data_4917 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of a lipid transfer protein extracted from rice seeds. Comparison with homologous proteins ; _BMRB_accession_number 4917 _BMRB_flat_file_name bmr4917.str _Entry_type original _Submission_date 2000-12-12 _Accession_date 2000-12-12 _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 Poznanski Jarek . . 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" 902 "coupling constants" 61 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-01-09 original author . stop_ _Original_release_date 2001-01-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of a lipid transfer protein extracted from rice seeds. Comparison with homologous proteins ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99192814 _PubMed_ID 10092854 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Poznanski Jaroslaw . . 2 Sodano Patric . . 3 Suh Se Won . 4 Lee Jae Young . 5 Ptak Marius . . 6 Vovelle Francoise . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_volume 259 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 692 _Page_last 708 _Year 1999 _Details . loop_ _Keyword 'Lipid transfer protein' NMR rice stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Yu YG, Chung CH, Fowler A, Suh SW. Amino acid sequence of a probable amylase/protease inhibitor from rice seeds. Arch Biochem Biophys. 1988 Sep;265(2):466-75. ; _Citation_title 'Amino acid sequence of a probable amylase/protease inhibitor from rice seeds.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 2458699 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yu Y.G. G. . 2 Chung C.H. H. . 3 Fowler A. . . 4 Suh S.W. W. . stop_ _Journal_abbreviation 'Arch. Biochem. Biophys.' _Journal_name_full 'Archives of biochemistry and biophysics' _Journal_volume 265 _Journal_issue 2 _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 466 _Page_last 475 _Year 1988 _Details ; The primary structure of a 9-kDa basic protein from rice seeds was determined by gas-phase sequencing of the intact protein and peptides derived from it by digestion with trypsin, chymotrypsin, and endopeptidase Lys-K. The protein consists of a single polypeptide chain of 91 amino acid residues with a calculated molecular mass of 8909 Da. It is rich in alanine, serine, glycine, and cysteine. The eight cysteines form four disulfide bonds. There is no methionine, histidine, phenylalanine, or tryptophan. The sequence is highly homologous with an alpha-amylase inhibitor, I-2, from seeds of Indian finger millet [F. A. P. Campos and M. Richardson (1984) FEBS Lett. 167, 221-225] and a 10-kDa barley seed protein, also called a probable amylase/protease inhibitor [B. Svensson et al. (1986) Carlsberg Res. Commun. 51, 493-500; J. Mundy and J. C. Rogers (1986) Planta 169, 51-63]. In analogy with the barley protein, the purified protein is tentatively called a rice probable amylase/protease inhibitor (PAPI). The rice PAPI does not show inhibitory activities against proteases and amylases tested. The amino acid sequence is as follows: Ile-Thr-Cys-Gly-Gln-Val-Asn-Ser-Ala-Val(10)-Gly-Pro-Cys-Leu-Thr-Tyr- Ala-Arg-Gly-Gly(20)-Ala-Gly-Pro-Ser-Ala-Ala-Cys-Cys-Ser-Gly(30)-Val-Arg- Ser-Leu-Lys-Ala-Ala-Ala-Ser-Thr(40)-Thr-Ala-Asp-Arg-Arg-Thr-Ala-Cys- Asn-Cys(50)-Leu-Lys-Asn-Ala-Ala-Arg-Gly-Ile-Lys-Gly(60)-Leu-Asn-Ala-Gly- Asn-Ala-Ala-Ser-Ile-Pro(70)-Ser-Lys-Cys-Gly-Val-Ser-Val-Pro-Tyr-Thr(80)- Ile-Ser-Ala-Ser-Ile-Asp-Cys-Ser-Arg-Val-Ser(91). ; save_ save_ref_2 _Saveframe_category citation _Citation_full . _Citation_title ; The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. ; _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 Bartels C. . . 2 Xia T.-H. . . 3 Billeter Martin . . 4 Guntert Peter . . 5 Wuthrich Kurt . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 6 _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 1 _Page_last 10 _Year 1995 _Details . save_ save_ref_3 _Saveframe_category citation _Citation_full ; Guntert P, Braun W, Wuthrich K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J Mol Biol. 1991 Feb 5;217(3):517-30. ; _Citation_title 'Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 1847217 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Guntert P. . . 2 Braun W. . . 3 Wuthrich K. