data_5989 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Cytotoxin I from the venom of the Central Asian cobra Naja Oxiana, in aqueous solution ; _BMRB_accession_number 5989 _BMRB_flat_file_name bmr5989.str _Entry_type original _Submission_date 2003-10-31 _Accession_date 2003-10-31 _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 Dubinnyi Maxim A. . 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" 684 "coupling constants" 107 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-05-20 original author . stop_ _Original_release_date 2005-05-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Interaction of three-finger toxins with phospholipid membranes: comparison of S- and P-type cytotoxins ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15584897 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Dubovskii P. V. . 2 Lesovoy D. M. . 3 Dubinnyi Maxim A. . 4 Konshina A. G. . 5 Utkin Yuri N. . 6 Efremov R. G. . 7 Arseniev Alexander S. . stop_ _Journal_abbreviation 'Biochem. J.' _Journal_volume 387 _Journal_issue 'Pt 3' _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 807 _Page_last 815 _Year 2005 _Details 'Structure determination in aqueous solution and in complex with DPC micelle.' loop_ _Keyword 'S-type cytotoxin' 'tigtly bound water molecule cys/trans isomerisation' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _Citation_full ; Grishin E.V., Sukhikh A.P., Adamovich T.B., Ovchinnikov Y.A. "Isolation, properties and sequence determination of the two cytotoxins from the venom of the Middle-Asian cobra Naja Naja oxiana." Bioorg. Khim. 2:1018-1034(1976). ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref-2 _Saveframe_category citation _Citation_full ; Bartles C., Xia T., Billiter M., Guntert P., Wutrich K. "The program XEASY for computer-supported NMR spectral analysis of biological macromolecules" Journal of Biomolecular NMR, 1995, v.5 pp.1-10. ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref-3 _Saveframe_category citation _Citation_full ; Herrmann T, Guntert P, Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol. 2002 May 24;319(1):209-27. ; _Citation_title 'Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12051947 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Herrmann Torsten . . 2 Guntert Peter . . 3 Wuthrich Kurt . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 319 _Journal_issue 1 _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 209 _Page_last 227 _Year 2002 _Details ; Combined automated NOE assignment and structure determination module (CANDID) is a new software for efficient NMR structure determination of proteins by automated assignment of the NOESY spectra. CANDID uses an iterative approach with multiple cycles of NOE cross-peak assignment and protein structure calculation using the fast DYANA torsion angle dynamics algorithm, so that the result from each CANDID cycle consists of exhaustive, possibly ambiguous NOE cross-peak assignments in all available spectra and a three-dimensional protein structure represented by a bundle of conformers. The input for the first CANDID cycle consists of the amino acid sequence, the chemical shift list from the sequence-specific resonance assignment, and listings of the cross-peak positions and volumes in one or several two, three or four-dimensional NOESY spectra. The input for the second and subsequent CANDID cycles contains the three-dimensional protein structure from the previous cycle, in addition to the complete input used for the first cycle. CANDID includes two new elements that make it robust with respect to the presence of artifacts in the input data, i.e. network-anchoring and constraint-combination, which have a key role in de novo protein structure determinations for the successful generation of the correct polypeptide fold by the first CANDID cycle. Network-anchoring makes use of the fact that any network of correct NOE cross-peak assignments forms a self-consistent set; the initial, chemical shift-based assignments for each individual NOE cross-peak are therefore weighted by the extent to which they can be embedded into the network formed by all other NOE cross-peak assignments. Constraint-combination reduces the deleterious impact of artifact NOE upper distance constraints in the input for a protein structure calculation by combining the assignments for two or several peaks into a single upper limit distance