data_4347 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H Chemical Shift Assignments and Interproton 3JHNHA Coupling Constants of Alpha2-D, a Nativelike de Novo Designed Four Helix Bundle ; _BMRB_accession_number 4347 _BMRB_flat_file_name bmr4347.str _Entry_type original _Submission_date 1999-05-12 _Accession_date 1999-05-12 _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 Hill R. Blake . 2 DeGrado William F. . 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" 242 "coupling constants" 27 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB 'Updating non-standard residue' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Hill, R. Blake and Degrado, William, F., "Solution Structure of Alpha2D, a Nativelike de Novo Designed Protein," J. Am. Chem. Soc. 120, 1138-1145 (1998). ; _Citation_title 'Solution Structure of Alpha2D, a Nativelike de Novo Designed Protein' _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 Hill R. Blake . 2 DeGrado William F. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 120 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1138 _Page_last 1145 _Year 1998 _Details . loop_ _Keyword 'bisecting U' 'de novo protein design' 'four helix bundle' NMR 'nuclear magnetic resonance' 'protein folding' 'protein structure' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_1 _Saveframe_category citation _Citation_full 'Kraulis, P.J. J. Magn. Res. 84:627-633(1989)' _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_alpha-2D _Saveframe_category molecular_system _Mol_system_name Alpha2D _Abbreviation_common A2D _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'A2D subunit A' $A2D_monomer 'A2D subunit B' $A2D_monomer stop_ _System_molecular_weight 8578 _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'A2D subunit A' 1 'A2D subunit B' stop_ loop_ _Biological_function 'de novo designed protein with nativelike behavior' stop_ _Database_query_date . _Details ; Helix-loop-helix that dimerizes to form a 4-helix bundle. Symmetric homodimer. ; save_ ######################## # Monomeric polymers # ######################## save_A2D_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Alpha2D _Abbreviation_common A2D _Molecular_mass 4289.1 _Mol_thiol_state . _Details ; The monomer molecular weight is 4289. Molecule has been shown to be dimeric by equilibrium sedimentation analysis at 50 uM - 2 mM. A helix-loop-helix with each helix comprising 2 heptads of the helical repeat. High sequence redundancy between helix 1 and helix 2. N-terminal is acetylated and C-terminal is amidated." ; ############################## # Polymer residue sequence # ############################## _Residue_count 37 _Mol_residue_sequence ; XGEVEELEKKFKELWKGPRR GEIEELHKKFHELIKGX ; loop_ _Residue_seq_code _Residue_label 1 ACE 2 GLY 3 GLU 4 VAL 5 GLU 6 GLU 7 LEU 8 GLU 9 LYS 10 LYS 11 PHE 12 LYS 13 GLU 14 LEU 15 TRP 16 LYS 17 GLY 18 PRO 19 ARG 20 ARG 21 GLY 22 GLU 23 ILE 24 GLU 25 GLU 26 LEU 27 HIS 