.1 1 144 . 49 SER CB C 64.416 0.1 1 145 . 51 ASN C C 174.926 0.1 1 146 . 52 PHE N N 127.390 0.2 1 147 . 52 PHE H H 8.994 0.02 1 148 . 52 PHE CA C 54.252 0.1 1 149 . 52 PHE C C 173.900 0.1 1 150 . 53 ALA N N 134.735 0.2 1 151 . 53 ALA H H 8.973 0.02 1 152 . 53 ALA CA C 50.100 0.1 1 153 . 53 ALA CB C 22.490 0.1 1 154 . 53 ALA C C 174.819 0.1 1 155 . 54 VAL N N 114.087 0.2 1 156 . 54 VAL H H 8.491 0.02 1 157 . 54 VAL CA C 57.894 0.1 1 158 . 54 VAL CB C 34.396 0.1 1 159 . 54 VAL C C 175.188 0.1 1 160 . 55 GLY N N 112.601 0.2 1 161 . 55 GLY H H 9.631 0.02 1 162 . 55 GLY CA C 48.505 0.1 1 163 . 55 GLY C C 173.926 0.1 1 164 . 56 ALA N N 129.064 0.2 1 165 . 56 ALA H H 8.598 0.02 1 166 . 56 ALA CA C 51.421 0.1 1 167 . 56 ALA CB C 19.141 0.1 1 168 . 56 ALA C C 174.173 0.1 1 169 . 57 ALA N N 121.586 0.2 1 170 . 57 ALA H H 7.327 0.02 1 171 . 57 ALA CA C 49.298 0.1 1 172 . 57 ALA CB C 19.581 0.1 1 173 . 62 LEU C C 177.525 0.1 1 174 . 63 HIS N N 122.344 0.2 1 175 . 63 HIS H H 9.725 0.02 1 176 . 63 HIS CA C 56.471 0.1 1 177 . 63 HIS CB C 30.056 0.1 1 178 . 63 HIS C C 174.844 0.1 1 179 . 64 ARG N N 115.724 0.2 1 180 . 64 ARG H H 7.455 0.02 1 181 . 64 ARG CA C 53.954 0.1 1 182 . 64 ARG CB C 32.354 0.1 1 183 . 64 ARG C C 171.753 0.1 1 184 . 65 TYR N N 109.888 0.2 1 185 . 65 TYR H H 7.335 0.02 1 186 . 65 TYR CA C 55.747 0.1 1 187 . 65 TYR CB C 38.238 0.1 1 188 . 65 TYR C C 173.368 0.1 1 189 . 66 TYR N N 121.550 0.2 1 190 . 66 TYR H H 9.044 0.02 1 191 . 66 TYR CA C 54.807 0.1 1 192 . 66 TYR CB C 38.710 0.1 1 193 . 66 TYR C C 173.920 0.1 1 194 . 67 GLN N N 128.920 0.2 1 195 . 67 GLN H H 9.249 0.02 1 196 . 67 GLN CA C 53.612 0.1 1 197 . 67 GLN CB C 28.270 0.1 1 198 . 67 GLN C C 177.108 0.1 1 199 . 68 ARG N N 127.742 0.2 1 200 . 68 ARG H H 8.548 0.02 1 201 . 68 ARG CA C 59.235 0.1 1 202 . 68 ARG CB C 28.715 0.1 1 203 . 68 ARG C C 178.140 0.1 1 204 . 69 GLN N N 116.402 0.2 1 205 . 69 GLN H H 8.831 0.02 1 206 . 69 GLN CA C 56.882 0.1 1 207 . 69 GLN CB C 26.053 0.1 1 208 . 69 GLN C C 176.433 0.1 1 209 . 70 LEU N N 116.652 0.2 1 210 . 70 LEU H H 6.897 0.02 1 211 . 70 LEU CA C 53.639 0.1 1 212 . 70 LEU CB C 40.970 0.1 1 213 . 70 LEU C C 177.692 0.1 1 214 . 71 SER N N 115.235 0.2 1 215 . 71 SER H H 7.498 0.02 1 216 . 71 SER CA C 62.016 0.1 1 217 . 71 SER CB C 62.575 0.1 1 218 . 71 SER C C 176.153 0.1 1 219 . 72 SER N N 124.403 0.2 1 220 . 72 SER H H 9.262 0.02 1 221 . 72 SER CA C 59.841 0.1 1 222 . 72 SER CB C 62.565 0.1 1 223 . 72 SER C C 175.991 0.1 1 224 . 73 THR N N 109.172 0.2 1 225 . 73 THR H H 7.898 0.02 1 226 . 73 THR CA C 60.519 0.1 1 227 . 73 THR CB C 68.478 0.1 1 228 . 73 THR C C 174.311 0.1 1 229 . 74 TYR N N 124.848 0.2 1 230 . 74 TYR H H 6.897 0.02 1 231 . 74 TYR CA C 58.753 0.1 1 232 . 74 TYR CB C 37.973 0.1 1 233 . 74 TYR C C 175.712 0.1 1 234 . 75 ARG N N 130.404 0.2 1 235 . 75 ARG H H 8.406 0.02 1 236 . 75 ARG CA C 53.810 0.1 1 237 . 75 ARG CB C 31.051 0.1 1 238 . 75 ARG C C 173.132 0.1 1 239 . 76 ASP N N 123.743 0.2 1 240 . 76 ASP H H 8.254 0.02 1 241 . 76 ASP CA C 54.069 0.1 1 242 . 76 ASP CB C 41.859 0.1 1 243 . 76 ASP C C 177.868 0.1 1 244 . 77 LEU N N 126.826 0.2 1 245 . 77 LEU H H 8.339 0.02 1 246 . 77 LEU CA C 54.973 0.1 1 247 . 77 LEU CB C 41.631 0.1 1 248 . 77 LEU C C 176.206 0.1 1 249 . 78 ARG N N 119.888 0.2 1 250 . 78 ARG H H 9.090 0.02 1 251 . 78 ARG CA C 56.060 0.1 1 252 . 78 ARG CB C 26.672 0.1 1 253 . 78 ARG C C 175.117 0.1 1 254 . 79 LYS N N 118.381 0.2 1 255 . 79 LYS H H 7.982 0.02 1 256 . 79 LYS CA C 55.829 0.1 1 257 . 79 LYS CB C 36.116 0.1 1 258 . 79 LYS C C 174.304 0.1 1 259 . 80 GLY N N 112.604 0.2 1 260 . 80 GLY H H 8.480 0.02 1 261 . 80 GLY CA C 43.753 0.1 1 262 . 80 GLY C C 172.302 0.1 1 263 . 81 VAL N N 115.931 0.2 1 264 . 81 VAL H H 8.019 0.02 1 265 . 81 VAL CA C 59.891 0.1 1 266 . 81 VAL CB C 33.869 0.1 1 267 . 81 VAL C C 171.091 0.1 1 268 . 82 TYR N N 127.800 0.2 1 269 . 82 TYR H H 7.933 0.02 1 270 . 82 TYR CA C 56.365 0.1 1 271 . 82 TYR CB C 39.979 0.1 1 272 . 82 TYR C C 173.786 0.1 1 273 . 83 VAL N N 126.772 0.2 1 274 . 83 VAL H H 7.992 0.02 1 275 . 83 VAL CA C 58.825 0.1 1 276 . 83 VAL CB C 32.699 0.1 1 277 . 84 PRO C C 175.856 0.1 1 278 . 85 TYR N N 124.491 0.2 1 279 . 85 TYR H H 8.191 0.02 1 280 . 85 TYR CA C 56.369 0.1 1 281 . 85 TYR CB C 39.619 0.1 1 282 . 87 GLN C C 175.014 0.1 1 283 . 88 GLY N N 110.018 0.2 1 284 . 88 GLY H H 7.934 0.02 1 285 . 88 GLY CA C 44.866 0.1 1 286 . 88 GLY C C 172.906 0.1 1 287 . 89 LYS N N 116.808 0.2 1 288 . 89 LYS H H 8.656 0.02 1 289 . 89 LYS CA C 55.121 0.1 1 290 . 89 LYS CB C 34.392 0.1 1 291 . 89 LYS C C 174.260 0.1 1 292 . 90 TRP N N 115.877 0.2 1 293 . 90 TRP H H 7.969 0.02 1 294 . 90 TRP CA C 55.809 0.1 1 295 . 90 TRP CB C 32.747 0.1 1 296 . 90 TRP C C 172.910 0.1 1 297 . 91 GLU N N 118.849 0.2 1 298 . 91 GLU H H 8.855 0.02 1 299 . 91 GLU CA C 54.257 0.1 1 300 . 91 GLU CB C 32.881 0.1 1 301 . 91 GLU C C 175.700 0.1 1 302 . 92 GLY N N 107.802 0.2 1 303 . 92 GLY H H 8.906 0.02 1 304 . 92 GLY CA C 46.042 0.1 1 305 . 92 GLY C C 172.764 0.1 1 306 . 93 GLU N N 121.496 0.2 1 307 . 93 GLU H H 8.495 0.02 1 308 . 93 GLU CA C 54.733 0.1 1 309 . 93 GLU CB C 32.020 0.1 1 310 . 93 GLU C C 176.703 0.1 1 311 . 94 LEU N N 123.759 0.2 1 312 . 94 LEU H H 9.044 0.02 1 313 . 94 LEU CA C 54.776 0.1 1 314 . 94 LEU CB C 43.438 0.1 1 315 . 94 LEU C C 176.986 0.1 1 316 . 95 GLY N N 111.857 0.2 1 317 . 95 GLY H H 8.683 0.02 1 318 . 95 GLY CA C 45.495 0.1 1 319 . 95 GLY C C 171.076 0.1 1 320 . 96 THR N N 109.156 0.2 1 321 . 96 THR H H 9.057 0.02 1 322 . 96 THR CA C 58.853 0.1 1 323 . 96 THR CB C 72.335 0.1 1 324 . 96 THR C C 173.313 0.1 1 325 . 97 ASP N N 116.940 0.2 1 326 . 97 ASP H H 8.420 0.02 1 327 . 97 ASP CA C 52.180 0.1 1 328 . 