data_18689 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N backbone resonance assignments of the TPR2A domain of mouse STI1 ; _BMRB_accession_number 18689 _BMRB_flat_file_name bmr18689.str _Entry_type original _Submission_date 2012-08-30 _Accession_date 2012-08-30 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Maciejewski Andrzej . . 2 Choy Wing-Yiu . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 132 "13C chemical shifts" 252 "15N chemical shifts" 132 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-19 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 17691 'tpr1 domain' stop_ _Original_release_date 2014-02-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title '(1)H, (15)N and (13)C backbone resonance assignments of the TPR1 and TPR2A domains of mouse STI1.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23070844 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Maciejewski Andrzej . . 2 Prado Marco A. . 3 Choy Wing-Yiu . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 7 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 305 _Page_last 310 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name tpr2a _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label tpr2a $tpr2a 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_tpr2a _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common tpr2a _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function co-chaperone stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 137 _Mol_residue_sequence . loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 216 GLY 2 217 ASP 3 218 LEU 4 219 PRO 5 220 GLU 6 221 ASN 7 222 LYS 8 223 LYS 9 224 GLN 10 225 ALA 11 226 LEU 12 227 LYS 13 228 GLU 14 229 LYS 15 230 GLU 16 231 LEU 17 232 GLY 18 233 ASN 19 234 ASP 20 235 ALA 21 236 TYR 22 237 LYS 23 238 LYS 24 239 LYS 25 240 ASP 26 241 PHE 27 242 ASP 28 243 LYS 29 244 ALA 30 245 LEU 31 246 LYS 32 247 HIS 33 248 TYR 34 249 ASP 35 250 ARG 36 251 ALA 37 252 LYS 38 253 GLU 39 254 LEU 40 255 ASP 41 256 PRO 42 257 THR 43 258 ASN 44 259 MET 45 260 THR 46 261 TYR 47 262 ILE 48 263 THR 49 264 ASN 50 265 GLN 51 266 ALA 52 267 ALA 53 268 VAL 54 269 HIS 55 270 PHE 56 271 GLU 57 272 LYS 58 273 GLY 59 274 ASP 60 275 TYR 61 276 ASN 62 277 LYS 63 278 CYS 64 279 ARG 65 280 GLU 66 281 LEU 67 282 CYS 68 283 GLU 69 284 LYS 70 285 ALA 71 286 ILE 72 287 GLU 73 288 VAL 74 289 GLY 75 290 ARG 76 291 GLU 77 292 ASN 78 293 ARG 79 294 GLU 80 295 ASP 81 296 TYR 82 297 ARG 83 298 GLN 84 299 ILE 85 300 ALA 86 301 LYS 87 302 ALA 88 303 TYR 89 304 ALA 90 305 ARG 91 306 ILE 92 307 GLY 93 308 ASN 94 309 SER 95 310 TYR 96 311 PHE 97 312 LYS 