data_27827 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Human IMP3 KH1-2 delta 1 amide chemical shifts ; _BMRB_accession_number 27827 _BMRB_flat_file_name bmr27827.str _Entry_type original _Submission_date 2019-03-06 _Accession_date 2019-03-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Human IMP3 KH1-2 delta1, residues K192-I355 carrying K213D, E214D as double mutation' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schlundt Andreas . . 2 Sattler Michael . . 3 Aziz Masood . . 4 Wagner Jacqueline . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 145 "15N chemical shifts" 145 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-06-12 update BMRB 'update entry citation' 2019-03-07 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27813 'Amide chemical shifts of human IMP3 RRM1-2 (1-156)' 27815 'Human IMP3 KH1-2 amide chemical shifts' 27816 'Human IMP3 KH1-2 delta2 amide chemical shifts' stop_ _Original_release_date 2019-03-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Combinatorial recognition of clustered RNA elements by the multidomain RNA-binding protein IMP3. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31118463 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schneider Tim . . 2 Hung Lee-Hsueh . . 3 Aziz Masood . . 4 Wilmen Anna . . 5 Thaum Stephanie . . 6 Wagner Jacqueline . . 7 Janowski Robert . . 8 Mueller Simon . . 9 Schreiner Silke . . 10 Friedhoff Peter . . 11 Huettelmaier Stefan . . 12 Niessing Dierk . . 13 Sattler Michael . . 14 Schlundt Andreas . . 15 Bindereif Albrecht . . stop_ _Journal_abbreviation 'Nat. Commun.' _Journal_name_full 'Nature communications' _Journal_volume 10 _Journal_issue 1 _Journal_ISSN 2041-1723 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2266 _Page_last 2266 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'IMP3 KH1-2 delta1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'IMP3 KH1-2 delta1' $IMP3_(IGF2BP3)_KH1-2_delta1 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_IMP3_(IGF2BP3)_KH1-2_delta1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common IMP3_(IGF2BP3)_KH1-2_delta1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 168 _Mol_residue_sequence ; GAMAKPCDLPLRLLVPTQFV GAIIGDDGATIRNITKQTQS KIDVHRKENAGAAEKSITIL STPEGTSAACKSILEIMHKE AQDIKFTEEIPLKILAHNNF VGRLIGKEGRNLKKIEQDTD TKITISPLQELTLYNPERTI TVKGNVETCAKAEEEIMKKI RESYENDI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 188 GLY 2 189 ALA 3 190 MET 4 191 ALA 5 192 LYS 6 193 PRO 7 194 CYS 8 195 ASP 9 196 LEU 10 197 PRO 11 198 LEU 12 199 ARG 13 200 LEU 14 201 LEU 15 202 VAL 16 203 PRO 17 204 THR 18 205 GLN 19 206 PHE 20 207 VAL 21 208 GLY 22 209 ALA 23 210 ILE 24 211 ILE 25 212 GLY 26 213 ASP 27 214 ASP 28 215 GLY 29 216 ALA 30 217 THR 31 218 ILE 32 219 ARG 33 220 ASN 34 221 ILE 35 222 THR 36 223 LYS 37 224 GLN 38 225 THR 39 226 GLN 40 227 SER 41 228 LYS 42 229 ILE 43 230 ASP 44 231 VAL 45 232 HIS 46 233 ARG 47 234 LYS 48 235 GLU 49 236 ASN 50 237 ALA 51 238 GLY 52 239 ALA 53 240 ALA 54 241 GLU 55 242 LYS 56 243 SER 57 244 ILE 58 245 