data_5056 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; ATT an Arabidopsis thaliana Inhibitor of Trypsin and Chymotrypsin: Sequence-Specific Multinuclear Magnetic Resonance Assignments and Secondary Structure ; _BMRB_accession_number 5056 _BMRB_flat_file_name bmr5056.str _Entry_type original _Submission_date 2001-06-13 _Accession_date 2001-06-14 _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 Zhao Qin . . 2 Chae Young-Kee . . 3 Markley John L. . 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" 333 "13C chemical shifts" 237 "15N chemical shifts" 68 "coupling constants" 50 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-01-06 original BMRB . stop_ _Original_release_date 2001-06-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Solution Structure of ATTp, an Arabidopsis thaliana Trypsin Inhibitor ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22257244 _PubMed_ID 12369816 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhao Qin . . 2 Chae Young-Kee . . 3 Markley John L. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 41 _Journal_issue 41 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 12284 _Page_last 12296 _Year 2002 _Details . loop_ _Keyword NMR 'chemical shift assignments' 'chemical shift index' chymotrypsin 'protease inhibitor' 'serine protease' trypsin stop_ save_ ################################## # Molecular system description # ################################## save_system_ATT _Saveframe_category molecular_system _Mol_system_name 'Arabidopsis thaliana trypsin/chymotrypsin inhibitor' _Abbreviation_common ATT _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ATT $ATT stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'disulfide bound and free' loop_ _Biological_function 'serine protease inhibitor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ATT _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ATT _Abbreviation_common ATT _Molecular_mass . _Mol_thiol_state 'disulfide bound and free' loop_ _Biological_function 'serine protease inhibitor' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 68 _Mol_residue_sequence ; CPEIEAQGNECLKEYGGDVG FGFCAPRIFPTICYTRCREN KGAKGGRCRWGQGSNVKCLC DFCGDTPQ ; loop_ _Residue_seq_code _Residue_label 1 CYS 2 PRO 3 GLU 4 ILE 5 GLU 6 ALA 7 GLN 8 GLY 9 ASN 10 GLU 11 CYS 12 LEU 13 LYS 14 GLU 15 TYR 16 GLY 17 GLY 18 ASP 19 VAL 20 GLY 21 PHE 22 GLY 23 PHE 24 CYS 25 ALA 26 PRO 27 ARG 28 ILE 29 PHE 30 PRO 31 THR 32 ILE 33 CYS 34 TYR 35 THR 36 ARG 37 CYS 38 ARG 39 GLU 40 ASN 41 LYS 42 GLY 43 ALA 44 LYS 45 GLY 46 GLY 47 ARG 48 CYS 49 ARG 50 TRP 51 GLY 52 GLN 53 GLY 54 SER 55 ASN 56 VAL 57 LYS 58 CYS 59 LEU 60 CYS 61 ASP 62 PHE 63 CYS 64 GLY 65 ASP 66 THR 67 PRO 68 GLN 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 5133 attm 91.18 62 100.00 100.00 3.72e-28 PDB 1JXC 'Minimized Nmr Structure Of Att, An Arabidopsis TrypsinCHYMOTRYPSIN INHIBITOR' 100.00 68 100.00 100.00 1.03e-31 EMBL CAB62548 'trypsin inhibitor [Arabidopsis thaliana]' 98.53 89 98.51 98.51 1.69e-31 EMBL CAG15155 'putative trypsin inhibitor 1 [Arabidopsis thaliana]' 98.53 89 98.51 98.51 1.69e-31 EMBL CAG15160 'putative trypsin inhibitor 1 [Arabidopsis thaliana]' 98.53 89 98.51 98.51 1.69e-31 EMBL CAG15165 'putative trypsin inhibitor 1 [Arabidopsis thaliana]' 98.53 89 98.51 98.51 1.69e-31 EMBL CAG15170 'putative trypsin inhibitor 1 [Arabidopsis thaliana]' 98.53 89 98.51 98.51 1.69e-31 GenBank AAB64325 'putative trypsin inhibitor [Arabidopsis thaliana]' 98.53 89 98.51 98.51 1.69e-31 GenBank AAK92724 'putative