data_5276 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of the Domain-I of the Kazal-type Thrombin Inhibitor Dipetalin ; _BMRB_accession_number 5276 _BMRB_flat_file_name bmr5276.str _Entry_type original _Submission_date 2002-02-06 _Accession_date 2002-02-06 _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 Schlott B. . . 2 Wohnert J. . . 3 Icke C. . . 4 Hartmann M. . . 5 Ramachandran R. . . 6 Guhrs K.-H. . . 7 Glusa E. . . 8 Flemming J. . . 9 Gorlach M. . . 10 Grosse F. . . 11 Ohlenschlager O. . . 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" 269 "13C chemical shifts" 183 "15N chemical shifts" 53 "coupling constants" 50 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-09-11 original author 'Original release' 2004-07-12 update BMRB 'Links to related BMRB entries inserted' stop_ loop_ _Related_BMRB_accession_number _Relationship 6242 'two-domain Thrombin inhibitor Dipetalin' stop_ _Original_release_date 2002-02-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Interaction of Kazal-type Inhibitor Domains with Serine Proteinases: Biochemical and Structural Studies ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22047862 _PubMed_ID 12051857 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schlott B. . . 2 Wohnert J. . . 3 Icke C. . . 4 Hartmann M. . . 5 Ramachandran R. . . 6 Guhrs K-H. . . 7 Glusa E. . . 8 Flemming J. . . 9 Gorlach M. . . 10 Grosse F. . . 11 Ohlenschlager O. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 318 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 533 _Page_last 546 _Year 2002 _Details . loop_ _Keyword Kazal-type 'disulphide-rich small alpha+beta fold' stop_ save_ ################################## # Molecular system description # ################################## save_system_DIPETALIN _Saveframe_category molecular_system _Mol_system_name DIPETALIN _Abbreviation_common DIPETALIN _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DIPETALIN $DIPETALIN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DIPETALIN _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DIPETALIN _Abbreviation_common DIPETALIN _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 55 _Mol_residue_sequence ; FQGNPCECPRALHRVCGSDG NTYSNPCMLTCAKHEGNPDL VQVHEGPCDEHDHDF ; loop_ _Residue_seq_code _Residue_label 1 PHE 2 GLN 3 GLY 4 ASN 5 PRO 6 CYS 7 GLU 8 CYS 9 PRO 10 ARG 11 ALA 12 LEU 13 HIS 14 ARG 15 VAL 16 CYS 17 GLY 18 SER 19 ASP 20 GLY 21 ASN 22 THR 23 TYR 24 SER 25 ASN 26 PRO 27 CYS 28 MET 29 LEU 30 THR 31 CYS 32 ALA 33 LYS 34 HIS 35 GLU 36 GLY 37 ASN 38 PRO 39 ASP 40 LEU 41 VAL 42 GLN 43 VAL 44 HIS 45 GLU 46 GLY 47 PRO 48 CYS 49 ASP 50 GLU 51 HIS 52 ASP 53 HIS 54 ASP 55 PHE stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 