data_19224 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence specific backbone assignment of protein phosphatase 1B (PTP1B) residues 1-393 ; _BMRB_accession_number 19224 _BMRB_flat_file_name bmr19224.str _Entry_type original _Submission_date 2013-05-03 _Accession_date 2013-05-03 _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 Koveal Dorothy . . 2 Miller Daniel . . 3 Page Rebecca . . 4 Peti Wolfgang . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 286 "13C chemical shifts" 553 "15N chemical shifts" 286 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-09-26 update BMRB 'update entry citation' 2014-05-20 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 19223 'PTP1B (residues 1-301)' 19225 'carbohydrate binding module of the muscle glycogen-targeting subunit of Protein Phosphatase-1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Targeting the disordered C terminus of PTP1B with an allosteric inhibitor.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24845231 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Krishnan Navasona . . 2 Koveal Dorothy . . 3 Miller Daniel H. . 4 Xue Bin . . 5 Akshinthala 'Sai Dipikaa' D. . 6 Kragelj Jaka . . 7 Jensen 'Malene Ringkjobing' R. . 8 Gauss Carla-Maria M. . 9 Page Rebecca . . 10 Blackledge Martin . . 11 Muthuswamy Senthil K. . 12 Peti Wolfgang . . 13 Tonks Nicholas K. . stop_ _Journal_abbreviation 'Nat. Chem. Biol.' _Journal_name_full 'Nature chemical biology' _Journal_volume 10 _Journal_issue 7 _Journal_ISSN 1552-4469 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 558 _Page_last 566 _Year 2014 _Details . loop_ _Keyword nmr 'proline rich domain' 'protein tyrosine phosphatase' PTP1B stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name PTP1B _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PTP1B $PTP1B stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Protein Tyrosine Phosphatase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PTP1B _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PTP1B _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 398 _Mol_residue_sequence ; GHMASMEMEKEFEQIDKSGS WAAIYQDIRHEASDFPCRVA KLPKNKNRNRYRDVSPFDHS RIKLHQEDNDYINASLIKME EAQRSYILTQGPLPNTCGHF WEMVWEQKSRGVVMLNRVME KGSLKCAQYWPQKEEKEMIF EDTNLKLTLISEDIKSYYTV RQLELENLTTQETREILHFH YTTWPDFGVPESPASFLNFL FKVRESGSLSPEHGPVVVHC SAGIGRSGTFCLADTCLLLM DKRKDPSSVDIKKVLLEMRK FRMGLIQTADQLRFSYLAVI EGAKFIMGDSSVQDQWKELS HEDLEPPPEHIPPPPRPPKR ILEPHNGKCREFFPNHQWVK EETQEDKDCPIKEEKGSPLN AAPYGIESMSQDTEVRSRVV GGSLRGAQAASPAKGEPS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLY 2 2 HIS 3 3 MET 4 4 ALA 5 5 SER 6 6 MET 7 7 GLU 8 8 MET 9 9 GLU 10 10 LYS 11 11 GLU 12 12 PHE 13 13 GLU 14 14 GLN 15 15 ILE 16 16 ASP 17 17 LYS 18 18 SER 19 19 GLY 20 20 SER 21 21 TRP 22 22 ALA 23 23 ALA 24 24 ILE 25 25 TYR 26 26 GLN 27 27 ASP 28 28 ILE 29 29 ARG 30 30 HIS 31 31 GLU 32 32 ALA 33 33 SER 34 34 ASP 35 35 PHE 36 36 PRO 37 37 CYS 38 38 ARG 39 39 VAL 40 40 ALA 41 41 LYS 42 42 LEU 43 43 PRO 44 44 LYS 45 45 ASN 46 46 LYS 47 47 ASN 48 48 ARG 49 49 ASN 50 50 ARG 51 51 TYR 52 52 ARG 53 53 ASP 54 54 VAL 55 55 SER 56 56 PRO 57 57 PHE 58 58 ASP 59 59 HIS 60 60 SER 61 61 ARG 62 62 ILE 63 63 LYS 64 64 LEU 65 65 HIS 66 66 GLN 67 67 GLU 68 68 ASP 69 69 ASN 70 70 ASP 71 71 TYR 72 72 ILE 73 73 ASN 74 74 ALA 75 75 SER 76 76 LEU 77 77 ILE 78 78 LYS 79 79 MET 80 80 GLU 81 81 GLU 82 82 ALA 83 83 GLN 84 84 ARG 85 85 SER 86 86 TYR 87 87 ILE 88 88 LEU 89 89 THR 90 90 GLN 91 91 GLY 92 92 PRO 93 93 LEU 94 94 PRO 95 95 ASN 96 96 THR 97 97 CYS 98 98 GLY 99 99 HIS 100 100 PHE 101 101 TRP 102 102 GLU 103 103 MET 104 104 VAL 105 105 TRP 106 106 GLU 107 107 GLN 108 108 LYS 109 109 SER 110 110 ARG 111 111 GLY 112 112 VAL 113 113 VAL 114 114 MET 115 115 LEU 116 116 ASN 117 117 ARG 118 118 VAL 119 119 MET 120 120 GLU 121 121 LYS 122 122 GLY 123 123 SER 124 124 LEU 125 125 LYS 126 126 CYS 127 127 ALA 128 128 GLN 129 129 TYR 130 130 TRP 131 131 PRO 132 132 GLN 133 133 LYS 134 134 GLU 135 135 GLU 136 136 LYS 137 137 GLU 138 138 MET 139 139 ILE 140 140 PHE 141 141 GLU 142 142 ASP 143 143 THR 144 144 ASN 145 145 LEU 146 146 LYS 147 147 LEU 148 148 THR 149 149 LEU 150 150 ILE 151 151 SER 152 152 GLU 153 153 ASP 154 154 ILE 155 155 LYS 156 156 SER 157 157 TYR 158 158 TYR 159 159 THR 160 160 VAL 161 161 ARG 162 162 GLN 163 163 LEU 164 164 GLU 165 165 LEU 166 166 GLU 167 167 ASN 168 168 LEU 169 169 THR 170 170 THR 171 171 GLN 172 172 GLU 173 173 THR 174 174 ARG 175 175 GLU 176 176 ILE 177 177 LEU 178 178 HIS 179 179 PHE 180 180 HIS 181 181 TYR 182 182 THR 183 183 THR 184 184 TRP 185 185 PRO 186 186 ASP 187 187 PHE 188 188 GLY 189 189 VAL 190 190 PRO 191 191 GLU 192 192 SER 193 193 PRO 194 194 ALA 195 195 SER 196 196 PHE 197 197 LEU 198 198 ASN 199 199 PHE 200 200 LEU 201 201 PHE 202 202 LYS 203 203 VAL 204 204 ARG 205 205 GLU 206 206 SER 207 207 GLY 208 208 SER 209 209 LEU 210 210 SER 211 211 PRO 212 212 GLU 213 213 HIS 214 214 GLY 215 215 PRO 216 216 VAL 217 217 VAL 218 218 VAL 219 219 HIS 220 220 CYS 221 221 SER 222 222 ALA 223 223 GLY 224 224 ILE 225 225 GLY 226 226 ARG 227 227 SER 228 228 GLY 229 229 THR 230 230 PHE 231 231 CYS 232 232 LEU 233 233 ALA 234 234 ASP 235 235 THR 236 236 CYS 237 237 LEU 238 238 LEU 239 239 LEU 240 240 MET 241 241 ASP 242 242 LYS 243 243 ARG 244 244 LYS 245 245 ASP 246 246 PRO 247 247 SER 248 248 SER 249 249 VAL 250 250 ASP 251 251 ILE 252 252 LYS 253 253 LYS 254 254 VAL 255 255 LEU 256 256 LEU 257 257 GLU 258 258 MET 259 259 ARG 260 260 LYS 261 261 PHE 262 262 ARG 263 263 MET 264 264 GLY 265 265 LEU 266 266 ILE 267 267 GLN 268 268 THR 269 269 ALA 270 270 ASP 271 271 GLN 272 272 LEU 273 273 ARG 274 274 PHE 275 275 SER 276 276 TYR 277 277 LEU 278 278 ALA 279 279 VAL 280 280 ILE 281 281 GLU 282 282 GLY 283 283 ALA 284 284 LYS 285 285 PHE 286 286 ILE 287 287 MET 288 288 GLY 289 289 ASP 290 290 SER 291 291 SER 292 292 VAL 293 293 GLN 294 294 ASP 295 295 GLN 296 296 TRP 297 297 LYS 298 298 GLU 299 299 LEU 300 300 SER 301 301 HIS 302 302 GLU 303 303 ASP 304 304 LEU 305 305 GLU 306 306 PRO 307 307 PRO 308 308 PRO 309 309 GLU 310 310 HIS 311 311 ILE 312 312 PRO 313 313 PRO 314 314 PRO 315 315 PRO 316 316 ARG 317 317 PRO 318 318 PRO 319 319 LYS 320 320 ARG 321 321 ILE 322 322 LEU 323 323 GLU 324 324 PRO 325 325 HIS 326 326 ASN 327 327 GLY 328 328 LYS 329 329 CYS 330 330 ARG 331 331 GLU 332 332 PHE 333 333 PHE 334 334 PRO 335 335 ASN 336 336 HIS 337 337 GLN 338 338 TRP 339 339 VAL 340 340 LYS 341 341 GLU 342 342 GLU 343 343 THR 344 344 GLN 345 345 GLU 346 346 ASP 347 347 LYS 348 348 ASP 349 349 CYS 350 350 PRO 351 351 ILE 352 352 LYS 353 353 GLU 354 354 GLU 355 355 LYS 356 356 GLY 357 357 SER 358 358 PRO 359 359 LEU 360 360 ASN 361 361 ALA 362 362 ALA 363 363 PRO 364 364 TYR 365 365 GLY 366 366 ILE 367 367 GLU 368 368 SER 369 369 MET 370 370 SER 371 371 GLN 372 372 ASP 373 373 THR 374 374 GLU 375 375 VAL 376 376 ARG 377 377 SER 378 378 ARG 379 379 VAL 380 380 VAL 381 381 GLY 382 382 GLY 383 383 SER 384 384 LEU 385 385 ARG 386 386 GLY 387 387 ALA 388 388 GLN 389 389 ALA 390 390 ALA 391 391 SER 392 392 PRO 393 393 ALA 394 394 LYS 395 395 GLY 396 396 GLU 397 397 PRO 398 398 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 BMRB 19223 PTP1B 76.88 308 100.00 100.00 0.00e+00 BMRB 25375 PTP1B 76.88 308 100.00 100.00 0.00e+00 PDB 1A5Y "Protein Tyrosine Phosphatase 1b Cysteinyl-Phosphate Intermediate" 82.91 330 98.79 99.39 0.00e+00 PDB 1AAX "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Two Bis(Para-Phosphophenyl)methane (Bppm) Molecules" 80.65 321 99.38 99.38 0.00e+00 PDB 1BZC "Human Ptp1b Catalytic Domain Complexed With Tpi" 80.65 321 99.38 100.00 0.00e+00 PDB 1BZH "Cyclic Peptide Inhibitor Of Human Ptp1b" 74.87 298 99.33 100.00 0.00e+00 PDB 1BZJ "Human Ptp1b Complexed With Tpicooh" 74.37 297 100.00 100.00 0.00e+00 PDB 1C83 "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With 6-(Oxalyl-Amino)-1h-Indole-5-Carboxylic Acid" 74.87 298 99.33 100.00 0.00e+00 PDB 1C84 "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With 3-(Oxalyl-Amino)-Naphthalene-2-Carboxlic Acid" 74.87 298 99.33 100.00 0.00e+00 PDB 1C85 "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With 2-(Oxalyl-Amino)-Benzoic Acid" 74.87 298 99.33 100.00 0.00e+00 PDB 1C86 "Crystal Structure Of Protein Tyrosine Phosphatase 1b (R47v, D48n) Complexed With 2-(Oxalyl-Amino-4,7-Dihydro-5h- Thieno[2,3-C]p" 74.87 298 98.66 99.66 0.00e+00 PDB 1C87 "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With 2-(Oxalyl-Amino-4,7-Dihydro-5h-Thieno[2,3- C]pyran-3-Carbox" 74.87 298 99.33 100.00 0.00e+00 PDB 1C88 "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With 2-(Oxalyl-Amino)-4,5,6,7-Tetrahydro- Thieno[2,3-C]pyridine-" 74.87 298 99.33 100.00 0.00e+00 PDB 1ECV "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With 5-Iodo-2-(Oxalyl-Amino)-Benzoic Acid" 74.87 298 99.33 100.00 0.00e+00 PDB 1EEN "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Acetyl-D-A-D-Bpa-Ptyr-L-I-P-Q-Q-G" 80.65 321 99.69 99.69 0.00e+00 PDB 1EEO "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Acetyl-E-L-E-F-Ptyr-M-D-Y-E-Nh2" 80.65 321 99.69 99.69 0.00e+00 PDB 1G1F "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With A Tri-Phosphorylated Peptide (Rdi(Ptr) Etd(Ptr)(Ptr)rk) Fro" 74.87 298 99.66 99.66 0.00e+00 PDB 1G1G "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With A Mono-Phosphorylated Peptide (Etdy(Ptr) Rkggkgll) From The" 74.87 298 99.66 99.66 0.00e+00 PDB 1G1H "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With A Bis-Phosphorylated Peptide (Etd(Ptr)(Ptr) Rkggkgll) From " 74.87 298 99.66 99.66 0.00e+00 PDB 1G7F "Human Ptp1b Catalytic Domain Complexed With Pnu177496" 74.87 298 99.66 100.00 0.00e+00 PDB 1G7G "Human Ptp1b Catalytic Domain Complexes With Pnu179326" 74.87 298 100.00 100.00 0.00e+00 PDB 1GFY "Residue 259 Is A Key Determinant Of Substrate Specificity Of Protein-Tyrosine Phosphatase 1b And Alpha" 74.87 298 97.99 98.99 0.00e+00 PDB 1I57 "Crystal Structure Of Apo Human Ptp1b (C215s) Mutant" 74.87 310 99.66 99.66 0.00e+00 PDB 1JF7 "Human Ptp1b Catalytic Domain Complexed With Pnu177836" 74.87 298 100.00 100.00 0.00e+00 PDB 1KAK "Human Tyrosine Phosphatase 1b Complexed With An Inhibitor" 74.87 298 100.00 100.00 0.00e+00 PDB 1KAV "Human Tyrosine Phosphatase 1b Complexed With An Inhibitor" 74.87 298 100.00 100.00 0.00e+00 PDB 1L8G "Crystal Structure Of Ptp1b Complexed With 7-(1,1-dioxo-1h- Benzo[d]isothiazol-3-yloxymethyl)-2-(oxalyl-amino)-4,7- Dihydro-5h-t" 80.65 321 99.38 100.00 0.00e+00 PDB 1LQF "Structure Of Ptp1b In Complex With A Peptidic Bisphosphonate Inhibitor" 71.11 295 100.00 100.00 0.00e+00 PDB 1NL9 "Potent, Selective Protein Tyrosine Phosphatase 1b Inhibitor Compound 12 Using A Linked-Fragment Strategy" 80.65 321 100.00 100.00 0.00e+00 PDB 1NNY "Potent, Selective Protein Tyrosine Phosphatase 1b Inhibitor Compound 23 Using A Linked-fragment Strategy" 80.65 321 100.00 100.00 0.00e+00 PDB 1NO6 "Potent, Selective Protein Tyrosine Phosphatase 1b Inhibitor Compound 5 Using A Linked-fragment Strategy" 80.65 321 100.00 100.00 0.00e+00 PDB 1NWE "Ptp1b R47c Modified At C47 With N-[4-(2-{2-[3-(2-Bromo- Acetylamino)-Propionylamino]-3-Hydroxy-Propionylamino}- Ethyl)-Phenyl]-" 74.87 298 98.99 98.99 0.00e+00 PDB 1NWL "Crystal Structure Of The Ptp1b Complexed With Sp7343-Sp7964, A Ptyr Mimetic" 74.87 298 98.99 98.99 0.00e+00 PDB 1NZ7 "Potent, Selective Inhibitors Of Protein Tyrosine Phosphatase 1b Using A Second Phosphotyrosine Binding Site, Complexed With Com" 80.65 321 100.00 100.00 0.00e+00 PDB 1OEM "Ptp1b With The Catalytic Cysteine Oxidized To A Sulfenyl-Amide Bond" 80.65 321 100.00 100.00 0.00e+00 PDB 1OEO "Ptp1b With The Catalytic Cysteine Oxidized To Sulfonic Acid" 80.65 321 99.69 99.69 0.00e+00 PDB 1OES "Oxidation State Of Protein Tyrosine Phosphatase 1b" 80.65 321 100.00 100.00 0.00e+00 PDB 1OET "Oxidation State Of Protein Tyrosine Phosphatase 1b" 80.65 321 99.69 99.69 0.00e+00 PDB 1OEU "Oxidation State Of Protein Tyrosine Phosphatase 1b" 80.65 321 99.69 99.69 0.00e+00 PDB 1OEV "Oxidation State Of Protein Tyrosine Phosphatase 1b" 80.65 321 99.69 99.69 0.00e+00 PDB 1ONY "Oxalyl-aryl-amino Benzoic Acid Inhibitors Of Ptp1b, Compound 17" 80.65 321 100.00 100.00 0.00e+00 PDB 1ONZ "Oxalyl-Aryl-Amino Benzoic Acid Inhibitors Of Ptp1b, Compound 8b" 80.65 321 100.00 100.00 0.00e+00 PDB 1PA1 "Crystal Structure Of The C215d Mutant Of Protein Tyrosine Phosphatase 1b" 74.87 310 99.66 99.66 0.00e+00 PDB 1PH0 "Non-Carboxylic Acid-Containing Inhibitor Of Ptp1b Targeting The Second Phosphotyrosine Site" 80.65 321 100.00 100.00 0.00e+00 PDB 1PTT "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Phosphotyrosine-Containing Tetra-Peptide (Ac-Depyl-Nh2)" 80.65 321 99.38 99.69 0.00e+00 PDB 1PTU "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Phosphotyrosine-Containing Hexa-Peptide (Dadepyl-Nh2)" 80.65 321 99.38 99.69 0.00e+00 PDB 1PTV "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Phosphotyrosine" 80.65 321 99.07 99.69 0.00e+00 PDB 1PTY "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Two Phosphotyrosine Molecules" 80.65 321 99.69 99.69 0.00e+00 PDB 1PXH "Crystal Structure Of Protein Tyrosine Phosphatase 1b With Potent And Selective Bidentate Inhibitor Compound 2" 80.65 321 100.00 100.00 0.00e+00 PDB 1PYN "Dual-Site Potent, Selective Protein Tyrosine Phosphatase 1b Inhibitor Using A Linked Fragment Strategy And A Malonate Head On T" 80.65 321 100.00 100.00 0.00e+00 PDB 1Q1M "A Highly Efficient Approach To A Selective And Cell Active Ptp1b Inhibitors" 80.65 321 100.00 100.00 0.00e+00 PDB 1Q6J "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 2" 74.87 310 100.00 100.00 0.00e+00 PDB 1Q6M "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 3" 74.87 310 100.00 100.00 0.00e+00 PDB 1Q6N "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 4" 74.87 310 100.00 100.00 0.00e+00 PDB 1Q6P "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 6" 74.87 310 100.00 100.00 0.00e+00 PDB 1Q6S "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 9" 74.87 310 100.00 100.00 0.00e+00 PDB 1Q6T "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 11" 74.87 310 100.00 100.00 0.00e+00 PDB 1QXK "Monoacid-Based, Cell Permeable, Selective Inhibitors Of Protein Tyrosine Phosphatase 1b" 80.65 321 100.00 100.00 0.00e+00 PDB 1SUG "1.95 A Structure Of Apo Protein Tyrosine Phosphatase 1b" 80.65 321 100.00 100.00 0.00e+00 PDB 1T48 "Allosteric Inhibition Of Protein Tyrosine Phosphatase 1b" 74.87 298 100.00 100.00 0.00e+00 PDB 1T49 "Allosteric Inhibition Of Protein Tyrosine Phosphatase 1b" 74.87 298 100.00 100.00 0.00e+00 PDB 1T4J "Allosteric Inhibition Of Protein Tyrosine Phosphatase 1b" 74.87 298 100.00 100.00 0.00e+00 PDB 1WAX "Protein Tyrosine Phosphatase 1b With Active Site Inhibitor" 80.65 321 100.00 100.00 0.00e+00 PDB 1XBO "Ptp1b Complexed With Isoxazole Carboxylic Acid" 80.65 321 100.00 100.00 0.00e+00 PDB 2AZR "Crystal Structure Of Ptp1b With Bicyclic Thiophene Inhibitor" 75.13 299 100.00 100.00 0.00e+00 PDB 2B07 "Crystal Structure Of Ptp1b With Tricyclic Thiophene Inhibitor." 