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 217 _Journal_issue 3 _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 517 _Page_last 530 _Year 1991 _Details ; A novel procedure for efficient computation of three-dimensional protein structures from nuclear magnetic resonance (n.m.r.) data in solution is described, which is based on using the program DIANA in combination with the supporting programs CALIBA, HABAS and GLOMSA. The first part of this paper describes the new programs DIANA. CALIBA and GLOMSA. DIANA is a new, fully vectorized implementation of the variable target function algorithm for the computation of protein structures from n.m.r. data. Its main advantages, when compared to previously available programs using the variable target function algorithm, are a significant reduction of the computation time, and a novel treatment of experimental distance constraints involving diastereotopic groups of hydrogen atoms that were not individually assigned. CALIBA converts the measured nuclear Overhauser effects into upper distance limits and thus prepares the input for the previously described program HABAS and for DIANA. GLOMSA is used for obtaining individual assignments for pairs of diastereotopic substituents by comparison of the experimental constraints with preliminary results of the structure calculations. With its general outlay, the presently used combination of the four programs is particularly user-friendly. In the second part of the paper, initial results are presented on the influence of the novel DIANA treatment of diastereotopic protons on the quality of the structures obtained, and a systematic study of the central processing unit times needed for the same protein structure calculation on a range of different, commonly available computers is described. ; save_ save_ref_4 _Saveframe_category citation _Citation_full . _Citation_title 'X-PLOR, version 3.1: A system for X-ray crystallography and NMR' _Citation_status published _Citation_type book _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Brunger Axel T. . stop_ _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title 'X-PLOR, version 3.1: A system for X-ray crystallography and NMR' _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher 'Yale University Press' _Book_publisher_city 'New Haven' _Book_ISBN 0300054025 _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 1992 _Details . save_ ################################## # Molecular system description # ################################## save_rice_LTP _Saveframe_category molecular_system _Mol_system_name 'Lipid Transfer Protein' _Abbreviation_common LTP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'rice ns-LTP' $rLTP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_rLTP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Nonspecific Lipid Transfer Protein' _Abbreviation_common ns-LTP _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 91 _Mol_residue_sequence ; ITCGQVNSAVGPCLTYARGG AGPSAACCSGVRSLKAAAST TADRRTACNCLKNAARGIKG LNAGNAASIPSKCGVSVPYT ISASIDCSRVS ; loop_ _Residue_seq_code _Residue_label 1 ILE 2 THR 3 CYS 4 GLY 5 GLN 6 VAL 7 ASN 8 SER 9 ALA 10 VAL 11 GLY 12 PRO 13 CYS 14 LEU 15 THR 16 TYR 17 ALA 18 ARG 19 GLY 20 GLY 21 ALA 22 GLY 23 PRO 24 SER 25 ALA 26 ALA 27 CYS 28 CYS 29 SER 30 GLY 31 VAL 32 ARG 33 SER 34 LEU 35 LYS 36 ALA 37 ALA 38 ALA 39 SER 40 THR 41 THR 42 ALA 43 ASP 44 ARG 45 ARG 46 THR 47 ALA 48 CYS 49 ASN 50 CYS 51 LEU 52 LYS 53 ASN 54 ALA 55 ALA 56 ARG 57 GLY 58 ILE 59 LYS 60 GLY 61 LEU 62 ASN 63 ALA 64 GLY 65 ASN 66 ALA 67 ALA 68 SER 69 ILE 70 PRO 71 SER 72 LYS 73 CYS 74 GLY 75 VAL 76 SER 77 VAL 78 PRO 79 TYR 80 THR 81 ILE 82 SER 83 ALA 84 SER 85 ILE 86 ASP 87 CYS 88 SER 89 ARG 90 VAL 91 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue $rLTP Rice 4530 Eukaryota Viridiplantae Oryza sativa seed 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 $rLTP '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 $rLTP 5 mM . 'phosphate buffer' 50 mM . stop_ save_ ############################ # Computer software used # ############################ save_UXNMR _Saveframe_category software _Name UXNMR _Version 930601.3 loop_ _Task Processing stop_ _Details . _Citation_label $ref_2 save_ save_XEasy _Saveframe_category software _Name XEASY _Version 1.3.11 loop_ _Task 'signal assignment' stop_ _Details . _Citation_label $ref_2 save_ save_diana _Saveframe_category software _Name DIANA _Version 1.? loop_ _Task 'simulated annealing in the redac strategy' stop_ _Details . _Citation_label $ref_3 save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.1 loop_ _Task 'final refinement' stop_ _Details . _Citation_label $ref_4 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 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_ save_P-COSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name P-COSY _Sample_label $sample_1 save_ save_2Q-COSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name 2Q-COSY _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_t25 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 6.4 0.1 n/a temperature 298 1 K stop_ save_ save_t10 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 6.4 0.1 n/a temperature 283 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 DSS H 1 'methyl protons' ppm 0 external indirect cylindrical external_to_the_sample parallel_to_Bo 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_rtp25 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $t25 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'rice ns-LTP' _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 ILE HA H 4.30 0.02 1 2 . 1 ILE HB H 1.85 0.02 1 3 . 1 ILE HG2 H 0.85 0.02 1 4 . 1 ILE HG12 H 1.62 0.02 2 5 . 