data_4644 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structures of two CCHC zinc fingers from the FOG family protein U-shaped that mediate protein-protein interactions ; _BMRB_accession_number 4644 _BMRB_flat_file_name bmr4644.str _Entry_type original _Submission_date 2000-09-18 _Accession_date 2001-03-16 _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 Liew C. K. . 2 Kowalski K. . . 3 Fox A. H. . 4 Newton A. . . 5 Sharpe B. K. . 6 Crossley M. . . 7 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" 181 "15N chemical shifts" 32 "coupling constants" 28 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-05-09 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4939 'ninth zinc-finger domain of the u-shaped transcription factor' stop_ _Original_release_date 2001-05-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structures of two CCHC zinc fingers from the FOG family protein U-shaped that mediate protein-protein interactions ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11080638 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liew C. K. . 2 Kowalski K. . . 3 Fox A. H. . 4 Newton A. . . 5 Sharpe B. K. . 6 Crossley M. . . 7 Mackay J. P. . stop_ _Journal_abbreviation 'Structure Fold Des.' _Journal_volume 8 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1157 _Page_last 1166 _Year 2000 _Details . loop_ _Keyword 'ZINC FINGER' CCHC 'PROTEIN INTERACTION' stop_ save_ ################################## # Molecular system description # ################################## save_system_1FV5 _Saveframe_category molecular_system _Mol_system_name 'FIRST ZINC FINGER FROM THE DROSOPHILA U-SHAPED TRANSCRIPTION FACTOR' _Abbreviation_common 'FIRST ZINC FINGER FROM THE DROSOPHILA U-SHAPED TRANSCRIPTION FACTOR' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'FIRST ZINC FINGER OF U-SHAPED' $U-shaped_1st_finger 'ZINC ION' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_U-shaped_1st_finger _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'FIRST ZINC FINGER OF U-SHAPED' _Abbreviation_common 'FIRST ZINC FINGER OF U-SHAPED' _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 36 _Mol_residue_sequence ; GSLLKPARFMCLPCGIAFSS PSTLEAHQAYYCSHRI ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 LEU 4 LEU 5 LYS 6 PRO 7 ALA 8 ARG 9 PHE 10 MET 11 CYS 12 LEU 13 PRO 14 CYS 15 GLY 16 ILE 17 ALA 18 PHE 19 SER 20 SER 21 PRO 22 SER 23 THR 24 LEU 25 GLU 26 ALA 27 HIS 28 GLN 29 ALA 30 TYR 31 TYR 32 CYS 33 SER 34 HIS 35 ARG 36 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 1FV5 "Solution Structure Of The First Zinc Finger From The Drosophila U-Shaped Transcription Factor" 100.00 36 100.00 100.00 9.22e-17 PDB 1Y0J "Zinc Fingers As Protein Recognition Motifs: Structural Basis For The