data_4910 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N chemical shift assignments for LEKTI domain one (HF6478) ; _BMRB_accession_number 4910 _BMRB_flat_file_name bmr4910.str _Entry_type original _Submission_date 2000-12-06 _Accession_date 2000-12-06 _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 Lauber Thomas . . 2 Adermann Knut . . 3 Schulz Axel . . 4 Forssmann Wolf Georg . 5 Roesch Paul . . 6 Marx Ute Charlotte . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 632 "15N chemical shifts" 51 "coupling constants" 13 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-11-11 original BMRB . stop_ _Original_release_date 2000-12-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Homologous proteins with different folds: the three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12684009 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lauber Thomas . . 2 Schulz Axel . . 3 Schweimer K. . . 4 Adermann Knut . . 5 Marx Ute Charlotte . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 328 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 205 _Page_last 219 _Year 2003 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _Citation_full . _Citation_title ; NMRView: A computer program for the visualization and analysis of NMR data ; _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 Johnson B. A. . 2 Blevins R. A. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 4 _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 603 _Page_last 614 _Year 1994 _Details . save_ ################################## # Molecular system description # ################################## save_system_HF6478 _Saveframe_category molecular_system _Mol_system_name 'LEKTI domain one' _Abbreviation_common HF6478 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label HF6478 $HF6478_monomer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'putative serine proteinase inhibitor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HF6478_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HF6478 _Abbreviation_common HF6478 _Molecular_mass 6478 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 55 _Mol_residue_sequence ; KNEDQEMCHEFQAFMKNGKL FCPQDKKFFQSLDGIMFINK CATCKMILEKEAKSQ ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 ASN 3 GLU 4 ASP 5 GLN 6 GLU 7 MET 8 CYS 9 HIS 10 GLU 11 PHE 12 GLN 13 ALA 14 PHE 15 MET 16 LYS 17 ASN 18 GLY 19 LYS 20 LEU 21 PHE 22 CYS 23 PRO 24 GLN 25 ASP 26 LYS 27 LYS 28 PHE 29 PHE 30 GLN 31 SER 32 LEU 33 ASP 34 GLY 35 ILE 36 MET 37 PHE 38 ILE 39 ASN 40 LYS 41 CYS 42 ALA 43 THR 44 CYS 45 LYS 46 MET 47 ILE 48 LEU 49 GLU 50 LYS 51 GLU 52 ALA 53 LYS 54 SER 55 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 PDB 1HDL 'Lekti Domain One' 100.00 55 100.00 100.00 1.92e-23 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue $HF6478_monomer human 9606 Eukaryota Metazoa Homo sapiens 'vaginal epithelium' 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_type _Vector_name $HF6478_monomer 'recombinant technology' 'E. coli' Escherichia coli origami DE3 plasmid pET32a 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 $HF6478_monomer 1.5 mM [U-15N] stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HF6478_monomer 1.2 mM . stop_ save_ ############################ # Computer software used # ############################ save_NDEE _Saveframe_category software _Name NDEE _Version . loop_ _Vendor _Address _Electronic_address 'Spinup Inc.' 