1 ILE HG13 H 1.27 0.02 2 6 . 1 ILE HD1 H 0.72 0.02 1 7 . 2 THR H H 8.01 0.02 1 8 . 2 THR HA H 4.88 0.02 1 9 . 2 THR HB H 4.67 0.02 1 10 . 2 THR HG2 H 1.27 0.02 1 11 . 3 CYS HA H 4.63 0.02 1 12 . 3 CYS HB2 H 3.37 0.02 2 13 . 3 CYS HB3 H 2.88 0.02 2 14 . 4 GLY HA2 H 3.92 0.02 2 15 . 4 GLY HA3 H 3.96 0.02 2 16 . 5 GLN H H 7.64 0.02 1 17 . 5 GLN HA H 4.14 0.02 1 18 . 5 GLN HB2 H 2.36 0.02 2 19 . 5 GLN HB3 H 2.04 0.02 2 20 . 5 GLN HG2 H 2.45 0.02 2 21 . 5 GLN HG3 H 2.36 0.02 2 22 . 5 GLN HE21 H 7.61 0.02 2 23 . 5 GLN HE22 H 6.92 0.02 2 24 . 6 VAL H H 7.83 0.02 1 25 . 6 VAL HA H 3.52 0.02 1 26 . 6 VAL HB H 2.19 0.02 1 27 . 6 VAL HG1 H 0.88 0.02 2 28 . 6 VAL HG2 H 0.98 0.02 2 29 . 7 ASN H H 8.88 0.02 1 30 . 7 ASN HA H 4.31 0.02 1 31 . 7 ASN HB2 H 2.83 0.02 2 32 . 7 ASN HB3 H 2.69 0.02 2 33 . 7 ASN HD21 H 7.24 0.02 2 34 . 7 ASN HD22 H 6.64 0.02 2 35 . 8 SER H H 7.94 0.02 1 36 . 8 SER HA H 4.28 0.02 1 37 . 8 SER HB2 H 3.99 0.02 1 38 . 8 SER HB3 H 3.99 0.02 1 39 . 9 ALA H H 7.70 0.02 1 40 . 9 ALA HA H 4.21 0.02 1 41 . 9 ALA HB H 1.57 0.02 1 42 . 10 VAL H H 7.44 0.02 1 43 . 10 VAL HA H 4.50 0.02 1 44 . 10 VAL HB H 2.27 0.02 1 45 . 10 VAL HG1 H 0.91 0.02 1 46 . 10 VAL HG2 H 0.91 0.02 1 47 . 11 GLY H H 7.68 0.02 1 48 . 11 GLY HA2 H 4.30 0.02 2 49 . 11 GLY HA3 H 4.05 0.02 2 50 . 12 PRO HA H 4.71 0.02 1 51 . 12 PRO HB2 H 1.34 0.02 2 52 . 12 PRO HB3 H 2.60 0.02 2 53 . 12 PRO HG2 H 2.02 0.02 2 54 . 12 PRO HG3 H 1.98 0.02 2 55 . 12 PRO HD2 H 3.62 0.02 2 56 . 12 PRO HD3 H 3.75 0.02 2 57 . 13 CYS H H 8.75 0.02 1 58 . 13 CYS HA H 4.83 0.02 1 59 . 13 CYS HB2 H 3.33 0.02 2 60 . 13 CYS HB3 H 3.40 0.02 2 61 . 14 LEU H H 8.14 0.02 1 62 . 14 LEU HA H 3.97 0.02 1 63 . 14 LEU HB2 H 2.08 0.02 2 64 . 14 LEU HB3 H 1.52 0.02 2 65 . 14 LEU HG H 2.00 0.02 1 66 . 14 LEU HD1 H 1.00 0.02 2 67 . 14 LEU HD2 H 0.77 0.02 2 68 . 15 THR HA H 4.01 0.02 1 69 . 15 THR HB H 4.29 0.02 1 70 . 15 THR HG2 H 1.43 0.02 1 71 . 16 TYR H H 7.33 0.02 1 72 . 16 TYR HA H 4.31 0.02 1 73 . 16 TYR HB2 H 3.42 0.02 2 74 . 16 TYR HB3 H 2.97 0.02 2 75 . 16 TYR HD1 H 6.9 0.02 1 76 . 16 TYR HD2 H 6.9 0.02 1 77 . 16 TYR HE1 H 6.7 0.02 1 78 . 16 TYR HE2 H 6.7 0.02 1 79 . 17 ALA H H 8.69 0.02 1 80 . 17 ALA HA H 3.72 0.02 1 81 . 17 ALA HB H 1.45 0.02 1 82 . 18 ARG H H 7.59 0.02 1 83 . 18 ARG HA H 4.55 0.02 1 84 . 18 ARG HB2 H 1.79 0.02 2 85 . 18 ARG HB3 H 2.23 0.02 2 86 . 18 ARG HG2 H 1.73 0.02 2 87 . 18 ARG HG3 H 1.34 0.02 2 88 . 18 ARG HD2 H 3.22 0.02 1 89 . 18 ARG HD3 H 3.22 0.02 1 90 . 18 ARG HE H 7.18 0.02 1 91 . 19 GLY H H 7.85 0.02 1 92 . 19 GLY HA2 H 3.52 0.02 2 93 . 19 GLY HA3 H 4.61 0.02 2 94 . 20 GLY H H 8.17 0.02 1 95 . 20 GLY HA2 H 4.38 0.02 2 96 . 20 GLY HA3 H 3.61 0.02 2 97 . 21 ALA H H 8.21 0.02 1 98 . 21 ALA HA H 4.48 0.02 1 99 . 21 ALA HB H 1.43 0.02 1 100 . 22 GLY H H 8.27 0.02 1 101 . 22 GLY HA2 H 3.27 0.02 2 102 . 22 GLY HA3 H 4.26 0.02 2 103 . 23 PRO HA H 4.09 0.02 1 104 . 23 PRO HB2 H 1.85 0.02 2 105 . 23 PRO HB3 H 1.91 0.02 2 106 . 23 PRO HG2 H 1.73 0.02 2 107 . 23 PRO HG3 H 1.41 0.02 2 108 . 23 PRO HD2 H 3.29 0.02 2 109 . 23 PRO HD3 H 2.47 0.02 2 110 . 24 SER H H 8.88 0.02 1 111 . 24 SER HA H 4.46 0.02 1 112 . 24 SER HB2 H 4.19 0.02 1 113 . 24 SER HB3 H 4.19 0.02 1 114 . 25 ALA H H 9.03 0.02 1 115 . 25 ALA HA H 4.17 0.02 1 116 . 25 ALA HB H 1.50 0.02 1 117 . 26 ALA H H 8.51 0.02 1 118 . 26 ALA HA H 4.25 0.02 1 119 . 26 ALA HB H 1.49 0.02 1 120 . 27 CYS H H 8.06 0.02 1 121 . 27 CYS HA H 4.37 0.02 1 122 . 27 CYS HB2 H 2.94 0.02 2 123 . 27 CYS HB3 H 3.43 0.02 2 124 . 28 CYS H H 8.21 0.02 1 125 . 28 CYS HA H 4.68 0.02 1 126 . 28 CYS HB2 H 2.84 0.02 2 127 . 28 CYS HB3 H 3.17 0.02 2 128 . 29 SER H H 8.96 0.02 1 129 . 29 SER HA H 4.25 0.02 1 130 . 29 SER HB2 H 4.02 0.02 1 131 . 29 SER HB3 H 4.02 0.02 1 132 . 30 GLY H H 8.16 0.02 1 133 . 30 GLY HA2 H 3.95 0.02 2 134 . 30 GLY HA3 H 4.47 0.02 2 135 . 31 VAL H H 8.44 0.02 1 136 . 31 VAL HA H 3.60 0.02 1 137 . 31 VAL HB H 2.22 0.02 1 138 . 31 VAL HG1 H 0.90 0.02 2 139 . 31 VAL HG2 H 1.09 0.02 2 140 . 32 ARG H H 8.34 0.02 1 141 . 32 ARG HA H 3.91 0.02 1 142 . 32 ARG HB2 H 2.04 0.02 2 143 . 32 ARG HB3 H 1.94 0.02 2 144 . 32 ARG HG2 H 1.59 0.02 2 145 . 32 ARG HG3 H 1.87 0.02 2 146 . 32 ARG HD2 H 3.34 0.02 2 147 . 32 ARG HD3 H 3.18 0.02 2 148 . 32 ARG HE H 7.37 0.02 1 149 . 33 SER H H 8.40 0.02 1 150 . 33 SER HA H 4.32 0.02 1 151 . 33 SER HB2 H 4.11 0.02 1 152 . 33 SER HB3 H 4.11 0.02 1 153 . 34 LEU H H 8.15 0.02 1 154 . 34 LEU HA H 4.10 0.02 1 155 . 34 LEU HB2 H 1.69 0.02 2 156 . 34 LEU HB3 H 2.02 0.02 2 157 . 34 LEU HG H 1.93 0.02 1 158 . 34 LEU HD1 H 0.91 0.02 1 159 . 34 LEU HD2 H 0.91 0.02 1 160 . 35 LYS H H 7.87 0.02 1 161 . 35 LYS HA H 4.18 0.02 1 162 . 35 LYS HB2 H 1.33 0.02 2 163 . 35 LYS HB3 H 1.98 0.02 2 164 . 35 LYS HG2 H 1.51 0.02 2 165 . 35 LYS HG3 H 1.43 0.02 2 166 . 35 LYS HD2 H 1.64 0.02 1 167 . 35 LYS HD3 H 1.64 0.02 1 168 . 35 LYS HE2 H 3.10 0.02 1 169 . 35 LYS HE3 H 3.10 0.02 1 170 . 36 ALA H H 7.47 0.02 1 171 . 36 ALA HA H 4.12 0.02 1 172 . 36 ALA HB H 1.50 0.02 1 173 . 