data_50003 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; EB3 200-281 NMR chemical shift assignments ; _BMRB_accession_number 50003 _BMRB_flat_file_name bmr50003.str _Entry_type original _Submission_date 2019-08-20 _Accession_date 2019-08-20 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details '1H, 13C and 15N Resonance Assignments for the C-Terminal Domain of the Microtubule End-Binding Protein 3 (EB3).' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gaponenko Vadim . . 2 Komarova Yulia . . 3 Hitchinson Ben . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 74 "13C chemical shifts" 119 "15N chemical shifts" 74 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-05-29 update BMRB 'update entry citation' 2020-04-17 original author 'original release' stop_ _Original_release_date 2019-08-23 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Resonance Assignment and Structure Prediction of the C-terminal Domain of the Microtubule End-Binding Protein 3 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32421702 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Abdelkarim Hazem . . 2 Hitchinson Ben . . 3 Qu Xinyan . . 4 Banerjee Avik . . 5 Komarova Yulia A. . 6 Gaponenko Vadim . . stop_ _Journal_abbreviation 'PLOS ONE' _Journal_volume 15 _Journal_issue 5 _Journal_ISSN 1932-6203 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first e0232338 _Page_last e0232338 _Year 2020 _Details . loop_ _Keyword 'EB3, Microtubule End-Binding Protein 3' stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'EB3 C-term' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'EB3 C-term' $entity_1 stop_ _System_molecular_weight 9500 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass . _Mol_thiol_state unknown loop_ _Biological_function 'Microtubule end binding protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 82 _Mol_residue_sequence ; AQILELNQQLVDLKLTVDGL EKERDFYFSKLRDIELICQE HESENSPVISGIIGILYATE EGFAPPEDDEIEEHQQEDQD EY ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 200 ALA 2 201 GLN 3 202 ILE 4 203 LEU 5 204 GLU 6 205 LEU 7 206 ASN 8 207 GLN 9 208 GLN 10 209 LEU 11 210 VAL 12 211 ASP 13 212 LEU 14 213 LYS 15 214 LEU 16 215 THR 17 216 VAL 18 217 ASP 19 218 GLY 20 219 LEU 21 220 GLU 22 221 LYS 23 222 GLU 24 223 ARG 25 224 ASP 26 225 PHE 27 226 TYR 28 227 PHE 29 228 SER 30 229 LYS 31 230 LEU 32 231 ARG 33 232 ASP 34 233 ILE 35 234 GLU 36 235 LEU 37 236 ILE 38 237 CYS 39 238 GLN 40 239 GLU 41 240 HIS 42 241 GLU 43 242 SER 44 243 GLU 45 244 ASN 46 245 SER 47 246 PRO 48 247 VAL 49 248 ILE 50 249 SER 51 250 GLY 52 251 ILE 53 252 ILE 54 253 GLY 55 254 ILE 56 255 LEU 57 256 TYR 58 257 ALA 59 258 THR 60 259 GLU 61 260 GLU 62 261 GLY 63 262 PHE 64 263 ALA 65 264 PRO 66 265 PRO 67 266 GLU 68 267 ASP 69 268 ASP 70 269 GLU 71 270 ILE 72 271 GLU 73 272 GLU 74 273 HIS 75 274 GLN 76 275 GLN 77 276 GLU 78 277 ASP 79 278 GLN 80 279 ASP 81 280 GLU 82 281 