'Dortmund, Germany.' . stop_ _Details . save_ save_nmrview _Saveframe_category software _Name NMRView _Version 4.1.0 _Details . _Citation_label $ref-1 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D-TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-TOCSY _Sample_label . save_ save_2D-NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-NOESY _Sample_label . save_ save_2D-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-COSY _Sample_label . save_ save_1H-15N-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-HSQC _Sample_label . save_ save_HNHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_3D-1H-15N-TOCSY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-1H-15N-TOCSY-HSQC _Sample_label . save_ save_3D-1H-15N-NOESY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-1H-15N-NOESY-HSQC _Sample_label . save_ save_3D-1H-15N/1H-15N-HMQC-NOESY-HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-1H-15N/1H-15N-HMQC-NOESY-HSQC _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 0.2 n/a temperature 298 1 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 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; several unassigned signals were observed that may correspond to peptide fragments due to self degradation of the protein ; loop_ _Experiment_label 2D-TOCSY 2D-NOESY 2D-COSY 1H-15N-HSQC HNHA 3D-1H-15N-TOCSY-HSQC 3D-1H-15N-NOESY-HSQC 3D-1H-15N/1H-15N-HMQC-NOESY-HSQC stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name HF6478 _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 LYS HA H 4.074 0.02 1 2 . 1 LYS HB2 H 1.932 0.02 1 3 . 1 LYS HB3 H 1.932 0.02 1 4 . 1 LYS HG2 H 1.434 0.02 1 5 . 1 LYS HG3 H 1.434 0.02 1 6 . 1 LYS HD2 H 1.714 0.02 1 7 . 1 LYS HD3 H 1.714 0.02 1 8 . 1 LYS HE2 H 3.011 0.02 1 9 . 1 LYS HE3 H 3.011 0.02 1 10 . 2 ASN HA H 4.698 0.02 2 11 . 2 ASN HB2 H 2.901 0.02 2 12 . 2 ASN HB3 H 2.841 0.02 2 13 . 2 ASN HD21 H 7.677 0.02 2 14 . 2 ASN HD22 H 6.977 0.02 2 15 . 2 ASN ND2 N 112.685 0.2 1 16 . 3 GLU H H 8.949 0.02 1 17 . 3 GLU HA H 4.22 0.02 1 18 . 3 GLU HB2 H 1.969 0.02 1 19 . 3 GLU HB3 H 1.969 0.02 1 20 . 3 GLU HG2 H 2.326 0.02 1 21 . 3 GLU HG3 H 2.326 0.02 1 22 . 3 GLU N N 122.075 0.2 1 23 . 4 ASP H H 8.359 0.02 1 24 . 4 ASP HA H 4.458 0.02 1 25 . 4 ASP HB2 H 2.686 0.02 1 26 . 4 ASP HB3 H 2.686 0.02 1 27 . 4 ASP N N 120.436 0.2 1 28 . 5 GLN H H 8.161 0.02 1 29 . 5 GLN HA H 4.102 0.02 1 30 . 5 GLN HB2 H 2.024 0.02 1 31 . 5 GLN HB3 H 2.024 0.02 1 32 . 5 GLN HG2 H 2.348 0.02 1 33 . 5 GLN HG3 H 2.348 0.02 1 34 . 5 GLN N N 119.264 0.2 1 35 . 6 GLU H H 8.263 0.02 1 36 . 6 GLU HA H 4.116 0.02 1 37 . 6 GLU HB2 H 2.065 0.02 1 38 . 6 GLU HB3 H 2.065 0.02 1 39 . 6 GLU HG2 H 2.328 0.02 1 40 . 6 GLU HG3 H 2.328 0.02 1 41 . 6 GLU N N 120.829 0.2 1 42 . 7 MET H H 8.347 0.02 1 43 . 7 MET HA H 4.353 0.02 1 44 . 7 MET HB2 H 2.211 0.02 1 45 . 7 MET HB3 H 2.211 0.02 1 46 . 7 MET HG2 H 2.686 0.02 1 47 . 7 MET HG3 H 2.686 0.02 1 48 . 7 MET N N 120.436 0.2 1 49 . 11 PHE H H 7.601 0.02 1 50 . 11 PHE HA H 4.729 0.02 1 51 . 11 PHE HB2 H 3.629 0.02 2 52 . 11 PHE HB3 H 2.719 0.02 2 53 . 11 PHE HD1 H 7.105 0.02 1 54 . 11 PHE HD2 H 7.105 0.02 1 55 . 11 PHE N N 116.129 0.2 1 56 . 12 GLN H H 7.563 0.02 1 57 . 12 GLN HA H 3.873 0.02 1 58 . 12 GLN HB2 H 2.105 0.02 1 59 . 12 GLN HB3 H 2.105 0.02 1 60 . 12 GLN HG2 H 2.469 0.02 1 61 . 12 GLN HG3 H 2.469 0.02 1 62 . 12 GLN HE21 H 7.388 0.02 2 63 . 12 GLN HE22 H 6.821 0.02 2 64 . 