data_25375 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of PTP1B bound to the inhibitor CPT-157633 ; _BMRB_accession_number 25375 _BMRB_flat_file_name bmr25375.str _Entry_type original _Submission_date 2014-12-01 _Accession_date 2014-12-01 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Protein Tyrosine Phosphatase 1B (residues 1-301) bound to the inhibitor CPT-157633' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Peti Wolfgang . . 2 Connors Christopher Ryan . 3 Page Rebecca . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 212 "13C chemical shifts" 244 "15N chemical shifts" 212 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-08-04 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 19223 'PTP1B (residues 1-301)' 19224 'PTP1B (residues 1-393)' stop_ _Original_release_date 2015-08-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; PTP1B inhibition suggests a therapeutic strategy for Rett syndrome ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26214522 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Krishnan Navasona . . 2 Krishnan Keerthi . . 3 Connors Christopher R. . 4 Choy Meng S. . 5 Page Rebecca . . 6 Peti Wolfgang . . 7 'Van Aelst' Linda . . 8 Shea Stephen D. . 9 Tonks Nicholas . . stop_ _Journal_abbreviation 'J. Clin. Invest.' _Journal_volume 125 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3163 _Page_last 3177 _Year 2015 _Details . loop_ _Keyword PTP1B 'Rett syndrome' phosphatase 'protein tyrosine phosphatase' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'PTP1B CPT-157633 Complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PTP1B $PTP1B CPT-157633 $CPT-157633 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _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' loop_ _Biological_function 'Protein Tyrosine Phosphatase' stop_ _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 -2 GLY 2 -1 HIS 3 0 MET 4 1 ALA 5 2 SER 6 3 MET 7 4 GLU 8 5 MET 9 6 GLU 10 7 LYS 11 8 GLU 12 9 PHE 13 10 GLU 14 11 GLN 15 12 ILE 16 13 ASP 17 14 LYS 18 15 SER 19 16 GLY 20 17 SER 21 18 TRP 22 19 ALA 23 20 ALA 24 21 ILE 25 22 TYR 26 23 GLN 27 24 ASP 28 25 ILE 29 26 ARG 30 27 HIS 31 28 GLU 32 29 ALA 33 30 SER 34 31 ASP 35 32 PHE 36 33 PRO 37 34 CYS 38 35 ARG 39 36 VAL 40 37 ALA 41 38 LYS 42 39 LEU 43 40 PRO 44 41 LYS 45 42 ASN 46 43 LYS 47 44 ASN 48 45 ARG 49 46 ASN 50 47 ARG 51 48 TYR 52 49 ARG 53 50 ASP 54 51 VAL 55 52 SER 56 53 PRO 57 54 PHE 58 55 ASP 59 56 HIS 60 57 SER 61 58 ARG 62 59 ILE 63 60 LYS 64 61 LEU 65 62 HIS 66 63 GLN 67 64 GLU 68 65 ASP 69 66 ASN 70 67 ASP 71 68 TYR 72 69 ILE 73 70 ASN 74 71 ALA 75 72 SER 76 73 LEU 77 74 ILE 78 75 LYS 79 76 MET 80 77 GLU 81 78 GLU 82 79 ALA 83 80 GLN 84 81 ARG 85 82 SER 86 83 TYR 87 84 ILE 88 85 LEU 89 86 THR 90 87 GLN 91 88 GLY 92 89 PRO 93 90 LEU 94 91 PRO 95 92 ASN 96 93 THR 97 94 CYS 98 95 GLY 99 96 HIS 100 97 PHE 101 98 TRP 102 99 GLU 103 100 MET 104 101 VAL 105 102 TRP 106 103 GLU 107 104 GLN 108 105 LYS 109 106 SER 110 107 ARG 111 108 GLY 112 109 VAL 113 110 VAL 114 111 MET 115 112 LEU 116 113 ASN 117 114 ARG 118 115 VAL 119 116 MET 120 117 GLU 121 118 LYS 122 119 GLY 123 120 SER 124 121 LEU 125 122 LYS 126 123 CYS 127 124 ALA 128 125 GLN 129 126 TYR 130 127 TRP 131 128 PRO 132 129 GLN 133 130 LYS 134 131 GLU 135 132 GLU 136 133 LYS 137 134 GLU 138 135 MET 139 136 ILE 140 137 PHE 141 138 GLU 142 139 ASP 143 140 THR 144 141 ASN 145 142 LEU 146 143 LYS 147 144 LEU 148 145 THR 149 146 LEU 150 147 ILE 151 148 SER 152 149 GLU 153 150 ASP 154 151 ILE 155 152 LYS 156 153 SER 157 154 TYR 158 155 TYR 159 156 THR 160 157 VAL 161 158 ARG 162 159 GLN 163 160 LEU 164 161 GLU 165 162 LEU 166 163 GLU 167 164 ASN 168 165 LEU 169 166 THR 170 167 THR 171 168 GLN 172 169 GLU 173 170 