75.13 299 100.00 100.00 0.00e+00 PDB 2B4S "Crystal Structure Of A Complex Between Ptp1b And The Insulin Receptor Tyrosine Kinase" 74.87 298 99.66 99.66 0.00e+00 PDB 2BGD "Structure-based Design Of Protein Tyrosine Phosphatase-1b Inhibitors" 80.65 321 100.00 100.00 0.00e+00 PDB 2BGE "Structure-Based Design Of Protein Tyrosine Phosphatase-1b Inhibitors" 80.65 321 100.00 100.00 0.00e+00 PDB 2CM2 "Structure Of Protein Tyrosine Phosphatase 1b (P212121)" 75.88 304 98.68 98.68 0.00e+00 PDB 2CM3 "Structure Of Protein Tyrosine Phosphatase 1b (C2)" 75.88 304 98.68 98.68 0.00e+00 PDB 2CM7 "Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics" 80.65 321 100.00 100.00 0.00e+00 PDB 2CM8 "Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics" 80.65 321 100.00 100.00 0.00e+00 PDB 2CMA "Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics" 81.66 327 98.77 98.77 0.00e+00 PDB 2CMB "Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics" 75.88 304 98.68 98.68 0.00e+00 PDB 2CMC "Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics" 75.88 304 98.68 98.68 0.00e+00 PDB 2CNE "Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b" 75.88 304 98.68 98.68 0.00e+00 PDB 2CNF "Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b" 80.65 321 100.00 100.00 0.00e+00 PDB 2CNG "Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b" 80.65 321 100.00 100.00 0.00e+00 PDB 2CNH "Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b" 80.65 321 100.00 100.00 0.00e+00 PDB 2CNI "Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b" 80.65 321 100.00 100.00 0.00e+00 PDB 2F6F "The Structure Of The S295f Mutant Of Human Ptp1b" 74.87 302 99.66 99.66 0.00e+00 PDB 2F6T "Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors" 74.87 298 100.00 100.00 0.00e+00 PDB 2F6V "Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors" 74.87 298 100.00 100.00 0.00e+00 PDB 2F6W "Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors" 74.87 298 100.00 100.00 0.00e+00 PDB 2F6Y "Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors" 74.87 298 100.00 100.00 0.00e+00 PDB 2F6Z "Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors" 74.87 298 100.00 100.00 0.00e+00 PDB 2F70 "Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors" 74.87 298 100.00 100.00 0.00e+00 PDB 2F71 "Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors" 74.87 298 100.00 100.00 0.00e+00 PDB 2FJM "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 2" 74.87 310 99.66 100.00 0.00e+00 PDB 2FJN "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 2" 74.87 310 100.00 100.00 0.00e+00 PDB 2H4G "Crystal Structure Of Ptp1b With Monocyclic Thiophene Inhibitor" 75.13 299 100.00 100.00 0.00e+00 PDB 2H4K "Crystal Structure Of Ptp1b With A Monocyclic Thiophene Inhibitor" 75.13 299 100.00 100.00 0.00e+00 PDB 2HB1 "Crystal Structure Of Ptp1b With Monocyclic Thiophene Inhibitor" 75.13 299 100.00 100.00 0.00e+00 PDB 2HNP "Crystal Structure Of Human Protein Tyrosine Phosphatase 1b" 80.65 321 100.00 100.00 0.00e+00 PDB 2HNQ "Crystal Structure Of Human Protein Tyrosine Phosphatase 1b" 80.65 321 100.00 100.00 0.00e+00 PDB 2NT7 "Crystal Structure Of Ptp1b-inhibitor Complex" 75.13 299 99.67 100.00 0.00e+00 PDB 2NTA "Crystal Structure Of Ptp1b-Inhibitor Complex" 75.13 299 99.67 100.00 0.00e+00 PDB 2QBP "Crystal Structure Of Ptp1b-inhibitor Complex" 75.13 299 100.00 100.00 0.00e+00 PDB 2QBQ "Crystal Structure Of Ptp1b-Inhibitor Complex" 75.13 299 100.00 100.00 0.00e+00 PDB 2QBR "Crystal Structure Of Ptp1b-Inhibitor Complex" 75.13 299 100.00 100.00 0.00e+00 PDB 2QBS "Crystal Structure Of Ptp1b-Inhibitor Complex" 75.13 299 100.00 100.00 0.00e+00 PDB 2VEU "Crystal Structure Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-containing Inhibitor" 80.65 321 100.00 100.00 0.00e+00 PDB 2VEV "Crystal Strucutre Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-Containing Inhibitor" 80.65 321 100.00 100.00 0.00e+00 PDB 2VEW "Crystal Strucutre Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-Containing Inhibitor" 80.65 321 100.00 100.00 0.00e+00 PDB 2VEX "Crystal Strucutre Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-Containing Inhibitor" 80.65 321 100.00 100.00 0.00e+00 PDB 2VEY "Crystal Strucutre Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-Containing Inhibitor" 80.65 321 100.00 100.00 0.00e+00 PDB 2ZMM "Crystal Structure Of Ptp1b-Inhibitor Complex" 75.13 299 100.00 100.00 0.00e+00 PDB 2ZN7 "Crystal Structures Of Ptp1b-Inhibitor Complexes" 75.13 299 100.00 100.00 0.00e+00 PDB 3A5J "Crystal Structure Of Protein-Tyrosine Phosphatase 1b" 81.66 327 98.77 98.77 0.00e+00 PDB 3A5K "Crystal Structure Of Protein-Tyrosine Phosphatase 1b" 75.88 304 98.34 98.34 0.00e+00 PDB 3CWE "Ptp1b In Complex With A Phosphonic Acid Inhibitor" 71.11 290 100.00 100.00 0.00e+00 PDB 3D9C "Crystal Structure Ptp1b Complex With Aryl Seleninic Acid" 80.65 321 100.00 100.00 0.00e+00 PDB 3EAX "Crystal Structure Ptp1b Complex With Small Molecule Compound Lzp-6" 80.65 321 100.00 100.00 0.00e+00 PDB 3EB1 "Crystal Structure Ptp1b Complex With Small Molecule Inhibitor Lzp-25" 80.65 321 100.00 100.00 0.00e+00 PDB 3EU0 "Crystal Structure Of The S-Nitrosylated Cys215 Of Ptp1b" 81.66 327 98.77 98.77 0.00e+00 PDB 3I7Z "Protein Tyrosine Phosphatase 1b - Transition State Analog Fo First Catalytic Step" 80.65 321 100.00 100.00 0.00e+00 PDB 3I80 "Protein Tyrosine Phosphatase 1b - Transition State Analog Fo Second Catalytic Step" 80.65 321 100.00 100.00 0.00e+00 PDB 3QKP "Protein Tyrosine Phosphatase 1b - Apo W179f Mutant With Open Wpd-Loop" 80.65 321 99.69 100.00 0.00e+00 PDB 3QKQ "Protein Tyrosine Phosphatase 1b - W179f Mutant Bound With Vanadate" 80.65 321 99.69 100.00 0.00e+00 PDB 3SME "Structure Of Ptp1b Inactivated By H2o2BICARBONATE" 76.13 300 99.01 99.01 0.00e+00 PDB 3ZMP "Src-derived Peptide Inhibitor Complex Of Ptp1b" 81.66 329 98.77 98.77 0.00e+00 PDB 3ZMQ "Src-derived Mutant Peptide Inhibitor Complex Of Ptp1b" 81.66 329 98.77 98.77 0.00e+00 PDB 3ZV2 "Human Protein-Tyrosine Phosphatase 1b C215a, S216a Mutant" 80.40 320 99.38 99.69 0.00e+00 PDB 4BJO "Nitrate In The Active Site Of Ptp1b Is A Putative Mimetic Of The Transition State" 80.40 338 100.00 100.00 0.00e+00 PDB 4I8N "Crystal Structure Of Protein Tyrosine Phosphatase 1b In Complex With An Inhibitor [(4-{(2s)-2-(1,3-benzoxazol-2-yl)-2-[(4-fluor" 80.90 354 99.69 99.69 0.00e+00 PDB 4QAP "The Second Sphere Residue T263 Is Important For Function And Activity Of Ptp1b Through Modulating Wpd Loop" 75.13 299 99.67 99.67 0.00e+00 PDB 4QBW "The Second Sphere Residue T263 Is Important For Function And Activity Of Ptp1b Through Modulating Wpd Loop" 75.13 299 100.00 100.00 0.00e+00 PDB 4Y14 "Structure Of Protein Tyrosine Phosphatase 1b Complexed With Inhibitor (ptp1b:cpt157633)" 76.88 308 100.00 100.00 0.00e+00 PDB 4ZRT "Ptp1bc215s Bound To Nephrin Peptide Substrate" 74.87 298 99.66 99.66 0.00e+00 DBJ BAF83327 "unnamed protein product [Homo sapiens]" 98.74 435 100.00 100.00 0.00e+00 DBJ BAG11007 "protein tyrosine phosphatase, non-receptor type 1 [synthetic construct]" 98.74 435 100.00 100.00 0.00e+00 DBJ BAG38152 "unnamed protein product [Homo sapiens]" 98.74 435 100.00 100.00 0.00e+00 DBJ BAG61697 "unnamed protein product [Homo sapiens]" 80.40 362 100.00 100.00 0.00e+00 EMBL CAH90487 "hypothetical protein [Pongo abelii]" 98.74 435 98.73 99.49 0.00e+00 GB AAA60157 "non-receptor tyrosine phosphatase 1 [Homo sapiens]" 98.74 435 100.00 100.00 0.00e+00 GB AAA60158 "non-receptor tyrosine phosphatase 1, partial [Homo sapiens]" 57.54 271 100.00 100.00 1.49e-165 GB AAA60223 "phosphotyrosyl-protein phosphatase (EC 3.1.3.48) [Homo sapiens]" 98.74 435 100.00 100.00 0.00e+00 GB AAH15660 "Protein tyrosine phosphatase, non-receptor type 1 [Homo sapiens]" 98.74 435 100.00 100.00 0.00e+00 GB AAH18164 "Protein tyrosine phosphatase, non-receptor type 1 [Homo sapiens]" 98.74 435 100.00 100.00 0.00e+00 REF NP_001125254 "tyrosine-protein phosphatase non-receptor type 1 [Pongo abelii]" 98.74 435 98.73 99.49 0.00e+00 REF NP_001245122 "tyrosine-protein phosphatase non-receptor type 1 [Macaca mulatta]" 98.74 435 98.47 99.24 0.00e+00 REF NP_001265547 "tyrosine-protein phosphatase non-receptor type 1 isoform 2 [Homo sapiens]" 80.40 362 100.00 100.00 0.00e+00 REF NP_002818 "tyrosine-protein phosphatase non-receptor type 1 isoform 1 [Homo sapiens]" 98.74 435 100.00 100.00 0.00e+00 REF XP_002747713 "PREDICTED: tyrosine-protein phosphatase non-receptor type 1 [Callithrix jacchus]" 98.74 435 96.95 98.47 0.00e+00 SP P18031 "RecName: Full=Tyrosine-protein phosphatase non-receptor type 1; AltName: Full=Protein-tyrosine phosphatase 1B; Short=PTP-1B" 98.74 435 100.00 100.00 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 $PTP1B 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 $PTP1B 'recombinant technology' . Escherichia coli . pRP1B 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 $PTP1B 0.3 mM '[U-99% 2H; U-99%15N]' HEPES 50 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' TCEP 0.5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PTP1B 0.3 mM '[U-99% 2H; U-99%15N; U-99% 13C]' HEPES 50 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' TCEP 0.5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PTP1B 0.3 mM [U-15N]-Phe HEPES 50 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' TCEP 0.5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PTP1B 0.3 mM [U-15N]-Val HEPES 50 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' TCEP 0.5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_3 save_ save_2D_1H-15N_TROSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_4 save_ save_2D_1H-15N_TROSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_1 save_ save_3D_TROSY_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCA' _Sample_label $sample_2 save_ save_3D_TROSY_HNCOCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCOCA' _Sample_label $sample_2 save_ save_3D_TROSY_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCACB' _Sample_label $sample_2 save_ save_3D_TROSY_HNCOCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCOCACB' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.2 . M pH 6.8 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . 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 C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N TROSY' '3D TROSY HNCA' '3D TROSY HNCOCA' '3D TROSY HNCACB' '3D TROSY HNCOCACB' stop_ loop_ _Sample_label $sample_3 $sample_4 $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name PTP1B _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 6 6 MET H H 8.671 0.010 1 2 6 6 MET CA C 60.318 0.100 1 3 6 6 MET CB C 33.430 0.100 1 4 6 6 MET N N 119.245 0.050 1 5 7 7 GLU H H 7.889 0.010 1 6 7 7 GLU CA C 60.252 0.100 1 7 7 7 GLU CB C 30.457 0.100 1 8 7 7 GLU N N 119.635 0.050 1 9 8 8 MET H H 7.681 0.010 1 10 8 8 MET CA C 59.988 0.100 1 11 8 8 MET CB C 31.910 0.100 1 12 8 8 MET N N 120.883 0.050 1 13 10 10 LYS H H 8.360 0.010 1 14 10 10 LYS CA C 59.644 0.100 1 15 10 10 LYS N N 119.930 0.050 1 16 12 12 PHE H H 8.492 0.010 1 17 12 12 PHE CA C 62.811 0.100 1 18 12 12 PHE CB C 40.213 0.100 1 19 12 12 PHE N N 119.724 0.050 1 20 13 13 GLU H H 8.196 0.010 1 21 13 13 GLU CA C 59.989 0.100 1 22 13 13 GLU CB C 29.598 0.100 1 23 13 13 GLU N N 117.846 0.050 1 24 14 14 GLN H H 7.753 0.010 1 25 14 14 GLN CA C 59.327 0.100 1 26 14 14 GLN CB C 28.277 0.100 1 27 14 14 GLN N N 119.117 0.050 1 28 15 15 ILE H H 8.168 0.010 1 29 15 15 ILE CA C 65.459 0.100 1 30 15 15 ILE N N 123.326 0.050 1 31 16 16 ASP H H 8.401 0.010 1 32 16 16 ASP CA C 58.319 0.100 1 33 16 16 ASP CB C 41.820 0.100 1 34 16 16 ASP N N 119.751 0.050 1 35 17 17 LYS H H 8.318 0.010 1 36 17 17 LYS CA C 59.437 0.100 1 37 17 17 LYS CB C 32.043 0.100 1 38 17 17 LYS N N 118.237 0.050 1 39 18 18 SER H H 7.509 0.010 1 40 18 18 SER CA C 59.129 0.100 1 41 18 18 SER CB C 64.811 0.100 1 42 18 18 SER N N 111.486 0.050 1 43 19 19 GLY H H 7.800 0.010 1 44 19 19 GLY CA C 47.502 0.100 1 45 19 19 GLY N N 113.265 0.050 1 46 20 20 SER H H 7.776 0.010 1 47 20 20 SER CA C 59.161 0.100 1 48 20 20 SER CB C 63.754 0.100 1 49 20 20 SER N N 111.676 0.050 1 50 21 21 TRP H H 7.112 0.010 1 51 21 21 TRP CA C 60.979 0.100 1 52 21 21 TRP CB C 29.202 0.100 1 53 21 21 TRP N N 121.981 0.050 1 54 22 22 ALA H H 8.661 0.010 1 55 22 22 ALA CA C 56.090 0.100 1 56 22 22 ALA CB C 17.773 0.100 1 57 22 22 ALA N N 119.607 0.050 1 58 23 23 ALA H H 7.620 0.010 1 59 23 23 ALA CA C 55.694 0.100 1 60 23 23 ALA CB C 18.037 0.100 1 61 23 23 ALA N N 122.864 0.050 1 62 24 24 ILE H H 7.899 0.010 1 63 24 24 ILE CA C 63.820 0.100 1 64 24 24 ILE CB C 37.130 0.100 1 65 24 24 ILE N N 119.495 0.050 1 66 25 25 TYR H H 8.521 0.010 1 67 25 25 TYR CA C 62.961 0.100 1 68 25 25 TYR CB C 38.649 0.100 1 69 25 25 TYR N N 120.422 0.050 1 70 26 26 GLN H H 8.136 0.010 1 71 26 26 GLN CA C 59.063 0.100 1 72 26 26 GLN CB C 27.880 0.100 1 73 26 26 GLN N N 118.229 0.050 1 74 27 27 ASP H H 7.785 0.010 1 75 27 27 ASP CA C 58.336 0.100 1 76 27 27 ASP CB C 40.367 0.100 1 77 27 27 ASP N N 121.116 0.050 1 78 28 28 ILE H H 7.635 0.010 1 79 28 28 ILE CA C 65.465 0.100 1 80 28 28 ILE CB C 37.196 0.100 1 81 28 28 ILE N N 120.611 0.050 1 82 29 29 ARG H H 7.672 0.010 1 83 29 29 ARG CA C 60.318 0.100 1 84 29 29 ARG CB C 29.928 0.100 1 85 29 29 ARG N N 117.784 0.050 1 86 31 31 GLU H H 7.755 0.010 1 87 31 31 GLU CA C 56.751 0.100 1 88 31 31 GLU CB C 30.919 0.100 1 89 31 31 GLU N N 117.928 0.050 1 90 32 32 ALA H H 7.364 0.010 1 91 32 32 ALA CA C 53.331 0.100 1 92 32 32 ALA CB C 19.322 0.100 1 93 32 32 ALA N N 123.606 0.050 1 94 33 33 SER H H 7.939 0.010 1 95 33 33 SER CA C 59.829 0.100 1 96 33 33 SER CB C 65.169 0.100 1 97 33 33 SER N N 117.371 0.050 1 98 34 34 ASP H H 8.027 0.010 1 99 34 34 ASP CA C 54.240 0.100 1 100 34 34 ASP CB C 43.868 0.100 1 101 34 34 ASP N N 122.902 0.050 1 102 35 35 PHE H H 6.714 0.010 1 103 35 35 PHE CA C 55.724 0.100 1 104 35 35 PHE CB C 40.961 0.100 1 105 35 35 PHE N N 119.681 0.050 1 106 37 37 CYS H H 9.106 0.010 1 107 37 37 CYS CA C 56.909 0.100 1 108 37 37 CYS CB C 28.805 0.100 1 109 37 37 CYS N N 126.464 0.050 1 110 38 38 ARG H H 9.461 0.010 1 111 38 38 ARG CA C 60.384 0.100 1 112 38 38 ARG CB C 30.523 0.100 1 113 38 38 ARG N N 122.048 0.050 1 114 39 39 VAL H H 9.488 0.010 1 115 39 39 VAL CA C 67.321 0.100 1 116 39 39 VAL CB C 30.952 0.100 1 117 39 39 VAL N N 121.615 0.050 1 118 40 40 ALA H H 8.488 0.010 1 119 40 40 ALA CA C 55.033 0.100 1 120 40 40 ALA CB C 21.208 0.100 1 121 40 40 ALA N N 121.765 0.050 1 122 41 41 LYS H H 6.756 0.010 1 123 41 41 LYS CA C 55.958 0.100 1 124 41 41 LYS CB C 32.835 0.100 1 125 41 41 LYS N N 111.365 0.050 1 126 42 42 LEU H H 7.436 0.010 1 127 42 42 LEU CA C 54.732 0.100 1 128 42 42 LEU CB C 41.057 0.100 1 129 42 42 LEU N N 123.733 0.050 1 130 44 44 LYS H H 8.077 0.010 1 131 44 44 LYS CA C 58.534 0.100 1 132 44 44 LYS CB C 31.184 0.100 1 133 44 44 LYS N N 114.335 0.050 1 134 45 45 ASN H H 7.699 0.010 1 135 45 45 ASN CA C 53.448 0.100 1 136 45 45 ASN CB C 39.640 0.100 1 137 45 45 ASN N N 117.039 0.050 1 138 46 46 LYS H H 7.361 0.010 1 139 46 46 LYS CA C 61.405 0.100 1 140 46 46 LYS CB C 32.469 0.100 1 141 46 46 LYS N N 123.604 0.050 1 142 47 47 ASN H H 8.347 0.010 1 143 47 47 ASN CA C 53.448 0.100 1 144 47 47 ASN CB C 37.328 0.100 1 145 47 47 ASN N N 113.865 0.050 1 146 48 48 ARG H H 7.832 0.010 1 147 48 48 ARG CA C 56.592 0.100 1 148 48 48 ARG CB C 31.382 0.100 1 149 48 48 ARG N N 115.359 0.050 1 150 49 49 ASN H H 7.438 0.010 1 151 49 49 ASN CA C 53.051 0.100 1 152 49 49 ASN CB C 41.688 0.100 1 153 49 49 ASN N N 120.009 0.050 1 154 50 50 ARG H H 9.151 0.010 1 155 50 50 ARG CA C 59.673 0.100 1 156 50 50 ARG CB C 30.985 0.100 1 157 50 50 ARG N N 126.240 0.050 1 158 51 51 TYR H H 9.383 0.010 1 159 51 51 TYR CA C 56.619 0.100 1 160 51 51 TYR CB C 40.367 0.100 1 161 51 51 TYR N N 117.487 0.050 1 162 53 53 ASP H H 8.569 0.010 1 163 53 53 ASP CA C 53.712 0.100 1 164 53 53 ASP CB C 40.631 0.100 1 165 53 53 ASP N N 113.256 0.050 1 166 54 54 VAL H H 6.962 0.010 1 167 54 54 VAL CA C 63.225 0.100 1 168 54 54 VAL CB C 32.637 0.100 1 169 54 54 VAL N N 119.613 0.050 1 170 55 55 SER H H 7.882 0.010 1 171 55 55 SER CA C 56.222 0.100 1 172 55 55 SER CB C 65.339 0.100 1 173 55 55 SER N N 123.656 0.050 1 174 57 57 PHE H H 7.190 0.010 1 175 57 57 PHE CA C 56.186 0.100 1 176 57 57 PHE CB C 39.604 0.100 1 177 57 57 PHE N N 124.619 0.050 1 178 58 58 ASP H H 9.246 0.010 1 179 58 58 ASP CA C 59.459 0.100 1 180 58 58 ASP CB C 40.961 0.100 1 181 58 58 ASP N N 124.752 0.050 1 182 59 59 HIS H H 8.984 0.010 1 183 59 59 HIS CA C 59.856 0.100 1 184 59 59 HIS CB C 30.457 0.100 1 185 59 59 HIS N N 115.607 0.050 1 186 60 60 SER H H 6.326 0.010 1 187 60 60 SER CA C 56.156 0.100 1 188 60 60 SER CB C 64.348 0.100 1 189 60 60 SER N N 108.489 0.050 1 190 61 61 ARG H H 7.261 0.010 1 191 61 61 ARG CA C 56.252 0.100 1 192 61 61 ARG CB C 28.637 0.100 1 193 61 61 ARG N N 123.245 0.050 1 194 62 62 ILE H H 7.084 0.010 1 195 62 62 ILE CA C 57.916 0.100 1 196 62 62 ILE CB C 36.168 0.100 1 197 62 62 ILE N N 122.252 0.050 1 198 63 63 LYS H H 8.490 0.010 1 199 63 63 LYS CA C 55.760 0.100 1 200 63 63 LYS CB C 32.901 0.100 1 201 63 63 LYS N N 127.816 0.050 1 202 64 64 LEU H H 9.201 0.010 1 203 64 64 LEU CA C 54.703 0.100 1 204 64 64 LEU CB C 42.349 0.100 1 205 64 64 LEU N N 125.614 0.050 1 206 65 65 HIS H H 9.557 0.010 1 207 65 65 HIS CA C 54.703 0.100 1 208 65 65 HIS CB C 27.022 0.100 1 209 