data_4396 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Anticoagulant protein from the nematode Ancylostoma caninum ; _BMRB_accession_number 4396 _BMRB_flat_file_name bmr4396.str _Entry_type original _Submission_date 1999-09-09 _Accession_date 1999-09-09 _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 Duggan Brendan M. . 2 Dyson H. Jane . 3 Wright Peter E. . 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" 463 "13C chemical shifts" 22 "15N chemical shifts" 85 "coupling constants" 76 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-06-19 original author . stop_ _Original_release_date 2007-06-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Inherent flexibility in a potent inhibitor of blood coagulation, recombinant nematode anticoagulant protein c2 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99435967 _PubMed_ID 10504384 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Duggan Brendan M. . 2 Dyson H. Jane . 3 Wright Peter E. . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_volume 265 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 539 _Page_last 548 _Year 1999 _Details . loop_ _Keyword anticoagulant 'protease inhibitor' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_4 _Saveframe_category citation _Citation_full ; Stassens P, Bergum PW, Gansemans Y, Jespers L, Laroche Y, Huang S, Maki S, Messens J, Lauwereys M, Cappello M, Hotez PJ, Lasters I, Vlasuk GP. Anticoagulant repertoire of the hookworm Ancylostoma caninum. Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2149-54. ; _Citation_title 'Anticoagulant repertoire of the hookworm Ancylostoma caninum.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8700900 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Stassens P . . 2 Bergum 'P W' W. . 3 Gansemans Y . . 4 Jespers L . . 5 Laroche Y . . 6 Huang S . . 7 Maki S . . 8 Messens J . . 9 Lauwereys M . . 10 Cappello M . . 11 Hotez 'P J' J. . 12 Lasters I . . 13 Vlasuk 'G P' P. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 93 _Journal_issue 5 _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 2149 _Page_last 2154 _Year 1996 _Details ; Hookworms are hematophagous nematodes that infect a wide range of mammalian hosts, including humans. There has been speculation for nearly a century as to the identity of the anticoagulant substances) used by these organisms to subvert host hemostasis. Using molecular cloning, we describe a family of potent small protein (75-84 amino acids) anticoagulants from the hookworm Ancylostoma caninum termed AcAP (A. caninum anticoagulant protein). Two recombinant AcAP members (AcAP5 and AcAP6) directly inhibited the catalytic activity of blood coagulation factor Xa (fXa), while a third form (AcAPc2) predominantly inhibited the catalytic activity of a complex composed of blood coagulation factor VIIa and tissue factor (fVIIa/TF). The inhibition of fVIIa/TF was by a unique mechanism that required the initial formation of a binary complex of the inhibitor with fXa at a site on the enzyme that is distinct from the catalytic center (exo-site). The sequence of AcAPc2 as well as the utilization of an exo-site on fXa distinguishes this inhibitor from the mammalian anticoagulant TFPI (tissue factor pathway inhibitor), which is functionally equivalent with respect to fXa-dependent inhibition of fIIa/TF. The relative sequence positions of the reactive site residues determined for AcAP5 with the homologous regions in AcAP6 and AcAPc2 as well as the pattern of 10 cysteine residues present in each of the inhibitors suggest that the AcAPs are distantly related to the family of small protein serine protease inhibitors found in the nonhematophagous nematode Ascaris lumbricoides var. suum. ; save_ save_ref_22 _Saveframe_category citation _Citation_full ; Guntert P, Mumenthaler C, Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol. 1997 Oct 17;273(1):283-98. ; _Citation_title 'Torsion angle dynamics for NMR structure calculation with the new program DYANA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9367762 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Guntert P . . 