data_4185 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H Chemical Shift Assignments for Gurmarin ; _BMRB_accession_number 4185 _BMRB_flat_file_name bmr4185.str _Entry_type original _Submission_date 1998-08-13 _Accession_date 1998-08-13 _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 Fletcher Jamie I. . 2 Dingley Andrew J. . 3 King Glenn F. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 232 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-16 update BMRB 'Updating non-standard residue' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; High-Resolution Solution Structure of Gurmarin,a Sweet-Taste-Suppressing Plant Polypeptide ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99421659 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fletcher Jamie I. . 2 Dingley Andrew J. . 3 Smith Ross . . 4 Connor Mark . . 5 MacDonald Christie J. . 6 King Glenn F. . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_name_full 'European Journal of Biochemistry' _Journal_volume 264 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 525 _Page_last 533 _Year 1999 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Bartels, C.,Xia, T-H., Billeter,M., Guentert, P., Wuthrich, K., "The Program XEASY for Computer-Supported NMR Spectral Analysis of Biological Macromolecules," J.Biomol.NMR 5 pp 1-10 (1995). ; _Citation_title . _Citation_status . _Citation_type . _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_citation_two _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_gmn _Saveframe_category molecular_system _Mol_system_name gurmarin _Abbreviation_common gmn _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label gmn $gmn stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'fully oxidized' loop_ _Biological_function 'Sweet-taste inhibitor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_gmn _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common gurmarin _Abbreviation_common gmn _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 35 _Mol_residue_sequence ; XQCVKKDELCIPYYLDCCEP LECKKVNWWDHKCIG ; loop_ _Residue_seq_code _Residue_label 1 PCA 2 GLN 3 CYS 4 VAL 5 LYS 6 LYS 7 ASP 8 GLU 9 LEU 10 CYS 11 ILE 12 PRO 13 TYR 14 TYR 15 LEU 16 ASP 17 CYS 18 CYS 19 GLU 20 PRO 21 LEU 22 GLU 23 CYS 24 LYS 25 LYS 26 VAL 27 ASN 28 TRP 29 TRP 30 ASP 31 HIS 32 LYS 33 CYS 34 ILE 35 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-06 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 1C4E "Gurmarin From Gymnema Sylvestre" 97.14 35 100.00 100.00 1.10e-14 PDB 1GUR "Gurmarin, A Sweet Taste-Suppressing Polypeptide, Nmr, 10 Structures" 97.14 35 100.00 100.00 1.10e-14 GB AAB22380 "gurmarin=sweet-taste-suppressing peptide [Gymnema sylvestre]" 97.14 35 100.00 100.00 9.98e-15 GB AAB35858 "gurmarin=sweetness-suppressing polypeptide [Gymnema sylvestre]" 97.14 35 100.00 100.00 9.98e-15 SP P25810 "RecName: Full=Gurmarin; AltName: Full=Sweet taste-suppressing peptide" 97.14 35 100.00 100.00 9.66e-15 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_PCA _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common 'PYROGLUTAMIC ACID' _BMRB_code . _PDB_code PCA _Standard_residue_derivative . _Molecular_mass 129.114 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jul 14 13:52:53 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? OE OE O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HXT HXT H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N CD ? ? SING N H ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG HG2 ? ? SING CG HG3 ? ? DOUB CD OE ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? 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 $gmn 'Gymnema sylvestre' 4068 Eukaryota Viridiplantae Gymnema sylvestre leaves 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 $gmn 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details 'Low solubility near pI (4.5)' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $gmn 2.5 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_one _Saveframe_category software _Name XWINMR _Version . loop_ _Task 'Spectral processing' stop_ _Details . save_ save_software_two _Saveframe_category software _Name XEASY _Version . loop_ _Task 'Spectral assignment' stop_ _Details . _Citation_label $citation_one save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H TOCSY' _Sample_label $sample_one save_ save_1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H NOESY' _Sample_label $sample_one save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_one save_ save_ECOSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name ECOSY _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.9 . n/a temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 _Indirect_shift_ratio_citation_label DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.0 $citation_two 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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name gmn _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 PCA H H 7.86 . 1 2 . 1 PCA HA H 4.37 . 1 3 . 1 PCA HB2 H 2.48 . 2 4 . 1 PCA HB3 H 2.05 . 2 5 . 1 PCA HG2 H 2.39 . 2 6 . 1 PCA HG3 H 2.31 . 2 7 . 2 GLN H H 8.68 . 1 8 . 2 GLN HA H 4.42 . 1 9 . 2 GLN HB2 H 2.11 . 2 10 . 2 GLN HB3 H 2.00 . 2 11 . 2 GLN HG2 H 2.41 . 1 12 . 2 GLN HG3 H 2.41 . 1 13 . 2 GLN HE21 H 6.89 . 2 14 . 2 GLN HE22 H 7.61 . 2 15 . 3 CYS H H 8.17 . 1 16 . 3 CYS HA H 4.90 . 1 17 . 3 CYS HB2 H 3.01 . 2 18 . 3 CYS HB3 H 3.13 . 2 19 . 4 VAL H H 8.79 . 1 20 . 4 VAL HA H 3.97 . 1 21 . 4 VAL HB H 1.90 . 1 22 . 4 VAL HG1 H 1.07 . 2 23 . 4 VAL HG2 H 0.88 . 2 24 . 5 LYS H H 7.65 . 1 25 . 5 LYS HA H 4.12 . 