THR 59 246 ILE 60 247 LEU 61 248 SER 62 249 THR 63 250 PRO 64 251 GLU 65 252 GLY 66 253 THR 67 254 SER 68 255 ALA 69 256 ALA 70 257 CYS 71 258 LYS 72 259 SER 73 260 ILE 74 261 LEU 75 262 GLU 76 263 ILE 77 264 MET 78 265 HIS 79 266 LYS 80 267 GLU 81 268 ALA 82 269 GLN 83 270 ASP 84 271 ILE 85 272 LYS 86 273 PHE 87 274 THR 88 275 GLU 89 276 GLU 90 277 ILE 91 278 PRO 92 279 LEU 93 280 LYS 94 281 ILE 95 282 LEU 96 283 ALA 97 284 HIS 98 285 ASN 99 286 ASN 100 287 PHE 101 288 VAL 102 289 GLY 103 290 ARG 104 291 LEU 105 292 ILE 106 293 GLY 107 294 LYS 108 295 GLU 109 296 GLY 110 297 ARG 111 298 ASN 112 299 LEU 113 300 LYS 114 301 LYS 115 302 ILE 116 303 GLU 117 304 GLN 118 305 ASP 119 306 THR 120 307 ASP 121 308 THR 122 309 LYS 123 310 ILE 124 311 THR 125 312 ILE 126 313 SER 127 314 PRO 128 315 LEU 129 316 GLN 130 317 GLU 131 318 LEU 132 319 THR 133 320 LEU 134 321 TYR 135 322 ASN 136 323 PRO 137 324 GLU 138 325 ARG 139 326 THR 140 327 ILE 141 328 THR 142 329 VAL 143 330 LYS 144 331 GLY 145 332 ASN 146 333 VAL 147 334 GLU 148 335 THR 149 336 CYS 150 337 ALA 151 338 LYS 152 339 ALA 153 340 GLU 154 341 GLU 155 342 GLU 156 343 ILE 157 344 MET 158 345 LYS 159 346 LYS 160 347 ILE 161 348 ARG 162 349 GLU 163 350 SER 164 351 TYR 165 352 GLU 166 353 ASN 167 354 ASP 168 355 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $IMP3_(IGF2BP3)_KH1-2_delta1 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 $IMP3_(IGF2BP3)_KH1-2_delta1 'recombinant technology' . Escherichia coli . pETTrx1a 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $IMP3_(IGF2BP3)_KH1-2_delta1 0.125 mM 0.05 0.2 [U-15N] BisTris 20 mM . . 'natural abundance' 'sodium chloride' 150 mM . . 'natural abundance' TCEP 2 mM . . 'natural abundance' 'sodium azide' 0.02 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_CCPNMR_Analysis _Saveframe_category software _Name CCPNMR_Analysis _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 950 _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.15 . M pH 6.5 . 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 H 1 'methyl protons' ppm 0 external direct . . . 1 DSS N 15 'methyl protons' ppm 0 external indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' 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 'IMP3 KH1-2 delta1' _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 1 189 2 ALA H H 8.542 0.000 1 2 189 2 ALA N N 123.243 0.000 1 3 190 3 MET H H 8.378 0.001 1 4 190 3 MET N N 119.842 0.052 1 5 191 4 ALA H H 8.304 0.001 1 6 191 4 ALA N N 126.077 0.009 1 7 192 5 LYS H H 8.262 0.002 1 8 192 5 LYS N N 122.186 0.005 1 9 194 7 CYS H H 8.360 0.010 1 10 194 7 CYS N N 119.555 0.011 1 11 195 8 ASP H H 8.208 0.003 1 12 195 8 ASP N N 123.789 0.027 1 13 196 9 LEU H H 7.696 0.004 1 14 196 9 LEU N N 122.688 0.003 1 15 198 11 LEU H H 7.858 0.003 1 16 198 11 LEU N N 123.560 0.004 1 17 199 12 ARG H H 8.868 0.013 1 18 199 12 ARG N N 128.664 0.028 1 19 200 13 LEU H H 8.890 0.002 1 20 200 13 LEU N N 121.449 0.018 1 21 201 14 LEU H H 7.924 0.003 1 22 201 14 LEU N N 119.969 0.052 1 23 202 15 VAL H