THR 174 171 ARG 175 172 GLU 176 173 ILE 177 174 LEU 178 175 HIS 179 176 PHE 180 177 HIS 181 178 TYR 182 179 THR 183 180 THR 184 181 TRP 185 182 PRO 186 183 ASP 187 184 PHE 188 185 GLY 189 186 VAL 190 187 PRO 191 188 GLU 192 189 SER 193 190 PRO 194 191 ALA 195 192 SER 196 193 PHE 197 194 LEU 198 195 ASN 199 196 PHE 200 197 LEU 201 198 PHE 202 199 LYS 203 200 VAL 204 201 ARG 205 202 GLU 206 203 SER 207 204 GLY 208 205 SER 209 206 LEU 210 207 SER 211 208 PRO 212 209 GLU 213 210 HIS 214 211 GLY 215 212 PRO 216 213 VAL 217 214 VAL 218 215 VAL 219 216 HIS 220 217 CYS 221 218 SER 222 219 ALA 223 220 GLY 224 221 ILE 225 222 GLY 226 223 ARG 227 224 SER 228 225 GLY 229 226 THR 230 227 PHE 231 228 CYS 232 229 LEU 233 230 ALA 234 231 ASP 235 232 THR 236 233 CYS 237 234 LEU 238 235 LEU 239 236 LEU 240 237 MET 241 238 ASP 242 239 LYS 243 240 ARG 244 241 LYS 245 242 ASP 246 243 PRO 247 244 SER 248 245 SER 249 246 VAL 250 247 ASP 251 248 ILE 252 249 LYS 253 250 LYS 254 251 VAL 255 252 LEU 256 253 LEU 257 254 GLU 258 255 MET 259 256 ARG 260 257 LYS 261 258 PHE 262 259 ARG 263 260 MET 264 261 GLY 265 262 LEU 266 263 ILE 267 264 GLN 268 265 THR 269 266 ALA 270 267 ASP 271 268 GLN 272 269 LEU 273 270 ARG 274 271 PHE 275 272 SER 276 273 TYR 277 274 LEU 278 275 ALA 279 276 VAL 280 277 ILE 281 278 GLU 282 279 GLY 283 280 ALA 284 281 LYS 285 282 PHE 286 283 ILE 287 284 MET 288 285 GLY 289 286 ASP 290 287 SER 291 288 SER 292 289 VAL 293 290 GLN 294 291 ASP 295 292 GLN 296 293 TRP 297 294 LYS 298 295 GLU 299 296 LEU 300 297 SER 301 298 HIS 302 299 GLU 303 300 ASP 304 301 LEU 305 302 GLU 306 303 PRO 307 304 HIS 308 305 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 100.00 308 100.00 100.00 0.00e+00 BMRB 19224 PTP1B 99.35 398 100.00 100.00 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 3.70e-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 3.70e-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_ ############# # Ligands # ############# save_CPT-157633 _Saveframe_category ligand _Mol_type non-polymer _Name_common CPT-157633 _Molecular_mass . _Details . _Mol_thiol_state 'all free' _Sequence_homology_query_date . 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 . RP1B stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '0.2 mM PTP1B, 0.3 mM CPT-157633, 50 mM HEPES pH 6.8, 150 mM NaCl, 0.5 mM TCEP + 10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PTP1B 0.2 mM '[U-99% 13C; U-99% 15N; U-95% 2H]' $CPT-157633 0.3 mM 'natural abundance' HEPES 50 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' TCEP 0.5 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.115 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.1.4 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _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_1 save_ save_3D_TROSY-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCA' _Sample_label $sample_1 save_ save_3D_TROSY-HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HN(CO)CA' _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' 150 . mM pH 6.8 . pH pressure ambient . 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' stop_ loop_ _Sample_label $sample_1 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 2 5 SER CA C 60.370 0.000 . 2 3 6 MET H H 8.593 0.001 . 3 3 6 MET CA C 60.099 0.008 . 4 3 6 MET N N 119.556 0.058 . 5 4 7 GLU H H 7.963 0.005 . 6 4 7 GLU CA C 60.439 0.085 . 7 4 7 GLU N N 119.636 0.036 . 8 5 8 MET H H 7.631 0.004 . 9 5 8 MET CA C 59.960 0.000 . 10 5 8 MET N N 120.667 0.100 . 11 6 9 GLU CA C 59.480 0.000 . 12 7 10 LYS H H 8.339 0.002 . 13 7 10 LYS CA C 59.710 0.010 . 14 7 10 LYS N N 119.763 0.034 . 15 8 11 GLU H H 8.201 0.002 . 16 8 11 GLU CA C 60.152 0.006 . 17 8 11 GLU N N 121.717 0.012 . 18 9 12 PHE H H 8.452 0.002 . 