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 'E. coli' 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli . plasmid PET42a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'EB3 C-terminus 350 uM' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 350 uM '[U-100% 13C; U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_software_2 _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _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_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _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 7.4 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 water C 13 protons ppm . internal indirect . . . . water H 1 protons ppm . internal direct . . . 1 water N 15 protons ppm . internal indirect . . . . 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_1 $software_2 stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-1H NOESY' '3D HNCO' '3D HNCACB' '3D CBCA(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name 'EB3 C-term' _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 1 201 2 GLN H H 7.468 . . 2 201 2 GLN CA C 56.51 . . 3 201 2 GLN N N 115.2 . . 4 202 3 ILE H H 8.09 . . 5 202 3 ILE CA C 61.39 . . 6 202 3 ILE CB C 38.81 . . 7 202 3 ILE N N 117.8 . . 8 203 4 LEU H H 8.825 . . 9 203 4 LEU CA C 57.96 . . 10 203 4 LEU N N 119 . . 11 205 6 LEU H H 8.473 . . 12 205 6 LEU CA C 56.78 . . 13 205 6 LEU CB C 41.49 . . 14 205 6 LEU N N 120.2 . . 15 206 7 ASN H H 8.197 . . 16 206 7 ASN CA C 54.61 . . 17 206 7 ASN CB C 41.46 . . 18 206 7 ASN N N 117.3 . . 19 207 8 GLN H H 8.33 . . 20 207 8 GLN CA C 55.42 . . 21 207 8 GLN CB C 30.48 . . 22 207 8 GLN N N 124.1 . . 23 208 9 GLN H H 7.937 . . 24 208 9 GLN CA C 56.74 . . 25 208 9 GLN CB C 30.98 . . 26 208 9 GLN N N 120 . . 27 209 10 LEU H H 8.463 . . 28 209 10 LEU CA C 58.46 . . 29 209 10 LEU CB C 41.52 . . 30 209 10 LEU N N 116.8 . . 31 210 11 VAL H H 7.9 . . 32 210 11 VAL CA C 64.49 . . 33 210 11 VAL N N 121.1 . . 34 211 12 ASP H H 8.282 . . 35 211 12 ASP CA C 54.7 . . 36 211 12 ASP CB C 41.44 . . 37 211 12 ASP N N 118.7 . . 38 212 13 LEU H H 8.232 . . 39 212 13 LEU CA C 54.97 . . 40 212 13 LEU CB C 41.59 . . 41 212 13 LEU N N 124.3 . . 42 213 14 LYS H H 8.186 . . 43 213 14 LYS CA C 56.74 . . 44 213 14 LYS N N 120.1 . . 45 215 16 THR H H 7.887 . . 46 215 16 THR CA C 67.31 . . 47 215 16 THR N N 120.4 . . 48 216 17 VAL H H 7.344 . . 49 216 17 VAL CA C 64.2 . . 50 216 17 VAL N N 121.4 . . 51 218 19 GLY H H 7.878 . . 52 218 19 GLY CA C 46.98 . . 53 218 19 GLY N N 110.1 . . 54 219 20 LEU H H 7.846 . . 55 219 20 LEU CA C 58.53 . . 56 219 20 LEU N N 118.8 . . 57 220 21 GLU H H 7.517 . . 58 220 21 GLU CA C 56.48 . . 59 220 21 GLU N N 117.1 . . 60 221 22 LYS H H 8.036 . . 61 221 22 LYS CA C 59.63 . . 62 221 22 LYS N N 119.2 . . 63 223 24 ARG H H 8.447 . . 64 223 24 ARG CA C 56.85 . . 65 223 24 ARG CB C 30.84 . . 66 223 24 ARG N N 122.7 . . 67 224 25 ASP H H 7.604 . . 