2 Mumenthaler C . . 3 Wuthrich K . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 273 _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 283 _Page_last 298 _Year 1997 _Details ; The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the "bundle" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures. ; save_ save_ref_24 _Saveframe_category citation _Citation_full ; Morris AL, MacArthur MW, Hutchinson EG, Thornton JM. Stereochemical quality of protein structure coordinates. Proteins. 1992 Apr;12(4):345-64. ; _Citation_title 'Stereochemical quality of protein structure coordinates.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 1579569 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Morris 'A L' L. . 2 MacArthur 'M W' W. . 3 Hutchinson 'E G' G. . 4 Thornton 'J M' M. . stop_ _Journal_abbreviation Proteins _Journal_name_full Proteins _Journal_volume 12 _Journal_issue 4 _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 345 _Page_last 364 _Year 1992 _Details ; Methods have been developed to assess the stereochemical quality of any protein structure both globally and locally using various criteria. Several parameters can be derived from the coordinates of a given structure. Global parameters include the distribution of phi, psi and chi 1 torsion angles, and hydrogen bond energies. There are clear correlations between these parameters and resolution; as the resolution improves, the distribution of the parameters becomes more clustered. These features show a broad distribution about ideal values derived from high-resolution structures. Some structures have tightly clustered distributions even at relatively low resolutions, while others show abnormal scatter though the data go to high resolution. Additional indicators of local irregularity include proline phi angles, peptide bond planarities, disulfide bond lengths, and their chi 3 torsion angles. These stereochemical parameters have been used to generate measures of stereochemical quality which provide a simple guide as to the reliability of a structure, in addition to the most important measures, resolution and R-factor. The parameters used in this evaluation are not novel, and are easily calculated from structure coordinates. A program suite is currently being developed which will quickly check a given structure, highlighting unusual stereochemistry and possible errors. ; save_ ################################## # Molecular system description # ################################## save_system_NAPc2 _Saveframe_category molecular_system _Mol_system_name 'Nematode Anticoagulant Protein c2' _Abbreviation_common NAPc2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label NAPc2 $NAPc2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function anticoagulant 'protease inhibitor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_NAPc2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Nematode Anticoagulant Protein c2' _Abbreviation_common NAPc2 _Molecular_mass 9643 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 85 _Mol_residue_sequence ; KATMQCGENEKYDSCGSKEC DKKCKYDGVEEEDDEEPNVP CLVRVCHQDCVCEEGFYRNK DDKCVSAEDCELDNMDFIYP GTRNP ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 ALA 3 THR 4 MET 5 GLN 6 CYS 7 GLY 8 GLU 9 ASN 10 GLU 11 LYS 12 TYR 13 ASP 14 SER 15 CYS 16 GLY 17 SER 18 LYS 19 GLU 20 CYS 21 ASP 22 LYS 23 LYS 24 CYS 25 LYS 26 TYR 27 ASP 28 GLY 29 VAL 