37 ALA H H 7.73 0.02 1 174 . 37 ALA HA H 4.32 0.02 1 175 . 37 ALA HB H 1.49 0.02 1 176 . 38 ALA H H 7.98 0.02 1 177 . 38 ALA HA H 4.75 0.02 1 178 . 38 ALA HB H 1.16 0.02 1 179 . 39 SER H H 8.60 0.02 1 180 . 39 SER HA H 4.68 0.02 1 181 . 39 SER HB2 H 4.09 0.02 2 182 . 39 SER HB3 H 3.90 0.02 2 183 . 40 THR H H 7.74 0.02 1 184 . 40 THR HA H 4.92 0.02 1 185 . 40 THR HB H 4.66 0.02 1 186 . 40 THR HG2 H 1.32 0.02 1 187 . 41 THR H H 9.04 0.02 1 188 . 41 THR HA H 4.03 0.02 1 189 . 41 THR HB H 3.87 0.02 1 190 . 41 THR HG2 H 1.31 0.02 1 191 . 42 ALA H H 8.57 0.02 1 192 . 42 ALA HA H 4.05 0.02 1 193 . 42 ALA HB H 1.43 0.02 1 194 . 43 ASP H H 7.87 0.02 1 195 . 43 ASP HA H 4.46 0.02 1 196 . 43 ASP HB2 H 2.75 0.02 2 197 . 43 ASP HB3 H 2.52 0.02 2 198 . 44 ARG H H 8.54 0.02 1 199 . 44 ARG HA H 3.91 0.02 1 200 . 44 ARG HB2 H 1.93 0.02 2 201 . 44 ARG HB3 H 2.13 0.02 2 202 . 44 ARG HG2 H 1.91 0.02 2 203 . 44 ARG HG3 H 1.82 0.02 2 204 . 44 ARG HD2 H 3.89 0.02 1 205 . 44 ARG HD3 H 3.89 0.02 1 206 . 45 ARG H H 8.56 0.02 1 207 . 45 ARG HA H 3.87 0.02 1 208 . 45 ARG HB2 H 1.89 0.02 2 209 . 45 ARG HB3 H 1.81 0.02 2 210 . 45 ARG HG2 H 1.88 0.02 1 211 . 45 ARG HG3 H 1.88 0.02 1 212 . 45 ARG HE H 7.28 0.02 1 213 . 46 THR H H 8.35 0.02 1 214 . 46 THR HA H 4.01 0.02 1 215 . 46 THR HB H 4.24 0.02 1 216 . 46 THR HG2 H 1.16 0.02 1 217 . 47 ALA H H 8.63 0.02 1 218 . 47 ALA HA H 3.57 0.02 1 219 . 47 ALA HB H 0.92 0.02 1 220 . 48 CYS H H 8.05 0.02 1 221 . 48 CYS HA H 3.96 0.02 1 222 . 48 CYS HB2 H 2.79 0.02 2 223 . 48 CYS HB3 H 3.57 0.02 2 224 . 49 ASN H H 8.44 0.02 1 225 . 49 ASN HA H 4.46 0.02 1 226 . 49 ASN HB2 H 2.92 0.02 2 227 . 49 ASN HB3 H 2.77 0.02 2 228 . 49 ASN HD21 H 7.28 0.02 2 229 . 49 ASN HD22 H 7.24 0.02 2 230 . 50 CYS H H 8.88 0.02 1 231 . 50 CYS HA H 4.45 0.02 1 232 . 50 CYS HB2 H 3.02 0.02 2 233 . 50 CYS HB3 H 2.93 0.02 2 234 . 51 LEU H H 8.40 0.02 1 235 . 51 LEU HA H 4.06 0.02 1 236 . 51 LEU HB2 H 2.14 0.02 2 237 . 51 LEU HB3 H 1.37 0.02 2 238 . 51 LEU HG H 1.70 0.02 1 239 . 51 LEU HD1 H 0.68 0.02 1 240 . 51 LEU HD2 H 0.68 0.02 1 241 . 52 LYS H H 8.64 0.02 1 242 . 52 LYS HA H 4.56 0.02 1 243 . 52 LYS HB2 H 1.98 0.02 2 244 . 52 LYS HB3 H 2.06 0.02 2 245 . 52 LYS HG2 H 1.29 0.02 1 246 . 52 LYS HG3 H 1.29 0.02 1 247 . 52 LYS HD2 H 1.81 0.02 2 248 . 52 LYS HD3 H 1.72 0.02 2 249 . 52 LYS HE2 H 3.07 0.02 2 250 . 52 LYS HE3 H 2.98 0.02 2 251 . 53 ASN H H 8.01 0.02 1 252 . 53 ASN HA H 4.45 0.02 1 253 . 53 ASN HB2 H 2.93 0.02 2 254 . 53 ASN HB3 H 2.84 0.02 2 255 . 53 ASN HD21 H 7.59 0.02 2 256 . 53 ASN HD22 H 7.03 0.02 2 257 . 54 ALA H H 8.18 0.02 1 258 . 54 ALA HA H 4.16 0.02 1 259 . 54 ALA HB H 1.49 0.02 1 260 . 55 ALA H H 8.44 0.02 1 261 . 55 ALA HA H 3.79 0.02 1 262 . 55 ALA HB H 1.38 0.02 1 263 . 56 ARG H H 7.63 0.02 1 264 . 56 ARG HA H 4.08 0.02 1 265 . 56 ARG HB2 H 2.04 0.02 2 266 . 56 ARG HB3 H 1.97 0.02 2 267 . 56 ARG HG2 H 1.81 0.02 1 268 . 56 ARG HG3 H 1.81 0.02 1 269 . 56 ARG HD2 H 3.31 0.02 1 270 . 56 ARG HD3 H 3.31 0.02 1 271 . 56 ARG HE H 7.27 0.02 1 272 . 57 GLY H H 7.62 0.02 1 273 . 57 GLY HA2 H 4.35 0.02 2 274 . 57 GLY HA3 H 3.77 0.02 2 275 . 58 ILE H H 7.20 0.02 1 276 . 58 ILE HA H 4.06 0.02 1 277 . 58 ILE HB H 1.80 0.02 1 278 . 58 ILE HG2 H 0.73 0.02 1 279 . 58 ILE HG12 H 0.99 0.02 2 280 . 58 ILE HG13 H 1.89 0.02 2 281 . 58 ILE HD1 H 0.68 0.02 1 282 . 59 LYS H H 8.69 0.02 1 283 . 59 LYS HA H 4.31 0.02 1 284 . 59 LYS HB2 H 1.81 0.02 2 285 . 59 LYS HB3 H 1.72 0.02 2 286 . 59 LYS HG2 H 1.55 0.02 2 287 . 59 LYS HG3 H 1.45 0.02 2 288 . 59 LYS HD2 H 1.72 0.02 1 289 . 59 LYS HD3 H 1.72 0.02 1 290 . 59 LYS HE2 H 3.04 0.02 1 291 . 59 LYS HE3 H 3.04 0.02 1 292 . 60 GLY H H 8.96 0.02 1 293 . 60 GLY HA2 H 3.80 0.02 2 294 . 60 GLY HA3 H 4.00 0.02 2 295 . 61 LEU H H 7.41 0.02 1 296 . 61 LEU HA H 3.76 0.02 1 297 . 61 LEU HB2 H 1.70 0.02 2 298 . 61 LEU HB3 H 1.60 0.02 2 299 . 61 LEU HG H 1.38 0.02 1 300 . 61 LEU HD1 H 0.87 0.02 2 301 . 61 LEU HD2 H 0.94 0.02 2 302 . 62 ASN H H 9.29 0.02 1 303 . 62 ASN HA H 4.83 0.02 1 304 . 62 ASN HB2 H 2.37 0.02 2 305 . 62 ASN HB3 H 2.73 0.02 2 306 . 62 ASN HD21 H 7.72 0.02 2 307 . 62 ASN HD22 H 6.87 0.02 2 308 . 63 ALA H H 8.85 0.02 1 309 . 63 ALA HA H 4.05 0.02 1 310 . 63 ALA HB H 1.49 0.02 1 311 . 64 GLY H H 8.65 0.02 1 312 . 64 GLY HA2 H 3.88 0.02 2 313 . 64 GLY HA3 H 3.99 0.02 2 314 . 65 ASN H H 8.23 0.02 1 315 . 65 ASN HA H 4.16 0.02 1 316 . 65 ASN HB2 H 2.42 0.02 1 317 . 65 ASN HB3 H 2.42 0.02 1 318 . 65 ASN HD21 H 6.69 0.02 2 319 . 65 ASN HD22 H 6.82 0.02 2 320 . 66 ALA H H 8.66 0.02 1 321 . 66 ALA HA H 3.88 0.02 1 322 . 66 ALA HB H 1.59 0.02 1 323 . 67 ALA H H 8.09 0.02 1 324 . 67 ALA HA H 4.26 0.02 1 325 . 67 ALA HB H 1.60 0.02 1 326 . 68 SER H H 7.75 0.02 1 327 . 68 SER HA H 4.63 0.02 1 328 . 68 SER HB2 H 4.16 0.02 2 329 . 68 SER HB3 H 4.33 0.02 2 330 . 69 ILE H H 7.21 0.02 1 331 . 69 ILE HA H 3.72 0.02 1 332 . 69 ILE HB H 2.08 0.02 1 333 . 69 ILE HG2 H 1.00 0.02 1 334 . 69 ILE HG12 H 2.57 0.02 2 335 . 69 ILE HG13 H 1.24 0.02 2 336 . 69 ILE HD1 H 1.09 0.02 1 337 . 