19 9 12 PHE CA C 62.998 0.090 . 20 9 12 PHE N N 119.303 0.129 . 21 10 13 GLU H H 8.126 0.008 . 22 10 13 GLU CA C 60.088 0.019 . 23 10 13 GLU N N 117.830 0.048 . 24 11 14 GLN H H 7.688 0.000 . 25 11 14 GLN CA C 59.531 0.034 . 26 11 14 GLN N N 118.788 0.060 . 27 12 15 ILE H H 8.021 0.003 . 28 12 15 ILE CA C 65.566 0.037 . 29 12 15 ILE N N 122.727 0.038 . 30 13 16 ASP H H 8.385 0.005 . 31 13 16 ASP CA C 58.542 0.027 . 32 13 16 ASP N N 119.659 0.039 . 33 14 17 LYS H H 8.263 0.001 . 34 14 17 LYS CA C 59.497 0.017 . 35 14 17 LYS N N 117.948 0.002 . 36 15 18 SER H H 7.399 0.004 . 37 15 18 SER CA C 59.199 0.025 . 38 15 18 SER N N 111.563 0.052 . 39 16 19 GLY H H 7.747 0.001 . 40 16 19 GLY CA C 47.587 0.007 . 41 16 19 GLY N N 113.044 0.020 . 42 17 20 SER H H 7.683 0.018 . 43 17 20 SER CA C 59.249 0.076 . 44 17 20 SER N N 111.537 0.044 . 45 18 21 TRP H H 7.042 0.002 . 46 18 21 TRP HE1 H 10.926 0.000 . 47 18 21 TRP CA C 61.151 0.126 . 48 18 21 TRP N N 121.926 0.100 . 49 18 21 TRP NE1 N 130.979 0.000 . 50 19 22 ALA H H 8.599 0.003 . 51 19 22 ALA CA C 56.273 0.057 . 52 19 22 ALA N N 119.576 0.026 . 53 20 23 ALA H H 7.595 0.000 . 54 20 23 ALA CA C 55.778 0.002 . 55 20 23 ALA N N 122.809 0.075 . 56 21 24 ILE H H 7.831 0.002 . 57 21 24 ILE CA C 64.155 0.010 . 58 21 24 ILE N N 119.454 0.067 . 59 22 25 TYR H H 8.533 0.023 . 60 22 25 TYR CA C 62.711 0.004 . 61 22 25 TYR N N 120.262 0.076 . 62 23 26 GLN H H 8.106 0.003 . 63 23 26 GLN CA C 59.282 0.022 . 64 23 26 GLN N N 118.324 0.038 . 65 24 27 ASP H H 7.755 0.003 . 66 24 27 ASP CA C 58.490 0.024 . 67 24 27 ASP N N 121.060 0.105 . 68 25 28 ILE H H 7.617 0.008 . 69 25 28 ILE CA C 65.755 0.021 . 70 25 28 ILE N N 120.653 0.102 . 71 26 29 ARG H H 7.637 0.003 . 72 26 29 ARG CA C 60.618 0.025 . 73 26 29 ARG N N 117.320 0.053 . 74 27 30 HIS H H 8.060 0.002 . 75 27 30 HIS CA C 58.748 0.048 . 76 27 30 HIS N N 116.555 0.022 . 77 28 31 GLU H H 7.784 0.002 . 78 28 31 GLU CA C 57.095 0.014 . 79 28 31 GLU N N 117.787 0.055 . 80 29 32 ALA H H 7.334 0.001 . 81 29 32 ALA CA C 53.450 0.019 . 82 29 32 ALA N N 123.363 0.040 . 83 30 33 SER H H 7.901 0.000 . 84 30 33 SER CA C 60.147 0.012 . 85 30 33 SER N N 117.455 0.058 . 86 31 34 ASP H H 8.001 0.004 . 87 31 34 ASP CA C 54.274 0.004 . 88 31 34 ASP N N 122.658 0.050 . 89 32 35 PHE H H 6.544 0.003 . 90 32 35 PHE CA C 55.894 0.000 . 91 32 35 PHE N N 119.742 0.038 . 92 33 36 PRO CA C 65.087 0.000 . 93 34 37 CYS H H 9.029 0.001 . 94 34 37 CYS CA C 57.151 0.007 . 95 34 37 CYS N N 126.452 0.062 . 96 35 38 ARG H H 9.382 0.002 . 97 35 38 ARG CA C 60.492 0.003 . 98 35 38 ARG N N 122.023 0.020 . 99 36 39 VAL H H 9.567 0.003 . 100 36 39 VAL CA C 67.611 0.019 . 101 36 39 VAL N N 121.739 0.019 . 102 37 40 ALA H H 8.387 0.003 . 103 37 40 ALA CA C 55.346 0.015 . 104 37 40 ALA N N 121.670 0.038 . 105 38 41 LYS H H 6.706 0.001 . 106 38 41 LYS CA C 55.873 0.047 . 107 38 41 LYS N N 111.116 0.027 . 108 39 42 LEU H H 7.392 0.000 . 109 39 42 LEU CA C 54.757 0.000 . 110 39 42 LEU N N 123.780 0.028 . 111 40 43 PRO CA C 66.910 0.000 . 112 41 44 LYS H H 8.025 0.002 . 113 41 44 LYS CA C 58.634 0.008 . 114 41 44 LYS N N 114.219 0.029 . 115 42 45 ASN H H 7.648 0.001 . 116 42 45 ASN CA C 53.622 0.002 . 117 42 45 ASN N N 117.016 0.050 . 118 43 46 LYS H H 7.293 0.001 . 119 43 46 LYS CA C 61.442 0.000 . 120 43 46 LYS N N 123.493 0.073 . 121 44 47 ASN H H 8.306 0.002 . 122 44 47 ASN CA C 53.766 0.007 . 123 44 47 ASN N N 113.701 0.034 . 124 45 48 ARG H H 7.780 0.002 . 125 45 48 ARG CA C 56.813 0.076 . 126 45 48 ARG N N 115.423 0.015 . 127 46 49 ASN H H 7.380 0.002 . 128 46 49 ASN CA C 53.203 0.025 . 129 46 49 ASN N N 119.857 0.059 . 130 47 50 ARG H H 9.082 0.003 . 131 47 50 ARG CA C 59.851 0.000 . 132 47 50 ARG N N 126.677 0.026 . 