30 GLU 31 GLU 32 GLU 33 ASP 34 ASP 35 GLU 36 GLU 37 PRO 38 ASN 39 VAL 40 PRO 41 CYS 42 LEU 43 VAL 44 ARG 45 VAL 46 CYS 47 HIS 48 GLN 49 ASP 50 CYS 51 VAL 52 CYS 53 GLU 54 GLU 55 GLY 56 PHE 57 TYR 58 ARG 59 ASN 60 LYS 61 ASP 62 ASP 63 LYS 64 CYS 65 VAL 66 SER 67 ALA 68 GLU 69 ASP 70 CYS 71 GLU 72 LEU 73 ASP 74 ASN 75 MET 76 ASP 77 PHE 78 ILE 79 TYR 80 PRO 81 GLY 82 THR 83 ARG 84 ASN 85 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-03-16 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1COU "Anticoagulant Protein From The Nematode Ancylostoma Caninum" 100.00 85 100.00 100.00 1.26e-52 PDB 2H9E "Crystal Structure Of FxaSELECTIDENAPC2 TERNARY COMPLEX" 98.82 84 100.00 100.00 1.17e-51 GB AAC47080 "anti-coagulant protein C2 precursor, partial [Ancylostoma caninum]" 98.82 91 100.00 100.00 1.15e-51 PRF 2208501A "anticoagulant protein:ISOTYPE=C2" 98.82 91 100.00 100.00 1.15e-51 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $NAPc2 'dog hookworm' 29170 Eukaryota Metazoa Ancylostoma caninum 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 $NAPc2 'recombinant technology' 'Pichia pastoris' Pichia pastoris GS115 pYAM7SP8 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'The 15N label is around 50-60%' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $NAPc2 2.0 mM '[U-55% 15N]' 'sodium chloride' 50 mM . DSS 20 uM . stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version '95 and 97' loop_ _Task 'data processing and analysis' stop_ _Details . save_ save_Dyana _Saveframe_category software _Name Dyana _Version 1.5 loop_ _Task 'molecular dynamics' stop_ _Details . _Citation_label $ref_22 save_ save_Amber _Saveframe_category software _Name Amber _Version 5.1 loop_ _Task 'molecular dynamics' stop_ _Details . save_ save_Procheck-NMR _Saveframe_category software _Name Procheck-NMR _Version 3.4.4 loop_ _Task 'structure analysis' stop_ _Details . _Citation_label $ref_24 save_ save_SANE _Saveframe_category software _Name SANE _Version 1 loop_ _Task 'In-house software: automated NOESY assignment and restraint generation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ save_spectrometer_5 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ save_DQ-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name DQ-COSY _Sample_label $sample_1 save_ save_15N_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _Sample_label $sample_1 save_ save_15N_NOESY-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '15N NOESY-HSQC' _Sample_label $sample_1 save_ save_15N_TOCSY-HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N TOCSY-HSQC' _Sample_label $sample_1 save_ save_15N_HSQC-NOESY-HSQ_6 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC-NOESY-HSQ' _Sample_label $sample_1 save_ save_HNHA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_13C_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC' _Sample_label $sample_1 save_ save_15N_{1H}_NOE_9 _Saveframe_category NMR_applied_experiment _Experiment_name '15N {1H} NOE' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 0.01 M pH 4.5 0.05 n/a pressure 1 . atm 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name NAPc2 _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 3.99 . . 2 . 1 LYS HB2 H 1.89 . . 3 . 1 LYS HB3 H 1.89 . . 4 . 1 LYS HG2 H 1.44 . . 5 . 1 LYS HG3 H 1.44 . . 6 . 2 ALA N N 127.737 . . 7 . 2 ALA CB C 19.3 . . 8 . 2 ALA H H 8.710 . . 9 . 2 ALA HA H 4.392 . . 10 . 2 ALA HB H 1.362 . . 11 . 3 THR N N 115.176 . . 12 . 3 THR CG2 C 21.5 . . 13 . 3 THR H H 8.125 . . 14 . 3 THR HA H 4.160 . . 15 . 3 THR HB H 3.994 . . 16 . 3 THR HG2 H 1.114 . . 17 . 4 MET N N 122.803 . . 18 . 4 MET CE C 17.1 . . 19 . 4 MET H H 7.737 . . 20 . 4 MET HA H 4.303 . . 21 . 4 MET HB2 H 1.910 . . 22 . 4 MET HB3 H 1.830 . . 23 . 4 MET HG2 H 2.37 . . 