data_19223 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence specific backbone assignment of the catalytic domain of protein phosphatase 1B (PTP1B) in the ligand-free state ; _BMRB_accession_number 19223 _BMRB_flat_file_name bmr19223.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 'PTP1B residues 1-301' 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" 232 "13C chemical shifts" 512 "15N chemical shifts" 232 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-09-26 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 19224 'PTP1B (residues 1-393)' 19225 'carbohydrate binding module of the muscle glycogen-targeting subunit of Protein Phosphatase-1' stop_ _Original_release_date 2014-09-26 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 '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 308 _Mol_residue_sequence ; GHMASMEMEKEFEQIDKSGS WAAIYQDIRHEASDFPCRVA KLPKNKNRNRYRDVSPFDHS RIKLHQEDNDYINASLIKME EAQRSYILTQGPLPNTCGHF WEMVWEQKSRGVVMLNRVME KGSLKCAQYWPQKEEKEMIF EDTNLKLTLISEDIKSYYTV RQLELENLTTQETREILHFH YTTWPDFGVPESPASFLNFL FKVRESGSLSPEHGPVVVHC SAGIGRSGTFCLADTCLLLM DKRKDPSSVDIKKVLLEMRK FRMGLIQTADQLRFSYLAVI EGAKFIMGDSSVQDQWKELS HEDLEPHN ; 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 HIS 308 308 ASN 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 19224 PTP1B 99.35 398 100.00 100.00 0.00e+00 BMRB 25375 PTP1B 100.00 308 100.00 100.00 0.00e+00 PDB 1A5Y "Protein Tyrosine Phosphatase 1b Cysteinyl-Phosphate Intermediate" 97.73 330 98.67 99.34 0.00e+00 PDB 1AAX "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Two Bis(Para-Phosphophenyl)methane (Bppm) Molecules" 97.73 321 99.67 99.67 0.00e+00 PDB 1BZC "Human Ptp1b Catalytic Domain Complexed With Tpi" 97.73 321 99.34 100.00 0.00e+00 PDB 1BZH "Cyclic Peptide Inhibitor Of Human Ptp1b" 96.75 298 99.33 100.00 0.00e+00 PDB 1BZJ "Human Ptp1b Complexed With Tpicooh" 96.10 297 100.00 100.00 0.00e+00 PDB 1C83 "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With 6-(Oxalyl-Amino)-1h-Indole-5-Carboxylic Acid" 96.75 298 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" 96.75 298 99.33 100.00 0.00e+00 PDB 1C85 "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With 2-(Oxalyl-Amino)-Benzoic Acid" 96.75 298 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" 96.75 298 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" 96.75 298 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-" 96.75 298 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" 96.75 298 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" 97.73 321 99.67 99.67 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" 97.73 321 99.67 99.67 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" 96.75 298 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" 96.75 298 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 " 96.75 298 99.66 99.66 0.00e+00 PDB 1G7F "Human Ptp1b Catalytic Domain Complexed With Pnu177496" 96.75 298 99.66 100.00 0.00e+00 PDB 1G7G "Human Ptp1b Catalytic Domain Complexes With Pnu179326" 96.75 298 100.00 100.00 0.00e+00 PDB 1GFY "Residue 259 Is A Key Determinant Of Substrate Specificity Of Protein-Tyrosine Phosphatase 1b And Alpha" 96.75 298 97.99 98.99 0.00e+00 PDB 1I57 "Crystal Structure Of Apo Human Ptp1b (C215s) Mutant" 96.75 310 99.66 99.66 0.00e+00 PDB 1JF7 "Human Ptp1b Catalytic Domain Complexed With Pnu177836" 96.75 298 100.00 100.00 0.00e+00 PDB 1KAK "Human Tyrosine Phosphatase 1b Complexed With An Inhibitor" 96.75 298 100.00 100.00 0.00e+00 PDB 1KAV "Human Tyrosine Phosphatase 1b Complexed With An Inhibitor" 96.75 298 100.00 100.00 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" 97.73 321 99.34 100.00 0.00e+00 PDB 1LQF "Structure Of Ptp1b In Complex With A Peptidic Bisphosphonate Inhibitor" 91.88 295 100.00 100.00 0.00e+00 PDB 1NL9 "Potent, Selective Protein Tyrosine Phosphatase 1b Inhibitor Compound 12 Using A Linked-Fragment Strategy" 97.73 321 100.00 100.00 0.00e+00 PDB 1NNY "Potent, Selective Protein Tyrosine Phosphatase 1b Inhibitor Compound 23 Using A Linked-fragment Strategy" 97.73 321 100.00 100.00 0.00e+00 PDB 1NO6 "Potent, Selective Protein Tyrosine Phosphatase 1b Inhibitor Compound 5 Using A Linked-fragment Strategy" 97.73 321 100.00 100.00 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]-" 96.75 298 98.99 98.99 0.00e+00 PDB 1NWL "Crystal Structure Of The Ptp1b Complexed With Sp7343-Sp7964, A Ptyr Mimetic" 96.75 298 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" 97.73 321 100.00 100.00 0.00e+00 PDB 1OEM "Ptp1b With The Catalytic Cysteine Oxidized To A Sulfenyl-Amide Bond" 97.73 321 100.00 100.00 0.00e+00 PDB 1OEO "Ptp1b With The Catalytic Cysteine Oxidized To Sulfonic Acid" 97.73 321 99.67 99.67 0.00e+00 PDB 1OES "Oxidation State Of Protein Tyrosine Phosphatase 1b" 97.73 321 100.00 100.00 0.00e+00 PDB 1OET "Oxidation State Of Protein Tyrosine Phosphatase 1b" 97.73 321 99.67 99.67 0.00e+00 PDB 1OEU "Oxidation State Of Protein Tyrosine Phosphatase 1b" 97.73 321 99.67 99.67 0.00e+00 PDB 1OEV "Oxidation State Of Protein Tyrosine Phosphatase 1b" 97.73 321 99.67 99.67 0.00e+00 PDB 1ONY "Oxalyl-aryl-amino Benzoic Acid Inhibitors Of Ptp1b, Compound 17" 97.73 321 100.00 100.00 0.00e+00 PDB 1ONZ "Oxalyl-Aryl-Amino Benzoic Acid Inhibitors Of Ptp1b, Compound 8b" 97.73 321 100.00 100.00 0.00e+00 PDB 1PA1 "Crystal Structure Of The C215d Mutant Of Protein Tyrosine Phosphatase 1b" 96.75 310 99.66 99.66 0.00e+00 PDB 1PH0 "Non-Carboxylic Acid-Containing Inhibitor Of Ptp1b Targeting The Second Phosphotyrosine Site" 97.73 321 100.00 100.00 0.00e+00 PDB 1PTT "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Phosphotyrosine-Containing Tetra-Peptide (Ac-Depyl-Nh2)" 97.73 321 99.34 99.67 0.00e+00 PDB 1PTU "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Phosphotyrosine-Containing Hexa-Peptide (Dadepyl-Nh2)" 97.73 321 99.34 99.67 0.00e+00 PDB 1PTV "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Phosphotyrosine" 97.73 321 99.00 99.67 0.00e+00 PDB 1PTY "Crystal Structure Of Protein Tyrosine Phosphatase 1b Complexed With Two Phosphotyrosine Molecules" 97.73 321 99.67 99.67 0.00e+00 PDB 1PXH "Crystal Structure Of Protein Tyrosine Phosphatase 1b With Potent And Selective Bidentate Inhibitor Compound 2" 97.73 321 100.00 100.00 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" 97.73 321 100.00 100.00 0.00e+00 PDB 1Q1M "A Highly Efficient Approach To A Selective And Cell Active Ptp1b Inhibitors" 97.73 321 100.00 100.00 0.00e+00 PDB 1Q6J "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 