133 48 51 TYR H H 9.281 0.000 . 134 48 51 TYR N N 117.203 0.000 . 135 49 52 ARG CA C 58.660 0.000 . 136 50 53 ASP H H 8.873 0.002 . 137 50 53 ASP CA C 53.486 0.002 . 138 50 53 ASP N N 113.270 0.032 . 139 51 54 VAL H H 6.837 0.001 . 140 51 54 VAL CA C 63.382 0.002 . 141 51 54 VAL N N 119.646 0.031 . 142 52 55 SER H H 7.698 0.000 . 143 52 55 SER CA C 56.377 0.000 . 144 52 55 SER N N 123.038 0.087 . 145 53 56 PRO CA C 62.658 0.000 . 146 54 57 PHE H H 7.038 0.003 . 147 54 57 PHE CA C 56.260 0.020 . 148 54 57 PHE N N 124.482 0.025 . 149 55 58 ASP H H 9.205 0.004 . 150 55 58 ASP CA C 59.788 0.141 . 151 55 58 ASP N N 124.572 0.033 . 152 56 59 HIS H H 8.923 0.001 . 153 56 59 HIS CA C 59.987 0.057 . 154 56 59 HIS N N 115.520 0.036 . 155 57 60 SER H H 6.279 0.006 . 156 57 60 SER CA C 56.137 0.061 . 157 57 60 SER N N 108.349 0.081 . 158 58 61 ARG H H 7.163 0.002 . 159 58 61 ARG CA C 56.407 0.008 . 160 58 61 ARG N N 123.241 0.037 . 161 59 62 ILE H H 7.054 0.000 . 162 59 62 ILE CA C 58.013 0.013 . 163 59 62 ILE N N 122.405 0.025 . 164 60 63 LYS H H 8.381 0.002 . 165 60 63 LYS CA C 55.779 0.014 . 166 60 63 LYS N N 127.260 0.021 . 167 61 64 LEU H H 9.160 0.001 . 168 61 64 LEU CA C 54.801 0.051 . 169 61 64 LEU N N 125.419 0.036 . 170 62 65 HIS H H 9.475 0.002 . 171 62 65 HIS CA C 54.840 0.034 . 172 62 65 HIS N N 123.976 0.067 . 173 63 66 GLN H H 7.350 0.004 . 174 63 66 GLN CA C 55.308 0.006 . 175 63 66 GLN N N 119.920 0.029 . 176 64 67 GLU H H 8.360 0.003 . 177 64 67 GLU CA C 58.663 0.020 . 178 64 67 GLU N N 121.351 0.033 . 179 65 68 ASP H H 8.246 0.000 . 180 65 68 ASP CA C 57.262 0.015 . 181 65 68 ASP N N 118.606 0.040 . 182 66 69 ASN H H 7.346 0.001 . 183 66 69 ASN CA C 54.088 0.043 . 184 66 69 ASN N N 114.293 0.036 . 185 67 70 ASP H H 8.057 0.001 . 186 67 70 ASP CA C 53.974 0.001 . 187 67 70 ASP N N 126.081 0.050 . 188 68 71 TYR H H 7.904 0.000 . 189 68 71 TYR CA C 61.712 0.022 . 190 68 71 TYR N N 118.752 0.041 . 191 69 72 ILE H H 7.585 0.001 . 192 69 72 ILE CA C 59.494 0.009 . 193 69 72 ILE N N 125.424 0.014 . 194 70 73 ASN H H 8.045 0.002 . 195 70 73 ASN CA C 53.154 0.009 . 196 70 73 ASN N N 125.800 0.080 . 197 71 74 ALA H H 7.641 0.000 . 198 71 74 ALA CA C 52.387 0.000 . 199 71 74 ALA N N 129.004 0.029 . 200 72 75 SER H H 9.015 0.002 . 201 72 75 SER CA C 58.220 0.022 . 202 72 75 SER N N 117.037 0.069 . 203 73 76 LEU H H 8.886 0.004 . 204 73 76 LEU CA C 54.795 0.023 . 205 73 76 LEU N N 126.933 0.025 . 206 74 77 ILE H H 9.389 0.003 . 207 74 77 ILE CA C 61.243 0.000 . 208 74 77 ILE N N 128.589 0.057 . 209 75 78 LYS CA C 54.050 0.000 . 210 76 79 MET H H 8.149 0.009 . 211 76 79 MET CA C 52.761 0.115 . 212 76 79 MET N N 124.283 0.095 . 213 77 80 GLU H H 8.272 0.000 . 214 77 80 GLU CA C 60.889 0.002 . 215 77 80 GLU N N 126.268 0.018 . 216 78 81 GLU H H 8.824 0.003 . 217 78 81 GLU CA C 59.707 0.007 . 218 78 81 GLU N N 121.278 0.030 . 219 79 82 ALA H H 7.345 0.001 . 220 79 82 ALA CA C 53.349 0.046 . 221 79 82 ALA N N 117.606 0.054 . 222 80 83 GLN H H 7.606 0.000 . 223 80 83 GLN CA C 56.840 0.019 . 224 80 83 GLN N N 111.616 0.049 . 225 81 84 ARG H H 7.160 0.001 . 226 81 84 ARG CA C 55.888 0.014 . 227 81 84 ARG N N 118.482 0.032 . 228 82 85 SER H H 7.647 0.003 . 229 82 85 SER CA C 57.275 0.073 . 230 82 85 SER N N 119.362 0.137 . 231 83 86 TYR H H 8.463 0.003 . 232 83 86 TYR CA C 55.929 0.039 . 233 83 86 TYR N N 117.053 0.111 . 234 84 87 ILE H H 9.255 0.007 . 235 84 87 ILE CA C 61.139 0.014 . 236 84 87 ILE N N 122.937 0.135 . 237 85 88 LEU H H 8.598 0.005 . 238 85 88 LEU CA C 54.817 0.018 . 239 85 88 LEU N N 129.085 0.040 . 240 86 89 THR H H 8.390 0.006 . 241 86 89 THR CA C 58.323 0.012 . 242 86 89 THR N N 116.100 0.052 . 243 87 90 GLN H H 6.297 0.002 . 244 87 90 GLN CA C 52.959 0.013 . 