Gata-1FRIEND OF GATA INTERACTION" 100.00 36 100.00 100.00 9.22e-17 PDB 2L6Z "Haddock Model Of Gata1nf:lmo2lim2-Ldb1lid With Fog" 100.00 36 100.00 100.00 9.22e-17 EMBL CAA72991 "u-shaped [Drosophila melanogaster]" 94.44 1191 100.00 100.00 3.30e-14 GB AAF51488 "u-shaped, isoform A [Drosophila melanogaster]" 94.44 1191 100.00 100.00 3.34e-14 GB AAT94507 "LD12631p [Drosophila melanogaster]" 94.44 1191 100.00 100.00 3.34e-14 GB ACO56241 "SD10668p [Drosophila melanogaster]" 94.44 1198 100.00 100.00 3.34e-14 GB AGB92365 "u-shaped, isoform B [Drosophila melanogaster]" 94.44 1198 100.00 100.00 3.31e-14 GB AGB92366 "u-shaped, isoform C [Drosophila melanogaster]" 94.44 1212 100.00 100.00 3.63e-14 REF NP_001259828 "u-shaped, isoform B [Drosophila melanogaster]" 94.44 1198 100.00 100.00 3.31e-14 REF NP_001259829 "u-shaped, isoform C [Drosophila melanogaster]" 94.44 1212 100.00 100.00 3.63e-14 REF NP_001259830 "u-shaped, isoform D [Drosophila melanogaster]" 94.44 1175 100.00 100.00 3.45e-14 REF NP_001259831 "u-shaped, isoform E [Drosophila melanogaster]" 94.44 1198 100.00 100.00 3.31e-14 REF NP_476780 "u-shaped, isoform A [Drosophila melanogaster]" 94.44 1191 100.00 100.00 3.34e-14 SP Q9VPQ6 "RecName: Full=Zinc finger protein ush; AltName: Full=Protein U-shaped" 94.44 1191 100.00 100.00 3.34e-14 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 Thu Jun 2 09:48:05 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 $U-shaped_1st_finger 'Fruit fly' 7227 Eukaryota Metazoa Drosophila melanogaster 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 $U-shaped_1st_finger 'recombinant technology' 'E. coil' Escherichia coli . pGEX-2T 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 $U-shaped_1st_finger 0.7 mM . H2O 95 % . D2O 5 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $U-shaped_1st_finger 0.7 mM [U-15N] H2O 95 % . D2O 5 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.6 loop_ _Task collection stop_ _Details Guenther save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.2 loop_ _Task 'data analysis' stop_ _Details 'Bartels, Xia, Billeter, Guntert, Wuthrich' save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure solution' stop_ _Details 'Guntert, Mumenthaler, Wuthrich' save_ save_CNS _Saveframe_category software _Name CNS _Version 1.0 loop_ _Task refinement stop_ _Details 'Warren, Nilges, Kuszewski, Clore, Brunger' 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_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_HNHA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HNHB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 . pH temperature 298 . K pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_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_citation_label _Correction_value_citation_label . H 1 . ppm . . . . . . $entry_citation $entry_citation . N 15 . ppm . . . . . . $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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_ref_1 _Mol_system_component_name 'FIRST ZINC FINGER OF U-SHAPED' _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 . 