H 9.055 0.004 1 24 202 15 VAL N N 119.570 0.031 1 25 204 17 THR H H 8.595 0.003 1 26 204 17 THR N N 122.340 0.015 1 27 205 18 GLN H H 9.040 0.001 1 28 205 18 GLN N N 118.727 0.014 1 29 206 19 PHE H H 7.581 0.001 1 30 206 19 PHE N N 115.436 0.018 1 31 207 20 VAL H H 7.503 0.002 1 32 207 20 VAL N N 119.722 0.033 1 33 208 21 GLY H H 8.621 0.001 1 34 208 21 GLY N N 107.622 0.019 1 35 209 22 ALA H H 7.788 0.003 1 36 209 22 ALA N N 124.184 0.015 1 37 210 23 ILE H H 7.347 0.002 1 38 210 23 ILE N N 117.639 0.030 1 39 212 25 GLY H H 8.062 0.002 1 40 212 25 GLY N N 106.460 0.019 1 41 214 27 ASP H H 8.585 0.000 1 42 214 27 ASP N N 121.850 0.000 1 43 215 28 GLY H H 8.182 0.341 1 44 215 28 GLY N N 108.455 2.379 1 45 216 29 ALA H H 8.030 0.004 1 46 216 29 ALA N N 123.481 0.020 1 47 217 30 THR H H 8.049 0.001 1 48 217 30 THR N N 114.150 0.010 1 49 218 31 ILE H H 8.061 0.001 1 50 218 31 ILE N N 123.332 0.040 1 51 219 32 ARG H H 8.191 0.000 1 52 219 32 ARG N N 124.771 0.000 1 53 221 34 ILE H H 8.206 0.010 1 54 221 34 ILE N N 121.555 0.017 1 55 222 35 THR H H 7.923 0.005 1 56 222 35 THR N N 115.547 0.017 1 57 223 36 LYS H H 8.181 0.001 1 58 223 36 LYS N N 125.593 0.021 1 59 225 38 THR H H 8.148 0.005 1 60 225 38 THR N N 115.853 0.051 1 61 226 39 GLN H H 8.243 0.002 1 62 226 39 GLN N N 124.099 0.013 1 63 227 40 SER H H 8.242 0.000 1 64 227 40 SER N N 116.519 0.000 1 65 228 41 LYS H H 8.287 0.002 1 66 228 41 LYS N N 123.334 0.073 1 67 229 42 ILE H H 7.951 0.004 1 68 229 42 ILE N N 121.326 0.003 1 69 230 43 ASP H H 8.294 0.001 1 70 230 43 ASP N N 124.529 0.016 1 71 231 44 VAL H H 7.967 0.006 1 72 231 44 VAL N N 120.227 0.062 1 73 232 45 HIS H H 8.310 0.002 1 74 232 45 HIS N N 121.076 0.022 1 75 233 46 ARG H H 8.026 0.001 1 76 233 46 ARG N N 122.383 0.035 1 77 234 47 LYS H H 8.143 0.000 1 78 234 47 LYS N N 122.619 0.018 1 79 235 48 GLU H H 8.333 0.003 1 80 235 48 GLU N N 121.623 0.086 1 81 236 49 ASN H H 8.464 0.006 1 82 236 49 ASN N N 118.477 0.025 1 83 237 50 ALA H H 8.210 0.003 1 84 237 50 ALA N N 124.852 0.027 1 85 238 51 GLY H H 8.328 0.007 1 86 238 51 GLY N N 108.083 0.027 1 87 239 52 ALA H H 7.823 0.001 1 88 239 52 ALA N N 122.866 0.005 1 89 240 53 ALA H H 8.594 0.003 1 90 240 53 ALA N N 123.245 0.036 1 91 241 54 GLU H H 7.556 0.003 1 92 241 54 GLU N N 117.790 0.012 1 93 242 55 LYS H H 8.922 0.002 1 94 242 55 LYS N N 118.970 0.018 1 95 243 56 SER H H 8.751 0.002 1 96 243 56 SER N N 116.841 0.014 1 97 244 57 ILE H H 8.841 0.004 1 98 244 57 ILE N N 122.021 0.002 1 99 245 58 THR H H 8.798 0.010 1 100 245 58 THR N N 121.868 0.086 1 101 246 59 ILE H H 8.178 0.002 1 102 246 59 ILE N N 124.297 0.076 1 103 247 60 LEU H H 8.277 0.001 1 104 247 60 LEU N N 126.508 0.019 1 105 248 61 SER H H 8.217 0.001 1 106 248 61 SER N N 117.055 0.037 1 107 249 62 THR H H 8.208 0.139 1 108 249 62 THR N N 115.002 3.495 1 109 251 64 GLU H H 9.022 0.010 1 110 251 64 GLU N N 116.183 0.101 1 111 252 65 GLY H H 8.194 0.003 1 112 252 65 GLY N N 112.257 0.020 1 113 253 66 THR H H 8.723 0.003 1 114 253 66 THR N N 117.791 0.047 1 115 254 67 SER