65 65 HIS N N 124.021 0.050 1 210 66 66 GLN H H 7.411 0.010 1 211 66 66 GLN CA C 55.153 0.100 1 212 66 66 GLN CB C 31.646 0.100 1 213 66 66 GLN N N 119.983 0.050 1 214 67 67 GLU H H 8.432 0.010 1 215 67 67 GLU CA C 58.733 0.100 1 216 67 67 GLU CB C 30.589 0.100 1 217 67 67 GLU N N 121.363 0.050 1 218 68 68 ASP H H 8.284 0.010 1 219 68 68 ASP CA C 57.314 0.100 1 220 68 68 ASP CB C 41.456 0.100 1 221 68 68 ASP N N 118.734 0.050 1 222 69 69 ASN H H 7.419 0.010 1 223 69 69 ASN CA C 53.976 0.100 1 224 69 69 ASN CB C 38.253 0.100 1 225 69 69 ASN N N 114.360 0.050 1 226 70 70 ASP H H 8.099 0.010 1 227 70 70 ASP CA C 53.712 0.100 1 228 70 70 ASP CB C 42.084 0.100 1 229 70 70 ASP N N 126.256 0.050 1 230 71 71 TYR H H 7.974 0.010 1 231 71 71 TYR CA C 61.640 0.100 1 232 71 71 TYR CB C 39.244 0.100 1 233 71 71 TYR N N 118.863 0.050 1 234 72 72 ILE H H 7.666 0.010 1 235 72 72 ILE CA C 59.471 0.100 1 236 72 72 ILE CB C 42.018 0.100 1 237 72 72 ILE N N 125.446 0.050 1 238 73 73 ASN H H 8.139 0.010 1 239 73 73 ASN CA C 53.087 0.100 1 240 73 73 ASN CB C 36.227 0.100 1 241 73 73 ASN N N 125.825 0.050 1 242 74 74 ALA H H 7.731 0.010 1 243 74 74 ALA CA C 52.267 0.100 1 244 74 74 ALA CB C 23.256 0.100 1 245 74 74 ALA N N 129.237 0.050 1 246 75 75 SER H H 8.917 0.010 1 247 75 75 SER CA C 58.072 0.100 1 248 75 75 SER CB C 67.519 0.100 1 249 75 75 SER N N 116.952 0.050 1 250 76 76 LEU H H 8.879 0.010 1 251 76 76 LEU CA C 54.769 0.100 1 252 76 76 LEU CB C 42.217 0.100 1 253 76 76 LEU N N 127.228 0.050 1 254 77 77 ILE H H 9.443 0.010 1 255 77 77 ILE CA C 60.913 0.100 1 256 77 77 ILE CB C 37.790 0.100 1 257 77 77 ILE N N 128.239 0.050 1 258 79 79 MET H H 8.228 0.010 1 259 79 79 MET CA C 52.590 0.100 1 260 79 79 MET CB C 29.832 0.100 1 261 79 79 MET N N 124.136 0.050 1 262 80 80 GLU H H 8.388 0.010 1 263 80 80 GLU CA C 60.715 0.100 1 264 80 80 GLU CB C 29.796 0.100 1 265 80 80 GLU N N 126.326 0.050 1 266 81 81 GLU H H 8.877 0.010 1 267 81 81 GLU CA C 59.658 0.100 1 268 81 81 GLU CB C 29.004 0.100 1 269 81 81 GLU N N 121.602 0.050 1 270 82 82 ALA H H 7.365 0.010 1 271 82 82 ALA CA C 53.117 0.100 1 272 82 82 ALA CB C 19.226 0.100 1 273 82 82 ALA N N 117.367 0.050 1 274 83 83 GLN H H 7.668 0.010 1 275 83 83 GLN CA C 56.619 0.100 1 276 83 83 GLN CB C 26.427 0.100 1 277 83 83 GLN N N 112.368 0.050 1 278 84 84 ARG H H 7.182 0.010 1 279 84 84 ARG CA C 54.732 0.100 1 280 84 84 ARG CB C 35.772 0.100 1 281 84 84 ARG N N 118.013 0.050 1 282 85 85 SER H H 7.710 0.010 1 283 85 85 SER CA C 57.197 0.100 1 284 85 85 SER CB C 66.669 0.100 1 285 85 85 SER N N 118.798 0.050 1 286 86 86 TYR H H 8.540 0.010 1 287 86 86 TYR CA C 55.760 0.100 1 288 86 86 TYR CB C 43.736 0.100 1 289 86 86 TYR N N 116.985 0.050 1 290 87 87 ILE H H 9.404 0.010 1 291 87 87 ILE CA C 60.979 0.100 1 292 87 87 ILE CB C 39.111 0.100 1 293 87 87 ILE N N 123.058 0.050 1 294 88 88 LEU H H 8.550 0.010 1 295 88 88 LEU CA C 54.240 0.100 1 296 88 88 LEU CB C 44.132 0.100 1 297 88 88 LEU N N 128.862 0.050 1 298 89 89 THR H H 8.388 0.010 1 299 89 89 THR CA C 58.468 0.100 1 300 89 89 THR CB C 72.342 0.100 1 301 89 89 THR N N 115.873 0.050 1 302 90 90 GLN H H 6.426 0.010 1 303 90 90 GLN CA C 53.249 0.100 1 304 90 90 GLN CB C 28.475 0.100 1 305 90 90 GLN N N 116.937 0.050 1 306 91 91 GLY H H 8.802 0.010 1 307 91 91 GLY CA C 45.454 0.100 1 308 91 91 GLY N N 112.844 0.050 1 309 93 93 LEU H H 7.959 0.010 1 310 93 93 LEU CA C 53.844 0.100 1 311 93 93 LEU CB C 42.217 0.100 1 312 93 93 LEU N N 124.102 0.050 1 313 95 95 ASN H H 8.575 0.010 1 314 95 95 ASN CA C 54.571 0.100 1 315 95 95 ASN CB C 37.460 0.100 1 316 95 95 ASN N N 107.046 0.050 1 317 96 96 THR H H 8.066 0.010 1 318 96 96 THR CA C 61.375 0.100 1 319 96 96 THR CB C 69.964 0.100 1 320 96 96 THR N N 111.858 0.050 1 321 97 97 CYS H H 7.563 0.010 1 322 97 97 CYS CA C 64.679 0.100 1 323 97 97 CYS CB C 28.673 0.100 1 324 97 97 CYS N N 121.576 0.050 1 325 98 98 GLY H H 8.279 0.010 1 326 98 98 GLY CA C 48.146 0.100 1 327 98 98 GLY N N 108.972 0.050 1 328 99 99 HIS H H 7.423 0.010 1 329 99 99 HIS CA C 57.639 0.100 1 330 99 99 HIS CB C 32.733 0.100 1 331 99 99 HIS N N 123.949 0.050 1 332 100 100 PHE H H 8.196 0.010 1 333 100 100 PHE CA C 62.631 0.100 1 334 100 100 PHE CB C 38.583 0.100 1 335 100 100 PHE N N 119.578 0.050 1 336 104 104 VAL H H 7.718 0.010 1 337 104 104 VAL CA C 63.952 0.100 1 338 104 104 VAL CB C 32.403 0.100 1 339 104 104 VAL N N 121.489 0.050 1 340 105 105 TRP H H 8.395 0.010 1 341 105 105 TRP CA C 56.563 0.100 1 342 105 105 TRP CB C 30.193 0.100 1 343 105 105 TRP N N 119.559 0.050 1 344 110 110 ARG H H 9.218 0.010 1 345 110 110 ARG CA C 55.760 0.100 1 346 110 110 ARG CB C 32.241 0.100 1 347 110 110 ARG N N 123.861 0.050 1 348 111 111 GLY H H 7.249 0.010 1 349 111 111 GLY CA C 44.463 0.100 1 350 111 111 GLY N N 102.486 0.050 1 351 115 115 LEU H H 7.871 0.010 1 352 115 115 LEU CA C 54.703 0.100 1 353 115 115 LEU CB C 43.009 0.100 1 354 115 115 LEU N N 124.865 0.050 1 355 116 116 ASN H H 7.442 0.010 1 356 116 116 ASN CA C 52.258 0.100 1 357 116 116 ASN CB C 42.217 0.100 1 358 116 116 ASN N N 114.738 0.050 1 359 118 118 VAL H H 8.881 0.010 1 360 118 118 VAL CA C 67.360 0.100 1 361 118 118 VAL CB C 31.910 0.100 1 362 118 118 VAL N N 121.620 0.050 1 363 122 122 GLY H H 8.542 0.010 1 364 122 122 GLY CA C 46.228 0.100 1 365 122 122 GLY N N 106.075 0.050 1 366 123 123 SER H H 7.892 0.010 1 367 123 123 SER CA C 57.742 0.100 1 368 123 123 SER CB C 65.405 0.100 1 369 123 123 SER N N 116.353 0.050 1 370 124 124 LEU H H 8.514 0.010 1 371 124 124 LEU CA C 56.045 0.100 1 372 124 124 LEU CB C 42.018 0.100 1 373 124 124 LEU N N 126.253 0.050 1 374 127 127 ALA H H 7.772 0.010 1 375 127 127 ALA CA C 52.101 0.100 1 376 127 127 ALA CB C 19.059 0.100 1 377 127 127 ALA N N 124.710 0.050 1 378 128 128 GLN H H 8.470 0.010 1 379 128 128 GLN CA C 56.047 0.100 1 380 128 128 GLN CB C 26.535 0.100 1 381 128 128 GLN N N 121.105 0.050 1 382 129 129 TYR H H 6.611 0.010 1 383 129 129 TYR CA C 57.015 0.100 1 384 129 129 TYR CB C 38.054 0.100 1 385 129 129 TYR N N 122.871 0.050 1 386 130 130 TRP H H 6.592 0.010 1 387 130 130 TRP CA C 56.024 0.100 1 388 130 130 TRP CB C 30.655 0.100 1 389 130 130 TRP N N 121.110 0.050 1 390 138 138 MET H H 8.857 0.010 1 391 138 138 MET CA C 55.760 0.100 1 392 138 138 MET CB C 38.649 0.100 1 393 138 138 MET N N 121.488 0.050 1 394 139 139 ILE H H 8.136 0.010 1 395 139 139 ILE CA C 60.450 0.100 1 396 139 139 ILE CB C 39.970 0.100 1 397 139 139 ILE N N 122.247 0.050 1 398 140 140 PHE H H 8.894 0.010 1 399 140 140 PHE CA C 57.213 0.100 1 400 140 140 PHE CB C 37.988 0.100 1 401 140 140 PHE N N 128.107 0.050 1 402 141 141 GLU H H 8.965 0.010 1 403 141 141 GLU CA C 59.525 0.100 1 404 141 141 GLU CB C 29.862 0.100 1 405 141 141 GLU N N 124.418 0.050 1 406 142 142 ASP H H 9.071 0.010 1 407 142 142 ASP CA C 56.288 0.100 1 408 142 142 ASP CB C 38.781 0.100 1 409 142 142 ASP N N 116.618 0.050 1 410 143 143 THR H H 7.456 0.010 1 411 143 143 THR CA C 60.979 0.100 1 412 143 143 THR CB C 69.303 0.100 1 413 143 143 THR N N 108.348 0.050 1 414 144 144 ASN H H 7.955 0.010 1 415 144 144 ASN CA C 54.240 0.100 1 416 144 144 ASN CB C 38.054 0.100 1 417 144 144 ASN N N 121.099 0.050 1 418 145 145 LEU H H 7.421 0.010 1 419 145 145 LEU CA C 54.059 0.100 1 420 145 145 LEU CB C 46.379 0.100 1 421 145 145 LEU N N 117.354 0.050 1 422 147 147 LEU H H 9.136 0.010 1 423 147 147 LEU CA C 53.117 0.100 1 424 147 147 LEU N N 129.979 0.050 1 425 149 149 LEU H H 8.960 0.010 1 426 149 149 LEU CA C 56.024 0.100 1 427 149 149 LEU CB C 42.811 0.100 1 428 149 149 LEU N N 128.235 0.050 1 429 150 150 ILE H H 8.856 0.010 1 430 150 150 ILE CA C 61.700 0.100 1 431 150 150 ILE N N 129.874 0.050 1 432 151 151 SER H H 7.778 0.010 1 433 151 151 SER CA C 58.402 0.100 1 434 151 151 SER CB C 65.934 0.100 1 435 151 151 SER N N 111.247 0.050 1 436 152 152 GLU H H 8.609 0.010 1 437 152 152 GLU CA C 56.354 0.100 1 438 152 152 GLU CB C 34.421 0.100 1 439 152 152 GLU N N 120.736 0.050 1 440 153 153 ASP H H 8.833 0.010 1 441 153 153 ASP CA C 53.627 0.100 1 442 153 153 ASP CB C 42.312 0.100 1 443 153 153 ASP N N 127.130 0.050 1 444 154 154 ILE H