data_4423 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the N-terminal zinc finger of murine GATA-1 ; _BMRB_accession_number 4423 _BMRB_flat_file_name bmr4423.str _Entry_type original _Submission_date 1999-09-28 _Accession_date 1999-09-30 _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 Kowalski K. . . 2 Czolij R. . . 3 King G. F. . 4 Crossley M. . . 5 Mackay J. P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 263 "15N chemical shifts" 36 "coupling constants" 20 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-09 original author . stop_ _Original_release_date 2000-03-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Kowalski, K., Czolij, R., King, G. F., Crossley, M., and Mackay, J. P., "The Solution Structure of the N-terminal Zinc Finger of GATA-1 Reveals a Specific Binding Face for the Transcriptional Co-factor FOG," J. Biomol. NMR 13, 249-262 (1999). ; _Citation_title ; The Solution Structure of the N-terminal Zinc Finger of GATA-1 Reveals a Specific Binding Face for the Transcriptional Co-factor FO ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99229455 _PubMed_ID 10212985 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kowalski K. . . 2 Czolij R. . . 3 King G. F. . 4 Crossley M. . . 5 Mackay J. P. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 13 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 249 _Page_last 262 _Year 1999 _Details . loop_ _Keyword 'zinc finger' 'transcription regulation' stop_ save_ ################################## # Molecular system description # ################################## save_system_GATA-1 _Saveframe_category molecular_system _Mol_system_name 'GATA-1 N-terminal zinc finger' _Abbreviation_common GATA-1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label GATA-1 $GATA-1 ZN $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'fully reduced' loop_ _Biological_function ; DNA-binding domain (putative) protein-protein recognition motif ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GATA-1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common GATA-1 _Name_variant none _Abbreviation_common GATA-1 _Molecular_mass 5189 _Mol_thiol_state 'fully reduced' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 46 _Mol_residue_sequence ; GSEARECVNCGATATPLWRR DRTGHYLCNACGLYHKMNGQ NRPLIR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 198 GLY 2 199 SER 3 200 GLU 4 201 ALA 5 202 ARG 6 203 GLU 7 204 CYS 8 205 VAL 9 206 ASN 10 207 CYS 11 208 GLY 12 209 ALA 13 210 THR 14 211 ALA 15 212 THR 16 213 PRO 17 214 LEU 18 215 TRP 19 216 ARG 20 217 ARG 21 218 ASP 22 219 ARG 23 220 THR 24 221 GLY 25 222 HIS 26 223 TYR 27 224 LEU 28 225 CYS 29 226 ASN 30 227 ALA 31 228 CYS 32 229 GLY 33 230 LEU 34 231 TYR 35 232 HIS 36 233 LYS 37 234 MET 38 235 ASN 39 236 GLY 40 237 GLN 41 238 ASN 42 