H H 7.996 0.014 1 116 254 67 SER N N 118.647 0.068 1 117 255 68 ALA H H 7.935 0.004 1 118 255 68 ALA N N 124.723 0.036 1 119 256 69 ALA H H 8.622 0.005 1 120 256 69 ALA N N 122.887 0.043 1 121 257 70 CYS H H 8.303 0.004 1 122 257 70 CYS N N 117.051 0.028 1 123 258 71 LYS H H 8.182 0.007 1 124 258 71 LYS N N 118.647 0.050 1 125 259 72 SER H H 8.297 0.002 1 126 259 72 SER N N 118.343 0.136 1 127 260 73 ILE H H 8.109 0.001 1 128 260 73 ILE N N 122.401 0.039 1 129 261 74 LEU H H 8.188 0.000 1 130 261 74 LEU N N 126.141 0.000 1 131 262 75 GLU H H 7.945 0.001 1 132 262 75 GLU N N 122.019 0.018 1 133 265 78 HIS H H 8.064 0.003 1 134 265 78 HIS N N 122.256 0.055 1 135 266 79 LYS H H 8.360 0.004 1 136 266 79 LYS N N 122.912 0.046 1 137 267 80 GLU H H 8.483 0.002 1 138 267 80 GLU N N 121.915 0.018 1 139 268 81 ALA H H 8.220 0.006 1 140 268 81 ALA N N 124.557 0.039 1 141 269 82 GLN H H 8.166 0.002 1 142 269 82 GLN N N 118.461 0.022 1 143 271 84 ILE H H 7.907 0.010 1 144 271 84 ILE N N 112.177 0.025 1 145 272 85 LYS H H 7.815 0.000 1 146 272 85 LYS N N 119.578 0.035 1 147 273 86 PHE H H 8.640 0.006 1 148 273 86 PHE N N 121.553 0.027 1 149 274 87 THR H H 8.151 0.000 1 150 274 87 THR N N 116.995 0.016 1 151 275 88 GLU H H 6.172 0.019 1 152 275 88 GLU N N 120.282 0.036 1 153 276 89 GLU H H 8.242 0.004 1 154 276 89 GLU N N 119.313 0.054 1 155 277 90 ILE H H 8.712 0.002 1 156 277 90 ILE N N 122.768 0.083 1 157 279 92 LEU H H 8.412 0.009 1 158 279 92 LEU N N 122.922 0.054 1 159 280 93 LYS H H 8.750 0.003 1 160 280 93 LYS N N 128.092 0.033 1 161 281 94 ILE H H 9.049 0.005 1 162 281 94 ILE N N 123.775 0.061 1 163 282 95 LEU H H 8.503 0.003 1 164 282 95 LEU N N 127.162 0.023 1 165 283 96 ALA H H 8.756 0.001 1 166 283 96 ALA N N 124.015 0.031 1 167 284 97 HIS H H 8.903 0.005 1 168 284 97 HIS N N 124.215 0.053 1 169 287 100 PHE H H 8.054 0.009 1 170 287 100 PHE N N 115.933 0.046 1 171 288 101 VAL H H 7.145 0.006 1 172 288 101 VAL N N 110.401 0.147 1 173 289 102 GLY H H 8.704 0.006 1 174 289 102 GLY N N 110.484 0.044 1 175 290 103 ARG H H 7.805 0.005 1 176 290 103 ARG N N 118.926 0.028 1 177 291 104 LEU H H 7.792 0.000 1 178 291 104 LEU N N 120.177 0.000 1 179 292 105 ILE H H 7.995 0.004 1 180 292 105 ILE N N 121.183 0.013 1 181 293 106 GLY H H 7.882 0.362 1 182 293 106 GLY N N 108.763 3.096 1 183 294 107 LYS H H 8.181 0.001 1 184 294 107 LYS N N 120.930 0.011 1 185 295 108 GLU H H 8.470 0.004 1 186 295 108 GLU N N 121.544 0.068 1 187 296 109 GLY H H 7.646 0.006 1 188 296 109 GLY N N 105.673 0.038 1 189 297 110 ARG H H 7.982 0.005 1 190 297 110 ARG N N 118.940 0.009 1 191 300 113 LYS H H 7.547 0.008 1 192 300 113 LYS N N 117.164 0.016 1 193 301 114 LYS H H 7.451 0.004 1 194 301 114 LYS N N 119.887 0.025 1 195 302 115 ILE H H 7.586 0.002 1 196 302 115 ILE N N 118.885 0.032 1 197 303 116 GLU H H 8.328 0.001 1 198 303 116 GLU N N 122.712 0.031 1 199 304 117 GLN H H 7.958 0.011 1 200 304 117 GLN N N 117.665 0.015 1 201 305 118 ASP H H 8.750 0.011 1 202 305 118 ASP N N 119.018 0.016 1 203 306 119 THR H H 7.768 0.007 1 204 306 