2" 96.75 310 100.00 100.00 0.00e+00 PDB 1Q6M "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 3" 96.75 310 100.00 100.00 0.00e+00 PDB 1Q6N "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 4" 96.75 310 100.00 100.00 0.00e+00 PDB 1Q6P "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 6" 96.75 310 100.00 100.00 0.00e+00 PDB 1Q6S "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 9" 96.75 310 100.00 100.00 0.00e+00 PDB 1Q6T "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 11" 96.75 310 100.00 100.00 0.00e+00 PDB 1QXK "Monoacid-Based, Cell Permeable, Selective Inhibitors Of Protein Tyrosine Phosphatase 1b" 97.73 321 100.00 100.00 0.00e+00 PDB 1SUG "1.95 A Structure Of Apo Protein Tyrosine Phosphatase 1b" 97.73 321 100.00 100.00 0.00e+00 PDB 1T48 "Allosteric Inhibition Of Protein Tyrosine Phosphatase 1b" 96.75 298 100.00 100.00 0.00e+00 PDB 1T49 "Allosteric Inhibition Of Protein Tyrosine Phosphatase 1b" 96.75 298 100.00 100.00 0.00e+00 PDB 1T4J "Allosteric Inhibition Of Protein Tyrosine Phosphatase 1b" 96.75 298 100.00 100.00 0.00e+00 PDB 1WAX "Protein Tyrosine Phosphatase 1b With Active Site Inhibitor" 97.73 321 100.00 100.00 0.00e+00 PDB 1XBO "Ptp1b Complexed With Isoxazole Carboxylic Acid" 97.73 321 100.00 100.00 0.00e+00 PDB 2AZR "Crystal Structure Of Ptp1b With Bicyclic Thiophene Inhibitor" 97.08 299 100.00 100.00 0.00e+00 PDB 2B07 "Crystal Structure Of Ptp1b With Tricyclic Thiophene Inhibitor." 97.08 299 100.00 100.00 0.00e+00 PDB 2B4S "Crystal Structure Of A Complex Between Ptp1b And The Insulin Receptor Tyrosine Kinase" 96.75 298 99.66 99.66 0.00e+00 PDB 2BGD "Structure-based Design Of Protein Tyrosine Phosphatase-1b Inhibitors" 97.73 321 100.00 100.00 0.00e+00 PDB 2BGE "Structure-Based Design Of Protein Tyrosine Phosphatase-1b Inhibitors" 97.73 321 100.00 100.00 0.00e+00 PDB 2CM2 "Structure Of Protein Tyrosine Phosphatase 1b (P212121)" 98.05 304 98.68 98.68 0.00e+00 PDB 2CM3 "Structure Of Protein Tyrosine Phosphatase 1b (C2)" 98.05 304 98.68 98.68 0.00e+00 PDB 2CM7 "Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics" 97.73 321 100.00 100.00 0.00e+00 PDB 2CM8 "Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics" 97.73 321 100.00 100.00 0.00e+00 PDB 2CMA "Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics" 99.03 327 98.69 98.69 0.00e+00 PDB 2CMB "Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics" 98.05 304 98.68 98.68 0.00e+00 PDB 2CMC "Structural Basis For Inhibition Of Protein Tyrosine Phosphatase 1b By Isothiazolidinone Heterocyclic Phosphonate Mimetics" 98.05 304 98.68 98.68 0.00e+00 PDB 2CNE "Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b" 98.05 304 98.68 98.68 0.00e+00 PDB 2CNF "Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b" 97.73 321 100.00 100.00 0.00e+00 PDB 2CNG "Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b" 97.73 321 100.00 100.00 0.00e+00 PDB 2CNH "Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b" 97.73 321 100.00 100.00 0.00e+00 PDB 2CNI "Structural Insights Into The Design Of Nonpeptidic Isothiazolidinone-Containing Inhibitors Of Protein Tyrosine Phosphatase 1b" 97.73 321 100.00 100.00 0.00e+00 PDB 2F6F "The Structure Of The S295f Mutant Of Human Ptp1b" 96.75 302 99.66 99.66 0.00e+00 PDB 2F6T "Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors" 96.75 298 100.00 100.00 0.00e+00 PDB 2F6V "Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors" 96.75 298 100.00 100.00 0.00e+00 PDB 2F6W "Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors" 96.75 298 100.00 100.00 0.00e+00 PDB 2F6Y "Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors" 96.75 298 100.00 100.00 0.00e+00 PDB 2F6Z "Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors" 96.75 298 100.00 100.00 0.00e+00 PDB 2F70 "Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors" 96.75 298 100.00 100.00 0.00e+00 PDB 2F71 "Protein Tyrosine Phosphatase 1b With Sulfamic Acid Inhibitors" 96.75 298 100.00 100.00 0.00e+00 PDB 2FJM "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 2" 96.75 310 99.66 100.00 0.00e+00 PDB 2FJN "The Structure Of Phosphotyrosine Phosphatase 1b In Complex With Compound 2" 96.75 310 100.00 100.00 0.00e+00 PDB 2H4G "Crystal Structure Of Ptp1b With Monocyclic Thiophene Inhibitor" 97.08 299 100.00 100.00 0.00e+00 PDB 2H4K "Crystal Structure Of Ptp1b With A Monocyclic Thiophene Inhibitor" 97.08 299 100.00 100.00 0.00e+00 PDB 2HB1 "Crystal Structure Of Ptp1b With Monocyclic Thiophene Inhibitor" 97.08 299 100.00 100.00 0.00e+00 PDB 2HNP "Crystal Structure Of Human Protein Tyrosine Phosphatase 1b" 97.73 321 100.00 100.00 0.00e+00 PDB 2HNQ "Crystal Structure Of Human Protein Tyrosine Phosphatase 1b" 97.73 321 100.00 100.00 0.00e+00 PDB 2NT7 "Crystal Structure Of Ptp1b-inhibitor Complex" 97.08 299 99.67 100.00 0.00e+00 PDB 2NTA "Crystal Structure Of Ptp1b-Inhibitor Complex" 97.08 299 99.67 100.00 0.00e+00 PDB 2QBP "Crystal Structure Of Ptp1b-inhibitor Complex" 97.08 299 100.00 100.00 0.00e+00 PDB 2QBQ "Crystal Structure Of Ptp1b-Inhibitor Complex" 97.08 299 100.00 100.00 0.00e+00 PDB 2QBR "Crystal Structure Of Ptp1b-Inhibitor Complex" 97.08 299 100.00 100.00 0.00e+00 PDB 2QBS "Crystal Structure Of Ptp1b-Inhibitor Complex" 97.08 299 100.00 100.00 0.00e+00 PDB 2VEU "Crystal Structure Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-containing Inhibitor" 97.73 321 100.00 100.00 0.00e+00 PDB 2VEV "Crystal Strucutre Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-Containing Inhibitor" 97.73 321 100.00 100.00 0.00e+00 PDB 2VEW "Crystal Strucutre Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-Containing Inhibitor" 97.73 321 100.00 100.00 0.00e+00 PDB 2VEX "Crystal Strucutre Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-Containing Inhibitor" 97.73 321 100.00 100.00 0.00e+00 PDB 2VEY "Crystal Strucutre Of Protein Tyrosine Phosphatase 1b In Complex With An Isothiazolidinone-Containing Inhibitor" 97.73 321 100.00 100.00 0.00e+00 PDB 2ZMM "Crystal Structure Of Ptp1b-Inhibitor Complex" 97.08 299 100.00 100.00 0.00e+00 PDB 2ZN7 "Crystal Structures Of Ptp1b-Inhibitor Complexes" 97.08 299 100.00 100.00 0.00e+00 PDB 3A5J "Crystal Structure Of Protein-Tyrosine Phosphatase 1b" 99.03 327 98.69 98.69 0.00e+00 PDB 3A5K "Crystal Structure Of Protein-Tyrosine Phosphatase 1b" 98.05 304 98.34 98.34 0.00e+00 PDB 3CWE "Ptp1b In Complex With A Phosphonic Acid Inhibitor" 91.88 290 100.00 100.00 0.00e+00 PDB 3D9C "Crystal Structure Ptp1b Complex With Aryl Seleninic Acid" 97.73 321 100.00 