trypsin inhibitor protein [Arabidopsis thaliana]' 98.53 89 98.51 98.51 1.69e-31 GenBank AAM20096 'putative trypsin inhibitor protein [Arabidopsis thaliana]' 98.53 89 98.51 98.51 1.69e-31 REF NP_181879 'ATTI1 (ARABIDOPSIS THALIANA TRYPSIN INHIBITOR PROTEIN 1) [Arabidopsis thaliana]' 98.53 89 98.51 98.51 1.69e-31 SWISS-PROT Q42328 'Trypsin inhibitor ATTI-2 precursor (diDi 4T-1) (ATTp)' 98.53 89 98.51 98.51 1.69e-31 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ATT 'thale cress' 3702 Eukaryota Virdiplanta Arabidopsis thaliana stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $ATT 'recombinant technology' 'E. coli' Escherichia coli BL21 (DE3)/pLysS . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; The protein was released from its n-terminal fusion partner (Snase) by CNBr cleaveage ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ATT 1.0 mM [U-15N] 'sodium acetate' 50 mM '[U-99% 2H]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details ; The protein was released from its n-terminal fusion partner (Snase) by CNBr cleaveage ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ATT 1.0 mM '[U-15N; U-13C]' 'sodium acetate' 50 mM '[U-99% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.6 loop_ _Task 'data acquisition' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.72 loop_ _Task assignments 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectromer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ save_spectromer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_C(CO)NH-SE_5 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH-SE _Sample_label . save_ save_H(CCO)NH-SE_6 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH-SE _Sample_label . save_ save_HCCH-COSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _Sample_label . save_ save_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 5.0 0.02 n/a pressure 1 . atm temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_csref _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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_cstbl_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCA HN(CO)CA HNCACB HNCO C(CO)NH-SE H(CCO)NH-SE HCCH-COSY HCCH-TOCSY stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $csref _Mol_system_component_name ATT _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 PRO HA H 4.437 0.02 1 2 . 2 PRO HB2 H 2.267 0.02 2 3 . 2 PRO HB3 H 1.846 0.02 2 4 . 2 PRO HG2 H 1.976 0.02 1 5 . 2 PRO HG3 H 1.976 0.02 1 6 . 2 PRO HD2 H 3.736 0.02 2 7 . 2 PRO HD3 H 3.637 0.02 2 8 . 2 PRO C C 176.19 0.05 1 9 . 2 PRO CA C 63.289 0.05 1 10 . 2 PRO CB C 31.992 0.05 1 11 . 2 PRO CG C 27.179 0.05 1 12 . 2 PRO CD C 50.626 0.05 1 13 . 3 GLU H H 8.523 0.02 1 14 . 3 GLU HA H 4.230 0.02 1 15 . 3 GLU HB2 H 1.972 0.02 2 16 . 3 GLU HB3 H 1.872 0.02 2 17 . 3 GLU HG2 H 2.261 0.02 1 18 . 3 GLU HG3 H 2.261 0.02 1 19 . 3 GLU C C 176.32 0.05 1 20 . 3 GLU CA C 56.562 0.05 1 21 . 3 GLU CB C 29.810 0.05 1 22 . 3 GLU CG C 35.439 0.05 1 23 . 3 GLU N N 123.03 0.05 1 24 . 4 ILE H H 8.126 0.02 1 25 . 4 ILE HA H 4.082 0.02 1 26 . 4 ILE HB H 1.777 0.02 1 27 . 4 ILE HG12 H 1.394 0.02 2 28 . 4 ILE HG13 H 1.123 0.02 2 29 . 4 ILE HG2 H 0.812 0.02 1 30 . 4 ILE HD1 H 0.795 0.02 1 31 . 4 ILE C C 176.14 0.05 1 32 . 4 ILE CA C 61.069 0.05 1 33 . 4 ILE CB C 38.684 0.05 1 34 . 4 ILE CG1 C 27.145 0.05 1 35 . 4 ILE CG2 C 17.331 0.05 1 36 . 4 ILE CD1 C 12.667 0.05 1 37 . 4 ILE N N 122.90 0.05 1 38 . 5 GLU H H 8.366 0.02 1 39 . 5 GLU HA H 4.216 0.02 1 40 . 5 GLU HB2 H 1.979 0.02 2 41 . 