98 313 GLU 99 314 GLU 100 315 LYS 101 316 TYR 102 317 LYS 103 318 ASP 104 319 ALA 105 320 ILE 106 321 HIS 107 322 PHE 108 323 TYR 109 324 ASN 110 325 LYS 111 326 SER 112 327 LEU 113 328 ALA 114 329 GLU 115 330 HIS 116 331 ARG 117 332 THR 118 333 PRO 119 334 ASP 120 335 VAL 121 336 LEU 122 337 LYS 123 338 LYS 124 339 CYS 125 340 GLN 126 341 GLN 127 342 ALA 128 343 GLU 129 344 LYS 130 345 ILE 131 346 LEU 132 347 LYS 133 348 GLU 134 349 GLN 135 350 GLU 136 351 ARG 137 352 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-04-15 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1ELR "Crystal Structure Of The Tpr2a Domain Of Hop In Complex With The Hsp90 Peptide Meevd" 94.89 131 97.69 99.23 2.29e-85 PDB 3ESK "Structure Of Hop Tpr2a Domain In Complex With The Non-cognate Hsc70 Peptide Ligand" 93.43 129 97.66 99.22 7.14e-84 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $tpr2a 'House mouse' 10090 Eukaryota Metazoa Mus musculus 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 $tpr2a 'recombinant technology' . Escherichia coli . pDEST17 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 'sodium phosphate' 50 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' DTT 1 mM 'natural abundance' DSS 100 uM 'natural abundance' $tpr2a 0.5 uM '[U-13C; U-15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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 7 . pH pressure 1 . atm temperature 273 . 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 HSQC' '3D HNCACB' '3D CBCA(CO)NH' 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 tpr2a _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 1 218 3 LEU H H 8.459 0.02 1 2 218 3 LEU N N 123.705 0.3 1 3 219 4 PRO CA C 62.949 0.3 1 4 219 4 PRO CB C 32.172 0.3 1 5 220 5 GLU H H 8.814 0.02 1 6 220 5 GLU CA C 59.21 0.3 1 7 220 5 GLU CB C 29.517 0.3 1 8 220 5 GLU N N 121.955 0.3 1 9 221 6 ASN H H 8.821 0.02 1 10 221 6 ASN CA C 56.663 0.3 1 11 221 6 ASN CB C 36.723 0.3 1 12 221 6 ASN N N 117.143 0.3 1 13 222 7 LYS H H 7.434 0.02 1 14 222 7 LYS CA C 59.978 0.3 1 15 222 7 LYS CB C 32.714 0.3 1 16 222 7 LYS N N 119.002 0.3 1 17 223 8 LYS H H 7.94 0.02 1 18 223 8 LYS CA C 59.969 0.3 1 19 223 8 LYS CB C 32.497 0.3 1 20 223 8 LYS N N 120.096 0.3 1 21 224 9 GLN H H 8.439 0.02 1 22 224 9 GLN CA C 58.289 0.3 1 23 224 9 GLN CB C 28.325 0.3 1 24 224 9 GLN N N 119.112 0.3 1 25 225 10 ALA H H 8.322 0.02 1 26 225 10 ALA CA C 55.796 0.3 1 27 225 10 ALA CB C 18.897 0.3 1 28 225 10 ALA N N 123.487 0.3 1 29 226 11 LEU H H 7.735 0.02 1 30 226 11 LEU CA C 58.018 0.3 1 31 226 11 LEU CB C 42.088 0.3 1 32 226 11 LEU N N 117.362 0.3 1 33 227 12 LYS H H 7.352 0.02 1 