239 ARG 43 240 PRO 44 241 LEU 45 242 ILE 46 243 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-11 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 1GNF "Solution Structure Of The N-Terminal Zinc Finger Of Murine Gata-1, Nmr, 25 Structures" 97.83 46 100.00 100.00 1.08e-24 PDB 1Y0J "Zinc Fingers As Protein Recognition Motifs: Structural Basis For The Gata-1FRIEND OF GATA INTERACTION" 100.00 46 100.00 100.00 2.39e-25 PDB 2L6Y "Haddock Model Of Gata1nf:lmo2lim2-Ldb1lid" 84.78 39 100.00 100.00 4.77e-20 PDB 2L6Z "Haddock Model Of Gata1nf:lmo2lim2-Ldb1lid With Fog" 84.78 39 100.00 100.00 4.77e-20 DBJ BAG68610 "GATA-binding protein 1 [Cyprinus carpio]" 95.65 277 97.73 97.73 6.05e-23 DBJ BAK39708 "GATA binding protein 1 [Tursiops truncatus]" 60.87 140 100.00 100.00 2.07e-11 GB AFX60070 "GATA binding protein 1, partial [Mesocricetus auratus]" 69.57 212 100.00 100.00 1.63e-15 GB EAW50750 "GATA binding protein 1 (globin transcription factor 1), isoform CRA_b, partial [Homo sapiens]" 95.65 183 100.00 100.00 2.75e-24 REF XP_007507788 "PREDICTED: erythroid transcription factor-like [Monodelphis domestica]" 95.65 121 97.73 97.73 7.27e-23 REF XP_008156485 "PREDICTED: erythroid transcription factor [Eptesicus fuscus]" 95.65 250 100.00 100.00 5.07e-24 REF XP_008695477 "PREDICTED: LOW QUALITY PROTEIN: erythroid transcription factor [Ursus maritimus]" 95.65 351 100.00 100.00 5.56e-24 REF XP_009437329 "PREDICTED: erythroid transcription factor [Pan troglodytes]" 95.65 208 100.00 100.00 4.72e-24 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jul 15 12:44:35 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GATA-1 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 $GATA-1 'recombinant technology' 'Escherichia coli' Escherichia coli BL21(DE3) . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; TCEP: Tris(2-Carboxyethyl) Phosphine Tris (2-Carboxyethyl) Phosphine(TCEP) is used for the fast, quantitative and specific reduction of disulfide bonds and maintaining monothiols in a reduced state ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $GATA-1 4 mM . Tris 10 mM . TCEP 5 mM . ZnSO4 5 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $GATA-1 2 mM [U-15N] Tris 20 mM . TCEP 3 mM . ZnSO4 3 mM . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version . loop_ _Task '1D/2D data processing' stop_ _Details . save_ save_Aurelia _Saveframe_category software _Name Aurelia _Version . loop_ _Task '3D data processing' stop_ _Details . save_ save_DIANA _Saveframe_category software _Name DIANA _Version . loop_ _Task 'distance geometry' stop_ _Details . save_ save_X-Plor _Saveframe_category software _Name X-Plor _Version . loop_ _Task 'dynamical simulated-annealing' stop_ _Details . save_ save_MOLMOL _Saveframe_category software _Name MOLMOL _Version . loop_ _Task 