constraint, which lowers the probability that the presence of an artifact peak will influence the outcome of the structure calculation. CANDID test calculations were performed with NMR data sets of four proteins for which high-quality structures had previously been solved by interactive protocols, and they yielded comparable results to these reference structure determinations with regard to both the residual constraint violations, and the precision and accuracy of the atomic coordinates. The CANDID approach has further been validated by de novo NMR structure determinations of four additional proteins. The experience gained in these calculations shows that once nearly complete sequence-specific resonance assignments are available, the automated CANDID approach results in greatly enhanced efficiency of the NOESY spectral analysis. The fact that the correct fold is obtained in cycle 1 of a de novo structure calculation is the single most important advance achieved with CANDID, when compared with previously proposed automated NOESY assignment methods that do not use network-anchoring and constraint-combination. ; save_ ################################## # Molecular system description # ################################## save_system_CTI _Saveframe_category molecular_system _Mol_system_name 'Cytotoxin I' _Abbreviation_common CTI _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CTI major form' $CTI 'CTI minor form' $CTI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'cell lysis' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CTI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Cytotocin I' _Abbreviation_common CTI _Molecular_mass 6821 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 60 _Mol_residue_sequence ; LKCNKLVPIAYKTCPEGKNL CYKMFMMSDLTIPVKRGCID VCPKNSLLVKYVCCNTDRCN ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 LYS 3 CYS 4 ASN 5 LYS 6 LEU 7 VAL 8 PRO 9 ILE 10 ALA 11 TYR 12 LYS 13 THR 14 CYS 15 PRO 16 GLU 17 GLY 18 LYS 19 ASN 20 LEU 21 CYS 22 TYR 23 LYS 24 MET 25 PHE 26 MET 27 MET 28 SER 29 ASP 30 LEU 31 THR 32 ILE 33 PRO 34 VAL 35 LYS 36 ARG 37 GLY 38 CYS 39 ILE 40 ASP 41 VAL 42 CYS 43 PRO 44 LYS 45 ASN 46 SER 47 LEU 48 LEU 49 VAL 50 LYS 51 TYR 52 VAL 53 CYS 54 CYS 55 ASN 56 THR 57 ASP 58 ARG 59 CYS 60 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-21 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 1RL5 "Nmr Structure With Tightly Bound Water Molecule Of Cytotoxin I From Naja Oxiana In Aqueous Solution (Major Form)" 100.00 60 100.00 100.00 8.43e-34 PDB 1ZAD "Structure Of Cytotoxin I (Cti) From Naja Oxiana In Complex With Dpc Micelle" 100.00 60 100.00 100.00 8.43e-34 GB AAB24495 "Vc-1=cytotoxin [Naja oxiana=snakes, venom, Peptide, 59 aa]" 100.00 59 98.33 98.33 4.05e-31 PRF 763620A "cytotoxin I" 100.00 60 100.00 100.00 8.43e-34 SP P01451 "RecName: Full=Cytotoxin 1; AltName: Full=Cytotoxin I; Short=CTI [Naja oxiana]" 100.00 60 100.00 100.00 8.43e-34 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 $CTI 'Central Asian Cobra' 8657 Eukaryota Metazoa Naja 'Naja oxiana' venom 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 $CTI 'purified from the natural source' . . . . . 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 $CTI 3.0 mM . KCl 0.05 M . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.1a loop_ _Task 'spectral data processing' stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.2.11 loop_ _Task 'peak picking' 'sequence-specific assignment' 'manual NOE assignment' stop_ _Details . _Citation_label $ref-2 save_ save_CYANA _Saveframe_category software _Name CYANA _Version 1.0.6 loop_ _Task 'automated NOE assignment' 'structure calculation' stop_ _Details . _Citation_label $ref-3 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_1 save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_1 save_ save_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.2 pH temperature 303 1 K 'ionic strength' 0.05 0.01 M 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 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_CTI_1H_Shifts_major _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CTI major form' _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 LEU HA H 4.184 0.005 1 2 . 1 LEU HB2 H 1.568 0.002 2 3 . 1 LEU HD1 H 0.772 0.004 1 4 . 1 LEU HD2 H 0.853 0.005 1 5 . 1 LEU HG H 1.508 0.005 1 6 . 2 LYS H H 8.590 0.002 1 7 . 2 LYS HA H 5.391 0.016 1 8 . 2 LYS HB2 H 1.323 0.002 1 9 . 