24 . 4 MET HG3 H 2.32 . . 25 . 4 MET HE H 2.08 . . 26 . 5 GLN N N 123.326 . . 27 . 5 GLN NE2 N 113.7 . . 28 . 5 GLN H H 8.355 . . 29 . 5 GLN HA H 4.371 . . 30 . 5 GLN HB2 H 2.060 . . 31 . 5 GLN HB3 H 1.940 . . 32 . 5 GLN HG2 H 2.332 . . 33 . 5 GLN HG3 H 2.332 . . 34 . 5 GLN HE21 H 7.488 . . 35 . 5 GLN HE22 H 6.780 . . 36 . 6 CYS N N 122.745 . . 37 . 6 CYS H H 8.515 . . 38 . 6 CYS HA H 5.054 . . 39 . 6 CYS HB2 H 3.369 . . 40 . 6 CYS HB3 H 2.643 . . 41 . 7 GLY N N 109.73 . . 42 . 7 GLY H H 8.437 . . 43 . 7 GLY HA2 H 4.355 . . 44 . 7 GLY HA3 H 3.576 . . 45 . 8 GLU N N 121.059 . . 46 . 8 GLU H H 8.299 . . 47 . 8 GLU HA H 3.926 . . 48 . 8 GLU HB2 H 1.926 . . 49 . 8 GLU HB3 H 1.926 . . 50 . 8 GLU HG2 H 2.333 . . 51 . 8 GLU HG3 H 2.333 . . 52 . 9 ASN N N 118.507 . . 53 . 9 ASN ND2 N 116.192 . . 54 . 9 ASN H H 8.942 . . 55 . 9 ASN HA H 3.732 . . 56 . 9 ASN HB2 H 2.647 . . 57 . 9 ASN HB3 H 1.245 . . 58 . 9 ASN HD21 H 7.346 . . 59 . 9 ASN HD22 H 6.841 . . 60 . 10 GLU N N 114.396 . . 61 . 10 GLU H H 7.194 . . 62 . 10 GLU HA H 5.152 . . 63 . 10 GLU HB2 H 1.943 . . 64 . 10 GLU HB3 H 1.613 . . 65 . 10 GLU HG2 H 2.133 . . 66 . 10 GLU HG3 H 2.067 . . 67 . 11 LYS N N 119.220 . . 68 . 11 LYS CG C 23.8 . . 69 . 11 LYS H H 9.524 . . 70 . 11 LYS HA H 4.688 . . 71 . 11 LYS HB2 H 1.711 . . 72 . 11 LYS HG2 H 1.180 . . 73 . 11 LYS HD2 H 1.637 . . 74 . 11 LYS HD3 H 1.637 . . 75 . 12 TYR N N 124.482 . . 76 . 12 TYR H H 8.592 . . 77 . 12 TYR HA H 4.620 . . 78 . 12 TYR HB2 H 3.074 . . 79 . 12 TYR HB3 H 2.782 . . 80 . 12 TYR HD1 H 6.920 . . 81 . 12 TYR HD2 H 6.920 . . 82 . 12 TYR HE1 H 6.686 . . 83 . 12 TYR HE2 H 6.686 . . 84 . 13 ASP N N 130.5 . . 85 . 13 ASP H H 8.453 . . 86 . 13 ASP HA H 4.588 . . 87 . 13 ASP HB2 H 2.508 . . 88 . 13 ASP HB3 H 2.234 . . 89 . 14 SER N N 120.197 . . 90 . 14 SER H H 8.359 . . 91 . 14 SER HA H 4.588 . . 92 . 14 SER HB2 H 4.045 . . 93 . 14 SER HB3 H 3.909 . . 94 . 15 CYS N N 124.85 . . 95 . 15 CYS H H 8.653 . . 96 . 15 CYS HA H 4.587 . . 97 . 15 CYS HB2 H 3.421 . . 98 . 15 CYS HB3 H 2.567 . . 99 . 16 GLY N N 111.383 . . 100 . 16 GLY H H 8.239 . . 101 . 16 GLY HA2 H 4.391 . . 102 . 16 GLY HA3 H 3.405 . . 103 . 17 SER N N 111.165 . . 104 . 17 SER H H 8.125 . . 105 . 17 SER HA H 4.885 . . 106 . 17 SER HB2 H 3.850 . . 107 . 17 SER HB3 H 3.554 . . 108 . 18 LYS N N 131.16 . . 109 . 18 LYS H H 9.249 . . 110 . 18 LYS HA H 4.160 . . 111 . 18 LYS HB2 H 1.892 . . 112 . 18 LYS HB3 H 1.749 . . 113 . 18 LYS HG2 H 1.438 . . 114 . 18 LYS HG3 H 1.438 . . 115 . 18 LYS HD2 H 1.595 . . 116 . 18 LYS HD3 H 1.595 . . 117 . 19 GLU N N 120.262 . . 118 . 19 GLU H H 8.553 . . 119 . 19 GLU HA H 4.172 . . 120 . 19 GLU HB2 H 2.100 . . 121 . 19 GLU HB3 H 1.984 . . 122 . 19 GLU HG2 H 2.387 . . 123 . 19 GLU HG3 H 2.387 . . 124 . 20 CYS N N 115.120 . . 125 . 20 CYS H H 7.638 . . 126 . 20 CYS HA H 4.782 . . 127 . 20 CYS HB2 H 3.479 . . 128 . 20 CYS HB3 H 3.111 . . 129 . 21 ASP N N 123.113 . . 130 . 21 ASP H H 7.481 . . 131 . 21 ASP HA H 4.546 . . 132 . 21 ASP HB2 H 2.801 . . 133 . 21 ASP HB3 H 2.726 . . 134 . 22 LYS N N 123.744 . . 135 . 22 LYS H H 8.942 . . 136 . 22 LYS HA H 4.353 . . 137 . 22 LYS HB2 H 1.949 . . 138 . 22 LYS HB3 H 1.949 . . 139 . 22 LYS HG2 H 1.560 . . 140 . 22 LYS HG3 H 1.560 . . 141 . 22 LYS HD2 H 1.695 . . 142 . 22 LYS HD3 H 1.695 . . 143 . 23 LYS N N 122.056 . . 144 . 23 LYS H H 8.591 . . 145 . 23 LYS HA H 4.978 . . 146 . 23 LYS HB2 H 2.097 . . 147 . 23 LYS HB3 H 2.097 . . 148 . 23 LYS HG2 H 1.556 . . 149 . 23 LYS HG3 H 1.556 . . 150 . 23 LYS HD2 H 1.696 . . 151 . 23 LYS HD3 H 1.696 . . 152 . 24 CYS N N 120.125 . . 153 . 24 CYS H H 8.396 . . 154 . 24 CYS HA H 4.082 . . 155 . 24 CYS HB2 H 2.722 . . 156 . 24 CYS HB3 H 2.642 . . 157 . 25 LYS HA H 4.199 . . 158 . 25 LYS HB2 H 2.10 . . 159 . 25 LYS HB3 H 1.98 . . 