245 87 90 GLN N N 116.338 0.061 . 246 88 91 GLY H H 9.054 0.004 . 247 88 91 GLY CA C 45.998 0.000 . 248 88 91 GLY N N 113.459 0.055 . 249 89 92 PRO CA C 64.674 0.000 . 250 90 93 LEU H H 7.786 0.002 . 251 90 93 LEU CA C 53.835 0.000 . 252 90 93 LEU N N 123.351 0.035 . 253 91 94 PRO CA C 66.881 0.000 . 254 92 95 ASN H H 8.486 0.000 . 255 92 95 ASN CA C 54.611 0.004 . 256 92 95 ASN N N 106.979 0.039 . 257 93 96 THR H H 8.021 0.001 . 258 93 96 THR CA C 61.441 0.031 . 259 93 96 THR N N 111.833 0.014 . 260 94 97 CYS H H 7.445 0.004 . 261 94 97 CYS CA C 64.741 0.005 . 262 94 97 CYS N N 121.429 0.066 . 263 95 98 GLY H H 8.228 0.001 . 264 95 98 GLY CA C 48.322 0.015 . 265 95 98 GLY N N 108.623 0.042 . 266 96 99 HIS H H 7.332 0.002 . 267 96 99 HIS CA C 57.650 0.005 . 268 96 99 HIS N N 123.814 0.028 . 269 97 100 PHE H H 8.141 0.001 . 270 97 100 PHE CA C 62.741 0.000 . 271 97 100 PHE N N 119.512 0.020 . 272 106 109 SER CA C 61.916 0.000 . 273 107 110 ARG H H 9.348 0.004 . 274 107 110 ARG CA C 55.546 0.000 . 275 107 110 ARG N N 123.445 0.038 . 276 108 111 GLY H H 7.182 0.001 . 277 108 111 GLY CA C 44.797 0.000 . 278 108 111 GLY N N 102.766 0.111 . 279 112 115 LEU H H 8.370 0.007 . 280 112 115 LEU CA C 54.642 0.015 . 281 112 115 LEU N N 124.783 0.167 . 282 113 116 ASN H H 7.891 0.001 . 283 113 116 ASN CA C 52.506 0.000 . 284 113 116 ASN N N 114.371 0.124 . 285 114 117 ARG CA C 57.639 0.000 . 286 115 118 VAL H H 8.790 0.004 . 287 115 118 VAL CA C 63.433 0.001 . 288 115 118 VAL N N 121.671 0.045 . 289 116 119 MET H H 8.620 0.004 . 290 116 119 MET CA C 56.383 0.000 . 291 116 119 MET N N 121.346 0.042 . 292 119 122 GLY H H 7.415 0.004 . 293 119 122 GLY CA C 46.285 0.024 . 294 119 122 GLY N N 107.505 0.025 . 295 120 123 SER H H 7.915 0.002 . 296 120 123 SER CA C 58.643 0.000 . 297 120 123 SER N N 116.342 0.118 . 298 123 126 CYS CA C 59.657 0.000 . 299 124 127 ALA H H 7.811 0.002 . 300 124 127 ALA CA C 52.847 0.000 . 301 124 127 ALA N N 126.870 0.028 . 302 125 128 GLN CA C 56.042 0.000 . 303 126 129 TYR H H 6.466 0.000 . 304 126 129 TYR CA C 57.025 0.033 . 305 126 129 TYR N N 122.398 0.014 . 306 127 130 TRP H H 6.501 0.004 . 307 127 130 TRP CA C 56.136 0.000 . 308 127 130 TRP N N 120.503 0.096 . 309 134 137 GLU CA C 54.822 0.000 . 310 135 138 MET H H 8.790 0.001 . 311 135 138 MET CA C 55.948 0.010 . 312 135 138 MET N N 121.245 0.031 . 313 136 139 ILE H H 8.109 0.007 . 314 136 139 ILE CA C 60.656 0.004 . 315 136 139 ILE N N 122.355 0.023 . 316 137 140 PHE H H 8.843 0.004 . 317 137 140 PHE CA C 57.325 0.004 . 318 137 140 PHE N N 127.890 0.053 . 319 138 141 GLU H H 8.902 0.001 . 320 138 141 GLU CA C 59.669 0.031 . 321 138 141 GLU N N 124.302 0.034 . 322 139 142 ASP H H 9.015 0.003 . 323 139 142 ASP CA C 56.491 0.014 . 324 139 142 ASP N N 116.545 0.061 . 325 140 143 THR H H 7.402 0.000 . 326 140 143 THR CA C 61.120 0.028 . 327 140 143 THR N N 108.177 0.035 . 328 141 144 ASN H H 7.907 0.003 . 329 141 144 ASN CA C 54.442 0.010 . 330 141 144 ASN N N 121.083 0.025 . 331 142 145 LEU H H 7.361 0.002 . 332 142 145 LEU CA C 54.281 0.000 . 333 142 145 LEU N N 117.340 0.001 . 334 145 148 THR CA C 62.123 0.000 . 335 146 149 LEU H H 8.877 0.001 . 336 146 149 LEU CA C 56.034 0.020 . 337 146 149 LEU N N 128.043 0.037 . 338 147 150 ILE H H 8.808 0.002 . 339 147 150 ILE CA C 61.910 0.121 . 340 147 150 ILE N N 129.432 0.040 . 341 148 151 SER H H 7.725 0.001 . 342 148 151 SER CA C 58.458 0.017 . 343 148 151 SER N N 111.295 0.109 . 344 149 152 GLU H H 8.517 0.020 . 345 149 152 GLU CA C 56.620 0.014 . 346 149 152 GLU N N 120.169 0.187 . 347 150 153 ASP H H 8.834 0.004 . 348 150 153 ASP CA C 53.894 0.033 . 349 150 153 ASP N N 126.909 0.034 . 350 151 154 ILE H H 8.418 0.000 . 351 151 154 ILE CA C 63.016 0.021 . 