12 GLN N N 120.496 0.2 1 65 . 12 GLN NE2 N 111.151 0.2 1 66 . 13 ALA H H 8.022 0.02 1 67 . 13 ALA HA H 4.108 0.02 1 68 . 13 ALA HB H 1.029 0.02 1 69 . 13 ALA N N 118.87 0.2 1 70 . 14 PHE H H 7.713 0.02 1 71 . 14 PHE HA H 4.792 0.02 1 72 . 14 PHE HB2 H 3.971 0.02 2 73 . 14 PHE HB3 H 2.961 0.02 2 74 . 14 PHE HD1 H 7.469 0.02 1 75 . 14 PHE HD2 H 7.469 0.02 1 76 . 14 PHE HE1 H 7.561 0.02 1 77 . 14 PHE HE2 H 7.561 0.02 1 78 . 14 PHE N N 115.793 0.2 1 79 . 15 MET H H 7.45 0.02 1 80 . 15 MET HA H 5.177 0.02 1 81 . 15 MET HB2 H 2.136 0.02 2 82 . 15 MET HB3 H 1.998 0.02 2 83 . 15 MET HG2 H 2.684 0.02 2 84 . 15 MET HG3 H 2.38 0.02 2 85 . 15 MET HE H 1.767 0.02 1 86 . 15 MET N N 120.918 0.2 1 87 . 16 LYS H H 9.506 0.02 1 88 . 16 LYS HA H 4.565 0.02 1 89 . 16 LYS HB2 H 1.844 0.02 1 90 . 16 LYS HB3 H 1.844 0.02 1 91 . 16 LYS HG2 H 1.389 0.02 1 92 . 16 LYS HG3 H 1.389 0.02 1 93 . 16 LYS HD2 H 1.573 0.02 1 94 . 16 LYS HD3 H 1.573 0.02 1 95 . 16 LYS HE2 H 2.877 0.02 1 96 . 16 LYS HE3 H 2.877 0.02 1 97 . 16 LYS N N 124.225 0.2 1 98 . 17 ASN H H 9.558 0.02 1 99 . 17 ASN HA H 4.407 0.02 1 100 . 17 ASN HB2 H 3.114 0.02 2 101 . 17 ASN HB3 H 2.842 0.02 2 102 . 17 ASN HD21 H 7.627 0.02 2 103 . 17 ASN HD22 H 6.97 0.02 2 104 . 17 ASN N N 124.885 0.2 1 105 . 17 ASN ND2 N 112.685 0.2 1 106 . 18 GLY H H 8.786 0.02 1 107 . 18 GLY HA2 H 4.146 0.02 2 108 . 18 GLY HA3 H 3.528 0.02 2 109 . 18 GLY N N 103.917 0.2 1 110 . 19 LYS H H 7.713 0.02 1 111 . 19 LYS HA H 4.663 0.02 1 112 . 19 LYS HB2 H 1.758 0.02 2 113 . 19 LYS HB3 H 1.37 0.02 2 114 . 19 LYS HG2 H 1.196 0.02 1 115 . 19 LYS HG3 H 1.196 0.02 1 116 . 19 LYS HD2 H 1.615 0.02 1 117 . 19 LYS HD3 H 1.615 0.02 1 118 . 19 LYS HE2 H 2.95 0.02 1 119 . 19 LYS HE3 H 2.95 0.02 1 120 . 19 LYS N N 119.685 0.2 1 121 . 21 PHE H H 8.179 0.02 1 122 . 21 PHE HA H 4.64 0.02 1 123 . 21 PHE HB2 H 3.082 0.02 1 124 . 21 PHE HB3 H 3.082 0.02 1 125 . 21 PHE HD1 H 7.372 0.02 1 126 . 21 PHE HD2 H 7.372 0.02 1 127 . 21 PHE HE1 H 7.454 0.02 1 128 . 21 PHE HE2 H 7.454 0.02 1 129 . 21 PHE N N 128.064 0.2 1 130 . 22 CYS H H 8.333 0.02 1 131 . 22 CYS HA H 4.299 0.02 1 132 . 22 CYS HB2 H 2.641 0.02 1 133 . 22 CYS HB3 H 2.641 0.02 1 134 . 22 CYS N N 122.885 0.2 1 135 . 24 GLN H H 8.514 0.02 1 136 . 24 GLN HA H 4.578 0.02 1 137 . 24 GLN HB2 H 1.929 0.02 1 138 . 24 GLN HB3 H 1.929 0.02 1 139 . 24 GLN HG2 H 2.346 0.02 1 140 . 24 GLN HG3 H 2.346 0.02 1 141 . 24 GLN HE21 H 7.456 0.02 2 142 . 24 GLN HE22 H 6.83 0.02 2 143 . 24 GLN N N 117.267 0.2 1 144 . 24 GLN NE2 N 112.695 0.2 1 145 . 25 ASP H H 7.984 0.02 1 146 . 25 ASP HA H 4.526 0.02 1 147 . 25 ASP HB3 H 2.682 0.02 1 148 . 25 ASP HB2 H 2.682 0.02 1 149 . 25 ASP N N 119.946 0.2 1 150 . 26 LYS H H 8.632 0.02 1 151 . 26 LYS HA H 4.159 0.02 1 152 . 26 LYS HB2 H 1.89 0.02 1 153 . 26 LYS HB3 H 1.89 0.02 1 154 . 26 LYS HG2 H 1.526 0.02 1 155 . 26 LYS HG3 H 1.526 0.02 1 156 . 26 LYS HD2 H 1.695 0.02 1 157 . 26 LYS HD3 H 1.695 0.02 1 158 . 26 LYS N N 124.086 0.2 1 159 . 27 LYS H H 8.71 0.02 1 160 . 27 LYS HA H 4.096 0.02 1 161 . 27 LYS HB2 H 1.679 0.02 2 162 . 27 LYS HB3 H 1.539 0.02 2 163 . 27 LYS HG2 H 0.992 0.02 2 164 . 27 LYS HG3 H 0.757 0.02 2 165 . 27 LYS HD2 H 1.425 0.02 1 166 . 27 LYS HD3 H 1.425 0.02 1 167 . 27 LYS N N 119.101 0.2 1 168 . 28 PHE H H 7.721 0.02 1 169 . 28 PHE HA H 4.227 0.02 1 170 . 28 PHE HB2 H 2.997 0.02 2 171 . 28 PHE HB3 H 2.607 0.02 2 172 . 28 PHE HD1 H 7.33 0.02 1 173 . 28 PHE HD2 H 7.33 0.02 1 174 . 28 PHE HE1 H 7.257 0.02 1 175 . 