34 227 12 LYS CA C 58.993 0.3 1 35 227 12 LYS CB C 31.738 0.3 1 36 227 12 LYS N N 119.768 0.3 1 37 228 13 GLU H H 7.946 0.02 1 38 228 13 GLU CA C 59.21 0.3 1 39 228 13 GLU N N 119.233 0.3 1 40 229 14 LYS H H 8.657 0.02 1 41 229 14 LYS CA C 60.294 0.3 1 42 229 14 LYS CB C 30.98 0.3 1 43 229 14 LYS N N 120.643 0.3 1 44 230 15 GLU H H 7.919 0.02 1 45 230 15 GLU CA C 59.535 0.3 1 46 230 15 GLU CB C 29.137 0.3 1 47 230 15 GLU N N 119.187 0.3 1 48 231 16 LEU H H 8.014 0.02 1 49 231 16 LEU N N 117.363 0.3 1 50 232 17 GLY H H 8.712 0.02 1 51 232 17 GLY CA C 47.994 0.3 1 52 232 17 GLY N N 109.487 0.3 1 53 233 18 ASN H H 9.04 0.02 1 54 233 18 ASN CA C 55.417 0.3 1 55 233 18 ASN CB C 37.428 0.3 1 56 233 18 ASN N N 121.846 0.3 1 57 234 19 ASP H H 8.152 0.02 1 58 234 19 ASP CA C 57.693 0.3 1 59 234 19 ASP CB C 41.221 0.3 1 60 234 19 ASP N N 121.737 0.3 1 61 235 20 ALA H H 7.53 0.02 1 62 235 20 ALA CA C 55.038 0.3 1 63 235 20 ALA CB C 17.217 0.3 1 64 235 20 ALA N N 120.971 0.3 1 65 236 21 TYR H H 9.135 0.02 1 66 236 21 TYR CA C 61.486 0.3 1 67 236 21 TYR CB C 39.27 0.3 1 68 236 21 TYR N N 121.08 0.3 1 69 237 22 LYS H H 8.357 0.02 1 70 237 22 LYS CA C 59.318 0.3 1 71 237 22 LYS CB C 32.28 0.3 1 72 237 22 LYS N N 121.19 0.3 1 73 238 23 LYS H H 7.209 0.02 1 74 238 23 LYS CA C 56.176 0.3 1 75 238 23 LYS CB C 32.497 0.3 1 76 238 23 LYS N N 117.252 0.3 1 77 239 24 LYS H H 7.687 0.02 1 78 239 24 LYS CA C 56.609 0.3 1 79 239 24 LYS CB C 28.216 0.3 1 80 239 24 LYS N N 113.533 0.3 1 81 240 25 ASP H H 8.056 0.02 1 82 240 25 ASP CB C 38.837 0.3 1 83 240 25 ASP N N 119.987 0.3 1 84 241 26 PHE H H 7.277 0.02 1 85 241 26 PHE CA C 60.077 0.3 1 86 241 26 PHE CB C 38.024 0.3 1 87 241 26 PHE N N 119.987 0.3 1 88 242 27 ASP H H 8.691 0.02 1 89 242 27 ASP CA C 57.639 0.3 1 90 242 27 ASP CB C 39.974 0.3 1 91 242 27 ASP N N 119.112 0.3 1 92 243 28 LYS H H 7.318 0.02 1 93 243 28 LYS CA C 59.102 0.3 1 94 243 28 LYS CB C 33.31 0.3 1 95 243 28 LYS N N 121.518 0.3 1 96 244 29 ALA H H 8.152 0.02 1 97 244 29 ALA CA C 55.796 0.3 1 98 244 29 ALA CB C 18.03 0.3 1 99 244 29 ALA N N 120.205 0.3 1 100 245 30 LEU H H 8.145 0.02 1 101 245 30 LEU CA C 58.397 0.3 1 102 245 30 LEU CB C 41.925 0.3 1 103 245 30 LEU N N 114.737 0.3 1 104 246 31 LYS H H 7.304 0.02 1 105 246 31 LYS CA C 59.373 0.3 1 106 246 31 LYS CB C 31.847 0.3 1 107 246 31 LYS N N 118.127 0.3 1 108 247 32 HIS H H 7.537 0.02 1 109 247 32 HIS CA C 59.643 0.3 1 110 247 32 HIS CB C 28 0.3 1 111 247 32 HIS N N 118.237 0.3 1 112 248 33 TYR H H 8.719 0.02 1 113 248 33 TYR CA C 58.614 0.3 1 114 248 33 TYR CB C 37.536 0.3 1 115 248 33 TYR N N 118.455 0.3 1 116 249 34 ASP H H 8.944 0.02 1 117 