H 8.499 0.010 1 445 154 154 ILE CA C 62.782 0.100 1 446 154 154 ILE CB C 38.583 0.100 1 447 154 154 ILE N N 127.226 0.050 1 448 155 155 LYS H H 8.136 0.010 1 449 155 155 LYS CA C 54.505 0.100 1 450 155 155 LYS CB C 32.967 0.100 1 451 155 155 LYS N N 128.980 0.050 1 452 157 157 TYR H H 7.097 0.010 1 453 157 157 TYR CA C 56.103 0.100 1 454 157 157 TYR CB C 39.325 0.100 1 455 157 157 TYR N N 112.871 0.050 1 456 158 158 TYR H H 6.562 0.010 1 457 158 158 TYR CA C 56.354 0.100 1 458 158 158 TYR CB C 41.093 0.100 1 459 158 158 TYR N N 114.014 0.050 1 460 159 159 THR H H 9.407 0.010 1 461 159 159 THR CA C 61.706 0.100 1 462 159 159 THR CB C 73.862 0.100 1 463 159 159 THR N N 117.677 0.050 1 464 160 160 VAL H H 8.720 0.010 1 465 160 160 VAL CA C 60.623 0.100 1 466 160 160 VAL N N 126.363 0.050 1 467 167 167 ASN H H 8.235 0.010 1 468 167 167 ASN N N 124.591 0.050 1 469 168 168 LEU H H 8.271 0.010 1 470 168 168 LEU CA C 57.341 0.100 1 471 168 168 LEU CB C 40.961 0.100 1 472 168 168 LEU N N 126.118 0.050 1 473 169 169 THR H H 8.218 0.010 1 474 169 169 THR CA C 66.000 0.100 1 475 169 169 THR CB C 68.973 0.100 1 476 169 169 THR N N 115.178 0.050 1 477 170 170 THR H H 7.032 0.010 1 478 170 170 THR CA C 62.102 0.100 1 479 170 170 THR CB C 70.558 0.100 1 480 170 170 THR N N 109.492 0.050 1 481 171 171 GLN H H 8.366 0.010 1 482 171 171 GLN CA C 58.799 0.100 1 483 171 171 GLN CB C 26.295 0.100 1 484 171 171 GLN N N 116.740 0.050 1 485 172 172 GLU H H 7.451 0.010 1 486 172 172 GLU CA C 56.780 0.100 1 487 172 172 GLU CB C 33.364 0.100 1 488 172 172 GLU N N 119.741 0.050 1 489 173 173 THR H H 8.442 0.010 1 490 173 173 THR CA C 60.758 0.100 1 491 173 173 THR CB C 72.487 0.100 1 492 173 173 THR N N 113.753 0.050 1 493 176 176 ILE H H 8.554 0.010 1 494 176 176 ILE CA C 62.080 0.100 1 495 176 176 ILE N N 114.648 0.050 1 496 178 178 HIS H H 8.137 0.010 1 497 178 178 HIS CA C 55.443 0.100 1 498 178 178 HIS CB C 38.864 0.100 1 499 178 178 HIS N N 117.773 0.050 1 500 182 182 THR H H 8.075 0.010 1 501 182 182 THR CA C 59.063 0.100 1 502 182 182 THR CB C 64.546 0.100 1 503 182 182 THR N N 115.862 0.050 1 504 183 183 THR H H 8.325 0.010 1 505 183 183 THR CA C 59.385 0.100 1 506 183 183 THR CB C 64.049 0.100 1 507 183 183 THR N N 118.238 0.050 1 508 184 184 TRP H H 7.005 0.010 1 509 184 184 TRP CA C 60.925 0.100 1 510 184 184 TRP CB C 29.400 0.100 1 511 184 184 TRP N N 121.612 0.050 1 512 186 186 ASP H H 8.301 0.010 1 513 186 186 ASP CA C 57.411 0.100 1 514 186 186 ASP CB C 41.424 0.100 1 515 186 186 ASP N N 121.628 0.050 1 516 188 188 GLY H H 8.235 0.010 1 517 188 188 GLY CA C 45.502 0.100 1 518 188 188 GLY N N 110.198 0.050 1 519 189 189 VAL H H 8.025 0.010 1 520 189 189 VAL CA C 58.147 0.100 1 521 189 189 VAL CB C 31.184 0.100 1 522 189 189 VAL N N 114.233 0.050 1 523 194 194 ALA H H 8.490 0.010 1 524 194 194 ALA CA C 53.576 0.100 1 525 194 194 ALA CB C 19.415 0.100 1 526 194 194 ALA N N 125.737 0.050 1 527 195 195 SER H H 8.178 0.010 1 528 195 195 SER CA C 59.207 0.100 1 529 195 195 SER CB C 64.246 0.100 1 530 195 195 SER N N 114.368 0.050 1 531 196 196 PHE H H 8.470 0.010 1 532 196 196 PHE CA C 57.197 0.100 1 533 196 196 PHE CB C 34.024 0.100 1 534 196 196 PHE N N 122.850 0.050 1 535 200 200 LEU H H 8.050 0.010 1 536 200 200 LEU CA C 55.844 0.100 1 537 200 200 LEU CB C 42.150 0.100 1 538 200 200 LEU N N 122.618 0.050 1 539 201 201 PHE H H 8.122 0.010 1 540 201 201 PHE CA C 54.749 0.100 1 541 201 201 PHE CB C 30.523 0.100 1 542 201 201 PHE N N 122.920 0.050 1 543 205 205 GLU H H 8.455 0.010 1 544 205 205 GLU CA C 59.129 0.100 1 545 205 205 GLU CB C 30.259 0.100 1 546 205 205 GLU N N 121.050 0.050 1 547 206 206 SER H H 7.382 0.010 1 548 206 206 SER CA C 60.781 0.100 1 549 206 206 SER CB C 66.462 0.100 1 550 206 206 SER N N 112.356 0.050 1 551 207 207 GLY H H 7.649 0.010 1 552 207 207 GLY CA C 46.511 0.100 1 553 207 207 GLY N N 110.366 0.050 1 554 208 208 SER H H 7.832 0.010 1 555 208 208 SER CA C 63.517 0.100 1 556 208 208 SER CB C 64.348 0.100 1 557 208 208 SER N N 114.238 0.050 1 558 209 209 LEU H H 8.240 0.010 1 559 209 209 LEU CA C 54.769 0.100 1 560 209 209 LEU CB C 40.631 0.100 1 561 209 209 LEU N N 116.559 0.050 1 562 210 210 SER H H 7.336 0.010 1 563 210 210 SER CA C 57.544 0.100 1 564 210 210 SER CB C 64.084 0.100 1 565 210 210 SER N N 116.354 0.050 1 566 212 212 GLU H H 8.146 0.010 1 567 212 212 GLU CA C 57.972 0.100 1 568 212 212 GLU CB C 29.106 0.100 1 569 212 212 GLU N N 117.874 0.050 1 570 213 213 HIS H H 7.466 0.010 1 571 213 213 HIS CA C 54.600 0.100 1 572 213 213 HIS CB C 33.985 0.100 1 573 213 213 HIS N N 118.856 0.050 1 574 214 214 GLY H H 7.274 0.010 1 575 214 214 GLY CA C 44.859 0.100 1 576 214 214 GLY N N 104.809 0.050 1 577 216 216 VAL H H 8.985 0.010 1 578 216 216 VAL CA C 62.033 0.100 1 579 216 216 VAL CB C 31.646 0.100 1 580 216 216 VAL N N 125.984 0.050 1 581 217 217 VAL H H 7.678 0.010 1 582 217 217 VAL CA C 61.970 0.100 1 583 217 217 VAL CB C 32.703 0.100 1 584 217 217 VAL N N 126.672 0.050 1 585 218 218 VAL H H 9.588 0.010 1 586 218 218 VAL CA C 60.680 0.100 1 587 218 218 VAL N N 129.360 0.050 1 588 219 219 HIS H H 9.169 0.010 1 589 219 219 HIS CA C 55.930 0.100 1 590 219 219 HIS N N 121.864 0.050 1 591 220 220 CYS H H 6.021 0.010 1 592 220 220 CYS CA C 57.312 0.100 1 593 220 220 CYS CB C 29.070 0.100 1 594 220 220 CYS N N 120.221 0.050 1 595 223 223 GLY H H 8.774 0.010 1 596 223 223 GLY CA C 48.162 0.100 1 597 223 223 GLY N N 112.090 0.050 1 598 224 224 ILE H H 7.258 0.010 1 599 224 224 ILE CA C 62.264 0.100 1 600 224 224 ILE N N 108.103 0.050 1 601 227 227 SER H H 7.482 0.010 1 602 227 227 SER CA C 59.874 0.100 1 603 227 227 SER N N 115.933 0.050 1 604 228 228 GLY H H 6.351 0.010 1 605 228 228 GLY CA C 47.700 0.100 1 606 228 228 GLY N N 106.490 0.050 1 607 229 229 THR H H 7.738 0.010 1 608 229 229 THR CA C 67.453 0.100 1 609 229 229 THR CB C 68.775 0.100 1 610 229 229 THR N N 117.754 0.050 1 611 230 230 PHE H H 7.556 0.010 1 612 230 230 PHE CA C 63.027 0.100 1 613 230 230 PHE CB C 40.367 0.100 1 614 230 230 PHE N N 120.365 0.050 1 615 231 231 CYS H H 7.389 0.010 1 616 231 231 CYS CA C 62.895 0.100 1 617 231 231 CYS CB C 26.956 0.100 1 618 231 231 CYS N N 115.464 0.050 1 619 232 232 LEU H H 8.505 0.010 1 620 232 232 LEU CA C 58.997 0.100 1 621 232 232 LEU CB C 42.877 0.100 1 622 232 232 LEU N N 121.763 0.050 1 623 233 233 ALA H H 8.063 0.010 1 624 233 233 ALA CA C 55.872 0.100 1 625 233 233 ALA CB C 16.980 0.100 1 626 233 233 ALA N N 120.034 0.050 1 627 234 234 ASP H H 7.506 0.010 1 628 234 234 ASP CA C 58.982 0.100 1 629 234 234 ASP CB C 41.820 0.100 1 630 234 234 ASP N N 114.277 0.050 1 631 235 235 THR H H 8.545 0.010 1 632 235 235 THR CA C 69.404 0.100 1 633 235 235 THR CB C 68.312 0.100 1 634 235 235 THR N N 114.706 0.050 1 635 236 236 CYS H H 8.327 0.010 1 636 236 236 CYS CA C 66.396 0.100 1 637 236 236 CYS CB C 28.211 0.100 1 638 236 236 CYS N N 118.103 0.050 1 639 237 237 LEU H H 7.878 0.010 1 640 237 237 LEU CA C 58.534 0.100 1 641 237 237 LEU CB C 41.159 0.100 1 642 237 237 LEU N N 117.638 0.050 1 643 239 239 LEU H H 7.860 0.010 1 644 239 239 LEU CA C 58.403 0.100 1 645 239 239 LEU CB C 42.577 0.100 1 646 239 239 LEU N N 122.336 0.050 1 647 240 240 MET H H 7.881 0.010 1 648 240 240 MET CA C 60.186 0.100 1 649 240 240 MET CB C 33.298 0.100 1 650 240 240 MET N N 117.380 0.050 1 651 241 241 ASP H H 7.160 0.010 1 652 241 241 ASP CA C 56.582 0.100 1 653 241 241 ASP CB C 42.841 0.100 1 654 241 241 ASP N N 116.996 0.050 1 655 242 242 LYS H H 7.974 0.010 1 656 242 242 LYS CA C 58.601 0.100 1 657 242 242 LYS CB C 33.694 0.100 1 658 242 242 LYS N N 117.878 0.050 1 659 243 243 ARG H H 7.953 0.010 1 660 243 243 ARG CA C 57.279 0.100 1 661 243 243 ARG CB C 31.184 0.100 1 662 243 243 ARG N N 117.265 0.050 1 663 244 244 LYS H H 7.974 0.010 1 664 244 244 LYS CA C 57.657 0.100 1 665 244 244 LYS CB C 30.919 0.100 1 666 244 244 LYS N N 118.796 0.050 1 667 247 247 SER H H 8.091 0.010 1 668 247 247 SER CA C 60.715 0.100 1 669 247 247 SER CB C 63.820 0.100 1 670 247 247 SER N N 112.992 0.050 1 671 248 248 SER H H 7.645 0.010 1 672 248 248 SER CA C 59.459 0.100 1 673 