97 ASP CB C 43.248 0.1 1 329 . 97 ASP C C 174.175 0.1 1 330 . 98 LEU N N 120.055 0.2 1 331 . 98 LEU H H 9.785 0.02 1 332 . 98 LEU CA C 53.668 0.1 1 333 . 98 LEU CB C 40.950 0.1 1 334 . 98 LEU C C 177.552 0.1 1 335 . 99 VAL N N 124.343 0.2 1 336 . 99 VAL H H 9.421 0.02 1 337 . 99 VAL CA C 60.244 0.1 1 338 . 99 VAL CB C 35.261 0.1 1 339 . 99 VAL C C 174.600 0.1 1 340 . 100 SER N N 119.828 0.2 1 341 . 100 SER H H 8.661 0.02 1 342 . 100 SER CA C 56.553 0.1 1 343 . 100 SER CB C 66.408 0.1 1 344 . 100 SER C C 172.900 0.1 1 345 . 101 ILE N N 122.781 0.2 1 346 . 101 ILE H H 9.235 0.02 1 347 . 101 ILE CA C 57.902 0.1 1 348 . 101 ILE CB C 38.718 0.1 1 349 . 102 PRO C C 178.216 0.1 1 350 . 103 HIS N N 118.366 0.2 1 351 . 103 HIS H H 9.140 0.02 1 352 . 103 HIS CA C 53.595 0.1 1 353 . 103 HIS CB C 28.660 0.1 1 354 . 103 HIS C C 173.720 0.1 1 355 . 104 GLY N N 106.284 0.2 1 356 . 104 GLY H H 7.123 0.02 1 357 . 104 GLY CA C 44.638 0.1 1 358 . 106 ASN C C 174.555 0.1 1 359 . 107 VAL N N 113.638 0.2 1 360 . 107 VAL H H 7.621 0.02 1 361 . 107 VAL CA C 58.723 0.1 1 362 . 107 VAL CB C 34.866 0.1 1 363 . 107 VAL C C 174.798 0.1 1 364 . 108 THR N N 120.003 0.2 1 365 . 108 THR H H 8.327 0.02 1 366 . 108 THR CA C 61.637 0.1 1 367 . 108 THR CB C 70.500 0.1 1 368 . 108 THR C C 173.005 0.1 1 369 . 109 VAL N N 121.479 0.2 1 370 . 109 VAL H H 8.538 0.02 1 371 . 109 VAL CA C 58.698 0.1 1 372 . 109 VAL CB C 34.756 0.1 1 373 . 109 VAL C C 174.213 0.1 1 374 . 110 ARG N N 125.902 0.2 1 375 . 110 ARG H H 8.999 0.02 1 376 . 110 ARG CA C 55.521 0.1 1 377 . 110 ARG CB C 34.899 0.1 1 378 . 110 ARG C C 174.512 0.1 1 379 . 111 ALA N N 131.116 0.2 1 380 . 111 ALA H H 8.669 0.02 1 381 . 111 ALA CA C 49.110 0.1 1 382 . 111 ALA CB C 22.610 0.1 1 383 . 111 ALA C C 175.684 0.1 1 384 . 112 ASN N N 116.663 0.2 1 385 . 112 ASN H H 8.594 0.02 1 386 . 112 ASN CA C 53.990 0.1 1 387 . 112 ASN CB C 39.230 0.1 1 388 . 112 ASN C C 175.083 0.1 1 389 . 113 ILE N N 121.486 0.2 1 390 . 113 ILE H H 9.406 0.02 1 391 . 113 ILE CA C 60.347 0.1 1 392 . 113 ILE CB C 41.848 0.1 1 393 . 113 ILE C C 174.575 0.1 1 394 . 114 ALA N N 129.079 0.2 1 395 . 114 ALA H H 8.555 0.02 1 396 . 114 ALA CA C 50.085 0.1 1 397 . 114 ALA CB C 19.141 0.1 1 398 . 114 ALA C C 173.905 0.1 1 399 . 115 ALA N N 129.751 0.2 1 400 . 115 ALA H H 9.029 0.02 1 401 . 115 ALA CA C 50.325 0.1 1 402 . 115 ALA CB C 16.300 0.1 1 403 . 115 ALA C C 175.679 0.1 1 404 . 116 ILE N N 125.471 0.2 1 405 . 116 ILE H H 9.053 0.02 1 406 . 116 ILE CA C 63.122 0.1 1 407 . 116 ILE CB C 37.995 0.1 1 408 . 116 ILE C C 177.065 0.1 1 409 . 117 THR N N 122.547 0.2 1 410 . 117 THR H H 9.041 0.02 1 411 . 117 THR CA C 61.530 0.1 1 412 . 117 THR CB C 68.178 0.1 1 413 . 117 THR C C 174.602 0.1 1 414 . 118 GLU N N 123.286 0.2 1 415 . 118 GLU H H 7.806 0.02 1 416 . 118 GLU CA C 55.972 0.1 1 417 . 118 GLU CB C 32.583 0.1 1 418 . 118 GLU C C 173.947 0.1 1 419 . 119 SER N N 115.487 0.2 1 420 . 119 SER H H 8.638 0.02 1 421 . 119 SER CA C 58.687 0.1 1 422 . 119 SER CB C 65.264 0.1 1 423 . 119 SER C C 172.636 0.1 1 424 . 120 ASP N N 120.025 0.2 1 425 . 120 ASP H H 8.767 0.02 1 426 . 120 ASP CA C 54.221 0.1 1 427 . 120 ASP CB C 44.046 0.1 1 428 . 120 ASP C C 174.210 0.1 1 429 . 121 LYS N N 120.711 0.2 1 430 . 121 LYS H H 8.672 0.02 1 431 . 121 LYS CA C 57.420 0.1 1 432 . 121 LYS CB C 29.015 0.1 1 433 . 121 LYS C C 173.605 0.1 1 434 . 122 PHE N N 119.690 0.2 1 435 . 122 PHE H H 8.379 0.02 1 436 . 122 PHE CA C 58.650 0.1 1 437 . 122 PHE CB C 41.663 0.1 1 438 . 122 PHE C C 174.573 0.1 1 439 . 123 PHE N N 116.968 0.2 1 440 . 123 PHE H H 8.137 0.02 1 441 . 123 PHE CA C 57.620 0.1 1 442 . 123 PHE CB C 38.087 0.1 1 443 . 123 PHE C C 176.038 0.1 1 444 . 124 ILE N N 122.209 0.2 1 445 . 124 ILE H H 7.932 0.02 1 446 . 124 ILE CA C 59.233 0.1 1 447 . 124 ILE CB C 39.605 0.1 1 448 . 129 TRP C C 173.530 0.1 1 449 . 130 GLU H H 11.141 0.02 1 450 . 130 GLU C C 174.899 0.1 1 451 . 131 GLY N N 106.782 0.2 1 452 . 131 GLY H H 8.262 0.02 1 453 . 131 GLY CA C 45.911 0.1 1 454 . 131 GLY C C 169.289 0.1 1 455 . 132 ILE N N 119.459 0.2 1 456 . 132 ILE H H 9.829 0.02 1 457 . 132 ILE CA C 60.263 0.1 1 458 . 132 ILE CB C 42.201 0.1 1 459 . 132 ILE C C 171.045 0.1 1 460 . 133 LEU N N 127.736 0.2 1 461 . 133 LEU H H 9.376 0.02 1 462 . 133 LEU CA C 52.664 0.1 1 463 . 133 LEU CB C 41.865 0.1 1 464 . 133 LEU C C 173.604 0.1 1 465 . 134 GLY N N 113.316 0.2 1 466 . 134 GLY H H 7.261 0.02 1 467 . 134 GLY CA C 47.449 0.1 1 468 . 134 GLY C C 176.098 0.1 1 469 . 135 LEU N N 128.715 0.2 1 470 . 135 LEU H H 8.242 0.02 1 471 . 135 LEU CA C 54.739 0.1 1 472 . 135 LEU CB C 42.905 0.1 1 473 . 135 LEU C C 175.630 0.1 1 474 . 136 ALA N N 125.587 0.2 1 475 . 136 ALA H H 8.584 0.02 1 476 . 136 ALA CA C 51.524 0.1 1 477 . 136 ALA CB C 14.675 0.1 1 478 . 136 ALA C C 175.183 0.1 1 479 . 137 TYR N N 112.180 0.2 1 480 . 137 TYR H H 7.280 0.02 1 481 . 137 TYR CA C 58.402 0.1 1 482 . 137 TYR CB C 38.320 0.1 1 483 . 137 TYR C C 178.376 0.1 1 484 . 138 ALA N N 124.565 0.2 1 485 . 138 ALA H H 9.864 0.02 1 486 . 138 ALA CA C 55.046 0.1 1 487 . 138 ALA CB C 17.204 0.1 1 488 . 138 ALA C C 178.207 0.1 1 489 . 139 GLU N N 114.713 0.2 1 490 . 139 GLU H H 8.104 0.02 1 491 . 139 GLU CA C 59.352 0.1 1 492 . 139 GLU CB C 30.300 0.1 1 493 . 139 GLU C C 177.664 0.1 1 494 . 140 ILE N N 105.102 0.2 1 495 . 140 ILE H H 6.712 0.02 1 496 . 140 ILE CA C 59.719 0.1 1 497 . 140 ILE CB C 36.547 0.1 1 498 . 140 ILE C C 176.477 0.1 1 499 . 141 ALA N N 127.766 0.2 1 500 . 141 ALA H H 7.921 0.02 1 501 . 141 ALA CA C 52.931 0.1 1 502 . 141 ALA CB C 18.760 0.1 1 503 . 141 ALA C C 175.442 0.1 1 504 . 142 ARG N N 118.789 0.2 1 505 . 142 ARG H H 8.590 0.02 1 506 . 142 ARG CA C 51.662 0.1 1 507 . 