119 THR N N 106.037 0.035 1 205 307 120 ASP H H 7.942 0.006 1 206 307 120 ASP N N 120.295 0.031 1 207 308 121 THR H H 7.759 0.009 1 208 308 121 THR N N 107.330 0.055 1 209 309 122 LYS H H 7.704 0.002 1 210 309 122 LYS N N 116.398 0.006 1 211 310 123 ILE H H 10.273 0.000 1 212 310 123 ILE N N 128.237 0.084 1 213 311 124 THR H H 8.823 0.009 1 214 311 124 THR N N 118.581 0.115 1 215 312 125 ILE H H 8.613 0.012 1 216 312 125 ILE N N 121.189 0.025 1 217 313 126 SER H H 8.562 0.004 1 218 313 126 SER N N 125.530 0.021 1 219 315 128 LEU H H 8.104 0.002 1 220 315 128 LEU N N 121.512 0.027 1 221 316 129 GLN H H 8.661 0.008 1 222 316 129 GLN N N 118.852 0.095 1 223 317 130 GLU H H 7.655 0.002 1 224 317 130 GLU N N 118.022 0.035 1 225 318 131 LEU H H 7.816 0.001 1 226 318 131 LEU N N 121.620 0.005 1 227 319 132 THR H H 7.761 0.005 1 228 319 132 THR N N 112.856 0.059 1 229 324 137 GLU H H 8.344 0.011 1 230 324 137 GLU N N 125.374 0.027 1 231 325 138 ARG H H 8.866 0.005 1 232 325 138 ARG N N 122.434 0.025 1 233 326 139 THR H H 8.380 0.301 1 234 326 139 THR N N 115.967 0.757 1 235 327 140 ILE H H 10.111 0.009 1 236 327 140 ILE N N 133.886 0.045 1 237 328 141 THR H H 9.133 0.004 1 238 328 141 THR N N 124.682 0.006 1 239 329 142 VAL H H 9.656 0.004 1 240 329 142 VAL N N 128.524 0.014 1 241 330 143 LYS H H 9.017 0.009 1 242 330 143 LYS N N 126.494 0.014 1 243 331 144 GLY H H 8.060 0.005 1 244 331 144 GLY N N 112.669 0.035 1 245 332 145 ASN H H 7.898 0.001 1 246 332 145 ASN N N 120.969 0.023 1 247 333 146 VAL H H 8.082 0.008 1 248 333 146 VAL N N 118.028 0.007 1 249 334 147 GLU H H 7.677 0.006 1 250 334 147 GLU N N 114.762 0.017 1 251 335 148 THR H H 8.705 0.001 1 252 335 148 THR N N 113.776 0.008 1 253 336 149 CYS H H 8.758 0.003 1 254 336 149 CYS N N 119.641 0.014 1 255 337 150 ALA H H 7.495 0.006 1 256 337 150 ALA N N 120.546 0.025 1 257 338 151 LYS H H 7.438 0.006 1 258 338 151 LYS N N 117.399 0.059 1 259 339 152 ALA H H 8.289 0.012 1 260 339 152 ALA N N 120.484 0.035 1 261 340 153 GLU H H 8.431 0.007 1 262 340 153 GLU N N 119.413 0.111 1 263 341 154 GLU H H 7.514 0.004 1 264 341 154 GLU N N 118.571 0.080 1 265 342 155 GLU H H 7.570 0.006 1 266 342 155 GLU N N 117.232 0.052 1 267 343 156 ILE H H 9.129 0.014 1 268 343 156 ILE N N 121.515 0.046 1 269 344 157 MET H H 8.697 0.019 1 270 344 157 MET N N 115.716 0.048 1 271 345 158 LYS H H 7.659 0.010 1 272 345 158 LYS N N 120.243 0.017 1 273 346 159 LYS H H 7.244 0.000 1 274 346 159 LYS N N 116.918 0.025 1 275 347 160 ILE H H 8.249 0.002 1 276 347 160 ILE N N 123.502 0.117 1 277 348 161 ARG H H 8.695 0.009 1 278 348 161 ARG N N 119.198 0.000 1 279 349 162 GLU H H 7.918 0.002 1 280 349 162 GLU N N 118.255 0.002 1 281 350 163 SER H H 7.564 0.006 1 282 350 163 SER N N 114.290 0.076 1 283 352 165 GLU H H 8.171 0.005 1 284 352 165 GLU N N 115.159 0.115 1 285 353 166 ASN H H 7.616 0.010 1 286 353 166 ASN N N 114.638 0.121 1 287 354 167 ASP H H 8.550 0.006 1 288 354 167 ASP N N 120.734 0.034 1 289 355 168 ILE H H 7.398 0.005 1 290 355 168 ILE N N 124.194 0.027 1 stop_ save_