68 224 25 ASP CA C 59.38 . . 69 224 25 ASP CB C 39.64 . . 70 224 25 ASP N N 123.1 . . 71 225 26 PHE H H 8.001 . . 72 225 26 PHE CA C 58.18 . . 73 225 26 PHE N N 118.9 . . 74 226 27 TYR H H 7.75 . . 75 226 27 TYR CA C 57.15 . . 76 226 27 TYR CB C 39.55 . . 77 226 27 TYR N N 114.9 . . 78 227 28 PHE H H 7.938 . . 79 227 28 PHE CA C 60.31 . . 80 227 28 PHE N N 121.6 . . 81 228 29 SER H H 8.929 . . 82 228 29 SER CA C 61.66 . . 83 228 29 SER CB C 60.34 . . 84 228 29 SER N N 119 . . 85 229 30 LYS H H 8.678 . . 86 229 30 LYS CA C 57.33 . . 87 229 30 LYS CB C 30.51 . . 88 229 30 LYS N N 122.2 . . 89 230 31 LEU H H 7.505 . . 90 230 31 LEU CA C 58.51 . . 91 230 31 LEU N N 118.6 . . 92 231 32 ARG H H 8.533 . . 93 231 32 ARG CA C 56.67 . . 94 231 32 ARG CB C 30.61 . . 95 231 32 ARG N N 114.2 . . 96 232 33 ASP H H 8.49 . . 97 232 33 ASP CA C 54.85 . . 98 232 33 ASP CB C 41.43 . . 99 232 33 ASP N N 114.2 . . 100 233 34 ILE H H 8.132 . . 101 233 34 ILE CA C 61.41 . . 102 233 34 ILE CB C 38.93 . . 103 233 34 ILE N N 121.2 . . 104 234 35 GLU H H 8.41 . . 105 234 35 GLU CA C 56.61 . . 106 234 35 GLU CB C 30.75 . . 107 234 35 GLU N N 114.4 . . 108 235 36 LEU H H 7.758 . . 109 235 36 LEU CA C 59.44 . . 110 235 36 LEU CB C 39.62 . . 111 235 36 LEU N N 118.2 . . 112 236 37 ILE H H 9.078 . . 113 236 37 ILE CA C 62.27 . . 114 236 37 ILE N N 120.2 . . 115 237 38 CYS H H 8.129 . . 116 237 38 CYS CA C 61.35 . . 117 237 38 CYS CB C 39.05 . . 118 237 38 CYS N N 121.2 . . 119 238 39 GLN H H 8.448 . . 120 238 39 GLN CA C 56.89 . . 121 238 39 GLN CB C 30.77 . . 122 238 39 GLN N N 114.2 . . 123 239 40 GLU H H 8.412 . . 124 239 40 GLU CA C 56.87 . . 125 239 40 GLU CB C 30.9 . . 126 239 40 GLU N N 115.3 . . 127 240 41 HIS H H 8.547 . . 128 240 41 HIS CA C 56.95 . . 129 240 41 HIS CB C 34.88 . . 130 240 41 HIS N N 123.6 . . 131 241 42 GLU H H 8.538 . . 132 241 42 GLU CA C 57.44 . . 133 241 42 GLU CB C 30.45 . . 134 241 42 GLU N N 122.1 . . 135 242 43 SER H H 7.245 . . 136 242 43 SER CA C 60.26 . . 137 242 43 SER N N 120.7 . . 138 243 44 GLU H H 8.215 . . 139 243 44 GLU CA C 56.64 . . 140 243 44 GLU CB C 31.21 . . 141 243 44 GLU N N 117.3 . . 142 244 45 ASN H H 8.232 . . 143 244 45 ASN CA C 54.69 . . 144 244 45 ASN CB C 41.56 . . 145 244 45 ASN N N 118.6 . . 146 245 46 SER H H 8.069 . . 147 245 46 SER CA C 59.64 . . 148 245 46 SER CB C 54.77 . . 149 245 46 SER N N 119.892 . . 150 247 48 VAL H H 7.09 . . 151 247 48 VAL CA C 64.15 . . 152 247 48 VAL N N 119.7 . . 153 248 49 ILE H H 8.235 . . 154 248 49 ILE CA C 62.58 . . 155 248 49 ILE N N 114.2 . . 156 249 50 SER H H 8.877 . . 157 249 50 SER CA C 58.01 . . 158 249 50 SER N N 120 . . 159 250 51 GLY H H 7.999 . . 160 250 51 GLY CA C 47.74 . . 161 250 51 GLY N N 105.1 . . 162 251 52 ILE H H 7.971 . . 163 251 52 ILE CA C 59.55 . . 164 251 52 ILE N N 119.9 . . 165 252 53 ILE H H 9.078 . . 166 252 53 ILE CA C 62.27 . . 167 252 53 ILE N N 120.2 . . 