2 LYS HB3 H 1.172 0.118 1 10 . 2 LYS HG2 H 1.120 0.000 2 11 . 2 LYS HD2 H 1.204 0.004 2 12 . 2 LYS HE2 H 2.820 0.000 2 13 . 3 CYS H H 8.819 0.000 1 14 . 3 CYS HA H 5.146 0.005 1 15 . 3 CYS HB2 H 2.492 0.003 1 16 . 3 CYS HB3 H 2.844 0.000 1 17 . 4 ASN H H 9.695 0.000 1 18 . 4 ASN HA H 4.949 0.007 1 19 . 4 ASN HB2 H 2.299 0.001 1 20 . 4 ASN HB3 H 2.710 0.002 1 21 . 4 ASN HD21 H 7.572 0.000 1 22 . 4 ASN HD22 H 6.643 0.003 1 23 . 5 LYS H H 7.915 0.005 1 24 . 5 LYS HA H 4.245 0.005 1 25 . 5 LYS HB2 H 1.552 0.000 1 26 . 5 LYS HB3 H 2.088 0.001 1 27 . 5 LYS HG2 H 1.254 0.007 2 28 . 5 LYS HD2 H 1.379 0.004 2 29 . 5 LYS HE2 H 2.888 0.005 2 30 . 6 LEU H H 8.173 0.001 1 31 . 6 LEU HA H 3.675 0.000 1 32 . 6 LEU HB2 H 1.652 0.000 1 33 . 6 LEU HB3 H 1.792 0.000 1 34 . 6 LEU HD1 H 0.701 0.003 1 35 . 6 LEU HD2 H 0.876 0.001 1 36 . 6 LEU HG H 1.547 0.000 1 37 . 7 VAL H H 7.548 0.000 1 38 . 7 VAL HA H 4.471 0.006 1 39 . 7 VAL HB H 2.123 0.005 1 40 . 7 VAL HG1 H 0.974 0.000 1 41 . 7 VAL HG2 H 1.004 0.004 1 42 . 8 PRO HA H 4.536 0.002 1 43 . 8 PRO HB2 H 1.856 0.005 1 44 . 8 PRO HB3 H 2.245 0.004 1 45 . 8 PRO HG2 H 1.920 0.000 1 46 . 8 PRO HG3 H 1.986 0.002 1 47 . 8 PRO HD2 H 3.835 0.000 1 48 . 8 PRO HD3 H 3.979 0.000 1 49 . 9 ILE H H 7.060 0.000 1 50 . 9 ILE HA H 4.190 0.000 1 51 . 9 ILE HB H 2.070 0.003 1 52 . 9 ILE HG12 H 1.093 0.000 1 53 . 9 ILE HG13 H 1.001 0.001 1 54 . 9 ILE HG2 H 0.910 0.004 1 55 . 9 ILE HD1 H 1.331 0.000 1 56 . 10 ALA H H 7.871 0.000 1 57 . 10 ALA HA H 4.624 0.004 1 58 . 10 ALA HB H 1.376 0.002 1 59 . 11 TYR H H 7.845 0.000 1 60 . 11 TYR HA H 5.317 0.005 1 61 . 11 TYR HB2 H 2.700 0.004 1 62 . 11 TYR HB3 H 2.837 0.003 1 63 . 11 TYR HD1 H 6.734 0.001 2 64 . 11 TYR HE1 H 6.793 0.002 2 65 . 12 LYS H H 8.982 0.105 1 66 . 12 LYS HA H 4.770 0.000 1 67 . 12 LYS HB2 H 1.730 0.000 1 68 . 12 LYS HB3 H 1.432 0.000 1 69 . 12 LYS HG2 H 1.280 0.000 1 70 . 12 LYS HG3 H 1.410 0.000 1 71 . 12 LYS HD2 H 1.710 0.000 2 72 . 12 LYS HE2 H 3.010 0.000 2 73 . 13 THR H H 8.726 0.001 1 74 . 13 THR HA H 4.666 0.002 1 75 . 13 THR HB H 4.074 0.005 1 76 . 13 THR HG2 H 1.270 0.009 1 77 . 14 CYS H H 9.143 0.000 1 78 . 14 CYS HA H 4.987 0.006 1 79 . 14 CYS HB2 H 2.842 0.003 1 80 . 14 CYS HB3 H 3.527 0.008 1 81 . 15 PRO HA H 4.625 0.001 1 82 . 15 PRO HB2 H 2.414 0.003 1 83 . 15 PRO HB3 H 1.971 0.005 1 84 . 15 PRO HG2 H 1.927 0.000 1 85 . 15 PRO HG3 H 2.184 0.003 1 86 . 15 PRO HD2 H 3.447 0.003 1 87 . 15 PRO HD3 H 3.995 0.005 1 88 . 16 GLU H H 8.572 0.000 1 89 . 16 GLU HA H 4.032 0.003 1 90 . 16 GLU HB2 H 1.961 0.000 1 91 . 16 GLU HB3 H 2.311 0.004 1 92 . 16 GLU HG2 H 2.012 0.000 2 93 . 17 GLY H H 8.894 0.000 1 94 . 17 GLY HA2 H 3.679 0.001 1 95 . 17 GLY HA3 H 4.301 0.003 1 96 . 18 LYS H H 7.613 0.000 1 97 . 18 LYS HA H 4.297 0.002 1 98 . 18 LYS HB2 H 1.936 0.000 2 99 . 18 LYS HG2 H 1.101 0.007 2 100 . 18 LYS HD2 H 1.360 0.000 1 101 . 18 LYS HD3 H 1.410 0.000 1 102 . 18 LYS HE2 H 2.960 0.000 2 103 . 18 LYS HZ H 7.700 0.000 1 104 . 19 ASN H H 7.929 0.000 1 105 . 19 ASN HA H 4.945 0.002 1 106 . 19 ASN HB2 H 3.017 0.000 1 107 . 19 ASN HB3 H 2.656 0.002 1 108 . 19 ASN HD21 H 7.488 0.000 1 109 . 19 ASN HD22 H 7.024 0.000 1 110 . 20 LEU H H 8.224 0.003 1 111 . 20 LEU HA H 4.858 0.008 1 112 . 20 LEU HB2 H 1.681 0.005 1 113 . 20 LEU HB3 H 1.391 0.001 1 114 . 20 LEU HD1 H 0.754 0.007 1 115 . 20 LEU HD2 H 0.892 0.006 1 116 . 20 LEU HG H 1.517 0.000 1 117 . 21 CYS H H 9.020 0.004 1 118 . 21 CYS HA H 6.108 0.000 1 119 . 21 CYS HB2 H 2.974 0.000 1 120 . 21 CYS HB3 H 3.040 0.000 1 121 . 22 TYR H H 8.967 0.000 1 122 . 22 TYR HA H 6.095 0.000 1 123 . 22 TYR HB2 H 3.123 0.000 1 124 . 22 TYR HB3 H 2.982 0.000 1 125 . 22 TYR HD1 H 6.839 0.003 2 126 . 22 TYR HE1 H 6.607 0.003 2 127 . 23 LYS H H 9.062 0.000 1 128 . 23 LYS HA H 4.859 0.007 1 129 . 23 LYS HB2 H 1.505 0.007 1 130 . 23 LYS HB3 H 1.659 0.002 1 131 . 23 LYS HG2 H 1.423 0.008 2 132 . 23 LYS HD2 H 1.756 0.000 2 133 . 23 LYS HE2 H 3.060 0.000 2 134 . 23 LYS HZ H 7.860 0.000 1 135 . 24 MET H H 8.297 0.004 1 136 . 24 MET HA H 5.151 0.005 1 137 . 24 MET HB2 H 1.787 0.000 1 138 . 24 MET HB3 H 1.693 0.004 1 139 . 24 MET HG2 H 1.317 0.007 1 140 . 24 MET HG3 H 1.546 0.007 1 141 . 24 MET HE H 2.080 0.000 1 142 . 25 PHE H H 9.508 0.003 1 143 . 25 PHE HA H 4.862 0.005 1 144 . 25 PHE HB2 H 2.491 0.003 1 145 . 25 PHE HB3 H 3.396 0.004 1 146 . 25 PHE HD1 H 7.082 0.004 2 147 . 25 PHE HE1 H 6.941 0.002 2 148 . 25 PHE HZ H 7.188 0.002 1 149 . 