352 151 154 ILE N N 127.013 0.036 . 353 152 155 LYS H H 8.123 0.001 . 354 152 155 LYS CA C 54.445 0.000 . 355 152 155 LYS N N 128.492 0.017 . 356 154 157 TYR CA C 55.805 0.000 . 357 155 158 TYR H H 6.372 0.005 . 358 155 158 TYR CA C 56.765 0.000 . 359 155 158 TYR N N 115.085 0.076 . 360 163 166 GLU CA C 55.731 0.000 . 361 164 167 ASN H H 8.076 0.000 . 362 164 167 ASN CA C 52.687 0.254 . 363 164 167 ASN N N 124.170 0.078 . 364 165 168 LEU H H 8.212 0.001 . 365 165 168 LEU CA C 57.519 0.003 . 366 165 168 LEU N N 125.941 0.023 . 367 166 169 THR H H 8.169 0.002 . 368 166 169 THR CA C 66.007 0.008 . 369 166 169 THR N N 115.132 0.029 . 370 167 170 THR H H 6.965 0.003 . 371 167 170 THR CA C 62.391 0.026 . 372 167 170 THR N N 109.388 0.039 . 373 168 171 GLN H H 8.306 0.000 . 374 168 171 GLN CA C 58.677 0.024 . 375 168 171 GLN N N 116.715 0.030 . 376 169 172 GLU H H 7.380 0.001 . 377 169 172 GLU CA C 56.945 0.029 . 378 169 172 GLU N N 119.718 0.013 . 379 170 173 THR H H 8.402 0.001 . 380 170 173 THR CA C 60.977 0.000 . 381 170 173 THR N N 113.975 0.042 . 382 173 176 ILE H H 8.579 0.007 . 383 173 176 ILE CA C 62.486 0.018 . 384 173 176 ILE N N 115.325 0.034 . 385 174 177 LEU H H 8.581 0.009 . 386 174 177 LEU CA C 58.390 0.000 . 387 174 177 LEU N N 119.646 0.080 . 388 180 183 THR H H 8.266 0.000 . 389 180 183 THR CA C 59.482 0.002 . 390 180 183 THR N N 117.859 0.000 . 391 181 184 TRP H H 6.917 0.000 . 392 181 184 TRP CA C 60.898 0.000 . 393 181 184 TRP N N 121.441 0.005 . 394 184 187 PHE CA C 61.589 0.000 . 395 185 188 GLY H H 8.030 0.000 . 396 185 188 GLY CA C 44.576 0.007 . 397 185 188 GLY N N 107.881 0.053 . 398 186 189 VAL H H 8.313 0.001 . 399 186 189 VAL CA C 58.999 0.000 . 400 186 189 VAL N N 113.903 0.020 . 401 190 193 PRO CA C 56.567 0.000 . 402 191 194 ALA H H 8.492 0.004 . 403 191 194 ALA CA C 53.767 0.000 . 404 191 194 ALA N N 125.537 0.050 . 405 192 195 SER H H 8.134 0.002 . 406 192 195 SER CA C 59.451 0.000 . 407 192 195 SER N N 114.434 0.048 . 408 196 199 PHE H H 8.289 0.205 . 409 196 199 PHE CA C 55.326 0.005 . 410 196 199 PHE N N 119.757 6.153 . 411 197 200 LEU H H 7.917 0.002 . 412 197 200 LEU CA C 55.729 0.025 . 413 197 200 LEU N N 122.201 0.013 . 414 198 201 PHE H H 8.176 0.001 . 415 198 201 PHE CA C 55.060 0.000 . 416 198 201 PHE N N 122.785 0.028 . 417 199 202 LYS H H 7.396 0.000 . 418 199 202 LYS N N 112.867 0.000 . 419 200 203 VAL CA C 66.568 0.000 . 420 201 204 ARG H H 8.362 0.002 . 421 201 204 ARG CA C 60.802 0.051 . 422 201 204 ARG N N 120.594 0.059 . 423 202 205 GLU H H 8.470 0.025 . 424 202 205 GLU CA C 59.148 0.007 . 425 202 205 GLU N N 120.547 0.126 . 426 203 206 SER H H 7.297 0.003 . 427 203 206 SER CA C 60.968 0.010 . 428 203 206 SER N N 112.538 0.086 . 429 204 207 GLY H H 7.569 0.000 . 430 204 207 GLY CA C 46.804 0.009 . 431 204 207 GLY N N 110.214 0.035 . 432 205 208 SER H H 7.807 0.001 . 433 205 208 SER CA C 63.728 0.031 . 434 205 208 SER N N 114.279 0.060 . 435 206 209 LEU H H 8.209 0.002 . 436 206 209 LEU CA C 54.478 0.042 . 437 206 209 LEU N N 116.508 0.031 . 438 207 210 SER H H 7.226 0.003 . 439 207 210 SER CA C 57.537 0.000 . 440 207 210 SER N N 115.997 0.062 . 441 208 211 PRO CA C 65.130 0.000 . 442 209 212 GLU H H 8.114 0.001 . 443 209 212 GLU CA C 58.158 0.018 . 444 209 212 GLU N N 117.880 0.018 . 445 210 213 HIS H H 7.393 0.003 . 446 210 213 HIS CA C 54.740 0.009 . 447 210 213 HIS N N 119.002 0.004 . 448 211 214 GLY H H 7.223 0.001 . 449 211 214 GLY CA C 45.181 0.000 . 450 211 214 GLY N N 104.606 0.042 . 451 213 216 VAL H H 8.845 0.004 . 452 213 216 VAL CA C 62.183 0.028 . 453 213 216 VAL N N 126.027 0.009 . 454 214 217 VAL H H 7.571 0.002 . 455 214 217 VAL CA C 62.016 0.000 . 456 214 217 VAL N N 126.419 0.053 . 457 215 218 VAL H H 9.536 0.000 . 