6242 Dipetalin-I+II 100.00 108 100.00 100.00 4.92e-25 PDB 1KMA 'Nmr Structure Of The Domain-I Of The Kazal-Type Thrombin Inhibitor Dipetalin' 100.00 55 100.00 100.00 6.64e-25 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $DIPETALIN 'Dipetalogaster maximus' 72496 Eukaryota Metazoa Dipetalogaster maximus 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 $DIPETALIN 'recombinant technology' 'E. COLI' Escherichia coli TG1 pMEX6 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 $DIPETALIN 1 mM [U-15N] 'phosphate buffer' 50 mM . NaCl 100 mM . EDTA 0.1 mM . D2O 6 % . H2O 94 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DIPETALIN 1.37 mM '[U-15N; U-13C]' 'phosphate buffer' 50 mM . NaCl 100 mM . EDTA 0.1 mM . D2O 6 % . H2O 94 % . stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure solution' stop_ _Details Guentert save_ save_OPAL _Saveframe_category software _Name OPAL _Version 2.6 loop_ _Task refinement stop_ _Details Luginbuehl save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_3D_13C-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_HNHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _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 6.68 . n/a pressure 1 . atm temperature 288 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 DIOXANE C 13 'methylene carbons' ppm 67.80 external direct . . . 1.0 DSS H 1 'methyl protons' ppm 0.00 external direct . . . 1.0 NH4Cl N 15 nitrogen ppm 24.93 external direct . . . 1.0 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_ _Experiment_label '3D 15N-separated NOESY' '3D 13C-separated NOESY' HNHA stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name DIPETALIN _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 PHE CA C 55.8 0.2 1 2 . 1 PHE HA H 4.03 0.02 1 3 . 1 PHE CB C 34.3 0.2 1 4 . 1 PHE HB2 H 1.96 0.02 1 5 . 1 PHE HB3 H 1.96 0.02 1 6 . 1 PHE C C 175.2 0.2 1 7 . 2 GLN N N 120.2 0.2 1 8 . 2 GLN H H 8.37 0.02 1 9 . 2 GLN CA C 54.3 0.2 1 10 . 2 GLN HA H 4.18 0.02 1 11 . 2 GLN CB C 27.9 0.2 1 12 . 2 GLN HB2 H 1.92 0.02 2 13 . 2 GLN HB3 H 1.79 0.02 2 14 . 2 GLN CG C 32.1 0.2 1 15 . 2 GLN HG2 H 2.16 0.02 1 16 . 2 GLN HG3 H 2.16 0.02 1 17 . 2 GLN NE2 N 114.2 0.2 1 18 . 2 GLN HE21 H 7.48 0.02 2 19 . 2 GLN HE22 H 6.79 0.02 2 20 . 2 GLN C C 173.9 0.2 1 21 . 3 GLY N N 111.8 0.2 1 22 . 3 GLY H H 8.04 0.02 1 23 . 3 GLY CA C 43.4 0.2 1 24 . 3 GLY HA2 H 3.76 0.02 1 25 . 3 GLY HA3 H 3.76 0.02 1 26 . 3 GLY C C 171.9 0.2 1 27 . 4 ASN N N 121.0 0.2 1 28 . 4 ASN H H 8.29 0.02 1 29 . 4 ASN CA C 49.6 0.2 1 30 . 4 ASN HA H 4.88 0.02 1 31 . 4 ASN CB C 37.2 0.2 1 32 . 4 ASN HB2 H 2.71 0.02 2 33 . 4 ASN HB3 H 2.57 0.02 2 34 . 4 ASN ND2 N 114.4 0.2 1 35 . 4 ASN HD21 H 7.56 0.02 2 36 . 