data_5176 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; SOLUTION STRUCTURE OF THE SQUASH TRYPSIN INHIBITOR MCoTI-II, NMR, 30 STRUCTURES. ; _BMRB_accession_number 5176 _BMRB_flat_file_name bmr5176.str _Entry_type original _Submission_date 2001-10-12 _Accession_date 2001-10-12 _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 Heitz A. . . 2 Hernandez J. F. . 3 Gagnon J. . . 4 Hong T. T. . 5 Pham T. T.C. . 6 Nguyen T. M. . 7 Le-Nguyen D. . . 8 Chiche L. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 186 "13C chemical shifts" 95 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-11-12 original author . stop_ _Original_release_date 2001-11-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of the squash trypsin inhibitor MCoTI-II. A new family for cyclic knottins. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11434766 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 HEITZ A. . . 2 HERNANDEZ J. F. . 3 GAGNON J. . . 4 HONG T. T. . 5 PHAM T. T.C. . 6 NGUYEN T. M. . 7 LE-NGUYEN D. . . 8 CHICHE L. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 40 _Journal_issue 27 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7973 _Page_last 7983 _Year 2001 _Details . loop_ _Keyword '3-10 HELIX' 'BACKBONE CYCLIC' 'CYCLIC KNOTTIN' 'PLANT PROTEIN' 'TRIPLE-STRANDED ANTI-PARALLEL BETA-SHEET' stop_ save_ ################################## # Molecular system description # ################################## save_system_MCoTI-II _Saveframe_category molecular_system _Mol_system_name 'Momordica Cochinchinensis Trypsin inhibitor II' _Abbreviation_common MCoTI-II _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'MCoTI-II subunit 1' $MCoTI-II stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'Trypsin inhibitor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MCoTI-II _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MCoTI-II _Name_variant none _Abbreviation_common MCoTI-II _Molecular_mass 3453 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 34 _Mol_residue_sequence ; SGSDGGVCPKILKKCRRDSD CPGACICRGNGYCG ; loop_ _Residue_seq_code _Residue_label 1 SER 2 GLY 3 SER 4 ASP 5 GLY 6 GLY 7 VAL 8 CYS 9 PRO 10 LYS 11 ILE 12 LEU 13 LYS 14 LYS 15 CYS 16 ARG 17 ARG 18 ASP 19 SER 20 ASP 21 CYS 22 PRO 23 GLY 24 ALA 25 CYS 26 ILE 27 CYS 28 ARG 29 GLY 30 ASN 31 GLY 32 TYR 33 CYS 34 GLY stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value SWISS-PROT P82409 'Trypsin inhibitor 2 (Trypsin inhibitor II) (MCoTI-II)' 100.00 34 100.00 