70 PRO HA H 4.01 0.02 1 338 . 70 PRO HB2 H 2.15 0.02 2 339 . 70 PRO HB3 H 2.45 0.02 2 340 . 70 PRO HG2 H 1.64 0.02 2 341 . 70 PRO HG3 H 2.39 0.02 2 342 . 70 PRO HD2 H 3.87 0.02 2 343 . 70 PRO HD3 H 3.72 0.02 2 344 . 71 SER H H 8.00 0.02 1 345 . 71 SER HA H 4.25 0.02 1 346 . 71 SER HB2 H 4.01 0.02 1 347 . 71 SER HB3 H 4.01 0.02 1 348 . 72 LYS H H 8.85 0.02 1 349 . 72 LYS HA H 4.18 0.02 1 350 . 72 LYS HB2 H 1.94 0.02 1 351 . 72 LYS HB3 H 1.94 0.02 1 352 . 72 LYS HG2 H 1.56 0.02 1 353 . 72 LYS HG3 H 1.56 0.02 1 354 . 72 LYS HD2 H 1.65 0.02 1 355 . 72 LYS HD3 H 1.65 0.02 1 356 . 72 LYS HE2 H 3.08 0.02 1 357 . 72 LYS HE3 H 3.08 0.02 1 358 . 73 CYS H H 8.15 0.02 1 359 . 73 CYS HA H 4.79 0.02 1 360 . 73 CYS HB2 H 2.91 0.02 2 361 . 73 CYS HB3 H 3.01 0.02 2 362 . 74 GLY H H 8.06 0.02 1 363 . 74 GLY HA2 H 3.93 0.02 2 364 . 74 GLY HA3 H 4.02 0.02 2 365 . 75 VAL H H 8.28 0.02 1 366 . 75 VAL HA H 4.33 0.02 1 367 . 75 VAL HB H 1.76 0.02 1 368 . 75 VAL HG1 H 0.85 0.02 2 369 . 75 VAL HG2 H 0.79 0.02 2 370 . 76 SER H H 8.68 0.02 1 371 . 76 SER HA H 4.54 0.02 1 372 . 76 SER HB2 H 3.79 0.02 2 373 . 76 SER HB3 H 3.73 0.02 2 374 . 77 VAL H H 7.64 0.02 1 375 . 77 VAL HA H 4.60 0.02 1 376 . 77 VAL HB H 1.04 0.02 1 377 . 77 VAL HG1 H 0.82 0.02 2 378 . 77 VAL HG2 H 0.61 0.02 2 379 . 78 PRO HA H 4.66 0.02 1 380 . 78 PRO HB2 H 2.12 0.02 2 381 . 78 PRO HB3 H 2.38 0.02 2 382 . 78 PRO HG2 H 1.74 0.02 2 383 . 78 PRO HG3 H 2.30 0.02 2 384 . 78 PRO HD2 H 3.19 0.02 2 385 . 78 PRO HD3 H 3.68 0.02 2 386 . 79 TYR H H 6.28 0.02 1 387 . 79 TYR HA H 4.75 0.02 1 388 . 79 TYR HB2 H 3.17 0.02 2 389 . 79 TYR HB3 H 2.76 0.02 2 390 . 79 TYR HD1 H 6.6 0.02 1 391 . 79 TYR HD2 H 6.6 0.02 1 392 . 79 TYR HE1 H 6.6 0.02 1 393 . 79 TYR HE2 H 6.6 0.02 1 394 . 80 THR H H 7.05 0.02 1 395 . 80 THR HA H 4.34 0.02 1 396 . 80 THR HB H 4.27 0.02 1 397 . 80 THR HG2 H 1.09 0.02 1 398 . 81 ILE H H 8.11 0.02 1 399 . 81 ILE HA H 3.84 0.02 1 400 . 81 ILE HB H 1.93 0.02 1 401 . 81 ILE HG2 H 0.78 0.02 1 402 . 81 ILE HG12 H 1.70 0.02 2 403 . 81 ILE HG13 H 0.98 0.02 2 404 . 81 ILE HD1 H 0.82 0.02 1 405 . 82 SER H H 6.99 0.02 1 406 . 82 SER HA H 4.51 0.02 1 407 . 82 SER HB2 H 3.85 0.02 2 408 . 82 SER HB3 H 3.26 0.02 2 409 . 83 ALA H H 9.11 0.02 1 410 . 83 ALA HA H 4.52 0.02 1 411 . 83 ALA HB H 1.40 0.02 1 412 . 84 SER H H 8.16 0.02 1 413 . 84 SER HA H 4.65 0.02 1 414 . 84 SER HB2 H 3.96 0.02 2 415 . 84 SER HB3 H 3.75 0.02 2 416 . 85 ILE H H 6.84 0.02 1 417 . 85 ILE HA H 4.02 0.02 1 418 . 85 ILE HB H 1.74 0.02 1 419 . 85 ILE HG2 H 1.09 0.02 1 420 . 85 ILE HG12 H 1.18 0.02 2 421 . 85 ILE HG13 H 1.59 0.02 2 422 . 85 ILE HD1 H 0.94 0.02 1 423 . 86 ASP H H 8.39 0.02 1 424 . 86 ASP HA H 4.88 0.02 1 425 . 86 ASP HB2 H 2.94 0.02 2 426 . 86 ASP HB3 H 2.64 0.02 2 427 . 87 CYS H H 8.81 0.02 1 428 . 87 CYS HA H 4.70 0.02 1 429 . 87 CYS HB2 H 3.19 0.02 2 430 . 87 CYS HB3 H 2.99 0.02 2 431 . 88 SER H H 8.56 0.02 1 432 . 88 SER HA H 4.25 0.02 1 433 . 88 SER HB2 H 3.99 0.02 1 434 . 88 SER HB3 H 3.99 0.02 1 435 . 89 ARG H H 7.24 0.02 1 436 . 89 ARG HA H 4.45 0.02 1 437 . 89 ARG HB2 H 2.16 0.02 2 438 . 89 ARG HB3 H 1.71 0.02 2 439 . 89 ARG HG2 H 1.58 0.02 2 440 . 89 ARG HD2 H 3.22 0.02 1 441 . 89 ARG HD3 H 3.22 0.02 1 442 . 89 ARG HE H 7.11 0.02 1 443 . 90 VAL H H 7.18 0.02 1 444 . 90 VAL HA H 4.01 0.02 1 445 . 90 VAL HB H 2.28 0.02 1 446 . 90 VAL HG1 H 1.04 0.02 2 447 . 90 VAL HG2 H 1.23 0.02 2 448 . 91 SER H H 8.10 0.02 1 449 . 91 SER HA H 4.47 0.02 1 450 . 91 SER HB2 H 3.90 0.02 1 451 . 91 SER HB3 H 3.90 0.02 1 stop_ save_ save_shift_rtp10 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $t10 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'rice ns-LTP' _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 ILE HA H 4.30 0.02 1 2 . 1 ILE HB H 1.85 0.02 1 3 . 1 ILE HG2 H 0.85 0.02 1 4 . 1 ILE HG12 H 1.62 0.02 2 5 . 1 ILE HG13 H 1.27 0.02 2 6 . 1 ILE HD1 H 0.72 0.02 1 7 . 2 THR H H 8.01 0.02 1 8 . 2 THR HA H 4.88 0.02 1 9 . 2 THR HB H 4.67 0.02 1 10 . 2 THR HG2 H 1.27 0.02 1 11 . 3 CYS HA H 4.63 0.02 1 12 . 3 CYS HB2 H 3.37 0.02 2 13 . 3 CYS HB3 H 2.88 0.02 2 14 . 4 GLY HA2 H 3.92 0.02 2 15 . 4 GLY HA3 H 3.96 0.02 2 16 . 5 GLN H H 7.64 0.02 1 17 . 5 GLN HA H 4.14 0.02 1 18 . 5 GLN HB2 H 2.36 0.02 2 19 . 5 GLN HB3 H 2.04 0.02 2 20 . 5 GLN HG2 H 2.45 0.02 2 21 . 5 GLN HG3 H 2.36 0.02 2 22 . 5 GLN HE21 H 7.61 0.02 2 23 . 5 GLN HE22 H 6.92 0.02 2 24 . 6 VAL H H 7.83 0.02 1 25 . 6 VAL HA H 3.52 0.02 1 26 . 6 VAL HB H 2.19 0.02 1 27 . 6 VAL HG1 H 0.88 0.02 2 28 . 6 VAL HG2 H 0.98 0.02 2 29 . 7 ASN H H 8.88 0.02 1 30 . 7 ASN HA H 4.31 0.02 1 31 . 7 ASN HB2 H 2.83 0.02 2 32 . 7 ASN HB3 H 2.69 0.02 2 33 . 7 ASN HD21 H 7.24 0.02 2 34 . 7 ASN HD22 H 6.64 0.02 2 35 . 8 SER H H 7.94 0.02 1 36 . 8 SER HA H 4.28 0.02 1 37 . 8 SER HB2 H 3.99 0.02 1 38 . 8 SER HB3 H 3.99 0.02 1 39 . 9 ALA H H 7.70 0.02 1 40 . 9 ALA HA H 4.21 0.02 1 41 . 9 ALA HB H 1.57 0.02 1 42 . 10 VAL H H 7.44 0.02 1 43 . 10 VAL HA H 4.50 0.02 1 44 . 10 VAL HB H 2.27 0.02 1 45 . 10 VAL HG1 H 0.91 0.02 1 46 . 10 VAL HG2 H 0.91 0.02 1 47 . 