data_5676 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H chemical shifts of Pi4, a four disulfide bridged scorpion toxin active on potassium channels ; _BMRB_accession_number 5676 _BMRB_flat_file_name bmr5676.str _Entry_type original _Submission_date 2003-01-24 _Accession_date 2003-01-24 _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 Guijarro J. I. . 2 M'Barek S. . . 3 Olamendi-Portugal T. . . 4 Gomez-Lagunas F. . . 5 Garnier D. . . 6 Rochat H. . . 7 Possani L. D. . 8 Sabatier J. M. . 9 Delepierre M. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 400 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-09-05 original BMRB . stop_ _Original_release_date 2003-01-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Synthesis and Characterization of Pi4, a Scorpion Toxin from Pandinus imperator that acts on K+ Channels ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12919322 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 M'Barek S. . . 2 Mosbah A. . . 3 Sandoz G. . . 4 Fajloun Z. . . 5 Olamendi-Portugal T. . . 6 Rochat H. . . 7 Sampieri F. . . 8 Guijarro J. I. . 9 Mansuelle P. . . 10 Delepierre M. . . 11 'De Waard' M. . . 12 Sabatier J. M. . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_volume 270 _Journal_issue 17 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3583 _Page_last 3592 _Year 2003 _Details . loop_ _Keyword 'disulfide bridge stabilized alpha beta motif' 'potassium channel blocker' 'scorpion toxin' stop_ save_ ################################## # Molecular system description # ################################## save_system_Pi4 _Saveframe_category molecular_system _Mol_system_name 'Pandinus imperator potassium channel blocking toxin 4' _Abbreviation_common Pi4 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Pi4 scorpion toxin' $Pi4 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'potassium channel blocker' toxin stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Pi4 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Pi4 scorpion toxin' _Abbreviation_common Pi4 _Molecular_mass 4180 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 38 _Mol_residue_sequence ; IEAIRCGGSRDCYRPCQKRT GCPNAKCINKTCKCYGCS ; loop_ _Residue_seq_code _Residue_label 1 ILE 2 GLU 3 ALA 4 ILE 5 ARG 6 CYS 7 GLY 8 GLY 9 SER 10 ARG 11 ASP 12 CYS 13 TYR 14 ARG 15 PRO 16 CYS 17 GLN 18 LYS 19 ARG 20 THR 21 GLY 22 CYS 