248 248 SER CB C 64.943 0.100 1 674 248 248 SER N N 115.345 0.050 1 675 249 249 VAL H H 7.178 0.010 1 676 249 249 VAL CA C 63.915 0.100 1 677 249 249 VAL CB C 32.006 0.100 1 678 249 249 VAL N N 123.720 0.050 1 679 250 250 ASP H H 8.407 0.010 1 680 250 250 ASP CA C 52.258 0.100 1 681 250 250 ASP CB C 42.150 0.100 1 682 250 250 ASP N N 129.547 0.050 1 683 251 251 ILE H H 8.416 0.010 1 684 251 251 ILE CA C 65.934 0.100 1 685 251 251 ILE CB C 38.187 0.100 1 686 251 251 ILE N N 126.586 0.050 1 687 252 252 LYS H H 7.836 0.010 1 688 252 252 LYS CA C 60.913 0.100 1 689 252 252 LYS CB C 30.919 0.100 1 690 252 252 LYS N N 118.237 0.050 1 691 253 253 LYS H H 7.123 0.010 1 692 253 253 LYS CA C 60.018 0.100 1 693 253 253 LYS CB C 32.601 0.100 1 694 253 253 LYS N N 117.616 0.050 1 695 254 254 VAL H H 8.058 0.010 1 696 254 254 VAL CA C 67.072 0.100 1 697 254 254 VAL N N 121.929 0.050 1 698 258 258 MET H H 8.582 0.010 1 699 258 258 MET CA C 61.573 0.100 1 700 258 258 MET CB C 33.694 0.100 1 701 258 258 MET N N 119.389 0.050 1 702 259 259 ARG H H 8.546 0.010 1 703 259 259 ARG CA C 58.667 0.100 1 704 259 259 ARG CB C 30.655 0.100 1 705 259 259 ARG N N 117.985 0.050 1 706 260 260 LYS H H 7.623 0.010 1 707 260 260 LYS CA C 59.327 0.100 1 708 260 260 LYS CB C 31.844 0.100 1 709 260 260 LYS N N 119.333 0.050 1 710 261 261 PHE H H 8.153 0.010 1 711 261 261 PHE CA C 60.120 0.100 1 712 261 261 PHE CB C 41.688 0.100 1 713 261 261 PHE N N 112.919 0.050 1 714 262 262 ARG H H 7.457 0.010 1 715 262 262 ARG CA C 57.279 0.100 1 716 262 262 ARG CB C 32.505 0.100 1 717 262 262 ARG N N 120.874 0.050 1 718 265 265 LEU H H 6.357 0.010 1 719 265 265 LEU CA C 56.506 0.100 1 720 265 265 LEU N N 115.249 0.050 1 721 266 266 ILE H H 8.322 0.010 1 722 266 266 ILE CA C 65.200 0.100 1 723 266 266 ILE N N 115.864 0.050 1 724 268 268 THR H H 6.662 0.010 1 725 268 268 THR CA C 58.534 0.100 1 726 268 268 THR CB C 73.795 0.100 1 727 268 268 THR N N 105.426 0.050 1 728 269 269 ALA H H 8.598 0.010 1 729 269 269 ALA CA C 54.901 0.100 1 730 269 269 ALA CB C 17.706 0.100 1 731 269 269 ALA N N 123.717 0.050 1 732 270 270 ASP H H 7.829 0.010 1 733 270 270 ASP CA C 57.477 0.100 1 734 270 270 ASP CB C 40.301 0.100 1 735 270 270 ASP N N 116.434 0.050 1 736 271 271 GLN H H 7.792 0.010 1 737 271 271 GLN CA C 59.592 0.100 1 738 271 271 GLN CB C 28.541 0.100 1 739 271 271 GLN N N 120.094 0.050 1 740 272 272 LEU H H 7.526 0.010 1 741 272 272 LEU CA C 59.068 0.100 1 742 272 272 LEU CB C 41.226 0.100 1 743 272 272 LEU N N 124.254 0.050 1 744 273 273 ARG H H 7.880 0.010 1 745 273 273 ARG CA C 60.306 0.100 1 746 273 273 ARG CB C 29.070 0.100 1 747 273 273 ARG N N 121.492 0.050 1 748 274 274 PHE H H 8.173 0.010 1 749 274 274 PHE CA C 62.432 0.100 1 750 274 274 PHE CB C 40.102 0.100 1 751 274 274 PHE N N 117.874 0.050 1 752 275 275 SER H H 7.925 0.010 1 753 275 275 SER CA C 56.156 0.100 1 754 275 275 SER CB C 64.679 0.100 1 755 275 275 SER N N 115.366 0.050 1 756 277 277 LEU H H 8.387 0.010 1 757 277 277 LEU CA C 58.336 0.100 1 758 277 277 LEU CB C 42.349 0.100 1 759 277 277 LEU N N 119.105 0.050 1 760 278 278 ALA H H 8.486 0.010 1 761 278 278 ALA CA C 60.040 0.100 1 762 278 278 ALA CB C 16.782 0.100 1 763 278 278 ALA N N 119.725 0.050 1 764 279 279 VAL H H 7.740 0.010 1 765 279 279 VAL CA C 67.388 0.100 1 766 279 279 VAL N N 118.789 0.050 1 767 280 280 ILE H H 8.447 0.010 1 768 280 280 ILE CA C 59.063 0.100 1 769 280 280 ILE CB C 39.045 0.100 1 770 280 280 ILE N N 120.243 0.050 1 771 282 282 GLY H H 8.679 0.010 1 772 282 282 GLY CA C 48.294 0.100 1 773 282 282 GLY N N 109.804 0.050 1 774 283 283 ALA H H 8.544 0.010 1 775 283 283 ALA CA C 55.412 0.100 1 776 283 283 ALA CB C 18.896 0.100 1 777 283 283 ALA N N 125.251 0.050 1 778 284 284 LYS H H 7.495 0.010 1 779 284 284 LYS CA C 59.874 0.100 1 780 284 284 LYS CB C 32.373 0.100 1 781 284 284 LYS N N 116.408 0.050 1 782 285 285 PHE H H 7.607 0.010 1 783 285 285 PHE CA C 60.318 0.100 1 784 285 285 PHE CB C 39.508 0.100 1 785 285 285 PHE N N 118.243 0.050 1 786 286 286 ILE H H 7.882 0.010 1 787 286 286 ILE CA C 63.555 0.100 1 788 286 286 ILE CB C 38.054 0.100 1 789 286 286 ILE N N 118.654 0.050 1 790 287 287 MET H H 8.074 0.010 1 791 287 287 MET CA C 56.304 0.100 1 792 287 287 MET N N 118.390 0.050 1 793 288 288 GLY H H 7.567 0.010 1 794 288 288 GLY CA C 46.048 0.100 1 795 288 288 GLY N N 108.121 0.050 1 796 289 289 ASP H H 8.031 0.010 1 797 289 289 ASP CA C 54.581 0.100 1 798 289 289 ASP CB C 41.622 0.100 1 799 289 289 ASP N N 121.096 0.050 1 800 290 290 SER H H 8.293 0.010 1 801 290 290 SER CA C 60.076 0.100 1 802 290 290 SER CB C 63.703 0.100 1 803 290 290 SER N N 118.509 0.050 1 804 291 291 SER H H 8.387 0.010 1 805 291 291 SER CA C 60.356 0.100 1 806 291 291 SER CB C 63.982 0.100 1 807 291 291 SER N N 118.610 0.050 1 808 292 292 VAL H H 7.737 0.010 1 809 292 292 VAL CA C 63.934 0.100 1 810 292 292 VAL CB C 32.109 0.100 1 811 292 292 VAL N N 121.492 0.050 1 812 296 296 TRP H H 8.027 0.010 1 813 296 296 TRP CA C 57.940 0.100 1 814 296 296 TRP CB C 29.004 0.100 1 815 296 296 TRP N N 121.274 0.050 1 816 297 297 LYS H H 7.714 0.010 1 817 297 297 LYS CA C 58.270 0.100 1 818 297 297 LYS CB C 32.835 0.100 1 819 297 297 LYS N N 122.011 0.050 1 820 298 298 GLU H H 8.012 0.010 1 821 298 298 GLU CA C 57.139 0.100 1 822 298 298 GLU CB C 27.854 0.100 1 823 298 298 GLU N N 121.227 0.050 1 824 299 299 LEU H H 8.039 0.010 1 825 299 299 LEU CA C 54.306 0.100 1 826 299 299 LEU CB C 43.736 0.100 1 827 299 299 LEU N N 122.400 0.050 1 828 301 301 HIS H H 7.949 0.010 1 829 301 301 HIS CA C 58.579 0.100 1 830 301 301 HIS N N 123.335 0.050 1 831 302 302 GLU CA C 56.995 0.100 1 832 302 302 GLU CB C 32.798 0.100 1 833 303 303 ASP H H 8.276 0.010 1 834 303 303 ASP CA C 55.082 0.100 1 835 303 303 ASP CB C 41.435 0.100 1 836 303 303 ASP N N 120.955 0.050 1 837 304 304 LEU H H 8.003 0.010 1 838 304 304 LEU CA C 55.443 0.100 1 839 304 304 LEU CB C 42.292 0.100 1 840 304 304 LEU N N 122.477 0.050 1 841 305 305 GLU H H 8.164 0.010 1 842 305 305 GLU CA C 54.668 0.100 1 843 305 305 GLU CB C 29.832 0.100 1 844 305 305 GLU N N 123.242 0.050 1 845 308 308 PRO CA C 63.545 0.100 1 846 308 308 PRO CB C 32.007 0.100 1 847 309 309 GLU H H 8.377 0.010 1 848 309 309 GLU CA C 57.196 0.100 1 849 309 309 GLU CB C 30.425 0.100 1 850 309 309 GLU N N 120.755 0.050 1 851 310 310 HIS H H 8.313 0.010 1 852 310 310 HIS CA C 56.162 0.100 1 853 310 310 HIS CB C 30.170 0.100 1 854 310 310 HIS N N 120.423 0.050 1 855 311 311 ILE H H 8.036 0.010 1 856 311 311 ILE CA C 58.977 0.100 1 857 311 311 ILE CB C 38.534 0.100 1 858 311 311 ILE N N 125.238 0.050 1 859 316 316 ARG H H 8.239 0.010 1 860 316 316 ARG CA C 54.179 0.100 1 861 316 316 ARG CB C 30.227 0.100 1 862 316 316 ARG N N 122.484 0.050 1 863 319 319 LYS H H 8.229 0.010 1 864 319 319 LYS CA C 56.909 0.100 1 865 319 319 LYS CB C 30.491 0.100 1 866 319 319 LYS N N 122.037 0.050 1 867 320 320 ARG H H 8.212 0.010 1 868 320 320 ARG CA C 56.478 0.100 1 869 320 320 ARG CB C 30.721 0.100 1 870 320 320 ARG N N 121.984 0.050 1 871 321 321 ILE H H 8.187 0.010 1 872 321 321 ILE CA C 61.505 0.100 1 873 321 321 ILE CB C 38.489 0.100 1 874 321 321 ILE N N 123.733 0.050 1 875 322 322 LEU H H 8.239 0.010 1 876 322 322 LEU CA C 55.280 0.100 1 877 322 322 LEU CB C 42.226 0.100 1 878 322 322 LEU N N 127.085 0.050 1 879 323 323 GLU H H 8.245 0.010 1 880 323 323 GLU CA C 54.725 0.100 1 881 323 323 GLU CB C 30.161 0.100 1 882 323 323 GLU N N 123.706 0.050 1 883 325 325 HIS CA C 64.005 0.100 1 884 325 325 HIS CB C 32.007 0.100 1 885 326 326 ASN H H 8.316 0.010 1 886 326 326 ASN CA C 53.834 0.100 1 887 326 326 ASN CB C 38.930 0.100 1 888 326 326 ASN N N 118.235 0.050 1 889 327 327 GLY H H 8.330 0.010 1 890 327 327 GLY CA C 45.905 0.100 1 891 327 327 GLY N N 109.704 0.050 1 892 330 330 ARG H H 8.278 0.010 1 893 330 330 ARG CA C 59.217 0.100 1 894 330 330 ARG CB C 28.249 0.100 1 895 330 330 ARG N N 120.639 0.050 1 896 331 331 GLU H H 8.348 0.010 1 897 331 331 GLU CA C 56.937 0.100 1 898 331 331 GLU CB C 30.512 0.100 1 899 331 331 GLU N N 123.966 0.050 1 900 332 332 PHE H H 8.035 0.010 1 901 332 332 PHE CA C 