26 MET H H 9.304 0.005 1 150 . 26 MET HA H 5.114 0.005 1 151 . 26 MET HB2 H 2.033 0.005 1 152 . 26 MET HB3 H 2.352 0.003 1 153 . 26 MET HG2 H 2.632 0.007 1 154 . 26 MET HG3 H 2.865 0.003 1 155 . 26 MET HE H 1.860 0.000 1 156 . 27 MET H H 8.371 0.000 1 157 . 27 MET HA H 4.157 0.005 1 158 . 27 MET HB2 H 1.916 0.004 1 159 . 27 MET HB3 H 2.030 0.003 1 160 . 27 MET HG2 H 2.119 0.000 1 161 . 27 MET HG3 H 2.643 0.004 1 162 . 27 MET HE H 2.080 0.000 1 163 . 28 SER H H 7.664 0.000 1 164 . 28 SER HA H 4.206 0.003 1 165 . 28 SER HB2 H 3.810 0.007 1 166 . 28 SER HB3 H 4.067 0.005 1 167 . 29 ASP H H 7.944 0.000 1 168 . 29 ASP HA H 4.672 0.004 1 169 . 29 ASP HB2 H 2.705 0.005 1 170 . 29 ASP HB3 H 2.904 0.009 1 171 . 30 LEU H H 8.792 0.000 1 172 . 30 LEU HA H 4.039 0.000 1 173 . 30 LEU HB2 H 1.483 0.000 1 174 . 30 LEU HB3 H 1.320 0.000 1 175 . 30 LEU HD1 H 0.677 0.001 1 176 . 30 LEU HD2 H 0.830 0.000 1 177 . 30 LEU HG H 1.630 0.000 1 178 . 31 THR H H 8.693 0.000 1 179 . 31 THR HA H 4.418 0.004 1 180 . 31 THR HB H 4.321 0.002 1 181 . 31 THR HG2 H 1.196 0.002 1 182 . 32 ILE H H 7.117 0.000 1 183 . 32 ILE HA H 4.871 0.003 1 184 . 32 ILE HB H 1.881 0.000 1 185 . 32 ILE HG2 H 0.900 0.000 1 186 . 32 ILE HG12 H 1.170 0.000 1 187 . 32 ILE HG13 H 1.210 0.000 1 188 . 32 ILE HD1 H 1.633 0.005 1 189 . 33 PRO HA H 4.054 0.010 1 190 . 33 PRO HB2 H 1.215 0.006 1 191 . 33 PRO HB3 H 1.498 0.005 1 192 . 33 PRO HG2 H 1.658 0.002 1 193 . 33 PRO HG3 H 1.910 0.000 1 194 . 33 PRO HD2 H 3.858 0.003 1 195 . 33 PRO HD3 H 3.948 0.003 1 196 . 34 VAL H H 8.747 0.004 1 197 . 34 VAL HA H 4.425 0.001 1 198 . 34 VAL HB H 2.295 0.003 1 199 . 34 VAL HG1 H 0.832 0.006 1 200 . 34 VAL HG2 H 1.032 0.002 1 201 . 35 LYS H H 7.355 0.005 1 202 . 35 LYS HA H 4.560 0.003 1 203 . 35 LYS HB2 H 1.727 0.005 1 204 . 35 LYS HB3 H 1.978 0.011 1 205 . 35 LYS HG2 H 1.550 0.000 1 206 . 35 LYS HG3 H 1.633 0.000 1 207 . 35 LYS HD2 H 1.790 0.000 1 208 . 35 LYS HD3 H 1.856 0.000 1 209 . 35 LYS HE2 H 3.054 0.002 2 210 . 35 LYS HZ H 7.530 0.000 1 211 . 36 ARG H H 8.224 0.011 1 212 . 36 ARG HA H 4.400 0.009 1 213 . 36 ARG HB2 H 1.034 0.000 1 214 . 36 ARG HB3 H 1.496 0.004 1 215 . 36 ARG HG2 H 1.390 0.003 1 216 . 36 ARG HG3 H 1.550 0.004 1 217 . 36 ARG HD2 H 3.037 0.008 2 218 . 36 ARG HE H 7.862 0.000 1 219 . 37 GLY H H 6.506 0.004 1 220 . 37 GLY HA2 H 3.873 0.006 1 221 . 37 GLY HA3 H 4.154 0.009 1 222 . 38 CYS H H 8.666 0.003 1 223 . 38 CYS HA H 5.968 0.004 1 224 . 38 CYS HB2 H 3.461 0.005 1 225 . 38 CYS HB3 H 2.930 0.009 1 226 . 39 ILE H H 9.830 0.867 1 227 . 39 ILE HA H 4.416 0.006 1 228 . 39 ILE HB H 1.733 0.008 1 229 . 39 ILE HG2 H 0.571 0.005 1 230 . 39 ILE HG12 H 1.200 0.000 1 231 . 39 ILE HG13 H 1.430 0.000 1 232 . 39 ILE HD1 H 0.412 0.005 1 233 . 40 ASP H H 8.725 0.000 1 234 . 40 ASP HA H 4.880 0.004 1 235 . 40 ASP HB2 H 2.796 0.005 2 236 . 41 VAL H H 7.744 0.003 1 237 . 41 VAL HA H 4.018 0.003 1 238 . 41 VAL HB H 1.730 0.002 1 239 . 41 VAL HG1 H 0.754 0.001 1 240 . 41 VAL HG2 H 0.763 0.002 1 241 . 42 CYS H H 8.877 0.003 1 242 . 42 CYS HA H 4.461 0.002 1 243 . 42 CYS HB2 H 2.756 0.003 1 244 . 42 CYS HB3 H 3.108 0.008 1 245 . 43 PRO HA H 4.081 0.000 1 246 . 43 PRO HB2 H 1.872 0.000 1 247 . 43 PRO HB3 H 0.741 0.006 1 248 . 43 PRO HG2 H 0.547 0.005 1 249 . 43 PRO HG3 H 1.233 0.000 1 250 . 43 PRO HD2 H 2.333 0.006 1 251 . 43 PRO HD3 H 3.885 0.005 1 252 . 44 LYS H H 7.921 0.000 1 253 . 44 LYS HA H 4.212 0.001 1 254 . 44 LYS HB2 H 1.711 0.002 1 255 . 44 LYS HB3 H 1.861 0.002 1 256 . 44 LYS HG2 H 1.557 0.000 2 257 . 44 LYS HE2 H 3.058 0.010 2 258 . 44 LYS HZ H 7.510 0.000 1 259 . 45 ASN H H 8.429 0.001 1 260 . 45 ASN HA H 4.957 0.007 1 261 . 45 ASN HB2 H 2.873 0.007 1 262 . 45 ASN HB3 H 3.258 0.000 1 263 . 45 ASN HD21 H 7.692 0.002 1 264 . 45 ASN HD22 H 7.371 0.001 1 265 . 46 SER H H 9.004 0.000 1 266 . 46 SER HA H 5.026 0.001 1 267 . 46 SER HB2 H 4.457 0.003 1 268 . 46 SER HB3 H 3.982 0.004 1 269 . 47 LEU H H 8.368 0.001 1 270 . 47 LEU HA H 4.296 0.003 1 271 . 47 LEU HB2 H 1.940 0.003 1 272 . 47 LEU HB3 H 1.633 0.000 1 273 . 47 LEU HD1 H 0.935 0.000 1 274 . 47 LEU HD2 H 0.964 0.000 1 275 . 47 LEU HG H 1.760 0.001 1 276 . 48 LEU H H 8.242 0.000 1 277 . 48 LEU HA H 4.499 0.001 1 278 . 48 LEU HB2 H 1.748 0.000 1 279 . 48 LEU HB3 H 1.667 0.002 1 280 . 48 LEU HD1 H 0.892 0.000 1 281 . 48 LEU HD2 H 0.960 0.000 1 282 . 49 VAL H H 7.549 0.001 1 283 . 49 VAL HA H 5.081 0.000 1 284 . 49 VAL HB H 1.878 0.003 1 285 . 