249 34 ASP CA C 57.476 0.3 1 118 249 34 ASP CB C 40.787 0.3 1 119 249 34 ASP N N 119.877 0.3 1 120 250 35 ARG H H 7.564 0.02 1 121 250 35 ARG CA C 58.126 0.3 1 122 250 35 ARG CB C 29.246 0.3 1 123 250 35 ARG N N 120.205 0.3 1 124 251 36 ALA H H 8.295 0.02 1 125 251 36 ALA CA C 55.905 0.3 1 126 251 36 ALA CB C 16.35 0.3 1 127 251 36 ALA N N 121.846 0.3 1 128 252 37 LYS H H 7.845 0.02 1 129 252 37 LYS CA C 58.56 0.3 1 130 252 37 LYS CB C 32.063 0.3 1 131 252 37 LYS N N 116.378 0.3 1 132 253 38 GLU H H 7.673 0.02 1 133 253 38 GLU CA C 58.56 0.3 1 134 253 38 GLU CB C 29.896 0.3 1 135 253 38 GLU N N 116.924 0.3 1 136 254 39 LEU H H 7.881 0.02 1 137 254 39 LEU CB C 43.659 0.3 1 138 254 39 LEU N N 119.004 0.3 1 139 255 40 ASP H H 8.179 0.02 1 140 255 40 ASP CA C 51.191 0.3 1 141 255 40 ASP CB C 41.492 0.3 1 142 255 40 ASP N N 115.83 0.3 1 143 256 41 PRO CA C 64.141 0.3 1 144 256 41 PRO CB C 32.714 0.3 1 145 257 42 THR H H 7.796 0.02 1 146 257 42 THR CA C 61.486 0.3 1 147 257 42 THR CB C 69.017 0.3 1 148 257 42 THR N N 108.283 0.3 1 149 258 43 ASN H H 6.908 0.02 1 150 258 43 ASN CA C 51.516 0.3 1 151 258 43 ASN CB C 39.487 0.3 1 152 258 43 ASN N N 118.893 0.3 1 153 259 44 MET H H 9.887 0.02 1 154 259 44 MET CA C 58.777 0.3 1 155 259 44 MET CB C 32.93 0.3 1 156 259 44 MET N N 126.112 0.3 1 157 260 45 THR H H 8.076 0.02 1 158 260 45 THR CA C 64.683 0.3 1 159 260 45 THR CB C 68.096 0.3 1 160 260 45 THR N N 115.174 0.3 1 161 261 46 TYR H H 6.505 0.02 1 162 261 46 TYR CA C 58.18 0.3 1 163 261 46 TYR CB C 35.748 0.3 1 164 261 46 TYR N N 119.987 0.3 1 165 262 47 ILE H H 7.206 0.02 1 166 262 47 ILE CA C 63.924 0.3 1 167 262 47 ILE CB C 38.511 0.3 1 168 262 47 ILE N N 117.476 0.3 1 169 263 48 THR H H 8.213 0.02 1 170 263 48 THR CA C 65.929 0.3 1 171 263 48 THR CB C 67.338 0.3 1 172 263 48 THR N N 113.643 0.3 1 173 264 49 ASN H H 8.24 0.02 1 174 264 49 ASN CA C 56.135 0.3 1 175 264 49 ASN CB C 35.694 0.3 1 176 264 49 ASN N N 121.737 0.3 1 177 265 50 GLN H H 7.168 0.02 1 178 265 50 GLN CA C 59.86 0.3 1 179 265 50 GLN CB C 29.625 0.3 1 180 265 50 GLN N N 117.58 0.3 1 181 266 51 ALA H H 8.319 0.02 1 182 266 51 ALA CA C 55.959 0.3 1 183 266 51 ALA CB C 19.655 0.3 1 184 266 51 ALA N N 121.192 0.3 1 185 267 52 ALA H H 8.07 0.02 1 186 267 52 ALA CA C 55.688 0.3 1 187 267 52 ALA CB C 17.924 0.3 1 188 267 52 ALA N N 120.315 0.3 1 189 268 53 VAL H H 7.386 0.02 1 190 268 53 VAL CA C 67.067 0.3 1 191 268 53 VAL CB C 30.871 0.3 1 192 268 53 VAL N N 117.799 0.3 1 193 269 54 HIS H H 7.503 0.02 1 194 269 54 HIS CA C 60.944 0.3 1 195 269 54 HIS CB C 30.004 0.3 1 196 269 54 HIS N N 116.815 0.3 1 197 270 55 PHE H H 8.575 0.02 1 198 