'molecular visualisation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_DQFCOSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name DQFCOSY _Sample_label . save_ save_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_ECOSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name ECOSY _Sample_label . save_ save_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _Sample_label . save_ save_TOCSY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY-HSQC _Sample_label . save_ save_NOESY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-HSQC _Sample_label . save_ save_J-MODULATED_HMQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'J-MODULATED HMQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name DQFCOSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name ECOSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'J-MODULATED HMQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.4 0.01 n/a temperature 288 0.1 K pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation 'liquid annonium' N 15 nitrogen ppm 0.0 external indirect . . . . $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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chem_shift_ref _Mol_system_component_name GATA-1 _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 GLY HA2 H 3.91 0.02 2 2 . 1 GLY HA3 H 3.97 0.02 2 3 . 2 SER H H 8.78 0.02 1 4 . 2 SER HA H 4.50 0.02 1 5 . 2 SER HB2 H 3.89 0.02 1 6 . 2 SER HB3 H 3.89 0.02 1 7 . 2 SER N N 114.5 0.02 1 8 . 3 GLU H H 8.73 0.02 1 9 . 3 GLU HA H 4.28 0.02 1 10 . 3 GLU HB2 H 1.92 0.02 2 11 . 3 GLU HB3 H 2.03 0.02 2 12 . 3 GLU HG2 H 2.25 0.02 2 13 . 3 GLU HG3 H 2.30 0.02 2 14 . 3 GLU N N 121.6 0.02 1 15 . 4 ALA H H 8.36 0.02 1 16 . 4 ALA HA H 4.24 0.02 1 17 . 4 ALA HB H 1.32 0.02 1 18 . 4 ALA N N 124.7 0.02 1 19 . 5 ARG H H 8.12 0.02 1 20 . 5 ARG HA H 3.79 0.92 1 21 . 5 ARG HB2 H 0.52 0.02 2 22 . 5 ARG HB3 H 0.79 0.02 2 23 . 5 ARG HG2 H 0.07 0.02 2 24 . 5 ARG HG3 H 0.23 0.02 2 25 . 5 ARG HE H 6.55 0.02 1 26 . 5 ARG N N 120.9 0.02 1 27 . 6 GLU H H 7.34 0.02 1 28 . 6 GLU HA H 5.03 0.02 1 29 . 6 GLU HB2 H 1.78 0.02 1 30 . 6 GLU HB3 H 1.78 0.02 1 31 . 6 GLU HG2 H 2.06 0.02 1 32 . 6 GLU HG3 H 2.06 0.02 1 33 . 6 GLU N N 118.4 0.02 1 34 . 7 CYS H H 9.33 0.02 1 35 . 7 CYS HA H 4.66 0.02 1 36 . 7 CYS HB2 H 3.08 0.02 2 37 . 7 CYS HB3 H 3.63 0.02 2 38 . 7 CYS N N 123.6 0.02 1 39 . 8 VAL H H 9.39 0.02 1 40 . 8 VAL HA H 4.16 0.02 1 41 . 8 VAL HB H 2.38 0.02 1 42 . 8 VAL HG1 H 0.95 0.02 2 43 . 8 VAL HG2 H 1.15 0.02 2 44 . 8 VAL N N 128.5 0.02 1 45 . 9 ASN H H 8.88 0.02 1 46 . 9 ASN HA H 4.96 0.02 1 47 . 9 ASN HB2 H 2.64 0.02 2 48 . 9 ASN HB3 H 3.45 0.02 2 49 . 9 ASN HD21 H 7.47 0.02 2 50 . 9 ASN HD22 H 8.75 0.02 2 51 . 9 ASN N N 119.7 0.02 1 52 . 10 CYS H H 8.59 0.02 1 53 . 10 CYS HA H 5.08 0.02 1 54 . 10 CYS HB2 H 2.50 0.02 2 55 . 