data_397 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of EETI-II, a Squash Inhibitor Knottin from Ecballium elaterium. ; _BMRB_accession_number 397 _BMRB_flat_file_name bmr397.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _Entry_origination BMRB _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 Annie . . 2 Chiche Laurent . . 3 Le-Nguyen Dung . . 4 Castro Bertrand . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 152 "13C chemical shifts" 81 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-01-18 revision Authors 'Updated NMR data' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation_1 _Saveframe_category entry_citation _Citation_full ; Heitz, Annie, Chiche, Laurent, Le-Nguyen, Dung, Castro, Bertrand, "1H 2D NMR and Distance Geometry Study of the Folding of Ecballium elaterium Trypsin Inhibitor, a Member of the Squash Inhibitors Family," Biochemistry 28, 2392-2398 (1989). ; _Citation_title ; 1H 2D NMR and Distance Geometry Study of the Folding of Ecballium elaterium Trypsin Inhibitor, a Member of the Squash Inhibitors Family ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 2730872 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Heitz Annie . . 2 Chiche Laurent . . 3 Le-Nguyen Dung . . 4 Castro Bertrand . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 28 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2392 _Page_last 2398 _Year 1989 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_entry_citation_2 _Saveframe_category citation _Citation_full . _Citation_title 'Knottin cyclization: Why has Nature evolved cyclic squash inhibitors.' _Citation_status 'in preparation' _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 HEITZ A. . . 2 AVRUTINA O. . . 3 LE-NGUYEN D. . . 4 DIEDERISCHEN U. . . 5 HERNANDEZ JF. . . 6 GRACY J. . . 7 KOLMAR H. . . 8 CHICHE L. . . stop_ _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 . loop_ _Keyword 'PLANT PROTEIN' 'LINEAR KNOTTIN' '3-10 HELIX' 'TRIPLE-STRANDED ANTI-PARALLEL BETA-SHEET' stop_ save_ ################################## # Molecular system description # ################################## save_system_EETI-II _Saveframe_category molecular_system _Mol_system_name EETI-II _Abbreviation_common EETI-II _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label EETI-II $EETI-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_EETI-II _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common EETI-II _Name_variant none _Abbreviation_common EETI-II _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 28 _Mol_residue_sequence ; GCPRILMRCKQDSDCLAGCV CGPNGFCG ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 CYS 3 PRO 4 ARG 5 ILE 6 LEU 7 MET 8 ARG 9 CYS 10 LYS 11 GLN 12 ASP 13 SER 14 ASP 15 CYS 16 LEU 17 ALA 18 GLY 19 CYS 20 VAL 21 CYS 22 GLY 23 PRO 24 ASN 25 GLY 26 PHE 27 CYS 28 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 2ETI "Use Of