5 GLU HB3 H 1.869 0.02 2 42 . 5 GLU HG2 H 2.247 0.02 1 43 . 5 GLU HG3 H 2.247 0.02 1 44 . 5 GLU C C 176.00 0.05 1 45 . 5 GLU CA C 56.280 0.05 1 46 . 5 GLU CB C 29.810 0.05 1 47 . 5 GLU CG C 35.330 0.05 1 48 . 5 GLU N N 125.85 0.05 1 49 . 6 ALA H H 8.255 0.02 1 50 . 6 ALA HA H 4.231 0.02 1 51 . 6 ALA HB H 1.316 0.02 1 52 . 6 ALA C C 177.52 0.05 1 53 . 6 ALA CA C 52.557 0.05 1 54 . 6 ALA CB C 19.202 0.05 1 55 . 6 ALA N N 126.41 0.05 1 56 . 7 GLN H H 8.278 0.02 1 57 . 7 GLN HA H 4.267 0.02 1 58 . 7 GLN HB2 H 2.079 0.02 2 59 . 7 GLN HB3 H 1.920 0.02 2 60 . 7 GLN HG2 H 2.308 0.02 1 61 . 7 GLN HG3 H 2.308 0.02 1 62 . 7 GLN HE21 H 7.462 0.02 2 63 . 7 GLN HE22 H 6.780 0.02 2 64 . 7 GLN C C 176.50 0.05 1 65 . 7 GLN CA C 55.909 0.05 1 66 . 7 GLN CB C 29.461 0.05 1 67 . 7 GLN CG C 33.890 0.05 1 68 . 7 GLN CD C 180.45 0.05 1 69 . 7 GLN N N 120.25 0.05 1 70 . 8 GLY H H 8.376 0.02 1 71 . 8 GLY HA2 H 3.924 0.02 2 72 . 8 GLY HA3 H 3.832 0.02 2 73 . 8 GLY C C 174.09 0.05 1 74 . 8 GLY CA C 45.477 0.05 1 75 . 8 GLY N N 110.91 0.05 1 76 . 9 ASN H H 8.304 0.02 1 77 . 9 ASN HA H 4.618 0.02 1 78 . 9 ASN HB2 H 2.760 0.02 1 79 . 9 ASN HB3 H 2.760 0.02 1 80 . 9 ASN HD21 H 7.566 0.02 2 81 . 9 ASN HD22 H 6.874 0.02 2 82 . 9 ASN C C 175.49 0.05 1 83 . 9 ASN CA C 53.478 0.05 1 84 . 9 ASN CB C 38.864 0.05 1 85 . 9 ASN CG C 177.05 0.05 1 86 . 9 ASN N N 120.08 0.05 1 87 . 9 ASN ND2 N 114.05 0.05 1 88 . 10 GLU H H 8.598 0.02 1 89 . 10 GLU HA H 4.263 0.02 1 90 . 10 GLU HB2 H 2.067 0.02 2 91 . 10 GLU HB3 H 1.905 0.02 2 92 . 10 GLU HG2 H 2.227 0.02 1 93 . 10 GLU HG3 H 2.227 0.02 1 94 . 10 GLU C C 176.63 0.05 1 95 . 10 GLU CA C 56.915 0.05 1 96 . 10 GLU CB C 29.204 0.05 1 97 . 10 GLU CG C 35.492 0.05 1 98 . 10 GLU N N 121.61 0.05 1 99 . 11 CYS H H 8.185 0.02 1 100 . 11 CYS HA H 4.551 0.02 1 101 . 11 CYS HB2 H 3.086 0.02 1 102 . 11 CYS HB3 H 2.949 0.02 1 103 . 11 CYS C C 173.92 0.05 1 104 . 11 CYS CA C 57.120 0.05 1 105 . 11 CYS CB C 41.472 0.05 1 106 . 11 CYS N N 118.19 0.05 1 107 . 12 LEU H H 7.779 0.02 1 108 . 12 LEU HA H 5.633 0.02 1 109 . 12 LEU HB2 H 1.742 0.02 1 110 . 12 LEU HB3 H 1.152 0.02 1 111 . 12 LEU HG H 0.769 0.02 1 112 . 12 LEU HD1 H 1.488 0.02 1 113 . 12 LEU HD2 H 0.718 0.02 1 114 . 12 LEU C C 176.65 0.05 1 115 . 12 LEU CA C 53.190 0.05 1 116 . 12 LEU CB C 43.766 0.05 1 117 . 12 LEU CG C 25.617 0.05 1 118 . 12 LEU CD1 C 23.054 0.05 1 119 . 12 LEU CD2 C 23.054 0.05 1 120 . 12 LEU N N 119.94 0.05 1 121 . 13 LYS H H 8.885 0.02 1 122 . 13 LYS HA H 4.661 0.02 1 123 . 13 LYS HB2 H 1.812 0.02 1 124 . 13 LYS HB3 H 1.727 0.02 1 125 . 13 LYS HG2 H 1.338 0.02 1 126 . 13 LYS HG3 H 1.338 0.02 1 127 . 13 LYS HD2 H 1.532 0.02 2 128 . 13 LYS HD3 H 1.392 0.02 2 129 . 13 LYS HE2 H 2.725 0.02 1 130 . 13 LYS HE3 H 2.725 0.02 1 131 . 13 LYS C C 175.90 0.05 1 132 . 13 LYS CA C 54.441 0.05 1 133 . 13 LYS CB C 36.511 0.05 1 134 . 13 LYS CG C 24.391 0.05 1 135 . 13 LYS CD C 29.019 0.05 1 136 . 13 LYS CE C 42.021 0.05 1 137 . 13 LYS N N 122.74 0.05 1 138 . 14 GLU H H 9.169 0.02 1 139 . 14 GLU HA H 4.481 0.02 1 140 . 14 GLU HB2 H 2.033 0.02 1 141 . 14 GLU HB3 H 2.033 0.02 1 142 . 14 GLU HG2 H 2.196 0.02 1 143 . 14 GLU HG3 H 2.196 0.02 1 144 . 14 GLU C C 176.60 0.05 1 145 . 14 GLU CA C 57.695 0.05 1 146 . 14 GLU CB C 29.982 0.05 1 147 . 14 GLU CG C 36.958 0.05 1 148 . 14 GLU N N 125.82 0.05 1 149 . 15 TYR H H 8.631 0.02 1 150 . 15 TYR HA H 3.898 0.02 1 151 . 15 TYR HB2 H 2.865 0.02 1 152 . 15 TYR HB3 H 2.649 0.02 1 153 . 15 TYR C C 175.75 0.05 1 154 . 15 TYR CA C 62.521 0.05 1 155 . 15 TYR CB C 39.014 0.05 1 156 . 