23 PRO 24 ASN 25 ALA 26 LYS 27 CYS 28 ILE 29 ASN 30 LYS 31 THR 32 CYS 33 LYS 34 CYS 35 TYR 36 GLY 37 CYS 38 SER 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 PDB 1N8M 'Solution Structure Of Pi4, A Four Disulfide Bridged Scorpion Toxin Active On Potassium Channels' 100.00 38 100.00 100.00 7.65e-13 SWISS-PROT P58498 'Potassium channel toxin alpha-KTx 6.4 (Potassium channel-blocking toxin 4) (Pi-4) (Pi4)' 100.00 38 100.00 100.00 7.65e-13 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Secretion $Pi4 Scorpion 55084 Eukaryota Metazoa Pandinus imperator venom 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 _Details $Pi4 'chemical synthesis' . . . . . ; Pi4 occurs naturally in the venom of Pandinus imperator scorpions, with an amidated C-terminus. It was established by NMR that the structure of the natural toxin extracted from scorpion venom is effectively identical to the structure of the synthetic toxin, which has a carboxylated C-terminus. ; 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 $Pi4 2.5 mM . 'sodium acetate' 5 mM . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Pi4 3.2 mM . 'sodium acetate' 5 mM . D2O 100 % . stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version 6.1C loop_ _Task collection 'raw spectral data processing' stop_ _Details 'Varian Inc., Palo Alto' save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.03 loop_ _Task 'data analysis' stop_ _Details 'Johnson, B.A. et al. (1994) J. Biomol. NMR 4, 603-614' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_P-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name P-COSY _Sample_label . save_ save_2D_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 5 0.02 mM pH 4.0 0.1 n/a pressure 1 . atm temperature 303 0.5 K stop_ save_ save_sample_cond_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 5 0.02 mM pH* 4.0 0.1 n/a pressure 1 . atm temperature 303 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D NOESY' P-COSY '2D TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Pi4 scorpion toxin' _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 3.86 0.02 1 2 . 1 ILE HB H 1.92 0.02 1 3 . 1 ILE HG12 H 1.21 0.02 2 4 . 1 ILE HG13 H 1.48 0.02 2 5 . 1 ILE HG2 H 0.95 0.02 1 6 . 1 ILE HD1 H 0.89 0.02 1 7 . 2 GLU H H 8.61 0.02 1 8 . 2 GLU HA H 4.39 0.02 1 9 . 2 GLU HB2 H 1.95 0.02 2 10 . 2 GLU HB3 H 2.05 0.02 2 11 . 2 GLU HG2 H 2.43 0.02 1 12 . 