100.00 4.33e-10 PDB 2PO8 'The Structure Of A Two-Disulfide Intermediate Of Mcoti-Ii' 79.41 34 100.00 100.00 1.07e-06 PDB 2IT8 'Solution Structure Of A Linear Analog Of The Cyclic Squash Trypsin Inhibitor Mcoti-Ii' 85.29 30 100.00 100.00 1.29e-07 PDB 1IB9 'Solution Structure Of Mcoti-Ii, A Macrocyclic Trypsin Inhibitor' 97.06 34 100.00 100.00 1.23e-09 PDB 1HA9 'Solution Structure Of The Squash Trypsin Inhibitor Mcoti-Ii, Nmr, 30 Structures.' 97.06 34 100.00 100.00 1.23e-09 BMRB 7361 lin_MCoTI 82.35 29 100.00 100.00 3.98e-07 BMRB 5028 'MCoTI II' 100.00 34 100.00 100.00 4.33e-10 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 $MCoTI-II 'Spiny bitter cucumber' 3674 Eukaryota Virdiplanta Momordica cochinchinensis SEEDS 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 $MCoTI-II '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 $MCoTI-II 2.5 mM . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 2.6 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _Sample_label $sample_1 save_ save_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_1 save_ save_1H-13C_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.40 0.2 n/a pressure 1 . atm temperature 305.0 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _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_citation_label _Correction_value_citation_label TSP C 13 'methyl carbons' ppm 0.00 internal direct . . . $entry_citation $entry_citation TSP H 1 'methyl protons' ppm 0.00 internal direct . . . $entry_citation $entry_citation 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 $chem_shift_ref _Mol_system_component_name 'MCoTI-II subunit 1' _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 SER H H 8.80 0.02 1 2 . 1 SER HA H 4.56 0.02 1 3 . 1 SER HB2 H 4.02 0.02 2 4 . 1 SER HB3 H 3.96 0.02 2 5 . 1 SER CA C 59.5 0.1 1 6 . 1 SER CB C 63.8 0.1 1 7 . 2 GLY H H 9.14 0.02 1 8 . 2 GLY HA2 H 4.47 0.02 1 9 . 2 GLY HA3 H 3.94 0.02 1 10 . 2 GLY CA C 44.6 0.1 1 11 . 3 SER H H 8.69 0.02 1 12 . 3 SER HA H 4.53 0.02 1 13 . 3 SER HB2 H 3.93 0.02 1 14 . 3 SER HB3 H 3.93 0.02 1 15 . 3 SER CA C 58.9 0.1 1 16 . 3 SER CB C 63.6 0.1 1 17 . 4 ASP H H 8.58 0.02 1 18 . 4 ASP HA H 4.80 0.02 1 19 . 4 ASP HB2 H 2.97 0.02 2 20 . 4 ASP HB3 H 2.90 0.02 2 21 . 4 ASP CA C 53.5 0.1 1 22 . 4 ASP CB C 39.9 0.1 1 23 . 5 GLY H H 8.24 0.02 1 24 . 5 GLY HA2 H 4.15 0.02 2 25 . 5 GLY HA3 H 3.89 0.02 2 26 . 5 GLY CA C 45.2 0.1 1 27 . 6 GLY H H 8.14 0.02 1 28 . 6 GLY HA2 H 4.02 0.02 1 29 . 6 GLY HA3 H 3.95 0.02 1 30 . 