160 . 25 LYS HG2 H 1.24 . . 161 . 25 LYS HG3 H 1.24 . . 162 . 25 LYS HD2 H 1.609 . . 163 . 25 LYS HD3 H 1.609 . . 164 . 26 TYR N N 122.090 . . 165 . 26 TYR H H 8.225 . . 166 . 26 TYR HA H 4.625 . . 167 . 26 TYR HB2 H 3.168 . . 168 . 26 TYR HB3 H 2.776 . . 169 . 26 TYR HD1 H 7.054 . . 170 . 26 TYR HD2 H 7.054 . . 171 . 26 TYR HE1 H 6.841 . . 172 . 26 TYR HE2 H 6.841 . . 173 . 27 ASP N N 121.092 . . 174 . 27 ASP H H 8.240 . . 175 . 27 ASP HA H 4.593 . . 176 . 27 ASP HB2 H 2.721 . . 177 . 27 ASP HB3 H 2.721 . . 178 . 28 GLY N N 109.440 . . 179 . 28 GLY H H 8.100 . . 180 . 28 GLY HA2 H 4.007 . . 181 . 28 GLY HA3 H 3.848 . . 182 . 29 VAL N N 119.706 . . 183 . 29 VAL H H 7.852 . . 184 . 29 VAL HA H 4.102 . . 185 . 29 VAL HB H 2.099 . . 186 . 29 VAL HG1 H 0.897 . . 187 . 29 VAL HG2 H 0.897 . . 188 . 30 GLU N N 124.047 . . 189 . 30 GLU H H 8.471 . . 190 . 30 GLU HA H 4.316 . . 191 . 30 GLU HB2 H 2.099 . . 192 . 30 GLU HB3 H 1.982 . . 193 . 30 GLU HG2 H 2.34 . . 194 . 30 GLU HG3 H 2.34 . . 195 . 31 GLU N N 122.045 . . 196 . 31 GLU H H 8.319 . . 197 . 31 GLU HA H 4.315 . . 198 . 31 GLU HB2 H 2.101 . . 199 . 31 GLU HB3 H 1.983 . . 200 . 31 GLU HG2 H 2.372 . . 201 . 31 GLU HG3 H 2.372 . . 202 . 32 GLU N N 121.888 . . 203 . 32 GLU H H 8.356 . . 204 . 32 GLU HA H 4.316 . . 205 . 32 GLU HB2 H 2.101 . . 206 . 32 GLU HB3 H 1.983 . . 207 . 32 GLU HG2 H 2.390 . . 208 . 32 GLU HG3 H 2.390 . . 209 . 33 ASP N N 121.05 . . 210 . 33 ASP H H 8.41 . . 211 . 33 ASP HA H 4.648 . . 212 . 33 ASP HB2 H 2.837 . . 213 . 33 ASP HB3 H 2.757 . . 214 . 34 ASP N N 120.528 . . 215 . 34 ASP H H 8.280 . . 216 . 34 ASP HA H 4.652 . . 217 . 34 ASP HB2 H 2.840 . . 218 . 34 ASP HB3 H 2.762 . . 219 . 35 GLU N N 120.506 . . 220 . 35 GLU H H 8.187 . . 221 . 35 GLU HA H 4.337 . . 222 . 35 GLU HB2 H 2.139 . . 223 . 35 GLU HB3 H 1.985 . . 224 . 35 GLU HG2 H 2.410 . . 225 . 35 GLU HG3 H 2.410 . . 226 . 36 GLU N N 122.444 . . 227 . 36 GLU H H 8.163 . . 228 . 36 GLU HA H 4.647 . . 229 . 36 GLU HB2 H 2.126 . . 230 . 36 GLU HB3 H 1.947 . . 231 . 36 GLU HG2 H 2.432 . . 232 . 36 GLU HG3 H 2.432 . . 233 . 37 PRO CD C 50.8 . . 234 . 37 PRO HA H 4.404 . . 235 . 37 PRO HB2 H 2.290 . . 236 . 37 PRO HB3 H 2.017 . . 237 . 37 PRO HG2 H 1.899 . . 238 . 37 PRO HG3 H 1.899 . . 239 . 37 PRO HD2 H 3.763 . . 240 . 37 PRO HD3 H 3.685 . . 241 . 38 ASN N N 119.682 . . 242 . 38 ASN ND2 N 113.7 . . 243 . 38 ASN H H 8.537 . . 244 . 38 ASN HA H 4.684 . . 245 . 38 ASN HB2 H 2.836 . . 246 . 38 ASN HB3 H 2.765 . . 247 . 38 ASN HD21 H 7.602 . . 248 . 38 ASN HD22 H 6.923 . . 249 . 39 VAL N N 122.476 . . 250 . 39 VAL H H 8.006 . . 251 . 39 VAL HA H 4.392 . . 252 . 39 VAL HB H 2.119 . . 253 . 39 VAL HG1 H 0.953 . . 254 . 39 VAL HG2 H 0.953 . . 255 . 40 PRO HA H 4.368 . . 256 . 40 PRO HB2 H 2.289 . . 257 . 40 PRO HB3 H 2.092 . . 258 . 40 PRO HG2 H 1.978 . . 259 . 40 PRO HG3 H 1.820 . . 260 . 40 PRO HD2 H 3.813 . . 261 . 40 PRO HD3 H 3.685 . . 262 . 41 CYS N N 121.122 . . 263 . 41 CYS H H 8.435 . . 264 . 41 CYS HA H 4.511 . . 265 . 41 CYS HB2 H 3.189 . . 266 . 41 CYS HB3 H 3.111 . . 267 . 42 LEU N N 128.458 . . 268 . 42 LEU CB C 42.6 . . 269 . 42 LEU H H 8.437 . . 270 . 42 LEU HA H 4.430 . . 271 . 42 LEU HB2 H 1.634 . . 272 . 42 LEU HB3 H 1.559 . . 273 . 42 LEU HD1 H 0.891 . . 274 . 42 LEU HD2 H 0.853 . . 275 . 43 VAL N N 122.730 . . 276 . 43 VAL H H 8.105 . . 277 . 43 VAL HA H 4.082 . . 278 . 43 VAL HB H 2.024 . . 279 . 43 VAL HG1 H 0.877 . . 280 . 43 VAL HG2 H 0.877 . . 281 . 44 ARG N N 125.838 . . 282 . 44 ARG H H 8.436 . . 283 . 44 ARG HA H 4.239 . . 284 . 44 ARG HB2 H 1.909 . . 285 . 44 ARG HB3 H 1.787 . . 286 . 44 ARG HG2 H 1.618 . . 287 . 44 ARG HG3 H 1.618 . . 288 . 44 ARG HD2 H 3.17 . . 289 . 44 ARG HD3 H 3.17 . . 290 . 45 VAL N N 119.467 . . 291 . 45 VAL H H 7.597 . . 