2 GLU HG3 H 2.43 0.02 1 13 . 3 ALA H H 8.45 0.02 1 14 . 3 ALA HA H 4.30 0.02 1 15 . 3 ALA HB H 1.34 0.02 1 16 . 4 ILE H H 8.68 0.02 1 17 . 4 ILE HA H 4.08 0.02 1 18 . 4 ILE HB H 1.41 0.02 1 19 . 4 ILE HG12 H 1.54 0.02 2 20 . 4 ILE HG13 H 1.01 0.02 2 21 . 4 ILE HG2 H 0.89 0.02 1 22 . 4 ILE HD1 H 0.73 0.02 1 23 . 5 ARG H H 8.45 0.02 1 24 . 5 ARG HA H 4.74 0.02 1 25 . 5 ARG HB2 H 1.73 0.02 2 26 . 5 ARG HB3 H 1.80 0.02 2 27 . 5 ARG HG2 H 1.63 0.02 1 28 . 5 ARG HG3 H 1.63 0.02 1 29 . 5 ARG HD2 H 3.19 0.02 1 30 . 5 ARG HD3 H 3.19 0.02 1 31 . 5 ARG HE H 7.13 0.02 1 32 . 6 CYS H H 7.89 0.02 1 33 . 6 CYS HA H 4.75 0.02 1 34 . 6 CYS HB2 H 2.94 0.02 2 35 . 6 CYS HB3 H 3.22 0.02 2 36 . 7 GLY H H 9.12 0.02 1 37 . 7 GLY HA2 H 3.68 0.02 2 38 . 7 GLY HA3 H 4.32 0.02 2 39 . 8 GLY H H 7.81 0.02 1 40 . 8 GLY HA2 H 3.98 0.02 2 41 . 8 GLY HA3 H 4.34 0.02 2 42 . 9 SER H H 9.10 0.02 1 43 . 9 SER HA H 3.73 0.02 1 44 . 9 SER HB2 H 3.91 0.02 1 45 . 9 SER HB3 H 3.91 0.02 1 46 . 10 ARG H H 8.53 0.02 1 47 . 10 ARG HA H 3.05 0.02 1 48 . 10 ARG HB2 H 1.67 0.02 2 49 . 10 ARG HB3 H 1.71 0.02 2 50 . 10 ARG HG2 H 1.56 0.02 1 51 . 10 ARG HG3 H 1.56 0.02 1 52 . 10 ARG HD2 H 3.16 0.02 1 53 . 10 ARG HD3 H 3.16 0.02 1 54 . 10 ARG HE H 7.21 0.02 1 55 . 11 ASP H H 7.36 0.02 1 56 . 11 ASP HA H 4.36 0.02 1 57 . 11 ASP HB2 H 2.80 0.02 2 58 . 11 ASP HB3 H 2.93 0.02 2 59 . 12 CYS H H 7.75 0.02 1 60 . 12 CYS HA H 4.53 0.02 1 61 . 12 CYS HB2 H 2.74 0.02 2 62 . 12 CYS HB3 H 2.99 0.02 2 63 . 13 TYR H H 6.89 0.02 1 64 . 13 TYR HA H 4.91 0.02 1 65 . 13 TYR HB2 H 3.05 0.02 2 66 . 13 TYR HB3 H 3.28 0.02 2 67 . 13 TYR HD1 H 7.21 0.02 1 68 . 13 TYR HD2 H 7.21 0.02 1 69 . 13 TYR HE1 H 6.83 0.02 1 70 . 13 TYR HE2 H 6.83 0.02 1 71 . 14 ARG H H 9.05 0.02 1 72 . 14 ARG HA H 4.39 0.02 1 73 . 14 ARG HB2 H 1.77 0.02 2 74 . 14 ARG HB3 H 1.94 0.02 2 75 . 14 ARG HG2 H 1.67 0.02 1 76 . 14 ARG HG3 H 1.67 0.02 1 77 . 14 ARG HD2 H 3.26 0.02 1 78 . 14 ARG HD3 H 3.26 0.02 1 79 . 14 ARG HE H 7.21 0.02 1 80 . 15 PRO HA H 4.34 0.02 1 81 . 15 PRO HB2 H 1.80 0.02 2 82 . 15 PRO HB3 H 2.34 0.02 2 83 . 15 PRO HG2 H 2.12 0.02 2 84 . 15 PRO HG3 H 2.25 0.02 2 85 . 15 PRO HD2 H 3.62 0.02 2 86 . 15 PRO HD3 H 3.69 0.02 2 87 . 16 CYS H H 8.34 0.02 1 88 . 16 CYS HA H 4.63 0.02 1 89 . 16 CYS HB2 H 3.05 0.02 2 90 . 16 CYS HB3 H 3.55 0.02 2 91 . 17 GLN H H 8.77 0.02 1 92 . 17 GLN HA H 3.63 0.02 1 93 . 17 GLN HB2 H 1.72 0.02 2 94 . 