data_1336 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; High-Resolution Three-Dimensional Structure of a Single Zinc Finger from a Human Enhancer Binding Protein Solution ; _BMRB_accession_number 1336 _BMRB_flat_file_name bmr1336.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _Entry_origination BMRB _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 Omichinski James G. . 2 Clore G. Marius . 3 Appella Ettore . . 4 Sakaguchi Kazuyasu . . 5 Gronenborn Angela M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 199 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-14 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Omichinski, James G., Clore, G. Marius, Appella, Ettore, Sakaguchi, Kazuyasu, Gronenborn, Angela M., "High-Resolution Three-Dimensional Structure of a Single Zinc Finger from a Human Enhancer Binding Protein Solution," Biochemistry 29 (40), 9324-9334 (1990). ; _Citation_title ; High-Resolution Three-Dimensional Structure of a Single Zinc Finger from a Human Enhancer Binding Protein Solution ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Omichinski James G. . 2 Clore G. Marius . 3 Appella Ettore . . 4 Sakaguchi Kazuyasu . . 5 Gronenborn Angela M. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 29 _Journal_issue 40 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9324 _Page_last 9334 _Year 1990 _Details . save_ ################################## # Molecular system description # ################################## save_system_enhancer-binding_protein _Saveframe_category molecular_system _Mol_system_name 'enhancer-binding protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'enhancer-binding protein' $enhancer-binding_protein stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_enhancer-binding_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'enhancer-binding protein' _Name_variant '30 aa of carboxyl-terminal zinc finger' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 30 _Mol_residue_sequence ; RPYHCSYCNFSFKTKGNLTK HMKSKAHSKK ; loop_ _Residue_seq_code _Residue_label 1 ARG 2 PRO 3 TYR 4 HIS 5 CYS 6 SER 7 TYR 8 CYS 9 ASN 10 PHE 11 SER 12 PHE 13 LYS 14 THR 15 LYS 16 GLY 17 ASN 18 LEU 19 THR 20 LYS 21 HIS 22 MET 23 LYS 24 SER 25 LYS 26 ALA 27 HIS 28 SER 29 LYS 30 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-31 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 1337 "enhancer-binding protein" 100.00 30 100.00 100.00 1.30e-11 PDB 3ZNF "High-Resolution Three-Dimensional Structure Of A Single Zinc Finger From A Human Enhancer Binding Protein In Solution" 100.00 30 100.00 100.00 1.30e-11 PDB 4ZNF "High-Resolution Three-Dimensional Structure Of A Single Zinc Finger From A Human Enhancer Binding Protein In Solution" 100.00 30 100.00 100.00 1.30e-11 DBJ BAE22097 "unnamed protein product [Mus musculus]" 100.00 876 100.00 100.00 2.73e-12 DBJ BAE22971 "unnamed protein product [Mus musculus]" 100.00 667 100.00 100.00 5.60e-13 EMBL CAA48762 "alphaA-CRYBP1 [Mus musculus]" 100.00 665 100.00 100.00 6.99e-13 GB EAW55309 "human