28 PHE HE2 H 7.257 0.02 1 176 . 28 PHE N N 118.37 0.2 1 177 . 29 PHE H H 7.523 0.02 1 178 . 29 PHE HA H 4.566 0.02 1 179 . 29 PHE HB2 H 3.416 0.02 2 180 . 29 PHE HB3 H 2.956 0.02 2 181 . 29 PHE HD1 H 7.328 0.02 1 182 . 29 PHE HD2 H 7.328 0.02 1 183 . 29 PHE N N 112.705 0.2 1 184 . 30 GLN H H 7.567 0.02 1 185 . 30 GLN HA H 4.402 0.02 1 186 . 30 GLN HB2 H 2.069 0.02 1 187 . 30 GLN HB3 H 2.069 0.02 1 188 . 30 GLN HG2 H 2.475 0.02 2 189 . 30 GLN HG3 H 2.354 0.02 2 190 . 30 GLN HE21 H 7.439 0.02 2 191 . 30 GLN HE22 H 6.876 0.02 2 192 . 30 GLN N N 115.984 0.2 1 193 . 30 GLN NE2 N 111.769 0.2 1 194 . 31 SER H H 7.719 0.02 1 195 . 31 SER HA H 4.769 0.02 1 196 . 31 SER HB2 H 4.193 0.02 2 197 . 31 SER HB3 H 3.929 0.02 2 198 . 31 SER N N 112.316 0.2 1 199 . 33 ASP H H 8.494 0.02 1 200 . 33 ASP HA H 4.44 0.02 1 201 . 33 ASP HB2 H 2.616 0.02 1 202 . 33 ASP HB3 H 2.616 0.02 1 203 . 33 ASP N N 117.189 0.2 1 204 . 34 GLY H H 8.096 0.02 1 205 . 34 GLY HA2 H 4.419 0.02 2 206 . 34 GLY HA3 H 3.967 0.02 2 207 . 34 GLY N N 111.248 0.2 1 208 . 35 ILE H H 8.052 0.02 1 209 . 35 ILE HA H 3.615 0.02 1 210 . 35 ILE HB H 1.952 0.02 1 211 . 35 ILE HG12 H 1.154 0.02 1 212 . 35 ILE HG13 H 1.154 0.02 1 213 . 35 ILE HG2 H 0.949 0.02 1 214 . 35 ILE HD1 H 0.915 0.02 1 215 . 35 ILE N N 123.229 0.2 1 216 . 36 MET H H 8.358 0.02 1 217 . 36 MET HA H 4.253 0.02 1 218 . 36 MET HB2 H 2.299 0.02 2 219 . 36 MET HB3 H 2.19 0.02 2 220 . 36 MET HG2 H 2.819 0.02 2 221 . 36 MET HG3 H 2.667 0.02 2 222 . 36 MET N N 118.955 0.2 1 223 . 37 PHE H H 8.014 0.02 1 224 . 37 PHE HA H 4.402 0.02 1 225 . 37 PHE HB2 H 3.453 0.02 2 226 . 37 PHE HB3 H 3.342 0.02 2 227 . 37 PHE N N 122.212 0.2 1 228 . 38 ILE H H 8.305 0.02 1 229 . 38 ILE HA H 3.491 0.02 1 230 . 38 ILE HB H 1.94 0.02 1 231 . 38 ILE HG12 H 1.408 0.02 2 232 . 38 ILE HG13 H 1.185 0.02 2 233 . 38 ILE HG2 H 0.829 0.02 1 234 . 38 ILE HD1 H 0.421 0.02 1 235 . 38 ILE N N 119.005 0.2 1 236 . 39 ASN H H 8.449 0.02 1 237 . 39 ASN HA H 4.45 0.02 1 238 . 39 ASN HB2 H 2.88 0.02 1 239 . 39 ASN HB3 H 2.88 0.02 1 240 . 39 ASN N N 121.208 0.2 1 241 . 40 LYS H H 8.401 0.02 1 242 . 40 LYS HA H 3.944 0.02 1 243 . 40 LYS HB2 H 2.022 0.02 2 244 . 40 LYS HB3 H 1.933 0.02 2 245 . 40 LYS HG2 H 1.595 0.02 1 246 . 40 LYS HG3 H 1.595 0.02 1 247 . 40 LYS HD2 H 1.823 0.02 1 248 . 40 LYS HD3 H 1.823 0.02 1 249 . 40 LYS HE2 H 3.039 0.02 1 250 . 40 LYS HE3 H 3.039 0.02 1 251 . 40 LYS N N 123.147 0.2 1 252 . 41 CYS H H 8.01 0.02 1 253 . 41 CYS HA H 3.516 0.02 1 254 . 41 CYS HB2 H 2.865 0.02 2 255 . 41 CYS HB3 H 2.19 0.02 2 256 . 41 CYS N N 120.58 0.2 1 257 . 42 ALA H H 7.675 0.02 1 258 . 42 ALA HA H 3.841 0.02 1 259 . 42 ALA HB H 1.471 0.02 1 260 . 42 ALA N N 120.227 0.2 1 261 . 43 THR H H 7.834 0.02 1 262 . 43 THR HA H 3.955 0.02 1 263 . 43 THR HB H 4.263 0.02 1 264 . 43 THR HG2 H 1.225 0.02 1 265 . 43 THR N N 115.791 0.2 1 266 . 44 CYS H H 8.165 0.02 1 267 . 44 CYS HA H 4.45 0.02 1 268 . 44 CYS HB2 H 2.731 0.02 1 269 . 44 CYS HB3 H 2.731 0.02 1 270 . 44 CYS N N 119.236 0.2 1 271 . 45 LYS H H 8.244 0.02 1 272 . 45 LYS HA H 3.767 0.02 1 273 . 45 LYS HB2 H 1.942 0.02 1 274 . 45 LYS HB3 H 1.942 0.02 1 275 . 45 LYS HG2 H 1.208 0.02 1 276 . 45 LYS HG3 H 1.208 0.02 1 277 . 45 LYS HD2 H 1.703 0.02 1 278 . 45 LYS HD3 H 1.703 0.02 1 279 . 45 LYS N N 123.721 0.2 1 280 . 46 MET H H 7.471 0.02 1 281 . 46 MET HA H 4.206 0.02 1 282 . 46 MET HB2 H 2.19 0.02 1 283 . 46 MET HB3 H 2.19 0.02 1 284 . 