data_19336 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR assignments of 5P12-RANTES-E66S in the presence of dodecylphosphocholine ; _BMRB_accession_number 19336 _BMRB_flat_file_name bmr19336.str _Entry_type original _Submission_date 2013-07-03 _Accession_date 2013-07-03 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'H, N, CA, CB and C assignments of 5P12-RANTES-E66S with cyclic N-terminal Q0 in the presence of dodecylphosphocholine' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wiktor Maciej . . 2 Grzesiek Stephan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 60 "13C chemical shifts" 181 "15N chemical shifts" 60 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-04 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 19335 'NMR assignments of 5P12-RANTES-E66S' stop_ _Original_release_date 2013-07-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Characterization of structure, dynamics, and detergent interactions of the anti-HIV chemokine variant 5P12-RANTES ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24314089 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wiktor Maciej . . 2 Hartley Oliver . . 3 Grzesiek Stephan . . stop_ _Journal_abbreviation 'Biophys. J.' _Journal_volume 105 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2586 _Page_last 2597 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 5P12-RANTES-E66S _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 5P12-RANTES-E66S $5P12-RANTES-E66S stop_ _System_molecular_weight 7884.1 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_5P12-RANTES-E66S _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 5P12-RANTES-E66S _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 69 _Mol_residue_sequence ; QGPPLMATQSCCFAYIARPL PRAHIKEYFYTSGKCSNPAV VFVTRKNRQVCANPEKKWVR EYINSLSMS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 GLN 2 1 GLY 3 2 PRO 4 3 PRO 5 4 LEU 6 5 MET 7 6 ALA 8 7 THR 9 8 GLN 10 9 SER 11 10 CYS 12 11 CYS 13 12 PHE 14 13 ALA 15 14 TYR 16 15 ILE 17 16 ALA 18 17 ARG 19 18 PRO 20 19 LEU 21 20 PRO 22 21 ARG 23 22 ALA 24 23 HIS 25 24 ILE 26 25 LYS 27 26 GLU 28 27 TYR 29 28 PHE 30 29 TYR 31 30 THR 32 31 SER 33 32 GLY 34 33 LYS 35 34 CYS 36 35 SER 37 36 ASN 38 37 PRO 39 38 ALA 40 39 VAL 41 40 VAL 42 41 PHE 43 42 VAL 44 43 THR 45 44 ARG 46 45 LYS 47 46 ASN 48 47 ARG 49 48 GLN 50 49 VAL 51 50 CYS 52 51 ALA 53 52 ASN 54 53 PRO 55 54 GLU 56 55 LYS 57 56 LYS 58 57 TRP 59 58 VAL 60 59 ARG 61 60 GLU 62 61 TYR 63 62 ILE 64 63 ASN 65 64 SER 66 65 LEU 67 66 SER 68 67 MET 69 68 SER 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 $5P12-RANTES-E66S . . . . . . 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 $5P12-RANTES-E66S 'recombinant technology' . Escherichia coli BL21(DE3) pGEV2 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 $5P12-RANTES-E66S 0.25 mM '[U-98% 13C; U-98% 15N]' 'sodium formate' 50 mM '[U-99% 2H]' 'sodium azide' 0.02 % 'natural abundance' dodecylphosphocholine 1 % 'natural abundance' H2O 1 % 'natural abundance' D2O 1 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _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_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_CBCANH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCANH' _Sample_label $sample_1 save_ save_3D_CBCACONH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCACONH' _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 pH 3.8 . 