11 GLY H H 7.68 0.02 1 48 . 11 GLY HA2 H 4.30 0.02 2 49 . 11 GLY HA3 H 4.05 0.02 2 50 . 12 PRO HA H 4.71 0.02 1 51 . 12 PRO HB2 H 1.34 0.02 2 52 . 12 PRO HB3 H 2.60 0.02 2 53 . 12 PRO HG2 H 2.02 0.02 2 54 . 12 PRO HG3 H 1.98 0.02 2 55 . 12 PRO HD2 H 3.62 0.02 2 56 . 12 PRO HD3 H 3.75 0.02 2 57 . 13 CYS H H 8.75 0.02 1 58 . 13 CYS HA H 4.83 0.02 1 59 . 13 CYS HB2 H 3.33 0.02 2 60 . 13 CYS HB3 H 3.40 0.02 2 61 . 14 LEU H H 8.14 0.02 1 62 . 14 LEU HA H 3.97 0.02 1 63 . 14 LEU HB2 H 2.08 0.02 2 64 . 14 LEU HB3 H 1.52 0.02 2 65 . 14 LEU HG H 2.00 0.02 1 66 . 14 LEU HD1 H 1.00 0.02 2 67 . 14 LEU HD2 H 0.77 0.02 2 68 . 15 THR HA H 4.01 0.02 1 69 . 15 THR HB H 4.29 0.02 1 70 . 15 THR HG2 H 1.43 0.02 1 71 . 16 TYR H H 7.33 0.02 1 72 . 16 TYR HA H 4.31 0.02 1 73 . 16 TYR HB2 H 3.42 0.02 2 74 . 16 TYR HB3 H 2.97 0.02 2 75 . 16 TYR HD1 H 6.9 . 1 76 . 16 TYR HD2 H 6.9 . 1 77 . 16 TYR HE1 H 6.7 . 1 78 . 16 TYR HE2 H 6.7 . 1 79 . 17 ALA H H 8.69 0.02 1 80 . 17 ALA HA H 3.72 0.02 1 81 . 17 ALA HB H 1.45 0.02 1 82 . 18 ARG H H 7.59 0.02 1 83 . 18 ARG HA H 4.55 0.02 1 84 . 18 ARG HB2 H 1.79 0.02 2 85 . 18 ARG HB3 H 2.23 0.02 2 86 . 18 ARG HG2 H 1.73 0.02 2 87 . 18 ARG HG3 H 1.34 0.02 2 88 . 18 ARG HD2 H 3.22 0.02 1 89 . 18 ARG HD3 H 3.22 0.02 1 90 . 18 ARG HE H 7.18 0.02 1 91 . 19 GLY H H 7.85 0.02 1 92 . 19 GLY HA2 H 3.52 0.02 2 93 . 19 GLY HA3 H 4.61 0.02 2 94 . 20 GLY H H 8.17 0.02 1 95 . 20 GLY HA2 H 4.38 0.02 2 96 . 20 GLY HA3 H 3.61 0.02 2 97 . 21 ALA H H 8.21 0.02 1 98 . 21 ALA HA H 4.48 0.02 1 99 . 21 ALA HB H 1.43 0.02 1 100 . 22 GLY H H 8.27 0.02 1 101 . 22 GLY HA2 H 3.27 0.02 2 102 . 22 GLY HA3 H 4.26 0.02 2 103 . 23 PRO HA H 4.09 0.02 1 104 . 23 PRO HB2 H 1.85 0.02 2 105 . 23 PRO HB3 H 1.91 0.02 2 106 . 23 PRO HG2 H 1.73 0.02 2 107 . 23 PRO HG3 H 1.41 0.02 2 108 . 23 PRO HD2 H 3.29 0.02 2 109 . 23 PRO HD3 H 2.47 0.02 2 110 . 24 SER H H 8.88 0.02 1 111 . 24 SER HA H 4.46 0.02 1 112 . 24 SER HB2 H 4.19 0.02 1 113 . 24 SER HB3 H 4.19 0.02 1 114 . 25 ALA H H 9.03 0.02 1 115 . 25 ALA HA H 4.17 0.02 1 116 . 25 ALA HB H 1.50 0.02 1 117 . 26 ALA H H 8.51 0.02 1 118 . 26 ALA HA H 4.25 0.02 1 119 . 26 ALA HB H 1.49 0.02 1 120 . 27 CYS H H 8.06 0.02 1 121 . 27 CYS HA H 4.37 0.02 1 122 . 27 CYS HB2 H 2.94 0.02 2 123 . 27 CYS HB3 H 3.43 0.02 2 124 . 28 CYS H H 8.21 0.02 1 125 . 28 CYS HA H 4.68 0.02 1 126 . 28 CYS HB2 H 2.84 0.02 2 127 . 28 CYS HB3 H 3.17 0.02 2 128 . 29 SER H H 8.96 0.02 1 129 . 29 SER HA H 4.25 0.02 1 130 . 29 SER HB2 H 4.02 0.02 1 131 . 29 SER HB3 H 4.02 0.02 1 132 . 30 GLY H H 8.16 0.02 1 133 . 30 GLY HA2 H 3.95 0.02 2 134 . 30 GLY HA3 H 4.47 0.02 2 135 . 31 VAL H H 8.44 0.02 1 136 . 31 VAL HA H 3.60 0.02 1 137 . 31 VAL HB H 2.22 0.02 1 138 . 31 VAL HG1 H 0.90 0.02 2 139 . 31 VAL HG2 H 1.09 0.02 2 140 . 32 ARG H H 8.34 0.02 1 141 . 32 ARG HA H 3.91 0.02 1 142 . 32 ARG HB2 H 2.04 0.02 2 143 . 32 ARG HB3 H 1.94 0.02 2 144 . 32 ARG HG2 H 1.59 0.02 2 145 . 32 ARG HG3 H 1.87 0.02 2 146 . 32 ARG HD2 H 3.34 0.02 2 147 . 32 ARG HD3 H 3.18 0.02 2 148 . 32 ARG HE H 7.37 0.02 1 149 . 33 SER H H 8.40 0.02 1 150 . 33 SER HA H 4.32 0.02 1 151 . 33 SER HB2 H 4.11 0.02 1 152 . 33 SER HB3 H 4.11 0.02 1 153 . 34 LEU H H 8.15 0.02 1 154 . 34 LEU HA H 4.10 0.02 1 155 . 34 LEU HB2 H 1.69 0.02 2 156 . 34 LEU HB3 H 2.02 0.02 2 157 . 34 LEU HG H 1.93 0.02 1 158 . 34 LEU HD1 H 0.91 0.02 1 159 . 34 LEU HD2 H 0.91 0.02 1 160 . 35 LYS H H 7.87 0.02 1 161 . 35 LYS HA H 4.18 0.02 1 162 . 35 LYS HB2 H 1.33 0.02 2 163 . 35 LYS HB3 H 1.98 0.02 2 164 . 35 LYS HG2 H 1.51 0.02 2 165 . 35 LYS HG3 H 1.43 0.02 2 166 . 35 LYS HD2 H 1.64 0.02 1 167 . 35 LYS HD3 H 1.64 0.02 1 168 . 35 LYS HE2 H 3.10 0.02 1 169 . 35 LYS HE3 H 3.10 0.02 1 170 . 36 ALA H H 7.47 0.02 1 171 . 36 ALA HA H 4.12 0.02 1 172 . 36 ALA HB H 1.50 0.02 1 173 . 37 ALA H H 7.73 0.02 1 174 . 37 ALA HA H 4.32 0.02 1 175 . 37 ALA HB H 1.49 0.02 1 176 . 38 ALA H H 7.98 0.02 1 177 . 38 ALA HA H 4.75 0.02 1 178 . 38 ALA HB H 1.16 0.02 1 179 . 39 SER H H 8.60 0.02 1 180 . 39 SER HA H 4.68 0.02 1 181 . 39 SER HB2 H 4.09 0.02 2 182 . 39 SER HB3 H 3.90 0.02 2 183 . 40 THR H H 7.74 0.02 1 184 . 40 THR HA H 4.92 0.02 1 185 . 40 THR HB H 4.66 0.02 1 186 . 40 THR HG2 H 1.32 0.02 1 187 . 41 THR H H 9.04 0.02 1 188 . 41 THR HA H 4.03 0.02 1 189 . 41 THR HB H 3.87 0.02 1 190 . 41 THR HG2 H 1.31 0.02 1 191 . 42 ALA H H 8.57 0.02 1 192 . 42 ALA HA H 4.05 0.02 1 193 . 42 ALA HB H 1.43 0.02 1 194 . 43 ASP H H 7.87 0.02 1 195 . 43 ASP HA H 4.46 0.02 1 196 . 43 ASP HB2 H 2.75 0.02 2 197 . 43 ASP HB3 H 2.52 0.02 2 198 . 44 ARG H H 8.54 0.02 1 199 . 44 ARG HA H 3.91 0.02 1 200 . 44 ARG HB2 H 1.93 0.02 2 201 . 44 ARG HB3 H 2.13 0.02 2 202 . 44 ARG HG2 H 1.91 0.02 2 203 . 44 ARG HG3 H 1.82 0.02 2 204 . 44 ARG HD2 H 3.89 0.02 1 205 . 44 ARG HD3 H 3.89 0.02 1 206 . 45 ARG H H 8.56 0.02 1 207 . 45 ARG HA H 3.87 0.02 1 208 . 45 ARG HB2 H 1.89 0.02 2 209 . 45 ARG HB3 H 1.81 0.02 2 210 . 45 ARG HG2 H 1.88 0.02 1 211 . 45 ARG HG3 H 1.88 0.02 1 212 . 45 ARG HE H 7.28 0.02 1 213 . 