1 26 . 5 LYS HB2 H 1.98 . 2 27 . 5 LYS HB3 H 1.61 . 2 28 . 5 LYS HG2 H 1.42 . 1 29 . 5 LYS HG3 H 1.42 . 1 30 . 5 LYS HD2 H 1.70 . 1 31 . 5 LYS HD3 H 1.70 . 1 32 . 5 LYS HE2 H 3.04 . 1 33 . 5 LYS HE3 H 3.04 . 1 34 . 5 LYS HZ H 7.53 . 1 35 . 6 LYS H H 7.79 . 1 36 . 6 LYS HA H 3.66 . 1 37 . 6 LYS HB2 H 1.67 . 1 38 . 6 LYS HB3 H 1.67 . 1 39 . 6 LYS HG2 H 1.39 . 2 40 . 6 LYS HG3 H 1.35 . 2 41 . 6 LYS HD2 H 1.72 . 1 42 . 6 LYS HD3 H 1.72 . 1 43 . 6 LYS HE2 H 3.00 . 1 44 . 6 LYS HE3 H 3.00 . 1 45 . 6 LYS HZ H 7.57 . 1 46 . 7 ASP H H 9.77 . 1 47 . 7 ASP HA H 4.14 . 1 48 . 7 ASP HB2 H 3.13 . 2 49 . 7 ASP HB3 H 3.08 . 2 50 . 8 GLU H H 7.66 . 1 51 . 8 GLU HA H 4.62 . 1 52 . 8 GLU HB2 H 2.17 . 2 53 . 8 GLU HB3 H 2.07 . 2 54 . 8 GLU HG2 H 2.35 . 2 55 . 8 GLU HG3 H 2.28 . 2 56 . 9 LEU H H 8.11 . 1 57 . 9 LEU HA H 4.79 . 1 58 . 9 LEU HB2 H 1.75 . 2 59 . 9 LEU HB3 H 1.57 . 2 60 . 9 LEU HG H 1.82 . 1 61 . 9 LEU HD1 H 1.03 . 2 62 . 9 LEU HD2 H 0.95 . 2 63 . 10 CYS H H 8.04 . 1 64 . 10 CYS HA H 5.03 . 1 65 . 10 CYS HB2 H 3.38 . 2 66 . 10 CYS HB3 H 3.22 . 2 67 . 11 ILE H H 8.60 . 1 68 . 11 ILE HA H 4.36 . 1 69 . 11 ILE HB H 1.68 . 1 70 . 11 ILE HG12 H 1.43 . 2 71 . 11 ILE HG13 H 1.08 . 2 72 . 11 ILE HG2 H 0.87 . 1 73 . 11 ILE HD1 H 0.86 . 1 74 . 12 PRO HA H 3.92 . 1 75 . 12 PRO HB2 H 1.94 . 2 76 . 12 PRO HB3 H 1.67 . 2 77 . 12 PRO HG2 H 1.34 . 1 78 . 12 PRO HG3 H 1.34 . 1 79 . 12 PRO HD2 H 3.29 . 2 80 . 12 PRO HD3 H 2.90 . 2 81 . 13 TYR H H 8.28 . 1 82 . 13 TYR HA H 4.08 . 1 83 . 13 TYR HB2 H 3.10 . 2 84 . 13 TYR HB3 H 3.02 . 2 85 . 13 TYR HD1 H 6.77 . 1 86 . 13 TYR HD2 H 6.77 . 1 87 . 13 TYR HE1 H 6.86 . 1 88 . 13 TYR HE2 H 6.86 . 1 89 . 14 TYR H H 7.96 . 1 90 . 14 TYR HA H 4.54 . 1 91 . 14 TYR HB2 H 2.92 . 2 92 . 14 TYR HB3 H 2.61 . 2 93 . 14 TYR HD1 H 6.85 . 1 94 . 14 TYR HD2 H 6.85 . 1 95 . 14 TYR HE1 H 7.14 . 1 96 . 14 TYR HE2 H 7.14 . 1 97 . 15 LEU H H 8.51 . 1 98 . 15 LEU HA H 4.50 . 1 99 . 15 LEU HB2 H 1.41 . 2 100 . 15 LEU HB3 H 1.37 . 2 101 . 15 LEU HG H 1.64 . 1 102 . 15 LEU HD1 H 0.86 . 2 103 . 15 LEU HD2 H 0.81 . 2 104 . 16 ASP H H 8.43 . 1 105 . 16 ASP HA H 4.73 . 1 106 . 16 ASP HB2 H 2.78 . 2 107 . 16 ASP HB3 H 2.71 . 2 108 . 17 CYS H H 8.88 . 1 109 . 17 CYS HA H 4.91 . 1 110 . 17 CYS HB2 H 2.81 . 2 111 . 17 CYS HB3 H 2.41 . 2 112 . 18 CYS H H 9.81 . 1 113 . 18 CYS HA H 4.57 . 1 114 . 18 CYS HB2 H 3.26 . 2 115 . 18 CYS HB3 H 2.54 . 2 116 . 19 GLU H H 8.95 . 1 117 . 19 GLU HA H 4.53 . 1 118 . 19 GLU HB2 H 2.54 . 2 119 . 19 GLU HB3 H 2.01 . 2 120 . 19 GLU HG2 H 2.60 . 1 121 . 19 GLU HG3 H 2.60 . 1 122 . 20 PRO HA H 4.91 . 1 123 . 20 PRO HB2 H 2.54 . 1 124 . 20 PRO HB3 H 2.54 . 1 125 . 20 PRO HG2 H 2.02 . 2 126 . 20 PRO HG3 H 1.60 . 2 127 . 20 PRO HD2 H 3.55 . 2 128 . 20 PRO HD3 H 3.27 . 2 129 . 21 LEU H H 8.68 . 1 130 . 21 LEU HA H 4.17 . 1 131 . 21 LEU HB2 H 2.02 . 