28 LYS 29 LYS 30 PHE 31 HIS 32 GLU 33 LEU 34 ILE 35 LYS 36 GLY 37 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-03-16 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 1QP6 "Solution Structure Of Alpha2d" 94.59 35 100.00 100.00 7.12e-13 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_ACE _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'ACETYL GROUP' _BMRB_code . _PDB_code ACE _Standard_residue_derivative . _Molecular_mass 44.053 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 14 16:15:33 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? O O O . 0 . ? CH3 CH3 C . 0 . ? H H H . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? H3 H3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C O ? ? SING C CH3 ? ? SING C H ? ? SING CH3 H1 ? ? SING CH3 H2 ? ? SING CH3 H3 ? ? stop_ save_ save_chem_comp_NH2 _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'AMINO GROUP' _BMRB_code . _PDB_code NH2 _Standard_residue_derivative . _Molecular_mass 16.023 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 14 16:09:34 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N HN1 ? ? SING N HN2 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $A2D_monomer . . . . . . 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 _Details $A2D_monomer 'chemically synthesized' . . . . . 'Synthesized using standard FMOC chemistry, C-terminal is amidated and the N-terminus is acetylated' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $A2D_monomer 2.0 mM . Tris 50 mM [U-2H] H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_AZARA _Saveframe_category software _Name AZARA _Version . loop_ _Task 'process data' stop_ _Details . save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version 3.3 loop_ _Vendor _Address _Electronic_address 'Per Kraulis' . http://www.scs.uiuc.edu/documentation/ansig/ansig.html#references stop_ loop_ _Task 'assignments and integration' stop_ _Details . _Citation_label $citation_1 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600.13 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label $sample_one save_ save_1H-1H_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H DQF-COSY' _Sample_label $sample_one save_ save_1H-1H_E-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H E-COSY' _Sample_label $sample_one save_ save_1H-1H_100ms_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H 100ms NOESY' _Sample_label $sample_one save_ save_1H-1H_200ms_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H 200ms NOESY' _Sample_label $sample_one save_ save_1H-13C_HMQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HMQC' _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' .052 .002 M pH 7.3 0.1 na temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 TSP H 1 'methyl protons' ppm 0.0 internal direct . . . 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'A2D subunit A' _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 GLY H H 8.47 0.02 1 2 . 