10 CYS HB3 H 3.34 0.02 2 56 . 10 CYS N N 115.3 0.02 1 57 . 11 GLY H H 8.22 0.02 1 58 . 11 GLY HA2 H 3.95 0.02 2 59 . 11 GLY HA3 H 4.35 0.02 2 60 . 11 GLY N N 111.6 0.02 1 61 . 12 ALA H H 9.21 0.02 1 62 . 12 ALA HA H 4.42 0.02 1 63 . 12 ALA HB H 1.60 0.02 1 64 . 12 ALA N N 124.2 0.02 1 65 . 13 THR H H 8.64 0.02 1 66 . 13 THR HA H 5.06 0.02 1 67 . 13 THR HG2 H 1.40 0.02 1 68 . 13 THR N N 106.1 0.02 1 69 . 14 ALA H H 7.72 0.02 1 70 . 14 ALA HB H 1.33 0.02 1 71 . 14 ALA N N 124.0 0.02 1 72 . 15 THR H H 7.80 0.02 1 73 . 15 THR HA H 4.70 0.02 1 74 . 15 THR HB H 3.82 0.02 1 75 . 15 THR HG2 H -0.83 0.02 1 76 . 16 PRO HA H 4.35 0.02 1 77 . 16 PRO HB2 H 1.78 0.02 2 78 . 16 PRO HB3 H 2.38 0.02 2 79 . 16 PRO HG2 H 1.89 0.02 1 80 . 16 PRO HG3 H 1.89 0.02 1 81 . 16 PRO HD2 H 3.72 0.02 2 82 . 16 PRO HD3 H 3.75 0.02 2 83 . 17 LEU H H 6.72 0.02 1 84 . 17 LEU HA H 4.40 0.02 1 85 . 17 LEU HB2 H 1.48 0.02 1 86 . 17 LEU HB3 H 1.48 0.02 1 87 . 17 LEU HG H 1.39 0.02 1 88 . 17 LEU HD1 H 0.83 0.02 2 89 . 17 LEU HD2 H 0.97 0.02 2 90 . 18 TRP H H 8.58 0.02 1 91 . 18 TRP HA H 4.75 0.02 1 92 . 18 TRP HB2 H 3.13 0.02 2 93 . 18 TRP HB3 H 3.25 0.02 2 94 . 18 TRP HD1 H 7.24 0.02 1 95 . 18 TRP HE1 H 10.15 0.02 1 96 . 18 TRP HE3 H 7.51 0.02 1 97 . 18 TRP HZ2 H 7.02 0.02 1 98 . 18 TRP HZ3 H 6.47 0.02 1 99 . 18 TRP HH2 H 7.05 0.02 1 100 . 18 TRP N N 123.2 0.02 1 101 . 19 ARG H H 9.31 0.02 1 102 . 19 ARG HA H 4.78 0.02 1 103 . 19 ARG HB2 H 1.69 0.02 2 104 . 19 ARG HB3 H 2.03 0.02 2 105 . 19 ARG HG2 H 1.57 0.02 1 106 . 19 ARG HG3 H 1.57 0.02 1 107 . 19 ARG HD2 H 3.10 0.02 2 108 . 19 ARG HD3 H 3.25 0.02 2 109 . 19 ARG HE H 7.68 0.02 1 110 . 20 ARG H H 8.51 0.02 1 111 . 20 ARG HA H 5.21 0.02 1 112 . 20 ARG HB2 H 1.58 0.02 2 113 . 20 ARG HB3 H 1.67 0.02 2 114 . 20 ARG HG2 H 1.26 0.02 2 115 . 20 ARG HG3 H 1.31 0.02 2 116 . 20 ARG HD2 H 2.83 0.02 2 117 . 20 ARG HD3 H 2.89 0.02 2 118 . 20 ARG HE H 6.56 0.02 1 119 . 20 ARG N N 118.3 0.02 1 120 . 21 ASP H H 8.68 0.02 1 121 . 21 ASP HA H 4.75 0.02 1 122 . 21 ASP HB2 H 2.53 0.02 2 123 . 21 ASP HB3 H 3.37 0.02 2 124 . 21 ASP N N 121.5 0.02 1 125 . 22 ARG H H 8.48 0.02 1 126 . 22 ARG HA H 4.22 0.02 1 127 . 22 ARG HB2 H 1.98 0.02 1 128 . 22 ARG HB3 H 1.98 0.02 1 129 . 22 ARG HG2 H 1.74 0.02 1 130 . 22 ARG HG3 H 1.74 0.02 1 131 . 22 ARG HD2 H 3.27 0.02 1 132 . 22 ARG HD3 H 3.27 0.02 1 133 . 22 ARG HE H 7.31 0.02 1 134 . 22 ARG N N 115.4 0.02 1 135 . 23 THR H H 8.16 0.02 1 136 . 23 THR HA H 4.50 0.02 1 137 . 23 THR HG2 H 1.19 0.02 1 138 . 23 THR N N 107.8 0.02 1 139 . 24 GLY H H 7.99 0.02 1 140 . 24 GLY HA2 H 3.46 0.02 2 141 . 24 GLY HA3 H 4.10 0.02 2 142 . 24 GLY N N 107.2 0.02 1 143 . 25 HIS H H 8.62 0.02 1 144 . 25 HIS HA H 4.58 0.02 1 145 . 25 HIS HB2 H 3.22 0.02 2 146 . 25 HIS HB3 H 3.35 0.02 2 147 . 25 HIS HD2 H 7.45 0.02 1 148 . 25 HIS HE1 H 8.56 0.02 1 149 . 