17 GLN HB3 H 2.29 0.02 2 95 . 17 GLN HG2 H 1.93 0.02 2 96 . 17 GLN HG3 H 2.12 0.02 2 97 . 17 GLN HE21 H 7.26 0.02 2 98 . 17 GLN HE22 H 6.68 0.02 2 99 . 18 LYS H H 8.16 0.02 1 100 . 18 LYS HA H 3.99 0.02 1 101 . 18 LYS HB2 H 1.85 0.02 2 102 . 18 LYS HB3 H 1.93 0.02 2 103 . 18 LYS HG2 H 1.46 0.02 2 104 . 18 LYS HG3 H 1.51 0.02 2 105 . 18 LYS HD2 H 1.63 0.02 2 106 . 18 LYS HD3 H 1.76 0.02 2 107 . 18 LYS HE2 H 2.95 0.02 1 108 . 18 LYS HE3 H 2.95 0.02 1 109 . 18 LYS HZ H 7.52 0.02 1 110 . 19 ARG H H 7.63 0.02 1 111 . 19 ARG HA H 4.24 0.02 1 112 . 19 ARG HB2 H 1.83 0.02 2 113 . 19 ARG HB3 H 1.99 0.02 2 114 . 19 ARG HG2 H 1.71 0.02 1 115 . 19 ARG HG3 H 1.71 0.02 1 116 . 19 ARG HD2 H 3.08 0.02 2 117 . 19 ARG HD3 H 3.21 0.02 2 118 . 19 ARG HE H 7.32 0.02 1 119 . 20 THR H H 8.34 0.02 1 120 . 20 THR HA H 4.77 0.02 1 121 . 20 THR HB H 4.46 0.02 1 122 . 20 THR HG2 H 1.22 0.02 1 123 . 21 GLY H H 8.22 0.02 1 124 . 21 GLY HA2 H 3.77 0.02 2 125 . 21 GLY HA3 H 4.75 0.02 2 126 . 22 CYS H H 8.24 0.02 1 127 . 22 CYS HA H 5.13 0.02 1 128 . 22 CYS HB2 H 2.17 0.02 2 129 . 22 CYS HB3 H 3.69 0.02 2 130 . 23 PRO HA H 4.55 0.02 1 131 . 23 PRO HB2 H 1.95 0.02 1 132 . 23 PRO HB3 H 1.95 0.02 1 133 . 23 PRO HG2 H 1.71 0.02 2 134 . 23 PRO HG3 H 1.88 0.02 2 135 . 23 PRO HD2 H 3.46 0.02 2 136 . 23 PRO HD3 H 3.70 0.02 2 137 . 24 ASN H H 7.10 0.02 1 138 . 24 ASN HA H 4.33 0.02 1 139 . 24 ASN HB2 H 2.77 0.02 2 140 . 24 ASN HB3 H 2.84 0.02 2 141 . 24 ASN HD21 H 7.67 0.02 2 142 . 24 ASN HD22 H 6.90 0.02 2 143 . 25 ALA H H 8.19 0.02 1 144 . 25 ALA HA H 5.32 0.02 1 145 . 25 ALA HB H 1.45 0.02 1 146 . 26 LYS H H 8.16 0.02 1 147 . 26 LYS HA H 4.65 0.02 1 148 . 26 LYS HB2 H 1.76 0.02 2 149 . 26 LYS HB3 H 1.85 0.02 2 150 . 26 LYS HG2 H 1.43 0.02 1 151 . 26 LYS HG3 H 1.43 0.02 1 152 . 26 LYS HD2 H 1.57 0.02 1 153 . 26 LYS HD3 H 1.57 0.02 1 154 . 26 LYS HE2 H 3.00 0.02 1 155 . 26 LYS HE3 H 3.00 0.02 1 156 . 27 CYS H H 8.37 0.02 1 157 . 27 CYS HA H 4.80 0.02 1 158 . 27 CYS HB2 H 2.35 0.02 2 159 . 27 CYS HB3 H 2.82 0.02 2 160 . 28 ILE H H 8.81 0.02 1 161 . 28 ILE HA H 4.27 0.02 1 162 . 28 ILE HB H 1.71 0.02 1 163 . 28 ILE HG13 H 1.40 0.02 2 164 . 28 ILE HG2 H 0.85 0.02 1 165 . 28 ILE HD1 H 0.94 0.02 1 166 . 29 ASN H H 9.37 0.02 1 167 . 29 ASN HA H 4.33 0.02 1 168 . 29 ASN HB2 H 2.73 0.02 2 169 . 29 ASN HB3 H 3.04 0.02 2 170 . 29 ASN HD21 H 7.54 0.02 2 171 . 29 ASN HD22 H 6.85 0.02 2 172 . 30 LYS H H 8.47 0.02 1 173 . 