270 55 PHE CA C 61.865 0.3 1 199 270 55 PHE CB C 38.728 0.3 1 200 270 55 PHE N N 119.59 0.3 1 201 271 56 GLU H H 8.128 0.02 1 202 271 56 GLU CA C 58.993 0.3 1 203 271 56 GLU CB C 29.137 0.3 1 204 271 56 GLU N N 121.343 0.3 1 205 272 57 LYS H H 7.639 0.02 1 206 272 57 LYS CA C 56.988 0.3 1 207 272 57 LYS CB C 32.551 0.3 1 208 272 57 LYS N N 115.612 0.3 1 209 273 58 GLY H H 7.489 0.02 1 210 273 58 GLY CA C 44.309 0.3 1 211 273 58 GLY N N 107.299 0.3 1 212 274 59 ASP H H 7.906 0.02 1 213 274 59 ASP CA C 51.028 0.3 1 214 274 59 ASP CB C 39.162 0.3 1 215 274 59 ASP N N 121.08 0.3 1 216 275 60 TYR H H 7.072 0.02 1 217 275 60 TYR CA C 61.052 0.3 1 218 275 60 TYR CB C 36.886 0.3 1 219 275 60 TYR N N 122.065 0.3 1 220 276 61 ASN H H 8.81 0.02 1 221 276 61 ASN CA C 56.896 0.3 1 222 276 61 ASN CB C 37.929 0.3 1 223 276 61 ASN N N 118.584 0.3 1 224 277 62 LYS H H 7.667 0.02 1 225 277 62 LYS CA C 57.747 0.3 1 226 277 62 LYS CB C 31.684 0.3 1 227 277 62 LYS N N 121.518 0.3 1 228 278 63 CYS H H 7.913 0.02 1 229 278 63 CYS CA C 62.353 0.3 1 230 278 63 CYS CB C 26.211 0.3 1 231 278 63 CYS N N 116.049 0.3 1 232 279 64 ARG H H 8.275 0.02 1 233 279 64 ARG CA C 62.407 0.3 1 234 279 64 ARG CB C 31.142 0.3 1 235 279 64 ARG N N 119.112 0.3 1 236 280 65 GLU H H 8.003 0.02 1 237 280 65 GLU CA C 59.156 0.3 1 238 280 65 GLU CB C 29.842 0.3 1 239 280 65 GLU N N 119.533 0.3 1 240 281 66 LEU H H 8.07 0.02 1 241 281 66 LEU CA C 57.368 0.3 1 242 281 66 LEU CB C 41.871 0.3 1 243 281 66 LEU N N 119.33 0.3 1 244 282 67 CYS H H 8.539 0.02 1 245 282 67 CYS CA C 65.55 0.3 1 246 282 67 CYS CB C 28.596 0.3 1 247 282 67 CYS N N 118.222 0.3 1 248 283 68 GLU H H 8.288 0.02 1 249 283 68 GLU CA C 60.239 0.3 1 250 283 68 GLU CB C 29.083 0.3 1 251 283 68 GLU N N 118.346 0.3 1 252 284 69 LYS H H 7.681 0.02 1 253 284 69 LYS CA C 58.072 0.3 1 254 284 69 LYS N N 120.97 0.3 1 255 285 70 ALA H H 8.821 0.02 1 256 285 70 ALA CA C 54.984 0.3 1 257 285 70 ALA CB C 18.626 0.3 1 258 285 70 ALA N N 121.299 0.3 1 259 286 71 ILE H H 8.056 0.02 1 260 286 71 ILE CA C 66.146 0.3 1 261 286 71 ILE CB C 38.511 0.3 1 262 286 71 ILE N N 118.455 0.3 1 263 287 72 GLU H H 7.499 0.02 1 264 287 72 GLU CA C 59.914 0.3 1 265 287 72 GLU CB C 29.625 0.3 1 266 287 72 GLU N N 119.659 0.3 1 267 288 73 VAL H H 8.203 0.02 1 268 288 73 VAL CA C 66.35 0.3 1 269 288 73 VAL CB C 32.389 0.3 1 270 288 73 VAL N N 120.53 0.3 1 271 289 74 GLY H H 9.265 0.02 1 272 289 74 GLY CA C 48.048 0.3 1 273 289 74 GLY N N 110.143 0.3 1 274 290 75 ARG H H 8.944 0.02 1 275 290 75 ARG CA C 59.271 0.3 1 276 290 75 ARG CB C 29.625 0.3 1 277 290 75 ARG N N 121.408 0.3 1 278 291 76 GLU H H 8.001 0.02 1 279 