292 . 45 VAL HA H 4.105 . . 293 . 45 VAL HB H 1.924 . . 294 . 45 VAL HG1 H 0.857 . . 295 . 45 VAL HG2 H 0.857 . . 296 . 46 CYS N N 124.023 . . 297 . 46 CYS H H 8.632 . . 298 . 46 CYS HA H 4.549 . . 299 . 46 CYS HB2 H 3.111 . . 300 . 46 CYS HB3 H 2.840 . . 301 . 47 HIS HA H 4.85 . . 302 . 47 HIS HB2 H 3.26 . . 303 . 47 HIS HB3 H 3.26 . . 304 . 47 HIS HD2 H 7.35 . . 305 . 47 HIS HE1 H 8.70 . . 306 . 48 GLN N N 120.652 . . 307 . 48 GLN NE2 N 113.0 . . 308 . 48 GLN H H 8.406 . . 309 . 48 GLN HA H 4.85 . . 310 . 48 GLN HB2 H 2.29 . . 311 . 48 GLN HB3 H 2.10 . . 312 . 48 GLN HG2 H 2.47 . . 313 . 48 GLN HG3 H 2.47 . . 314 . 48 GLN HE21 H 7.539 . . 315 . 48 GLN HE22 H 6.879 . . 316 . 49 ASP N N 123.482 . . 317 . 49 ASP H H 8.550 . . 318 . 49 ASP HA H 4.862 . . 319 . 49 ASP HB2 H 2.487 . . 320 . 49 ASP HB3 H 2.257 . . 321 . 50 CYS N N 119.515 . . 322 . 50 CYS H H 8.644 . . 323 . 50 CYS HA H 5.209 . . 324 . 50 CYS HB2 H 2.957 . . 325 . 50 CYS HB3 H 2.841 . . 326 . 51 VAL N N 116.200 . . 327 . 51 VAL CG1 C 21.4 . . 328 . 51 VAL H H 8.709 . . 329 . 51 VAL HA H 4.666 . . 330 . 51 VAL HB H 2.839 . . 331 . 51 VAL HG1 H 0.757 . . 332 . 51 VAL HG2 H 0.643 . . 333 . 52 CYS N N 118.373 . . 334 . 52 CYS H H 9.449 . . 335 . 52 CYS HA H 4.912 . . 336 . 52 CYS HB2 H 3.151 . . 337 . 52 CYS HB3 H 2.647 . . 338 . 53 GLU N N 121.210 . . 339 . 53 GLU H H 8.328 . . 340 . 53 GLU HA H 3.965 . . 341 . 53 GLU HB2 H 1.655 . . 342 . 53 GLU HB3 H 1.655 . . 343 . 53 GLU HG2 H 2.099 . . 344 . 53 GLU HG3 H 2.099 . . 345 . 54 GLU N N 122.655 . . 346 . 54 GLU H H 8.666 . . 347 . 54 GLU HA H 4.047 . . 348 . 54 GLU HB2 H 2.061 . . 349 . 54 GLU HB3 H 1.986 . . 350 . 54 GLU HG2 H 2.396 . . 351 . 54 GLU HG3 H 2.396 . . 352 . 55 GLY N N 113.471 . . 353 . 55 GLY H H 8.512 . . 354 . 55 GLY HA2 H 4.060 . . 355 . 55 GLY HA3 H 3.452 . . 356 . 56 PHE N N 118.209 . . 357 . 56 PHE H H 7.735 . . 358 . 56 PHE HA H 4.859 . . 359 . 56 PHE HB2 H 3.036 . . 360 . 56 PHE HB3 H 2.645 . . 361 . 56 PHE HD1 H 6.727 . . 362 . 56 PHE HD2 H 6.727 . . 363 . 56 PHE HE1 H 7.192 . . 364 . 56 PHE HE2 H 7.192 . . 365 . 56 PHE HZ H 7.348 . . 366 . 57 TYR N N 120.327 . . 367 . 57 TYR H H 9.754 . . 368 . 57 TYR HA H 4.563 . . 369 . 57 TYR HB2 H 2.644 . . 370 . 57 TYR HB3 H 2.528 . . 371 . 57 TYR HD1 H 6.883 . . 372 . 57 TYR HD2 H 6.883 . . 373 . 57 TYR HE1 H 6.670 . . 374 . 57 TYR HE2 H 6.670 . . 375 . 58 ARG N N 120.097 . . 376 . 58 ARG H H 9.249 . . 377 . 58 ARG HA H 4.900 . . 378 . 58 ARG HB2 H 2.100 . . 379 . 58 ARG HB3 H 1.948 . . 380 . 58 ARG HG2 H 1.869 . . 381 . 58 ARG HG3 H 1.719 . . 382 . 59 ASN N N 127.920 . . 383 . 59 ASN ND2 N 113.6 . . 384 . 59 ASN H H 9.292 . . 385 . 59 ASN HA H 4.787 . . 386 . 59 ASN HB2 H 4.336 . . 387 . 59 ASN HB3 H 3.034 . . 388 . 59 ASN HD21 H 7.740 . . 389 . 59 ASN HD22 H 7.232 . . 390 . 60 LYS N N 119.505 . . 391 . 60 LYS H H 8.864 . . 392 . 60 LYS HA H 4.174 . . 393 . 60 LYS HB2 H 1.869 . . 394 . 60 LYS HB3 H 1.778 . . 395 . 60 LYS HG2 H 1.365 . . 396 . 60 LYS HG3 H 1.365 . . 397 . 60 LYS HD2 H 1.579 . . 398 . 60 LYS HD3 H 1.579 . . 399 . 61 ASP N N 119.503 . . 400 . 61 ASP H H 7.464 . . 401 . 61 ASP HA H 4.897 . . 402 . 61 ASP HB2 H 2.995 . . 403 . 61 ASP HB3 H 2.528 . . 404 . 62 ASP N N 117.211 . . 405 . 62 ASP CB C 39.1 . . 406 . 62 ASP H H 8.512 . . 407 . 62 ASP HA H 4.354 . . 408 . 62 ASP HB2 H 3.304 . . 409 . 62 ASP HB3 H 2.667 . . 410 . 63 LYS N N 120.606 . . 411 . 63 LYS H H 8.126 . . 412 . 63 LYS HA H 4.584 . . 413 . 63 LYS HB2 H 1.829 . . 414 . 63 LYS HB3 H 1.829 . . 415 . 63 LYS HG2 H 1.459 . . 416 . 63 LYS HG3 H 1.355 . . 417 . 63 LYS HD2 H 1.646 . . 418 . 63 LYS HD3 H 1.646 . . 419 . 64 CYS N N 122.460 . . 420 . 64 CYS H H 9.216 . . 421 . 64 CYS HA H 4.939 . . 422 . 64 CYS HB2 H 2.993 . . 423 . 64 CYS HB3 H 2.484 . . 424 . 