100.00 0.00e+00 PDB 3EAX "Crystal Structure Ptp1b Complex With Small Molecule Compound Lzp-6" 97.73 321 100.00 100.00 0.00e+00 PDB 3EB1 "Crystal Structure Ptp1b Complex With Small Molecule Inhibitor Lzp-25" 97.73 321 100.00 100.00 0.00e+00 PDB 3EU0 "Crystal Structure Of The S-Nitrosylated Cys215 Of Ptp1b" 99.03 327 98.69 98.69 0.00e+00 PDB 3I7Z "Protein Tyrosine Phosphatase 1b - Transition State Analog Fo First Catalytic Step" 97.73 321 100.00 100.00 0.00e+00 PDB 3I80 "Protein Tyrosine Phosphatase 1b - Transition State Analog Fo Second Catalytic Step" 97.73 321 100.00 100.00 0.00e+00 PDB 3QKP "Protein Tyrosine Phosphatase 1b - Apo W179f Mutant With Open Wpd-Loop" 97.73 321 99.67 100.00 0.00e+00 PDB 3QKQ "Protein Tyrosine Phosphatase 1b - W179f Mutant Bound With Vanadate" 97.73 321 99.67 100.00 0.00e+00 PDB 3SME "Structure Of Ptp1b Inactivated By H2o2BICARBONATE" 98.38 300 99.01 99.01 0.00e+00 PDB 3ZMP "Src-derived Peptide Inhibitor Complex Of Ptp1b" 99.03 329 98.69 98.69 0.00e+00 PDB 3ZMQ "Src-derived Mutant Peptide Inhibitor Complex Of Ptp1b" 99.03 329 98.69 98.69 0.00e+00 PDB 3ZV2 "Human Protein-Tyrosine Phosphatase 1b C215a, S216a Mutant" 97.73 320 99.34 99.67 0.00e+00 PDB 4BJO "Nitrate In The Active Site Of Ptp1b Is A Putative Mimetic Of The Transition State" 97.40 338 100.00 100.00 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" 98.38 354 99.67 99.67 0.00e+00 PDB 4QAP "The Second Sphere Residue T263 Is Important For Function And Activity Of Ptp1b Through Modulating Wpd Loop" 97.08 299 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" 97.08 299 100.00 100.00 0.00e+00 PDB 4Y14 "Structure Of Protein Tyrosine Phosphatase 1b Complexed With Inhibitor (ptp1b:cpt157633)" 100.00 308 100.00 100.00 0.00e+00 PDB 4ZRT "Ptp1bc215s Bound To Nephrin Peptide Substrate" 96.75 298 99.66 99.66 0.00e+00 DBJ BAF83327 "unnamed protein product [Homo sapiens]" 97.73 435 100.00 100.00 0.00e+00 DBJ BAG11007 "protein tyrosine phosphatase, non-receptor type 1 [synthetic construct]" 97.73 435 100.00 100.00 0.00e+00 DBJ BAG38152 "unnamed protein product [Homo sapiens]" 97.73 435 100.00 100.00 0.00e+00 DBJ BAG61697 "unnamed protein product [Homo sapiens]" 74.03 362 100.00 100.00 3.61e-165 EMBL CAH90487 "hypothetical protein [Pongo abelii]" 97.73 435 99.34 99.67 0.00e+00 EMBL CAN13184 "protein tyrosine phosphatase, non-receptor type 1 [Sus scrofa]" 97.73 427 98.01 99.67 0.00e+00 GB AAA60157 "non-receptor tyrosine phosphatase 1 [Homo sapiens]" 97.73 435 100.00 100.00 0.00e+00 GB AAA60223 "phosphotyrosyl-protein phosphatase (EC 3.1.3.48) [Homo sapiens]" 97.73 435 100.00 100.00 0.00e+00 GB AAH15660 "Protein tyrosine phosphatase, non-receptor type 1 [Homo sapiens]" 97.73 435 100.00 100.00 0.00e+00 GB AAH18164 "Protein tyrosine phosphatase, non-receptor type 1 [Homo sapiens]" 97.73 435 100.00 100.00 0.00e+00 GB AAP35398 "protein tyrosine phosphatase, non-receptor type 1 [Homo sapiens]" 97.73 435 100.00 100.00 0.00e+00 REF NP_001106906 "tyrosine-protein phosphatase non-receptor type 1 [Sus scrofa]" 97.73 427 98.01 99.67 0.00e+00 REF NP_001125254 "tyrosine-protein phosphatase non-receptor type 1 [Pongo abelii]" 97.73 435 99.34 99.67 0.00e+00 REF NP_001245122 "tyrosine-protein phosphatase non-receptor type 1 [Macaca mulatta]" 97.73 435 100.00 100.00 0.00e+00 REF NP_001265547 "tyrosine-protein phosphatase non-receptor type 1 isoform 2 [Homo sapiens]" 74.03 362 100.00 100.00 3.61e-165 REF NP_002818 "tyrosine-protein phosphatase non-receptor type 1 isoform 1 [Homo sapiens]" 97.73 435 100.00 100.00 0.00e+00 SP P18031 "RecName: Full=Tyrosine-protein phosphatase non-receptor type 1; AltName: Full=Protein-tyrosine phosphatase 1B; Short=PTP-1B" 97.73 435 100.00 100.00 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 1 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 1 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 0.42 mM [U-15N]-Leu 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 1.0 mM [U-15N]-Tyr 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_5 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PTP1B 1.0 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_6 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PTP1B 0.6 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_5 save_ save_2D_1H-15N_TROSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_6 save_ save_2D_1H-15N_TROSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_1 save_ save_3D_TROSY_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCA' _Sample_label $sample_2 save_ save_3D_TROSY_HNCOCA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCOCA' _Sample_label $sample_2 save_ save_3D_TROSY_HNCACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCACB' _Sample_label $sample_2 save_ save_3D_TROSY_HNCOCACB_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCOCACB' _Sample_label $sample_2 save_ save_3D_1H-15N_TROSY_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TROSY NOESY' _Sample_label $sample_1 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' '3D 1H-15N TROSY NOESY' stop_ loop_ _Sample_label $sample_3 $sample_4 $sample_5 $sample_6 $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 5 5 SER CA C 60.461 0.100 1 2 6 6 MET H H 8.659 0.010 1 3 6 6 MET CA C 59.994 0.100 1 4 6 6 MET CB C 33.577 0.100 1 5 6 6 MET N N 119.416 0.050 1 6 7 7 GLU H H 7.904 0.010 1 7 7 7 GLU CA C 60.315 0.100 1 8 7 7 GLU CB C 30.111 0.100 1 9 7 7 GLU N N 119.741 0.050 1 10 8 8 MET H H 7.683 0.010 1 11 8 8 MET CA C 59.789 0.100 1 12 8 8 MET CB C 31.986 0.100 1 13 8 8 MET N N 120.983 0.050 1 14 9 9 GLU CA C 59.409 0.100 1 15 10 10 LYS H H 8.363 0.010 1 16 10 10 LYS CA C 59.760 0.100 1 17 10 10 LYS CB C 29.636 0.100 1 18 10 10 LYS N N 120.105 0.050 1 19 11 11 GLU H H 8.198 0.010 1 20 11 11 GLU CA C 60.023 0.100 1 21 11 11 GLU CB C 29.880 0.100 1 22 11 11 GLU N N 121.829 0.050 1 23 12 12 PHE H H 8.498 0.010 1 24 12 12 PHE CA C 62.828 0.100 1 25 12 12 PHE CB C 40.372 0.100 1 26 12 12 PHE N N 119.839 0.050 1 27 13 13 GLU H H 8.208 0.010 1 28 13 13 GLU CA C 59.965 0.100 1 29 13 13 GLU CB C 29.636 0.100 1 30 13 13 GLU N N 117.957 0.050 1 31 14 14 GLN H H 7.751 0.010 1 32 14 14 GLN CA C 59.322 0.100 1 33 14 14 GLN CB C 28.272 0.100 1 34 14 14 GLN N N 119.229 0.050 1 35 15 15 ILE H H 8.144 0.010 1 36 15 15 ILE CA C 65.410 0.100 1 37 15 15 ILE CB C 37.917 0.100 1 38 15 15 ILE N N 123.314 0.050 1 39 16 16 ASP H H 8.401 0.010 1 40 16 16 ASP CA C 58.351 0.100 1 41 16 16 ASP CB C 41.687 0.100 1 42 16 16 ASP N N 119.839 0.050 1 43 