46 MET HG2 H 2.697 0.02 2 285 . 46 MET HG3 H 2.609 0.02 2 286 . 46 MET N N 114.914 0.2 1 287 . 47 ILE H H 7.413 0.02 1 288 . 47 ILE HA H 3.796 0.02 1 289 . 47 ILE HB H 1.977 0.02 1 290 . 47 ILE HG12 H 1.7 0.02 2 291 . 47 ILE HG13 H 1.201 0.02 2 292 . 47 ILE HG2 H 0.863 0.02 1 293 . 47 ILE HD1 H 0.881 0.02 1 294 . 47 ILE N N 118.77 0.2 1 295 . 49 GLU H H 8.013 0.02 1 296 . 49 GLU HA H 4.117 0.02 1 297 . 49 GLU HB2 H 2.098 0.02 1 298 . 49 GLU HB3 H 2.098 0.02 1 299 . 49 GLU HG2 H 2.671 0.02 2 300 . 49 GLU HG3 H 2.468 0.02 2 301 . 49 GLU N N 116.888 0.2 1 302 . 50 LYS H H 7.569 0.02 1 303 . 50 LYS HA H 4.214 0.02 1 304 . 50 LYS HB2 H 1.945 0.02 1 305 . 50 LYS HB3 H 1.945 0.02 1 306 . 50 LYS HG2 H 1.508 0.02 1 307 . 50 LYS HG3 H 1.508 0.02 1 308 . 50 LYS HD2 H 1.722 0.02 1 309 . 50 LYS HD3 H 1.722 0.02 1 310 . 50 LYS HE2 H 3.004 0.02 1 311 . 50 LYS HE3 H 3.004 0.02 1 312 . 50 LYS N N 119.836 0.2 1 313 . 51 GLU H H 7.987 0.02 1 314 . 51 GLU HB2 H 2.015 0.02 1 315 . 51 GLU HB3 H 2.015 0.02 1 316 . 51 GLU HG2 H 2.423 0.02 2 317 . 51 GLU HG3 H 2.343 0.02 2 318 . 51 GLU N N 119.829 0.2 1 319 . 52 ALA H H 7.923 0.02 1 320 . 52 ALA HA H 4.238 0.02 1 321 . 52 ALA HB H 1.442 0.02 1 322 . 52 ALA N N 123.279 0.2 1 323 . 53 LYS H H 8.001 0.02 1 324 . 53 LYS HA H 4.33 0.02 1 325 . 53 LYS HB2 H 1.841 0.02 1 326 . 53 LYS HB3 H 1.841 0.02 1 327 . 53 LYS HG2 H 1.457 0.02 1 328 . 53 LYS HG3 H 1.457 0.02 1 329 . 53 LYS HD2 H 1.704 0.02 1 330 . 53 LYS HD3 H 1.704 0.02 1 331 . 53 LYS HE2 H 3.011 0.02 1 332 . 53 LYS HE3 H 3.011 0.02 1 333 . 53 LYS N N 119.569 0.2 1 334 . 54 SER H H 8.255 0.02 1 335 . 54 SER HA H 4.463 0.02 1 336 . 54 SER HB2 H 3.907 0.02 1 337 . 54 SER HB3 H 3.907 0.02 1 338 . 54 SER N N 117.314 0.2 1 339 . 55 GLN H H 7.96 0.02 1 340 . 55 GLN HA H 4.196 0.02 1 341 . 55 GLN HB2 H 2.135 0.02 2 342 . 55 GLN HB3 H 1.962 0.02 2 343 . 55 GLN HG2 H 2.311 0.02 1 344 . 55 GLN HG3 H 2.311 0.02 1 345 . 55 GLN N N 126.692 0.2 1 stop_ save_ save_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details ; several unassigned signals were observed that may correspond to peptide fragments due to self degradation of the protein ; loop_ _Experiment_label 2D-TOCSY 2D-NOESY 2D-COSY 1H-15N-HSQC HNHA 3D-1H-15N-TOCSY-HSQC 3D-1H-15N-NOESY-HSQC 3D-1H-15N/1H-15N-HMQC-NOESY-HSQC stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name HF6478 _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 LYS HA H 4.074 0.02 1 2 . 1 LYS HB2 H 1.932 0.02 1 3 . 1 LYS HB3 H 1.932 0.02 1 4 . 1 LYS HG2 H 1.434 0.02 1 5 . 1 LYS HG3 H 1.434 0.02 1 6 . 1 LYS HD2 H 1.714 0.02 1 7 . 1 LYS HD3 H 1.714 0.02 1 8 . 1 LYS HE2 H 3.011 0.02 1 9 . 1 LYS HE3 H 3.011 0.02 1 10 . 2 ASN HA H 4.707 0.02 1 11 . 2 ASN HB2 H 2.831 0.02 2 12 . 2 ASN HB3 H 2.681 0.02 2 13 . 2 ASN HD21 H 7.681 0.02 2 14 . 2 ASN HD22 H 6.982 0.02 2 15 . 3 GLU H H 8.934 0.02 1 16 . 3 GLU HA H 4.237 0.02 1 17 . 3 GLU HB2 H 2.082 0.02 2 18 . 3 GLU HB3 H 1.972 0.02 2 19 . 3 GLU HG2 H 2.349 0.02 1 20 . 3 GLU HG3 H 2.349 0.02 1 21 . 4 ASP H H 8.376 0.02 1 22 . 4 ASP HA H 4.468 0.02 1 23 . 4 ASP HB2 H 2.709 0.02 1 24 . 4 ASP HB3 H 2.709 0.02 1 25 . 5 GLN H H 8.189 0.02 1 26 . 5 GLN HA H 4.115 0.02 1 27 . 5 GLN HB2 H 2.118 0.02 2 28 . 5 GLN HB3 H 2.027 0.02 2 29 . 5 GLN HG2 H 2.364 0.02 1 30 . 5 GLN HG3 H 2.364 0.02 1 31 . 6 GLU H H 8.268 0.02 1 32 . 6 GLU HA H 4.139 0.02 1 33 . 6 GLU HB2 H 2.062 0.02 1 34 . 6 GLU HB3 H 2.062 0.02 1 35 . 6 GLU HG2 H 2.354 0.02 1 36 . 