2 GLY HA2 H 4.00 0.02 1 3 . 2 GLY HA3 H 4.00 0.02 1 4 . 3 GLU H H 8.24 0.02 1 5 . 3 GLU HA H 4.03 0.02 1 6 . 4 VAL H H 8.12 0.02 1 7 . 4 VAL HA H 3.45 0.02 1 8 . 4 VAL HB H 2.04 0.02 1 9 . 4 VAL HG1 H 0.87 0.02 1 10 . 4 VAL HG2 H 0.87 0.02 1 11 . 5 GLU H H 8.05 0.02 1 12 . 5 GLU HA H 4.10 0.02 1 13 . 5 GLU HB2 H 1.98 0.02 1 14 . 5 GLU HB3 H 2.01 0.02 1 15 . 5 GLU HG2 H 2.29 0.02 1 16 . 5 GLU HG3 H 2.29 0.02 1 17 . 6 GLU H H 8.04 0.02 1 18 . 6 GLU HA H 4.03 0.02 1 19 . 6 GLU HB2 H 2.04 0.02 1 20 . 6 GLU HB3 H 2.04 0.02 1 21 . 6 GLU HG2 H 2.24 0.02 1 22 . 6 GLU HG3 H 2.24 0.02 1 23 . 7 LEU H H 7.65 0.02 1 24 . 7 LEU HA H 4.07 0.02 1 25 . 7 LEU HB2 H 1.72 0.02 1 26 . 7 LEU HB3 H 1.72 0.02 1 27 . 7 LEU HG H 1.72 0.02 1 28 . 7 LEU HD1 H 0.76 0.02 1 29 . 7 LEU HD2 H 0.86 0.02 1 30 . 8 GLU H H 8.34 0.02 1 31 . 8 GLU HA H 3.97 0.02 1 32 . 8 GLU HB2 H 2.33 0.02 1 33 . 8 GLU HB3 H 2.12 0.02 1 34 . 8 GLU HG2 H 2.23 0.02 1 35 . 8 GLU HG3 H 2.23 0.02 1 36 . 9 LYS H H 8.02 0.02 1 37 . 9 LYS HA H 3.98 0.02 1 38 . 9 LYS HB2 H 1.93 0.02 1 39 . 9 LYS HB3 H 1.93 0.02 1 40 . 9 LYS HG2 H 1.40 0.02 1 41 . 9 LYS HG3 H 1.63 0.02 1 42 . 9 LYS HD2 H 1.67 0.02 1 43 . 9 LYS HD3 H 1.67 0.02 1 44 . 9 LYS HE2 H 2.92 0.02 1 45 . 9 LYS HE3 H 2.92 0.02 1 46 . 10 LYS H H 8.11 0.02 1 47 . 10 LYS HA H 4.16 0.02 1 48 . 10 LYS HB2 H 1.89 0.02 1 49 . 10 LYS HB3 H 1.96 0.02 1 50 . 10 LYS HG2 H 1.54 0.02 1 51 . 10 LYS HG3 H 1.54 0.02 1 52 . 10 LYS HD2 H 1.68 0.02 1 53 . 10 LYS HD3 H 1.68 0.02 1 54 . 10 LYS HE2 H 2.86 0.02 1 55 . 10 LYS HE3 H 2.95 0.02 1 56 . 11 PHE H H 8.72 0.02 1 57 . 11 PHE HA H 3.80 0.02 1 58 . 11 PHE HB2 H 2.93 0.02 1 59 . 11 PHE HB3 H 2.93 0.02 1 60 . 11 PHE HD1 H 6.52 0.02 1 61 . 11 PHE HD2 H 6.52 0.02 1 62 . 11 PHE HE1 H 6.59 0.02 1 63 . 11 PHE HE2 H 6.59 0.02 1 64 . 11 PHE HZ H 6.64 0.02 1 65 . 12 LYS H H 8.13 0.02 1 66 . 12 LYS HA H 3.98 0.02 1 67 . 12 LYS HB2 H 1.89 0.02 1 68 . 12 LYS HB3 H 2.04 0.02 1 69 . 12 LYS HG2 H 0.87 0.02 1 70 . 12 LYS HG3 H 0.87 0.02 1 71 . 12 LYS HD2 H 1.49 0.02 1 72 . 12 LYS HD3 H 1.49 0.02 1 73 . 12 LYS HE2 H 2.28 0.02 1 74 . 12 LYS HE3 H 2.28 0.02 1 75 . 13 GLU H H 8.18 0.02 1 76 . 13 GLU HA H 4.01 0.02 1 77 . 13 GLU HB2 H 2.20 0.02 1 78 . 13 GLU HB3 H 2.11 0.02 1 79 . 13 GLU HG2 H 2.36 0.02 1 80 . 13 GLU HG3 H 2.36 0.02 1 81 . 14 LEU H H 7.65 0.02 1 82 . 14 LEU HA H 4.07 0.02 1 83 . 14 LEU HB2 H 1.72 0.02 1 84 . 14 LEU HB3 H 1.72 0.02 1 85 . 14 LEU HG H 1.72 0.02 1 86 . 14 LEU HD1 H 0.76 0.02 1 87 . 14 LEU HD2 H 0.86 0.02 1 88 . 15 TRP H H 8.48 0.02 1 89 . 15 TRP HA H 3.82 0.02 1 90 . 15 TRP HB2 H 3.37 0.02 1 91 . 15 TRP HB3 H 3.07 0.02 1 92 . 15 TRP HD1 H 6.95 0.02 1 93 . 15 TRP HE1 H 11.18 0.02 1 94 . 15 TRP HE3 H 7.34 0.02 1 95 . 15 TRP HZ2 H 7.34 0.02 1 96 . 15 TRP HZ3 H 6.95 0.02 1 97 . 15 TRP HH2 H 7.03 0.02 1 98 . 16 LYS H H 7.28 0.02 1 99 . 16 LYS HA H 3.78 0.02 1 100 . 16 LYS HB2 H 1.88 0.02 1 101 . 16 LYS HB3 H 1.84 0.02 1 102 . 16 LYS HG2 H 1.50 0.02 1 103 . 16 LYS HG3 H 1.50 0.02 1 104 . 