49 VAL HG1 H 0.832 0.003 1 286 . 49 VAL HG2 H 0.903 0.003 1 287 . 50 LYS H H 8.788 0.002 1 288 . 50 LYS HA H 4.810 0.000 1 289 . 50 LYS HB2 H 1.799 0.006 1 290 . 50 LYS HB3 H 1.638 0.004 1 291 . 50 LYS HG2 H 1.223 0.000 2 292 . 50 LYS HD2 H 1.497 0.000 2 293 . 50 LYS HE2 H 2.877 0.002 2 294 . 50 LYS HZ H 7.630 0.000 1 295 . 51 TYR H H 9.289 0.006 1 296 . 51 TYR HA H 5.332 0.004 1 297 . 51 TYR HB2 H 2.982 0.004 1 298 . 51 TYR HB3 H 2.755 0.006 1 299 . 51 TYR HD1 H 6.840 0.002 2 300 . 51 TYR HE1 H 6.468 0.000 2 301 . 52 VAL H H 8.981 0.005 1 302 . 52 VAL HA H 4.575 0.005 1 303 . 52 VAL HB H 2.091 0.007 1 304 . 52 VAL HG1 H 1.078 0.004 1 305 . 52 VAL HG2 H 1.163 0.002 1 306 . 53 CYS H H 9.535 0.005 1 307 . 53 CYS HA H 5.893 0.004 1 308 . 53 CYS HB2 H 3.099 0.003 1 309 . 53 CYS HB3 H 3.804 0.003 1 310 . 54 CYS H H 9.190 0.002 1 311 . 54 CYS HA H 5.114 0.002 1 312 . 54 CYS HB2 H 3.440 0.004 1 313 . 54 CYS HB3 H 3.649 0.003 1 314 . 55 ASN H H 8.579 0.001 1 315 . 55 ASN HA H 5.154 0.007 1 316 . 55 ASN HB2 H 2.655 0.003 1 317 . 55 ASN HB3 H 3.384 0.002 1 318 . 55 ASN HD21 H 6.728 0.002 1 319 . 55 ASN HD22 H 7.536 0.005 1 320 . 56 THR H H 7.590 0.006 1 321 . 56 THR HA H 4.717 0.000 1 322 . 56 THR HB H 4.297 0.000 1 323 . 56 THR HG2 H 1.206 0.000 1 324 . 57 ASP H H 8.232 0.000 1 325 . 57 ASP HA H 4.817 0.004 1 326 . 57 ASP HB2 H 2.493 0.005 1 327 . 57 ASP HB3 H 2.272 0.005 1 328 . 58 ARG H H 9.657 0.003 1 329 . 58 ARG HA H 3.397 0.006 1 330 . 58 ARG HB2 H 1.798 0.001 1 331 . 58 ARG HB3 H 2.185 0.002 1 332 . 58 ARG HG2 H 1.321 0.000 1 333 . 58 ARG HG3 H 1.370 0.000 1 334 . 58 ARG HE H 7.850 0.000 1 335 . 59 CYS H H 7.598 0.004 1 336 . 59 CYS HA H 4.464 0.003 1 337 . 59 CYS HB2 H 3.363 0.000 1 338 . 59 CYS HB3 H 3.651 0.002 1 339 . 60 ASN H H 9.024 0.000 1 340 . 60 ASN HA H 4.369 0.004 1 341 . 60 ASN HB2 H 2.722 0.003 1 342 . 60 ASN HB3 H 2.327 0.007 1 343 . 60 ASN HD21 H 7.398 0.006 1 344 . 60 ASN HD22 H 7.518 0.000 1 stop_ save_ save_CTI_1H_Shifts_minor _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CTI minor form' _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 LEU HA H 4.184 0.005 1 2 . 1 LEU HB2 H 1.568 0.002 2 3 . 1 LEU HD1 H 0.772 0.004 1 4 . 1 LEU HD2 H 0.853 0.005 1 5 . 1 LEU HG H 1.508 0.005 1 6 . 2 LYS H H 8.619 0.000 1 7 . 2 LYS HA H 5.391 0.000 1 8 . 2 LYS HB2 H 1.420 0.000 2 9 . 2 LYS HG2 H 1.120 0.000 2 10 . 2 LYS HD2 H 1.204 0.000 2 11 . 2 LYS HE2 H 2.820 0.000 2 12 . 3 CYS H H 8.659 0.001 1 13 . 3 CYS HA H 5.130 0.000 1 14 . 3 CYS HB2 H 2.562 0.002 1 15 . 3 CYS HB3 H 2.938 0.000 1 16 . 4 ASN H H 9.647 0.000 1 17 . 4 ASN HA H 5.042 0.002 1 18 . 4 ASN HB2 H 2.246 0.000 1 19 . 4 ASN HB3 H 2.572 0.000 1 20 . 4 ASN HD21 H 7.452 0.000 1 21 . 4 ASN HD22 H 6.672 0.000 1 22 . 5 LYS H H 7.961 0.001 1 23 . 5 LYS HA H 4.568 0.000 1 24 . 5 LYS HB2 H 1.457 0.000 1 25 . 5 LYS HB3 H 1.900 0.000 1 26 . 5 LYS HG2 H 1.378 0.000 2 27 . 5 LYS HD2 H 1.379 0.000 2 28 . 5 LYS HE2 H 2.888 0.000 2 29 . 6 LEU H H 8.218 0.000 1 30 . 6 LEU HA H 4.381 0.000 1 31 . 6 LEU HB2 H 1.652 0.000 1 32 . 6 LEU HB3 H 1.792 0.000 1 33 . 6 LEU HD1 H 0.701 0.000 1 34 . 6 LEU HD2 H 0.876 0.000 1 35 . 6 LEU HG H 1.547 0.000 1 36 . 7 VAL H H 8.025 0.000 1 37 . 7 VAL HA H 4.109 0.000 1 38 . 7 VAL HB H 2.048 0.000 1 39 . 7 VAL HG1 H 0.956 0.000 1 40 . 7 VAL HG2 H 1.003 0.000 1 41 . 8 PRO HA H 4.715 0.000 1 42 . 8 PRO HB2 H 2.159 0.001 1 43 . 8 PRO HB3 H 2.360 0.001 1 44 . 8 PRO HG2 H 1.684 0.001 1 45 . 8 PRO HG3 H 2.018 0.001 1 46 . 8 PRO HD2 H 3.455 0.000 1 47 . 8 PRO HD3 H 3.600 0.000 1 48 . 9 ILE H H 8.360 0.000 1 49 . 9 ILE HA H 4.045 0.000 1 50 . 9 ILE HB H 2.105 0.000 1 51 . 9 ILE HG2 H 0.910 0.000 1 52 . 9 ILE HG12 H 0.858 0.000 2 53 . 9 ILE HD1 H 1.331 0.000 1 54 . 10 ALA H H 8.174 0.000 1 55 . 10 ALA HA H 4.277 0.000 1 56 . 10 ALA HB H 1.389 0.000 1 57 . 11 TYR H H 7.413 0.000 1 58 . 11 TYR HA H 5.058 0.000 1 59 . 11 TYR HB2 H 2.618 0.002 1 60 . 11 TYR HB3 H 3.184 0.000 1 61 . 11 TYR HD1 H 6.772 0.000 2 62 . 11 TYR HE1 H 6.772 0.000 2 63 . 12 LYS H H 8.714 0.000 1 64 . 12 LYS HA H 4.707 0.000 1 65 . 12 LYS HB2 H 1.670 0.000 1 66 . 12 LYS HB3 H 1.463 0.000 1 67 . 12 LYS HG2 H 1.280 0.000 1 68 . 12 LYS HG3 H 1.410 0.000 1 69 . 12 LYS HD2 H 1.730 0.000 2 70 . 12 LYS HE2 H 3.010 0.000 2 71 . 13 THR H H 8.685 0.000 1 72 . 13 THR HA H 4.605 0.000 1 73 . 13 THR HB H 4.068 0.000 1 74 . 13 THR HG2 H 1.281 0.000 1 75 . 14 CYS H H 9.234 0.001 1 76 . 14 CYS HA H 4.989 0.002 1 77 . 