2 132 . 21 LEU HB3 H 1.12 . 2 133 . 21 LEU HG H 1.58 . 1 134 . 21 LEU HD1 H 0.83 . 2 135 . 21 LEU HD2 H 0.65 . 2 136 . 22 GLU H H 8.56 . 1 137 . 22 GLU HA H 4.58 . 1 138 . 22 GLU HB2 H 1.98 . 2 139 . 22 GLU HB3 H 1.84 . 2 140 . 22 GLU HG2 H 2.47 . 2 141 . 22 GLU HG3 H 2.37 . 2 142 . 23 CYS H H 8.94 . 1 143 . 23 CYS HA H 4.77 . 1 144 . 23 CYS HB2 H 3.37 . 2 145 . 23 CYS HB3 H 2.87 . 2 146 . 24 LYS H H 8.70 . 1 147 . 24 LYS HA H 4.78 . 1 148 . 24 LYS HB2 H 1.84 . 1 149 . 24 LYS HB3 H 1.84 . 1 150 . 24 LYS HG2 H 1.41 . 2 151 . 24 LYS HG3 H 1.30 . 2 152 . 24 LYS HD2 H 1.64 . 1 153 . 24 LYS HD3 H 1.64 . 1 154 . 24 LYS HE2 H 2.95 . 1 155 . 24 LYS HE3 H 2.95 . 1 156 . 24 LYS HZ H 7.53 . 1 157 . 25 LYS H H 8.76 . 1 158 . 25 LYS HA H 3.93 . 1 159 . 25 LYS HB2 H 1.76 . 2 160 . 25 LYS HB3 H 1.29 . 2 161 . 25 LYS HG2 H 0.96 . 1 162 . 25 LYS HG3 H 0.96 . 1 163 . 25 LYS HD2 H 1.41 . 1 164 . 25 LYS HD3 H 1.41 . 1 165 . 25 LYS HE2 H 2.81 . 2 166 . 25 LYS HE3 H 2.70 . 2 167 . 25 LYS HZ H 7.27 . 1 168 . 26 VAL H H 8.11 . 1 169 . 26 VAL HA H 4.37 . 1 170 . 26 VAL HB H 2.16 . 1 171 . 26 VAL HG1 H 0.90 . 2 172 . 26 VAL HG2 H 0.70 . 2 173 . 27 ASN H H 7.87 . 1 174 . 27 ASN HA H 4.43 . 1 175 . 27 ASN HB2 H 3.08 . 2 176 . 27 ASN HB3 H 2.97 . 2 177 . 27 ASN HD21 H 7.82 . 2 178 . 27 ASN HD22 H 7.20 . 2 179 . 28 TRP H H 7.99 . 1 180 . 28 TRP HA H 4.05 . 1 181 . 28 TRP HB2 H 2.75 . 2 182 . 28 TRP HB3 H 2.44 . 2 183 . 28 TRP HD1 H 6.59 . 1 184 . 28 TRP HE1 H 10.04 . 1 185 . 28 TRP HE3 H 7.29 . 1 186 . 28 TRP HZ2 H 7.43 . 1 187 . 28 TRP HZ3 H 7.09 . 1 188 . 28 TRP HH2 H 7.19 . 1 189 . 29 TRP H H 7.80 . 1 190 . 29 TRP HA H 4.67 . 1 191 . 29 TRP HB2 H 2.94 . 1 192 . 29 TRP HB3 H 2.94 . 1 193 . 29 TRP HD1 H 7.06 . 1 194 . 29 TRP HE1 H 10.20 . 1 195 . 29 TRP HE3 H 7.44 . 1 196 . 29 TRP HZ2 H 7.46 . 1 197 . 29 TRP HZ3 H 7.19 . 1 198 . 29 TRP HH2 H 7.23 . 1 199 . 30 ASP H H 8.30 . 1 200 . 30 ASP HA H 4.98 . 1 201 . 30 ASP HB2 H 2.42 . 2 202 . 30 ASP HB3 H 2.39 . 2 203 . 31 HIS H H 8.66 . 1 204 . 31 HIS HA H 5.40 . 1 205 . 31 HIS HB2 H 3.40 . 2 206 . 31 HIS HB3 H 3.07 . 2 207 . 31 HIS HD2 H 7.00 . 1 208 . 31 HIS HE1 H 8.76 . 1 209 . 32 LYS H H 8.96 . 1 210 . 32 LYS HA H 5.25 . 1 211 . 32 LYS HB2 H 1.44 . 1 212 . 32 LYS HB3 H 1.44 . 1 213 . 32 LYS HG2 H 1.13 . 1 214 . 32 LYS HG3 H 1.13 . 1 215 . 32 LYS HD2 H 1.51 . 1 216 . 32 LYS HD3 H 1.51 . 1 217 . 32 LYS HE2 H 2.75 . 1 218 . 32 LYS HE3 H 2.75 . 1 219 . 33 CYS H H 7.83 . 1 220 . 33 CYS HA H 5.14 . 1 221 . 33 CYS HB2 H 3.08 . 2 222 . 33 CYS HB3 H 2.60 . 2 223 . 34 ILE H H 9.30 . 1 224 . 34 ILE HA H 4.73 . 1 225 . 34 ILE HB H 1.96 . 1 226 . 34 ILE HG12 H 1.41 . 2 227 . 34 ILE HG13 H 1.31 . 2 228 . 34 ILE HG2 H 0.95 . 1 229 . 34 ILE HD1 H 0.80 . 1 230 . 35 GLY H H 8.32 . 1 231 . 35 GLY HA2 H 4.00 . 2 232 . 35 GLY HA3 H 3.86 . 2 stop_ save_