65 VAL N N 120.922 . . 425 . 65 VAL CG2 C 18.6 . . 426 . 65 VAL H H 10.069 . . 427 . 65 VAL HA H 5.150 . . 428 . 65 VAL HB H 2.607 . . 429 . 65 VAL HG1 H 1.05 . . 430 . 65 VAL HG2 H 0.935 . . 431 . 66 SER N N 118.728 . . 432 . 66 SER H H 9.250 . . 433 . 66 SER HA H 4.242 . . 434 . 66 SER HB2 H 3.962 . . 435 . 66 SER HB3 H 3.962 . . 436 . 67 ALA N N 122.354 . . 437 . 67 ALA CA C 56.0 . . 438 . 67 ALA CB C 18.1 . . 439 . 67 ALA H H 8.941 . . 440 . 67 ALA HA H 3.644 . . 441 . 67 ALA HB H 1.323 . . 442 . 68 GLU N N 116.779 . . 443 . 68 GLU H H 8.512 . . 444 . 68 GLU HA H 4.048 . . 445 . 68 GLU HB2 H 2.061 . . 446 . 68 GLU HB3 H 1.983 . . 447 . 68 GLU HG2 H 2.464 . . 448 . 68 GLU HG3 H 2.373 . . 449 . 69 ASP N N 121.852 . . 450 . 69 ASP H H 7.852 . . 451 . 69 ASP HA H 4.665 . . 452 . 69 ASP HB2 H 3.032 . . 453 . 69 ASP HB3 H 2.760 . . 454 . 70 CYS N N 122.467 . . 455 . 70 CYS H H 8.278 . . 456 . 70 CYS HA H 4.368 . . 457 . 70 CYS HB2 H 3.205 . . 458 . 70 CYS HB3 H 2.896 . . 459 . 71 GLU N N 117.291 . . 460 . 71 GLU H H 7.675 . . 461 . 71 GLU HA H 4.236 . . 462 . 71 GLU HB2 H 2.215 . . 463 . 71 GLU HB3 H 2.103 . . 464 . 71 GLU HG2 H 2.486 . . 465 . 71 GLU HG3 H 2.486 . . 466 . 72 LEU N N 119.786 . . 467 . 72 LEU CB C 41.6 . . 468 . 72 LEU H H 7.617 . . 469 . 72 LEU HA H 4.224 . . 470 . 72 LEU HB2 H 1.901 . . 471 . 72 LEU HB3 H 1.649 . . 472 . 72 LEU HG H 1.769 . . 473 . 72 LEU HD1 H 0.965 . . 474 . 72 LEU HD2 H 0.888 . . 475 . 73 ASP N N 119.226 . . 476 . 73 ASP H H 7.870 . . 477 . 73 ASP HA H 4.567 . . 478 . 73 ASP HB3 H 2.898 . . 479 . 73 ASP HB2 H 2.778 . . 480 . 74 ASN N N 118.213 . . 481 . 74 ASN ND2 N 112.9 . . 482 . 74 ASN H H 7.834 . . 483 . 74 ASN HA H 4.665 . . 484 . 74 ASN HB2 H 2.892 . . 485 . 74 ASN HB3 H 2.666 . . 486 . 74 ASN HD21 H 7.504 . . 487 . 74 ASN HD22 H 6.725 . . 488 . 75 MET N N 120.800 . . 489 . 75 MET CE C 17.1 . . 490 . 75 MET H H 8.084 . . 491 . 75 MET HA H 4.406 . . 492 . 75 MET HB2 H 2.062 . . 493 . 75 MET HB3 H 1.974 . . 494 . 75 MET HG2 H 2.507 . . 495 . 75 MET HG3 H 2.507 . . 496 . 75 MET HE H 2.08 . . 497 . 76 ASP N N 120.094 . . 498 . 76 ASP H H 8.205 . . 499 . 76 ASP HA H 4.588 . . 500 . 76 ASP HB2 H 2.721 . . 501 . 76 ASP HB3 H 2.631 . . 502 . 77 PHE N N 120.586 . . 503 . 77 PHE H H 7.891 . . 504 . 77 PHE HA H 4.519 . . 505 . 77 PHE HB2 H 2.996 . . 506 . 77 PHE HB3 H 2.996 . . 507 . 77 PHE HD1 H 7.102 . . 508 . 77 PHE HD2 H 7.102 . . 509 . 77 PHE HE1 H 7.212 . . 510 . 77 PHE HE2 H 7.212 . . 511 . 77 PHE HZ H 7.32 . . 512 . 78 ILE N N 123.193 . . 513 . 78 ILE CB C 38.7 . . 514 . 78 ILE CG1 C 27.1 . . 515 . 78 ILE CG2 C 17.4 . . 516 . 78 ILE CD1 C 12.7 . . 517 . 78 ILE H H 7.735 . . 518 . 78 ILE HA H 4.041 . . 519 . 78 ILE HB H 1.673 . . 520 . 78 ILE HG12 H 1.340 . . 521 . 78 ILE HG13 H 1.063 . . 522 . 78 ILE HG2 H 0.72 . . 523 . 78 ILE HD1 H 0.78 . . 524 . 79 TYR N N 126.280 . . 525 . 79 TYR CA C 55.9 . . 526 . 79 TYR H H 8.221 . . 527 . 79 TYR HA H 4.743 . . 528 . 79 TYR HB3 H 3.046 . . 529 . 79 TYR HB2 H 2.894 . . 530 . 79 TYR HD1 H 7.190 . . 531 . 79 TYR HD2 H 7.190 . . 532 . 79 TYR HE1 H 6.842 . . 533 . 79 TYR HE2 H 6.842 . . 534 . 80 PRO CD C 50.8 . . 535 . 80 PRO HA H 4.40 . . 536 . 80 PRO HB2 H 2.253 . . 537 . 80 PRO HB3 H 1.981 . . 538 . 80 PRO HD2 H 3.82 . . 539 . 80 PRO HD3 H 3.54 . . 540 . 81 GLY N N 109.439 . . 541 . 81 GLY H H 8.046 . . 542 . 81 GLY HA2 H 4.01 . . 543 . 81 GLY HA3 H 3.97 . . 544 . 82 THR N N 114.580 . . 545 . 82 THR CG2 C 21.6 . . 546 . 82 THR H H 7.990 . . 547 . 82 THR HA H 4.339 . . 548 . 82 THR HB H 4.199 . . 549 . 82 THR HG2 H 1.226 . . 550 . 83 ARG N N 124.269 . . 551 . 83 ARG H H 8.357 . . 552 . 83 ARG HA H 4.353 . . 553 . 83 ARG HB2 H 1.831 . . 554 . 83 ARG HB3 H 1.750 . . 555 . 83 ARG HG2 H 1.595 . . 556 . 83 ARG HG3 H 1.595 . . 557 . 