291 76 GLU CA C 59.102 0.3 1 280 291 76 GLU CB C 29.733 0.3 1 281 291 76 GLU N N 119.987 0.3 1 282 292 77 ASN H H 7.728 0.02 1 283 292 77 ASN CA C 53.683 0.3 1 284 292 77 ASN CB C 39.703 0.3 1 285 292 77 ASN N N 114.08 0.3 1 286 293 78 ARG H H 7.844 0.02 1 287 293 78 ARG CA C 57.097 0.3 1 288 293 78 ARG CB C 26.645 0.3 1 289 293 78 ARG N N 116.924 0.3 1 290 294 79 GLU H H 8.534 0.02 1 291 294 79 GLU CA C 56.013 0.3 1 292 294 79 GLU CB C 30.871 0.3 1 293 294 79 GLU N N 118.783 0.3 1 294 295 80 ASP H H 8.719 0.02 1 295 295 80 ASP CA C 55.146 0.3 1 296 295 80 ASP CB C 42.792 0.3 1 297 295 80 ASP N N 122.83 0.3 1 298 296 81 TYR H H 8.065 0.02 1 299 296 81 TYR CA C 59.914 0.3 1 300 296 81 TYR CB C 37.344 0.3 1 301 296 81 TYR N N 126.553 0.3 1 302 297 82 ARG H H 8.117 0.02 1 303 297 82 ARG CA C 59.156 0.3 1 304 297 82 ARG CB C 29.517 0.3 1 305 297 82 ARG N N 121.19 0.3 1 306 298 83 GLN H H 7.788 0.02 1 307 298 83 GLN CA C 57.603 0.3 1 308 298 83 GLN CB C 28.868 0.3 1 309 298 83 GLN N N 117.037 0.3 1 310 299 84 ILE H H 7.223 0.02 1 311 299 84 ILE CA C 64.628 0.3 1 312 299 84 ILE CB C 36.778 0.3 1 313 299 84 ILE N N 121.846 0.3 1 314 300 85 ALA H H 8.575 0.02 1 315 300 85 ALA CA C 56.284 0.3 1 316 300 85 ALA CB C 20.414 0.3 1 317 300 85 ALA N N 120.424 0.3 1 318 301 86 LYS H H 7.578 0.02 1 319 301 86 LYS CA C 59.535 0.3 1 320 301 86 LYS CB C 32.876 0.3 1 321 301 86 LYS N N 120.315 0.3 1 322 302 87 ALA H H 7.571 0.02 1 323 302 87 ALA CA C 55.417 0.3 1 324 302 87 ALA CB C 17.867 0.3 1 325 302 87 ALA N N 124.362 0.3 1 326 303 88 TYR H H 7.892 0.02 1 327 303 88 TYR CA C 61.594 0.3 1 328 303 88 TYR CB C 38.566 0.3 1 329 303 88 TYR N N 115.721 0.3 1 330 304 89 ALA H H 8.21 0.02 1 331 304 89 ALA CA C 56.013 0.3 1 332 304 89 ALA CB C 18.138 0.3 1 333 304 89 ALA N N 120.941 0.3 1 334 305 90 ARG H H 7.981 0.02 1 335 305 90 ARG CA C 59.264 0.3 1 336 305 90 ARG CB C 27.945 0.3 1 337 305 90 ARG N N 119.002 0.3 1 338 306 91 ILE H H 7.828 0.02 1 339 306 91 ILE CA C 66.471 0.3 1 340 306 91 ILE CB C 37.807 0.3 1 341 306 91 ILE N N 120.736 0.3 1 342 307 92 GLY H H 8.65 0.02 1 343 307 92 GLY CA C 48.861 0.3 1 344 307 92 GLY N N 108.83 0.3 1 345 308 93 ASN H H 9.409 0.02 1 346 308 93 ASN CA C 55.417 0.3 1 347 308 93 ASN CB C 37.861 0.3 1 348 308 93 ASN N N 120.205 0.3 1 349 309 94 SER H H 8.5 0.02 1 350 309 94 SER N N 119.44 0.3 1 351 310 95 TYR H H 7.347 0.02 1 352 310 95 TYR CA C 61.973 0.3 1 353 310 95 TYR N N 121.082 0.3 1 354 311 96 PHE H H 9.033 0.02 1 355 311 96 PHE CA C 62.028 0.3 1 356 311 96 PHE CB C 40.191 0.3 1 357 311 96 PHE N N 123.705 0.3 1 358 312 97 LYS H H 8.186 0.02 1 359 312 97 LYS CA C 57.53 0.3 1 360 