14 CYS HB2 H 2.837 0.000 1 78 . 14 CYS HB3 H 3.497 0.000 1 79 . 15 PRO HA H 4.611 0.000 1 80 . 15 PRO HB2 H 2.415 0.000 1 81 . 15 PRO HB3 H 1.971 0.000 1 82 . 15 PRO HG2 H 1.918 0.000 1 83 . 15 PRO HG3 H 2.183 0.000 1 84 . 15 PRO HD2 H 3.457 0.000 1 85 . 15 PRO HD3 H 3.989 0.000 1 86 . 16 GLU H H 8.551 0.000 1 87 . 16 GLU HA H 4.023 0.000 1 88 . 16 GLU HB2 H 1.950 0.000 1 89 . 16 GLU HB3 H 2.026 0.000 1 90 . 16 GLU HG2 H 2.296 0.000 2 91 . 17 GLY H H 8.929 0.000 1 92 . 17 GLY HA2 H 3.695 0.000 1 93 . 17 GLY HA3 H 4.306 0.000 1 94 . 18 LYS H H 7.634 0.000 1 95 . 18 LYS HA H 4.300 0.007 1 96 . 18 LYS HB2 H 1.936 0.000 2 97 . 18 LYS HG2 H 1.101 0.000 2 98 . 18 LYS HD2 H 1.358 0.000 1 99 . 18 LYS HD3 H 1.415 0.000 1 100 . 18 LYS HE2 H 2.960 0.000 2 101 . 18 LYS HZ H 7.700 0.000 1 102 . 19 ASN H H 7.960 0.000 1 103 . 19 ASN HA H 4.936 0.000 1 104 . 19 ASN HB2 H 3.010 0.000 1 105 . 19 ASN HB3 H 2.660 0.000 1 106 . 19 ASN HD21 H 7.488 0.000 1 107 . 19 ASN HD22 H 7.024 0.000 1 108 . 20 LEU H H 8.253 0.000 1 109 . 20 LEU HA H 4.844 0.000 1 110 . 20 LEU HB2 H 1.674 0.000 1 111 . 20 LEU HB3 H 1.392 0.000 1 112 . 20 LEU HD1 H 0.754 0.000 1 113 . 20 LEU HD2 H 0.892 0.000 1 114 . 20 LEU HG H 1.515 0.000 1 115 . 21 CYS H H 8.982 0.000 1 116 . 21 CYS HA H 6.117 0.000 1 117 . 21 CYS HB2 H 2.974 0.000 1 118 . 21 CYS HB3 H 3.139 0.000 1 119 . 22 TYR H H 9.136 0.000 1 120 . 22 TYR HA H 6.105 0.000 1 121 . 22 TYR HB2 H 3.129 0.000 1 122 . 22 TYR HB3 H 3.018 0.000 1 123 . 22 TYR HD1 H 6.679 0.000 2 124 . 22 TYR HE1 H 6.621 0.000 2 125 . 23 LYS H H 9.088 0.000 1 126 . 23 LYS HA H 4.869 0.000 1 127 . 23 LYS HB2 H 1.508 0.000 1 128 . 23 LYS HB3 H 1.656 0.000 1 129 . 23 LYS HG2 H 1.435 0.000 2 130 . 23 LYS HD2 H 1.756 0.000 2 131 . 23 LYS HE2 H 3.070 0.000 2 132 . 23 LYS HZ H 7.860 0.000 1 133 . 24 MET H H 8.320 0.000 1 134 . 24 MET HA H 5.165 0.000 1 135 . 24 MET HB2 H 1.788 0.001 1 136 . 24 MET HB3 H 1.696 0.001 1 137 . 24 MET HG2 H 1.324 0.001 1 138 . 24 MET HG3 H 1.558 0.000 1 139 . 24 MET HE H 2.080 0.000 1 140 . 25 PHE H H 9.545 0.001 1 141 . 25 PHE HA H 4.870 0.000 1 142 . 25 PHE HB2 H 2.506 0.000 1 143 . 25 PHE HB3 H 3.397 0.000 1 144 . 25 PHE HD1 H 7.082 0.000 2 145 . 25 PHE HE1 H 6.941 0.000 2 146 . 25 PHE HZ H 7.188 0.000 1 147 . 26 MET H H 9.255 0.000 1 148 . 26 MET HA H 5.110 0.000 1 149 . 26 MET HB2 H 2.036 0.000 1 150 . 26 MET HB3 H 2.349 0.000 1 151 . 26 MET HG2 H 2.635 0.000 1 152 . 26 MET HG3 H 2.868 0.000 1 153 . 26 MET HE H 1.860 0.000 1 154 . 27 MET H H 8.371 0.000 1 155 . 27 MET HA H 4.157 0.005 1 156 . 27 MET HB2 H 1.916 0.004 1 157 . 27 MET HB3 H 2.030 0.003 1 158 . 27 MET HG2 H 2.119 0.000 1 159 . 27 MET HG3 H 2.643 0.004 1 160 . 27 MET HE H 2.080 0.000 1 161 . 28 SER H H 7.664 0.000 1 162 . 28 SER HA H 4.206 0.003 1 163 . 28 SER HB2 H 3.810 0.007 1 164 . 28 SER HB3 H 4.067 0.005 1 165 . 29 ASP H H 7.961 0.000 1 166 . 29 ASP HA H 4.643 0.001 1 167 . 29 ASP HB2 H 2.651 0.000 1 168 . 29 ASP HB3 H 2.907 0.000 1 169 . 30 LEU H H 8.826 0.000 1 170 . 30 LEU HA H 4.050 0.001 1 171 . 30 LEU HB2 H 1.635 0.000 1 172 . 30 LEU HB3 H 1.493 0.000 1 173 . 30 LEU HD1 H 0.677 0.000 1 174 . 30 LEU HD2 H 0.830 0.000 1 175 . 30 LEU HG H 1.640 0.000 1 176 . 31 THR H H 8.677 0.000 1 177 . 31 THR HA H 4.416 0.000 1 178 . 31 THR HB H 4.329 0.000 1 179 . 31 THR HG2 H 1.179 0.000 1 180 . 32 ILE H H 7.116 0.000 1 181 . 32 ILE HA H 4.875 0.000 1 182 . 32 ILE HB H 1.887 0.000 1 183 . 32 ILE HG2 H 1.210 0.000 1 184 . 32 ILE HG12 H 0.903 0.000 2 185 . 32 ILE HD1 H 1.619 0.000 1 186 . 33 PRO HA H 4.054 0.010 1 187 . 33 PRO HB2 H 1.215 0.006 1 188 . 33 PRO HB3 H 1.498 0.005 1 189 . 33 PRO HG2 H 1.658 0.002 1 190 . 33 PRO HG3 H 1.910 0.000 1 191 . 33 PRO HD2 H 3.858 0.003 1 192 . 33 PRO HD3 H 3.948 0.003 1 193 . 34 VAL H H 8.726 0.000 1 194 . 34 VAL HA H 4.366 0.000 1 195 . 34 VAL HB H 2.240 0.000 1 196 . 34 VAL HG1 H 0.862 0.000 1 197 . 34 VAL HG2 H 1.027 0.000 1 198 . 35 LYS H H 7.378 0.000 1 199 . 35 LYS HA H 4.567 0.000 1 200 . 35 LYS HB2 H 1.714 0.000 1 201 . 35 LYS HB3 H 1.997 0.000 1 202 . 35 LYS HG2 H 1.531 0.000 1 203 . 35 LYS HG3 H 1.606 0.000 1 204 . 35 LYS HD2 H 1.811 0.000 1 205 . 35 LYS HD3 H 1.870 0.000 1 206 . 35 LYS HE2 H 3.052 0.000 2 207 . 35 LYS HZ H 7.530 0.000 1 208 . 36 ARG H H 8.297 0.000 1 209 . 36 ARG HA H 4.421 0.000 1 210 . 36 ARG HB2 H 1.308 0.000 1 211 . 36 ARG HB3 H 1.684 0.000 1 212 . 36 ARG HG2 H 1.554 0.000 1 213 . 36 ARG HG3 H 0.857 0.000 1 214 . 