17 17 LYS H H 8.337 0.010 1 44 17 17 LYS CA C 59.421 0.100 1 45 17 17 LYS CB C 32.213 0.100 1 46 17 17 LYS N N 118.363 0.050 1 47 18 18 SER H H 7.519 0.010 1 48 18 18 SER CA C 59.059 0.100 1 49 18 18 SER CB C 64.698 0.100 1 50 18 18 SER N N 111.723 0.050 1 51 19 19 GLY H H 7.801 0.010 1 52 19 19 GLY CA C 47.432 0.100 1 53 19 19 GLY N N 113.394 0.050 1 54 20 20 SER H H 7.777 0.010 1 55 20 20 SER CA C 59.176 0.100 1 56 20 20 SER CB C 63.743 0.100 1 57 20 20 SER N N 111.868 0.050 1 58 21 21 TRP H H 7.109 0.010 1 59 21 21 TRP CA C 61.016 0.100 1 60 21 21 TRP CB C 29.235 0.100 1 61 21 21 TRP N N 122.153 0.050 1 62 22 22 ALA H H 8.664 0.010 1 63 22 22 ALA CA C 56.021 0.100 1 64 22 22 ALA CB C 17.812 0.100 1 65 22 22 ALA N N 119.712 0.050 1 66 23 23 ALA H H 7.617 0.010 1 67 23 23 ALA CA C 55.553 0.100 1 68 23 23 ALA CB C 18.061 0.100 1 69 23 23 ALA N N 123.018 0.050 1 70 24 24 ILE H H 7.896 0.010 1 71 24 24 ILE CA C 63.821 0.100 1 72 24 24 ILE CB C 37.064 0.100 1 73 24 24 ILE N N 119.532 0.050 1 74 25 25 TYR H H 8.516 0.010 1 75 25 25 TYR CA C 62.740 0.100 1 76 25 25 TYR CB C 38.807 0.100 1 77 25 25 TYR N N 120.489 0.050 1 78 26 26 GLN H H 8.125 0.010 1 79 26 26 GLN CA C 59.127 0.100 1 80 26 26 GLN CB C 27.871 0.100 1 81 26 26 GLN N N 118.413 0.050 1 82 27 27 ASP H H 7.772 0.010 1 83 27 27 ASP CA C 58.241 0.100 1 84 27 27 ASP CB C 40.323 0.100 1 85 27 27 ASP N N 121.091 0.050 1 86 28 28 ILE H H 7.617 0.010 1 87 28 28 ILE CA C 65.457 0.100 1 88 28 28 ILE CB C 37.215 0.100 1 89 28 28 ILE N N 120.665 0.050 1 90 29 29 ARG H H 7.657 0.010 1 91 29 29 ARG CA C 60.315 0.100 1 92 29 29 ARG CB C 29.788 0.100 1 93 29 29 ARG N N 117.975 0.050 1 94 30 30 HIS H H 8.099 0.010 1 95 30 30 HIS CA C 58.535 0.100 1 96 30 30 HIS CB C 29.863 0.100 1 97 30 30 HIS N N 116.927 0.050 1 98 31 31 GLU H H 7.745 0.010 1 99 31 31 GLU CA C 56.868 0.100 1 100 31 31 GLU CB C 30.900 0.100 1 101 31 31 GLU N N 118.039 0.050 1 102 32 32 ALA H H 7.363 0.010 1 103 32 32 ALA CA C 53.362 0.100 1 104 32 32 ALA CB C 19.345 0.100 1 105 32 32 ALA N N 123.680 0.050 1 106 33 33 SER H H 7.938 0.010 1 107 33 33 SER CA C 59.789 0.100 1 108 33 33 SER CB C 65.107 0.100 1 109 33 33 SER N N 117.557 0.050 1 110 34 34 ASP H H 8.045 0.010 1 111 34 34 ASP CA C 54.268 0.100 1 112 34 34 ASP CB C 43.730 0.100 1 113 34 34 ASP N N 122.763 0.050 1 114 35 35 PHE H H 6.723 0.010 1 115 35 35 PHE CA C 55.728 0.100 1 116 35 35 PHE CB C 41.012 0.100 1 117 35 35 PHE N N 119.800 0.050 1 118 36 36 PRO CA C 64.902 0.100 1 119 36 36 PRO CB C 32.895 0.100 1 120 37 37 CYS H H 9.111 0.010 1 121 37 37 CYS CA C 56.926 0.100 1 122 37 37 CYS CB C 28.802 0.100 1 123 37 37 CYS N N 126.602 0.050 1 124 38 38 ARG H H 9.461 0.010 1 125 38 38 ARG CA C 60.344 0.100 1 126 38 38 ARG CB C 30.546 0.100 1 127 38 38 ARG N N 122.145 0.050 1 128 39 39 VAL H H 9.484 0.010 1 129 39 39 VAL CA C 67.473 0.100 1 130 39 39 VAL CB C 30.621 0.100 1 131 39 39 VAL N N 121.718 0.050 1 132 40 40 ALA H H 8.492 0.010 1 133 40 40 ALA CA C 55.173 0.100 1 134 40 40 ALA CB C 21.147 0.100 1 135 40 40 ALA N N 121.902 0.050 1 136 41 41 LYS H H 6.752 0.010 1 137 41 41 LYS CA C 55.845 0.100 1 138 41 41 LYS CB C 32.744 0.100 1 139 41 41 LYS N N 111.437 0.050 1 140 42 42 LEU H H 7.438 0.010 1 141 42 42 LEU CA C 54.589 0.100 1 142 42 42 LEU CB C 41.081 0.100 1 143 42 42 LEU N N 123.792 0.050 1 144 43 43 PRO CA C 66.596 0.100 1 145 43 43 PRO CB C 31.356 0.100 1 146 44 44 LYS H H 8.080 0.010 1 147 44 44 LYS CA C 58.533 0.100 1 148 44 44 LYS CB C 31.304 0.100 1 149 44 44 LYS N N 114.427 0.050 1 150 45 45 ASN H H 7.697 0.010 1 151 45 45 ASN CA C 53.508 0.100 1 152 45 45 ASN CB C 39.717 0.100 1 153 45 45 ASN N N 117.163 0.050 1 154 46 46 LYS H H 7.362 0.010 1 155 46 46 LYS CA C 61.279 0.100 1 156 46 46 LYS CB C 32.481 0.100 1 157 46 46 LYS N N 123.743 0.050 1 158 47 47 ASN H H 8.349 0.010 1 159 47 47 ASN CA C 53.567 0.100 1 160 47 47 ASN CB C 37.291 0.100 1 161 47 47 ASN N N 113.975 0.050 1 162 48 48 ARG H H 7.840 0.010 1 163 48 48 ARG CA C 56.693 0.100 1 164 48 48 ARG CB C 31.455 0.100 1 165 48 48 ARG N N 115.406 0.050 1 166 49 49 ASN H H 7.446 0.010 1 167 49 49 ASN CA C 53.041 0.100 1 168 49 49 ASN CB C 41.692 0.100 1 169 49 49 ASN N N 120.143 0.050 1 170 50 50 ARG H H 9.150 0.010 1 171 50 50 ARG CA C 59.639 0.100 1 172 50 50 ARG CB C 31.109 0.100 1 173 50 50 ARG N N 126.360 0.050 1 174 51 51 TYR H H 9.390 0.010 1 175 51 51 TYR CA C 56.693 0.100 1 176 51 51 TYR CB C 40.323 0.100 1 177 51 51 TYR N N 117.616 0.050 1 178 52 52 ARG CA C 58.738 0.100 1 179 52 52 ARG CB C 30.091 0.100 1 180 53 53 ASP H H 8.557 0.010 1 181 53 53 ASP CA C 53.859 0.100 1 182 53 53 ASP CB C 40.626 0.100 1 183 53 53 ASP N N 113.370 0.050 1 184 54 54 VAL H H 6.962 0.010 1 185 54 54 VAL CA C 63.266 0.100 1 186 54 54 VAL CB C 32.632 0.100 1 187 54 54 VAL N N 119.747 0.050 1 188 55 55 SER H H 7.892 0.010 1 189 55 55 SER CA C 56.167 0.100 1 190 55 55 SER CB C 65.259 0.100 1 191 55 55 SER N N 123.903 0.050 1 192 56 56 PRO CA C 62.565 0.100 1 193 56 56 PRO CB C 32.255 0.100 1 194 57 57 PHE H H 7.194 0.010 1 195 57 57 PHE CA C 56.167 0.100 1 196 57 57 PHE CB C 39.578 0.100 1 197 57 57 PHE N N 124.706 0.050 1 198 58 58 ASP H H 9.240 0.010 1 199 58 58 ASP CA C 59.497 0.100 1 200 58 58 ASP CB C 41.005 0.100 1 201 58 58 ASP N N 124.866 0.050 1 202 59 59 HIS H H 8.983 0.010 1 203 59 59 HIS CA C 59.789 0.100 1 204 59 59 HIS CB C 30.518 0.100 1 205 59 59 HIS N N 115.726 0.050 1 206 60 60 SER H H 6.324 0.010 1 207 60 60 SER CA C 56.108 0.100 1 208 60 60 SER CB C 64.187 0.100 1 209 60 60 SER N N 108.673 0.050 1 210 61 61 ARG H H 7.262 0.010 1 211 61 61 ARG CA C 56.167 0.100 1 212 61 61 ARG CB C 28.764 0.100 1 213 61 61 ARG N N 123.380 0.050 1 214 62 62 ILE H H 7.084 0.010 1 215 62 62 ILE CA C 57.890 0.100 1 216 62 62 ILE CB C 36.180 0.100 1 217 62 62 ILE N N 122.373 0.050 1 218 63 63 LYS H H 8.487 0.010 1 219 63 63 LYS CA C 55.699 0.100 1 220 63 63 LYS CB C 32.971 0.100 1 221 63 63 LYS N N 127.914 0.050 1 222 64 64 LEU H H 9.188 0.010 1 223 64 64 LEU CA C 54.589 0.100 1 224 64 64 LEU CB C 42.293 0.100 1 225 64 64 LEU N N 125.697 0.050 1 226 65 65 HIS H H 9.528 0.010 1 227 65 65 HIS CA C 54.677 0.100 1 228 65 65 HIS CB C 27.286 0.100 1 229 65 65 HIS N N 124.273 0.050 1 230 66 66 GLN H H 7.405 0.010 1 231 66 66 GLN CA C 55.144 0.100 1 232 66 66 GLN CB C 31.651 0.100 1 233 66 66 GLN N N 119.981 0.050 1 234 67 67 GLU H H 8.422 0.010 1 235 67 67 GLU CA C 58.460 0.100 1 236 67 67 GLU CB C 30.552 0.100 1 237 67 67 GLU N N 121.442 0.050 1 238 68 68 ASP H H 8.278 