142 ARG CB C 28.985 0.1 1 508 . 143 PRO C C 175.839 0.1 1 509 . 144 ASP N N 115.891 0.2 1 510 . 144 ASP H H 7.318 0.02 1 511 . 144 ASP CA C 52.892 0.1 1 512 . 144 ASP CB C 41.324 0.1 1 513 . 144 ASP C C 173.490 0.1 1 514 . 145 ASP N N 113.745 0.2 1 515 . 145 ASP H H 8.055 0.02 1 516 . 145 ASP CA C 54.159 0.1 1 517 . 145 ASP CB C 40.574 0.1 1 518 . 145 ASP C C 176.349 0.1 1 519 . 146 SER N N 116.505 0.2 1 520 . 146 SER H H 8.721 0.02 1 521 . 146 SER CA C 59.791 0.1 1 522 . 146 SER CB C 63.241 0.1 1 523 . 146 SER C C 174.818 0.1 1 524 . 147 LEU N N 127.601 0.2 1 525 . 147 LEU H H 7.409 0.02 1 526 . 147 LEU CA C 53.087 0.1 1 527 . 147 LEU CB C 39.505 0.1 1 528 . 147 LEU C C 174.496 0.1 1 529 . 148 GLU N N 130.101 0.2 1 530 . 148 GLU H H 7.509 0.02 1 531 . 148 GLU CA C 55.722 0.1 1 532 . 148 GLU CB C 32.548 0.1 1 533 . 149 PRO C C 175.493 0.1 1 534 . 150 PHE N N 122.368 0.2 1 535 . 150 PHE H H 9.100 0.02 1 536 . 150 PHE CA C 62.104 0.1 1 537 . 150 PHE CB C 39.960 0.1 1 538 . 150 PHE C C 176.444 0.1 1 539 . 151 PHE N N 120.081 0.2 1 540 . 151 PHE H H 9.948 0.02 1 541 . 151 PHE CA C 62.093 0.1 1 542 . 151 PHE CB C 39.416 0.1 1 543 . 151 PHE C C 176.952 0.1 1 544 . 152 ASP N N 114.964 0.2 1 545 . 152 ASP H H 7.020 0.02 1 546 . 152 ASP CA C 57.018 0.1 1 547 . 152 ASP CB C 40.255 0.1 1 548 . 152 ASP C C 178.587 0.1 1 549 . 153 SER N N 116.799 0.2 1 550 . 153 SER H H 7.755 0.02 1 551 . 153 SER CA C 61.204 0.1 1 552 . 153 SER C C 174.882 0.1 1 553 . 154 LEU N N 121.854 0.2 1 554 . 154 LEU H H 7.920 0.02 1 555 . 154 LEU CA C 57.780 0.1 1 556 . 154 LEU CB C 39.605 0.1 1 557 . 154 LEU C C 179.189 0.1 1 558 . 155 VAL N N 120.395 0.2 1 559 . 155 VAL H H 7.735 0.02 1 560 . 155 VAL CA C 64.950 0.1 1 561 . 155 VAL CB C 30.577 0.1 1 562 . 155 VAL C C 178.004 0.1 1 563 . 156 LYS N N 118.384 0.2 1 564 . 156 LYS H H 7.694 0.02 1 565 . 156 LYS CA C 58.923 0.1 1 566 . 156 LYS CB C 32.265 0.1 1 567 . 156 LYS C C 179.252 0.1 1 568 . 157 GLN N N 113.672 0.2 1 569 . 157 GLN H H 7.855 0.02 1 570 . 157 GLN CA C 56.763 0.1 1 571 . 157 GLN CB C 30.158 0.1 1 572 . 157 GLN C C 176.738 0.1 1 573 . 158 THR N N 108.762 0.2 1 574 . 158 THR H H 7.256 0.02 1 575 . 158 THR CA C 60.733 0.1 1 576 . 158 THR CB C 70.700 0.1 1 577 . 161 PRO C C 176.385 0.1 1 578 . 162 ASN N N 117.524 0.2 1 579 . 162 ASN H H 8.300 0.02 1 580 . 162 ASN CA C 51.792 0.1 1 581 . 162 ASN CB C 36.679 0.1 1 582 . 162 ASN C C 173.901 0.1 1 583 . 163 LEU N N 122.614 0.2 1 584 . 163 LEU H H 9.127 0.02 1 585 . 163 LEU CA C 56.077 0.1 1 586 . 163 LEU CB C 44.335 0.1 1 587 . 163 LEU C C 174.810 0.1 1 588 . 164 PHE N N 116.408 0.2 1 589 . 164 PHE H H 7.796 0.02 1 590 . 164 PHE CA C 53.818 0.1 1 591 . 164 PHE CB C 40.779 0.1 1 592 . 164 PHE C C 171.823 0.1 1 593 . 165 SER N N 113.699 0.2 1 594 . 165 SER H H 9.495 0.02 1 595 . 165 SER CA C 55.803 0.1 1 596 . 165 SER CB C 66.718 0.1 1 597 . 165 SER C C 172.034 0.1 1 598 . 166 LEU N N 121.591 0.2 1 599 . 166 LEU H H 9.265 0.02 1 600 . 166 LEU CA C 53.342 0.1 1 601 . 166 LEU CB C 46.208 0.1 1 602 . 166 LEU C C 174.781 0.1 1 603 . 167 GLN N N 127.677 0.2 1 604 . 167 GLN H H 9.472 0.02 1 605 . 167 GLN CA C 53.910 0.1 1 606 . 167 GLN CB C 30.830 0.1 1 607 . 170 GLY C C 173.924 0.1 1 608 . 171 ALA N N 124.012 0.2 1 609 . 171 ALA H H 8.485 0.02 1 610 . 171 ALA CA C 52.559 0.1 1 611 . 171 ALA CB C 18.611 0.1 1 612 . 171 ALA C C 178.200 0.1 1 613 . 172 GLY N N 107.431 0.2 1 614 . 172 GLY H H 8.288 0.02 1 615 . 172 GLY CA C 45.091 0.1 1 616 . 172 GLY C C 173.602 0.1 1 617 . 173 PHE N N 122.100 0.2 1 618 . 173 PHE H H 7.791 0.02 1 619 . 173 PHE CA C 55.192 0.1 1 620 . 173 PHE CB C 38.548 0.1 1 621 . 179 GLU C C 176.366 0.1 1 622 . 180 VAL N N 119.551 0.2 1 623 . 180 VAL H H 7.924 0.02 1 624 . 180 VAL CA C 62.098 0.1 1 625 . 180 VAL CB C 32.042 0.1 1 626 . 180 VAL C C 176.165 0.1 1 627 . 181 LEU N N 124.947 0.2 1 628 . 181 LEU H H 8.124 0.02 1 629 . 181 LEU CA C 55.198 0.1 1 630 . 181 LEU CB C 41.505 0.1 1 631 . 181 LEU C C 176.818 0.1 1 632 . 182 ALA N N 123.476 0.2 1 633 . 182 ALA H H 8.205 0.02 1 634 . 182 ALA CA C 51.900 0.1 1 635 . 182 ALA CB C 19.030 0.1 1 636 . 182 ALA C C 176.729 0.1 1 637 . 183 SER N N 114.831 0.2 1 638 . 183 SER H H 8.015 0.02 1 639 . 183 SER CA C 58.211 0.1 1 640 . 183 SER CB C 64.370 0.1 1 641 . 183 SER C C 173.932 0.1 1 642 . 184 VAL N N 117.233 0.2 1 643 . 184 VAL H H 7.894 0.02 1 644 . 184 VAL CA C 60.046 0.1 1 645 . 184 VAL CB C 32.500 0.1 1 646 . 185 GLY N N 107.365 0.2 1 647 . 185 GLY C C 171.310 0.1 1 648 . 186 GLY N N 107.563 0.2 1 649 . 186 GLY H H 7.479 0.02 1 650 . 186 GLY CA C 45.609 0.1 1 651 . 186 GLY C C 172.848 0.1 1 652 . 187 SER N N 114.689 0.2 1 653 . 187 SER H H 9.375 0.02 1 654 . 187 SER CA C 58.130 0.1 1 655 . 187 SER CB C 66.671 0.1 1 656 . 187 SER C C 171.652 0.1 1 657 . 188 MET N N 128.246 0.2 1 658 . 188 MET H H 10.528 0.02 1 659 . 188 MET CA C 54.186 0.1 1 660 . 188 MET CB C 34.330 0.1 1 661 . 188 MET C C 173.881 0.1 1 662 . 189 ILE N N 126.287 0.2 1 663 . 189 ILE H H 8.719 0.02 1 664 . 189 ILE CA C 58.057 0.1 1 665 . 189 ILE CB C 34.224 0.1 1 666 . 189 ILE C C 176.476 0.1 1 667 . 190 ILE N N 129.937 0.2 1 668 . 190 ILE H H 7.943 0.02 1 669 . 190 ILE CA C 61.800 0.1 1 670 . 190 ILE CB C 37.670 0.1 1 671 . 190 ILE C C 174.763 0.1 1 672 . 191 GLY N N 114.725 0.2 1 673 . 191 GLY H H 8.770 0.02 1 674 . 191 GLY CA C 45.803 0.1 1 675 . 191 GLY C C 173.278 0.1 1 676 . 192 GLY N N 102.433 0.2 1 677 . 192 GLY H H 6.360 0.02 1 678 . 192 GLY CA C 45.320 0.1 1 679 . 192 GLY C C 169.209 0.1 1 680 . 193 ILE N N 119.499 0.2 1 681 . 193 ILE H H 7.815 0.02 1 682 . 193 ILE CA C 59.704 0.1 1 683 . 193 ILE CB C 41.346 0.1 1 684 . 193 ILE C C 173.586 0.1 1 685 . 194 ASP N N 125.423 0.2 1 686 . 