58.000 0.100 1 902 332 332 PHE CB C 39.919 0.100 1 903 332 332 PHE N N 121.063 0.050 1 904 333 333 PHE H H 8.066 0.010 1 905 333 333 PHE CA C 55.939 0.100 1 906 333 333 PHE CB C 39.589 0.100 1 907 333 333 PHE N N 123.359 0.050 1 908 337 337 GLN CA C 56.449 0.100 1 909 337 337 GLN CB C 29.325 0.100 1 910 338 338 TRP H H 8.035 0.010 1 911 338 338 TRP CA C 57.857 0.100 1 912 338 338 TRP CB C 29.620 0.100 1 913 338 338 TRP N N 122.690 0.050 1 914 339 339 VAL H H 7.780 0.010 1 915 339 339 VAL CA C 62.466 0.100 1 916 339 339 VAL CB C 33.128 0.100 1 917 339 339 VAL N N 122.702 0.050 1 918 340 340 LYS H H 8.101 0.010 1 919 340 340 LYS CA C 56.937 0.100 1 920 340 340 LYS CB C 33.035 0.100 1 921 340 340 LYS N N 125.612 0.050 1 922 341 341 GLU H H 8.263 0.010 1 923 341 341 GLU CA C 56.621 0.100 1 924 341 341 GLU CB C 30.161 0.100 1 925 341 341 GLU N N 123.437 0.050 1 926 342 342 GLU H H 8.416 0.010 1 927 342 342 GLU CA C 57.081 0.100 1 928 342 342 GLU CB C 30.426 0.100 1 929 342 342 GLU N N 123.023 0.050 1 930 343 343 THR H H 8.192 0.010 1 931 343 343 THR CA C 62.339 0.100 1 932 343 343 THR CB C 70.443 0.100 1 933 343 343 THR N N 115.998 0.050 1 934 344 344 GLN H H 8.413 0.010 1 935 344 344 GLN CA C 56.449 0.100 1 936 344 344 GLN CB C 30.314 0.100 1 937 344 344 GLN N N 123.115 0.050 1 938 345 345 GLU H H 8.412 0.010 1 939 345 345 GLU CA C 57.167 0.100 1 940 345 345 GLU CB C 30.248 0.100 1 941 345 345 GLU N N 122.752 0.050 1 942 346 346 ASP H H 8.336 0.010 1 943 346 346 ASP CA C 55.041 0.100 1 944 346 346 ASP CB C 41.369 0.100 1 945 346 346 ASP N N 122.053 0.050 1 946 347 347 LYS H H 8.126 0.010 1 947 347 347 LYS CA C 57.081 0.100 1 948 347 347 LYS CB C 32.864 0.100 1 949 347 347 LYS N N 122.006 0.050 1 950 350 350 PRO CA C 63.919 0.100 1 951 350 350 PRO CB C 32.271 0.100 1 952 351 351 ILE H H 8.073 0.010 1 953 351 351 ILE CA C 61.649 0.100 1 954 351 351 ILE CB C 38.534 0.100 1 955 351 351 ILE N N 121.512 0.050 1 956 352 352 LYS H H 8.296 0.010 1 957 352 352 LYS CA C 56.610 0.100 1 958 352 352 LYS CB C 33.035 0.100 1 959 352 352 LYS N N 126.519 0.050 1 960 353 353 GLU H H 8.362 0.010 1 961 353 353 GLU CA C 57.015 0.100 1 962 353 353 GLU CB C 30.512 0.100 1 963 353 353 GLU N N 123.483 0.050 1 964 354 354 GLU H H 8.438 0.010 1 965 354 354 GLU CA C 56.867 0.100 1 966 354 354 GLU CB C 30.427 0.100 1 967 354 354 GLU N N 123.741 0.050 1 968 355 355 LYS H H 8.385 0.010 1 969 355 355 LYS CA C 56.986 0.100 1 970 355 355 LYS CB C 32.951 0.100 1 971 355 355 LYS N N 123.492 0.050 1 972 356 356 GLY H H 8.364 0.010 1 973 356 356 GLY CA C 45.502 0.100 1 974 356 356 GLY N N 110.363 0.050 1 975 357 357 SER H H 8.133 0.010 1 976 357 357 SER CA C 56.851 0.100 1 977 357 357 SER CB C 63.982 0.100 1 978 357 357 SER N N 117.254 0.050 1 979 358 358 PRO CA C 63.948 0.100 1 980 358 358 PRO CB C 32.139 0.100 1 981 359 359 LEU H H 8.182 0.010 1 982 359 359 LEU CA C 56.018 0.100 1 983 359 359 LEU CB C 42.028 0.100 1 984 359 359 LEU N N 121.987 0.050 1 985 360 360 ASN H H 8.202 0.010 1 986 360 360 ASN CA C 53.662 0.100 1 987 360 360 ASN CB C 39.193 0.100 1 988 360 360 ASN N N 119.308 0.050 1 989 361 361 ALA H H 8.025 0.010 1 990 361 361 ALA CA C 52.714 0.100 1 991 361 361 ALA CB C 19.568 0.100 1 992 361 361 ALA N N 124.531 0.050 1 993 362 362 ALA H H 8.134 0.010 1 994 362 362 ALA CA C 50.929 0.100 1 995 362 362 ALA CB C 18.294 0.100 1 996 362 362 ALA N N 124.955 0.050 1 997 363 363 PRO CA C 63.784 0.100 1 998 363 363 PRO CB C 31.875 0.100 1 999 364 364 TYR H H 8.044 0.010 1 1000 364 364 TYR CA C 58.378 0.100 1 1001 364 364 TYR CB C 38.798 0.100 1 1002 364 364 TYR N N 120.107 0.050 1 1003 365 365 GLY H H 8.139 0.010 1 1004 365 365 GLY CA C 45.790 0.100 1 1005 365 365 GLY N N 111.179 0.050 1 1006 366 366 ILE H H 7.857 0.010 1 1007 366 366 ILE CA C 61.965 0.100 1 1008 366 366 ILE CB C 38.666 0.100 1 1009 366 366 ILE N N 120.398 0.050 1 1010 367 367 GLU H H 8.549 0.010 1 1011 367 367 GLU CA C 57.521 0.100 1 1012 367 367 GLU CB C 30.029 0.100 1 1013 367 367 GLU N N 124.748 0.050 1 1014 368 368 SER H H 8.180 0.010 1 1015 368 368 SER CA C 59.063 0.100 1 1016 368 368 SER CB C 64.048 0.100 1 1017 368 368 SER N N 116.880 0.050 1 1018 369 369 MET H H 8.153 0.010 1 1019 369 369 MET CA C 56.888 0.100 1 1020 369 369 MET CB C 30.491 0.100 1 1021 369 369 MET N N 123.313 0.050 1 1022 370 370 SER H H 8.126 0.010 1 1023 370 370 SER CA C 59.092 0.100 1 1024 370 370 SER CB C 64.127 0.100 1 1025 370 370 SER N N 116.489 0.050 1 1026 371 371 GLN H H 8.378 0.010 1 1027 371 371 GLN CA C 56.535 0.100 1 1028 371 371 GLN CB C 29.634 0.100 1 1029 371 371 GLN N N 122.536 0.050 1 1030 372 372 ASP H H 8.296 0.010 1 1031 372 372 ASP CA C 55.185 0.100 1 1032 372 372 ASP CB C 41.435 0.100 1 1033 372 372 ASP N N 121.720 0.050 1 1034 373 373 THR H H 8.007 0.010 1 1035 373 373 THR CA C 63.086 0.100 1 1036 373 373 THR CB C 70.114 0.100 1 1037 373 373 THR N N 114.601 0.050 1 1038 374 374 GLU H H 8.257 0.010 1 1039 374 374 GLU CA C 57.483 0.100 1 1040 374 374 GLU CB C 30.227 0.100 1 1041 374 374 GLU N N 123.553 0.050 1 1042 375 375 VAL H H 8.051 0.010 1 1043 375 375 VAL CA C 63.718 0.100 1 1044 375 375 VAL CB C 32.403 0.100 1 1045 375 375 VAL N N 121.978 0.050 1 1046 376 376 ARG H H 8.254 0.010 1 1047 376 376 ARG CA C 56.995 0.100 1 1048 376 376 ARG CB C 30.623 0.100 1 1049 376 376 ARG N N 124.232 0.050 1 1050 378 378 ARG H H 8.101 0.010 1 1051 378 378 ARG CA C 56.679 0.100 1 1052 378 378 ARG CB C 30.095 0.100 1 1053 378 378 ARG N N 119.505 0.050 1 1054 379 379 VAL H H 8.043 0.010 1 1055 379 379 VAL CA C 62.999 0.100 1 1056 379 379 VAL CB C 32.564 0.100 1 1057 379 379 VAL N N 121.978 0.050 1 1058 380 380 VAL H H 8.206 0.010 1 1059 380 380 VAL CA C 63.108 0.100 1 1060 380 380 VAL CB C 32.798 0.100 1 1061 380 380 VAL N N 125.072 0.050 1 1062 381 381 GLY H H 8.429 0.010 1 1063 381 381 GLY CA C 45.847 0.100 1 1064 381 381 GLY N N 113.403 0.050 1 1065 382 382 GLY H H 8.193 0.010 1 1066 382 382 GLY CA C 45.784 0.100 1 1067 382 382 GLY N N 109.238 0.050 1 1068 383 383 SER H H 8.166 0.010 1 1069 383 383 SER CA C 58.977 0.100 1 1070 383 383 SER CB C 64.246 0.100 1 1071 383 383 SER N N 115.973 0.050 1 1072 384 384 LEU H H 8.248 0.010 1 1073 384 384 LEU CA C 55.903 0.100 1 1074 384 384 LEU CB C 42.050 0.100 1 1075 384 384 LEU N N 124.448 0.050 1 1076 385 385 ARG H H 8.221 0.010 1 1077 385 385 ARG CA C 56.928 0.100 1 1078 385 385 ARG CB C 30.623 0.100 1 1079 385 385 ARG N N 121.947 0.050 1 1080 386 386 GLY H H 8.275 0.010 1 1081 386 386 GLY CA C 45.560 0.100 1 1082 386 386 GLY N N 110.368 0.050 1 1083 387 387 ALA H H 8.103 0.010 1 1084 387 387 ALA CA C 53.116 0.100 1 1085 387 387 ALA CB C 19.349 0.100 1 1086 387 387 ALA N N 124.240 0.050 1 1087 388 388 GLN H H 8.260 0.010 1 1088 388 388 GLN CA C 56.219 0.100 1 1089 388 388 GLN CB C 29.568 0.100 1 1090 388 388 GLN N N 119.724 0.050 1 1091 389 389 ALA H H 8.170 0.010 1 1092 389 389 ALA CA C 52.829 0.100 1 1093 389 389 ALA CB C 19.436 0.100 1 1094 389 389 ALA N N 125.721 0.050 1 1095 390 390 ALA H H 8.172 0.010 1 1096 390 390 ALA CA C 52.727 0.100 1 1097 390 390 ALA CB C 19.481 0.100 1 1098 390 390 ALA N N 123.734 0.050 1 1099 391 391 SER H H 8.199 0.010 1 1100 391 391 SER CA C 59.063 0.100 1 1101 391 391 SER CB C 64.048 0.100 1 1102 391 391 SER N N 116.996 0.050 1 1103 392 392 PRO CA C 63.719 0.100 1 1104 392 392 PRO CB C 32.139 0.100 1 1105 393 393 ALA H H 8.280 0.010 1 1106 393 393 ALA CA C 52.935 0.100 1 1107 393 393 ALA CB C 19.283 0.100 1 1108 393 393 ALA N N 124.980 0.050 1 1109 394 394 LYS H H 8.235 0.010 1 1110 394 394 LYS CA C 56.909 0.100 1 1111 394 394 LYS CB C 32.930 0.100 1 1112 394 394 LYS N N 121.304 0.050 1 1113 395 395 GLY H H 8.279 0.010 1 1114 395 395 GLY CA C 45.560 0.100 1 1115 395 395 GLY N N 110.627 0.050 1 1116 396 396 GLU H H 8.123 0.010 1 1117 396 396 GLU CA C 54.840 0.100 1 1118 396 396 GLU CB C 29.766 0.100 1 1119 396 396 GLU N N 122.091 0.050 1 1120 397 397 PRO CA C 64.114 0.100 1 1121 397 397 PRO CB C 31.941 0.100 1 1122 398 398 SER H H 7.919 0.010 1 1123 398 398 SER CA C 60.422 0.100 1 1124 398 398 SER CB C 65.301 0.100 1 1125 398 398 SER N N 122.236 0.050 1 stop_ save_