36 ARG HD2 H 2.741 0.000 2 215 . 36 ARG HE H 7.996 0.000 1 216 . 37 GLY H H 6.796 0.000 1 217 . 37 GLY HA2 H 3.941 0.000 1 218 . 37 GLY HA3 H 4.280 0.000 1 219 . 38 CYS H H 8.660 0.000 1 220 . 38 CYS HA H 5.968 0.000 1 221 . 38 CYS HB2 H 3.461 0.000 1 222 . 38 CYS HB3 H 2.949 0.000 1 223 . 39 ILE H H 9.802 0.000 1 224 . 39 ILE HA H 4.395 0.000 1 225 . 39 ILE HB H 1.733 0.000 1 226 . 39 ILE HG2 H 0.571 0.000 1 227 . 39 ILE HG12 H 1.200 0.000 1 228 . 39 ILE HG13 H 1.430 0.000 1 229 . 39 ILE HD1 H 0.412 0.000 1 230 . 40 ASP H H 8.777 0.000 1 231 . 40 ASP HA H 4.894 0.000 1 232 . 40 ASP HB2 H 2.802 0.001 2 233 . 41 VAL H H 7.617 0.000 1 234 . 41 VAL HA H 4.029 0.000 1 235 . 41 VAL HB H 1.720 0.000 1 236 . 41 VAL HG1 H 0.770 0.000 2 237 . 42 CYS H H 8.877 0.003 1 238 . 42 CYS HA H 4.461 0.002 1 239 . 42 CYS HB2 H 2.756 0.003 1 240 . 42 CYS HB3 H 3.108 0.008 1 241 . 43 PRO HA H 4.092 0.000 1 242 . 43 PRO HB2 H 1.905 0.000 1 243 . 43 PRO HB3 H 0.749 0.000 1 244 . 43 PRO HG2 H 0.547 0.000 1 245 . 43 PRO HG3 H 1.220 0.000 1 246 . 43 PRO HD2 H 2.354 0.000 1 247 . 43 PRO HD3 H 3.915 0.000 1 248 . 44 LYS H H 7.856 0.000 1 249 . 44 LYS HA H 4.206 0.000 1 250 . 44 LYS HB2 H 1.714 0.000 1 251 . 44 LYS HB3 H 1.847 0.000 1 252 . 44 LYS HG2 H 1.553 0.000 2 253 . 44 LYS HE2 H 3.041 0.000 2 254 . 44 LYS HZ H 7.510 0.000 1 255 . 45 ASN H H 8.423 0.001 1 256 . 45 ASN HA H 4.960 0.001 1 257 . 45 ASN HB2 H 2.881 0.000 1 258 . 45 ASN HB3 H 3.257 0.000 1 259 . 45 ASN HD21 H 7.692 0.000 1 260 . 45 ASN HD22 H 7.371 0.000 1 261 . 46 SER H H 9.047 0.000 1 262 . 46 SER HA H 5.041 0.001 1 263 . 46 SER HB2 H 4.481 0.000 1 264 . 46 SER HB3 H 3.993 0.000 1 265 . 47 LEU H H 8.341 0.000 1 266 . 47 LEU HA H 4.283 0.001 1 267 . 47 LEU HB2 H 1.931 0.000 1 268 . 47 LEU HB3 H 1.632 0.000 1 269 . 47 LEU HD1 H 0.935 0.000 1 270 . 47 LEU HD2 H 0.964 0.000 1 271 . 47 LEU HG H 1.758 0.000 1 272 . 48 LEU H H 8.216 0.000 1 273 . 48 LEU HA H 4.497 0.000 1 274 . 48 LEU HB2 H 1.748 0.000 1 275 . 48 LEU HB3 H 1.667 0.000 1 276 . 48 LEU HD1 H 0.882 0.000 1 277 . 48 LEU HD2 H 0.958 0.000 1 278 . 49 VAL H H 7.515 0.000 1 279 . 49 VAL HA H 5.051 0.000 1 280 . 49 VAL HB H 1.860 0.000 1 281 . 49 VAL HG1 H 0.819 0.000 1 282 . 49 VAL HG2 H 0.895 0.000 1 283 . 50 LYS H H 8.812 0.000 1 284 . 50 LYS HA H 4.804 0.000 1 285 . 50 LYS HB2 H 1.793 0.000 1 286 . 50 LYS HB3 H 1.608 0.000 1 287 . 50 LYS HG2 H 1.220 0.000 2 288 . 50 LYS HD2 H 1.521 0.000 2 289 . 50 LYS HE2 H 2.867 0.000 2 290 . 50 LYS HZ H 7.630 0.000 1 291 . 51 TYR H H 9.251 0.000 1 292 . 51 TYR HA H 5.385 0.000 1 293 . 51 TYR HB2 H 2.989 0.000 1 294 . 51 TYR HB3 H 2.785 0.001 1 295 . 51 TYR HD1 H 6.894 0.000 2 296 . 51 TYR HE1 H 6.554 0.000 2 297 . 52 VAL H H 9.022 0.000 1 298 . 52 VAL HA H 4.577 0.000 1 299 . 52 VAL HB H 2.092 0.000 1 300 . 52 VAL HG1 H 1.071 0.000 1 301 . 52 VAL HG2 H 1.162 0.000 1 302 . 53 CYS H H 9.495 0.000 1 303 . 53 CYS HA H 5.870 0.001 1 304 . 53 CYS HB2 H 3.087 0.000 1 305 . 53 CYS HB3 H 3.810 0.000 1 306 . 54 CYS H H 9.227 0.000 1 307 . 54 CYS HA H 5.113 0.000 1 308 . 54 CYS HB2 H 3.443 0.000 1 309 . 54 CYS HB3 H 3.658 0.000 1 310 . 55 ASN H H 8.547 0.000 1 311 . 55 ASN HA H 5.177 0.000 1 312 . 55 ASN HB2 H 2.639 0.000 1 313 . 55 ASN HB3 H 3.372 0.000 1 314 . 55 ASN HD21 H 6.728 0.000 1 315 . 55 ASN HD22 H 7.536 0.000 1 316 . 56 THR H H 7.590 0.006 1 317 . 56 THR HA H 4.717 0.000 1 318 . 56 THR HB H 4.297 0.000 1 319 . 56 THR HG2 H 1.206 0.000 1 320 . 57 ASP H H 8.232 0.000 1 321 . 57 ASP HA H 4.817 0.004 1 322 . 57 ASP HB2 H 2.493 0.005 1 323 . 57 ASP HB3 H 2.272 0.005 1 324 . 58 ARG H H 9.649 0.000 1 325 . 58 ARG HA H 3.397 0.000 1 326 . 58 ARG HB2 H 1.798 0.000 1 327 . 58 ARG HB3 H 2.192 0.000 1 328 . 58 ARG HG2 H 1.321 0.000 1 329 . 58 ARG HG3 H 1.370 0.000 1 330 . 58 ARG HE H 7.850 0.000 1 331 . 59 CYS H H 7.583 0.000 1 332 . 59 CYS HA H 4.465 0.000 1 333 . 59 CYS HB2 H 3.365 0.000 1 334 . 59 CYS HB3 H 3.649 0.000 1 335 . 60 ASN H H 8.956 0.000 1 336 . 60 ASN HA H 4.382 0.000 1 337 . 60 ASN HB2 H 2.774 0.000 1 338 . 60 ASN HB3 H 2.310 0.000 1 339 . 60 ASN HD21 H 7.563 0.000 1 340 . 60 ASN HD22 H 7.752 0.000 1 stop_ save_ ######################## # Coupling constants # ######################## save_J_values_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name 'CTI major form' _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 LYS H 2 LYS HA 9.2 . . 0.4 2 3JHNHA 3 CYS H 3 CYS HA 10.5 . . 0.4 3 3JHNHA 5 LYS H 5 LYS HA 7.9 . . 