194 ASP H H 7.737 0.02 1 687 . 194 ASP CA C 52.388 0.1 1 688 . 194 ASP CB C 41.845 0.1 1 689 . 194 ASP C C 176.309 0.1 1 690 . 195 HIS N N 122.913 0.2 1 691 . 195 HIS H H 8.053 0.02 1 692 . 195 HIS CA C 57.074 0.1 1 693 . 195 HIS CB C 28.845 0.1 1 694 . 196 SER C C 176.373 0.1 1 695 . 197 LEU N N 119.255 0.2 1 696 . 197 LEU H H 7.067 0.02 1 697 . 197 LEU CA C 54.996 0.1 1 698 . 197 LEU CB C 38.687 0.1 1 699 . 197 LEU C C 175.682 0.1 1 700 . 198 TYR N N 115.750 0.2 1 701 . 198 TYR H H 6.961 0.02 1 702 . 198 TYR CA C 54.568 0.1 1 703 . 198 TYR CB C 41.568 0.1 1 704 . 198 TYR C C 172.868 0.1 1 705 . 199 THR N N 111.087 0.2 1 706 . 199 THR H H 8.536 0.02 1 707 . 199 THR CA C 59.208 0.1 1 708 . 199 THR CB C 70.500 0.1 1 709 . 199 THR C C 174.795 0.1 1 710 . 200 GLY N N 110.471 0.2 1 711 . 200 GLY H H 8.588 0.02 1 712 . 200 GLY CA C 45.692 0.1 1 713 . 200 GLY C C 173.557 0.1 1 714 . 201 SER N N 116.894 0.2 1 715 . 201 SER H H 8.317 0.02 1 716 . 201 SER CA C 57.965 0.1 1 717 . 201 SER CB C 64.585 0.1 1 718 . 201 SER C C 173.682 0.1 1 719 . 202 LEU N N 123.580 0.2 1 720 . 202 LEU H H 8.029 0.02 1 721 . 202 LEU CA C 54.434 0.1 1 722 . 202 LEU CB C 43.232 0.1 1 723 . 202 LEU C C 176.352 0.1 1 724 . 203 TRP N N 125.233 0.2 1 725 . 203 TRP H H 8.072 0.02 1 726 . 203 TRP CA C 56.110 0.1 1 727 . 203 TRP CB C 29.816 0.1 1 728 . 203 TRP C C 174.240 0.1 1 729 . 204 TYR N N 117.494 0.2 1 730 . 204 TYR H H 8.156 0.02 1 731 . 204 TYR CA C 56.661 0.1 1 732 . 204 TYR CB C 41.331 0.1 1 733 . 204 TYR C C 175.148 0.1 1 734 . 205 THR N N 118.425 0.2 1 735 . 205 THR H H 9.610 0.02 1 736 . 205 THR CA C 55.306 0.1 1 737 . 205 THR CB C 72.247 0.1 1 738 . 206 PRO C C 177.389 0.1 1 739 . 207 ILE N N 124.005 0.2 1 740 . 207 ILE H H 8.146 0.02 1 741 . 207 ILE CA C 61.160 0.1 1 742 . 207 ILE CB C 37.845 0.1 1 743 . 207 ILE C C 176.832 0.1 1 744 . 208 ARG N N 131.450 0.2 1 745 . 208 ARG H H 8.854 0.02 1 746 . 208 ARG CA C 58.559 0.1 1 747 . 208 ARG CB C 30.789 0.1 1 748 . 208 ARG C C 175.786 0.1 1 749 . 209 ARG N N 115.783 0.2 1 750 . 209 ARG H H 7.071 0.02 1 751 . 209 ARG CA C 55.123 0.1 1 752 . 209 ARG CB C 32.565 0.1 1 753 . 209 ARG C C 173.944 0.1 1 754 . 210 GLU N N 125.558 0.2 1 755 . 210 GLU H H 8.483 0.02 1 756 . 210 GLU CA C 55.061 0.1 1 757 . 210 GLU CB C 31.270 0.1 1 758 . 210 GLU C C 174.259 0.1 1 759 . 211 TRP N N 123.366 0.2 1 760 . 211 TRP H H 8.705 0.02 1 761 . 211 TRP CA C 57.840 0.1 1 762 . 211 TRP C C 175.723 0.1 1 763 . 212 TYR N N 124.543 0.2 1 764 . 212 TYR H H 6.711 0.02 1 765 . 212 TYR CA C 58.867 0.1 1 766 . 212 TYR CB C 40.967 0.1 1 767 . 212 TYR C C 176.122 0.1 1 768 . 213 TYR N N 119.483 0.2 1 769 . 213 TYR H H 9.556 0.02 1 770 . 213 TYR CA C 59.046 0.1 1 771 . 213 TYR CB C 35.008 0.1 1 772 . 213 TYR C C 174.537 0.1 1 773 . 214 GLU N N 125.269 0.2 1 774 . 214 GLU H H 7.039 0.02 1 775 . 214 GLU CA C 54.960 0.1 1 776 . 214 GLU CB C 30.578 0.1 1 777 . 214 GLU C C 175.109 0.1 1 778 . 215 VAL N N 120.074 0.2 1 779 . 215 VAL H H 8.462 0.02 1 780 . 215 VAL CA C 58.339 0.1 1 781 . 215 VAL CB C 35.005 0.1 1 782 . 215 VAL C C 173.959 0.1 1 783 . 216 ILE N N 120.096 0.2 1 784 . 216 ILE H H 9.067 0.02 1 785 . 216 ILE CA C 59.915 0.1 1 786 . 216 ILE CB C 38.797 0.1 1 787 . 216 ILE C C 174.543 0.1 1 788 . 217 ILE N N 128.304 0.2 1 789 . 217 ILE H H 9.111 0.02 1 790 . 217 ILE CA C 59.947 0.1 1 791 . 217 ILE CB C 38.472 0.1 1 792 . 217 ILE C C 177.669 0.1 1 793 . 218 VAL N N 116.696 0.2 1 794 . 218 VAL H H 8.729 0.02 1 795 . 218 VAL CA C 59.791 0.1 1 796 . 218 VAL CB C 32.008 0.1 1 797 . 218 VAL C C 174.929 0.1 1 798 . 219 ARG N N 120.107 0.2 1 799 . 219 ARG H H 7.169 0.02 1 800 . 219 ARG CA C 56.007 0.1 1 801 . 219 ARG CB C 31.772 0.1 1 802 . 219 ARG C C 172.878 0.1 1 803 . 220 VAL N N 123.985 0.2 1 804 . 220 VAL H H 7.302 0.02 1 805 . 220 VAL CA C 61.240 0.1 1 806 . 220 VAL CB C 34.236 0.1 1 807 . 220 VAL C C 173.939 0.1 1 808 . 221 GLU N N 118.145 0.2 1 809 . 221 GLU H H 8.665 0.02 1 810 . 221 GLU CA C 53.159 0.1 1 811 . 221 GLU CB C 34.384 0.1 1 812 . 221 GLU C C 175.363 0.1 1 813 . 222 ILE N N 120.731 0.2 1 814 . 222 ILE H H 8.195 0.02 1 815 . 222 ILE CA C 59.260 0.1 1 816 . 222 ILE CB C 38.093 0.1 1 817 . 222 ILE C C 177.299 0.1 1 818 . 223 ASN N N 130.433 0.2 1 819 . 223 ASN H H 9.352 0.02 1 820 . 223 ASN CA C 53.276 0.1 1 821 . 223 ASN CB C 38.148 0.1 1 822 . 223 ASN C C 175.370 0.1 1 823 . 224 GLY N N 103.103 0.2 1 824 . 224 GLY H H 8.581 0.02 1 825 . 224 GLY CA C 45.255 0.1 1 826 . 224 GLY C C 172.975 0.1 1 827 . 225 GLN N N 119.750 0.2 1 828 . 225 GLN H H 7.550 0.02 1 829 . 225 GLN CA C 53.749 0.1 1 830 . 225 GLN CB C 28.540 0.1 1 831 . 226 ASP C C 177.070 0.1 1 832 . 227 LEU N N 128.757 0.2 1 833 . 227 LEU H H 8.448 0.02 1 834 . 227 LEU CA C 56.730 0.1 1 835 . 227 LEU CB C 41.303 0.1 1 836 . 227 LEU C C 178.132 0.1 1 837 . 228 LYS N N 113.845 0.2 1 838 . 228 LYS H H 9.134 0.02 1 839 . 228 LYS CA C 56.835 0.1 1 840 . 228 LYS CB C 28.752 0.1 1 841 . 228 LYS C C 175.553 0.1 1 842 . 229 MET N N 116.178 0.2 1 843 . 229 MET H H 6.776 0.02 1 844 . 229 MET CA C 54.104 0.1 1 845 . 229 MET CB C 32.885 0.1 1 846 . 229 MET C C 175.133 0.1 1 847 . 230 ASP N N 122.391 0.2 1 848 . 230 ASP H H 8.245 0.02 1 849 . 230 ASP CA C 54.210 0.1 1 850 . 230 ASP CB C 41.339 0.1 1 851 . 230 ASP C C 178.609 0.1 1 852 . 231 CYS N N 123.743 0.2 1 853 . 231 CYS H H 8.707 0.02 1 854 . 231 CYS CA C 58.951 0.1 1 855 . 231 CYS CB C 41.838 0.1 1 856 . 231 CYS C C 176.413 0.1 1 857 . 232 LYS N N 122.910 0.2 1 858 . 232 LYS H H 8.331 0.02 1 859 . 232 LYS CA C 58.782 0.1 1 860 . 232 LYS CB C 32.123 0.1 1 861 . 232 LYS C C 180.804 0.1 1 862 . 233 GLU N N 114.526 0.2 1 863 . 233 GLU H H 7.986 0.02 1 864 . 