6 GLU HG3 H 2.354 0.02 1 37 . 7 MET H H 8.357 0.02 1 38 . 7 MET HA H 4.355 0.02 1 39 . 7 MET HB2 H 2.208 0.02 1 40 . 7 MET HB3 H 2.208 0.02 1 41 . 7 MET HG2 H 2.643 0.02 1 42 . 7 MET HG3 H 2.643 0.02 1 43 . 11 PHE H H 7.604 0.02 1 44 . 11 PHE HA H 4.745 0.02 1 45 . 11 PHE HB2 H 3.646 0.02 2 46 . 11 PHE HB3 H 2.727 0.02 2 47 . 11 PHE HD1 H 7.121 0.02 1 48 . 11 PHE HD2 H 7.121 0.02 1 49 . 11 PHE HE1 H 6.602 0.02 1 50 . 11 PHE HE2 H 6.602 0.02 1 51 . 11 PHE HZ H 6.784 0.02 1 52 . 12 GLN H H 7.568 0.02 1 53 . 12 GLN HA H 3.887 0.02 1 54 . 12 GLN HB2 H 2.120 0.02 2 55 . 12 GLN HB3 H 2.078 0.02 2 56 . 12 GLN HG2 H 2.502 0.02 1 57 . 12 GLN HG3 H 2.502 0.02 1 58 . 12 GLN HE21 H 7.397 0.02 2 59 . 12 GLN HE22 H 6.832 0.02 2 60 . 13 ALA H H 8.044 0.02 1 61 . 13 ALA HA H 4.110 0.02 1 62 . 13 ALA HB H 1.036 0.02 1 63 . 14 PHE H H 7.725 0.02 1 64 . 14 PHE HA H 4.795 0.02 1 65 . 14 PHE HB2 H 3.980 0.02 2 66 . 14 PHE HB3 H 2.969 0.02 2 67 . 14 PHE HD1 H 7.469 0.02 1 68 . 14 PHE HD2 H 7.469 0.02 1 69 . 14 PHE HE1 H 7.561 0.02 1 70 . 14 PHE HE2 H 7.561 0.02 1 71 . 15 MET H H 7.453 0.02 1 72 . 15 MET HA H 5.188 0.02 1 73 . 15 MET HB2 H 2.141 0.02 2 74 . 15 MET HB3 H 1.992 0.02 2 75 . 15 MET HG2 H 2.689 0.02 2 76 . 15 MET HG3 H 2.382 0.02 2 77 . 16 LYS H H 9.507 0.02 1 78 . 16 LYS HA H 4.587 0.02 1 79 . 16 LYS HB2 H 1.856 0.02 1 80 . 16 LYS HB3 H 1.856 0.02 1 81 . 16 LYS HG2 H 1.433 0.02 2 82 . 16 LYS HG3 H 1.390 0.02 2 83 . 16 LYS HD2 H 1.573 0.02 1 84 . 16 LYS HD3 H 1.573 0.02 1 85 . 16 LYS HE2 H 2.877 0.02 1 86 . 16 LYS HE3 H 2.877 0.02 1 87 . 17 ASN H H 9.556 0.02 1 88 . 17 ASN HA H 4.417 0.02 1 89 . 17 ASN HB2 H 3.112 0.02 2 90 . 17 ASN HB3 H 2.858 0.02 2 91 . 17 ASN HD21 H 7.635 0.02 2 92 . 17 ASN HD22 H 6.977 0.02 2 93 . 18 GLY H H 8.785 0.02 1 94 . 18 GLY HA2 H 4.148 0.02 2 95 . 18 GLY HA3 H 3.532 0.02 2 96 . 19 LYS H H 7.721 0.02 1 97 . 19 LYS HA H 4.667 0.02 1 98 . 19 LYS HB2 H 1.761 0.02 1 99 . 19 LYS HB3 H 1.761 0.02 1 100 . 19 LYS HG2 H 1.387 0.02 2 101 . 19 LYS HG3 H 1.199 0.02 2 102 . 19 LYS HD2 H 1.604 0.02 1 103 . 19 LYS HD3 H 1.604 0.02 1 104 . 19 LYS HE2 H 2.966 0.02 1 105 . 19 LYS HE3 H 2.966 0.02 1 106 . 20 LEU H H 8.627 0.02 1 107 . 20 LEU HA H 4.529 0.02 1 108 . 20 LEU HB2 H 1.723 0.02 2 109 . 20 LEU HB3 H 1.287 0.02 2 110 . 20 LEU HG H 1.424 0.02 1 111 . 20 LEU HD1 H 0.919 0.02 2 112 . 20 LEU HD2 H 0.715 0.02 2 113 . 21 PHE H H 8.188 0.02 1 114 . 21 PHE HA H 4.661 0.02 1 115 . 21 PHE HB2 H 3.085 0.02 1 116 . 21 PHE HB3 H 3.085 0.02 1 117 . 21 PHE HD1 H 7.372 0.02 1 118 . 21 PHE HD2 H 7.372 0.02 1 119 . 21 PHE HE1 H 7.454 0.02 1 120 . 21 PHE HE2 H 7.454 0.02 1 121 . 21 PHE HZ H 7.319 0.02 1 122 . 22 CYS H H 8.336 0.02 1 123 . 22 CYS HA H 4.305 0.02 1 124 . 22 CYS HB2 H 2.651 0.02 1 125 . 22 CYS HB3 H 2.651 0.02 1 126 . 23 PRO HA H 4.310 0.02 1 127 . 23 PRO HB2 H 2.329 0.02 2 128 . 23 PRO HB3 H 1.938 0.02 2 129 . 23 PRO HG2 H 1.841 0.02 2 130 . 23 PRO HG3 H 1.594 0.02 2 131 . 23 PRO HD2 H 3.109 0.02 2 132 . 23 PRO HD3 H 2.981 0.02 2 133 . 24 GLN H H 8.524 0.02 1 134 . 24 GLN HA H 4.589 0.02 1 135 . 24 GLN HB2 H 1.942 0.02 1 136 . 24 GLN HB3 H 1.942 0.02 1 137 . 24 GLN HG2 H 2.388 0.02 2 138 . 24 GLN HG3 H 2.326 0.02 2 139 . 24 GLN HE21 H 7.464 0.02 2 140 . 24 GLN HE22 H 6.841 0.02 2 141 . 25 ASP H H 7.986 0.02 1 142 . 25 ASP HA H 4.518 0.02 1 143 . 25 ASP HB2 H 2.701 0.02 1 144 . 25 ASP HB3 H 2.701 0.02 1 145 . 26 LYS H H 8.624 0.02 1 146 . 26 LYS HA H 4.150 0.02 1 147 . 