15 TYR N N 125.52 0.05 1 157 . 16 GLY H H 8.457 0.02 1 158 . 16 GLY HA2 H 4.445 0.02 2 159 . 16 GLY HA3 H 3.473 0.02 2 160 . 16 GLY C C 174.38 0.05 1 161 . 16 GLY CA C 44.722 0.05 1 162 . 16 GLY N N 107.93 0.05 1 163 . 17 GLY H H 8.478 0.02 1 164 . 17 GLY HA2 H 4.181 0.02 2 165 . 17 GLY HA3 H 3.783 0.02 2 166 . 17 GLY C C 175.08 0.05 1 167 . 17 GLY CA C 44.034 0.05 1 168 . 17 GLY N N 113.21 0.05 1 169 . 18 ASP H H 8.727 0.02 1 170 . 18 ASP HA H 4.901 0.02 1 171 . 18 ASP HB2 H 2.768 0.02 1 172 . 18 ASP HB3 H 2.456 0.02 1 173 . 18 ASP C C 177.07 0.05 1 174 . 18 ASP CA C 53.512 0.05 1 175 . 18 ASP CB C 38.793 0.05 1 176 . 18 ASP N N 123.10 0.05 1 177 . 19 VAL H H 7.137 0.02 1 178 . 19 VAL HA H 3.855 0.02 1 179 . 19 VAL HB H 0.280 0.02 1 180 . 19 VAL HG1 H 0.469 0.02 1 181 . 19 VAL HG2 H 0.127 0.02 1 182 . 19 VAL C C 176.85 0.05 1 183 . 19 VAL CA C 60.635 0.05 1 184 . 19 VAL CB C 31.844 0.05 1 185 . 19 VAL CG1 C 20.543 0.05 1 186 . 19 VAL CG2 C 18.054 0.05 1 187 . 19 VAL N N 112.03 0.05 1 188 . 20 GLY H H 8.305 0.02 1 189 . 20 GLY HA2 H 3.689 0.02 2 190 . 20 GLY HA3 H 2.977 0.02 2 191 . 20 GLY C C 174.26 0.05 1 192 . 20 GLY CA C 48.137 0.05 1 193 . 20 GLY N N 110.14 0.05 1 194 . 21 PHE H H 8.770 0.02 1 195 . 21 PHE HA H 3.649 0.02 1 196 . 21 PHE HB2 H 3.013 0.02 1 197 . 21 PHE HB3 H 2.882 0.02 1 198 . 21 PHE C C 178.17 0.05 1 199 . 21 PHE CA C 63.156 0.05 1 200 . 21 PHE CB C 38.697 0.05 1 201 . 21 PHE N N 123.76 0.05 1 202 . 22 GLY H H 8.480 0.02 1 203 . 22 GLY HA2 H 3.812 0.02 1 204 . 22 GLY HA3 H 3.812 0.02 1 205 . 22 GLY C C 175.69 0.05 1 206 . 22 GLY CA C 46.485 0.05 1 207 . 22 GLY N N 107.01 0.05 1 208 . 23 PHE H H 7.898 0.02 1 209 . 23 PHE HA H 4.746 0.02 1 210 . 23 PHE HB2 H 2.933 0.02 2 211 . 23 PHE HB3 H 2.680 0.02 2 212 . 23 PHE C C 178.23 0.05 1 213 . 23 PHE CA C 54.720 0.05 1 214 . 23 PHE CB C 36.779 0.05 1 215 . 23 PHE N N 115.85 0.05 1 216 . 24 CYS H H 8.175 0.02 1 217 . 24 CYS HA H 4.908 0.02 1 218 . 24 CYS HB2 H 2.83 0.02 1 219 . 24 CYS HB3 H 2.55 0.02 1 220 . 24 CYS C C 173.28 0.05 1 221 . 24 CYS CA C 56.840 0.05 1 222 . 24 CYS CB C 45.666 0.05 1 223 . 24 CYS N N 119.11 0.05 1 224 . 25 ALA H H 8.604 0.02 1 225 . 25 ALA CA C 55.236 0.05 1 226 . 25 ALA N N 125.68 0.05 1 227 . 27 ARG HA H 4.272 0.02 1 228 . 27 ARG HB2 H 1.801 0.02 1 229 . 27 ARG HB3 H 1.739 0.02 1 230 . 27 ARG HG2 H 1.635 0.02 2 231 . 27 ARG HG3 H 1.523 0.02 2 232 . 27 ARG HD2 H 3.153 0.02 1 233 . 27 ARG HD3 H 3.153 0.02 1 234 . 27 ARG HE H 7.040 0.02 1 235 . 27 ARG CA C 55.338 0.05 1 236 . 27 ARG CB C 27.93 0.05 1 237 . 27 ARG CG C 26.469 0.05 1 238 . 27 ARG CD C 43.259 0.05 1 239 . 28 ILE H H 7.345 0.02 1 240 . 28 ILE HA H 4.156 0.02 1 241 . 28 ILE HB H 1.554 0.02 1 242 . 28 ILE HG12 H 1.312 0.02 2 243 . 28 ILE HG13 H 0.929 0.02 2 244 . 28 ILE HG2 H 0.792 0.02 1 245 . 28 ILE HD1 H 0.765 0.02 1 246 . 28 ILE CA C 59.530 0.05 1 247 . 28 ILE CB C 41.016 0.05 1 248 . 28 ILE CG1 C 27.028 0.05 1 249 . 28 ILE CG2 C 16.061 0.05 1 250 . 28 ILE CD1 C 13.065 0.05 1 251 . 28 ILE N N 125.06 0.05 1 252 . 29 PHE H H 8.102 0.02 1 253 . 29 PHE CA C 54.462 0.05 1 254 . 29 PHE CB C 42.168 0.05 1 255 . 29 PHE N N 125.52 0.05 1 256 . 30 PRO HA H 3.712 0.02 1 257 . 30 PRO HB2 H 1.449 0.02 1 258 . 30 PRO HB3 H 1.237 0.02 1 259 . 30 PRO HG2 H 1.449 0.02 2 260 . 30 PRO HG3 H 1.168 0.02 2 261 . 30 PRO HD2 H 3.229 0.02 2 262 . 30 PRO HD3 H 3.053 0.02 2 263 . 30 PRO C C 175.36 0.05 1 264 . 30 PRO CA C 62.685 0.05 1 265 . 30 PRO CB C 34.247 0.05 1 266 . 30 PRO CG C 24.93 0.05 1 267 . 30 PRO CD C 49.244 0.05 1 268 . 