0.4 4 3JHNHA 6 LEU H 6 LEU HA 3.6 . . 0.4 5 3JHNHA 7 VAL H 7 VAL HA 8.3 . . 0.4 6 3JHNHA 9 ILE H 9 ILE HA 8.5 . . 0.4 7 3JHNHA 10 ALA H 10 ALA HA 6.2 . . 0.4 8 3JHNHA 11 TYR H 11 TYR HA 9.0 . . 0.4 9 3JHNHA 12 LYS H 12 LYS HA 9.9 . . 0.4 10 3JHNHA 13 THR H 13 THR HA 9.0 . . 0.4 11 3JHNHA 14 CYS H 14 CYS HA 5.3 . . 0.4 12 3JHNHA 16 GLU H 16 GLU HA 4.2 . . 0.4 13 3JHNHA 18 LYS H 18 LYS HA 8.6 . . 0.4 14 3JHNHA 19 ASN H 19 ASN HA 9.7 . . 0.4 15 3JHNHA 20 LEU H 20 LEU HA 8.5 . . 0.4 16 3JHNHA 22 TYR H 22 TYR HA 10.0 . . 0.4 17 3JHNHA 21 CYS H 21 CYS HA 10.4 . . 0.4 18 3JHNHA 23 LYS H 23 LYS HA 3.6 . . 0.4 19 3JHNHA 24 MET H 24 MET HA 9.8 . . 0.4 20 3JHNHA 25 PHE H 25 PHE HA 9.0 . . 0.4 21 3JHNHA 26 MET H 26 MET HA 7.4 . . 0.4 22 3JHNHA 27 MET H 27 MET HA 5.5 . . 0.4 23 3JHNHA 28 SER H 28 SER HA 5.3 . . 0.4 24 3JHNHA 29 ASP H 29 ASP HA 5.6 . . 0.4 25 3JHNHA 30 LEU H 30 LEU HA 6.5 . . 0.4 26 3JHNHA 31 THR H 31 THR HA 7.0 . . 1.0 27 3JHNHA 34 VAL H 34 VAL HA 10.1 . . 0.4 28 3JHNHA 36 ARG H 36 ARG HA 8.1 . . 0.4 29 3JHNHA 38 CYS H 38 CYS HA 9.7 . . 0.4 30 3JHNHA 39 ILE H 39 ILE HA 7.5 . . 0.4 31 3JHNHA 40 ASP H 40 ASP HA 8.0 . . 0.4 32 3JHNHA 41 VAL H 41 VAL HA 10.5 . . 0.4 33 3JHNHA 42 CYS H 42 CYS HA 5.7 . . 0.4 34 3JHNHA 44 LYS H 44 LYS HA 5.8 . . 0.4 35 3JHNHA 45 ASN H 45 ASN HA 6.3 . . 0.4 36 3JHNHA 46 SER H 46 SER HA 8.3 . . 0.4 37 3JHNHA 47 LEU H 47 LEU HA 6.5 . . 1.0 38 3JHNHA 48 LEU H 48 LEU HA 8.8 . . 0.4 39 3JHNHA 49 VAL H 49 VAL HA 10.3 . . 0.4 40 3JHNHA 51 TYR H 51 TYR HA 10.4 . . 0.4 41 3JHNHA 52 VAL H 52 VAL HA 8.9 . . 0.4 42 3JHNHA 53 CYS H 53 CYS HA 9.7 . . 0.4 43 3JHNHA 54 CYS H 54 CYS HA 7.4 . . 0.4 44 3JHNHA 55 ASN H 55 ASN HA 9.3 . . 0.4 45 3JHNHA 56 THR H 56 THR HA 9.4 . . 0.4 46 3JHNHA 58 ARG H 58 ARG HA 9.2 . . 0.4 47 3JHNHA 60 ASN H 60 ASN HA 8.4 . . 0.4 48 3JHAHB 2 LYS HA 2 LYS HB2 11.7 . . 0.8 49 3JHAHB 3 CYS HA 3 CYS HB2 12.3 . . 0.5 50 3JHAHB 4 ASN HA 4 ASN HB2 12.4 . . 0.5 51 3JHAHB 5 LYS HA 5 LYS HB2 13.2 . . 0.5 52 3JHAHB 6 LEU HA 6 LEU HB3 11.6 . . 0.5 53 3JHAHB 7 VAL HA 7 VAL HB 10.1 . . 0.5 54 3JHAHB 8 PRO HA 8 PRO HB2 8.5 . . 0.5 55 3JHAHB 9 ILE HA 9 ILE HB 5.2 . . 0.5 56 3JHAHB 11 TYR HA 11 TYR HB2 4.4 . . 0.5 57 3JHAHB 13 THR HA 13 THR HB 9.4 . . 0.5 58 3JHAHB 14 CYS HA 14 CYS HB2 13.5 . . 0.5 59 3JHAHB 15 PRO HA 15 PRO HB3 9.5 . . 1.0 60 3JHAHB 15 PRO HA 15 PRO HB2 5.5 . . 1.0 61 3JHAHB 16 GLU HA 16 GLU HB2 12.5 . . 0.5 62 3JHAHB 19 ASN HA 19 ASN HB3 11.5 . . 0.5 63 3JHAHB 19 ASN HA 19 ASN HB2 4.7 . . 0.5 64 3JHAHB 20 LEU HA 20 LEU HB2 12.4 . . 0.5 65 3JHAHB 21 CYS HA 21 CYS HB2 12.8 . . 1.0 66 3JHAHB 23 LYS HA 23 LYS HB2 4.9 . . 0.5 67 3JHAHB 24 MET HA 24 MET HB2 12.0 . . 0.5 68 3JHAHB 25 PHE HA 25 PHE HB2 12.7 . . 0.5 69 3JHAHB 26 MET HA 26 MET HB2 13.7 . . 0.5 70 3JHAHB 27 MET HA 27 MET HB2 11.5 . . 0.5 71 3JHAHB 29 ASP HA 29 ASP HB3 12.4 . . 0.5 72 3JHAHB 30 LEU HA 30 LEU HB2 13.1 . . 0.5 73 3JHAHB 31 THR HA 31 THR HB 5.3 . . 0.5 74 3JHAHB 32 ILE HA 32 ILE HB 9.8 . . 0.5 75 3JHAHB 34 VAL HA 34 VAL HB 5.1 . . 0.5 76 3JHAHB 35 LYS HA 35 LYS HB2 11.7 . . 0.5 77 3JHAHB 35 LYS HA 35 LYS HB3 5.0 . . 0.5 78 3JHAHB 36 ARG HA 36 ARG HB2 10.9 . . 1.0 79 3JHAHB 38 CYS HA 38 CYS HB3 3.5 . . 0.5 80 3JHAHB 38 CYS HA 38 CYS HB2 12.4 . . 0.5 81 3JHAHB 39 ILE HA 39 ILE HB 2.0 . . 0.5 82 3JHAHB 41 VAL HA 41 VAL HB 8.9 . . 0.5 83 3JHAHB 42 CYS HA 42 CYS HB3 11.2 . . 0.5 84 3JHAHB 43 PRO HA 43 PRO HB3 9.4 . . 0.5 85 3JHAHB 43 PRO HA 43 PRO HB2 8.8 . . 0.5 86 3JHAHB 44 LYS HA 44 LYS HB2 11.9 . . 0.5 87 3JHAHB 45 ASN HA 45 ASN HB2 11.8 . . 0.5 88 3JHAHB 46 SER HA 46 SER HB3 3.2 . . 1.0 89 3JHAHB 46 SER HA 46 SER HB2 3.2 . . 0.5 90 3JHAHB 47 LEU HA 47 LEU HB2 13.2 . . 0.5 91 3JHAHB 48 LEU HA 48 LEU HB3 4.3 . . 0.5 92 3JHAHB 48 LEU HA 48 LEU HB2 12.0 . . 0.5 93 3JHAHB 49 VAL HA 49 VAL HB 6.2 . . 0.5 94 3JHAHB 50 LYS HA 50 LYS HB3 12.4 . . 0.5 95 3JHAHB 51 TYR HA 51 TYR HB2 12.1 . . 0.5 96 3JHAHB 52 VAL HA 52 VAL HB 10.6 . . 0.5 97 3JHAHB 53 CYS HA 53 CYS HB2 12.4 . . 0.5 98 3JHAHB 53 CYS HA 53 CYS HB3 4.0 . . 0.5 99 3JHAHB 54 CYS HA 54 CYS HB2 5.1 . . 0.5 100 3JHAHB 55 ASN HA 55 ASN HB2 3.3 . . 0.5 101 3JHAHB 55 ASN HA 55 ASN HB3 4.4 . . 0.5 102 3JHAHB 57 ASP HA 57 ASP HB2 11.0 . . 0.5 103 3JHAHB 58 ARG HA 58 ARG HB2 12.8 . . 0.5 104 3JHAHB 59 CYS HA 59 CYS HB2 2.6 . . 0.5 105 3JHAHB 59 CYS HA 59 CYS HB3 4.0 . . 0.5 106 3JHAHB 60 ASN HA 60 ASN HB3 3.9 . . 1.0 107 3JHAHB 60 ASN HA 60 ASN HB2 3.6 . . 1.0 stop_ save_