6 GLY CA C 44.4 0.1 1 31 . 7 VAL H H 8.48 0.02 1 32 . 7 VAL HA H 4.07 0.02 1 33 . 7 VAL HB H 2.04 0.02 1 34 . 7 VAL HG1 H 0.99 0.02 2 35 . 7 VAL HG2 H 0.89 0.02 2 36 . 7 VAL CA C 62.5 0.1 1 37 . 7 VAL CB C 32.3 0.1 1 38 . 7 VAL CG1 C 20.7 0.1 2 39 . 7 VAL CG2 C 20.8 0.1 2 40 . 8 CYS H H 8.68 0.02 1 41 . 8 CYS HA H 5.23 0.02 1 42 . 8 CYS HB2 H 2.90 0.02 1 43 . 8 CYS HB3 H 2.95 0.02 1 44 . 8 CYS CA C 52.1 0.1 1 45 . 8 CYS CB C 40.3 0.1 1 46 . 9 PRO HA H 4.42 0.02 1 47 . 9 PRO HB2 H 2.36 0.02 2 48 . 9 PRO HB3 H 1.90 0.02 2 49 . 9 PRO HG2 H 2.05 0.02 2 50 . 9 PRO HG3 H 1.98 0.02 2 51 . 9 PRO HD2 H 3.89 0.02 1 52 . 9 PRO HD3 H 3.89 0.02 1 53 . 9 PRO CA C 62.8 0.1 1 54 . 9 PRO CB C 32.4 0.1 1 55 . 9 PRO CG C 27.1 0.1 1 56 . 9 PRO CD C 51.3 0.1 1 57 . 10 LYS H H 8.25 0.02 1 58 . 10 LYS HA H 4.32 0.02 1 59 . 10 LYS HB2 H 1.89 0.02 2 60 . 10 LYS HB3 H 1.80 0.02 2 61 . 10 LYS HG2 H 1.52 0.02 2 62 . 10 LYS HG3 H 1.42 0.02 2 63 . 10 LYS HD2 H 1.74 0.02 1 64 . 10 LYS HD3 H 1.74 0.02 1 65 . 10 LYS HE2 H 3.04 0.02 1 66 . 10 LYS HE3 H 3.04 0.02 1 67 . 10 LYS HZ H 7.54 0.02 1 68 . 10 LYS CA C 56.2 0.1 1 69 . 10 LYS CB C 32.2 0.1 1 70 . 10 LYS CG C 24.7 0.1 1 71 . 10 LYS CD C 28.9 0.1 1 72 . 10 LYS CE C 41.9 0.1 1 73 . 11 ILE H H 7.75 0.02 1 74 . 11 ILE HA H 4.44 0.02 1 75 . 11 ILE HB H 1.84 0.02 1 76 . 11 ILE HG12 H 1.39 0.02 2 77 . 11 ILE HG13 H 1.12 0.02 2 78 . 11 ILE HG2 H 0.88 0.02 1 79 . 11 ILE HD1 H 0.89 0.02 1 80 . 11 ILE CA C 59.5 0.1 1 81 . 11 ILE CB C 41.0 0.1 1 82 . 11 ILE CG1 C 26.8 0.1 1 83 . 11 ILE CG2 C 17.2 0.1 1 84 . 11 ILE CD1 C 13.9 0.1 1 85 . 12 LEU H H 8.69 0.02 1 86 . 12 LEU HA H 4.59 0.02 1 87 . 12 LEU HB2 H 1.78 0.02 2 88 . 12 LEU HB3 H 1.55 0.02 2 89 . 12 LEU HG H 1.53 0.02 1 90 . 12 LEU HD1 H 0.84 0.02 2 91 . 12 LEU HD2 H 0.80 0.02 2 92 . 12 LEU CA C 54.2 0.1 1 93 . 12 LEU CB C 41.6 0.1 1 94 . 12 LEU CG C 27.2 0.1 1 95 . 12 LEU CD1 C 24.3 0.1 2 96 . 12 LEU CD2 C 24.2 0.1 2 97 . 13 LYS H H 8.91 0.02 1 98 . 13 LYS HA H 4.63 0.02 1 99 . 13 LYS HB2 H 1.65 0.02 2 100 . 13 LYS HB3 H 1.62 0.02 2 101 . 13 LYS HG2 H 1.67 0.02 2 102 . 13 LYS HG3 H 1.46 0.02 2 103 . 13 LYS HD2 H 1.81 0.02 1 104 . 13 LYS HD3 H 1.81 0.02 1 105 . 13 LYS HE2 H 3.13 0.02 1 106 . 13 LYS HE3 H 3.13 0.02 1 107 . 13 LYS HZ H 7.64 0.02 1 108 . 13 LYS CA C 55.4 0.1 1 109 . 13 LYS CB C 36.1 0.1 1 110 . 13 LYS CG C 25.0 0.1 1 111 . 13 LYS CD C 29.1 0.1 1 112 . 13 LYS CE C 42.3 0.1 1 113 . 14 LYS H H 8.63 0.02 1 114 . 14 LYS HA H 4.39 0.02 1 115 . 14 LYS HB2 H 1.68 0.02 2 116 . 