312 97 LYS CB C 31.684 0.3 1 361 312 97 LYS N N 119.002 0.3 1 362 313 98 GLU H H 6.806 0.02 1 363 313 98 GLU CA C 56.338 0.3 1 364 313 98 GLU CB C 31.305 0.3 1 365 313 98 GLU N N 115.612 0.3 1 366 314 99 GLU H H 7.646 0.02 1 367 314 99 GLU CA C 56.934 0.3 1 368 314 99 GLU CB C 26.049 0.3 1 369 314 99 GLU N N 112.658 0.3 1 370 315 100 LYS H H 7.762 0.02 1 371 315 100 LYS CA C 53.792 0.3 1 372 315 100 LYS CB C 30.839 0.3 1 373 315 100 LYS N N 121.518 0.3 1 374 316 101 TYR H H 6.799 0.02 1 375 316 101 TYR CA C 62.624 0.3 1 376 316 101 TYR CB C 38.403 0.3 1 377 316 101 TYR N N 117.799 0.3 1 378 317 102 LYS H H 8.787 0.02 1 379 317 102 LYS CA C 60.348 0.3 1 380 317 102 LYS CB C 31.793 0.3 1 381 317 102 LYS N N 119.658 0.3 1 382 318 103 ASP H H 7.53 0.02 1 383 318 103 ASP CA C 57.151 0.3 1 384 318 103 ASP CB C 39.487 0.3 1 385 318 103 ASP N N 119.658 0.3 1 386 319 104 ALA H H 8.05 0.02 1 387 319 104 ALA CB C 17.921 0.3 1 388 319 104 ALA N N 120.522 0.3 1 389 320 105 ILE H H 8.35 0.02 1 390 320 105 ILE CA C 65.766 0.3 1 391 320 105 ILE CB C 39.541 0.3 1 392 320 105 ILE N N 117.033 0.3 1 393 321 106 HIS H H 7.656 0.02 1 394 321 106 HIS CA C 59.969 0.3 1 395 321 106 HIS CB C 29.759 0.3 1 396 321 106 HIS N N 118.795 0.3 1 397 322 107 PHE H H 7.742 0.02 1 398 322 107 PHE CA C 63.816 0.3 1 399 322 107 PHE CB C 38.782 0.3 1 400 322 107 PHE N N 116.049 0.3 1 401 323 108 TYR H H 9.614 0.02 1 402 323 108 TYR CA C 58.668 0.3 1 403 323 108 TYR CB C 36.181 0.3 1 404 323 108 TYR N N 122.393 0.3 1 405 324 109 ASN H H 8.937 0.02 1 406 324 109 ASN CA C 56.663 0.3 1 407 324 109 ASN CB C 37.482 0.3 1 408 324 109 ASN N N 118.674 0.3 1 409 325 110 LYS H H 7.332 0.02 1 410 325 110 LYS CA C 59.21 0.3 1 411 325 110 LYS CB C 30.46 0.3 1 412 325 110 LYS N N 121.299 0.3 1 413 326 111 SER H H 8.035 0.02 1 414 326 111 SER CA C 62.407 0.3 1 415 326 111 SER N N 112.112 0.3 1 416 327 112 LEU H H 8.76 0.02 1 417 327 112 LEU CA C 56.934 0.3 1 418 327 112 LEU CB C 42.359 0.3 1 419 327 112 LEU N N 117.799 0.3 1 420 328 113 ALA H H 7.673 0.02 1 421 328 113 ALA CA C 54.008 0.3 1 422 328 113 ALA CB C 18.138 0.3 1 423 328 113 ALA N N 119.002 0.3 1 424 329 114 GLU H H 7.304 0.02 1 425 329 114 GLU CA C 57.584 0.3 1 426 329 114 GLU CB C 30.275 0.3 1 427 329 114 GLU N N 116.815 0.3 1 428 330 115 HIS H H 8.418 0.02 1 429 330 115 HIS CA C 55.688 0.3 1 430 330 115 HIS CB C 33.635 0.3 1 431 330 115 HIS N N 117.033 0.3 1 432 331 116 ARG H H 8.889 0.02 1 433 331 116 ARG CA C 57.855 0.3 1 434 331 116 ARG CB C 29.625 0.3 1 435 331 116 ARG N N 130.815 0.3 1 436 332 117 THR H H 6.573 0.02 1 437 332 117 THR CA C 57.584 0.3 1 438 332 117 THR CB C 70.48 0.3 