30 LYS HA H 3.96 0.02 1 174 . 30 LYS HB2 H 2.14 0.02 2 175 . 30 LYS HB3 H 2.23 0.02 2 176 . 30 LYS HG2 H 1.35 0.02 1 177 . 30 LYS HG3 H 1.35 0.02 1 178 . 30 LYS HD2 H 1.65 0.02 2 179 . 30 LYS HD3 H 1.70 0.02 2 180 . 30 LYS HE2 H 3.00 0.02 1 181 . 30 LYS HE3 H 3.00 0.02 1 182 . 30 LYS HZ H 7.49 0.02 1 183 . 31 THR H H 7.72 0.02 1 184 . 31 THR HA H 5.18 0.02 1 185 . 31 THR HB H 4.02 0.02 1 186 . 31 THR HG2 H 1.15 0.02 1 187 . 32 CYS H H 8.90 0.02 1 188 . 32 CYS HA H 4.68 0.02 1 189 . 32 CYS HB2 H 2.51 0.02 2 190 . 32 CYS HB3 H 2.78 0.02 2 191 . 33 LYS H H 9.19 0.02 1 192 . 33 LYS HA H 4.46 0.02 1 193 . 33 LYS HB2 H 1.60 0.02 2 194 . 33 LYS HB3 H 1.76 0.02 2 195 . 33 LYS HG2 H 0.88 0.02 2 196 . 33 LYS HG3 H 0.99 0.02 2 197 . 33 LYS HD2 H 1.51 0.02 1 198 . 33 LYS HD3 H 1.51 0.02 1 199 . 33 LYS HE2 H 2.72 0.02 2 200 . 33 LYS HE3 H 2.85 0.02 2 201 . 33 LYS HZ H 7.46 0.02 1 202 . 34 CYS H H 8.60 0.02 1 203 . 34 CYS HA H 4.93 0.02 1 204 . 34 CYS HB2 H 2.62 0.02 2 205 . 34 CYS HB3 H 3.62 0.02 2 206 . 35 TYR H H 8.25 0.02 1 207 . 35 TYR HA H 4.42 0.02 1 208 . 35 TYR HB2 H 2.46 0.02 2 209 . 35 TYR HB3 H 3.21 0.02 2 210 . 35 TYR HD1 H 6.96 0.02 1 211 . 35 TYR HD2 H 6.96 0.02 1 212 . 35 TYR HE1 H 6.66 0.02 1 213 . 35 TYR HE2 H 6.66 0.02 1 214 . 36 GLY H H 9.48 0.02 1 215 . 36 GLY HA2 H 3.90 0.02 2 216 . 36 GLY HA3 H 4.24 0.02 2 217 . 37 CYS H H 8.79 0.02 1 218 . 37 CYS HA H 4.67 0.02 1 219 . 37 CYS HB2 H 2.83 0.02 2 220 . 37 CYS HB3 H 3.24 0.02 2 221 . 38 SER H H 8.36 0.02 1 222 . 38 SER HA H 4.43 0.02 1 223 . 38 SER HB2 H 3.88 0.02 2 224 . 38 SER HB3 H 3.91 0.02 2 stop_ save_ save_chemical_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D NOESY' P-COSY '2D TOCSY' stop_ loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $sample_cond_2 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Pi4 scorpion toxin' _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 3.89 0.02 1 2 . 1 ILE HB H 1.95 0.02 1 3 . 1 ILE HG12 H 1.22 0.02 2 4 . 1 ILE HG13 H 1.51 0.02 2 5 . 1 ILE HG2 H 0.96 0.02 1 6 . 1 ILE HD1 H 0.91 0.02 1 7 . 2 GLU HA H 4.41 0.02 1 8 . 2 GLU HB2 H 1.99 0.02 2 9 . 2 GLU HB3 H 2.08 0.02 2 10 . 2 GLU HG2 H 2.47 0.02 1 11 . 2 GLU HG3 H 2.47 0.02 1 12 . 3 ALA HA H 4.31 0.02 1 13 . 3 ALA HB H 1.35 0.02 1 14 . 4 ILE HA H 4.10 0.02 1 15 . 4 ILE HB H 1.44 0.02 1 16 . 4 ILE HG12 H 1.56 0.02 2 17 . 4 ILE HG13 H 1.03 0.02 2 18 . 4 ILE HG2 H 0.90 0.02 1 19 . 