14 LYS HB3 H 1.58 0.02 2 117 . 14 LYS HG2 H 1.36 0.02 2 118 . 14 LYS HG3 H 1.00 0.02 2 119 . 14 LYS HD2 H 1.55 0.02 1 120 . 14 LYS HD3 H 1.55 0.02 1 121 . 14 LYS HE2 H 2.97 0.02 1 122 . 14 LYS HE3 H 2.97 0.02 1 123 . 14 LYS HZ H 7.47 0.02 1 124 . 14 LYS CA C 56.2 0.1 1 125 . 14 LYS CB C 33.3 0.1 1 126 . 14 LYS CG C 25.5 0.1 1 127 . 14 LYS CD C 28.9 0.1 1 128 . 14 LYS CE C 41.7 0.1 1 129 . 15 CYS H H 8.46 0.02 1 130 . 15 CYS HA H 4.94 0.02 1 131 . 15 CYS HB2 H 3.25 0.02 1 132 . 15 CYS HB3 H 2.98 0.02 1 133 . 15 CYS CA C 53.6 0.1 1 134 . 15 CYS CB C 47.8 0.1 1 135 . 16 ARG H H 9.42 0.02 1 136 . 16 ARG HA H 4.49 0.02 1 137 . 16 ARG HB2 H 1.93 0.02 2 138 . 16 ARG HB3 H 1.78 0.02 2 139 . 16 ARG HG2 H 1.68 0.02 1 140 . 16 ARG HG3 H 1.68 0.02 1 141 . 16 ARG HD2 H 3.24 0.02 1 142 . 16 ARG HD3 H 3.24 0.02 1 143 . 16 ARG HE H 7.32 0.02 1 144 . 16 ARG CA C 56.0 0.1 1 145 . 16 ARG CB C 30.8 0.1 1 146 . 16 ARG CG C 27.0 0.1 1 147 . 16 ARG CD C 42.9 0.1 1 148 . 17 ARG H H 8.11 0.02 1 149 . 17 ARG HA H 4.82 0.02 1 150 . 17 ARG HB2 H 2.07 0.02 2 151 . 17 ARG HB3 H 1.84 0.02 2 152 . 17 ARG HG2 H 1.61 0.02 2 153 . 17 ARG HG3 H 1.51 0.02 2 154 . 17 ARG HD2 H 3.20 0.02 1 155 . 17 ARG HD3 H 3.20 0.02 1 156 . 17 ARG HE H 7.19 0.02 1 157 . 17 ARG CA C 53.5 0.1 1 158 . 17 ARG CB C 32.9 0.1 1 159 . 17 ARG CG C 25.6 0.1 1 160 . 17 ARG CD C 43.3 0.1 1 161 . 18 ASP H H 9.28 0.02 1 162 . 18 ASP HA H 4.17 0.02 1 163 . 18 ASP HB2 H 2.85 0.02 1 164 . 18 ASP HB3 H 3.02 0.02 1 165 . 18 ASP CA C 58.8 0.1 1 166 . 18 ASP CB C 39.2 0.1 1 167 . 19 SER H H 8.16 0.02 1 168 . 19 SER HA H 4.35 0.02 1 169 . 19 SER HB2 H 4.15 0.02 2 170 . 19 SER HB3 H 3.89 0.02 2 171 . 19 SER CA C 59.8 0.1 1 172 . 19 SER CB C 62.1 0.1 1 173 . 20 ASP H H 7.77 0.02 1 174 . 20 ASP HA H 4.67 0.02 1 175 . 20 ASP HB2 H 3.08 0.02 1 176 . 20 ASP HB3 H 3.01 0.02 1 177 . 20 ASP CA C 55.6 0.1 1 178 . 20 ASP CB C 42.2 0.1 1 179 . 21 CYS H H 8.17 0.02 1 180 . 21 CYS HA H 5.10 0.02 1 181 . 21 CYS HB2 H 2.90 0.02 1 182 . 21 CYS HB3 H 2.73 0.02 1 183 . 21 CYS CA C 51.6 0.1 1 184 . 21 CYS CB C 40.1 0.1 1 185 . 22 PRO HA H 4.67 0.02 1 186 . 22 PRO HB2 H 2.32 0.02 2 187 . 22 PRO HB3 H 1.98 0.02 2 188 . 22 PRO HG2 H 2.13 0.02 2 189 . 22 PRO HG3 H 2.08 0.02 2 190 . 22 PRO HD2 H 3.79 0.02 2 191 . 22 PRO HD3 H 3.48 0.02 2 192 . 22 PRO CA C 61.9 0.1 1 193 . 22 PRO CB C 32.4 0.1 1 194 . 22 PRO CG C 27.2 0.1 1 195 . 22 PRO CD C 49.9 0.1 1 196 . 23 GLY H H 8.48 0.02 1 197 . 23 GLY HA2 H 3.89 0.02 2 198 . 23 GLY HA3 H 3.80 0.02 2 199 . 