31 THR H H 8.309 0.02 1 269 . 31 THR HA H 4.159 0.02 1 270 . 31 THR HB H 4.570 0.02 1 271 . 31 THR HG2 H 1.682 0.02 1 272 . 31 THR C C 175.42 0.05 1 273 . 31 THR CA C 62.098 0.05 1 274 . 31 THR CB C 71.837 0.05 1 275 . 31 THR CG2 C 22.108 0.05 1 276 . 31 THR N N 110.76 0.05 1 277 . 32 ILE H H 8.259 0.02 1 278 . 32 ILE HA H 3.474 0.02 1 279 . 32 ILE HB H 2.048 0.02 1 280 . 32 ILE HG12 H 1.580 0.02 2 281 . 32 ILE HG13 H 1.033 0.02 2 282 . 32 ILE HG2 H 0.303 0.02 1 283 . 32 ILE HD1 H 0.833 0.02 1 284 . 32 ILE C C 177.61 0.05 1 285 . 32 ILE CA C 64.933 0.05 1 286 . 32 ILE CB C 36.536 0.05 1 287 . 32 ILE CG1 C 28.788 0.05 1 288 . 32 ILE CG2 C 18.187 0.05 1 289 . 32 ILE CD1 C 18.187 0.05 1 290 . 32 ILE N N 121.66 0.05 1 291 . 33 CYS H H 7.154 0.02 1 292 . 33 CYS HA H 3.891 0.02 1 293 . 33 CYS HB2 H 2.865 0.02 1 294 . 33 CYS HB3 H 2.700 0.02 1 295 . 33 CYS C C 173.40 0.05 1 296 . 33 CYS CA C 58.473 0.05 1 297 . 33 CYS CB C 37.937 0.05 1 298 . 33 CYS N N 115.09 0.05 1 299 . 34 TYR H H 7.813 0.02 1 300 . 34 TYR HA H 3.373 0.02 1 301 . 34 TYR HB2 H 3.401 0.02 1 302 . 34 TYR HB3 H 2.825 0.02 1 303 . 34 TYR C C 176.25 0.05 1 304 . 34 TYR CA C 62.219 0.05 1 305 . 34 TYR CB C 37.994 0.05 1 306 . 34 TYR N N 121.82 0.05 1 307 . 35 THR H H 7.987 0.02 1 308 . 35 THR HA H 3.584 0.02 1 309 . 35 THR HB H 3.942 0.02 1 310 . 35 THR HG2 H 1.058 0.02 1 311 . 35 THR C C 176.52 0.05 1 312 . 35 THR CA C 66.731 0.05 1 313 . 35 THR CB C 68.614 0.05 1 314 . 35 THR CG2 C 21.906 0.05 1 315 . 35 THR N N 117.55 0.05 1 316 . 36 ARG H H 9.190 0.02 1 317 . 36 ARG HA H 3.962 0.02 1 318 . 36 ARG HB2 H 1.474 0.02 1 319 . 36 ARG HB3 H 1.236 0.02 1 320 . 36 ARG HD2 H 2.879 0.02 2 321 . 36 ARG HD3 H 2.501 0.02 2 322 . 36 ARG HE H 6.874 0.02 1 323 . 36 ARG C C 180.40 0.05 1 324 . 36 ARG CA C 58.123 0.05 1 325 . 36 ARG CB C 28.906 0.05 1 326 . 36 ARG CG C 26.842 0.05 1 327 . 36 ARG N N 121.56 0.05 1 328 . 37 CYS H H 8.588 0.02 1 329 . 37 CYS HA H 4.136 0.02 1 330 . 37 CYS HB2 H 2.695 0.02 1 331 . 37 CYS HB3 H 2.310 0.02 1 332 . 37 CYS C C 177.51 0.05 1 333 . 37 CYS CA C 60.232 0.05 1 334 . 37 CYS CB C 37.353 0.05 1 335 . 37 CYS N N 120.37 0.05 1 336 . 38 ARG H H 7.341 0.02 1 337 . 38 ARG HA H 3.934 0.02 1 338 . 38 ARG HB2 H 1.664 0.02 1 339 . 38 ARG HB3 H 1.534 0.02 1 340 . 38 ARG HG2 H 1.007 0.02 2 341 . 38 ARG HG3 H 0.864 0.02 2 342 . 38 ARG HD2 H 2.647 0.02 2 343 . 38 ARG HD3 H 2.395 0.02 2 344 . 38 ARG C C 178.69 0.05 1 345 . 38 ARG CA C 59.439 0.05 1 346 . 38 ARG CB C 30.219 0.05 1 347 . 38 ARG CG C 26.523 0.05 1 348 . 38 ARG CD C 43.763 0.05 1 349 . 38 ARG N N 120.85 0.05 1 350 . 39 GLU H H 8.533 0.02 1 351 . 39 GLU HA H 3.955 0.02 1 352 . 39 GLU HB2 H 1.932 0.02 1 353 . 39 GLU HB3 H 1.885 0.02 1 354 . 39 GLU HG2 H 2.428 0.02 2 355 . 39 GLU HG3 H 2.200 0.02 2 356 . 39 GLU C C 178.45 0.05 1 357 . 39 GLU CA C 58.817 0.05 1 358 . 39 GLU CB C 30.238 0.05 1 359 . 39 GLU CG C 35.735 0.05 1 360 . 39 GLU N N 117.83 0.05 1 361 . 40 ASN H H 8.673 0.02 1 362 . 40 ASN HA H 4.970 0.02 1 363 . 40 ASN HB2 H 3.095 0.02 1 364 . 40 ASN HB3 H 2.901 0.02 1 365 . 40 ASN C C 176.71 0.05 1 366 . 40 ASN CA C 54.018 0.05 1 367 . 40 ASN CB C 39.767 0.05 1 368 . 40 ASN N N 113.80 0.05 1 369 . 41 LYS H H 6.987 0.02 1 370 . 41 LYS HA H 4.758 0.02 1 371 . 41 LYS HB2 H 2.400 0.02 1 372 . 41 LYS HB3 H 2.109 0.02 1 373 . 41 LYS HG2 H 1.443 0.02 1 374 . 41 LYS HD2 H 1.396 0.02 2 375 . 41 LYS HD3 H 1.330 0.02 2 376 . 41 LYS HE2 H 2.184 0.02 2 377 . 41 LYS HE3 H 2.125 0.02 2 378 . 41 LYS C C 177.09 0.05 1 379 . 