2 SER H H 7.817 0.000 . 2 . 2 SER HA H 4.259 0.003 . 3 . 2 SER N N 110.212 . . 4 . 3 LEU H H 8.467 0.001 . 5 . 3 LEU HA H 4.383 0.005 . 6 . 3 LEU HG H 1.615 0.005 . 7 . 3 LEU HD1 H 0.937 0.009 1 8 . 3 LEU HD2 H 0.887 0.004 1 9 . 3 LEU N N 123.037 . . 10 . 4 LEU H H 8.243 0.001 . 11 . 4 LEU HA H 4.336 0.002 . 12 . 4 LEU HB2 H 1.630 0.003 . 13 . 4 LEU HB3 H 1.553 0.002 . 14 . 4 LEU HG H 1.584 0.000 . 15 . 4 LEU HD1 H 0.926 0.001 1 16 . 4 LEU HD2 H 0.869 0.001 1 17 . 4 LEU N N 121.954 . . 18 . 5 LYS H H 8.263 0.005 . 19 . 5 LYS HA H 4.607 0.004 . 20 . 5 LYS HB2 H 1.806 0.005 . 21 . 5 LYS HB3 H 1.693 0.012 . 22 . 5 LYS HG2 H 1.464 0.002 . 23 . 5 LYS HG3 H 1.400 0.008 . 24 . 5 LYS N N 122.010 . . 25 . 6 PRO HA H 4.354 0.004 . 26 . 6 PRO HB2 H 2.265 0.005 . 27 . 6 PRO HB3 H 1.832 0.006 . 28 . 6 PRO HD2 H 3.779 0.005 . 29 . 6 PRO HD3 H 3.618 0.005 . 30 . 7 ALA H H 8.288 0.001 . 31 . 7 ALA HA H 4.236 0.000 . 32 . 7 ALA HB H 1.304 0.002 1 33 . 7 ALA N N 123.120 . . 34 . 8 ARG H H 7.853 0.001 . 35 . 8 ARG HA H 4.229 0.009 . 36 . 8 ARG HB2 H 1.434 0.012 . 37 . 8 ARG HB3 H 1.395 0.013 . 38 . 8 ARG HG2 H 1.352 0.016 . 39 . 8 ARG HG3 H 1.271 0.008 . 40 . 8 ARG HE H 7.043 0.003 . 41 . 8 ARG N N 117.596 . . 42 . 9 PHE H H 8.507 0.000 . 43 . 9 PHE HA H 4.700 0.005 . 44 . 9 PHE HD1 H 7.350 0.001 1 45 . 9 PHE HD2 H 7.350 0.001 1 46 . 9 PHE HE1 H 7.160 0.002 1 47 . 9 PHE HE2 H 7.160 0.002 1 48 . 9 PHE N N 119.567 . . 49 . 10 MET H H 8.507 0.003 . 50 . 10 MET HA H 5.071 0.005 . 51 . 10 MET N N 120.511 . . 52 . 11 CYS H H 8.889 0.004 . 53 . 11 CYS HA H 4.700 0.005 . 54 . 11 CYS HB2 H 3.157 0.008 . 55 . 11 CYS HB3 H 2.828 0.007 . 56 . 11 CYS N N 123.953 . . 57 . 12 LEU H H 9.153 0.003 . 58 . 12 LEU HA H 4.228 0.005 . 59 . 12 LEU HB2 H 1.957 0.002 . 60 . 12 LEU HB3 H 1.580 0.004 . 61 . 12 LEU HG H 1.710 0.003 . 62 . 12 LEU HD1 H 0.993 0.002 1 63 . 12 LEU HD2 H 0.893 0.001 1 64 . 12 LEU N N 119.706 . . 65 . 13 PRO HA H 4.160 0.006 . 66 . 13 PRO HB2 H 1.953 0.004 . 67 . 13 PRO HB3 H 1.401 0.005 . 68 . 13 PRO HG2 H 2.037 0.006 . 69 . 13 PRO HG3 H 1.906 0.007 . 70 . 13 PRO HD2 H 4.901 0.005 . 71 . 13 PRO HD3 H 3.633 0.003 . 72 . 14 CYS H H 7.694 0.004 . 73 . 14 CYS HA H 4.432 0.005 . 74 . 14 CYS HB2 H 3.129 0.007 . 75 . 14 CYS HB3 H 2.925 0.009 . 76 . 14 CYS N N 128.200 . . 77 . 15 GLY H H 8.592 0.002 . 78 . 15 GLY HA2 H 3.977 0.009 . 79 . 15 GLY HA3 H 3.768 0.004 . 80 . 15 GLY N N 109.435 . . 81 . 16 ILE H H 7.046 0.006 . 