immunodeficiency virus type I enhancer binding protein 1, isoform CRA_a [Homo sapiens]" 53.33 645 100.00 100.00 6.65e-01 REF XP_009986318 "PREDICTED: zinc finger protein 40-like, partial [Tauraco erythrolophus]" 50.00 206 100.00 100.00 4.71e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $enhancer-binding_protein human 9606 Eukaryota Metazoa Homo sapiens generic 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 $enhancer-binding_protein 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.8 . na temperature 279 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label DSS H . . ppm 0 . . . . . $entry_citation $entry_citation 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'enhancer-binding protein' _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 . 1 ARG HA H 3.84 . 1 2 . 1 ARG HB2 H 1.58 . 2 3 . 1 ARG HB3 H 1 . 2 4 . 1 ARG HG2 H 1.75 . 2 5 . 1 ARG HG3 H 1.65 . 2 6 . 1 ARG HD2 H 2.58 . 2 7 . 1 ARG HD3 H 2.69 . 2 8 . 2 PRO HA H 4.28 . 1 9 . 2 PRO HB2 H 1.22 . 1 10 . 2 PRO HB3 H 2.04 . 1 11 . 2 PRO HG2 H 2.04 . 2 12 . 2 PRO HG3 H 2.16 . 2 13 . 2 PRO HD2 H 3.7 . 1 14 . 2 PRO HD3 H 3.7 . 1 15 . 3 TYR H H 7.42 . 1 16 . 3 TYR HA H 4.96 . 1 17 . 3 TYR HB2 H 2.71 . 1 18 . 3 TYR HB3 H 2.95 . 1 19 . 3 TYR HD1 H 6.91 . 1 20 . 3 TYR HD2 H 6.91 . 1 21 . 3 TYR HE1 H 6.81 . 1 22 . 3 TYR HE2 H 6.81 . 1 23 . 4 HIS H H 9.56 . 1 24 . 4 HIS HA H 4.47 . 1 25 . 4 HIS HB2 H 2.97 . 1 26 . 4 HIS HB3 H 3.26 . 1 27 . 4 HIS HD2 H 6.76 . 1 28 . 4 HIS HE1 H 7.91 . 1 29 . 5 CYS H H 8.34 . 1 30 . 5 CYS HA H 4.51 . 1 31 . 5 CYS HB2 H 2.71 . 1 32 . 5 CYS HB3 H 3.4 . 1 33 . 6 SER H H 9.04 . 1 34 . 6 SER HA H 4.32 . 1 35 . 6 SER HB2 H 3.3 . 1 36 . 6 SER HB3 H 3.51 . 1 37 . 7 TYR H H 9.83 . 1 38 . 7 TYR HA H 4.52 . 1 39 . 7 TYR HB2 H 1.56 . 1 40 . 7 TYR HB3 H 2.72 . 1 41 . 7 TYR HD1 H 6.88 . 1 42 . 7 TYR HD2 H 6.88 . 1 43 . 7 TYR HE1 H 6.74 . 1 44 . 7 TYR HE2 H 6.74 . 1 45 . 8 CYS H H 8.01 . 1 46 . 8 CYS HA H 4.93 . 1 47 . 8 CYS HB2 H 3.18 . 1 48 . 8 CYS HB3 H 3.28 . 1 49 . 9 ASN H H 8.23 . 1 50 . 9 ASN HA H 4.92 . 1 51 . 9 ASN HB2 H 2.9 . 1 52 . 9 ASN HB3 H 2.9 . 1 53 . 9 ASN HD21 H 7.64 . 1 54 . 9 ASN HD22 H 6.94 . 1 55 . 10 PHE H H 9.03 . 1 56 . 10 PHE HA H 4.3 . 1 57 . 10 PHE HB2 H 2.7 . 1 58 . 10 PHE HB3 H 2.41 . 1 59 . 10 PHE HD1 H 7.18 . 1 60 . 10 PHE HD2 H 7.18 . 1 61 . 10 PHE HE1 H 7.37 . 1 62 . 10 PHE HE2 H 7.37 . 1 63 . 10 PHE HZ H 7.31 . 1 64 . 11 SER H H 7.91 . 1 65 . 11 SER HA H 4.71 . 1 66 . 11 SER HB2 H 2.63 . 1 67 . 11 SER HB3 H 2.56 . 1 68 . 12 PHE H H 8.97 . 1 69 . 12 PHE HA H 4.92 . 1 70 . 12 PHE HB2 H 2.64 . 1 71 . 12 PHE HB3 H 3.57 . 1 72 . 12 PHE HD1 H 7.26 . 1 73 . 12 PHE HD2 H 7.26 . 1 74 . 12 PHE HE1 H 6.42 . 1 75 . 12 PHE HE2 H 6.42 . 1 76 . 12 PHE HZ H 6.66 . 1 77 . 13 LYS H H 9.75 . 1 78 . 13 LYS HA H 4.24 . 1 79 . 13 LYS HB2 H 2.05 . 1 80 . 13 LYS HB3 H 2.05 . 1 81 . 13 LYS HG2 H 1.48 . 1 82 . 13 LYS HG3 H 1.48 . 1 83 . 13 LYS HD2 H 1.74 . 1 84 . 13 LYS HD3 H 1.74 . 1 85 . 13 LYS HE2 H 2.97 . 1 86 . 13 LYS HE3 H 2.97 . 1 87 . 14 THR H H 7.31 . 1 88 . 14 THR HA H 4.79 . 1 89 . 