25 HIS N N 118.6 0.02 1 150 . 26 TYR H H 8.93 0.02 1 151 . 26 TYR HA H 4.98 0.02 1 152 . 26 TYR HB2 H 2.76 0.02 2 153 . 26 TYR HB3 H 2.92 0.02 2 154 . 26 TYR HD1 H 7.10 0.02 1 155 . 26 TYR HD2 H 7.10 0.02 1 156 . 26 TYR HE1 H 6.62 0.02 1 157 . 26 TYR HE2 H 6.62 0.02 1 158 . 26 TYR N N 118.3 0.02 1 159 . 27 LEU H H 9.00 0.02 1 160 . 27 LEU HA H 5.96 0.02 1 161 . 27 LEU HB2 H 1.45 0.02 2 162 . 27 LEU HB3 H 1.58 0.02 2 163 . 27 LEU HG H 1.68 0.02 1 164 . 27 LEU HD1 H 0.86 0.02 2 165 . 27 LEU HD2 H 1.05 0.02 2 166 . 28 CYS H H 9.68 0.02 1 167 . 28 CYS HA H 4.38 0.02 1 168 . 28 CYS HB2 H 2.70 0.02 2 169 . 28 CYS HB3 H 3.03 0.02 2 170 . 28 CYS N N 118.8 0.02 1 171 . 29 ASN H H 8.14 0.02 1 172 . 29 ASN HA H 4.22 0.02 1 173 . 29 ASN HB2 H 2.66 0.02 2 174 . 29 ASN HB3 H 3.25 0.02 2 175 . 29 ASN HD21 H 7.08 0.02 2 176 . 29 ASN HD22 H 7.73 0.02 2 177 . 30 ALA H H 8.11 0.02 1 178 . 30 ALA HA H 4.15 0.02 1 179 . 30 ALA HB H 1.55 0.02 1 180 . 30 ALA N N 118.1 0.02 1 181 . 31 CYS H H 9.06 0.02 1 182 . 31 CYS HA H 4.07 0.02 1 183 . 31 CYS HB2 H 3.11 0.02 2 184 . 31 CYS HB3 H 3.27 0.02 2 185 . 31 CYS N N 120.3 0.02 1 186 . 32 GLY H H 9.26 0.02 1 187 . 32 GLY HA2 H 3.60 0.02 2 188 . 32 GLY HA3 H 4.00 0.02 2 189 . 32 GLY N N 107.8 0.02 1 190 . 33 LEU H H 8.53 0.02 1 191 . 33 LEU HA H 4.15 0.02 1 192 . 33 LEU HB2 H 1.47 0.02 2 193 . 33 LEU HB3 H 1.71 0.02 2 194 . 33 LEU HG H 1.61 0.02 1 195 . 33 LEU HD1 H 0.85 0.02 1 196 . 33 LEU HD2 H 0.85 0.02 1 197 . 34 TYR H H 7.80 0.02 1 198 . 34 TYR HA H 4.22 0.02 1 199 . 34 TYR HB2 H 3.14 0.02 1 200 . 34 TYR HB3 H 3.14 0.02 1 201 . 34 TYR HD1 H 7.20 0.02 1 202 . 34 TYR HD2 H 7.20 0.02 1 203 . 34 TYR HE1 H 6.72 0.02 1 204 . 34 TYR HE2 H 6.72 0.02 1 205 . 34 TYR N N 117.1 0.02 1 206 . 35 HIS H H 8.25 0.02 1 207 . 35 HIS HA H 4.63 0.02 1 208 . 35 HIS HB2 H 3.33 0.02 1 209 . 35 HIS HB3 H 3.33 0.02 1 210 . 35 HIS HD2 H 7.09 0.02 1 211 . 35 HIS HE1 H 8.52 0.02 1 212 . 35 HIS N N 117.2 0.02 1 213 . 36 LYS H H 8.26 0.02 1 214 . 36 LYS HA H 4.17 0.02 1 215 . 36 LYS HB2 H 1.96 0.02 1 216 . 36 LYS HB3 H 1.96 0.02 1 217 . 36 LYS HG2 H 1.44 0.02 2 218 . 36 LYS HG3 H 1.53 0.02 2 219 . 36 LYS HD2 H 1.73 0.02 1 220 . 36 LYS HD3 H 1.73 0.02 1 221 . 36 LYS HE2 H 3.03 0.02 1 222 . 36 LYS HE3 H 3.03 0.02 1 223 . 36 LYS N N 120.0 0.02 1 224 . 37 MET H H 8.15 0.02 1 225 . 37 MET HA H 4.38 0.02 1 226 . 37 MET HB2 H 1.98 0.02 2 227 . 37 MET HB3 H 2.04 0.02 2 228 . 37 MET HG2 H 2.56 0.02 2 229 . 37 MET HG3 H 2.63 0.02 2 230 . 37 MET HE H 2.06 0.02 1 231 . 37 MET N N 115.1 0.02 1 232 . 38 ASN H H 8.28 0.02 1 233 . 38 ASN HA H 4.76 0.02 1 234 . 38 ASN HB2 H 2.46 0.02 2 235 . 38 ASN HB3 H 2.68 0.02 2 236 . 38 ASN HD21 H 6.88 0.02 1 237 . 38 ASN HD22 H 6.88 0.02 1 238 . 38 ASN N N 114.0 0.02 1 239 . 39 GLY H H 8.43 0.02 1 240 . 39 GLY HA2 H 3.67 0.02 2 241 . 