0.010 1 239 68 68 ASP CA C 57.160 0.100 1 240 68 68 ASP CB C 41.460 0.100 1 241 68 68 ASP N N 118.885 0.050 1 242 69 69 ASN H H 7.423 0.010 1 243 69 69 ASN CA C 54.005 0.100 1 244 69 69 ASN CB C 38.276 0.100 1 245 69 69 ASN N N 114.438 0.050 1 246 70 70 ASP H H 8.095 0.010 1 247 70 70 ASP CA C 53.830 0.100 1 248 70 70 ASP CB C 42.142 0.100 1 249 70 70 ASP N N 126.376 0.050 1 250 71 71 TYR H H 7.966 0.010 1 251 71 71 TYR CA C 61.454 0.100 1 252 71 71 TYR CB C 39.280 0.100 1 253 71 71 TYR N N 118.935 0.050 1 254 72 72 ILE H H 7.670 0.010 1 255 72 72 ILE CA C 59.409 0.100 1 256 72 72 ILE CB C 42.218 0.100 1 257 72 72 ILE N N 125.537 0.050 1 258 73 73 ASN H H 8.139 0.010 1 259 73 73 ASN CA C 53.099 0.100 1 260 73 73 ASN CB C 36.230 0.100 1 261 73 73 ASN N N 125.837 0.050 1 262 74 74 ALA H H 7.728 0.010 1 263 74 74 ALA CA C 52.310 0.100 1 264 74 74 ALA CB C 23.269 0.100 1 265 74 74 ALA N N 129.350 0.050 1 266 75 75 SER H H 8.915 0.010 1 267 75 75 SER CA C 58.066 0.100 1 268 75 75 SER CB C 67.608 0.100 1 269 75 75 SER N N 117.074 0.050 1 270 76 76 LEU H H 8.873 0.010 1 271 76 76 LEU CA C 54.794 0.100 1 272 76 76 LEU CB C 42.369 0.100 1 273 76 76 LEU N N 127.305 0.050 1 274 77 77 ILE H H 9.444 0.010 1 275 77 77 ILE CA C 60.929 0.100 1 276 77 77 ILE CB C 37.766 0.100 1 277 77 77 ILE N N 128.348 0.050 1 278 78 78 LYS CA C 55.553 0.100 1 279 78 78 LYS CB C 33.577 0.100 1 280 79 79 MET H H 8.222 0.010 1 281 79 79 MET CA C 52.573 0.100 1 282 79 79 MET CB C 30.015 0.100 1 283 79 79 MET N N 124.202 0.050 1 284 80 80 GLU H H 8.390 0.010 1 285 80 80 GLU CA C 60.783 0.100 1 286 80 80 GLU CB C 29.506 0.100 1 287 80 80 GLU N N 126.423 0.050 1 288 81 81 GLU H H 8.877 0.010 1 289 81 81 GLU CA C 59.672 0.100 1 290 81 81 GLU CB C 29.008 0.100 1 291 81 81 GLU N N 121.705 0.050 1 292 82 82 ALA H H 7.364 0.010 1 293 82 82 ALA CA C 52.953 0.100 1 294 82 82 ALA CB C 19.118 0.100 1 295 82 82 ALA N N 117.481 0.050 1 296 83 83 GLN H H 7.668 0.010 1 297 83 83 GLN CA C 56.722 0.100 1 298 83 83 GLN CB C 26.453 0.100 1 299 83 83 GLN N N 112.512 0.050 1 300 84 84 ARG H H 7.181 0.010 1 301 84 84 ARG CA C 54.677 0.100 1 302 84 84 ARG CB C 35.878 0.100 1 303 84 84 ARG N N 118.112 0.050 1 304 85 85 SER H H 7.710 0.010 1 305 85 85 SER CA C 57.218 0.100 1 306 85 85 SER CB C 66.547 0.100 1 307 85 85 SER N N 118.974 0.050 1 308 86 86 TYR H H 8.542 0.010 1 309 86 86 TYR CA C 55.641 0.100 1 310 86 86 TYR CB C 43.734 0.100 1 311 86 86 TYR N N 117.104 0.050 1 312 87 87 ILE H H 9.406 0.010 1 313 87 87 ILE CA C 61.045 0.100 1 314 87 87 ILE CB C 39.125 0.100 1 315 87 87 ILE N N 123.155 0.050 1 316 88 88 LEU H H 8.543 0.010 1 317 88 88 LEU CA C 54.209 0.100 1 318 88 88 LEU CB C 44.037 0.100 1 319 88 88 LEU N N 128.945 0.050 1 320 89 89 THR H H 8.387 0.010 1 321 89 89 THR CA C 58.358 0.100 1 322 89 89 THR CB C 72.232 0.100 1 323 89 89 THR N N 115.982 0.050 1 324 90 90 GLN H H 6.424 0.010 1 325 90 90 GLN CA C 53.158 0.100 1 326 90 90 GLN CB C 28.555 0.100 1 327 90 90 GLN N N 117.015 0.050 1 328 91 91 GLY H H 8.802 0.010 1 329 91 91 GLY CA C 45.504 0.100 1 330 91 91 GLY N N 112.916 0.050 1 331 92 92 PRO CA C 64.405 0.100 1 332 92 92 PRO CB C 32.289 0.100 1 333 93 93 LEU H H 7.956 0.010 1 334 93 93 LEU CA C 53.946 0.100 1 335 93 93 LEU CB C 42.218 0.100 1 336 93 93 LEU N N 124.157 0.050 1 337 94 94 PRO CA C 66.771 0.100 1 338 94 94 PRO CB C 31.422 0.100 1 339 95 95 ASN H H 8.573 0.010 1 340 95 95 ASN CA C 54.443 0.100 1 341 95 95 ASN CB C 37.508 0.100 1 342 95 95 ASN N N 107.160 0.050 1 343 96 96 THR H H 8.067 0.010 1 344 96 96 THR CA C 61.250 0.100 1 345 96 96 THR CB C 69.883 0.100 1 346 96 96 THR N N 111.949 0.050 1 347 97 97 CYS H H 7.558 0.010 1 348 97 97 CYS CA C 64.697 0.100 1 349 97 97 CYS CB C 28.555 0.100 1 350 97 97 CYS N N 121.741 0.050 1 351 98 98 GLY H H 8.277 0.010 1 352 98 98 GLY CA C 48.133 0.100 1 353 98 98 GLY N N 109.049 0.050 1 354 99 99 HIS H H 7.413 0.010 1 355 99 99 HIS CA C 57.540 0.100 1 356 99 99 HIS CB C 32.744 0.100 1 357 99 99 HIS N N 124.050 0.050 1 358 100 100 PHE H H 8.183 0.010 1 359 100 100 PHE CA C 62.535 0.100 1 360 100 100 PHE CB C 38.428 0.100 1 361 100 100 PHE N N 119.712 0.050 1 362 103 103 MET CA C 60.198 0.100 1 363 104 104 VAL H H 7.725 0.010 1 364 104 104 VAL CA C 63.850 0.100 1 365 104 104 VAL CB C 32.219 0.100 1 366 104 104 VAL N N 121.580 0.050 1 367 105 105 TRP H H 8.374 0.010 1 368 105 105 TRP CA C 55.787 0.100 1 369 105 105 TRP CB C 30.034 0.100 1 370 105 105 TRP N N 119.682 0.050 1 371 109 109 SER CA C 61.863 0.100 1 372 109 109 SER CB C 63.317 0.100 1 373 110 110 ARG H H 9.216 0.010 1 374 110 110 ARG CA C 55.582 0.100 1 375 110 110 ARG CB C 32.213 0.100 1 376 110 110 ARG N N 124.033 0.050 1 377 111 111 GLY H H 7.246 0.010 1 378 111 111 GLY CA C 44.352 0.100 1 379 111 111 GLY N N 102.530 0.050 1 380 112 112 VAL H H 8.804 0.010 1 381 112 112 VAL CA C 61.033 0.100 1 382 112 112 VAL CB C 35.721 0.100 1 383 112 112 VAL N N 121.046 0.050 1 384 114 114 MET CA C 54.677 0.100 1 385 114 114 MET CB C 34.315 0.100 1 386 115 115 LEU H H 7.863 0.010 1 387 115 115 LEU CA C 54.648 0.100 1 388 115 115 LEU CB C 43.051 0.100 1 389 115 115 LEU N N 124.967 0.050 1 390 116 116 ASN H H 7.439 0.010 1 391 116 116 ASN CA C 52.340 0.100 1 392 116 116 ASN CB C 42.046 0.100 1 393 116 116 ASN N N 114.913 0.050 1 394 117 117 ARG H H 9.243 0.010 1 395 117 117 ARG CA C 56.483 0.100 1 396 117 117 ARG CB C 31.906 0.100 1 397 117 117 ARG N N 120.071 0.050 1 398 118 118 VAL H H 8.883 0.010 1 399 118 118 VAL CA C 67.385 0.100 1 400 118 118 VAL CB C 32.028 0.100 1 401 118 118 VAL N N 121.691 0.050 1 402 121 121 LYS CA C 57.158 0.100 1 403 121 121 LYS CB C 30.982 0.100 1 404 122 122 GLY H H 8.542 0.010 1 405 122 122 GLY CA C 46.292 0.100 1 406 122 122 GLY N N 106.127 0.050 1 407 123 123 SER H H 7.892 0.010 1 408 123 123 SER CA C 57.832 0.100 1 409 123 123 SER CB C 65.334 0.100 1 410 123 123 SER N N 116.504 0.050 1 411 124 124 LEU H H 8.516 0.010 1 412 124 124 LEU CA C 56.137 0.100 1 413 124 124 LEU CB C 41.914 0.100 1 414 124 124 LEU N N 126.376 0.050 1 415 126 126 CYS CA C 58.884 0.100 1 416 126 126 CYS CB C 29.560 0.100 1 417 127 127 ALA H H 7.765 0.010 1 418 127 127 ALA CA C 52.164 0.100 1 419 127 127 ALA CB C 19.101 0.100 1 420 127 127 ALA N N 124.780 0.050 1 421 128 128 GLN H H 8.470 0.010 1 422 128 128 GLN CA C 56.021 0.100 1 423 128 128 GLN CB C 26.529 0.100 1 424 128 128 GLN N N 121.201 0.050 1 425 129 129 TYR H H 6.610 0.010 1 426 129 129 TYR CA C 57.014 0.100 1 427 129 129 TYR CB C 38.219 0.100 1 428 129 129 TYR