26 LYS HB2 H 1.817 0.02 1 148 . 26 LYS HB3 H 1.817 0.02 1 149 . 26 LYS HG2 H 1.539 0.02 1 150 . 26 LYS HG3 H 1.539 0.02 1 151 . 26 LYS HD2 H 1.660 0.02 1 152 . 26 LYS HD3 H 1.660 0.02 1 153 . 27 LYS H H 8.708 0.02 1 154 . 27 LYS HA H 4.101 0.02 1 155 . 27 LYS HB2 H 1.682 0.02 2 156 . 27 LYS HB3 H 1.547 0.02 2 157 . 27 LYS HG2 H 1.008 0.02 2 158 . 27 LYS HG3 H 0.783 0.02 2 159 . 27 LYS HD2 H 1.411 0.02 1 160 . 27 LYS HD3 H 1.411 0.02 1 161 . 27 LYS HE2 H 2.686 0.02 1 162 . 27 LYS HE3 H 2.686 0.02 1 163 . 28 PHE H H 7.728 0.02 1 164 . 28 PHE HA H 4.231 0.02 1 165 . 28 PHE HB2 H 3.003 0.02 2 166 . 28 PHE HB3 H 2.613 0.02 2 167 . 28 PHE HD1 H 7.330 0.02 1 168 . 28 PHE HD2 H 7.330 0.02 1 169 . 28 PHE HE1 H 7.257 0.02 1 170 . 28 PHE HE2 H 7.257 0.02 1 171 . 28 PHE HZ H 7.368 0.02 1 172 . 29 PHE H H 7.533 0.02 1 173 . 29 PHE HA H 4.574 0.02 1 174 . 29 PHE HB2 H 3.422 0.02 2 175 . 29 PHE HB3 H 2.963 0.02 2 176 . 29 PHE HD1 H 7.328 0.02 1 177 . 29 PHE HD2 H 7.328 0.02 1 178 . 30 GLN H H 7.570 0.02 1 179 . 30 GLN HA H 4.411 0.02 1 180 . 30 GLN HB2 H 2.078 0.02 1 181 . 30 GLN HB3 H 2.078 0.02 1 182 . 30 GLN HG2 H 2.497 0.02 2 183 . 30 GLN HG3 H 2.355 0.02 2 184 . 30 GLN HE21 H 7.449 0.02 2 185 . 30 GLN HE22 H 6.884 0.02 2 186 . 31 SER H H 7.724 0.02 1 187 . 31 SER HA H 4.792 0.02 1 188 . 31 SER HB2 H 4.201 0.02 2 189 . 31 SER HB3 H 3.938 0.02 2 190 . 32 LEU H H 8.831 0.02 1 191 . 32 LEU HA H 4.217 0.02 1 192 . 32 LEU HB2 H 1.763 0.02 1 193 . 32 LEU HB3 H 1.763 0.02 1 194 . 32 LEU HG H 1.705 0.02 1 195 . 32 LEU HD1 H 0.997 0.02 2 196 . 32 LEU HD2 H 0.950 0.02 2 197 . 33 ASP H H 8.496 0.02 1 198 . 33 ASP HA H 4.466 0.02 1 199 . 33 ASP HB2 H 2.619 0.02 1 200 . 33 ASP HB3 H 2.619 0.02 1 201 . 34 GLY H H 8.107 0.02 1 202 . 34 GLY HA2 H 4.422 0.02 2 203 . 34 GLY HA3 H 3.977 0.02 2 204 . 35 ILE H H 8.062 0.02 1 205 . 35 ILE HA H 3.631 0.02 1 206 . 35 ILE HB H 1.960 0.02 1 207 . 35 ILE HG12 H 1.161 0.02 1 208 . 35 ILE HG13 H 1.161 0.02 1 209 . 35 ILE HG2 H 0.949 0.02 1 210 . 35 ILE HD1 H 0.915 0.02 1 211 . 36 MET H H 8.355 0.02 1 212 . 36 MET HA H 4.271 0.02 1 213 . 36 MET HB2 H 2.314 0.02 2 214 . 36 MET HB3 H 2.207 0.02 2 215 . 36 MET HG2 H 2.828 0.02 2 216 . 36 MET HG3 H 2.678 0.02 2 217 . 37 PHE H H 8.023 0.02 1 218 . 37 PHE HA H 4.398 0.02 1 219 . 37 PHE HB2 H 3.467 0.02 2 220 . 37 PHE HB3 H 3.351 0.02 2 221 . 37 PHE HD1 H 7.209 0.02 1 222 . 37 PHE HD2 H 7.209 0.02 1 223 . 37 PHE HE1 H 7.032 0.02 1 224 . 37 PHE HE2 H 7.032 0.02 1 225 . 37 PHE HZ H 7.082 0.02 1 226 . 38 ILE H H 8.310 0.02 1 227 . 38 ILE HA H 3.529 0.02 1 228 . 38 ILE HB H 1.948 0.02 1 229 . 38 ILE HG12 H 1.413 0.02 2 230 . 38 ILE HG13 H 1.201 0.02 2 231 . 38 ILE HG2 H 0.834 0.02 1 232 . 38 ILE HD1 H 0.432 0.02 1 233 . 39 ASN H H 8.463 0.02 1 234 . 39 ASN HA H 4.473 0.02 1 235 . 39 ASN HB2 H 2.902 0.02 2 236 . 39 ASN HB3 H 2.801 0.02 2 237 . 39 ASN HD21 H 7.486 0.02 2 238 . 39 ASN HD22 H 6.898 0.02 2 239 . 40 LYS H H 8.401 0.02 1 240 . 40 LYS HA H 3.965 0.02 1 241 . 40 LYS HB2 H 2.022 0.02 2 242 . 40 LYS HB3 H 1.933 0.02 2 243 . 40 LYS HG2 H 1.624 0.02 1 244 . 40 LYS HG3 H 1.624 0.02 1 245 . 40 LYS HD2 H 1.823 0.02 1 246 . 40 LYS HD3 H 1.823 0.02 1 247 . 40 LYS HE2 H 3.040 0.02 1 248 . 40 LYS HE3 H 3.040 0.02 1 249 . 41 CYS H H 8.018 0.02 1 250 . 41 CYS HA H 3.527 0.02 1 251 . 41 CYS HB2 H 2.877 0.02 2 252 . 41 CYS HB3 H 2.188 0.02 2 253 . 42 ALA H H 7.688 0.02 1 254 . 42 ALA HA H 3.848 0.02 1 255 . 