Restrained Molecular Dynamics In Water To Determine Three-Dimensional Protein Structure: Prediction Of The Three-Dimensi" 100.00 28 100.00 100.00 6.37e-10 PDB 2IT7 "Solution Structure Of The Squash Trypsin Inhibitor Eeti-Ii" 100.00 28 100.00 100.00 6.37e-10 PRF 1702179A "trypsin inhibitor" 100.00 28 100.00 100.00 6.37e-10 SP P12071 "RecName: Full=Trypsin inhibitor 2; AltName: Full=EETI-II; AltName: Full=Trypsin inhibitor II" 100.00 30 100.00 100.00 6.52e-10 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide EETI-II 2 CYS SG EETI-II 19 CYS SG single disulfide EETI-II 9 CYS SG EETI-II 21 CYS SG single disulfide EETI-II 15 CYS SG EETI-II 27 CYS SG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $EETI-II 'Jumping cucumber' 3679 Eukaryota Virdiplanta Ecballium elaterium 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 $EETI-II synthetic . . . . . 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 $EETI-II 4.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.1 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name COSY _Sample_label . save_ save_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_1H-13C_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label . save_ save_1H-13C_HSQC-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC-TOCSY' _Sample_label . 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_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC-TOCSY' _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 2.7 0.2 n/a temperature 290 1 K pressure 1 . atm 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 TSP H 1 'methyl protons' ppm 0.00 internal direct . . . 1.0 TSP C 13 'methyl carbons' ppm 0.00 internal direct . . . 1.0 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_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 EETI-II _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 GLY HA2 H 3.93 0.02 2 2 . 1 GLY HA3 H 3.83 0.02 2 3 . 1 GLY CA C 43.1 0.1 1 4 . 2 CYS H H 8.87 0.02 1 5 . 2 CYS HA H 5.03 0.02 1 6 . 2 CYS HB2 H 3.15 0.02 1 7 . 2 CYS HB3 H 2.83 0.02 1 8 . 2 CYS CA C 52.8 0.1 1 9 . 2 CYS CB C 41.1 0.1 1 10 . 3 PRO HA H 4.41 0.02 1 11 . 3 PRO HB2 H 1.80 0.02 2 12 . 3 PRO HB3 H 2.41 0.02 2 13 . 3 PRO HG2 H 2.10 0.02 1 14 . 3 PRO HG3 H 2.10 0.02 1 15 . 3 PRO HD2 H 3.73 0.02 2 16 . 3 PRO HD3 H 4.26 0.02 2 17 . 3 PRO CA C 63.1 0.1 1 18 . 3 PRO CB C 32.6 0.1 1 19 . 3 PRO CG C 27.8 0.1 1 20 . 3 PRO CD C 51.7 0.1 1 21 . 4 ARG H H 8.74 0.02 1 22 . 4 ARG HA H 4.41 0.02 1 23 . 4 ARG HB2 H 1.94 0.02 2 24 . 4 ARG HB3 H 1.75 0.02 2 25 . 4 ARG HG2 H 1.68 0.02 1 26 . 4 ARG HG3 H 1.68 0.02 1 27 . 4 ARG HD2 H 3.27 0.02 1 28 . 4 ARG HD3 H 3.27 0.02 1 29 . 4 ARG HE H 7.25 0.02 1 30 . 4 ARG CA C 55.5 0.1 1 31 . 4 ARG CB C 28.0 0.1 1 32 . 4 ARG CG C 26.9 0.1 1 33 . 4 ARG CD C 43.2 0.1 1 34 . 5 ILE H H 7.65 0.02 1 35 . 5 ILE HA H 4.22 0.02 1 36 . 5 ILE HB H 1.68 0.02 1 37 . 5 ILE HG12 H 1.06 0.02 2 38 . 