233 GLU CA C 57.140 0.1 1 865 . 233 GLU CB C 27.270 0.1 1 866 . 233 GLU C C 179.835 0.1 1 867 . 234 TYR N N 113.852 0.2 1 868 . 234 TYR H H 6.640 0.02 1 869 . 234 TYR CA C 57.104 0.1 1 870 . 234 TYR CB C 36.499 0.1 1 871 . 234 TYR C C 174.271 0.1 1 872 . 235 ASN N N 111.875 0.2 1 873 . 235 ASN H H 6.919 0.02 1 874 . 235 ASN CA C 50.253 0.1 1 875 . 235 ASN CB C 40.887 0.1 1 876 . 235 ASN C C 173.251 0.1 1 877 . 236 TYR N N 119.521 0.2 1 878 . 236 TYR H H 6.452 0.02 1 879 . 236 TYR CA C 50.367 0.1 1 880 . 236 TYR CB C 37.677 0.1 1 881 . 236 TYR C C 175.836 0.1 1 882 . 237 ASP N N 123.632 0.2 1 883 . 237 ASP H H 7.234 0.02 1 884 . 237 ASP CA C 56.539 0.1 1 885 . 237 ASP CB C 39.721 0.1 1 886 . 237 ASP C C 173.816 0.1 1 887 . 238 LYS N N 115.614 0.2 1 888 . 238 LYS H H 7.051 0.02 1 889 . 238 LYS CA C 55.137 0.1 1 890 . 238 LYS CB C 33.759 0.1 1 891 . 238 LYS C C 174.491 0.1 1 892 . 239 SER N N 118.128 0.2 1 893 . 239 SER H H 8.455 0.02 1 894 . 239 SER CA C 58.291 0.1 1 895 . 239 SER CB C 63.650 0.1 1 896 . 239 SER C C 174.484 0.1 1 897 . 240 ILE N N 113.951 0.2 1 898 . 240 ILE H H 8.011 0.02 1 899 . 240 ILE CA C 58.028 0.1 1 900 . 240 ILE CB C 41.949 0.1 1 901 . 240 ILE C C 174.491 0.1 1 902 . 241 VAL N N 110.427 0.2 1 903 . 241 VAL C C 177.077 0.1 1 904 . 242 ASP N N 131.041 0.2 1 905 . 242 ASP H H 8.285 0.02 1 906 . 242 ASP CA C 52.428 0.1 1 907 . 242 ASP CB C 43.367 0.1 1 908 . 243 SER C C 175.155 0.1 1 909 . 244 GLY N N 114.189 0.2 1 910 . 244 GLY H H 9.128 0.02 1 911 . 244 GLY CA C 45.080 0.1 1 912 . 244 GLY C C 173.911 0.1 1 913 . 245 THR N N 119.667 0.2 1 914 . 245 THR H H 7.114 0.02 1 915 . 245 THR CA C 61.278 0.1 1 916 . 245 THR CB C 70.489 0.1 1 917 . 246 THR C C 173.585 0.1 1 918 . 247 ASN N N 119.002 0.2 1 919 . 247 ASN H H 7.390 0.02 1 920 . 247 ASN CA C 53.335 0.1 1 921 . 247 ASN CB C 37.429 0.1 1 922 . 247 ASN C C 176.265 0.1 1 923 . 248 LEU N N 116.685 0.2 1 924 . 248 LEU H H 7.324 0.02 1 925 . 248 LEU CA C 53.670 0.1 1 926 . 248 LEU CB C 41.880 0.1 1 927 . 248 LEU C C 174.650 0.1 1 928 . 249 ARG N N 125.927 0.2 1 929 . 249 ARG H H 8.814 0.02 1 930 . 249 ARG CA C 52.940 0.1 1 931 . 249 ARG CB C 30.303 0.1 1 932 . 249 ARG C C 175.476 0.1 1 933 . 250 LEU N N 121.753 0.2 1 934 . 250 LEU H H 8.724 0.02 1 935 . 250 LEU CA C 50.620 0.1 1 936 . 250 LEU CB C 44.354 0.1 1 937 . 251 PRO C C 177.366 0.1 1 938 . 252 LYS N N 125.103 0.2 1 939 . 252 LYS H H 8.455 0.02 1 940 . 252 LYS CA C 62.000 0.1 1 941 . 252 LYS CB C 33.092 0.1 1 942 . 252 LYS C C 176.997 0.1 1 943 . 253 LYS N N 117.260 0.2 1 944 . 253 LYS H H 9.374 0.02 1 945 . 253 LYS CA C 59.868 0.1 1 946 . 253 LYS CB C 32.637 0.1 1 947 . 253 LYS C C 179.804 0.1 1 948 . 254 VAL N N 119.254 0.2 1 949 . 254 VAL H H 7.295 0.02 1 950 . 254 VAL CA C 64.193 0.1 1 951 . 254 VAL CB C 30.567 0.1 1 952 . 254 VAL C C 177.000 0.1 1 953 . 255 PHE N N 120.954 0.2 1 954 . 255 PHE H H 9.146 0.02 1 955 . 255 PHE CA C 62.061 0.1 1 956 . 255 PHE CB C 37.970 0.1 1 957 . 255 PHE C C 176.258 0.1 1 958 . 256 GLU N N 116.363 0.2 1 959 . 256 GLU H H 8.353 0.02 1 960 . 256 GLU CA C 59.136 0.1 1 961 . 256 GLU CB C 28.741 0.1 1 962 . 256 GLU C C 179.264 0.1 1 963 . 257 ALA N N 121.464 0.2 1 964 . 257 ALA H H 7.076 0.02 1 965 . 257 ALA CA C 54.667 0.1 1 966 . 257 ALA CB C 18.771 0.1 1 967 . 257 ALA C C 180.107 0.1 1 968 . 258 ALA N N 122.094 0.2 1 969 . 258 ALA H H 8.992 0.02 1 970 . 258 ALA CA C 54.741 0.1 1 971 . 258 ALA CB C 16.040 0.1 1 972 . 258 ALA C C 179.227 0.1 1 973 . 259 VAL N N 118.084 0.2 1 974 . 259 VAL H H 8.507 0.02 1 975 . 259 VAL CA C 66.580 0.1 1 976 . 259 VAL CB C 30.136 0.1 1 977 . 259 VAL C C 177.253 0.1 1 978 . 260 LYS N N 119.556 0.2 1 979 . 260 LYS H H 7.236 0.02 1 980 . 260 LYS CA C 59.988 0.1 1 981 . 260 LYS CB C 31.499 0.1 1 982 . 260 LYS C C 179.514 0.1 1 983 . 261 SER N N 114.353 0.2 1 984 . 261 SER H H 7.353 0.02 1 985 . 261 SER CA C 61.528 0.1 1 986 . 261 SER CB C 63.180 0.1 1 987 . 262 ILE C C 178.889 0.1 1 988 . 263 LYS N N 122.389 0.2 1 989 . 263 LYS H H 8.498 0.02 1 990 . 263 LYS CA C 59.197 0.1 1 991 . 263 LYS CB C 32.150 0.1 1 992 . 263 LYS C C 178.896 0.1 1 993 . 264 ALA N N 119.942 0.2 1 994 . 264 ALA H H 7.369 0.02 1 995 . 264 ALA CA C 54.562 0.1 1 996 . 264 ALA CB C 17.437 0.1 1 997 . 264 ALA C C 180.479 0.1 1 998 . 265 ALA N N 119.818 0.2 1 999 . 265 ALA H H 7.721 0.02 1 1000 . 265 ALA CA C 53.848 0.1 1 1001 . 265 ALA CB C 17.765 0.1 1 1002 . 265 ALA C C 177.979 0.1 1 1003 . 266 SER N N 110.916 0.2 1 1004 . 266 SER H H 7.570 0.02 1 1005 . 266 SER CA C 57.597 0.1 1 1006 . 266 SER CB C 64.298 0.1 1 1007 . 266 SER C C 175.423 0.1 1 1008 . 267 SER N N 114.611 0.2 1 1009 . 267 SER H H 7.104 0.02 1 1010 . 267 SER CA C 60.729 0.1 1 1011 . 267 SER CB C 63.283 0.1 1 1012 . 267 SER C C 175.159 0.1 1 1013 . 268 THR N N 114.365 0.2 1 1014 . 268 THR H H 7.626 0.02 1 1015 . 268 THR CA C 63.430 0.1 1 1016 . 268 THR CB C 68.277 0.1 1 1017 . 268 THR C C 174.878 0.1 1 1018 . 269 GLU N N 122.034 0.2 1 1019 . 269 GLU H H 8.131 0.02 1 1020 . 269 GLU CA C 55.058 0.1 1 1021 . 269 GLU CB C 31.506 0.1 1 1022 . 274 GLY C C 177.343 0.1 1 1023 . 275 PHE N N 124.042 0.2 1 1024 . 275 PHE H H 8.205 0.02 1 1025 . 275 PHE CA C 59.760 0.1 1 1026 . 275 PHE CB C 38.090 0.1 1 1027 . 275 PHE C C 178.276 0.1 1 1028 . 276 TRP N N 119.515 0.2 1 1029 . 276 TRP H H 6.788 0.02 1 1030 . 276 TRP CA C 56.535 0.1 1 1031 . 276 TRP CB C 28.033 0.1 1 1032 . 276 TRP C C 176.018 0.1 1 1033 . 277 LEU N N 114.815 0.2 1 1034 . 277 LEU H H 7.056 0.02 1 1035 . 277 LEU CA C 54.034 0.1 1 1036 . 277 LEU CB C 41.795 0.1 1 1037 . 277 LEU C C 177.671 0.1 1 1038 . 278 GLY N N 107.915 0.2 1 1039 . 278 GLY H H 7.912 0.02 1 1040 . 278 GLY CA C 46.235 0.1 1 1041 . 278 GLY C C 174.980 0.1 1 1042 . 