42 ALA HB H 1.477 0.02 1 256 . 43 THR H H 7.835 0.02 1 257 . 43 THR HA H 3.973 0.02 1 258 . 43 THR HB H 4.267 0.02 1 259 . 43 THR HG2 H 1.223 0.02 1 260 . 44 CYS H H 8.151 0.02 1 261 . 44 CYS HA H 4.459 0.02 1 262 . 44 CYS HB2 H 2.782 0.02 2 263 . 44 CYS HB3 H 2.691 0.02 2 264 . 45 LYS H H 8.243 0.02 1 265 . 45 LYS HA H 3.776 0.02 1 266 . 45 LYS HB2 H 1.958 0.02 1 267 . 45 LYS HB3 H 1.958 0.02 1 268 . 45 LYS HG2 H 1.203 0.02 1 269 . 45 LYS HG3 H 1.203 0.02 1 270 . 45 LYS HD2 H 1.714 0.02 1 271 . 45 LYS HD3 H 1.714 0.02 1 272 . 45 LYS HE2 H 2.774 0.02 1 273 . 45 LYS HE3 H 2.774 0.02 1 274 . 46 MET H H 7.507 0.02 1 275 . 46 MET HA H 4.220 0.02 1 276 . 46 MET HB2 H 2.202 0.02 1 277 . 46 MET HB3 H 2.202 0.02 1 278 . 46 MET HG2 H 2.706 0.02 2 279 . 46 MET HG3 H 2.605 0.02 2 280 . 47 ILE H H 7.438 0.02 1 281 . 47 ILE HA H 3.779 0.02 1 282 . 47 ILE HB H 1.994 0.02 1 283 . 47 ILE HG12 H 1.710 0.02 2 284 . 47 ILE HG13 H 1.205 0.02 2 285 . 47 ILE HG2 H 0.883 0.02 1 286 . 47 ILE HD1 H 0.862 0.02 1 287 . 48 LEU H H 8.621 0.02 1 288 . 48 LEU HA H 4.149 0.02 1 289 . 48 LEU HB2 H 1.817 0.02 1 290 . 48 LEU HB3 H 1.817 0.02 1 291 . 48 LEU HG H 1.655 0.02 1 292 . 48 LEU HD1 H 0.960 0.02 2 293 . 48 LEU HD2 H 0.882 0.02 2 294 . 49 GLU H H 8.048 0.02 1 295 . 49 GLU HA H 4.110 0.02 1 296 . 49 GLU HB2 H 2.133 0.02 2 297 . 49 GLU HB3 H 2.086 0.02 2 298 . 49 GLU HG2 H 2.682 0.02 2 299 . 49 GLU HG3 H 2.470 0.02 2 300 . 50 LYS H H 7.586 0.02 1 301 . 50 LYS HA H 4.225 0.02 1 302 . 50 LYS HB2 H 1.962 0.02 1 303 . 50 LYS HB3 H 1.962 0.02 1 304 . 50 LYS HG2 H 1.503 0.02 1 305 . 50 LYS HG3 H 1.503 0.02 1 306 . 50 LYS HD2 H 1.731 0.02 1 307 . 50 LYS HD3 H 1.731 0.02 1 308 . 50 LYS HE2 H 3.004 0.02 1 309 . 50 LYS HE3 H 3.004 0.02 1 310 . 51 GLU H H 7.966 0.02 1 311 . 51 GLU HA H 4.230 0.02 1 312 . 51 GLU HB2 H 2.071 0.02 1 313 . 51 GLU HB3 H 2.071 0.02 1 314 . 51 GLU HG2 H 2.491 0.02 2 315 . 51 GLU HG3 H 2.334 0.02 2 316 . 52 ALA H H 7.898 0.02 1 317 . 52 ALA HA H 4.316 0.02 1 318 . 52 ALA HB H 1.451 0.02 1 319 . 53 LYS H H 7.974 0.02 1 320 . 53 LYS HA H 4.374 0.02 1 321 . 53 LYS HB2 H 1.929 0.02 2 322 . 53 LYS HB3 H 1.836 0.02 2 323 . 53 LYS HG2 H 1.464 0.02 1 324 . 53 LYS HG3 H 1.464 0.02 1 325 . 53 LYS HD2 H 1.698 0.02 1 326 . 53 LYS HD3 H 1.698 0.02 1 327 . 53 LYS HE2 H 3.029 0.02 1 328 . 53 LYS HE3 H 3.029 0.02 1 329 . 54 SER H H 8.239 0.02 1 330 . 54 SER HA H 4.481 0.02 1 331 . 54 SER HB2 H 3.918 0.02 1 332 . 54 SER HB3 H 3.918 0.02 1 333 . 55 GLN H H 7.962 0.02 1 334 . 55 GLN HA H 4.212 0.02 1 335 . 55 GLN HB2 H 2.144 0.02 2 336 . 55 GLN HB3 H 1.961 0.02 2 337 . 55 GLN HG2 H 2.328 0.02 1 338 . 55 GLN HG3 H 2.328 0.02 1 stop_ save_ ######################## # Coupling constants # ######################## save_J_values_set_1 _Saveframe_category coupling_constants _Details . loop_ _Experiment_label 2D-TOCSY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name HF6478 _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 5.75 . . 1 2 3JHNHA 12 GLN H 12 GLN HA 3.84 . . 1 3 3JHNHA 13 ALA H 13 ALA HA 3.94 . . 1 4 3JHNHA 14 PHE H 14 PHE HA 9.57 . . 1 5 3JHNHA 16 LYS H 16 LYS HA 9.01 . . 1 6 3JHNHA 19 LYS H 19 LYS HA 10.10 . . 1 7 3JHNHA 21 PHE H 21 PHE HA 10.25 . . 1 8 3JHNHA 26 LYS H 26 LYS HA 3.49 . . 1 9 3JHNHA 27 LYS H 27 LYS HA 3.62 . . 1 10 3JHNHA 42 ALA H 42 ALA HA 4.02 . . 1 11 3JHNHA 43 THR H 43 THR HA 5.40 . . 1 12 3JHNHA 46 MET H 46 MET HA 4.75 . . 1 13 3JHNHA 55 GLN H 55 GLN HA 8.28 . . 1 stop_ save_