14 THR HB H 4.38 . 1 90 . 14 THR HG2 H 1.16 . 1 91 . 15 LYS H H 8.52 . 1 92 . 15 LYS HA H 2.93 . 1 93 . 15 LYS HB2 H 1.16 . 1 94 . 15 LYS HB3 H 1.44 . 1 95 . 15 LYS HG2 H .97 . 1 96 . 15 LYS HG3 H .97 . 1 97 . 15 LYS HD2 H 1.08 . 1 98 . 15 LYS HD3 H 1.08 . 1 99 . 15 LYS HE2 H 2.84 . 1 100 . 15 LYS HE3 H 2.84 . 1 101 . 16 GLY H H 8.64 . 1 102 . 16 GLY HA2 H 3.64 . 2 103 . 16 GLY HA3 H 3.74 . 2 104 . 17 ASN H H 7.56 . 1 105 . 17 ASN HA H 4.53 . 1 106 . 17 ASN HB2 H 2.88 . 1 107 . 17 ASN HB3 H 2.7 . 1 108 . 17 ASN HD21 H 8.03 . 1 109 . 17 ASN HD22 H 7.2 . 1 110 . 18 LEU H H 7.08 . 1 111 . 18 LEU HA H 3.21 . 1 112 . 18 LEU HB2 H 1.17 . 1 113 . 18 LEU HB3 H 2.02 . 1 114 . 18 LEU HG H 1.56 . 1 115 . 18 LEU HD1 H 1.02 . 1 116 . 18 LEU HD2 H 1.05 . 1 117 . 19 THR H H 8.64 . 1 118 . 19 THR HA H 3.68 . 1 119 . 19 THR HB H 4.3 . 1 120 . 19 THR HG2 H 1.12 . 1 121 . 20 LYS H H 7.75 . 1 122 . 20 LYS HA H 3.8 . 1 123 . 20 LYS HB2 H 1.75 . 1 124 . 20 LYS HB3 H 1.75 . 1 125 . 20 LYS HG2 H 1.3 . 2 126 . 20 LYS HG3 H 1.58 . 2 127 . 20 LYS HD2 H 1.61 . 1 128 . 20 LYS HD3 H 1.61 . 1 129 . 20 LYS HE2 H 2.87 . 1 130 . 20 LYS HE3 H 2.87 . 1 131 . 21 HIS H H 7.37 . 1 132 . 21 HIS HA H 4.27 . 1 133 . 21 HIS HB2 H 3.28 . 1 134 . 21 HIS HB3 H 2.91 . 1 135 . 21 HIS HE1 H 7.33 . 1 136 . 22 MET H H 8.57 . 1 137 . 22 MET HA H 4.12 . 1 138 . 22 MET HB2 H 2.29 . 1 139 . 22 MET HB3 H 2.15 . 1 140 . 22 MET HG2 H 2.77 . 2 141 . 22 MET HG3 H 2.92 . 2 142 . 22 MET HE H 2.07 . 1 143 . 23 LYS H H 7.68 . 1 144 . 23 LYS HA H 4.24 . 1 145 . 23 LYS HB2 H 1.69 . 2 146 . 23 LYS HB3 H 1.9 . 2 147 . 23 LYS HG2 H 1.54 . 1 148 . 23 LYS HG3 H 1.54 . 1 149 . 23 LYS HD2 H 1.39 . 1 150 . 23 LYS HD3 H 1.39 . 1 151 . 23 LYS HE2 H 2.83 . 1 152 . 23 LYS HE3 H 2.83 . 1 153 . 24 SER H H 7.42 . 1 154 . 24 SER HA H 4.38 . 1 155 . 24 SER HB2 H 4.3 . 1 156 . 24 SER HB3 H 4.3 . 1 157 . 25 LYS H H 8.42 . 1 158 . 25 LYS HA H 4.13 . 1 159 . 25 LYS HB2 H 1.65 . 1 160 . 25 LYS HB3 H 1.65 . 1 161 . 25 LYS HG2 H 1.24 . 1 162 . 25 LYS HG3 H 1.24 . 1 163 . 25 LYS HD2 H 1.75 . 1 164 . 25 LYS HD3 H 1.75 . 1 165 . 25 LYS HE2 H 2.88 . 1 166 . 25 LYS HE3 H 2.88 . 1 167 . 26 ALA H H 7.79 . 1 168 . 26 ALA HA H 3.79 . 1 169 . 26 ALA HB H .74 . 1 170 . 27 HIS H H 7.63 . 1 171 . 27 HIS HA H 4.76 . 1 172 . 27 HIS HB2 H 2.77 . 2 173 . 27 HIS HB3 H 2.84 . 2 174 . 27 HIS HD2 H 6.49 . 1 175 . 27 HIS HE1 H 7.75 . 1 176 . 28 SER H H 7.87 . 1 177 . 28 SER HA H 4.29 . 1 178 . 28 SER HB2 H 3.75 . 1 179 . 28 SER HB3 H 3.75 . 1 180 . 29 LYS H H 8.42 . 1 181 . 29 LYS HA H 4.27 . 1 182 . 29 LYS HB2 H 1.69 . 2 183 . 29 LYS HB3 H 1.81 . 2 184 . 29 LYS HG2 H 1.37 . 1 185 . 29 LYS HG3 H 1.37 . 1 186 . 29 LYS HD2 H 1.8 . 1 187 . 29 LYS HD3 H 1.8 . 1 188 . 29 LYS HE2 H 2.91 . 1 189 . 29 LYS HE3 H 2.91 . 1 190 . 30 LYS H H 8.07 . 1 191 . 30 LYS HA H 4.06 . 1 192 . 30 LYS HB2 H 1.64 . 2 193 . 30 LYS HB3 H 1.74 . 2 194 . 30 LYS HG2 H 1.32 . 1 195 . 30 LYS HG3 H 1.32 . 1 196 . 30 LYS HD2 H 1.63 . 1 197 . 30 LYS HD3 H 1.63 . 1 198 . 30 LYS HE2 H 2.89 . 1 199 . 30 LYS HE3 H 2.89 . 1 stop_ save_