46 THR H H 8.35 0.02 1 214 . 46 THR HA H 4.01 0.02 1 215 . 46 THR HB H 4.24 0.02 1 216 . 46 THR HG2 H 1.16 0.02 1 217 . 47 ALA H H 8.63 0.02 1 218 . 47 ALA HA H 3.57 0.02 1 219 . 47 ALA HB H 0.92 0.02 1 220 . 48 CYS H H 8.05 0.02 1 221 . 48 CYS HA H 3.96 0.02 1 222 . 48 CYS HB2 H 2.79 0.02 2 223 . 48 CYS HB3 H 3.57 0.02 2 224 . 49 ASN H H 8.44 0.02 1 225 . 49 ASN HA H 4.46 0.02 1 226 . 49 ASN HB2 H 2.92 0.02 2 227 . 49 ASN HB3 H 2.77 0.02 2 228 . 49 ASN HD21 H 7.28 0.02 2 229 . 49 ASN HD22 H 7.24 0.02 2 230 . 50 CYS H H 8.88 0.02 1 231 . 50 CYS HA H 4.45 0.02 1 232 . 50 CYS HB2 H 3.02 0.02 2 233 . 50 CYS HB3 H 2.93 0.02 2 234 . 51 LEU H H 8.40 0.02 1 235 . 51 LEU HA H 4.06 0.02 1 236 . 51 LEU HB2 H 2.14 0.02 2 237 . 51 LEU HB3 H 1.37 0.02 2 238 . 51 LEU HG H 1.70 0.02 1 239 . 51 LEU HD1 H 0.68 0.02 1 240 . 51 LEU HD2 H 0.68 0.02 1 241 . 52 LYS H H 8.64 0.02 1 242 . 52 LYS HA H 4.56 0.02 1 243 . 52 LYS HB2 H 1.98 0.02 2 244 . 52 LYS HB3 H 2.06 0.02 2 245 . 52 LYS HG2 H 1.29 0.02 1 246 . 52 LYS HG3 H 1.29 0.02 1 247 . 52 LYS HD2 H 1.81 0.02 2 248 . 52 LYS HD3 H 1.72 0.02 2 249 . 52 LYS HE2 H 3.07 0.02 2 250 . 52 LYS HE3 H 2.98 0.02 2 251 . 53 ASN H H 8.01 0.02 1 252 . 53 ASN HA H 4.45 0.02 1 253 . 53 ASN HB2 H 2.93 0.02 2 254 . 53 ASN HB3 H 2.84 0.02 2 255 . 53 ASN HD21 H 7.59 0.02 2 256 . 53 ASN HD22 H 7.03 0.02 2 257 . 54 ALA H H 8.18 0.02 1 258 . 54 ALA HA H 4.16 0.02 1 259 . 54 ALA HB H 1.49 0.02 1 260 . 55 ALA H H 8.44 0.02 1 261 . 55 ALA HA H 3.79 0.02 1 262 . 55 ALA HB H 1.38 0.02 1 263 . 56 ARG H H 7.63 0.02 1 264 . 56 ARG HA H 4.08 0.02 1 265 . 56 ARG HB2 H 2.04 0.02 2 266 . 56 ARG HB3 H 1.97 0.02 2 267 . 56 ARG HG2 H 1.81 0.02 1 268 . 56 ARG HG3 H 1.81 0.02 1 269 . 56 ARG HD2 H 3.31 0.02 1 270 . 56 ARG HD3 H 3.31 0.02 1 271 . 56 ARG HE H 7.27 0.02 1 272 . 57 GLY H H 7.62 0.02 1 273 . 57 GLY HA2 H 4.35 0.02 2 274 . 57 GLY HA3 H 3.77 0.02 2 275 . 58 ILE H H 7.20 0.02 1 276 . 58 ILE HA H 4.06 0.02 1 277 . 58 ILE HB H 1.80 0.02 1 278 . 58 ILE HG2 H 0.73 0.02 1 279 . 58 ILE HG12 H 0.99 0.02 2 280 . 58 ILE HG13 H 1.89 0.02 2 281 . 58 ILE HD1 H 0.68 0.02 1 282 . 59 LYS H H 8.69 0.02 1 283 . 59 LYS HA H 4.31 0.02 1 284 . 59 LYS HB2 H 1.81 0.02 2 285 . 59 LYS HB3 H 1.72 0.02 2 286 . 59 LYS HG2 H 1.55 0.02 2 287 . 59 LYS HG3 H 1.45 0.02 2 288 . 59 LYS HD2 H 1.72 0.02 1 289 . 59 LYS HD3 H 1.72 0.02 1 290 . 59 LYS HE2 H 3.04 0.02 1 291 . 59 LYS HE3 H 3.04 0.02 1 292 . 60 GLY H H 8.96 0.02 1 293 . 60 GLY HA2 H 3.80 0.02 2 294 . 60 GLY HA3 H 4.00 0.02 2 295 . 61 LEU H H 7.41 0.02 1 296 . 61 LEU HA H 3.76 0.02 1 297 . 61 LEU HB2 H 1.70 0.02 2 298 . 61 LEU HB3 H 1.60 0.02 2 299 . 61 LEU HG H 1.38 0.02 1 300 . 61 LEU HD1 H 0.87 0.02 2 301 . 61 LEU HD2 H 0.94 0.02 2 302 . 62 ASN H H 9.29 0.02 1 303 . 62 ASN HA H 4.83 0.02 1 304 . 62 ASN HB2 H 2.37 0.02 2 305 . 62 ASN HB3 H 2.73 0.02 2 306 . 62 ASN HD21 H 7.72 0.02 2 307 . 62 ASN HD22 H 6.87 0.02 2 308 . 63 ALA H H 8.85 0.02 1 309 . 63 ALA HA H 4.05 0.02 1 310 . 63 ALA HB H 1.49 0.02 1 311 . 64 GLY H H 8.65 0.02 1 312 . 64 GLY HA2 H 3.88 0.02 2 313 . 64 GLY HA3 H 3.99 0.02 2 314 . 65 ASN H H 8.23 0.02 1 315 . 65 ASN HA H 4.16 0.02 1 316 . 65 ASN HB2 H 2.42 0.02 1 317 . 65 ASN HB3 H 2.42 0.02 1 318 . 65 ASN HD21 H 6.69 0.02 2 319 . 65 ASN HD22 H 6.82 0.02 2 320 . 66 ALA H H 8.66 0.02 1 321 . 66 ALA HA H 3.88 0.02 1 322 . 66 ALA HB H 1.59 0.02 1 323 . 67 ALA H H 8.09 0.02 1 324 . 67 ALA HA H 4.26 0.02 1 325 . 67 ALA HB H 1.60 0.02 1 326 . 68 SER H H 7.75 0.02 1 327 . 68 SER HA H 4.63 0.02 1 328 . 68 SER HB2 H 4.16 0.02 2 329 . 68 SER HB3 H 4.33 0.02 2 330 . 69 ILE H H 7.21 0.02 1 331 . 69 ILE HA H 3.72 0.02 1 332 . 69 ILE HB H 2.08 0.02 1 333 . 69 ILE HG2 H 1.00 0.02 1 334 . 69 ILE HG12 H 2.57 0.02 2 335 . 69 ILE HG13 H 1.24 0.02 2 336 . 69 ILE HD1 H 1.09 0.02 1 337 . 70 PRO HA H 4.01 0.02 1 338 . 70 PRO HB2 H 2.15 0.02 2 339 . 70 PRO HB3 H 2.45 0.02 2 340 . 70 PRO HG2 H 1.64 0.02 2 341 . 70 PRO HG3 H 2.39 0.02 2 342 . 70 PRO HD2 H 3.87 0.02 2 343 . 70 PRO HD3 H 3.72 0.02 2 344 . 71 SER H H 8.00 0.02 1 345 . 71 SER HA H 4.25 0.02 1 346 . 71 SER HB2 H 4.01 0.02 1 347 . 71 SER HB3 H 4.01 0.02 1 348 . 72 LYS H H 8.85 0.02 1 349 . 72 LYS HA H 4.18 0.02 1 350 . 72 LYS HB2 H 1.94 0.02 1 351 . 72 LYS HB3 H 1.94 0.02 1 352 . 72 LYS HG2 H 1.56 0.02 1 353 . 72 LYS HG3 H 1.56 0.02 1 354 . 72 LYS HD2 H 1.65 0.02 1 355 . 72 LYS HD3 H 1.65 0.02 1 356 . 72 LYS HE2 H 3.08 0.02 1 357 . 72 LYS HE3 H 3.08 0.02 1 358 . 73 CYS H H 8.15 0.02 1 359 . 73 CYS HA H 4.79 0.02 1 360 . 73 CYS HB2 H 2.91 0.02 2 361 . 73 CYS HB3 H 3.01 0.02 2 362 . 74 GLY H H 8.06 0.02 1 363 . 74 GLY HA2 H 3.93 0.02 2 364 . 74 GLY HA3 H 4.02 0.02 2 365 . 75 VAL H H 8.28 0.02 1 366 . 75 VAL HA H 4.33 0.02 1 367 . 75 VAL HB H 1.76 0.02 1 368 . 75 VAL HG1 H 0.85 0.02 2 369 . 75 VAL HG2 H 0.79 0.02 2 370 . 76 SER H H 8.68 0.02 1 371 . 76 SER HA H 4.54 0.02 1 372 . 76 SER HB2 H 3.79 0.02 2 373 . 76 SER HB3 H 3.73 0.02 2 374 . 77 VAL H H 7.64 0.02 1 375 . 77 VAL HA H 4.60 0.02 1 376 . 77 VAL HB H 1.04 0.02 1 377 . 