N N 123.010 0.050 1 429 130 130 TRP H H 6.594 0.010 1 430 130 130 TRP CA C 55.962 0.100 1 431 130 130 TRP CB C 30.896 0.100 1 432 130 130 TRP N N 121.331 0.050 1 433 137 137 GLU CA C 54.764 0.100 1 434 137 137 GLU CB C 33.463 0.100 1 435 138 138 MET H H 8.853 0.010 1 436 138 138 MET CA C 55.728 0.100 1 437 138 138 MET CB C 38.580 0.100 1 438 138 138 MET N N 121.576 0.050 1 439 139 139 ILE H H 8.142 0.010 1 440 139 139 ILE CA C 60.490 0.100 1 441 139 139 ILE CB C 40.106 0.100 1 442 139 139 ILE N N 122.430 0.050 1 443 140 140 PHE H H 8.894 0.010 1 444 140 140 PHE CA C 57.072 0.100 1 445 140 140 PHE CB C 37.973 0.100 1 446 140 140 PHE N N 128.195 0.050 1 447 141 141 GLU H H 8.964 0.010 1 448 141 141 GLU CA C 59.585 0.100 1 449 141 141 GLU CB C 29.939 0.100 1 450 141 141 GLU N N 124.526 0.050 1 451 142 142 ASP H H 9.068 0.010 1 452 142 142 ASP CA C 56.313 0.100 1 453 142 142 ASP CB C 38.883 0.100 1 454 142 142 ASP N N 116.750 0.050 1 455 143 143 THR H H 7.454 0.010 1 456 143 143 THR CA C 60.987 0.100 1 457 143 143 THR CB C 69.226 0.100 1 458 143 143 THR N N 108.441 0.050 1 459 144 144 ASN H H 7.952 0.010 1 460 144 144 ASN CA C 54.355 0.100 1 461 144 144 ASN CB C 38.201 0.100 1 462 144 144 ASN N N 121.213 0.050 1 463 145 145 LEU H H 7.421 0.010 1 464 145 145 LEU CA C 54.122 0.100 1 465 145 145 LEU CB C 46.448 0.100 1 466 145 145 LEU N N 117.435 0.050 1 467 146 146 LYS CA C 54.798 0.100 1 468 146 146 LYS CB C 36.875 0.100 1 469 147 147 LEU H H 9.133 0.010 1 470 147 147 LEU CA C 53.132 0.100 1 471 147 147 LEU CB C 48.340 0.100 1 472 147 147 LEU N N 129.972 0.050 1 473 148 148 THR CA C 61.951 0.100 1 474 148 148 THR CB C 71.701 0.100 1 475 149 149 LEU H H 8.958 0.010 1 476 149 149 LEU CA C 55.845 0.100 1 477 149 149 LEU CB C 42.824 0.100 1 478 149 149 LEU N N 128.307 0.050 1 479 150 150 ILE H H 8.852 0.010 1 480 150 150 ILE CA C 61.746 0.100 1 481 150 150 ILE CB C 36.994 0.100 1 482 150 150 ILE N N 130.063 0.050 1 483 151 151 SER H H 7.785 0.010 1 484 151 151 SER CA C 58.270 0.100 1 485 151 151 SER CB C 65.789 0.100 1 486 151 151 SER N N 111.437 0.050 1 487 152 152 GLU H H 8.611 0.010 1 488 152 152 GLU CA C 56.488 0.100 1 489 152 152 GLU CB C 34.411 0.100 1 490 152 152 GLU N N 120.880 0.050 1 491 153 153 ASP H H 8.826 0.010 1 492 153 153 ASP CA C 53.654 0.100 1 493 153 153 ASP CB C 42.366 0.100 1 494 153 153 ASP N N 127.266 0.050 1 495 154 154 ILE H H 8.501 0.010 1 496 154 154 ILE CA C 62.769 0.100 1 497 154 154 ILE CB C 38.655 0.100 1 498 154 154 ILE N N 127.319 0.050 1 499 155 155 LYS H H 8.139 0.010 1 500 155 155 LYS CA C 54.414 0.100 1 501 155 155 LYS CB C 33.123 0.100 1 502 155 155 LYS N N 129.117 0.050 1 503 157 157 TYR H H 7.097 0.010 1 504 157 157 TYR CA C 56.120 0.100 1 505 157 157 TYR CB C 39.110 0.100 1 506 157 157 TYR N N 113.002 0.050 1 507 158 158 TYR H H 6.568 0.010 1 508 158 158 TYR CA C 56.488 0.100 1 509 158 158 TYR CB C 41.157 0.100 1 510 158 158 TYR N N 114.120 0.050 1 511 159 159 THR H H 9.405 0.010 1 512 159 159 THR CA C 61.601 0.100 1 513 159 159 THR CB C 73.838 0.100 1 514 159 159 THR N N 117.789 0.050 1 515 160 160 VAL H H 8.710 0.010 1 516 160 160 VAL CA C 60.490 0.100 1 517 160 160 VAL CB C 34.335 0.100 1 518 160 160 VAL N N 126.509 0.050 1 519 166 166 GLU CA C 53.985 0.100 1 520 166 166 GLU CB C 33.426 0.100 1 521 167 167 ASN H H 8.196 0.010 1 522 167 167 ASN CA C 52.475 0.100 1 523 167 167 ASN CB C 38.201 0.100 1 524 167 167 ASN N N 124.705 0.050 1 525 168 168 LEU H H 8.263 0.010 1 526 168 168 LEU CA C 57.423 0.100 1 527 168 168 LEU CB C 40.929 0.100 1 528 168 168 LEU N N 126.177 0.050 1 529 169 169 THR H H 8.220 0.010 1 530 169 169 THR CA C 65.807 0.100 1 531 169 169 THR CB C 68.972 0.100 1 532 169 169 THR N N 115.269 0.050 1 533 170 170 THR H H 7.032 0.010 1 534 170 170 THR CA C 62.272 0.100 1 535 170 170 THR CB C 70.687 0.100 1 536 170 170 THR N N 109.635 0.050 1 537 171 171 GLN H H 8.366 0.010 1 538 171 171 GLN CA C 58.504 0.100 1 539 171 171 GLN CB C 26.301 0.100 1 540 171 171 GLN N N 116.917 0.050 1 541 172 172 GLU H H 7.441 0.010 1 542 172 172 GLU CA C 56.780 0.100 1 543 172 172 GLU CB C 33.463 0.100 1 544 172 172 GLU N N 119.817 0.050 1 545 173 173 THR H H 8.436 0.010 1 546 173 173 THR CA C 60.753 0.100 1 547 173 173 THR CB C 72.459 0.100 1 548 173 173 THR N N 113.762 0.050 1 549 175 175 GLU CA C 57.335 0.100 1 550 176 176 ILE H H 8.579 0.010 1 551 176 176 ILE CA C 62.126 0.100 1 552 176 176 ILE CB C 39.970 0.100 1 553 176 176 ILE N N 114.849 0.050 1 554 177 177 LEU H H 8.623 0.010 1 555 177 177 LEU CA C 57.461 0.100 1 556 177 177 LEU CB C 41.675 0.100 1 557 177 177 LEU N N 119.734 0.050 1 558 178 178 HIS H H 8.117 0.010 1 559 178 178 HIS CA C 57.847 0.100 1 560 178 178 HIS CB C 38.883 0.100 1 561 178 178 HIS N N 117.803 0.050 1 562 181 181 TYR CA C 56.021 0.100 1 563 181 181 TYR CB C 42.266 0.100 1 564 182 182 THR H H 8.105 0.010 1 565 182 182 THR CA C 58.971 0.100 1 566 182 182 THR CB C 64.219 0.100 1 567 182 182 THR N N 116.120 0.050 1 568 183 183 THR H H 8.314 0.010 1 569 183 183 THR CA C 59.283 0.100 1 570 183 183 THR CB C 63.807 0.100 1 571 183 183 THR N N 118.423 0.050 1 572 184 184 TRP H H 7.008 0.010 1 573 184 184 TRP CA C 60.899 0.100 1 574 184 184 TRP CB C 29.386 0.100 1 575 184 184 TRP N N 121.813 0.050 1 576 185 185 PRO CA C 56.926 0.100 1 577 185 185 PRO CB C 29.863 0.100 1 578 186 186 ASP H H 8.287 0.010 1 579 186 186 ASP CA C 57.511 0.100 1 580 186 186 ASP CB C 41.460 0.100 1 581 186 186 ASP N N 121.736 0.050 1 582 187 187 PHE H H 7.584 0.010 1 583 187 187 PHE CA C 57.126 0.100 1 584 187 187 PHE CB C 41.370 0.100 1 585 187 187 PHE N N 114.960 0.050 1 586 188 188 GLY H H 8.319 0.010 1 587 188 188 GLY CA C 45.562 0.100 1 588 188 188 GLY N N 110.244 0.050 1 589 189 189 VAL H H 8.019 0.010 1 590 189 189 VAL CA C 58.124 0.100 1 591 189 189 VAL CB C 31.152 0.100 1 592 189 189 VAL N N 114.280 0.050 1 593 193 193 PRO CA C 56.305 0.100 1 594 193 193 PRO CB C 33.047 0.100 1 595 194 194 ALA H H 8.514 0.010 1 596 194 194 ALA CA C 53.567 0.100 1 597 194 194 ALA CB C 19.404 0.100 1 598 194 194 ALA N N 125.767 0.050 1 599 195 195 SER H H 8.166 0.010 1 600 195 195 SER CA C 59.208 0.100 1 601 195 195 SER CB C 64.198 0.100 1 602 195 195 SER N N 114.467 0.050 1 603 196 196 PHE H H 8.464 0.010 1 604 196 196 PHE CA C 57.218 0.100 1 605 196 196 PHE CB C 33.931 0.100 1 606 196 196 PHE N N 122.982 0.050 1 607 199 199 PHE CA C 55.115 0.100 1 608 199 199 PHE CB C 41.524 0.100 1 609 200 200 LEU H H 8.036 0.010 1 610 200 200 LEU CA C 55.495 0.100 1 611 200 200 