4 ASN HD22 H 6.98 0.02 2 37 . 5 PRO CD C 49.4 0.2 1 38 . 5 PRO CA C 62.2 0.2 1 39 . 5 PRO HA H 4.27 0.02 1 40 . 5 PRO CB C 30.7 0.2 1 41 . 5 PRO HB2 H 2.08 0.02 2 42 . 5 PRO HB3 H 1.74 0.02 2 43 . 5 PRO CG C 25.6 0.2 1 44 . 5 PRO HG2 H 1.73 0.02 1 45 . 5 PRO HG3 H 1.73 0.02 1 46 . 5 PRO HD2 H 3.65 0.02 2 47 . 5 PRO HD3 H 3.51 0.02 2 48 . 9 PRO CD C 49.4 0.2 1 49 . 9 PRO CA C 60.8 0.2 1 50 . 9 PRO HA H 4.47 0.02 1 51 . 9 PRO CB C 30.9 0.2 1 52 . 9 PRO HB2 H 2.37 0.02 2 53 . 9 PRO HB3 H 1.82 0.02 2 54 . 9 PRO CG C 26.0 0.2 1 55 . 9 PRO HG2 H 1.98 0.02 1 56 . 9 PRO HG3 H 1.98 0.02 1 57 . 9 PRO HD2 H 3.90 0.02 2 58 . 9 PRO HD3 H 3.44 0.02 2 59 . 9 PRO C C 174.9 0.2 1 60 . 10 ARG N N 121.2 0.2 1 61 . 10 ARG H H 8.48 0.02 1 62 . 10 ARG CA C 54.7 0.2 1 63 . 10 ARG HA H 4.04 0.02 1 64 . 10 ARG CB C 28.5 0.2 1 65 . 10 ARG HB2 H 1.79 0.02 2 66 . 10 ARG HB3 H 1.61 0.02 2 67 . 10 ARG CG C 25.8 0.2 1 68 . 10 ARG HG2 H 1.56 0.02 1 69 . 10 ARG HG3 H 1.56 0.02 1 70 . 10 ARG CD C 41.6 0.2 1 71 . 10 ARG HD2 H 3.10 0.02 1 72 . 10 ARG HD3 H 3.10 0.02 1 73 . 10 ARG C C 175.6 0.2 1 74 . 11 ALA N N 123.5 0.2 1 75 . 11 ALA H H 7.24 0.02 1 76 . 11 ALA CA C 51.2 0.2 1 77 . 11 ALA HA H 4.04 0.02 1 78 . 11 ALA HB H 1.25 0.02 1 79 . 11 ALA CB C 17.7 0.2 1 80 . 11 ALA C C 175.6 0.2 1 81 . 12 LEU N N 125.7 0.2 1 82 . 12 LEU H H 8.52 0.02 1 83 . 12 LEU CA C 53.8 0.2 1 84 . 12 LEU HA H 4.34 0.02 1 85 . 12 LEU CB C 41.5 0.2 1 86 . 12 LEU HB2 H 1.64 0.02 2 87 . 12 LEU HB3 H 1.48 0.02 2 88 . 12 LEU CG C 25.8 0.2 1 89 . 12 LEU HG H 1.64 0.02 1 90 . 12 LEU HD1 H 0.90 0.02 2 91 . 12 LEU HD2 H 0.84 0.02 2 92 . 12 LEU CD1 C 23.3 0.2 1 93 . 12 LEU CD2 C 22.8 0.2 1 94 . 12 LEU C C 175.8 0.2 1 95 . 13 HIS N N 128.2 0.2 1 96 . 13 HIS H H 9.37 0.02 1 97 . 13 HIS CA C 53.8 0.2 1 98 . 13 HIS HA H 4.53 0.02 1 99 . 13 HIS CB C 28.4 0.2 1 100 . 13 HIS HB2 H 3.02 0.02 2 101 . 13 HIS HB3 H 2.89 0.02 2 102 . 13 HIS C C 170.9 0.2 1 103 . 14 ARG N N 122.9 0.2 1 104 . 14 ARG H H 8.31 0.02 1 105 . 14 ARG CA C 56.7 0.2 1 106 . 14 ARG HA H 4.34 0.02 1 107 . 14 ARG CB C 29.5 0.2 1 108 . 14 ARG HB2 H 1.56 0.02 2 109 . 14 ARG HB3 H 1.14 0.02 2 110 . 14 ARG CG C 27.1 0.2 1 111 . 14 ARG HG2 H 1.78 0.02 2 112 . 14 ARG HG3 H 1.56 0.02 2 113 . 14 ARG CD C 42.4 0.2 1 114 . 14 ARG HD2 H 3.01 0.02 1 115 . 14 ARG HD3 H 3.01 0.02 1 116 . 14 ARG NE N 112.3 0.2 1 117 . 14 ARG HE H 8.34 0.02 1 118 . 14 ARG C C 176.4 0.2 1 119 . 15 VAL N N 113.4 0.2 1 120 . 15 VAL H H 8.29 0.02 1 121 . 15 VAL CA C 58.2 0.2 1 122 . 15 VAL HA H 4.61 0.02 1 123 . 15 VAL CB C 35.3 0.2 1 124 . 15 VAL HB H 1.81 0.02 1 125 . 15 VAL HG1 H 0.90 0.02 2 126 . 15 VAL HG2 H 0.52 0.02 2 127 . 15 VAL CG1 C 20.5 0.2 1 128 . 15 VAL CG2 C 16.6 0.2 1 129 . 15 VAL C C 171.5 0.2 1 130 . 