5 ILE HG13 H 1.39 0.02 2 39 . 5 ILE HG2 H 0.89 0.02 1 40 . 5 ILE HD1 H 0.89 0.02 1 41 . 5 ILE CA C 59.9 0.1 1 42 . 5 ILE CB C 40.8 0.1 1 43 . 5 ILE CG1 C 27.1 0.1 1 44 . 5 ILE CG2 C 17.0 0.1 1 45 . 5 ILE CD1 C 13.1 0.1 1 46 . 6 LEU H H 8.86 0.02 1 47 . 6 LEU HA H 4.47 0.02 1 48 . 6 LEU HB2 H 1.61 0.02 2 49 . 6 LEU HB3 H 1.76 0.02 2 50 . 6 LEU HG H 1.56 0.02 1 51 . 6 LEU HD1 H 0.79 0.02 2 52 . 6 LEU HD2 H 0.84 0.02 2 53 . 6 LEU CA C 55.6 0.1 1 54 . 6 LEU CB C 41.5 0.1 1 55 . 6 LEU CG C 27.0 0.1 1 56 . 6 LEU CD1 C 24.5 0.1 2 57 . 6 LEU CD2 C 24.5 0.1 2 58 . 7 MET H H 9.30 0.02 1 59 . 7 MET HA H 4.68 0.02 1 60 . 7 MET HB2 H 1.89 0.02 2 61 . 7 MET HB3 H 2.10 0.02 2 62 . 7 MET HG2 H 2.54 0.02 2 63 . 7 MET HG3 H 2.70 0.02 2 64 . 7 MET HE H 2.23 0.02 1 65 . 7 MET CA C 55.8 0.1 1 66 . 7 MET CB C 37.0 0.1 1 67 . 7 MET CG C 31.4 0.1 1 68 . 7 MET CE C 32.1 0.1 1 69 . 8 ARG H H 8.82 0.02 1 70 . 8 ARG HA H 4.58 0.02 1 71 . 8 ARG HB2 H 1.63 0.02 2 72 . 8 ARG HB3 H 1.71 0.02 2 73 . 8 ARG HG2 H 1.18 0.02 2 74 . 8 ARG HG3 H 1.59 0.02 2 75 . 8 ARG HD2 H 2.90 0.02 2 76 . 8 ARG HD3 H 2.99 0.02 2 77 . 8 ARG HE H 7.13 0.02 1 78 . 8 ARG CA C 55.5 0.1 1 79 . 8 ARG CB C 31.0 0.1 1 80 . 8 ARG CG C 28.0 0.1 1 81 . 8 ARG CD C 42.8 0.1 1 82 . 9 CYS H H 8.28 0.02 1 83 . 9 CYS HA H 4.91 0.02 1 84 . 9 CYS HB2 H 3.19 0.02 1 85 . 9 CYS HB3 H 3.19 0.02 1 86 . 9 CYS CA C 54.1 0.1 1 87 . 9 CYS CB C 48.4 0.1 1 88 . 10 LYS H H 9.15 0.02 1 89 . 10 LYS HA H 4.50 0.02 1 90 . 10 LYS HB2 H 1.83 0.02 2 91 . 10 LYS HB3 H 1.92 0.02 2 92 . 10 LYS HG2 H 1.47 0.02 1 93 . 10 LYS HG3 H 1.47 0.02 1 94 . 10 LYS HD2 H 1.72 0.02 1 95 . 10 LYS HD3 H 1.72 0.02 1 96 . 10 LYS HE2 H 3.02 0.02 1 97 . 10 LYS HE3 H 3.02 0.02 1 98 . 10 LYS HZ H 7.58 0.02 1 99 . 10 LYS CA C 56.5 0.1 1 100 . 10 LYS CB C 34.4 0.1 1 101 . 10 LYS CG C 24.7 0.1 1 102 . 10 LYS CD C 28.8 0.1 1 103 . 10 LYS CE C 42.0 0.1 1 104 . 11 GLN H H 8.12 0.02 1 105 . 11 GLN HA H 4.81 0.02 1 106 . 11 GLN HB2 H 2.12 0.02 2 107 . 11 GLN HB3 H 2.33 0.02 2 108 . 11 GLN HG2 H 2.27 0.02 1 109 . 11 GLN HG3 H 2.27 0.02 1 110 . 11 GLN HE21 H 6.10 0.02 2 111 . 11 GLN HE22 H 7.72 0.02 2 112 . 11 GLN CA C 53.6 0.1 1 113 . 11 GLN CB C 31.4 0.1 1 114 . 11 GLN CG C 32.0 0.1 1 115 . 12 ASP H H 9.59 0.02 1 116 . 12 ASP HA H 4.17 0.02 1 117 . 12 ASP HB2 H 3.00 0.02 1 118 . 12 ASP HB3 H 3.13 0.02 1 119 . 12 ASP CA C 57.8 0.1 1 120 . 12 ASP CB C 37.6 0.1 1 121 . 13 SER H H 8.60 0.02 1 122 . 13 SER HA H 4.33 0.02 1 123 . 13 SER HB2 H 3.89 0.02 2 124 . 13 SER HB3 H 4.17 0.02 2 125 . 13 SER CA C 60.1 0.1 1 126 . 13 SER CB C 62.2 0.1 1 127 . 14 ASP H H 7.78 0.02 1 128 . 14 ASP HA H 4.71 0.02 1 129 . 14 ASP HB2 H 3.01 0.02 1 130 . 14 ASP HB3 H 3.16 0.02 1 131 . 14 ASP CA C 55.5 0.1 1 132 . 14 ASP CB C 41.6 0.1 1 133 . 15 CYS H H 7.87 0.02 1 134 . 15 CYS HA H 5.03 0.02 1 135 . 15 CYS HB2 H 2.79 0.02 1 136 . 15 CYS HB3 H 3.32 0.02 1 137 . 15 CYS CA C 52.5 0.1 1 138 . 