279 GLU N N 116.141 0.2 1 1043 . 279 GLU H H 7.723 0.02 1 1044 . 279 GLU CA C 56.321 0.1 1 1045 . 279 GLU CB C 31.021 0.1 1 1046 . 279 GLU C C 175.861 0.1 1 1047 . 280 GLN N N 116.125 0.2 1 1048 . 280 GLN H H 6.884 0.02 1 1049 . 280 GLN CA C 53.639 0.1 1 1050 . 280 GLN CB C 32.157 0.1 1 1051 . 280 GLN C C 174.221 0.1 1 1052 . 281 LEU N N 122.981 0.2 1 1053 . 281 LEU H H 8.443 0.02 1 1054 . 281 LEU CA C 53.688 0.1 1 1055 . 281 LEU CB C 42.808 0.1 1 1056 . 281 LEU C C 177.007 0.1 1 1057 . 282 VAL N N 118.255 0.2 1 1058 . 282 VAL H H 8.284 0.02 1 1059 . 282 VAL CA C 60.370 0.1 1 1060 . 282 VAL CB C 33.364 0.1 1 1061 . 282 VAL C C 173.517 0.1 1 1062 . 283 CYS N N 122.061 0.2 1 1063 . 283 CYS H H 7.704 0.02 1 1064 . 283 CYS CA C 54.641 0.1 1 1065 . 283 CYS CB C 49.362 0.1 1 1066 . 283 CYS C C 173.117 0.1 1 1067 . 284 TRP N N 122.626 0.2 1 1068 . 284 TRP H H 9.067 0.02 1 1069 . 284 TRP CA C 58.661 0.1 1 1070 . 284 TRP CB C 32.229 0.1 1 1071 . 284 TRP C C 174.791 0.1 1 1072 . 285 GLN N N 121.167 0.2 1 1073 . 285 GLN H H 8.461 0.02 1 1074 . 285 GLN CA C 56.799 0.1 1 1075 . 285 GLN CB C 27.883 0.1 1 1076 . 285 GLN C C 177.388 0.1 1 1077 . 286 ALA N N 128.826 0.2 1 1078 . 286 ALA H H 8.929 0.02 1 1079 . 286 ALA CA C 53.910 0.1 1 1080 . 286 ALA CB C 17.665 0.1 1 1081 . 286 ALA C C 178.696 0.1 1 1082 . 287 GLY N N 110.879 0.2 1 1083 . 287 GLY H H 8.800 0.02 1 1084 . 287 GLY CA C 45.740 0.1 1 1085 . 287 GLY C C 176.621 0.1 1 1086 . 288 THR N N 109.912 0.2 1 1087 . 288 THR H H 8.254 0.02 1 1088 . 288 THR CA C 61.482 0.1 1 1089 . 288 THR CB C 69.694 0.1 1 1090 . 288 THR C C 174.211 0.1 1 1091 . 289 THR N N 121.300 0.2 1 1092 . 289 THR H H 7.479 0.02 1 1093 . 289 THR CA C 61.114 0.1 1 1094 . 289 THR CB C 69.110 0.1 1 1095 . 290 PRO C C 175.102 0.1 1 1096 . 291 TRP N N 122.454 0.2 1 1097 . 291 TRP H H 7.348 0.02 1 1098 . 291 TRP CA C 59.930 0.1 1 1099 . 291 TRP C C 177.671 0.1 1 1100 . 292 ASN N N 109.056 0.2 1 1101 . 292 ASN H H 8.141 0.02 1 1102 . 292 ASN CA C 55.145 0.1 1 1103 . 292 ASN CB C 37.289 0.1 1 1104 . 292 ASN C C 176.692 0.1 1 1105 . 293 ILE N N 115.193 0.2 1 1106 . 293 ILE H H 7.526 0.02 1 1107 . 293 ILE CA C 62.059 0.1 1 1108 . 293 ILE CB C 36.915 0.1 1 1109 . 293 ILE C C 175.728 0.1 1 1110 . 294 PHE N N 119.618 0.2 1 1111 . 294 PHE H H 7.542 0.02 1 1112 . 294 PHE CA C 55.741 0.1 1 1113 . 294 PHE CB C 38.540 0.1 1 1114 . 295 PRO C C 178.279 0.1 1 1115 . 296 VAL N N 112.516 0.2 1 1116 . 296 VAL H H 8.134 0.02 1 1117 . 296 VAL CA C 60.672 0.1 1 1118 . 296 VAL CB C 30.959 0.1 1 1119 . 296 VAL C C 176.091 0.1 1 1120 . 297 ILE N N 121.454 0.2 1 1121 . 297 ILE H H 8.256 0.02 1 1122 . 297 ILE CA C 60.287 0.1 1 1123 . 297 ILE CB C 39.794 0.1 1 1124 . 297 ILE C C 174.774 0.1 1 1125 . 298 SER N N 121.360 0.2 1 1126 . 298 SER H H 9.156 0.02 1 1127 . 298 SER CA C 56.585 0.1 1 1128 . 298 SER CB C 64.318 0.1 1 1129 . 298 SER C C 172.583 0.1 1 1130 . 299 LEU N N 123.922 0.2 1 1131 . 299 LEU H H 8.784 0.02 1 1132 . 299 LEU CA C 53.298 0.1 1 1133 . 299 LEU CB C 41.896 0.1 1 1134 . 299 LEU C C 174.592 0.1 1 1135 . 300 TYR N N 122.228 0.2 1 1136 . 300 TYR H H 8.694 0.02 1 1137 . 300 TYR CA C 55.089 0.1 1 1138 . 300 TYR CB C 38.428 0.1 1 1139 . 300 TYR C C 175.154 0.1 1 1140 . 301 LEU N N 125.176 0.2 1 1141 . 301 LEU H H 8.333 0.02 1 1142 . 301 LEU CA C 52.117 0.1 1 1143 . 301 LEU CB C 42.293 0.1 1 1144 . 301 LEU C C 175.191 0.1 1 1145 . 302 MET N N 118.018 0.2 1 1146 . 302 MET H H 7.278 0.02 1 1147 . 302 MET CA C 56.846 0.1 1 1148 . 302 MET CB C 33.712 0.1 1 1149 . 302 MET C C 176.193 0.1 1 1150 . 303 GLY N N 114.950 0.2 1 1151 . 303 GLY H H 8.523 0.02 1 1152 . 303 GLY CA C 44.115 0.1 1 1153 . 303 GLY C C 174.310 0.1 1 1154 . 304 GLU N N 116.010 0.2 1 1155 . 304 GLU H H 8.391 0.02 1 1156 . 304 GLU CA C 58.299 0.1 1 1157 . 304 GLU CB C 31.105 0.1 1 1158 . 304 GLU C C 176.965 0.1 1 1159 . 305 VAL N N 120.300 0.2 1 1160 . 305 VAL H H 7.937 0.02 1 1161 . 305 VAL CA C 60.746 0.1 1 1162 . 305 VAL CB C 32.494 0.1 1 1163 . 305 VAL C C 175.770 0.1 1 1164 . 306 THR N N 122.175 0.2 1 1165 . 306 THR H H 8.078 0.02 1 1166 . 306 THR CA C 64.123 0.1 1 1167 . 306 THR CB C 68.705 0.1 1 1168 . 306 THR C C 174.478 0.1 1 1169 . 307 ASN N N 118.424 0.2 1 1170 . 307 ASN H H 8.696 0.02 1 1171 . 307 ASN CA C 54.596 0.1 1 1172 . 307 ASN CB C 36.211 0.1 1 1173 . 307 ASN C C 174.216 0.1 1 1174 . 308 GLN N N 118.824 0.2 1 1175 . 308 GLN H H 7.915 0.02 1 1176 . 308 GLN CA C 54.964 0.1 1 1177 . 308 GLN CB C 30.902 0.1 1 1178 . 308 GLN C C 174.237 0.1 1 1179 . 309 SER N N 116.973 0.2 1 1180 . 309 SER H H 9.041 0.02 1 1181 . 309 SER CA C 56.551 0.1 1 1182 . 309 SER CB C 68.092 0.1 1 1183 . 309 SER C C 173.609 0.1 1 1184 . 310 PHE N N 115.294 0.2 1 1185 . 310 PHE H H 8.123 0.02 1 1186 . 310 PHE CA C 55.621 0.1 1 1187 . 310 PHE CB C 40.278 0.1 1 1188 . 310 PHE C C 171.345 0.1 1 1189 . 311 ARG N N 118.046 0.2 1 1190 . 311 ARG H H 9.299 0.02 1 1191 . 311 ARG CA C 52.628 0.1 1 1192 . 311 ARG CB C 32.308 0.1 1 1193 . 311 ARG C C 174.230 0.1 1 1194 . 312 ILE N N 118.509 0.2 1 1195 . 312 ILE H H 8.380 0.02 1 1196 . 312 ILE CA C 58.253 0.1 1 1197 . 312 ILE CB C 37.422 0.1 1 1198 . 312 ILE C C 174.825 0.1 1 1199 . 313 THR N N 121.600 0.2 1 1200 . 313 THR H H 8.991 0.02 1 1201 . 313 THR CA C 61.246 0.1 1 1202 . 313 THR CB C 70.911 0.1 1 1203 . 313 THR C C 173.833 0.1 1 1204 . 314 ILE N N 118.655 0.2 1 1205 . 314 ILE H H 9.012 0.02 1 1206 . 314 ILE CA C 59.173 0.1 1 1207 . 314 ILE CB C 40.229 0.1 1 1208 . 314 ILE C C 176.293 0.1 1 1209 . 315 LEU N N 127.948 0.2 1 1210 . 315 LEU H H 8.008 0.02 1 1211 . 315 LEU CA C 54.075 0.1 1 1212 . 315 LEU CB C 36.747 0.1 1 1213 . 317 GLN C C 177.540 0.1 1 1214 . 318 GLN N N 115.280 0.2 1 1215 . 