77 VAL HG1 H 0.82 0.02 2 378 . 77 VAL HG2 H 0.61 0.02 2 379 . 78 PRO HA H 4.66 0.02 1 380 . 78 PRO HB2 H 2.12 0.02 2 381 . 78 PRO HB3 H 2.38 0.02 2 382 . 78 PRO HG2 H 1.74 0.02 2 383 . 78 PRO HG3 H 2.30 0.02 2 384 . 78 PRO HD2 H 3.19 0.02 2 385 . 78 PRO HD3 H 3.68 0.02 2 386 . 79 TYR H H 6.28 0.02 1 387 . 79 TYR HA H 4.75 0.02 1 388 . 79 TYR HB2 H 3.17 0.02 2 389 . 79 TYR HB3 H 2.76 0.02 2 390 . 79 TYR HD1 H 6.6 . 1 391 . 79 TYR HD2 H 6.6 . 1 392 . 79 TYR HE1 H 6.6 . 1 393 . 79 TYR HE2 H 6.6 . 1 394 . 80 THR H H 7.05 0.02 1 395 . 80 THR HA H 4.34 0.02 1 396 . 80 THR HB H 4.27 0.02 1 397 . 80 THR HG2 H 1.09 0.02 1 398 . 81 ILE H H 8.11 0.02 1 399 . 81 ILE HA H 3.84 0.02 1 400 . 81 ILE HB H 1.93 0.02 1 401 . 81 ILE HG2 H 0.78 0.02 1 402 . 81 ILE HG12 H 1.70 0.02 2 403 . 81 ILE HG13 H 0.98 0.02 2 404 . 81 ILE HD1 H 0.82 0.02 1 405 . 82 SER H H 6.99 0.02 1 406 . 82 SER HA H 4.51 0.02 1 407 . 82 SER HB2 H 3.85 0.02 2 408 . 82 SER HB3 H 3.26 0.02 2 409 . 83 ALA H H 9.11 0.02 1 410 . 83 ALA HA H 4.52 0.02 1 411 . 83 ALA HB H 1.40 0.02 1 412 . 84 SER H H 8.16 0.02 1 413 . 84 SER HA H 4.65 0.02 1 414 . 84 SER HB2 H 3.96 0.02 2 415 . 84 SER HB3 H 3.75 0.02 2 416 . 85 ILE H H 6.84 0.02 1 417 . 85 ILE HA H 4.02 0.02 1 418 . 85 ILE HB H 1.74 0.02 1 419 . 85 ILE HG2 H 1.09 0.02 1 420 . 85 ILE HG12 H 1.18 0.02 2 421 . 85 ILE HG13 H 1.59 0.02 2 422 . 85 ILE HD1 H 0.94 0.02 1 423 . 86 ASP H H 8.39 0.02 1 424 . 86 ASP HA H 4.88 0.02 1 425 . 86 ASP HB2 H 2.94 0.02 2 426 . 86 ASP HB3 H 2.64 0.02 2 427 . 87 CYS H H 8.81 0.02 1 428 . 87 CYS HA H 4.70 0.02 1 429 . 87 CYS HB2 H 3.19 0.02 2 430 . 87 CYS HB3 H 2.99 0.02 2 431 . 88 SER H H 8.56 0.02 1 432 . 88 SER HA H 4.25 0.02 1 433 . 88 SER HB2 H 3.99 0.02 1 434 . 88 SER HB3 H 3.99 0.02 1 435 . 89 ARG H H 7.24 0.02 1 436 . 89 ARG HA H 4.45 0.02 1 437 . 89 ARG HB2 H 2.16 0.02 2 438 . 89 ARG HB3 H 1.71 0.02 2 439 . 89 ARG HG2 H 1.58 0.02 2 440 . 89 ARG HD2 H 3.22 0.02 1 441 . 89 ARG HD3 H 3.22 0.02 1 442 . 89 ARG HE H 7.11 0.02 1 443 . 90 VAL H H 7.18 0.02 1 444 . 90 VAL HA H 4.01 0.02 1 445 . 90 VAL HB H 2.28 0.02 1 446 . 90 VAL HG1 H 1.04 0.02 2 447 . 90 VAL HG2 H 1.23 0.02 2 448 . 91 SER H H 8.10 0.02 1 449 . 91 SER HA H 4.47 0.02 1 450 . 91 SER HB2 H 3.90 0.02 1 451 . 91 SER HB3 H 3.90 0.02 1 stop_ save_ ######################## # Coupling constants # ######################## save_J_values_rtp25 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $t25 _Spectrometer_frequency_1H 500 _Mol_system_component_name 'rice ns-LTP' _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 5 GLN H 5 GLN HA 5.65 . . . 2 3JHNHA 6 VAL H 6 VAL HA 5.70 . . . 3 3JHNHA 7 ASN H 7 ASN HA 5.29 . . . 4 3JHNHA 8 SER H 8 SER HA 5.18 . . . 5 3JHNHA 9 ALA H 9 ALA HA 5.09 . . . 6 3JHNHA 10 VAL H 10 VAL HA 4.29 . . . 7 3JHNHA 13 CYS H 13 CYS HA 8.01 . . . 8 3JHNHA 14 LEU H 14 LEU HA 4.85 . . . 9 3JHNHA 15 THR H 15 THR HA 5.30 . . . 10 3JHNHA 16 TYR H 16 TYR HA 5.92 . . . 11 3JHNHA 17 ALA H 17 ALA HA 4.73 . . . 12 3JHNHA 18 ARG H 18 ARG HA 8.40 . . . 13 3JHNHA 21 ALA H 21 ALA HA 5.25 . . . 14 3JHNHA 25 ALA H 25 ALA HA 4.37 . . . 15 3JHNHA 27 CYS H 27 CYS HA 5.03 . . . 16 3JHNHA 28 CYS H 28 CYS HA 4.90 . . . 17 3JHNHA 29 SER H 29 SER HA 4.94 . . . 18 3JHNHA 31 VAL H 31 VAL HA 4.73 . . . 19 3JHNHA 32 ARG H 32 ARG HA 4.89 . . . 20 3JHNHA 33 SER H 33 SER HA 4.98 . . . 21 3JHNHA 34 LEU H 34 LEU HA 4.74 . . . 22 3JHNHA 35 LYS H 35 LYS HA 4.72 . . . 23 3JHNHA 36 ALA H 36 ALA HA 4.84 . . . 24 3JHNHA 37 ALA H 37 ALA HA 6.99 . . . 25 3JHNHA 38 ALA H 38 ALA HA 7.81 . . . 26 3JHNHA 40 THR H 40 THR HA 4.79 . . . 27 3JHNHA 42 ALA H 42 ALA HA 6.93 . . . 28 3JHNHA 43 ASP H 43 ASP HA 5.79 . . . 29 3JHNHA 45 ARG H 45 ARG HA 5.81 . . . 30 3JHNHA 46 THR H 46 THR HA 5.57 . . . 31 3JHNHA 47 ALA H 47 ALA HA 6.26 . . . 32 3JHNHA 49 ASN H 49 ASN HA 5.62 . . . 33 3JHNHA 51 LEU H 51 LEU HA 5.31 . . . 34 3JHNHA 52 LYS H 52 LYS HA 4.60 . . . 35 3JHNHA 53 ASN H 53 ASN HA 4.44 . . . 36 3JHNHA 54 ALA H 54 ALA HA 5.75 . . . 37 3JHNHA 55 ALA H 55 ALA HA 4.51 . . . 38 3JHNHA 56 ARG H 56 ARG HA 4.58 . . . 39 3JHNHA 58 ILE H 58 ILE HA 8.42 . . . 40 3JHNHA 59 LYS H 59 LYS HA 7.38 . . . 41 3JHNHA 61 LEU H 61 LEU HA 4.97 . . . 42 3JHNHA 62 ASN H 62 ASN HA 7.74 . . . 43 3JHNHA 63 ALA H 63 ALA HA 3.46 . . . 44 3JHNHA 65 ASN H 65 ASN HA 5.10 . . . 45 3JHNHA 66 ALA H 66 ALA HA 4.11 . . . 46 3JHNHA 67 ALA H 67 ALA HA 4.62 . . . 47 3JHNHA 68 SER H 68 SER HA 5.43 . . . 48 3JHNHA 69 ILE H 69 ILE HA 4.76 . . . 49 3JHNHA 71 SER H 71 SER HA 5.58 . . . 50 3JHNHA 72 LYS H 72 LYS HA 3.26 . . . 51 3JHNHA 73 CYS H 73 CYS HA 7.44 . . . 52 3JHNHA 75 VAL H 75 VAL HA 11.09 . . . 53 3JHNHA 77 VAL H 77 VAL HA 8.03 . . . 54 3JHNHA 79 TYR H 79 TYR HA 8.33 . . . 55 3JHNHA 80 THR H 80 THR HA 7.97 . . . 56 3JHNHA 82 SER H 82 SER HA 8.88 . . . 57 3JHNHA 83 ALA H 83 ALA HA 6.13 . . . 58 3JHNHA 85 ILE H 85 ILE HA 5.91 . . . 59 3JHNHA 86 ASP H 86 ASP HA 10.57 . . . 60 3JHNHA 88 SER H 88 SER HA 6.23 . . . 61 3JHNHA 90 VAL H 90 VAL HA 8.80 . . . stop_ save_