4 ILE HD1 H 0.76 0.02 1 20 . 5 ARG HA H 4.75 0.02 1 21 . 5 ARG HB2 H 1.75 0.02 2 22 . 5 ARG HB3 H 1.81 0.02 2 23 . 5 ARG HG2 H 1.65 0.02 1 24 . 5 ARG HG3 H 1.65 0.02 1 25 . 5 ARG HD2 H 3.21 0.02 1 26 . 5 ARG HD3 H 3.21 0.02 1 27 . 6 CYS HA H 4.76 0.02 1 28 . 6 CYS HB2 H 2.97 0.02 2 29 . 6 CYS HB3 H 3.25 0.02 2 30 . 7 GLY HA2 H 3.69 0.02 2 31 . 7 GLY HA3 H 4.34 0.02 2 32 . 8 GLY HA2 H 4.00 0.02 2 33 . 8 GLY HA3 H 4.36 0.02 2 34 . 9 SER HA H 3.76 0.02 1 35 . 9 SER HB2 H 3.92 0.02 1 36 . 9 SER HB3 H 3.92 0.02 1 37 . 10 ARG HA H 3.06 0.02 1 38 . 10 ARG HB2 H 1.68 0.02 2 39 . 10 ARG HB3 H 1.74 0.02 2 40 . 10 ARG HG2 H 1.58 0.02 1 41 . 10 ARG HG3 H 1.58 0.02 1 42 . 10 ARG HD2 H 3.18 0.02 1 43 . 10 ARG HD3 H 3.18 0.02 1 44 . 11 ASP HA H 4.37 0.02 1 45 . 11 ASP HB2 H 2.81 0.02 2 46 . 11 ASP HB3 H 2.96 0.02 2 47 . 12 CYS HA H 4.55 0.02 1 48 . 12 CYS HB2 H 2.77 0.02 2 49 . 12 CYS HB3 H 3.02 0.02 2 50 . 13 TYR HA H 4.93 0.02 1 51 . 13 TYR HB2 H 3.06 0.02 2 52 . 13 TYR HB3 H 3.29 0.02 2 53 . 13 TYR HD1 H 7.23 0.02 1 54 . 13 TYR HD2 H 7.23 0.02 1 55 . 13 TYR HE1 H 6.85 0.02 1 56 . 13 TYR HE2 H 6.85 0.02 1 57 . 14 ARG HA H 4.40 0.02 1 58 . 14 ARG HB2 H 1.78 0.02 2 59 . 14 ARG HB3 H 1.95 0.02 2 60 . 14 ARG HG2 H 1.70 0.02 1 61 . 14 ARG HG3 H 1.70 0.02 1 62 . 14 ARG HD2 H 3.27 0.02 1 63 . 14 ARG HD3 H 3.27 0.02 1 64 . 15 PRO HA H 4.35 0.02 1 65 . 15 PRO HB2 H 1.82 0.02 2 66 . 15 PRO HB3 H 2.35 0.02 2 67 . 15 PRO HG2 H 2.14 0.02 2 68 . 15 PRO HG3 H 2.27 0.02 2 69 . 15 PRO HD2 H 3.63 0.02 2 70 . 15 PRO HD3 H 3.70 0.02 2 71 . 16 CYS HA H 4.65 0.02 1 72 . 16 CYS HB2 H 3.08 0.02 2 73 . 16 CYS HB3 H 3.58 0.02 2 74 . 17 GLN HA H 3.65 0.02 1 75 . 17 GLN HB2 H 1.74 0.02 2 76 . 17 GLN HB3 H 2.31 0.02 2 77 . 17 GLN HG2 H 1.96 0.02 2 78 . 17 GLN HG3 H 2.13 0.02 2 79 . 18 LYS HA H 4.01 0.02 1 80 . 18 LYS HB2 H 1.91 0.02 2 81 . 18 LYS HB3 H 1.96 0.02 2 82 . 18 LYS HG2 H 1.47 0.02 2 83 . 18 LYS HG3 H 1.53 0.02 2 84 . 18 LYS HD2 H 1.68 0.02 1 85 . 18 LYS HD3 H 1.68 0.02 1 86 . 18 LYS HE2 H 2.96 0.02 1 87 . 18 LYS HE3 H 2.96 0.02 1 88 . 19 ARG HA H 4.25 0.02 1 89 . 19 ARG HB2 H 1.84 0.02 2 90 . 19 ARG HB3 H 2.00 0.02 2 91 . 19 ARG HG2 H 1.72 0.02 1 92 . 19 ARG HG3 H 1.72 0.02 1 93 . 19 ARG HD2 H 3.09 0.02 2 94 . 19 ARG HD3 H 3.22 0.02 2 95 . 20 THR HA H 4.78 0.02 1 96 . 20 THR HB H 4.47 0.02 1 97 . 20 THR HG2 H 1.24 0.02 1 98 . 21 GLY HA2 H 3.79 0.02 2 99 . 