318 GLN H H 7.698 0.02 1 1216 . 318 GLN CA C 59.080 0.1 1 1217 . 318 GLN CB C 29.133 0.1 1 1218 . 318 GLN C C 176.008 0.1 1 1219 . 319 TYR N N 111.309 0.2 1 1220 . 319 TYR H H 6.803 0.02 1 1221 . 319 TYR CA C 57.840 0.1 1 1222 . 319 TYR CB C 37.242 0.1 1 1223 . 319 TYR C C 172.571 0.1 1 1224 . 320 LEU N N 125.785 0.2 1 1225 . 320 LEU H H 8.123 0.02 1 1226 . 320 LEU CA C 53.738 0.1 1 1227 . 320 LEU CB C 39.971 0.1 1 1228 . 320 LEU C C 175.233 0.1 1 1229 . 321 ARG N N 123.421 0.2 1 1230 . 321 ARG H H 8.977 0.02 1 1231 . 321 ARG CA C 52.213 0.1 1 1232 . 321 ARG CB C 30.836 0.1 1 1233 . 322 PRO C C 177.070 0.1 1 1234 . 323 VAL N N 121.311 0.2 1 1235 . 323 VAL H H 7.861 0.02 1 1236 . 323 VAL CA C 60.576 0.1 1 1237 . 323 VAL CB C 33.739 0.1 1 1238 . 323 VAL C C 175.203 0.1 1 1239 . 324 GLU N N 125.045 0.2 1 1240 . 324 GLU H H 8.448 0.02 1 1241 . 324 GLU CA C 56.124 0.1 1 1242 . 324 GLU CB C 29.400 0.1 1 1243 . 324 GLU C C 175.807 0.1 1 1244 . 325 ASP N N 122.307 0.2 1 1245 . 325 ASP H H 8.335 0.02 1 1246 . 325 ASP CA C 53.611 0.1 1 1247 . 325 ASP CB C 41.345 0.1 1 1248 . 325 ASP C C 176.310 0.1 1 1249 . 326 VAL N N 119.563 0.2 1 1250 . 326 VAL H H 7.964 0.02 1 1251 . 326 VAL CA C 62.192 0.1 1 1252 . 326 VAL CB C 31.722 0.1 1 1253 . 326 VAL C C 176.564 0.1 1 1254 . 327 ALA N N 124.828 0.2 1 1255 . 327 ALA H H 8.217 0.02 1 1256 . 327 ALA CA C 52.964 0.1 1 1257 . 327 ALA CB C 19.000 0.1 1 1258 . 327 ALA C C 178.237 0.1 1 1259 . 328 THR N N 110.774 0.2 1 1260 . 328 THR H H 7.757 0.02 1 1261 . 328 THR CA C 60.995 0.1 1 1262 . 328 THR CB C 68.912 0.1 1 1263 . 328 THR C C 177.626 0.1 1 1264 . 329 SER N N 117.534 0.2 1 1265 . 329 SER H H 8.011 0.02 1 1266 . 329 SER CA C 58.752 0.1 1 1267 . 329 SER CB C 62.953 0.1 1 1268 . 330 GLN C C 175.358 0.1 1 1269 . 331 ASP N N 120.636 0.2 1 1270 . 331 ASP H H 7.889 0.02 1 1271 . 331 ASP CA C 53.783 0.1 1 1272 . 331 ASP CB C 42.908 0.1 1 1273 . 331 ASP C C 174.803 0.1 1 1274 . 332 ASP N N 121.500 0.2 1 1275 . 332 ASP H H 8.842 0.02 1 1276 . 332 ASP CA C 53.848 0.1 1 1277 . 332 ASP CB C 42.008 0.1 1 1278 . 332 ASP C C 174.467 0.1 1 1279 . 333 CYS N N 121.105 0.2 1 1280 . 333 CYS H H 8.205 0.02 1 1281 . 333 CYS CA C 54.547 0.1 1 1282 . 333 CYS CB C 47.891 0.1 1 1283 . 333 CYS C C 173.944 0.1 1 1284 . 334 TYR N N 118.020 0.2 1 1285 . 334 TYR H H 9.065 0.02 1 1286 . 334 TYR CA C 57.078 0.1 1 1287 . 334 TYR CB C 43.715 0.1 1 1288 . 334 TYR C C 174.504 0.1 1 1289 . 335 LYS N N 118.675 0.2 1 1290 . 335 LYS H H 8.954 0.02 1 1291 . 335 LYS CA C 53.764 0.1 1 1292 . 335 LYS CB C 35.894 0.1 1 1293 . 335 LYS C C 175.207 0.1 1 1294 . 336 PHE N N 126.401 0.2 1 1295 . 336 PHE H H 8.877 0.02 1 1296 . 336 PHE CA C 57.389 0.1 1 1297 . 336 PHE CB C 39.121 0.1 1 1298 . 336 PHE C C 175.783 0.1 1 1299 . 337 ALA N N 132.629 0.2 1 1300 . 337 ALA H H 8.715 0.02 1 1301 . 337 ALA CA C 51.621 0.1 1 1302 . 337 ALA CB C 19.129 0.1 1 1303 . 337 ALA C C 174.086 0.1 1 1304 . 338 ILE N N 116.119 0.2 1 1305 . 338 ILE H H 5.503 0.02 1 1306 . 338 ILE CA C 58.850 0.1 1 1307 . 338 ILE CB C 37.426 0.1 1 1308 . 338 ILE C C 175.151 0.1 1 1309 . 339 SER N N 119.205 0.2 1 1310 . 339 SER H H 8.774 0.02 1 1311 . 339 SER CA C 56.847 0.1 1 1312 . 339 SER CB C 65.454 0.1 1 1313 . 339 SER C C 172.293 0.1 1 1314 . 340 GLN N N 119.850 0.2 1 1315 . 340 GLN H H 7.756 0.02 1 1316 . 340 GLN CA C 55.229 0.1 1 1317 . 340 GLN CB C 29.802 0.1 1 1318 . 340 GLN C C 175.231 0.1 1 1319 . 341 SER N N 118.850 0.2 1 1320 . 341 SER H H 8.154 0.02 1 1321 . 341 SER CA C 55.146 0.1 1 1322 . 341 SER CB C 65.615 0.1 1 1323 . 342 SER C C 175.126 0.1 1 1324 . 343 THR N N 114.987 0.2 1 1325 . 343 THR H H 8.460 0.02 1 1326 . 343 THR CA C 59.849 0.1 1 1327 . 343 THR CB C 68.171 0.1 1 1328 . 343 THR C C 174.547 0.1 1 1329 . 344 GLY N N 110.994 0.2 1 1330 . 344 GLY H H 8.076 0.02 1 1331 . 344 GLY CA C 43.294 0.1 1 1332 . 344 GLY C C 174.549 0.1 1 1333 . 345 THR N N 119.171 0.2 1 1334 . 345 THR H H 8.602 0.02 1 1335 . 345 THR CA C 63.080 0.1 1 1336 . 345 THR CB C 67.071 0.1 1 1337 . 345 THR C C 176.519 0.1 1 1338 . 346 VAL N N 128.963 0.2 1 1339 . 346 VAL H H 9.435 0.02 1 1340 . 346 VAL CA C 61.415 0.1 1 1341 . 346 VAL CB C 33.197 0.1 1 1342 . 346 VAL C C 175.577 0.1 1 1343 . 347 MET N N 126.988 0.2 1 1344 . 347 MET H H 9.106 0.02 1 1345 . 347 MET CA C 55.066 0.1 1 1346 . 347 MET CB C 32.578 0.1 1 1347 . 347 MET C C 174.371 0.1 1 1348 . 348 GLY N N 110.264 0.2 1 1349 . 348 GLY H H 6.582 0.02 1 1350 . 348 GLY CA C 43.549 0.1 1 1351 . 348 GLY C C 175.777 0.1 1 1352 . 349 ALA N N 125.910 0.2 1 1353 . 349 ALA H H 9.388 0.02 1 1354 . 349 ALA CA C 56.268 0.1 1 1355 . 349 ALA CB C 17.455 0.1 1 1356 . 353 GLU C C 177.902 0.1 1 1357 . 354 GLY N N 104.801 0.2 1 1358 . 354 GLY H H 7.789 0.02 1 1359 . 354 GLY CA C 44.111 0.1 1 1360 . 354 GLY C C 172.621 0.1 1 1361 . 355 PHE N N 113.573 0.2 1 1362 . 355 PHE H H 7.462 0.02 1 1363 . 355 PHE CA C 57.558 0.1 1 1364 . 355 PHE CB C 42.736 0.1 1 1365 . 355 PHE C C 174.762 0.1 1 1366 . 356 TYR N N 125.453 0.2 1 1367 . 356 TYR H H 9.454 0.02 1 1368 . 356 TYR CA C 55.087 0.1 1 1369 . 356 TYR CB C 42.503 0.1 1 1370 . 356 TYR C C 173.870 0.1 1 1371 . 357 VAL N N 126.090 0.2 1 1372 . 357 VAL H H 7.832 0.02 1 1373 . 357 VAL CA C 59.565 0.1 1 1374 . 357 VAL CB C 32.319 0.1 1 1375 . 357 VAL C C 174.718 0.1 1 1376 . 358 VAL N N 127.160 0.2 1 1377 . 358 VAL H H 8.788 0.02 1 1378 . 358 VAL CA C 60.382 0.1 1 1379 . 358 VAL CB C 33.193 0.1 1 1380 . 358 VAL C C 173.892 0.1 1 1381 . 359 PHE N N 129.006 0.2 1 1382 . 359 PHE H H 8.927 0.02 1 1383 . 359 PHE CA C 56.160 0.1 1 1384 . 359 PHE CB C 35.798 0.1 1 1385 . 359 PHE C C 173.656 0.1 1 1386 . 360 ASP N N 124.712 0.2 1 1387 . 360 ASP H H 7.973 0.02 1 1388 . 