15 CYS CB C 40.6 0.1 1 139 . 16 LEU H H 8.89 0.02 1 140 . 16 LEU HA H 4.28 0.02 1 141 . 16 LEU HB2 H 1.60 0.02 2 142 . 16 LEU HB3 H 1.76 0.02 2 143 . 16 LEU HG H 1.76 0.02 1 144 . 16 LEU HD1 H 0.98 0.02 2 145 . 16 LEU HD2 H 1.01 0.02 2 146 . 16 LEU CA C 54.7 0.1 1 147 . 16 LEU CB C 42.3 0.1 1 148 . 16 LEU CG C 27.0 0.1 1 149 . 16 LEU CD1 C 25.7 0.1 2 150 . 16 LEU CD2 C 22.1 0.1 2 151 . 17 ALA H H 8.19 0.02 1 152 . 17 ALA HA H 4.17 0.02 1 153 . 17 ALA HB H 1.42 0.02 1 154 . 17 ALA CA C 53.8 0.1 1 155 . 17 ALA CB C 18.0 0.1 1 156 . 18 GLY H H 8.77 0.02 1 157 . 18 GLY HA2 H 3.64 0.02 2 158 . 18 GLY HA3 H 4.51 0.02 2 159 . 18 GLY CA C 44.4 0.1 1 160 . 19 CYS H H 8.29 0.02 1 161 . 19 CYS HA H 5.03 0.02 1 162 . 19 CYS HB2 H 3.62 0.02 1 163 . 19 CYS HB3 H 3.13 0.02 1 164 . 19 CYS CA C 54.5 0.1 1 165 . 19 CYS CB C 46.3 0.1 1 166 . 20 VAL H H 9.26 0.02 1 167 . 20 VAL HA H 4.38 0.02 1 168 . 20 VAL HB H 2.17 0.02 1 169 . 20 VAL HG1 H 0.84 0.02 2 170 . 20 VAL HG2 H 0.93 0.02 2 171 . 20 VAL CA C 59.6 0.1 1 172 . 20 VAL CB C 34.8 0.1 1 173 . 20 VAL CG1 C 18.5 0.1 2 174 . 20 VAL CG2 C 21.4 0.1 2 175 . 21 CYS H H 8.84 0.02 1 176 . 21 CYS HA H 4.98 0.02 1 177 . 21 CYS HB2 H 2.53 0.02 1 178 . 21 CYS HB3 H 2.93 0.02 1 179 . 21 CYS CA C 55.5 0.1 1 180 . 21 CYS CB C 38.7 0.1 1 181 . 22 GLY H H 8.43 0.02 1 182 . 22 GLY HA2 H 4.53 0.02 1 183 . 22 GLY HA3 H 4.22 0.02 1 184 . 22 GLY CA C 45.2 0.1 1 185 . 23 PRO HA H 4.48 0.02 1 186 . 23 PRO HB2 H 2.10 0.02 2 187 . 23 PRO HB3 H 2.43 0.02 2 188 . 23 PRO HG2 H 2.15 0.02 1 189 . 23 PRO HG3 H 2.15 0.02 1 190 . 23 PRO HD2 H 3.77 0.02 2 191 . 23 PRO HD3 H 3.86 0.02 2 192 . 23 PRO CA C 64.5 0.1 1 193 . 23 PRO CB C 31.5 0.1 1 194 . 23 PRO CG C 27.1 0.1 1 195 . 23 PRO CD C 49.9 0.1 1 196 . 24 ASN H H 8.19 0.02 1 197 . 24 ASN HA H 4.78 0.02 1 198 . 24 ASN HB2 H 3.29 0.02 1 199 . 24 ASN HB3 H 3.07 0.02 1 200 . 24 ASN HD21 H 7.11 0.02 2 201 . 24 ASN HD22 H 7.81 0.02 2 202 . 24 ASN CA C 52.4 0.1 1 203 . 24 ASN CB C 37.5 0.1 1 204 . 25 GLY H H 8.41 0.02 1 205 . 25 GLY HA2 H 3.77 0.02 2 206 . 25 GLY HA3 H 4.01 0.02 2 207 . 25 GLY CA C 46.6 0.1 1 208 . 26 PHE H H 7.43 0.02 1 209 . 26 PHE HA H 5.40 0.02 1 210 . 26 PHE HB2 H 2.80 0.02 1 211 . 26 PHE HB3 H 3.15 0.02 1 212 . 26 PHE HD1 H 7.07 0.02 1 213 . 26 PHE HD2 H 7.07 0.02 1 214 . 26 PHE HE1 H 7.31 0.02 1 215 . 26 PHE HE2 H 7.31 0.02 1 216 . 26 PHE HZ H 7.31 0.02 1 217 . 26 PHE CA C 56.6 0.1 1 218 . 26 PHE CB C 42.2 0.1 1 219 . 26 PHE CD1 C 132.0 0.1 1 220 . 26 PHE CD2 C 132.0 0.1 1 221 . 26 PHE CE1 C 131.0 0.1 1 222 . 26 PHE CE2 C 131.0 0.1 1 223 . 26 PHE CZ C 129.4 0.1 1 224 . 27 CYS H H 8.90 0.02 1 225 . 27 CYS HA H 5.24 0.02 1 226 . 27 CYS HB2 H 3.18 0.02 1 227 . 27 CYS HB3 H 3.04 0.02 1 228 . 27 CYS CA C 55.2 0.1 1 229 . 27 CYS CB C 43.2 0.1 1 230 . 28 GLY H H 9.45 0.02 1 231 . 28 GLY HA2 H 4.04 0.02 2 232 . 28 GLY HA3 H 4.43 0.02 2 233 . 28 GLY CA C 46.8 0.1 1 stop_ save_