16 LYS HD2 H 1.68 0.02 1 105 . 16 LYS HD3 H 1.72 0.02 1 106 . 16 LYS HE2 H 2.96 0.02 1 107 . 16 LYS HE3 H 2.96 0.02 1 108 . 17 GLY H H 6.99 0.02 1 109 . 17 GLY HA2 H 4.04 0.02 1 110 . 17 GLY HA3 H 4.36 0.02 1 111 . 18 PRO HA H 4.37 0.02 1 112 . 18 PRO HB2 H 1.93 0.02 1 113 . 18 PRO HB3 H 2.34 0.02 1 114 . 18 PRO HG2 H 1.92 0.02 1 115 . 18 PRO HG3 H 2.01 0.02 1 116 . 18 PRO HD2 H 3.57 0.02 1 117 . 18 PRO HD3 H 3.68 0.02 1 118 . 19 ARG H H 9.01 0.02 1 119 . 19 ARG HA H 4.65 0.02 1 120 . 19 ARG HB2 H 1.65 0.02 1 121 . 19 ARG HB3 H 1.65 0.02 1 122 . 19 ARG HG2 H 1.57 0.02 1 123 . 19 ARG HG3 H 2.04 0.02 1 124 . 19 ARG HD2 H 1.49 0.02 1 125 . 19 ARG HD3 H 3.07 0.02 1 126 . 20 ARG H H 7.44 0.02 1 127 . 20 ARG HA H 3.65 0.02 1 128 . 20 ARG HB2 H 2.05 0.02 1 129 . 20 ARG HB3 H 1.40 0.02 1 130 . 20 ARG HG2 H 1.01 0.02 1 131 . 20 ARG HG3 H 1.10 0.02 1 132 . 20 ARG HD2 H 2.66 0.02 1 133 . 20 ARG HD3 H 2.69 0.02 1 134 . 21 GLY H H 8.83 0.02 1 135 . 21 GLY HA2 H 3.79 0.02 1 136 . 21 GLY HA3 H 3.87 0.02 1 137 . 22 GLU H H 7.82 0.02 1 138 . 22 GLU HA H 4.09 0.02 1 139 . 22 GLU HB2 H 2.09 0.02 1 140 . 22 GLU HB3 H 2.19 0.02 1 141 . 22 GLU HG2 H 2.28 0.02 1 142 . 22 GLU HG3 H 2.28 0.02 1 143 . 23 ILE H H 8.06 0.02 1 144 . 23 ILE HA H 3.79 0.02 1 145 . 23 ILE HB H 2.29 0.02 1 146 . 23 ILE HG12 H 0.91 0.02 1 147 . 23 ILE HG13 H 1.45 0.02 1 148 . 23 ILE HG2 H 0.47 0.02 1 149 . 23 ILE HD1 H 0.44 0.02 1 150 . 24 GLU H H 8.69 0.02 1 151 . 24 GLU HA H 3.97 0.02 1 152 . 24 GLU HB2 H 2.14 0.02 1 153 . 24 GLU HB3 H 2.25 0.02 1 154 . 24 GLU HG2 H 2.87 0.02 1 155 . 24 GLU HG3 H 2.24 0.02 1 156 . 25 GLU H H 7.87 0.02 1 157 . 25 GLU HA H 4.10 0.02 1 158 . 25 GLU HB2 H 2.04 0.02 1 159 . 25 GLU HB3 H 2.08 0.02 1 160 . 25 GLU HG2 H 2.30 0.02 1 161 . 25 GLU HG3 H 2.30 0.02 1 162 . 26 LEU H H 7.85 0.02 1 163 . 26 LEU HA H 3.86 0.02 1 164 . 26 LEU HB2 H 1.74 0.02 1 165 . 26 LEU HB3 H 1.60 0.02 1 166 . 26 LEU HG H 1.16 0.02 1 167 . 26 LEU HD1 H 0.68 0.02 1 168 . 26 LEU HD2 H 0.70 0.02 1 169 . 27 HIS H H 8.58 0.02 1 170 . 27 HIS HA H 4.09 0.02 1 171 . 27 HIS HB2 H 3.36 0.02 1 172 . 27 HIS HB3 H 3.04 0.02 1 173 . 27 HIS HD2 H 6.76 0.02 1 174 . 27 HIS HE1 H 7.00 0.02 1 175 . 28 LYS H H 7.82 0.02 1 176 . 28 LYS HA H 4.01 0.02 1 177 . 28 LYS HB2 H 2.00 0.02 1 178 . 28 LYS HB3 H 2.00 0.02 1 179 . 28 LYS HG2 H 1.46 0.02 1 180 . 28 LYS HG3 H 1.46 0.02 1 181 . 28 LYS HD2 H 1.71 0.02 1 182 . 28 LYS HD3 H 1.71 0.02 1 183 . 28 LYS HE2 H 2.93 0.02 1 184 . 28 LYS HE3 H 2.93 0.02 1 185 . 29 LYS H H 7.91 0.02 1 186 . 29 LYS HA H 3.99 0.02 1 187 . 29 LYS HB2 H 1.74 0.02 1 188 . 29 LYS HB3 H 1.85 0.02 1 189 . 29 LYS HG2 H 1.26 0.02 1 190 . 29 LYS HG3 H 1.26 0.02 1 191 . 29 LYS HD2 H 1.52 0.02 1 192 . 29 LYS HD3 H 1.52 0.02 1 193 . 29 LYS HE2 H 2.81 0.02 1 194 . 29 LYS HE3 H 2.81 0.02 1 195 . 30 PHE H H 8.42 0.02 1 196 . 30 PHE HA H 4.07 0.02 1 197 . 30 PHE HB2 H 2.52 0.02 1 198 . 30 PHE HB3 H 2.88 0.02 1 199 . 30 PHE HD1 H 6.59 0.02 1 200 . 