41 LYS CA C 53.532 0.05 1 380 . 41 LYS CB C 32.529 0.05 1 381 . 41 LYS CG C 24.834 0.05 1 382 . 41 LYS CD C 27.640 0.05 1 383 . 41 LYS CE C 41.235 0.05 1 384 . 41 LYS N N 115.11 0.05 1 385 . 42 GLY H H 7.508 0.02 1 386 . 42 GLY HA2 H 3.918 0.02 1 387 . 42 GLY HA3 H 3.918 0.02 1 388 . 42 GLY C C 174.33 0.05 1 389 . 42 GLY CA C 46.364 0.05 1 390 . 42 GLY N N 108.62 0.05 1 391 . 43 ALA H H 7.175 0.02 1 392 . 43 ALA HA H 3.822 0.02 1 393 . 43 ALA HB H 0.457 0.02 1 394 . 43 ALA C C 175.31 0.05 1 395 . 43 ALA CA C 50.595 0.05 1 396 . 43 ALA CB C 19.485 0.05 1 397 . 43 ALA N N 121.18 0.05 1 398 . 44 LYS H H 7.910 0.02 1 399 . 44 LYS HA H 4.029 0.02 1 400 . 44 LYS HB2 H 1.484 0.02 1 401 . 44 LYS HB3 H 1.275 0.02 1 402 . 44 LYS HG2 H 1.194 0.02 1 403 . 44 LYS HG3 H 1.194 0.02 1 404 . 44 LYS HD2 H 1.376 0.02 2 405 . 44 LYS HD3 H 1.194 0.02 2 406 . 44 LYS HE2 H 2.825 0.02 1 407 . 44 LYS HE3 H 2.825 0.02 1 408 . 44 LYS C C 176.63 0.05 1 409 . 44 LYS CA C 56.840 0.05 1 410 . 44 LYS CB C 32.838 0.05 1 411 . 44 LYS CG C 25.233 0.05 1 412 . 44 LYS CD C 28.726 0.05 1 413 . 44 LYS CE C 42.081 0.05 1 414 . 44 LYS N N 117.65 0.05 1 415 . 45 GLY H H 7.314 0.02 1 416 . 45 GLY HA2 H 3.912 0.02 2 417 . 45 GLY HA3 H 2.950 0.02 2 418 . 45 GLY C C 172.23 0.05 1 419 . 45 GLY CA C 45.150 0.05 1 420 . 45 GLY N N 105.25 0.05 1 421 . 46 GLY H H 7.462 0.02 1 422 . 46 GLY HA2 H 4.815 0.02 2 423 . 46 GLY HA3 H 3.834 0.02 2 424 . 46 GLY C C 170.89 0.05 1 425 . 46 GLY CA C 46.355 0.05 1 426 . 46 GLY N N 110.79 0.05 1 427 . 47 ARG H H 9.670 0.02 1 428 . 47 ARG HA H 4.696 0.02 1 429 . 47 ARG HB2 H 1.899 0.02 1 430 . 47 ARG HB3 H 1.693 0.02 1 431 . 47 ARG HG2 H 1.527 0.02 2 432 . 47 ARG HG3 H 1.53 0.02 2 433 . 47 ARG HD2 H 3.186 0.02 2 434 . 47 ARG HD3 H 3.063 0.02 2 435 . 47 ARG HE H 7.335 0.02 1 436 . 47 ARG C C 173.31 0.05 1 437 . 47 ARG CA C 54.236 0.05 1 438 . 47 ARG CB C 33.447 0.05 1 439 . 47 ARG CG C 26.422 0.05 1 440 . 47 ARG CD C 43.332 0.05 1 441 . 47 ARG N N 121.86 0.05 1 442 . 47 ARG NE N 124.06 0.05 1 443 . 48 CYS H H 8.857 0.02 1 444 . 48 CYS HA H 5.143 0.02 1 445 . 48 CYS HB2 H 3.332 0.02 1 446 . 48 CYS HB3 H 2.214 0.02 1 447 . 48 CYS C C 174.08 0.05 1 448 . 48 CYS CA C 56.823 0.05 1 449 . 48 CYS CB C 45.750 0.05 1 450 . 48 CYS N N 123.23 0.05 1 451 . 49 ARG H H 8.966 0.02 1 452 . 49 ARG HA H 4.734 0.02 1 453 . 49 ARG HB2 H 1.689 0.02 2 454 . 49 ARG HB3 H 1.471 0.02 2 455 . 49 ARG HG2 H 1.905 0.02 2 456 . 49 ARG HG3 H 1.520 0.02 2 457 . 49 ARG HD2 H 3.171 0.02 2 458 . 49 ARG HD3 H 3.077 0.02 2 459 . 49 ARG HE H 7.568 0.02 1 460 . 49 ARG C C 175.04 0.05 1 461 . 49 ARG CA C 54.448 0.05 1 462 . 49 ARG CB C 31.978 0.05 1 463 . 49 ARG CG C 26.219 0.05 1 464 . 49 ARG CD C 43.322 0.05 1 465 . 49 ARG N N 127.08 0.05 1 466 . 50 TRP H H 9.310 0.02 1 467 . 50 TRP HA H 4.372 0.02 1 468 . 50 TRP HB2 H 3.417 0.02 1 469 . 50 TRP HB3 H 3.088 0.02 1 470 . 50 TRP C C 176.78 0.05 1 471 . 50 TRP CA C 58.468 0.05 1 472 . 50 TRP CB C 29.479 0.05 1 473 . 50 TRP N N 133.19 0.05 1 474 . 50 TRP NE1 N 130.6 0.05 1 475 . 51 GLY H H 8.715 0.02 1 476 . 51 GLY HA2 H 4.443 0.02 2 477 . 51 GLY HA3 H 3.614 0.02 2 478 . 51 GLY C C 173.52 0.05 1 479 . 51 GLY CA C 44.401 0.05 1 480 . 51 GLY N N 114.21 0.05 1 481 . 52 GLN H H 8.675 0.02 1 482 . 52 GLN HA H 4.366 0.02 1 483 . 52 GLN HB2 H 2.072 0.02 1 484 . 52 GLN HB3 H 1.963 0.02 1 485 . 52 GLN HG2 H 2.379 0.02 1 486 . 52 GLN HG3 H 2.379 0.02 1 487 . 52 GLN HE21 H 7.525 0.02 1 488 . 52 GLN HE22 H 6.836 0.02 1 489 . 52 GLN C C 177.42 0.05 1 490 . 52 GLN CA C 55.647 0.05 1 491 . 