16 CYS N N 121.1 0.2 1 131 . 16 CYS H H 8.16 0.02 1 132 . 16 CYS CA C 52.5 0.2 1 133 . 16 CYS HA H 5.02 0.02 1 134 . 16 CYS CB C 37.0 0.2 1 135 . 16 CYS HB2 H 2.37 0.02 2 136 . 16 CYS HB3 H 0.97 0.02 2 137 . 16 CYS C C 173.8 0.2 1 138 . 17 GLY N N 117.1 0.2 1 139 . 17 GLY H H 9.32 0.02 1 140 . 17 GLY CA C 43.2 0.2 1 141 . 17 GLY HA2 H 4.86 0.02 2 142 . 17 GLY HA3 H 3.96 0.02 2 143 . 17 GLY C C 174.2 0.2 1 144 . 18 SER N N 119.4 0.2 1 145 . 18 SER H H 9.23 0.02 1 146 . 18 SER CA C 59.1 0.2 1 147 . 18 SER HA H 3.96 0.02 1 148 . 18 SER CB C 60.5 0.2 1 149 . 18 SER HB2 H 4.09 0.02 2 150 . 18 SER HB3 H 3.67 0.02 2 151 . 18 SER C C 172.2 0.2 1 152 . 19 ASP N N 121.7 0.2 1 153 . 19 ASP H H 8.10 0.02 1 154 . 19 ASP CA C 51.6 0.2 1 155 . 19 ASP HA H 4.39 0.02 1 156 . 19 ASP CB C 38.8 0.2 1 157 . 19 ASP HB2 H 2.88 0.02 2 158 . 19 ASP HB3 H 2.47 0.02 2 159 . 19 ASP C C 175.1 0.2 1 160 . 20 GLY N N 110.1 0.2 1 161 . 20 GLY H H 8.19 0.02 1 162 . 20 GLY CA C 44.0 0.2 1 163 . 20 GLY HA2 H 4.01 0.02 2 164 . 20 GLY HA3 H 3.60 0.02 2 165 . 20 GLY C C 172.2 0.2 1 166 . 21 ASN N N 120.3 0.2 1 167 . 21 ASN H H 8.02 0.02 1 168 . 21 ASN CA C 50.3 0.2 1 169 . 21 ASN HA H 4.75 0.02 1 170 . 21 ASN CB C 38.2 0.2 1 171 . 21 ASN HB2 H 2.75 0.02 2 172 . 21 ASN HB3 H 1.96 0.02 2 173 . 21 ASN ND2 N 116.4 0.2 1 174 . 21 ASN HD21 H 6.82 0.02 2 175 . 21 ASN HD22 H 6.87 0.02 2 176 . 21 ASN C C 171.9 0.2 1 177 . 22 THR N N 122.3 0.2 1 178 . 22 THR H H 8.45 0.02 1 179 . 22 THR CA C 60.9 0.2 1 180 . 22 THR HA H 4.79 0.02 1 181 . 22 THR CB C 67.7 0.2 1 182 . 22 THR HB H 3.85 0.02 1 183 . 22 THR HG2 H 1.03 0.02 1 184 . 22 THR CG2 C 21.0 0.2 1 185 . 22 THR C C 173.1 0.2 1 186 . 23 TYR N N 129.0 0.2 1 187 . 23 TYR H H 9.22 0.02 1 188 . 23 TYR CA C 56.0 0.2 1 189 . 23 TYR HA H 4.45 0.02 1 190 . 23 TYR CB C 40.6 0.2 1 191 . 23 TYR HB2 H 2.72 0.02 2 192 . 23 TYR HB3 H 2.36 0.02 2 193 . 23 TYR HE1 H 6.22 0.02 1 194 . 23 TYR HE2 H 6.22 0.02 1 195 . 23 TYR C C 175.2 0.2 1 196 . 24 SER N N 118.8 0.2 1 197 . 24 SER H H 9.15 0.02 1 198 . 24 SER CA C 60.4 0.2 1 199 . 24 SER HA H 3.87 0.02 1 200 . 24 SER CB C 61.7 0.2 1 201 . 24 SER HB2 H 3.81 0.02 1 202 . 24 SER HB3 H 3.81 0.02 1 203 . 24 SER C C 171.3 0.2 1 204 . 25 ASN N N 110.9 0.2 1 205 . 25 ASN H H 7.31 0.02 1 206 . 25 ASN CA C 50.3 0.2 1 207 . 25 ASN HA H 5.39 0.02 1 208 . 25 ASN CB C 35.7 0.2 1 209 . 25 ASN HB2 H 3.29 0.02 2 210 . 25 ASN HB3 H 3.06 0.02 2 211 . 25 ASN ND2 N 114.9 0.2 1 212 . 25 ASN HD21 H 7.29 0.02 2 213 . 25 ASN HD22 H 6.34 0.02 2 214 . 26 PRO CD C 48.9 0.2 1 215 . 26 PRO CA C 64.4 0.2 1 216 . 26 PRO HA H 4.04 0.02 1 217 . 26 PRO CB C 30.7 0.2 1 218 . 26 PRO HB2 H 2.48 0.02 2 219 . 26 PRO HB3 H 1.87 0.02 2 220 . 26 PRO CG C 26.5 0.2 1 221 . 