83 ARG HD2 H 3.14 . . 558 . 83 ARG HD3 H 3.14 . . 559 . 84 ASN N N 122.371 . . 560 . 84 ASN CA C 51.5 . . 561 . 84 ASN ND2 N 114.2 . . 562 . 84 ASN H H 8.454 . . 563 . 84 ASN HA H 4.960 . . 564 . 84 ASN HB2 H 2.827 . . 565 . 84 ASN HB3 H 2.644 . . 566 . 84 ASN HD21 H 7.602 . . 567 . 84 ASN HD22 H 6.899 . . 568 . 85 PRO CD C 50.5 . . 569 . 85 PRO HD2 H 3.73 . . 570 . 85 PRO HD3 H 3.68 . . stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_set_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 750 _Mol_system_component_name NAPc2 _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 ALA H 2 ALA HA 5.24 . . 0.1 2 3JHNHA 3 THR H 3 THR HA 7.13 . . 0.1 3 3JHNHA 4 MET H 4 MET HA 6.23 . . 0.1 4 3JHNHA 5 GLN H 5 GLN HA 7.44 . . 0.1 5 3JHNHA 6 CYS H 6 CYS HA 7.53 . . 0.1 6 3JHNHA 7 GLY H 7 GLY HA 6.62 . . 0.1 7 3JHNHA 8 GLU H 8 GLU HA 2.69 . . 0.1 8 3JHNHA 9 ASN H 9 ASN HA 6.37 . . 0.1 9 3JHNHA 10 GLU H 10 GLU HA 8.14 . . 0.1 10 3JHNHA 11 LYS H 11 LYS HA 8.11 . . 0.1 11 3JHNHA 12 TYR H 12 TYR HA 3.99 . . 0.1 12 3JHNHA 13 ASP H 13 ASP HA 8.67 . . 0.1 13 3JHNHA 14 SER H 14 SER HA 3.90 . . 0.1 14 3JHNHA 15 CYS H 15 CYS HA 6.40 . . 0.1 15 3JHNHA 16 GLY H 16 GLY HA 6.69 . . 0.1 16 3JHNHA 16 GLY H 16 GLY HA 1.82 . . 0.1 17 3JHNHA 17 SER H 17 SER HA 6.38 . . 0.1 18 3JHNHA 19 GLU H 19 GLU HA 5.50 . . 0.1 19 3JHNHA 20 CYS H 20 CYS HA 3.18 . . 0.1 20 3JHNHA 21 ASP H 21 ASP HA 4.13 . . 0.1 21 3JHNHA 22 LYS H 22 LYS HA 5.26 . . 0.1 22 3JHNHA 23 LYS H 23 LYS HA 7.53 . . 0.1 23 3JHNHA 26 TYR H 26 TYR HA 7.30 . . 0.1 24 3JHNHA 27 ASP H 27 ASP HA 5.65 . . 0.1 25 3JHNHA 28 GLY H 28 GLY HA 6.16 . . 0.1 26 3JHNHA 28 GLY H 28 GLY HA 4.58 . . 0.1 27 3JHNHA 29 VAL H 29 VAL HA 7.24 . . 0.1 28 3JHNHA 30 GLU H 30 GLU HA 6.05 . . 0.1 29 3JHNHA 31 GLU H 31 GLU HA 6.19 . . 0.1 30 3JHNHA 32 GLU H 32 GLU HA 6.49 . . 0.1 31 3JHNHA 33 ASP H 33 ASP HA 6.24 . . 0.1 32 3JHNHA 34 ASP H 34 ASP HA 7.08 . . 0.1 33 3JHNHA 35 GLU H 35 GLU HA 5.95 . . 0.1 34 3JHNHA 36 GLU H 36 GLU HA 6.56 . . 0.1 35 3JHNHA 38 ASN H 38 ASN HA 7.07 . . 0.1 36 3JHNHA 39 VAL H 39 VAL HA 7.09 . . 0.1 37 3JHNHA 41 CYS H 41 CYS HA 4.06 . . 0.1 38 3JHNHA 42 LEU H 42 LEU HA 6.79 . . 0.1 39 3JHNHA 43 VAL H 43 VAL HA 6.35 . . 0.1 40 3JHNHA 44 ARG H 44 ARG HA 6.62 . . 0.1 41 3JHNHA 45 VAL H 45 VAL HA 6.25 . . 0.1 42 3JHNHA 46 CYS H 46 CYS HA 4.20 . . 0.1 43 3JHNHA 48 GLN H 48 GLN HA 4.74 . . 0.1 44 3JHNHA 49 ASP H 49 ASP HA 6.43 . . 0.1 45 3JHNHA 50 CYS H 50 CYS HA 8.22 . . 0.1 46 3JHNHA 51 VAL H 51 VAL HA 8.18 . . 0.1 47 3JHNHA 53 GLU H 53 GLU HA 2.65 . . 0.1 48 3JHNHA 54 GLU H 54 GLU HA 2.31 . . 0.1 49 3JHNHA 55 GLY H 55 GLY HA 7.21 . . 0.1 50 3JHNHA 55 GLY H 55 GLY HA 4.14 . . 0.1 51 3JHNHA 56 PHE H 56 PHE HA 8.55 . . 0.1 52 3JHNHA 57 TYR H 57 TYR HA 8.56 . . 0.1 53 3JHNHA 58 ARG H 58 ARG HA 4.64 . . 0.1 54 3JHNHA 59 ASN H 59 ASN HA 6.73 . . 0.1 55 3JHNHA 61 ASP H 61 ASP HA 8.58 . . 0.1 56 3JHNHA 62 ASP H 62 ASP HA 5.21 . . 0.1 57 3JHNHA 63 LYS H 63 LYS HA 5.66 . . 0.1 58 3JHNHA 64 CYS H 64 CYS HA 6.27 . . 0.1 59 3JHNHA 65 VAL H 65 VAL HA 8.48 . . 0.1 60 3JHNHA 66 SER H 66 SER HA 3.68 . . 0.1 61 3JHNHA 67 ALA H 67 ALA HA 1.88 . . 0.1 62 3JHNHA 68 GLU H 68 GLU HA 4.00 . . 0.1 63 3JHNHA 69 ASP H 69 ASP HA 6.10 . . 0.1 64 3JHNHA 70 CYS H 70 CYS HA 4.05 . . 0.1 65 3JHNHA 71 GLU H 71 GLU HA 4.60 . . 0.1 66 3JHNHA 72 LEU H 72 LEU HA 4.63 . . 0.1 67 3JHNHA 73 ASP H 73 ASP HA 5.70 . . 0.1 68 3JHNHA 74 ASN H 74 ASN HA 7.18 . . 0.1 69 3JHNHA 75 MET H 75 MET HA 6.14 . . 0.1 70 3JHNHA 76 ASP H 76 ASP HA 6.15 . . 0.1 71 3JHNHA 77 PHE H 77 PHE HA 6.81 . . 0.1 72 3JHNHA 78 ILE H 78 ILE HA 7.60 . . 0.1 73 3JHNHA 79 TYR H 79 TYR HA 6.41 . . 0.1 74 3JHNHA 82 THR H 82 THR HA 7.11 . . 0.1 75 3JHNHA 83 ARG H 83 ARG HA 6.82 . . 0.1 76 3JHNHA 84 ASN H 84 ASN HA 14.09 . . 0.1 stop_ save_