23 GLY CA C 47.3 0.1 1 200 . 24 ALA H H 8.43 0.02 1 201 . 24 ALA HA H 4.57 0.02 1 202 . 24 ALA HB H 1.41 0.02 1 203 . 24 ALA CA C 51.4 0.1 1 204 . 24 ALA CB C 18.2 0.1 1 205 . 25 CYS H H 8.33 0.02 1 206 . 25 CYS HA H 4.66 0.02 1 207 . 25 CYS HB2 H 3.26 0.02 1 208 . 25 CYS HB3 H 3.26 0.02 1 209 . 25 CYS CA C 55.6 0.1 1 210 . 25 CYS CB C 44.2 0.1 1 211 . 26 ILE H H 9.08 0.02 1 212 . 26 ILE HA H 4.48 0.02 1 213 . 26 ILE HB H 1.98 0.02 1 214 . 26 ILE HG12 H 1.12 0.02 2 215 . 26 ILE HG13 H 1.02 0.02 2 216 . 26 ILE HG2 H 0.91 0.02 1 217 . 26 ILE HD1 H 0.88 0.02 1 218 . 26 ILE CA C 58.8 0.1 1 219 . 26 ILE CB C 41.2 0.1 1 220 . 26 ILE CG1 C 25.9 0.1 1 221 . 26 ILE CG2 C 19.4 0.1 1 222 . 26 ILE CD1 C 14.2 0.1 1 223 . 27 CYS H H 9.05 0.02 1 224 . 27 CYS HA H 5.01 0.02 1 225 . 27 CYS HB2 H 2.52 0.02 1 226 . 27 CYS HB3 H 2.84 0.02 1 227 . 27 CYS CA C 54.8 0.1 1 228 . 27 CYS CB C 37.8 0.1 1 229 . 28 ARG H H 8.10 0.02 1 230 . 28 ARG HA H 4.38 0.02 1 231 . 28 ARG HB2 H 2.54 0.02 2 232 . 28 ARG HB3 H 2.11 0.02 2 233 . 28 ARG HG2 H 1.80 0.02 2 234 . 28 ARG HG3 H 1.65 0.02 2 235 . 28 ARG HD2 H 3.30 0.02 1 236 . 28 ARG HD3 H 3.30 0.02 1 237 . 28 ARG HE H 7.02 0.02 1 238 . 28 ARG CA C 56.2 0.1 1 239 . 28 ARG CB C 30.8 0.1 1 240 . 28 ARG CG C 27.8 0.1 1 241 . 28 ARG CD C 43.1 0.1 1 242 . 29 GLY H H 8.90 0.02 1 243 . 29 GLY HA2 H 3.98 0.02 1 244 . 29 GLY HA3 H 3.98 0.02 1 245 . 29 GLY CA C 46.7 0.1 1 246 . 30 ASN H H 7.85 0.02 1 247 . 30 ASN HA H 4.78 0.02 1 248 . 30 ASN HB2 H 3.37 0.02 1 249 . 30 ASN HB3 H 2.92 0.02 1 250 . 30 ASN HD21 H 7.59 0.02 2 251 . 30 ASN HD22 H 6.64 0.02 2 252 . 30 ASN CA C 52.1 0.1 1 253 . 30 ASN CB C 36.9 0.1 1 254 . 31 GLY H H 8.46 0.02 1 255 . 31 GLY HA2 H 4.05 0.02 2 256 . 31 GLY HA3 H 3.73 0.02 2 257 . 31 GLY CA C 46.1 0.1 1 258 . 32 TYR H H 7.33 0.02 1 259 . 32 TYR HA H 5.32 0.02 1 260 . 32 TYR HB2 H 2.69 0.02 1 261 . 32 TYR HB3 H 3.12 0.02 1 262 . 32 TYR HD1 H 6.93 0.02 1 263 . 32 TYR HD2 H 6.93 0.02 1 264 . 32 TYR HE1 H 6.76 0.02 1 265 . 32 TYR HE2 H 6.76 0.02 1 266 . 32 TYR CA C 56.9 0.1 1 267 . 32 TYR CB C 41.6 0.1 1 268 . 32 TYR CD1 C 133.2 0.1 1 269 . 32 TYR CD2 C 133.2 0.1 1 270 . 32 TYR CE1 C 117.6 0.1 1 271 . 32 TYR CE2 C 117.6 0.1 1 272 . 33 CYS H H 8.84 0.02 1 273 . 33 CYS HA H 5.44 0.02 1 274 . 33 CYS HB2 H 3.11 0.02 1 275 . 33 CYS HB3 H 2.85 0.02 1 276 . 33 CYS CA C 55.4 0.1 1 277 . 33 CYS CB C 40.6 0.1 1 278 . 34 GLY H H 9.86 0.02 1 279 . 34 GLY HA2 H 4.56 0.02 1 280 . 34 GLY HA3 H 4.01 0.02 1 281 . 34 GLY CA C 45.7 0.1 1 stop_ save_