52 GLN CB C 29.298 0.05 1 492 . 52 GLN CG C 33.899 0.05 1 493 . 52 GLN CD C 180.48 0.05 1 494 . 52 GLN N N 123.96 0.05 1 495 . 52 GLN NE2 N 113.55 0.05 1 496 . 53 GLY H H 8.848 0.02 1 497 . 53 GLY HA2 H 3.915 0.02 1 498 . 53 GLY HA3 H 3.765 0.02 1 499 . 53 GLY C C 174.98 0.05 1 500 . 53 GLY CA C 46.925 0.05 1 501 . 53 GLY N N 113.77 0.05 1 502 . 54 SER H H 8.661 0.02 1 503 . 54 SER HA H 4.629 0.02 1 504 . 54 SER HB2 H 3.858 0.02 1 505 . 54 SER HB3 H 3.858 0.02 1 506 . 54 SER C C 173.69 0.05 1 507 . 54 SER CA C 57.882 0.05 1 508 . 54 SER CB C 62.993 0.05 1 509 . 54 SER N N 120.30 0.05 1 510 . 55 ASN H H 7.899 0.02 1 511 . 55 ASN HA H 4.606 0.02 1 512 . 55 ASN HB2 H 2.884 0.02 1 513 . 55 ASN HB3 H 2.743 0.02 1 514 . 55 ASN HD21 H 7.617 0.02 1 515 . 55 ASN HD22 H 6.929 0.02 1 516 . 55 ASN C C 173.35 0.05 1 517 . 55 ASN CA C 53.611 0.05 1 518 . 55 ASN CB C 38.964 0.05 1 519 . 55 ASN CG C 177.41 0.05 1 520 . 55 ASN N N 121.55 0.05 1 521 . 55 ASN ND2 N 114.81 0.05 1 522 . 56 VAL H H 7.914 0.02 1 523 . 56 VAL HA H 4.427 0.02 1 524 . 56 VAL HB H 1.083 0.02 1 525 . 56 VAL HG1 H 0.033 0.02 1 526 . 56 VAL HG2 H -0.623 0.02 1 527 . 56 VAL C C 172.34 0.05 1 528 . 56 VAL CA C 59.370 0.05 1 529 . 56 VAL CB C 32.174 0.05 1 530 . 56 VAL CG1 C 20.058 0.05 1 531 . 56 VAL CG2 C 17.786 0.05 1 532 . 56 VAL N N 123.30 0.05 1 533 . 57 LYS H H 7.688 0.02 1 534 . 57 LYS HA H 4.544 0.02 1 535 . 57 LYS C C 174.26 0.05 1 536 . 57 LYS CA C 53.338 0.05 1 537 . 57 LYS CB C 36.785 0.05 1 538 . 57 LYS CG C 24.661 0.05 1 539 . 57 LYS CD C 29.189 0.05 1 540 . 57 LYS CE C 42.151 0.05 1 541 . 57 LYS N N 124.40 0.05 1 542 . 58 CYS H H 9.514 0.02 1 543 . 58 CYS HA H 4.954 0.02 1 544 . 58 CYS HB2 H 2.757 0.02 1 545 . 58 CYS HB3 H 2.419 0.02 1 546 . 58 CYS C C 172.20 0.05 1 547 . 58 CYS CA C 54.261 0.05 1 548 . 58 CYS CB C 36.946 0.05 1 549 . 58 CYS N N 121.56 0.05 1 550 . 59 LEU H H 9.126 0.02 1 551 . 59 LEU HA H 4.546 0.02 1 552 . 59 LEU HB2 H 1.829 0.02 2 553 . 59 LEU HB3 H 1.041 0.02 2 554 . 59 LEU HG H 1.462 0.02 1 555 . 59 LEU HD1 H 0.757 0.02 2 556 . 59 LEU HD2 H 0.668 0.02 2 557 . 59 LEU C C 175.16 0.05 1 558 . 59 LEU CA C 52.799 0.05 1 559 . 59 LEU CB C 42.959 0.05 1 560 . 59 LEU CG C 26.382 0.05 1 561 . 59 LEU CD1 C 23.846 0.05 1 562 . 59 LEU N N 130.21 0.05 1 563 . 60 CYS H H 8.986 0.02 1 564 . 60 CYS HA H 5.052 0.02 1 565 . 60 CYS HB2 H 2.947 0.02 1 566 . 60 CYS HB3 H 2.358 0.02 1 567 . 60 CYS C C 172.42 0.05 1 568 . 60 CYS CA C 51.934 0.05 1 569 . 60 CYS CB C 34.253 0.05 1 570 . 60 CYS N N 122.20 0.05 1 571 . 61 ASP H H 7.867 0.02 1 572 . 61 ASP HA H 5.231 0.02 1 573 . 61 ASP HB2 H 2.422 0.02 1 574 . 61 ASP HB3 H 1.952 0.02 1 575 . 61 ASP C C 175.77 0.05 1 576 . 61 ASP CA C 51.866 0.05 1 577 . 61 ASP CB C 42.871 0.05 1 578 . 61 ASP N N 123.02 0.05 1 579 . 62 PHE H H 9.698 0.02 1 580 . 62 PHE HA H 4.288 0.02 1 581 . 62 PHE HB2 H 3.493 0.02 1 582 . 62 PHE HB3 H 2.869 0.02 1 583 . 62 PHE C C 175.38 0.05 1 584 . 62 PHE CA C 59.070 0.05 1 585 . 62 PHE CB C 39.033 0.05 1 586 . 62 PHE N N 125.84 0.05 1 587 . 63 CYS H H 9.189 0.02 1 588 . 63 CYS HA H 4.519 0.02 1 589 . 63 CYS HB2 H 3.656 0.02 1 590 . 63 CYS HB3 H 3.024 0.02 1 591 . 63 CYS C C 174.15 0.05 1 592 . 63 CYS CA C 55.569 0.05 1 593 . 63 CYS CB C 44.204 0.05 1 594 . 63 CYS N N 120.65 0.05 1 595 . 64 GLY H H 8.639 0.02 1 596 . 64 GLY HA2 H 3.932 0.02 2 597 . 64 GLY HA3 H 3.817 0.02 2 598 . 64 GLY C C 172.18 0.05 1 599 . 64 GLY CA C 45.576 0.05 1 600 . 64 GLY N N 111.40 0.05 1 601 . 65 ASP H H 8.091 0.02 1 602 . 65 ASP HA H 4.620 0.02 1 603 . 