LEU CB C 42.296 0.100 1 612 200 200 LEU N N 122.569 0.050 1 613 201 201 PHE H H 8.122 0.010 1 614 201 201 PHE CA C 54.764 0.100 1 615 201 201 PHE CB C 30.065 0.100 1 616 201 201 PHE N N 122.920 0.050 1 617 203 203 VAL CA C 66.771 0.100 1 618 204 204 ARG H H 8.393 0.010 1 619 204 204 ARG CA C 60.549 0.100 1 620 204 204 ARG CB C 30.853 0.100 1 621 204 204 ARG N N 120.995 0.050 1 622 205 205 GLU H H 8.453 0.010 1 623 205 205 GLU CA C 59.147 0.100 1 624 205 205 GLU CB C 30.091 0.100 1 625 205 205 GLU N N 121.064 0.050 1 626 206 206 SER H H 7.386 0.010 1 627 206 206 SER CA C 60.761 0.100 1 628 206 206 SER CB C 66.484 0.100 1 629 206 206 SER N N 112.571 0.050 1 630 207 207 GLY H H 7.649 0.010 1 631 207 207 GLY CA C 46.555 0.100 1 632 207 207 GLY N N 110.474 0.050 1 633 208 208 SER H H 7.828 0.010 1 634 208 208 SER CA C 63.587 0.100 1 635 208 208 SER CB C 64.425 0.100 1 636 208 208 SER N N 114.375 0.050 1 637 209 209 LEU H H 8.232 0.010 1 638 209 209 LEU CA C 54.589 0.100 1 639 209 209 LEU CB C 40.550 0.100 1 640 209 209 LEU N N 116.588 0.050 1 641 210 210 SER H H 7.344 0.010 1 642 210 210 SER CA C 57.452 0.100 1 643 210 210 SER CB C 64.038 0.100 1 644 210 210 SER N N 116.482 0.050 1 645 211 211 PRO CA C 64.960 0.100 1 646 211 211 PRO CB C 31.762 0.100 1 647 212 212 GLU H H 8.138 0.010 1 648 212 212 GLU CA C 58.036 0.100 1 649 212 212 GLU CB C 29.081 0.100 1 650 212 212 GLU N N 118.013 0.050 1 651 213 213 HIS H H 7.457 0.010 1 652 213 213 HIS CA C 54.648 0.100 1 653 213 213 HIS CB C 33.916 0.100 1 654 213 213 HIS N N 119.192 0.050 1 655 214 214 GLY H H 7.270 0.010 1 656 214 214 GLY CA C 44.919 0.100 1 657 214 214 GLY N N 104.869 0.050 1 658 215 215 PRO CA C 63.120 0.100 1 659 215 215 PRO CB C 31.545 0.100 1 660 216 216 VAL H H 8.980 0.010 1 661 216 216 VAL CA C 62.068 0.100 1 662 216 216 VAL CB C 31.682 0.100 1 663 216 216 VAL N N 126.090 0.050 1 664 217 217 VAL H H 7.679 0.010 1 665 217 217 VAL CA C 62.075 0.100 1 666 217 217 VAL CB C 32.744 0.100 1 667 217 217 VAL N N 126.806 0.050 1 668 218 218 VAL H H 9.594 0.010 1 669 218 218 VAL CA C 60.702 0.100 1 670 218 218 VAL CB C 34.136 0.100 1 671 218 218 VAL N N 129.389 0.050 1 672 219 219 HIS H H 9.167 0.010 1 673 219 219 HIS CA C 55.949 0.100 1 674 219 219 HIS CB C 35.078 0.100 1 675 219 219 HIS N N 122.000 0.050 1 676 220 220 CYS H H 6.027 0.010 1 677 220 220 CYS CA C 57.277 0.100 1 678 220 220 CYS CB C 29.159 0.100 1 679 220 220 CYS N N 120.430 0.050 1 680 222 222 ALA CA C 52.310 0.100 1 681 222 222 ALA CB C 20.834 0.100 1 682 223 223 GLY H H 8.774 0.010 1 683 223 223 GLY CA C 48.133 0.100 1 684 223 223 GLY N N 112.170 0.050 1 685 224 224 ILE H H 7.256 0.010 1 686 224 224 ILE CA C 62.068 0.100 1 687 224 224 ILE CB C 40.588 0.100 1 688 224 224 ILE N N 108.175 0.050 1 689 226 226 ARG CA C 59.117 0.100 1 690 226 226 ARG CB C 38.655 0.100 1 691 227 227 SER H H 7.485 0.010 1 692 227 227 SER CA C 63.624 0.100 1 693 227 227 SER CB C 69.205 0.100 1 694 227 227 SER N N 115.930 0.050 1 695 228 228 GLY H H 6.361 0.010 1 696 228 228 GLY CA C 47.782 0.100 1 697 228 228 GLY N N 106.642 0.050 1 698 229 229 THR H H 7.733 0.010 1 699 229 229 THR CA C 67.531 0.100 1 700 229 229 THR CB C 68.982 0.100 1 701 229 229 THR N N 117.692 0.050 1 702 230 230 PHE H H 7.542 0.010 1 703 230 230 PHE CA C 63.065 0.100 1 704 230 230 PHE CB C 40.415 0.100 1 705 230 230 PHE N N 120.488 0.050 1 706 231 231 CYS H H 7.390 0.010 1 707 231 231 CYS CA C 62.886 0.100 1 708 231 231 CYS CB C 27.059 0.100 1 709 231 231 CYS N N 115.676 0.050 1 710 232 232 LEU H H 8.513 0.010 1 711 232 232 LEU CA C 58.854 0.100 1 712 232 232 LEU CB C 42.900 0.100 1 713 232 232 LEU N N 121.931 0.050 1 714 233 233 ALA H H 8.077 0.010 1 715 233 233 ALA CA C 55.710 0.100 1 716 233 233 ALA CB C 16.909 0.100 1 717 233 233 ALA N N 119.991 0.050 1 718 234 234 ASP H H 7.506 0.010 1 719 234 234 ASP CA C 58.914 0.100 1 720 234 234 ASP CB C 41.763 0.100 1 721 234 234 ASP N N 114.277 0.050 1 722 235 235 THR H H 8.508 0.010 1 723 235 235 THR CA C 69.518 0.100 1 724 235 235 THR CB C 68.366 0.100 1 725 235 235 THR N N 114.792 0.050 1 726 236 236 CYS H H 8.344 0.010 1 727 236 236 CYS CA C 66.548 0.100 1 728 236 236 CYS CB C 28.120 0.100 1 729 236 236 CYS N N 118.108 0.050 1 730 237 237 LEU H H 7.884 0.010 1 731 237 237 LEU CA C 58.638 0.100 1 732 237 237 LEU CB C 41.379 0.100 1 733 237 237 LEU N N 117.685 0.050 1 734 238 238 LEU H H 8.176 0.010 1 735 238 238 LEU CA C 58.974 0.100 1 736 238 238 LEU CB C 41.447 0.100 1 737 238 238 LEU N N 119.379 0.050 1 738 239 239 LEU H H 7.853 0.010 1 739 239 239 LEU CA C 58.440 0.100 1 740 239 239 LEU CB C 42.416 0.100 1 741 239 239 LEU N N 122.428 0.050 1 742 240 240 MET H H 7.880 0.010 1 743 240 240 MET CA C 60.140 0.100 1 744 240 240 MET CB C 33.166 0.100 1 745 240 240 MET N N 117.527 0.050 1 746 241 241 ASP H H 7.161 0.010 1 747 241 241 ASP CA C 56.576 0.100 1 748 241 241 ASP CB C 42.900 0.100 1 749 241 241 ASP N N 117.100 0.050 1 750 242 242 LYS H H 7.977 0.010 1 751 242 242 LYS CA C 58.504 0.100 1 752 242 242 LYS CB C 33.488 0.100 1 753 242 242 LYS N N 118.019 0.050 1 754 243 243 ARG H H 7.968 0.010 1 755 243 243 ARG CA C 57.248 0.100 1 756 243 243 ARG CB C 31.304 0.100 1 757 243 243 ARG N N 117.320 0.050 1 758 244 244 LYS H H 7.974 0.010 1 759 244 244 LYS CA C 57.773 0.100 1 760 244 244 LYS CB C 31.012 0.100 1 761 244 244 LYS N N 118.747 0.050 1 762 246 246 PRO CA C 65.457 0.100 1 763 246 246 PRO CB C 32.440 0.100 1 764 247 247 SER H H 8.088 0.010 1 765 247 247 SER CA C 60.870 0.100 1 766 247 247 SER CB C 63.743 0.100 1 767 247 247 SER N N 113.235 0.050 1 768 248 248 SER H H 7.646 0.010 1 769 248 248 SER CA C 59.672 0.100 1 770 248 248 SER CB C 64.880 0.100 1 771 248 248 SER N N 115.510 0.050 1 772 249 249 VAL H H 7.190 0.010 1 773 249 249 VAL CA C 63.938 0.100 1 774 249 249 VAL CB C 31.953 0.100 1 775 249 249 VAL N N 123.826 0.050 1 776 250 250 ASP H H 8.405 0.010 1 777 250 250 ASP CA C 52.340 0.100 1 778 250 250 ASP CB C 42.369 0.100 1 779 250 250 ASP N N 129.656 0.050 1 780 251 251 ILE H H 8.424 0.010 1 781 251 251 ILE CA C 65.953 0.100 1 782 251 251 ILE CB C 38.125 0.100 1 783 251 251 ILE N N 126.680 0.050 1 784 252 252 LYS H H 7.831 0.010 1 785 252 252 LYS CA C 60.929 0.100 1 786 252 252 LYS CB C 30.980 0.100 1 787 252 252 LYS N N 118.373 0.050 1 788 253 253 LYS H H 7.126 0.010 1 789 253 253 LYS CA C 59.818 0.100 1 790 253 253 LYS CB C 32.632 0.100 1 791 253 253 LYS N N 117.769 0.050 1 792 254 254 VAL H H 8.058 0.010 1 793 254 254 VAL CA C 67.064 0.100 1 794 254 254 