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 water C 13 protons ppm 4.453 internal indirect . . . 0.251449530 water H 1 protons ppm 4.453 internal direct . . . 1.000000000 water N 15 protons ppm 4.453 internal 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 '3D HNCO' '3D CBCANH' 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 5P12-RANTES-E66S _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 0 1 GLN H H 7.751 . . 2 0 1 GLN C C 177.948 . . 3 0 1 GLN CA C 59.888 . . 4 0 1 GLN CB C 28.014 . . 5 0 1 GLN N N 124.812 . . 6 1 2 GLY H H 8.163 . . 7 1 2 GLY CA C 44.422 . . 8 1 2 GLY N N 108.818 . . 9 3 4 PRO C C 176.743 . . 10 3 4 PRO CB C 31.803 . . 11 4 5 LEU H H 8.083 . . 12 4 5 LEU C C 177.365 . . 13 4 5 LEU CA C 55.735 . . 14 4 5 LEU CB C 42.629 . . 15 4 5 LEU N N 121.358 . . 16 5 6 MET H H 8.152 . . 17 5 6 MET C C 175.931 . . 18 5 6 MET CA C 55.744 . . 19 5 6 MET CB C 33.198 . . 20 5 6 MET N N 119.529 . . 21 6 7 ALA H H 8.109 . . 22 6 7 ALA C C 177.792 . . 23 6 7 ALA CA C 52.950 . . 24 6 7 ALA CB C 19.427 . . 25 6 7 ALA N N 124.068 . . 26 7 8 THR H H 7.859 . . 27 7 8 THR C C 174.789 . . 28 7 8 THR CA C 62.262 . . 29 7 8 THR CB C 69.791 . . 30 7 8 THR N N 111.725 . . 31 8 9 GLN H H 8.184 . . 32 8 9 GLN C C 176.074 . . 33 8 9 GLN CA C 56.410 . . 34 8 9 GLN CB C 29.613 . . 35 8 9 GLN N N 121.381 . . 36 9 10 SER H H 8.127 . . 37 9 10 SER C C 174.776 . . 38 9 10 SER CA C 59.027 . . 39 9 10 SER CB C 64.145 . . 40 9 10 SER N N 115.660 . . 41 10 11 CYS H H 8.336 . . 42 10 11 CYS CA C 56.015 . . 43 10 11 CYS CB C 41.540 . . 44 10 11 CYS N N 119.586 . . 45 11 12 CYS H H 8.291 . . 46 11 12 CYS CA C 56.658 . . 47 11 12 CYS CB C 41.526 . . 48 11 12 CYS N N 119.133 . . 49 12 13 PHE C C 175.066 . . 50 13 14 ALA H H 7.883 . . 51 13 14 ALA C C 177.074 . . 52 13 14 ALA CA C 53.091 . . 53 13 14 ALA CB C 19.869 . . 54 13 14 ALA N N 122.472 . . 55 14 15 TYR H H 7.782 . . 56 14 15 TYR CA C 58.482 . . 57 14 15 TYR CB C 40.170 . . 58 14 15 TYR N N 117.029 . . 59 15 16 ILE C C 174.747 . . 60 16 17 ALA H H 7.873 . . 61 16 17 ALA C C 176.845 . . 62 16 17 ALA CA C 52.283 . . 63 16 17 ALA CB C 19.670 . . 64 16 17 ALA N N 124.077 . . 65 17 18 ARG H H 7.706 . . 66 17 18 ARG CA C 54.997 . . 67 17 18 ARG CB C 30.503 . . 68 17 18 ARG N N 119.255 . . 69 18 19 PRO C C 176.146 . . 70 18 19 PRO CB C 31.860 . . 71 19 20 LEU H H 7.854 . . 72 19 20 LEU CA C 53.227 . . 73 19 20 LEU CB C 42.359 . . 74 19 20 LEU N N 121.444 . . 75 20 21 PRO C C 176.937 . . 76 20 21 PRO CB C 31.761 . . 77 21 22 ARG H H 8.124 . . 78 21 22 ARG C C 176.069 . . 79 21 22 ARG CA C 56.882 . . 80 21 22 ARG CB C 30.462 . . 81 21 22 ARG N N 118.299 . . 82 22 23 ALA H H 7.951 . . 83 22 23 ALA C C 177.350 . . 84 22 23 ALA CA C 52.834 . . 85 22 23 ALA CB C 19.746 . . 86 22 23 ALA N N 121.559 . . 87 23 24 HIS H H 8.297 . . 88 23 24 HIS C C 174.977 . . 89 23 24 HIS CA C 55.868 . . 