1 439 332 117 THR N N 113.752 0.3 1 440 333 118 PRO CA C 64.628 0.3 1 441 333 118 PRO CB C 31.63 0.3 1 442 334 119 ASP H H 8.705 0.02 1 443 334 119 ASP CA C 56.772 0.3 1 444 334 119 ASP CB C 40.029 0.3 1 445 334 119 ASP N N 115.94 0.3 1 446 335 120 VAL H H 7.045 0.02 1 447 335 120 VAL CA C 66.037 0.3 1 448 335 120 VAL CB C 31.088 0.3 1 449 335 120 VAL N N 119.768 0.3 1 450 336 121 LEU H H 7.529 0.02 1 451 336 121 LEU CA C 58.56 0.3 1 452 336 121 LEU CB C 41.763 0.3 1 453 336 121 LEU N N 121.541 0.3 1 454 337 122 LYS H H 7.776 0.02 1 455 337 122 LYS CA C 59.156 0.3 1 456 337 122 LYS CB C 32.226 0.3 1 457 337 122 LYS N N 117.362 0.3 1 458 338 123 LYS H H 7.366 0.02 1 459 338 123 LYS CA C 58.289 0.3 1 460 338 123 LYS CB C 31.738 0.3 1 461 338 123 LYS N N 120.096 0.3 1 462 339 124 CYS H H 8.288 0.02 1 463 339 124 CYS CA C 63.165 0.3 1 464 339 124 CYS CB C 26.374 0.3 1 465 339 124 CYS N N 119.768 0.3 1 466 340 125 GLN H H 8.302 0.02 1 467 340 125 GLN CA C 58.885 0.3 1 468 340 125 GLN CB C 28.054 0.3 1 469 340 125 GLN N N 117.471 0.3 1 470 341 126 GLN H H 8.234 0.02 1 471 341 126 GLN CA C 59.047 0.3 1 472 341 126 GLN CB C 28.216 0.3 1 473 341 126 GLN N N 120.862 0.3 1 474 342 127 ALA H H 8.541 0.02 1 475 342 127 ALA CA C 55.525 0.3 1 476 342 127 ALA CB C 18.734 0.3 1 477 342 127 ALA N N 121.627 0.3 1 478 343 128 GLU H H 8.575 0.02 1 479 343 128 GLU CA C 59.698 0.3 1 480 343 128 GLU CB C 30.113 0.3 1 481 343 128 GLU N N 116.924 0.3 1 482 344 129 LYS H H 7.905 0.02 1 483 344 129 LYS CB C 32.605 0.3 1 484 344 129 LYS N N 120.428 0.3 1 485 345 130 ILE H H 7.824 0.02 1 486 345 130 ILE CA C 64.899 0.3 1 487 345 130 ILE CB C 38.078 0.3 1 488 345 130 ILE N N 120.205 0.3 1 489 346 131 LEU H H 7.878 0.02 1 490 346 131 LEU CA C 57.855 0.3 1 491 346 131 LEU CB C 42.088 0.3 1 492 346 131 LEU N N 119.768 0.3 1 493 347 132 LYS H H 7.899 0.02 1 494 347 132 LYS CA C 58.614 0.3 1 495 347 132 LYS CB C 32.226 0.3 1 496 347 132 LYS N N 118.018 0.3 1 497 348 133 GLU H H 7.869 0.02 1 498 348 133 GLU CA C 58.397 0.3 1 499 348 133 GLU CB C 29.571 0.3 1 500 348 133 GLU N N 118.459 0.3 1 501 349 134 GLN H H 8.008 0.02 1 502 349 134 GLN CA C 57.476 0.3 1 503 349 134 GLN CB C 29.029 0.3 1 504 349 134 GLN N N 117.908 0.3 1 505 350 135 GLU H H 7.885 0.02 1 506 350 135 GLU CA C 57.205 0.3 1 507 350 135 GLU CB C 29.95 0.3 1 508 350 135 GLU N N 118.893 0.3 1 509 351 136 ARG H H 7.858 0.02 1 510 351 136 ARG CA C 56.121 0.3 1 511 351 136 ARG CB C 30.438 0.3 1 512 351 136 ARG N N 120.424 0.3 1 513 352 137 LEU H H 7.762 0.02 1 514 352 137 LEU CA C 56.609 0.3 1 515 352 137 LEU CB C 43.334 0.3 1 516 352 137 LEU N N 128.627 0.3 1 stop_ save_