82 . 16 ILE HA H 4.118 0.003 . 83 . 16 ILE HB H 1.267 0.007 . 84 . 16 ILE HG2 H 0.309 0.002 1 85 . 16 ILE HG12 H 1.357 0.006 . 86 . 16 ILE HD1 H 0.823 0.004 1 87 . 17 ALA H H 8.105 0.002 . 88 . 17 ALA HA H 4.819 0.005 . 89 . 17 ALA HB H 1.218 0.003 1 90 . 17 ALA N N 125.424 . . 91 . 18 PHE H H 8.671 0.004 . 92 . 18 PHE HA H 4.679 0.005 . 93 . 18 PHE HB2 H 3.594 0.007 . 94 . 18 PHE HB3 H 2.842 0.008 . 95 . 18 PHE HZ H 6.299 0.001 . 96 . 18 PHE HD1 H 7.264 0.002 1 97 . 18 PHE HD2 H 7.264 0.002 1 98 . 18 PHE HE1 H 6.907 0.002 1 99 . 18 PHE HE2 H 6.907 0.002 1 100 . 18 PHE N N 117.763 . . 101 . 19 SER H H 8.960 0.000 . 102 . 19 SER HA H 4.652 0.012 . 103 . 19 SER HB2 H 4.153 0.011 . 104 . 19 SER HB3 H 4.031 0.005 . 105 . 19 SER N N 112.211 . . 106 . 20 SER H H 7.629 0.002 . 107 . 20 SER HA H 4.628 0.005 . 108 . 20 SER HB2 H 4.120 0.002 . 109 . 20 SER HB3 H 3.878 0.006 . 110 . 20 SER N N 112.472 . . 111 . 21 PRO HA H 3.823 0.004 . 112 . 21 PRO HB2 H 2.130 0.003 . 113 . 21 PRO HB3 H 1.838 0.005 . 114 . 21 PRO HG2 H 1.949 0.004 . 115 . 21 PRO HG3 H 1.595 0.004 . 116 . 21 PRO HD2 H 3.648 0.007 . 117 . 21 PRO HD3 H 2.765 0.002 . 118 . 22 SER HA H 4.263 0.001 . 119 . 22 SER N N 112.970 . . 120 . 23 THR H H 7.658 0.005 . 121 . 23 THR HA H 4.172 0.002 . 122 . 23 THR HB H 4.402 0.003 . 123 . 23 THR HG2 H 1.361 0.005 1 124 . 23 THR N N 114.846 . 5 125 . 24 LEU H H 7.380 0.002 . 126 . 24 LEU HA H 3.303 0.004 . 127 . 24 LEU HB2 H 1.910 0.007 . 128 . 24 LEU HB3 H 1.331 0.005 . 129 . 24 LEU HG H 1.404 0.006 . 130 . 24 LEU HD1 H 1.012 0.003 1 131 . 24 LEU HD2 H 0.900 0.005 1 132 . 24 LEU N N 123.437 . . 133 . 25 GLU H H 8.339 0.003 . 134 . 25 GLU HA H 4.033 0.005 . 135 . 25 GLU HB2 H 2.083 0.006 . 136 . 25 GLU HB3 H 2.025 0.007 . 137 . 25 GLU HG2 H 2.366 0.001 . 138 . 25 GLU HG3 H 2.210 0.006 . 139 . 25 GLU N N 118.012 . . 140 . 26 ALA H H 7.767 0.002 . 141 . 26 ALA HA H 4.191 0.001 . 142 . 26 ALA HB H 1.647 0.004 1 143 . 26 ALA N N 119.639 . . 144 . 27 HIS H H 7.654 0.003 . 145 . 27 HIS HA H 4.439 0.008 . 146 . 27 HIS HB2 H 3.288 0.006 . 147 . 27 HIS HB3 H 2.870 0.006 . 148 . 27 HIS HD2 H 6.878 0.002 . 149 . 27 HIS HE1 H 8.319 0.001 . 150 . 27 HIS N N 114.846 . 5 151 . 28 GLN H H 8.615 0.004 . 152 . 28 GLN HA H 3.718 0.005 . 153 . 28 GLN HB2 H 2.243 0.004 . 154 . 28 GLN HB3 H 1.988 0.005 . 155 . 28 GLN HG2 H 2.788 0.004 . 156 . 28 GLN HG3 H 2.661 0.003 . 157 . 28 GLN HE21 H 8.107 0.003 . 158 . 28 GLN HE22 H 7.048 0.001 . 159 . 28 GLN N N 115.903 . . 160 . 28 GLN NE2 N 111.296 . . 161 . 29 ALA H H 7.907 0.001 . 162 . 29 ALA HA H 3.957 0.003 . 163 . 29 ALA HB H 0.777 0.004 1 164 . 29 ALA N N 117.263 . . 165 . 30 TYR H H 7.432 0.001 . 166 . 30 TYR HA H 4.641 0.001 . 167 . 30 TYR HB3 H 2.441 0.004 . 168 . 30 TYR HB2 H 1.953 0.004 . 