90 23 24 HIS CB C 28.675 . . 91 23 24 HIS N N 115.398 . . 92 24 25 ILE H H 8.011 . . 93 24 25 ILE C C 176.250 . . 94 24 25 ILE CA C 62.717 . . 95 24 25 ILE CB C 38.741 . . 96 24 25 ILE N N 119.252 . . 97 25 26 LYS H H 8.264 . . 98 25 26 LYS C C 176.780 . . 99 25 26 LYS CA C 58.463 . . 100 25 26 LYS CB C 32.737 . . 101 25 26 LYS N N 121.267 . . 102 26 27 GLU H H 7.939 . . 103 26 27 GLU C C 176.507 . . 104 26 27 GLU CA C 57.318 . . 105 26 27 GLU CB C 29.244 . . 106 26 27 GLU N N 117.557 . . 107 27 28 TYR H H 7.848 . . 108 27 28 TYR C C 175.600 . . 109 27 28 TYR CA C 59.379 . . 110 27 28 TYR CB C 39.015 . . 111 27 28 TYR N N 118.673 . . 112 28 29 PHE H H 7.783 . . 113 28 29 PHE C C 175.199 . . 114 28 29 PHE CA C 58.482 . . 115 28 29 PHE CB C 40.170 . . 116 28 29 PHE N N 117.133 . . 117 29 30 TYR H H 7.937 . . 118 29 30 TYR C C 175.802 . . 119 29 30 TYR CA C 58.280 . . 120 29 30 TYR CB C 39.271 . . 121 29 30 TYR N N 118.997 . . 122 30 31 THR H H 7.873 . . 123 30 31 THR C C 174.430 . . 124 30 31 THR CA C 61.907 . . 125 30 31 THR CB C 69.987 . . 126 30 31 THR N N 113.544 . . 127 31 32 SER H H 8.028 . . 128 31 32 SER C C 175.007 . . 129 31 32 SER CA C 58.803 . . 130 31 32 SER CB C 64.195 . . 131 31 32 SER N N 116.863 . . 132 32 33 GLY H H 8.206 . . 133 32 33 GLY C C 174.146 . . 134 32 33 GLY CA C 45.750 . . 135 32 33 GLY N N 109.943 . . 136 33 34 LYS H H 8.004 . . 137 33 34 LYS C C 176.493 . . 138 33 34 LYS CA C 56.673 . . 139 33 34 LYS CB C 33.070 . . 140 33 34 LYS N N 119.922 . . 141 34 35 CYS H H 8.229 . . 142 34 35 CYS C C 174.260 . . 143 34 35 CYS CA C 55.539 . . 144 34 35 CYS CB C 41.677 . . 145 34 35 CYS N N 118.132 . . 146 35 36 SER H H 8.130 . . 147 35 36 SER C C 173.594 . . 148 35 36 SER CA C 58.686 . . 149 35 36 SER CB C 64.067 . . 150 35 36 SER N N 116.429 . . 151 36 37 ASN H H 8.006 . . 152 36 37 ASN CA C 51.526 . . 153 36 37 ASN CB C 39.449 . . 154 36 37 ASN N N 120.209 . . 155 37 38 PRO C C 176.610 . . 156 37 38 PRO CB C 32.302 . . 157 38 39 ALA H H 8.075 . . 158 38 39 ALA C C 177.942 . . 159 38 39 ALA CA C 53.501 . . 160 38 39 ALA CB C 19.296 . . 161 38 39 ALA N N 120.629 . . 162 39 40 VAL H H 7.624 . . 163 39 40 VAL C C 176.363 . . 164 39 40 VAL CA C 63.282 . . 165 39 40 VAL CB C 32.634 . . 166 39 40 VAL N N 115.992 . . 167 40 41 VAL H H 7.703 . . 168 40 41 VAL C C 175.895 . . 169 40 41 VAL CA C 63.439 . . 170 40 41 VAL CB C 32.624 . . 171 40 41 VAL N N 120.114 . . 172 41 42 PHE H H 7.939 . . 173 41 42 PHE C C 175.886 . . 174 41 42 PHE CA C 58.594 . . 175 41 42 PHE CB C 39.765 . . 176 41 42 PHE N N 120.280 . . 177 42 43 VAL H H 7.795 . . 178 42 43 VAL C C 176.121 . . 179 42 43 VAL CA C 63.111 . . 180 42 43 VAL CB C 32.707 . . 181 42 43 VAL N N 118.186 . . 182 43 44 THR H H 7.967 . . 183 43 44 THR C C 174.889 . . 184 43 44 THR CA C 62.256 . . 185 43 44 THR CB C 70.028 . . 186 43 44 THR N N 114.524 . . 187 44 45 ARG H H 8.120 . . 188 44 45 ARG C C 176.569 . . 189 44 45 ARG CA C 57.058 . . 190 44 45 ARG CB C 30.590 . . 191 44 45 ARG N N 121.417 . . 192 45 46 LYS H H 8.036 . . 193 45 46 LYS C C 176.277 . . 194 45 46 LYS CA C 57.024 . . 195 45 46 LYS CB C 32.708 . . 