26 PRO HG2 H 2.05 0.02 2 222 . 26 PRO HG3 H 1.87 0.02 2 223 . 26 PRO HD2 H 4.10 0.02 2 224 . 26 PRO HD3 H 3.90 0.02 2 225 . 26 PRO C C 176.2 0.2 1 226 . 27 CYS N N 119.5 0.2 1 227 . 27 CYS H H 7.92 0.02 1 228 . 27 CYS CA C 58.5 0.2 1 229 . 27 CYS HA H 4.14 0.02 1 230 . 27 CYS CB C 34.2 0.2 1 231 . 27 CYS HB2 H 3.22 0.02 2 232 . 27 CYS HB3 H 2.98 0.02 2 233 . 27 CYS C C 175.6 0.2 1 234 . 28 MET N N 122.4 0.2 1 235 . 28 MET H H 8.27 0.02 1 236 . 28 MET CA C 55.9 0.2 1 237 . 28 MET HA H 4.22 0.02 1 238 . 28 MET CB C 31.1 0.2 1 239 . 28 MET HB2 H 2.76 0.02 2 240 . 28 MET HB3 H 2.69 0.02 2 241 . 28 MET CG C 30.4 0.2 1 242 . 28 MET HG2 H 2.19 0.02 1 243 . 28 MET HG3 H 2.19 0.02 1 244 . 28 MET HE H 2.06 0.02 1 245 . 28 MET CE C 15.7 0.2 1 246 . 28 MET C C 177.8 0.2 1 247 . 29 LEU N N 125.6 0.2 1 248 . 29 LEU H H 7.17 0.02 1 249 . 29 LEU CA C 58.1 0.2 1 250 . 29 LEU HA H 2.88 0.02 1 251 . 29 LEU CB C 39.3 0.2 1 252 . 29 LEU HB2 H 1.61 0.02 2 253 . 29 LEU HB3 H 0.85 0.02 2 254 . 29 LEU CG C 26.1 0.2 1 255 . 29 LEU HG H 0.80 0.02 1 256 . 29 LEU HD1 H 0.50 0.02 2 257 . 29 LEU HD2 H 0.44 0.02 2 258 . 29 LEU CD1 C 25.5 0.2 1 259 . 29 LEU CD2 C 22.2 0.2 1 260 . 29 LEU C C 176.3 0.2 1 261 . 30 THR N N 119.1 0.2 1 262 . 30 THR H H 8.14 0.02 1 263 . 30 THR CA C 65.3 0.2 1 264 . 30 THR HA H 3.48 0.02 1 265 . 30 THR CB C 66.4 0.2 1 266 . 30 THR HB H 4.22 0.02 1 267 . 30 THR HG2 H 1.08 0.02 1 268 . 30 THR CG2 C 21.4 0.2 1 269 . 30 THR C C 174.7 0.2 1 270 . 31 CYS N N 122.2 0.2 1 271 . 31 CYS H H 8.51 0.02 1 272 . 31 CYS CA C 56.9 0.2 1 273 . 31 CYS HA H 4.14 0.02 1 274 . 31 CYS CB C 38.3 0.2 1 275 . 31 CYS HB2 H 3.27 0.02 2 276 . 31 CYS HB3 H 3.13 0.02 2 277 . 31 CYS C C 174.6 0.2 1 278 . 32 ALA N N 123.6 0.2 1 279 . 32 ALA H H 7.44 0.02 1 280 . 32 ALA CA C 53.5 0.2 1 281 . 32 ALA HA H 4.05 0.02 1 282 . 32 ALA HB H 1.40 0.02 1 283 . 32 ALA CB C 16.8 0.2 1 284 . 32 ALA C C 178.9 0.2 1 285 . 33 LYS N N 123.6 0.2 1 286 . 33 LYS H H 8.06 0.02 1 287 . 33 LYS CA C 56.0 0.2 1 288 . 33 LYS HA H 4.24 0.02 1 289 . 33 LYS CB C 31.8 0.2 1 290 . 33 LYS HB2 H 1.91 0.02 2 291 . 33 LYS HB3 H 1.53 0.02 2 292 . 33 LYS CG C 28.7 0.2 1 293 . 33 LYS HG2 H 1.53 0.02 2 294 . 33 LYS HG3 H 1.41 0.02 2 295 . 33 LYS CD C 22.4 0.2 1 296 . 33 LYS HD2 H 1.61 0.02 2 297 . 33 LYS HD3 H 0.96 0.02 2 298 . 33 LYS CE C 40.6 0.2 1 299 . 33 LYS HE2 H 2.93 0.02 2 300 . 33 LYS HE3 H 2.84 0.02 2 301 . 33 LYS C C 177.5 0.2 1 302 . 34 HIS N N 118.8 0.2 1 303 . 34 HIS H H 7.76 0.02 1 304 . 34 HIS CA C 56.3 0.2 1 305 . 34 HIS HA H 4.33 0.02 1 306 . 34 HIS CB C 28.4 0.2 1 307 . 34 HIS HB2 H 3.24 0.02 2 308 . 34 HIS HB3 H 3.08 0.02 2 309 . 34 HIS C C 174.9 0.2 1 310 . 35 GLU N N 121.5 0.2 1 311 . 35 GLU H H 8.02 0.02 1 312 . 