458 215 218 VAL N N 129.502 0.000 . 459 217 220 CYS CA C 57.475 0.000 . 460 218 221 SER H H 6.881 0.001 . 461 218 221 SER CA C 58.745 0.010 . 462 218 221 SER N N 107.817 0.064 . 463 219 222 ALA H H 8.227 0.002 . 464 219 222 ALA CA C 55.246 0.000 . 465 219 222 ALA N N 119.957 0.064 . 466 220 223 GLY CA C 47.625 0.000 . 467 221 224 ILE H H 7.633 0.021 . 468 221 224 ILE CA C 59.389 0.064 . 469 221 224 ILE N N 111.470 0.110 . 470 224 227 SER CA C 64.897 0.000 . 471 225 228 GLY H H 6.249 0.004 . 472 225 228 GLY CA C 48.455 0.000 . 473 225 228 GLY N N 104.773 0.084 . 474 226 229 THR CA C 64.680 0.000 . 475 227 230 PHE H H 7.470 0.002 . 476 227 230 PHE CA C 62.882 0.000 . 477 227 230 PHE N N 120.169 0.008 . 478 228 231 CYS CA C 63.749 0.000 . 479 229 232 LEU H H 8.404 0.006 . 480 229 232 LEU CA C 58.845 0.088 . 481 229 232 LEU N N 121.656 0.013 . 482 230 233 ALA H H 8.145 0.098 . 483 230 233 ALA CA C 55.252 0.000 . 484 230 233 ALA N N 119.394 0.125 . 485 231 234 ASP H H 7.439 0.002 . 486 231 234 ASP CA C 59.421 0.000 . 487 231 234 ASP N N 114.552 0.017 . 488 233 236 CYS H H 8.383 0.002 . 489 233 236 CYS CA C 66.618 0.101 . 490 233 236 CYS N N 118.346 0.003 . 491 234 237 LEU H H 7.796 0.005 . 492 234 237 LEU CA C 58.842 0.001 . 493 234 237 LEU N N 117.962 0.083 . 494 235 238 LEU H H 7.822 0.003 . 495 235 238 LEU CA C 58.770 0.056 . 496 235 238 LEU N N 117.858 0.050 . 497 236 239 LEU H H 7.858 0.002 . 498 236 239 LEU CA C 58.691 0.024 . 499 236 239 LEU N N 122.748 0.045 . 500 237 240 MET H H 7.817 0.001 . 501 237 240 MET CA C 59.859 0.004 . 502 237 240 MET N N 117.036 0.092 . 503 238 241 ASP H H 7.172 0.002 . 504 238 241 ASP CA C 56.679 0.075 . 505 238 241 ASP N N 117.009 0.012 . 506 239 242 LYS H H 7.858 0.001 . 507 239 242 LYS CA C 58.678 0.028 . 508 239 242 LYS N N 117.449 0.035 . 509 240 243 ARG H H 7.883 0.001 . 510 240 243 ARG CA C 57.270 0.009 . 511 240 243 ARG N N 116.890 0.027 . 512 241 244 LYS H H 7.941 0.001 . 513 241 244 LYS CA C 57.652 0.000 . 514 241 244 LYS N N 118.551 0.045 . 515 243 246 PRO CA C 65.632 0.000 . 516 244 247 SER H H 8.044 0.000 . 517 244 247 SER CA C 60.897 0.062 . 518 244 247 SER N N 112.830 0.068 . 519 245 248 SER H H 7.607 0.000 . 520 245 248 SER CA C 59.672 0.019 . 521 245 248 SER N N 115.154 0.050 . 522 246 249 VAL H H 7.182 0.001 . 523 246 249 VAL CA C 64.219 0.004 . 524 246 249 VAL N N 123.523 0.016 . 525 247 250 ASP H H 8.331 0.002 . 526 247 250 ASP CA C 52.505 0.033 . 527 247 250 ASP N N 129.657 0.035 . 528 248 251 ILE H H 8.408 0.002 . 529 248 251 ILE CA C 66.473 0.040 . 530 248 251 ILE N N 126.308 0.018 . 531 249 252 LYS H H 7.772 0.002 . 532 249 252 LYS CA C 60.956 0.069 . 533 249 252 LYS N N 117.452 0.045 . 534 250 253 LYS H H 7.112 0.001 . 535 250 253 LYS CA C 59.965 0.006 . 536 250 253 LYS N N 117.593 0.022 . 537 251 254 VAL H H 8.092 0.001 . 538 251 254 VAL CA C 67.135 0.084 . 539 251 254 VAL N N 121.817 0.039 . 540 252 255 LEU H H 8.338 0.004 . 541 252 255 LEU CA C 58.904 0.102 . 542 252 255 LEU N N 120.802 0.027 . 543 253 256 LEU H H 8.080 0.004 . 544 253 256 LEU CA C 58.706 0.000 . 545 253 256 LEU N N 119.860 0.056 . 546 255 258 MET H H 8.702 0.004 . 547 255 258 MET CA C 61.490 0.079 . 548 255 258 MET N N 119.161 0.068 . 549 256 259 ARG H H 8.475 0.002 . 550 256 259 ARG CA C 58.735 0.051 . 551 256 259 ARG N N 117.301 0.060 . 552 257 260 LYS H H 7.592 0.002 . 553 257 260 LYS CA C 59.684 0.018 . 554 257 260 LYS N N 119.266 0.036 . 555 258 261 PHE H H 8.155 0.002 . 556 258 261 PHE CA C 60.216 0.048 . 557 258 261 PHE N N 112.721 0.047 . 558 259 262 ARG H H 7.352 0.000 . 559 259 262 ARG CA C 57.498 0.030 . 560 259 262 ARG N N 120.653 0.054 . 561 260 263 MET H H 8.142 0.000 . 562 260 263 MET CA C 55.874 0.009 . 563 260 263 MET N N 121.616 0.055 . 