169 . 30 TYR HD1 H 7.013 0.004 1 170 . 30 TYR HD2 H 7.013 0.004 1 171 . 30 TYR HE1 H 6.777 0.002 1 172 . 30 TYR HE2 H 6.777 0.002 1 173 . 30 TYR N N 109.375 . . 174 . 31 TYR H H 7.693 0.002 . 175 . 31 TYR HA H 4.920 0.002 . 176 . 31 TYR HB3 H 3.489 0.005 . 177 . 31 TYR HB2 H 2.736 0.005 . 178 . 31 TYR HD1 H 7.240 0.003 1 179 . 31 TYR HD2 H 7.240 0.003 1 180 . 31 TYR HE1 H 6.866 0.002 1 181 . 31 TYR HE2 H 6.866 0.002 1 182 . 31 TYR N N 113.806 . . 183 . 32 CYS H H 7.755 0.005 . 184 . 32 CYS HA H 3.750 0.009 . 185 . 32 CYS HB2 H 2.558 0.007 . 186 . 32 CYS HB3 H 1.973 0.015 . 187 . 32 CYS N N 121.402 . . 188 . 33 SER H H 8.761 0.005 . 189 . 33 SER HA H 4.326 0.004 . 190 . 33 SER N N 123.870 . . 191 . 34 HIS H H 8.820 0.004 . 192 . 34 HIS HA H 4.680 0.005 . 193 . 34 HIS HB2 H 3.402 0.006 . 194 . 34 HIS HB3 H 2.979 0.005 . 195 . 34 HIS HD2 H 7.013 0.000 . 196 . 34 HIS HE1 H 7.439 0.000 . 197 . 34 HIS N N 120.011 . . 198 . 35 ARG H H 7.576 0.006 . 199 . 35 ARG HA H 4.356 0.004 . 200 . 35 ARG HB2 H 1.845 0.005 . 201 . 35 ARG HB3 H 1.768 0.007 . 202 . 35 ARG HG2 H 1.672 0.006 . 203 . 35 ARG HG3 H 1.551 0.005 . 204 . 35 ARG HE H 7.118 0.000 . 205 . 35 ARG N N 119.865 . . 206 . 36 ILE H H 7.776 0.002 . 207 . 36 ILE HA H 4.082 0.006 . 208 . 36 ILE HB H 1.824 0.008 . 209 . 36 ILE HG2 H 0.899 0.003 . 210 . 36 ILE HG12 H 1.428 0.003 . 211 . 36 ILE HG13 H 1.153 0.003 . 212 . 36 ILE HD1 H 0.856 0.000 . 213 . 36 ILE N N 124.369 . . stop_ save_ ######################## # Coupling constants # ######################## save_JHNHA _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name 'FIRST ZINC FINGER OF U-SHAPED' _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 2 SER H 2 SER HA 5.1 . . . 2 3JHNHA 3 LEU H 3 LEU HA 7.3 . . . 3 3JHNHA 7 ALA H 7 ALA HA 6.4 . . . 4 3JHNHA 8 ARG H 8 ARG HA 8.3 . . . 5 3JHNHA 9 PHE H 9 PHE HA 9.4 . . . 6 3JHNHA 10 MET H 10 MET HA 8.1 . . . 7 3JHNHA 11 CYS H 11 CYS HA 9.8 . . . 8 3JHNHA 12 LEU H 12 LEU HA 5.3 . . . 9 3JHNHA 14 CYS H 14 CYS HA 8.8 . . . 10 3JHNHA 16 ILE H 16 ILE HA 5.5 . . . 11 3JHNHA 17 ALA H 17 ALA HA 9.7 . . . 12 3JHNHA 18 PHE H 18 PHE HA 10.5 . . . 13 3JHNHA 19 SER H 19 SER HA 5.4 . . . 14 3JHNHA 20 SER H 20 SER HA 7.9 . . . 15 3JHNHA 23 THR H 23 THR HA 6.0 . . . 16 3JHNHA 24 LEU H 24 LEU HA 4.3 . . . 17 3JHNHA 25 GLU H 25 GLU HA 3.7 . . . 18 3JHNHA 26 ALA H 26 ALA HA 4.6 . . . 19 3JHNHA 27 HIS H 27 HIS HA 4.0 . . . 20 3JHNHA 28 GLN H 28 GLN HA 4.5 . . . 21 3JHNHA 29 ALA H 29 ALA HA 5.9 . . . 22 3JHNHA 30 TYR H 30 TYR HA 10.3 . . . 23 3JHNHA 31 TYR H 31 TYR HA 11.1 . . . 24 3JHNHA 32 CYS H 32 CYS HA 4.0 . . . 25 3JHNHA 33 SER H 33 SER HA 4.6 . . . 26 3JHNHA 34 HIS H 34 HIS HA 9.4 . . . 27 3JHNHA 35 ARG H 35 ARG HA 6.9 . . . 28 3JHNHA 36 ILE H 36 ILE HA 8.6 . . . stop_ save_