35 GLU CA C 54.7 0.2 1 313 . 35 GLU HA H 4.26 0.02 1 314 . 35 GLU CB C 27.6 0.2 1 315 . 35 GLU HB2 H 2.08 0.02 2 316 . 35 GLU HB3 H 1.91 0.02 2 317 . 35 GLU CG C 35.0 0.2 1 318 . 35 GLU HG2 H 2.34 0.02 2 319 . 35 GLU HG3 H 2.15 0.02 2 320 . 35 GLU C C 175.6 0.2 1 321 . 36 GLY N N 106.1 0.2 1 322 . 36 GLY H H 7.54 0.02 1 323 . 36 GLY CA C 44.6 0.2 1 324 . 36 GLY HA2 H 4.08 0.02 2 325 . 36 GLY HA3 H 3.91 0.02 2 326 . 36 GLY C C 172.1 0.2 1 327 . 37 ASN N N 118.1 0.2 1 328 . 37 ASN H H 7.57 0.02 1 329 . 37 ASN CA C 49.3 0.2 1 330 . 37 ASN HA H 5.19 0.02 1 331 . 37 ASN CB C 37.6 0.2 1 332 . 37 ASN HB2 H 2.68 0.02 2 333 . 37 ASN HB3 H 2.58 0.02 2 334 . 37 ASN ND2 N 114.5 0.2 1 335 . 37 ASN HD21 H 7.68 0.02 2 336 . 37 ASN HD22 H 6.87 0.02 2 337 . 38 PRO CD C 48.9 0.2 1 338 . 38 PRO CA C 63.1 0.2 1 339 . 38 PRO HA H 4.16 0.02 1 340 . 38 PRO CB C 30.5 0.2 1 341 . 38 PRO HB2 H 2.23 0.02 2 342 . 38 PRO HB3 H 1.84 0.02 2 343 . 38 PRO CG C 25.5 0.2 1 344 . 38 PRO HG2 H 1.90 0.02 2 345 . 38 PRO HG3 H 1.82 0.02 2 346 . 38 PRO HD2 H 3.69 0.02 2 347 . 38 PRO HD3 H 3.39 0.02 2 348 . 38 PRO C C 176.1 0.2 1 349 . 39 ASP N N 118.7 0.2 1 350 . 39 ASP H H 7.98 0.02 1 351 . 39 ASP CA C 52.5 0.2 1 352 . 39 ASP HA H 4.49 0.02 1 353 . 39 ASP CB C 39.3 0.2 1 354 . 39 ASP HB2 H 2.67 0.02 2 355 . 39 ASP HB3 H 2.42 0.02 2 356 . 39 ASP C C 174.0 0.2 1 357 . 40 LEU N N 124.9 0.2 1 358 . 40 LEU H H 7.34 0.02 1 359 . 40 LEU CA C 54.9 0.2 1 360 . 40 LEU HA H 3.74 0.02 1 361 . 40 LEU CB C 41.4 0.2 1 362 . 40 LEU HB2 H 1.62 0.02 2 363 . 40 LEU HB3 H 1.26 0.02 2 364 . 40 LEU CG C 21.5 0.2 1 365 . 40 LEU HG H 0.91 0.02 1 366 . 40 LEU HD1 H 1.04 0.02 2 367 . 40 LEU HD2 H 0.65 0.02 2 368 . 40 LEU CD1 C 25.3 0.2 1 369 . 40 LEU CD2 C 25.6 0.2 1 370 . 40 LEU C C 174.0 0.2 1 371 . 41 VAL N N 121.9 0.2 1 372 . 41 VAL H H 8.42 0.02 1 373 . 41 VAL CA C 57.4 0.2 1 374 . 41 VAL HA H 4.45 0.02 1 375 . 41 VAL CB C 35.0 0.2 1 376 . 41 VAL HB H 1.97 0.02 1 377 . 41 VAL HG1 H 0.75 0.02 2 378 . 41 VAL HG2 H 0.70 0.02 2 379 . 41 VAL CG1 C 19.9 0.2 1 380 . 41 VAL CG2 C 17.1 0.2 1 381 . 41 VAL C C 173.1 0.2 1 382 . 42 GLN N N 124.7 0.2 1 383 . 42 GLN H H 8.74 0.02 1 384 . 42 GLN CA C 54.7 0.2 1 385 . 42 GLN HA H 4.08 0.02 1 386 . 42 GLN CB C 28.2 0.2 1 387 . 42 GLN HB2 H 1.76 0.02 2 388 . 42 GLN HB3 H 1.61 0.02 2 389 . 42 GLN CG C 41.7 0.2 1 390 . 42 GLN HG2 H 3.10 0.02 1 391 . 42 GLN HG3 H 3.10 0.02 1 392 . 42 GLN NE2 N 112.9 0.2 1 393 . 42 GLN HE21 H 7.21 0.02 2 394 . 42 GLN HE22 H 6.78 0.02 2 395 . 42 GLN C C 174.6 0.2 1 396 . 43 VAL N N 126.8 0.2 1 397 . 43 VAL H H 9.07 0.02 1 398 . 43 VAL CA C 62.1 0.2 1 399 . 43 VAL HA H 4.14 0.02 1 400 . 43 VAL CB C 31.2 0.2 1 401 . 43 VAL HB H 1.76 0.02 1 402 . 43 VAL HG1 H 0.90 0.02 2 403 . 