168 253 54 GLY H H 7.76 . . 169 253 54 GLY CA C 47.23 . . 170 253 54 GLY N N 105 . . 171 254 55 ILE H H 8.12 . . 172 254 55 ILE CA C 61.33 . . 173 254 55 ILE CB C 39.13 . . 174 254 55 ILE N N 120.5 . . 175 255 56 LEU H H 8.127 . . 176 255 56 LEU CA C 58.68 . . 177 255 56 LEU N N 120.5 . . 178 256 57 TYR H H 7.805 . . 179 256 57 TYR CA C 57.17 . . 180 256 57 TYR N N 114.7 . . 181 257 58 ALA H H 7.352 . . 182 257 58 ALA CA C 53.73 . . 183 257 58 ALA CB C 19.15 . . 184 257 58 ALA N N 124.3 . . 185 258 59 THR H H 8.928 . . 186 258 59 THR CA C 61.62 . . 187 258 59 THR N N 119 . . 188 259 60 GLU H H 8.519 . . 189 259 60 GLU CA C 55.99 . . 190 259 60 GLU CB C 29.83 . . 191 259 60 GLU N N 122.4 . . 192 260 61 GLU H H 8.465 . . 193 260 61 GLU CA C 56.75 . . 194 260 61 GLU CB C 30.6 . . 195 260 61 GLU N N 121 . . 196 261 62 GLY H H 8.318 . . 197 261 62 GLY CA C 45.39 . . 198 261 62 GLY N N 109.8 . . 199 262 63 PHE H H 8.009 . . 200 262 63 PHE CA C 57.82 . . 201 262 63 PHE CB C 40.12 . . 202 262 63 PHE N N 120.3 . . 203 263 64 ALA H H 8.137 . . 204 263 64 ALA CA C 50.23 . . 205 263 64 ALA CB C 18.87 . . 206 263 64 ALA N N 128 . . 207 266 67 GLU H H 8.517 . . 208 266 67 GLU CA C 56.66 . . 209 266 67 GLU CB C 30.67 . . 210 266 67 GLU N N 121.4 . . 211 267 68 ASP H H 8.358 . . 212 267 68 ASP CA C 54.71 . . 213 267 68 ASP CB C 41.56 . . 214 267 68 ASP N N 121.7 . . 215 268 69 ASP H H 8.299 . . 216 268 69 ASP CA C 54.73 . . 217 268 69 ASP CB C 41.49 . . 218 268 69 ASP N N 121.1 . . 219 269 70 GLU H H 8.205 . . 220 269 70 GLU CA C 56.73 . . 221 269 70 GLU CB C 30.49 . . 222 269 70 GLU N N 121 . . 223 270 71 ILE H H 8.15 . . 224 270 71 ILE CA C 61.23 . . 225 270 71 ILE CB C 38.99 . . 226 270 71 ILE N N 122.5 . . 227 271 72 GLU H H 8.437 . . 228 271 72 GLU CA C 56.73 . . 229 271 72 GLU CB C 30.8 . . 230 271 72 GLU N N 125.8 . . 231 272 73 GLU H H 8.437 . . 232 272 73 GLU CA C 56.78 . . 233 272 73 GLU CB C 30.73 . . 234 272 73 GLU N N 123.1 . . 235 273 74 HIS H H 7.661 . . 236 273 74 HIS CA C 59.4 . . 237 273 74 HIS CB C 39.61 . . 238 273 74 HIS N N 118.5 . . 239 274 75 GLN H H 7.812 . . 240 274 75 GLN N N 120 . . 241 275 76 GLN H H 8.322 . . 242 275 76 GLN CA C 55.97 . . 243 275 76 GLN N N 118.1 . . 244 276 77 GLU H H 8.581 . . 245 276 77 GLU CA C 56.74 . . 246 276 77 GLU CB C 30.64 . . 247 276 77 GLU N N 122.9 . . 248 277 78 ASP H H 8.456 . . 249 277 78 ASP CA C 54.72 . . 250 277 78 ASP CB C 41.38 . . 251 277 78 ASP N N 121.8 . . 252 278 79 GLN H H 8.333 . . 253 278 79 GLN CA C 55.84 . . 254 278 79 GLN CB C 30.02 . . 255 278 79 GLN N N 120.6 . . 256 279 80 ASP H H 8.383 . . 257 279 80 ASP CA C 54.86 . . 258 279 80 ASP CB C 41.51 . . 259 279 80 ASP N N 122 . . 260 280 81 GLU H H 8.322 . . 261 280 81 GLU CA C 56.73 . . 262 280 81 GLU CB C 30.93 . . 263 280 81 GLU N N 121.4 . . 264 281 82 TYR H H 7.729 . . 265 281 82 TYR CA C 59.43 . . 266 281 82 TYR CB C 39.73 . . 267 281 82 TYR N N 126 . . stop_ save_