65 ASP HB2 H 2.735 0.02 1 604 . 65 ASP HB3 H 2.506 0.02 1 605 . 65 ASP C C 176.94 0.05 1 606 . 65 ASP CA C 53.080 0.05 1 607 . 65 ASP CB C 41.639 0.05 1 608 . 65 ASP N N 119.98 0.05 1 609 . 66 THR H H 8.120 0.02 1 610 . 66 THR HA H 4.476 0.02 1 611 . 66 THR HB H 4.057 0.02 1 612 . 66 THR HG2 H 1.208 0.02 1 613 . 66 THR CA C 60.626 0.05 1 614 . 66 THR CB C 69.627 0.05 1 615 . 66 THR N N 119.42 0.05 1 616 . 67 PRO HA H 4.184 0.02 1 617 . 67 PRO HB2 H 1.884 0.02 1 618 . 67 PRO HB3 H 1.779 0.02 1 619 . 67 PRO HG2 H 2.002 0.02 2 620 . 67 PRO HG3 H 1.884 0.02 2 621 . 67 PRO HD2 H 3.890 0.02 2 622 . 67 PRO HD3 H 3.693 0.02 2 623 . 67 PRO CA C 63.536 0.05 1 624 . 67 PRO CB C 31.727 0.05 1 625 . 67 PRO CG C 29.383 0.05 1 626 . 68 GLN H H 7.523 0.02 1 627 . 68 GLN HA H 4.140 0.02 1 628 . 68 GLN HB2 H 2.091 0.02 2 629 . 68 GLN HB3 H 1.924 0.02 2 630 . 68 GLN HG2 H 2.035 0.02 1 631 . 68 GLN HG3 H 2.035 0.02 1 632 . 68 GLN HE21 H 7.474 0.02 2 633 . 68 GLN HE22 H 6.770 0.02 2 634 . 68 GLN CA C 57.344 0.05 1 635 . 68 GLN CB C 31.307 0.05 1 636 . 68 GLN CD C 181.24 0.05 1 637 . 68 GLN N N 126.30 0.05 1 638 . 68 GLN NE2 N 113.56 0.05 1 stop_ save_ ######################## # Coupling constants # ######################## save_HNHA _Saveframe_category coupling_constants _Details . loop_ _Experiment_label HNCA HN(CO)CA HNCACB HNCO C(CO)NH-SE H(CCO)NH-SE HCCH-COSY HCCH-TOCSY stop_ _Sample_conditions_label $cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name ATT _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 ILE HA 4 ILE H 6.70 . . . 2 3JHNHA 5 GLU HA 5 GLU H 5.64 . . . 3 3JHNHA 6 ALA HA 6 ALA H 6.34 . . . 4 3JHNHA 10 GLU HA 10 GLU H 5.92 . . . 5 3JHNHA 12 LEU HA 12 LEU H 8.45 . . . 6 3JHNHA 14 GLU HA 14 GLU H 8.89 . . . 7 3JHNHA 17 GLY HA2 17 GLY H 6.79 . . . 8 3JHNHA 17 GLY HA3 17 GLY H 4.83 . . . 9 3JHNHA 18 ASP HA 18 ASP H 6.48 . . . 10 3JHNHA 19 VAL HA 19 VAL H 8.44 . . . 11 3JHNHA 20 GLY HA2 20 GLY H 5.65 . . . 12 3JHNHA 20 GLY HA3 20 GLY H 5.65 . . . 13 3JHNHA 21 PHE HA 21 PHE H 3.50 . . . 14 3JHNHA 22 GLY HA2 22 GLY H 4.03 . . . 15 3JHNHA 22 GLY HA3 22 GLY H 5.00 . . . 16 3JHNHA 23 PHE HA 23 PHE H 5.29 . . . 17 3JHNHA 24 CYS HA 24 CYS H 9.49 . . . 18 3JHNHA 28 ILE HA 28 ILE H 7.91 . . . 19 3JHNHA 29 PHE HA 29 PHE H 8.14 . . . 20 3JHNHA 31 THR HA 31 THR H 4.07 . . . 21 3JHNHA 32 ILE HA 32 ILE H 3.68 . . . 22 3JHNHA 34 TYR HA 34 TYR H 3.18 . . . 23 3JHNHA 35 THR HA 35 THR H 3.57 . . . 24 3JHNHA 37 CYS HA 37 CYS H 4.03 . . . 25 3JHNHA 39 GLU HA 39 GLU H 4.71 . . . 26 3JHNHA 40 ASN HA 40 ASN H 7.48 . . . 27 3JHNHA 41 LYS HA 41 LYS H 9.58 . . . 28 3JHNHA 42 GLY HA2 42 GLY H 6.57 . . . 29 3JHNHA 42 GLY HA3 42 GLY H 6.57 . . . 30 3JHNHA 43 ALA HA 43 ALA H 6.35 . . . 31 3JHNHA 44 LYS HA 44 LYS H 7.64 . . . 32 3JHNHA 45 GLY HA2 45 GLY H 4.40 . . . 33 3JHNHA 46 GLY HA3 46 GLY H 4.94 . . . 34 3JHNHA 47 ARG HA 47 ARG H 8.75 . . . 35 3JHNHA 48 CYS HA 48 CYS H 7.71 . . . 36 3JHNHA 49 ARG HA 49 ARG H 8.46 . . . 37 3JHNHA 50 TRP HA 50 TRP H 6.55 . . . 38 3JHNHA 51 GLY HA2 51 GLY H 7.69 . . . 39 3JHNHA 51 GLY HA3 51 GLY H 7.69 . . . 40 3JHNHA 52 GLN HA 52 GLN H 6.48 . . . 41 3JHNHA 53 GLY HA2 53 GLY H 2.97 . . . 42 3JHNHA 53 GLY HA3 53 GLY H 5.44 . . . 43 3JHNHA 55 ASN HA 55 ASN H 6.70 . . . 44 3JHNHA 56 VAL HA 56 VAL H 6.53 . . . 45 3JHNHA 57 LYS HA 57 LYS H 9.44 . . . 46 3JHNHA 58 CYS HA 58 CYS H 8.71 . . . 47 3JHNHA 59 LEU HA 59 LEU H 8.74 . . . 48 3JHNHA 60 CYS HA 60 CYS H 7.70 . . . 49 3JHNHA 61 ASP HA 61 ASP H 8.46 . . . 50 3JHNHA 66 THR HA 66 THR H 5.78 . . . stop_ save_