43 VAL HG2 H 0.69 0.02 2 404 . 43 VAL CG1 C 20.4 0.2 1 405 . 43 VAL CG2 C 18.9 0.2 1 406 . 43 VAL C C 174.8 0.2 1 407 . 44 HIS N N 111.9 0.2 1 408 . 44 HIS H H 7.05 0.02 1 409 . 44 HIS CA C 53.8 0.2 1 410 . 44 HIS HA H 4.87 0.02 1 411 . 44 HIS CB C 28.2 0.2 1 412 . 44 HIS HB2 H 3.61 0.02 2 413 . 44 HIS HB3 H 3.21 0.02 2 414 . 44 HIS C C 172.0 0.2 1 415 . 45 GLU N N 121.5 0.2 1 416 . 45 GLU H H 9.19 0.02 1 417 . 45 GLU CA C 55.8 0.2 1 418 . 45 GLU HA H 4.36 0.02 1 419 . 45 GLU CB C 29.7 0.2 1 420 . 45 GLU HB2 H 2.18 0.02 2 421 . 45 GLU HB3 H 2.04 0.02 2 422 . 45 GLU CG C 35.6 0.2 1 423 . 45 GLU HG2 H 2.35 0.02 2 424 . 45 GLU HG3 H 2.16 0.02 2 425 . 45 GLU C C 177.0 0.2 1 426 . 46 GLY N N 116.4 0.2 1 427 . 46 GLY H H 8.43 0.02 1 428 . 46 GLY CA C 43.4 0.2 1 429 . 46 GLY HA2 H 4.40 0.02 2 430 . 46 GLY HA3 H 3.57 0.02 2 431 . 47 PRO CD C 47.6 0.2 1 432 . 47 PRO CA C 60.0 0.2 1 433 . 47 PRO HA H 4.24 0.02 1 434 . 47 PRO CB C 30.9 0.2 1 435 . 47 PRO HB2 H 1.94 0.02 1 436 . 47 PRO HB3 H 1.94 0.02 1 437 . 47 PRO CG C 25.9 0.2 1 438 . 47 PRO HG2 H 1.88 0.02 2 439 . 47 PRO HG3 H 1.77 0.02 2 440 . 47 PRO HD2 H 3.52 0.02 2 441 . 47 PRO HD3 H 3.26 0.02 2 442 . 47 PRO C C 172.8 0.2 1 443 . 48 CYS N N 120.0 0.2 1 444 . 48 CYS H H 8.19 0.02 1 445 . 48 CYS CA C 53.0 0.2 1 446 . 48 CYS HA H 4.51 0.02 1 447 . 48 CYS CB C 36.0 0.2 1 448 . 48 CYS HB2 H 3.10 0.02 2 449 . 48 CYS HB3 H 2.45 0.02 2 450 . 48 CYS C C 173.4 0.2 1 451 . 49 ASP N N 123.5 0.2 1 452 . 49 ASP H H 8.77 0.02 1 453 . 49 ASP CA C 52.4 0.2 1 454 . 49 ASP HA H 4.53 0.02 1 455 . 49 ASP CB C 40.2 0.2 1 456 . 49 ASP HB2 H 2.57 0.02 1 457 . 49 ASP HB3 H 2.57 0.02 1 458 . 49 ASP C C 174.7 0.2 1 459 . 50 GLU N N 122.6 0.2 1 460 . 50 GLU H H 8.51 0.02 1 461 . 50 GLU CA C 55.7 0.2 1 462 . 50 GLU HA H 4.02 0.02 1 463 . 50 GLU CB C 28.2 0.2 1 464 . 50 GLU HB2 H 1.75 0.02 2 465 . 50 GLU HB3 H 1.59 0.02 2 466 . 50 GLU CG C 41.6 0.2 1 467 . 50 GLU HG2 H 3.08 0.02 2 468 . 50 GLU HG3 H 3.00 0.02 2 469 . 50 GLU C C 175.2 0.2 1 470 . 51 HIS N N 122.8 0.2 1 471 . 51 HIS H H 8.07 0.02 1 472 . 51 HIS CA C 54.4 0.2 1 473 . 51 HIS HA H 4.50 0.02 1 474 . 51 HIS CB C 27.8 0.2 1 475 . 51 HIS HB2 H 3.11 0.02 2 476 . 51 HIS HB3 H 2.97 0.02 2 477 . 52 ASP N N 122.1 0.2 1 478 . 52 ASP H H 8.06 0.02 1 479 . 52 ASP CA C 53.3 0.2 1 480 . 52 ASP HA H 4.45 0.02 1 481 . 52 ASP CB C 39.5 0.2 1 482 . 52 ASP HB2 H 2.53 0.02 1 483 . 52 ASP HB3 H 2.53 0.02 1 484 . 53 HIS N N 120.0 0.2 1 485 . 53 HIS H H 8.11 0.02 1 486 . 53 HIS CA C 53.7 0.2 1 487 . 53 HIS HA H 4.52 0.02 1 488 . 53 HIS CB C 28.4 0.2 1 489 . 53 HIS HB2 H 3.04 0.02 2 490 . 53 HIS HB3 H 2.89 0.02 2 491 . 54 ASP N N 123.2 0.2 1 492 . 54 ASP H H 8.22 0.02 1 493 . 54 ASP CA C 52.9 0.2 1 494 . 