21 GLY HA3 H 4.76 0.02 2 100 . 22 CYS HA H 5.15 0.02 1 101 . 22 CYS HB2 H 2.19 0.02 2 102 . 22 CYS HB3 H 3.70 0.02 2 103 . 23 PRO HA H 4.57 0.02 1 104 . 23 PRO HB2 H 1.96 0.02 1 105 . 23 PRO HB3 H 1.96 0.02 1 106 . 23 PRO HG2 H 1.73 0.02 2 107 . 23 PRO HG3 H 1.90 0.02 2 108 . 23 PRO HD2 H 3.49 0.02 2 109 . 23 PRO HD3 H 3.72 0.02 2 110 . 24 ASN HA H 4.34 0.02 1 111 . 24 ASN HB2 H 2.80 0.02 2 112 . 24 ASN HB3 H 2.86 0.02 2 113 . 25 ALA HA H 5.34 0.02 1 114 . 25 ALA HB H 1.47 0.02 1 115 . 26 LYS HA H 4.67 0.02 1 116 . 26 LYS HB2 H 1.78 0.02 2 117 . 26 LYS HB3 H 1.86 0.02 2 118 . 26 LYS HG2 H 1.44 0.02 1 119 . 26 LYS HG3 H 1.44 0.02 1 120 . 26 LYS HD2 H 1.59 0.02 1 121 . 26 LYS HD3 H 1.59 0.02 1 122 . 26 LYS HE2 H 2.98 0.02 1 123 . 26 LYS HE3 H 2.98 0.02 1 124 . 27 CYS HA H 4.83 0.02 1 125 . 27 CYS HB2 H 2.37 0.02 2 126 . 27 CYS HB3 H 2.83 0.02 2 127 . 28 ILE HA H 4.29 0.02 1 128 . 28 ILE HB H 1.73 0.02 1 129 . 28 ILE HG13 H 1.41 0.02 2 130 . 28 ILE HG2 H 0.87 0.02 1 131 . 28 ILE HD1 H 0.97 0.02 1 132 . 29 ASN HA H 4.34 0.02 1 133 . 29 ASN HB2 H 2.74 0.02 2 134 . 29 ASN HB3 H 3.05 0.02 2 135 . 30 LYS HA H 3.99 0.02 1 136 . 30 LYS HB2 H 2.16 0.02 2 137 . 30 LYS HB3 H 2.25 0.02 2 138 . 30 LYS HG2 H 1.38 0.02 1 139 . 30 LYS HG3 H 1.38 0.02 1 140 . 30 LYS HD2 H 1.68 0.02 2 141 . 30 LYS HD3 H 1.72 0.02 2 142 . 30 LYS HE2 H 3.01 0.02 1 143 . 30 LYS HE3 H 3.01 0.02 1 144 . 31 THR HA H 5.20 0.02 1 145 . 31 THR HB H 4.03 0.02 1 146 . 31 THR HG2 H 1.16 0.02 1 147 . 32 CYS HA H 4.70 0.02 1 148 . 32 CYS HB2 H 2.52 0.02 2 149 . 32 CYS HB3 H 2.80 0.02 2 150 . 33 LYS HA H 4.48 0.02 1 151 . 33 LYS HB2 H 1.62 0.02 2 152 . 33 LYS HB3 H 1.78 0.02 2 153 . 33 LYS HG2 H 0.91 0.02 2 154 . 33 LYS HG3 H 1.01 0.02 2 155 . 33 LYS HD2 H 1.53 0.02 1 156 . 33 LYS HD3 H 1.53 0.02 1 157 . 33 LYS HE2 H 2.73 0.02 2 158 . 33 LYS HE3 H 2.86 0.02 2 159 . 34 CYS HA H 4.95 0.02 1 160 . 34 CYS HB2 H 2.64 0.02 2 161 . 34 CYS HB3 H 3.65 0.02 2 162 . 35 TYR HA H 4.44 0.02 1 163 . 35 TYR HB2 H 2.48 0.02 2 164 . 35 TYR HB3 H 3.23 0.02 2 165 . 35 TYR HD1 H 6.98 0.02 1 166 . 35 TYR HD2 H 6.98 0.02 1 167 . 35 TYR HE1 H 6.69 0.02 1 168 . 35 TYR HE2 H 6.69 0.02 1 169 . 36 GLY HA2 H 3.92 0.02 2 170 . 36 GLY HA3 H 4.25 0.02 2 171 . 37 CYS HA H 4.70 0.02 1 172 . 37 CYS HB2 H 2.84 0.02 2 173 . 37 CYS HB3 H 3.25 0.02 2 174 . 38 SER HA H 4.48 0.02 1 175 . 38 SER HB2 H 3.89 0.02 2 176 . 38 SER HB3 H 3.93 0.02 2 stop_ save_