196 45 46 LYS N N 119.563 . . 197 46 47 ASN H H 8.044 . . 198 46 47 ASN C C 174.932 . . 199 46 47 ASN CA C 53.602 . . 200 46 47 ASN CB C 38.940 . . 201 46 47 ASN N N 117.512 . . 202 47 48 ARG H H 8.016 . . 203 47 48 ARG C C 175.923 . . 204 47 48 ARG CA C 56.662 . . 205 47 48 ARG CB C 30.753 . . 206 47 48 ARG N N 119.816 . . 207 48 49 GLN H H 8.191 . . 208 48 49 GLN C C 175.968 . . 209 48 49 GLN CA C 56.120 . . 210 48 49 GLN CB C 29.754 . . 211 48 49 GLN N N 120.120 . . 212 49 50 VAL H H 8.029 . . 213 49 50 VAL CA C 62.713 . . 214 49 50 VAL C C 175.751 . . 215 49 50 VAL N N 119.420 . . 216 50 51 CYS H H 8.203 . . 217 50 51 CYS C C 173.734 . . 218 50 51 CYS CA C 55.256 . . 219 50 51 CYS CB C 41.651 . . 220 50 51 CYS N N 120.125 . . 221 51 52 ALA H H 8.146 . . 222 51 52 ALA C C 176.404 . . 223 51 52 ALA CA C 52.280 . . 224 51 52 ALA CB C 20.041 . . 225 51 52 ALA N N 124.050 . . 226 52 53 ASN H H 8.261 . . 227 52 53 ASN CA C 52.374 . . 228 52 53 ASN CB C 39.028 . . 229 52 53 ASN N N 118.021 . . 230 53 54 PRO CB C 31.847 . . 231 54 55 GLU H H 7.833 . . 232 54 55 GLU C C 176.832 . . 233 54 55 GLU CA C 57.362 . . 234 54 55 GLU CB C 29.106 . . 235 54 55 GLU N N 117.825 . . 236 55 56 LYS H H 8.141 . . 237 55 56 LYS C C 177.655 . . 238 55 56 LYS CA C 58.610 . . 239 55 56 LYS CB C 32.729 . . 240 55 56 LYS N N 120.270 . . 241 56 57 LYS H H 8.035 . . 242 56 57 LYS CA C 58.856 . . 243 56 57 LYS CB C 32.708 . . 244 56 57 LYS N N 119.435 . . 245 57 58 TRP CA C 59.402 . . 246 57 58 TRP C C 177.913 . . 247 57 58 TRP CB C 29.298 . . 248 58 59 VAL H H 7.620 . . 249 58 59 VAL C C 177.268 . . 250 58 59 VAL CA C 66.285 . . 251 58 59 VAL CB C 31.731 . . 252 58 59 VAL N N 118.183 . . 253 59 60 ARG H H 7.816 . . 254 59 60 ARG C C 177.939 . . 255 59 60 ARG CA C 59.278 . . 256 59 60 ARG CB C 29.977 . . 257 59 60 ARG N N 118.654 . . 258 60 61 GLU H H 7.977 . . 259 60 61 GLU C C 178.310 . . 260 60 61 GLU CA C 58.851 . . 261 60 61 GLU CB C 28.635 . . 262 60 61 GLU N N 117.232 . . 263 61 62 TYR H H 8.019 . . 264 61 62 TYR C C 178.021 . . 265 61 62 TYR CA C 61.274 . . 266 61 62 TYR CB C 38.838 . . 267 61 62 TYR N N 119.359 . . 268 62 63 ILE H H 8.124 . . 269 62 63 ILE C C 177.519 . . 270 62 63 ILE CA C 64.049 . . 271 62 63 ILE CB C 37.558 . . 272 62 63 ILE N N 118.196 . . 273 63 64 ASN H H 8.114 . . 274 63 64 ASN C C 176.747 . . 275 63 64 ASN CA C 55.485 . . 276 63 64 ASN CB C 38.726 . . 277 63 64 ASN N N 118.209 . . 278 64 65 SER H H 7.822 . . 279 64 65 SER C C 174.777 . . 280 64 65 SER CA C 60.267 . . 281 64 65 SER CB C 63.766 . . 282 64 65 SER N N 114.565 . . 283 65 66 LEU H H 7.556 . . 284 65 66 LEU C C 176.804 . . 285 65 66 LEU CA C 55.846 . . 286 65 66 LEU CB C 42.543 . . 287 65 66 LEU N N 121.528 . . 288 66 67 SER H H 7.837 . . 289 66 67 SER C C 174.246 . . 290 66 67 SER CA C 58.662 . . 291 66 67 SER CB C 64.138 . . 292 66 67 SER N N 113.399 . . 293 67 68 MET H H 8.037 . . 294 67 68 MET C C 175.268 . . 295 67 68 MET CA C 55.697 . . 296 67 68 MET CB C 33.552 . . 297 67 68 MET N N 120.895 . . 298 68 69 SER H H 7.848 . . 299 68 69 SER CA C 59.397 . . 300 68 69 SER CB C 64.859 . . 301 68 69 SER N N 119.147 . . stop_ save_