30 PHE HD2 H 6.59 0.02 1 201 . 30 PHE HE1 H 6.74 0.02 1 202 . 30 PHE HE2 H 6.74 0.02 1 203 . 30 PHE HZ H 6.93 0.02 1 204 . 31 HIS H H 8.27 0.02 1 205 . 31 HIS HA H 3.75 0.02 1 206 . 31 HIS HB2 H 3.33 0.02 1 207 . 31 HIS HB3 H 2.98 0.02 1 208 . 31 HIS HD2 H 6.87 0.02 1 209 . 31 HIS HE1 H 7.51 0.02 1 210 . 32 GLU H H 7.40 0.02 1 211 . 32 GLU HA H 3.78 0.02 1 212 . 32 GLU HB2 H 2.00 0.02 1 213 . 32 GLU HB3 H 2.00 0.02 1 214 . 32 GLU HG2 H 2.26 0.02 1 215 . 32 GLU HG3 H 2.33 0.02 1 216 . 33 LEU H H 7.29 0.02 1 217 . 33 LEU HA H 3.85 0.02 1 218 . 33 LEU HB2 H 1.40 0.02 1 219 . 33 LEU HB3 H 1.35 0.02 1 220 . 33 LEU HG H 0.87 0.02 1 221 . 33 LEU HD1 H 0.54 0.02 1 222 . 33 LEU HD2 H 0.61 0.02 1 223 . 34 ILE H H 7.48 0.02 1 224 . 34 ILE HA H 3.51 0.02 1 225 . 34 ILE HB H 1.40 0.02 1 226 . 34 ILE HG12 H 0.60 0.02 1 227 . 34 ILE HG13 H 0.89 0.02 1 228 . 34 ILE HG2 H 0.37 0.02 1 229 . 34 ILE HD1 H 0.24 0.02 1 230 . 35 LYS H H 7.71 0.02 1 231 . 35 LYS HA H 3.99 0.02 1 232 . 35 LYS HB2 H 1.59 0.02 1 233 . 35 LYS HB3 H 1.59 0.02 1 234 . 35 LYS HG2 H 1.20 0.02 1 235 . 35 LYS HG3 H 1.20 0.02 1 236 . 35 LYS HD2 H 1.45 0.02 1 237 . 35 LYS HD3 H 1.45 0.02 1 238 . 35 LYS HE2 H 2.76 0.02 1 239 . 35 LYS HE3 H 2.76 0.02 1 240 . 36 GLY H H 7.68 0.02 1 241 . 36 GLY HA2 H 3.85 0.02 1 242 . 36 GLY HA3 H 3.85 0.02 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constant _Saveframe_category coupling_constants _Details ; 3JHNHA coupling constants were measured at two transforms, one phased in pure absorption and the other in pure dispersion, of the DQF-COSY spectrum. From these values the real coupling constants were calculated according to Kim, Y. and Prestegard, J.H. (1989) J. Magn. Reson. 84, 9-13 ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Spectrometer_frequency_1H . _Mol_system_component_name 'A2D subunit A' _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 3 GLU H 3 GLU HA 11.0 . . 1.0 2 3JHNHA 4 VAL H 4 VAL HA 3.0 . . 1.0 3 3JHNHA 5 GLU H 5 GLU HA 6.0 . . 1.0 4 3JHNHA 6 GLU H 6 GLU HA 4.0 . . 1.0 5 3JHNHA 7 LEU H 7 LEU HA 4.0 . . 1.0 6 3JHNHA 8 GLU H 8 GLU HA 4.5 . . 1.0 7 3JHNHA 9 LYS H 9 LYS HA 4.5 . . 1.0 8 3JHNHA 10 LYS H 10 LYS HA 6.0 . . 1.0 9 3JHNHA 11 PHE H 11 PHE HA 5.0 . . 1.0 10 3JHNHA 12 LYS H 12 LYS HA 6.0 . . 1.0 11 3JHNHA 13 GLU H 13 GLU HA 5.0 . . 1.0 12 3JHNHA 14 LEU H 14 LEU HA 3.0 . . 1.0 13 3JHNHA 16 LYS H 16 LYS HA 7.0 . . 1.0 14 3JHNHA 19 ARG H 19 ARG HA 7.0 . . 1.0 15 3JHNHA 21 GLY H 21 GLY HA 10.0 . . 1.0 16 3JHNHA 22 GLU H 22 GLU HA 10.0 . . 1.0 17 3JHNHA 23 ILE H 23 ILE HA 4.0 . . 1.0 18 3JHNHA 24 GLU H 24 GLU HA 7.0 . . 1.0 19 3JHNHA 25 GLU H 25 GLU HA 5.0 . . 1.0 20 3JHNHA 26 LEU H 26 LEU HA 5.0 . . 1.0 21 3JHNHA 28 LYS H 28 LYS HA 5.0 . . 1.0 22 3JHNHA 29 LYS H 29 LYS HA 7.0 . . 1.0 23 3JHNHA 30 PHE H 30 PHE HA 12.0 . . 1.0 24 3JHNHA 32 GLU H 32 GLU HA 5.0 . . 1.0 25 3JHNHA 33 LEU H 33 LEU HA 4.0 . . 1.0 26 3JHNHA 34 ILE H 34 ILE HA 6.0 . . 1.0 27 3JHNHA 35 LYS H 35 LYS HA 5.0 . . 1.0 stop_ save_