564 261 264 GLY H H 8.703 0.003 . 565 261 264 GLY CA C 47.523 0.007 . 566 261 264 GLY N N 100.751 0.013 . 567 262 265 LEU H H 6.306 0.001 . 568 262 265 LEU CA C 56.264 0.005 . 569 262 265 LEU N N 115.084 0.023 . 570 263 266 ILE H H 8.253 0.003 . 571 263 266 ILE CA C 68.335 0.003 . 572 263 266 ILE N N 116.171 0.034 . 573 264 267 GLN H H 8.707 0.003 . 574 264 267 GLN CA C 57.580 0.000 . 575 264 267 GLN N N 126.739 0.016 . 576 265 268 THR CA C 58.749 0.000 . 577 266 269 ALA H H 8.549 0.000 . 578 266 269 ALA CA C 55.049 0.009 . 579 266 269 ALA N N 123.721 0.037 . 580 267 270 ASP H H 7.697 0.001 . 581 267 270 ASP CA C 57.312 0.000 . 582 267 270 ASP N N 116.768 0.041 . 583 268 271 GLN H H 7.719 0.000 . 584 268 271 GLN CA C 59.949 0.000 . 585 268 271 GLN N N 120.075 0.030 . 586 269 272 LEU H H 7.536 0.004 . 587 269 272 LEU CA C 59.127 0.019 . 588 269 272 LEU N N 123.429 0.083 . 589 270 273 ARG H H 7.851 0.002 . 590 270 273 ARG CA C 60.187 0.038 . 591 270 273 ARG N N 121.082 0.012 . 592 271 274 PHE H H 8.242 0.003 . 593 271 274 PHE CA C 62.630 0.041 . 594 271 274 PHE N N 117.935 0.025 . 595 272 275 SER H H 8.024 0.002 . 596 272 275 SER CA C 64.717 0.000 . 597 272 275 SER N N 116.351 0.118 . 598 273 276 TYR H H 7.822 0.000 . 599 273 276 TYR CA C 58.569 0.000 . 600 273 276 TYR N N 120.989 0.000 . 601 274 277 LEU H H 8.374 0.003 . 602 274 277 LEU CA C 58.550 0.019 . 603 274 277 LEU N N 119.460 0.034 . 604 275 278 ALA H H 8.478 0.004 . 605 275 278 ALA CA C 55.562 0.000 . 606 275 278 ALA N N 119.551 0.091 . 607 276 279 VAL CA C 67.135 0.000 . 608 277 280 ILE H H 8.328 0.003 . 609 277 280 ILE CA C 66.848 0.000 . 610 277 280 ILE N N 120.649 0.032 . 611 278 281 GLU CA C 59.419 0.000 . 612 279 282 GLY H H 8.676 0.003 . 613 279 282 GLY CA C 48.421 0.036 . 614 279 282 GLY N N 108.693 0.067 . 615 280 283 ALA H H 8.491 0.000 . 616 280 283 ALA CA C 55.470 0.007 . 617 280 283 ALA N N 124.631 0.051 . 618 281 284 LYS H H 7.549 0.004 . 619 281 284 LYS CA C 60.236 0.011 . 620 281 284 LYS N N 116.119 0.047 . 621 282 285 PHE H H 7.445 0.003 . 622 282 285 PHE CA C 60.400 0.000 . 623 282 285 PHE N N 117.804 0.025 . 624 283 286 ILE CA C 63.647 0.000 . 625 284 287 MET H H 7.951 0.008 . 626 284 287 MET CA C 56.672 0.014 . 627 284 287 MET N N 118.062 0.025 . 628 285 288 GLY H H 7.285 0.002 . 629 285 288 GLY CA C 46.362 0.001 . 630 285 288 GLY N N 106.727 0.001 . 631 286 289 ASP H H 7.777 0.009 . 632 286 289 ASP CA C 53.806 0.001 . 633 286 289 ASP N N 120.951 0.042 . 634 287 290 SER H H 8.119 0.002 . 635 287 290 SER CA C 60.756 0.028 . 636 287 290 SER N N 118.962 0.063 . 637 288 291 SER H H 8.342 0.000 . 638 288 291 SER CA C 60.811 0.000 . 639 288 291 SER N N 118.602 0.072 . 640 289 292 VAL CA C 63.855 0.000 . 641 290 293 GLN H H 8.319 0.001 . 642 290 293 GLN CA C 56.003 0.000 . 643 290 293 GLN N N 119.537 0.025 . 644 293 296 TRP CA C 58.430 0.000 . 645 294 297 LYS H H 8.413 0.001 . 646 294 297 LYS CA C 57.713 0.046 . 647 294 297 LYS N N 116.883 0.032 . 648 295 298 GLU H H 8.005 0.007 . 649 295 298 GLU CA C 57.761 0.009 . 650 295 298 GLU N N 121.094 0.049 . 651 296 299 LEU H H 7.924 0.010 . 652 296 299 LEU CA C 55.958 0.000 . 653 296 299 LEU N N 122.409 0.082 . 654 297 300 SER CA C 59.398 0.000 . 655 298 301 HIS H H 8.400 0.002 . 656 298 301 HIS CA C 57.285 0.000 . 657 298 301 HIS N N 122.456 0.137 . 658 300 303 ASP CA C 55.297 0.000 . 659 301 304 LEU H H 8.001 0.003 . 660 301 304 LEU CA C 55.810 0.000 . 661 301 304 LEU N N 122.527 0.045 . 662 302 305 GLU H H 7.900 0.002 . 663 302 305 GLU CA C 54.230 0.000 . 664 302 305 GLU N N 120.741 0.011 . 665 303 306 PRO CA C 58.759 0.000 . 666 304 307 HIS H H 7.917 0.003 . 667 304 307 HIS CA C 57.505 0.000 . 668 304 307 HIS N N 118.088 0.035 . stop_ save_