54 ASP HA H 4.48 0.02 1 495 . 54 ASP CB C 39.3 0.2 1 496 . 54 ASP HB2 H 2.54 0.02 2 497 . 54 ASP HB3 H 2.40 0.02 2 498 . 54 ASP C C 173.4 0.2 1 499 . 55 PHE N N 126.3 0.2 1 500 . 55 PHE H H 7.63 0.02 1 501 . 55 PHE CA C 57.6 0.2 1 502 . 55 PHE HA H 4.30 0.02 1 503 . 55 PHE CB C 38.6 0.2 1 504 . 55 PHE HB2 H 3.01 0.02 2 505 . 55 PHE HB3 H 2.88 0.02 2 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constant_set_1 _Saveframe_category coupling_constants _Details . loop_ _Experiment_label '3D 15N-separated NOESY' '3D 13C-separated NOESY' HNHA stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name DIPETALIN _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 GLN H 2 GLN HA 6.9 . . 1.5 2 3JHNHA 3 GLY H 3 GLY HA2 8.1 . . 1.5 3 3JHNHA 3 GLY H 3 GLY HA3 8.1 . . 1.5 4 3JHNHA 4 ASN H 4 ASN HA 7.2 . . 1.5 5 3JHNHA 10 ARG H 10 ARG HA 6.3 . . 1.5 6 3JHNHA 11 ALA H 11 ALA HA 3.2 . . 1.5 7 3JHNHA 12 LEU H 12 LEU HA 5.8 . . 1.5 8 3JHNHA 13 HIS H 13 HIS HA 6.0 . . 1.5 9 3JHNHA 14 ARG H 14 ARG HA 2.7 . . 1.5 10 3JHNHA 15 VAL H 15 VAL HA 6.8 . . 1.5 11 3JHNHA 16 CYS H 16 CYS HA 7.8 . . 1.5 12 3JHNHA 17 GLY H 17 GLY HA2 5.6 . . 1.5 13 3JHNHA 17 GLY H 17 GLY HA3 4.0 . . 1.5 14 3JHNHA 18 SER H 18 SER HA 3.0 . . 1.5 15 3JHNHA 19 ASP H 19 ASP HA 7.5 . . 1.5 16 3JHNHA 20 GLY H 20 GLY HA2 6.2 . . 1.5 17 3JHNHA 20 GLY H 20 GLY HA3 4.2 . . 1.5 18 3JHNHA 21 ASN H 21 ASN HA 7.7 . . 1.5 19 3JHNHA 22 THR H 22 THR HA 5.9 . . 1.5 20 3JHNHA 23 TYR H 23 TYR HA 8.8 . . 1.5 21 3JHNHA 24 SER H 24 SER HA 2.2 . . 1.5 22 3JHNHA 25 ASN H 25 ASN HA 3.4 . . 1.5 23 3JHNHA 27 CYS H 27 CYS HA 3.3 . . 1.5 24 3JHNHA 28 MET H 28 MET HA 4.2 . . 1.5 25 3JHNHA 29 LEU H 29 LEU HA 4.1 . . 1.5 26 3JHNHA 30 THR H 30 THR HA 2.5 . . 1.5 27 3JHNHA 31 CYS H 31 CYS HA 3.9 . . 1.5 28 3JHNHA 32 ALA H 32 ALA HA 4.3 . . 1.5 29 3JHNHA 33 LYS H 33 LYS HA 3.1 . . 1.5 30 3JHNHA 34 HIS H 34 HIS HA 4.8 . . 1.5 31 3JHNHA 35 GLU H 35 GLU HA 6.6 . . 1.5 32 3JHNHA 36 GLY H 36 GLY HA2 4.7 . . 1.5 33 3JHNHA 36 GLY H 36 GLY HA3 4.9 . . 1.5 34 3JHNHA 37 ASN H 37 ASN HA 8.0 . . 1.5 35 3JHNHA 39 ASP H 39 ASP HA 7.5 . . 1.5 36 3JHNHA 40 LEU H 40 LEU HA 3.3 . . 1.5 37 3JHNHA 41 VAL H 41 VAL HA 5.6 . . 1.5 38 3JHNHA 42 GLN H 42 GLN HA 5.6 . . 1.5 39 3JHNHA 43 VAL H 43 VAL HA 6.1 . . 1.5 40 3JHNHA 44 HIS H 44 HIS HA 4.3 . . 1.5 41 3JHNHA 45 GLU H 45 GLU HA 5.6 . . 1.5 42 3JHNHA 46 GLY H 46 GLY HA2 6.3 . . 1.5 43 3JHNHA 46 GLY H 46 GLY HA3 3.4 . . 1.5 44 3JHNHA 48 CYS H 48 CYS HA 4.7 . . 1.5 45 3JHNHA 49 ASP H 49 ASP HA 6.5 . . 1.5 46 3JHNHA 50 GLU H 50 GLU HA 4.8 . . 1.5 47 3JHNHA 52 ASP H 52 ASP HA 6.2 . . 1.5 48 3JHNHA 53 HIS H 53 HIS HA 7.3 . . 1.5 49 3JHNHA 54 ASP H 54 ASP HA 6.4 . . 1.5 50 3JHNHA 55 PHE H 55 PHE HA 5.8 . . 1.5 stop_ save_