39 GLY HA3 H 3.96 0.02 2 242 . 39 GLY N N 107.8 0.02 1 243 . 40 GLN H H 7.51 0.02 1 244 . 40 GLN HA H 4.52 0.02 1 245 . 40 GLN HB2 H 1.92 0.02 2 246 . 40 GLN HB3 H 2.27 0.02 2 247 . 40 GLN HG2 H 2.37 0.02 1 248 . 40 GLN HG3 H 2.37 0.02 1 249 . 40 GLN HE21 H 6.93 0.02 2 250 . 40 GLN HE22 H 7.60 0.02 2 251 . 41 ASN H H 8.69 0.02 1 252 . 41 ASN HA H 4.85 0.02 1 253 . 41 ASN HB2 H 2.71 0.02 2 254 . 41 ASN HB3 H 2.79 0.02 2 255 . 41 ASN HD21 H 7.04 0.02 2 256 . 41 ASN HD22 H 7.77 0.02 2 257 . 41 ASN N N 116.8 0.02 1 258 . 42 ARG H H 8.79 0.02 1 259 . 42 ARG HB2 H 1.39 0.02 2 260 . 42 ARG HB3 H 1.79 0.02 2 261 . 42 ARG HG2 H 1.19 0.02 2 262 . 42 ARG HG3 H 1.48 0.02 2 263 . 42 ARG HD2 H 3.03 0.02 2 264 . 42 ARG HD3 H 3.28 0.02 2 265 . 42 ARG HE H 7.52 0.02 1 266 . 42 ARG N N 122.4 0.02 1 267 . 43 PRO HA H 4.39 0.02 1 268 . 43 PRO HB2 H 1.86 0.02 2 269 . 43 PRO HB3 H 2.26 0.02 2 270 . 43 PRO HG2 H 1.99 0.02 1 271 . 43 PRO HG3 H 1.99 0.02 1 272 . 43 PRO HD2 H 3.27 0.02 2 273 . 43 PRO HD3 H 3.74 0.02 2 274 . 44 LEU H H 8.41 0.02 1 275 . 44 LEU HA H 4.37 0.02 1 276 . 44 LEU HB2 H 1.53 0.02 2 277 . 44 LEU HB3 H 1.62 0.02 2 278 . 44 LEU HG H 1.65 0.02 1 279 . 44 LEU HD1 H 0.80 0.02 2 280 . 44 LEU HD2 H 0.91 0.02 2 281 . 44 LEU N N 121.2 0.02 1 282 . 45 ILE H H 8.16 0.02 1 283 . 45 ILE HA H 4.19 0.02 1 284 . 45 ILE HB H 1.88 0.02 1 285 . 45 ILE HG12 H 1.19 0.02 2 286 . 45 ILE HG13 H 1.47 0.02 2 287 . 45 ILE HG2 H 0.92 0.02 1 288 . 45 ILE HD1 H 0.85 0.02 1 289 . 45 ILE N N 121.3 0.02 1 290 . 46 ARG H H 8.08 0.02 1 291 . 46 ARG HA H 4.21 0.02 1 292 . 46 ARG HB2 H 1.72 0.02 2 293 . 46 ARG HB3 H 1.85 0.02 2 294 . 46 ARG HG2 H 1.58 0.02 1 295 . 46 ARG HG3 H 1.58 0.02 1 296 . 46 ARG HD2 H 3.19 0.02 1 297 . 46 ARG HD3 H 3.19 0.02 1 298 . 46 ARG HE H 7.24 0.02 1 299 . 46 ARG N N 129.3 0.02 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_set_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H . _Mol_system_component_name GATA-1 _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 4 ALA H 4 ALA HA 5.8 . . 0.1 2 3JHNHA 6 GLU H 6 GLU HA 9.8 . . 1.1 3 3JHNHA 7 CYS H 7 CYS HA 0.7 . . 8.9 4 3JHNHA 8 VAL H 8 VAL HA 1.3 . . 5.5 5 3JHNHA 9 ASN H 9 ASN HA 9.3 . . 0.1 6 3JHNHA 10 CYS H 10 CYS HA 8.8 . . 0.1 7 3JHNHA 12 ALA H 12 ALA HA 2.2 . . 2.5 8 3JHNHA 13 THR H 13 THR HA 9.7 . . 0.2 9 3JHNHA 14 ALA H 14 ALA HA 8.3 . . 0.6 10 3JHNHA 20 ARG H 20 ARG HA 8.1 . . 0.1 11 3JHNHA 22 ARG H 22 ARG HA 3.5 . . 0.1 12 3JHNHA 23 THR H 23 THR HA 8.9 . . 0.1 13 3JHNHA 28 CYS H 28 CYS HA 9.4 . . 1.8 14 3JHNHA 30 ALA H 30 ALA HA 4.6 . . 1.5 15 3JHNHA 31 CYS H 31 CYS HA 4.6 . . 1.2 16 3JHNHA 34 TYR H 34 TYR HA 4.8 . . 0.1 17 3JHNHA 35 HIS H 35 HIS HA 5.5 . . 0.1 18 3JHNHA 36 LYS H 36 LYS HA 4.8 . . 0.1 19 3JHNHA 40 GLN H 40 GLN HA 4.3 . . 0.6 20 3JHNHA 45 ILE H 45 ILE HA 8.4 . . 0.1 stop_ save_