VAL N N 121.951 0.050 1 795 255 255 LEU H H 8.371 0.010 1 796 255 255 LEU CA C 58.736 0.100 1 797 255 255 LEU CB C 40.926 0.100 1 798 255 255 LEU N N 121.225 0.050 1 799 257 257 GLU CA C 60.111 0.100 1 800 257 257 GLU CB C 29.118 0.100 1 801 258 258 MET H H 8.577 0.010 1 802 258 258 MET CA C 61.513 0.100 1 803 258 258 MET CB C 33.798 0.100 1 804 258 258 MET N N 119.485 0.050 1 805 259 259 ARG H H 8.542 0.010 1 806 259 259 ARG CA C 58.591 0.100 1 807 259 259 ARG CB C 30.621 0.100 1 808 259 259 ARG N N 118.088 0.050 1 809 260 260 LYS H H 7.617 0.010 1 810 260 260 LYS CA C 59.497 0.100 1 811 260 260 LYS CB C 31.834 0.100 1 812 260 260 LYS N N 119.382 0.050 1 813 261 261 PHE H H 8.149 0.010 1 814 261 261 PHE CA C 59.935 0.100 1 815 261 261 PHE CB C 41.692 0.100 1 816 261 261 PHE N N 113.010 0.050 1 817 262 262 ARG H H 7.458 0.010 1 818 262 262 ARG CA C 57.218 0.100 1 819 262 262 ARG CB C 32.557 0.100 1 820 262 262 ARG N N 121.037 0.050 1 821 263 263 MET H H 8.362 0.010 1 822 263 263 MET CA C 55.816 0.100 1 823 263 263 MET CB C 32.592 0.100 1 824 263 263 MET N N 122.733 0.050 1 825 264 264 GLY H H 8.778 0.010 1 826 264 264 GLY CA C 46.954 0.100 1 827 264 264 GLY N N 102.142 0.050 1 828 265 265 LEU H H 6.358 0.010 1 829 265 265 LEU CA C 56.275 0.100 1 830 265 265 LEU CB C 41.675 0.100 1 831 265 265 LEU N N 115.378 0.050 1 832 266 266 ILE H H 8.332 0.010 1 833 266 266 ILE CA C 65.200 0.100 1 834 266 266 ILE CB C 32.074 0.100 1 835 266 266 ILE N N 115.953 0.050 1 836 267 267 GLN H H 8.731 0.010 1 837 267 267 GLN CA C 58.036 0.100 1 838 267 267 GLN CB C 33.183 0.100 1 839 267 267 GLN N N 126.391 0.050 1 840 268 268 THR H H 6.661 0.010 1 841 268 268 THR CA C 58.416 0.100 1 842 268 268 THR CB C 73.754 0.100 1 843 268 268 THR N N 105.483 0.050 1 844 269 269 ALA H H 8.599 0.010 1 845 269 269 ALA CA C 54.998 0.100 1 846 269 269 ALA CB C 17.737 0.100 1 847 269 269 ALA N N 123.837 0.050 1 848 270 270 ASP H H 7.833 0.010 1 849 270 270 ASP CA C 57.364 0.100 1 850 270 270 ASP CB C 40.247 0.100 1 851 270 270 ASP N N 116.564 0.050 1 852 271 271 GLN H H 7.792 0.010 1 853 271 271 GLN CA C 59.585 0.100 1 854 271 271 GLN CB C 28.651 0.100 1 855 271 271 GLN N N 120.174 0.050 1 856 272 272 LEU H H 7.536 0.010 1 857 272 272 LEU CA C 58.971 0.100 1 858 272 272 LEU CB C 41.384 0.100 1 859 272 272 LEU N N 124.415 0.050 1 860 273 273 ARG H H 7.879 0.010 1 861 273 273 ARG CA C 60.227 0.100 1 862 273 273 ARG CB C 29.030 0.100 1 863 273 273 ARG N N 121.626 0.050 1 864 274 274 PHE H H 8.188 0.010 1 865 274 274 PHE CA C 62.272 0.100 1 866 274 274 PHE CB C 39.868 0.100 1 867 274 274 PHE N N 117.977 0.050 1 868 275 275 SER H H 7.940 0.010 1 869 275 275 SER CA C 64.463 0.100 1 870 275 275 SER CB C 63.440 0.100 1 871 275 275 SER N N 115.885 0.050 1 872 276 276 TYR CA C 58.351 0.100 1 873 276 276 TYR CB C 41.778 0.100 1 874 277 277 LEU H H 8.382 0.010 1 875 277 277 LEU CA C 58.409 0.100 1 876 277 277 LEU CB C 42.183 0.100 1 877 277 277 LEU N N 119.178 0.050 1 878 278 278 ALA H H 8.493 0.010 1 879 278 278 ALA CA C 55.232 0.100 1 880 278 278 ALA CB C 16.827 0.100 1 881 278 278 ALA N N 119.839 0.050 1 882 279 279 VAL H H 7.769 0.010 1 883 279 279 VAL CA C 67.473 0.100 1 884 279 279 VAL CB C 31.223 0.100 1 885 279 279 VAL N N 118.708 0.050 1 886 280 280 ILE H H 8.443 0.010 1 887 280 280 ILE CA C 66.645 0.100 1 888 280 280 ILE CB C 38.553 0.100 1 889 280 280 ILE N N 120.243 0.050 1 890 281 281 GLU CA C 59.380 0.100 1 891 281 281 GLU CB C 28.722 0.100 1 892 282 282 GLY H H 8.677 0.010 1 893 282 282 GLY CA C 48.308 0.100 1 894 282 282 GLY N N 109.948 0.050 1 895 283 283 ALA H H 8.543 0.010 1 896 283 283 ALA CA C 55.407 0.100 1 897 283 283 ALA CB C 18.722 0.100 1 898 283 283 ALA N N 125.420 0.050 1 899 284 284 LYS H H 7.484 0.010 1 900 284 284 LYS CA C 59.818 0.100 1 901 284 284 LYS CB C 32.406 0.100 1 902 284 284 LYS N N 116.521 0.050 1 903 285 285 PHE H H 7.607 0.010 1 904 285 285 PHE CA C 60.549 0.100 1 905 285 285 PHE CB C 39.489 0.100 1 906 285 285 PHE N N 118.373 0.050 1 907 286 286 ILE H H 7.896 0.010 1 908 286 286 ILE CA C 63.587 0.100 1 909 286 286 ILE CB C 38.322 0.100 1 910 286 286 ILE N N 118.688 0.050 1 911 287 287 MET H H 8.071 0.010 1 912 287 287 MET CA C 56.371 0.100 1 913 287 287 MET CB C 32.440 0.100 1 914 287 287 MET N N 118.609 0.050 1 915 288 288 GLY H H 7.579 0.010 1 916 288 288 GLY CA C 46.000 0.100 1 917 288 288 GLY N N 108.309 0.050 1 918 289 289 ASP H H 8.036 0.010 1 919 289 289 ASP CA C 54.618 0.100 1 920 289 289 ASP CB C 41.763 0.100 1 921 289 289 ASP N N 121.052 0.050 1 922 290 290 SER H H 8.301 0.010 1 923 290 290 SER CA C 60.052 0.100 1 924 290 290 SER CB C 63.847 0.100 1 925 290 290 SER N N 118.629 0.050 1 926 291 291 SER H H 8.388 0.010 1 927 291 291 SER CA C 60.198 0.100 1 928 291 291 SER CB C 63.959 0.100 1 929 291 291 SER N N 118.796 0.050 1 930 292 292 VAL H H 7.756 0.010 1 931 292 292 VAL CA C 66.804 0.100 1 932 292 292 VAL CB C 30.408 0.100 1 933 292 292 VAL N N 121.603 0.050 1 934 295 295 GLN CA C 59.804 0.100 1 935 296 296 TRP H H 8.026 0.010 1 936 296 296 TRP CA C 58.321 0.100 1 937 296 296 TRP CB C 29.158 0.100 1 938 296 296 TRP N N 121.202 0.050 1 939 297 297 LYS H H 7.703 0.010 1 940 297 297 LYS CA C 57.817 0.100 1 941 297 297 LYS CB C 32.895 0.100 1 942 297 297 LYS N N 122.246 0.050 1 943 298 298 GLU H H 8.033 0.010 1 944 298 298 GLU CA C 57.773 0.100 1 945 298 298 GLU CB C 29.712 0.100 1 946 298 298 GLU N N 121.201 0.050 1 947 299 299 LEU H H 8.063 0.010 1 948 299 299 LEU CA C 55.957 0.100 1 949 299 299 LEU N N 122.384 0.050 1 950 300 300 SER CA C 61.316 0.100 1 951 301 301 HIS H H 7.959 0.010 1 952 301 301 HIS CA C 58.499 0.100 1 953 301 301 HIS CB C 30.482 0.100 1 954 301 301 HIS N N 123.415 0.050 1 955 302 302 GLU H H 7.939 0.010 1 956 302 302 GLU CA C 57.452 0.100 1 957 302 302 GLU CB C 30.334 0.100 1 958 302 302 GLU N N 118.491 0.050 1 959 303 303 ASP H H 8.306 0.010 1 960 303 303 ASP CA C 55.057 0.100 1 961 303 303 ASP CB C 41.384 0.100 1 962 303 303 ASP N N 121.270 0.050 1 963 304 304 LEU H H 7.956 0.010 1 964 304 304 LEU CA C 55.524 0.100 1 965 304 304 LEU CB C 42.521 0.100 1 966 304 304 LEU N N 122.860 0.050 1 967 305 305 GLU H H 7.939 0.010 1 968 305 305 GLU CA C 54.443 0.100 1 969 305 305 GLU CB C 30.697 0.100 1 970 305 305 GLU N N 120.819 0.050 1 971 307 307 HIS CA C 55.203 0.100 1 972 307 307 HIS CB C 33.292 0.100 1 973 308 308 ASN H H 8.736 0.010 1 974 308 308 ASN CA C 54.531 0.100 1 975 308 308 ASN CB C 40.635 0.100 1 976 308 308 ASN N N 123.452 0.050 1 stop_ save_