360 ASP CA C 51.531 0.1 1 1389 . 360 ASP CB C 39.639 0.1 1 1390 . 360 ASP C C 176.162 0.1 1 1391 . 361 ARG N N 124.384 0.2 1 1392 . 361 ARG H H 7.267 0.02 1 1393 . 361 ARG CA C 58.502 0.1 1 1394 . 361 ARG CB C 29.192 0.1 1 1395 . 361 ARG C C 180.345 0.1 1 1396 . 362 ALA N N 123.476 0.2 1 1397 . 362 ALA H H 8.202 0.02 1 1398 . 362 ALA CA C 54.628 0.1 1 1399 . 362 ALA CB C 19.030 0.1 1 1400 . 362 ALA C C 179.023 0.1 1 1401 . 363 ARG N N 114.921 0.2 1 1402 . 363 ARG H H 7.193 0.02 1 1403 . 363 ARG CA C 54.534 0.1 1 1404 . 363 ARG CB C 28.733 0.1 1 1405 . 363 ARG C C 174.575 0.1 1 1406 . 364 LYS N N 120.729 0.2 1 1407 . 364 LYS H H 7.719 0.02 1 1408 . 364 LYS CA C 62.422 0.1 1 1409 . 364 LYS C C 175.373 0.1 1 1410 . 365 ARG N N 116.999 0.2 1 1411 . 365 ARG H H 8.527 0.02 1 1412 . 365 ARG CA C 55.086 0.1 1 1413 . 365 ARG CB C 31.941 0.1 1 1414 . 365 ARG C C 172.609 0.1 1 1415 . 366 ILE N N 120.563 0.2 1 1416 . 366 ILE H H 9.354 0.02 1 1417 . 366 ILE CA C 57.944 0.1 1 1418 . 366 ILE CB C 39.308 0.1 1 1419 . 366 ILE C C 175.504 0.1 1 1420 . 367 GLY N N 115.725 0.2 1 1421 . 367 GLY H H 9.533 0.02 1 1422 . 367 GLY CA C 43.754 0.1 1 1423 . 367 GLY C C 171.118 0.1 1 1424 . 368 PHE N N 119.231 0.2 1 1425 . 368 PHE H H 8.847 0.02 1 1426 . 368 PHE CA C 56.952 0.1 1 1427 . 368 PHE C C 174.493 0.1 1 1428 . 369 ALA N N 120.159 0.2 1 1429 . 369 ALA H H 8.255 0.02 1 1430 . 369 ALA CA C 50.815 0.1 1 1431 . 369 ALA CB C 25.050 0.1 1 1432 . 369 ALA C C 176.713 0.1 1 1433 . 370 VAL N N 124.004 0.2 1 1434 . 370 VAL H H 9.117 0.02 1 1435 . 370 VAL CA C 65.374 0.1 1 1436 . 370 VAL CB C 30.631 0.1 1 1437 . 370 VAL C C 175.495 0.1 1 1438 . 371 SER N N 119.178 0.2 1 1439 . 371 SER H H 7.932 0.02 1 1440 . 371 SER CA C 57.317 0.1 1 1441 . 371 SER CB C 62.605 0.1 1 1442 . 372 ALA N N 130.484 0.2 1 1443 . 373 CYS N N 111.686 0.2 1 1444 . 378 GLU C C 176.051 0.1 1 1445 . 379 PHE N N 117.969 0.2 1 1446 . 379 PHE H H 8.843 0.02 1 1447 . 379 PHE CA C 58.258 0.1 1 1448 . 379 PHE CB C 40.183 0.1 1 1449 . 379 PHE C C 176.102 0.1 1 1450 . 380 ARG N N 119.541 0.2 1 1451 . 380 ARG H H 8.489 0.02 1 1452 . 380 ARG CA C 55.481 0.1 1 1453 . 380 ARG CB C 33.918 0.1 1 1454 . 380 ARG C C 173.411 0.1 1 1455 . 381 THR N N 109.291 0.2 1 1456 . 381 THR H H 7.559 0.02 1 1457 . 381 THR CA C 59.715 0.1 1 1458 . 381 THR CB C 71.524 0.1 1 1459 . 381 THR C C 173.917 0.1 1 1460 . 382 ALA N N 127.565 0.2 1 1461 . 382 ALA H H 9.436 0.02 1 1462 . 382 ALA CA C 52.940 0.1 1 1463 . 382 ALA C C 176.667 0.1 1 1464 . 383 ALA N N 118.743 0.2 1 1465 . 383 ALA H H 7.891 0.02 1 1466 . 383 ALA CA C 51.940 0.1 1 1467 . 383 ALA CB C 23.127 0.1 1 1468 . 383 ALA C C 175.455 0.1 1 1469 . 384 VAL N N 120.950 0.2 1 1470 . 384 VAL H H 8.028 0.02 1 1471 . 384 VAL CA C 62.144 0.1 1 1472 . 384 VAL CB C 32.673 0.1 1 1473 . 384 VAL C C 175.779 0.1 1 1474 . 385 GLU N N 123.452 0.2 1 1475 . 385 GLU H H 8.653 0.02 1 1476 . 385 GLU CA C 54.430 0.1 1 1477 . 385 GLU CB C 34.766 0.1 1 1478 . 385 GLU C C 173.815 0.1 1 1479 . 386 GLY N N 107.334 0.2 1 1480 . 386 GLY H H 7.731 0.02 1 1481 . 386 GLY CA C 44.278 0.1 1 1482 . 389 VAL C C 177.255 0.1 1 1483 . 390 THR N N 126.561 0.2 1 1484 . 390 THR H H 8.143 0.02 1 1485 . 390 THR CA C 61.413 0.1 1 1486 . 390 THR CB C 71.537 0.1 1 1487 . 390 THR C C 171.989 0.1 1 1488 . 391 LEU N N 124.283 0.2 1 1489 . 391 LEU H H 8.257 0.02 1 1490 . 391 LEU CA C 54.069 0.1 1 1491 . 391 LEU CB C 41.859 0.1 1 1492 . 391 LEU C C 177.248 0.1 1 1493 . 392 ASP N N 117.465 0.2 1 1494 . 392 ASP H H 8.626 0.02 1 1495 . 392 ASP CA C 55.044 0.1 1 1496 . 392 ASP CB C 38.965 0.1 1 1497 . 392 ASP C C 177.312 0.1 1 1498 . 393 MET N N 118.392 0.2 1 1499 . 393 MET H H 8.577 0.02 1 1500 . 393 MET CA C 58.916 0.1 1 1501 . 393 MET CB C 33.051 0.1 1 1502 . 393 MET C C 178.292 0.1 1 1503 . 394 GLU N N 117.702 0.2 1 1504 . 394 GLU H H 8.907 0.02 1 1505 . 394 GLU CA C 58.788 0.1 1 1506 . 394 GLU CB C 28.303 0.1 1 1507 . 394 GLU C C 178.568 0.1 1 1508 . 395 ASP N N 119.266 0.2 1 1509 . 395 ASP H H 7.635 0.02 1 1510 . 395 ASP CA C 54.998 0.1 1 1511 . 395 ASP CB C 40.013 0.1 1 1512 . 395 ASP C C 176.578 0.1 1 1513 . 396 CYS N N 116.469 0.2 1 1514 . 396 CYS H H 7.790 0.02 1 1515 . 396 CYS CA C 56.154 0.1 1 1516 . 396 CYS CB C 38.520 0.1 1 1517 . 396 CYS C C 175.496 0.1 1 1518 . 397 GLY N N 105.158 0.2 1 1519 . 397 GLY H H 7.629 0.02 1 1520 . 397 GLY CA C 44.414 0.1 1 1521 . 397 GLY C C 172.563 0.1 1 1522 . 398 TYR N N 125.761 0.2 1 1523 . 398 TYR H H 9.479 0.02 1 1524 . 398 TYR CA C 58.420 0.1 1 1525 . 398 TYR CB C 39.222 0.1 1 1526 . 398 TYR C C 175.803 0.1 1 1527 . 399 ASN N N 126.872 0.2 1 1528 . 399 ASN H H 7.624 0.02 1 1529 . 399 ASN CA C 51.830 0.1 1 1530 . 399 ASN CB C 40.380 0.1 1 1531 . 399 ASN C C 172.956 0.1 1 1532 . 400 ILE N N 124.288 0.2 1 1533 . 400 ILE H H 8.121 0.02 1 1534 . 400 ILE CA C 59.209 0.1 1 1535 . 400 ILE CB C 37.815 0.1 1 1536 . 401 PRO C C 176.781 0.1 1 1537 . 402 GLN N N 121.887 0.2 1 1538 . 402 GLN H H 8.406 0.02 1 1539 . 402 GLN CA C 55.352 0.1 1 1540 . 402 GLN CB C 28.779 0.1 1 1541 . 402 GLN C C 176.262 0.1 1 1542 . 403 THR N N 115.961 0.2 1 1543 . 403 THR H H 8.132 0.02 1 1544 . 403 THR CA C 61.219 0.1 1 1545 . 403 THR CB C 69.444 0.1 1 1546 . 403 THR C C 174.180 0.1 1 1547 . 404 ASP N N 123.081 0.2 1 1548 . 404 ASP H H 8.326 0.02 1 1549 . 404 ASP CA C 53.840 0.1 1 1550 . 404 ASP CB C 40.747 0.1 1 1551 . 404 ASP C C 176.249 0.1 1 1552 . 405 GLU N N 121.867 0.2 1 1553 . 405 GLU H H 8.302 0.02 1 1554 . 405 GLU CA C 56.254 0.1 1 1555 . 405 GLU CB C 29.676 0.1 1 1556 . 405 GLU C C 176.442 0.1 1 1557 . 406 SER N N 117.767 0.2 1 1558 . 406 SER H H 8.320 0.02 1 1559 . 406 SER CA C 58.348 0.1 1 1560 . 406 SER CB C 63.567 0.1 1 stop_ save_