data_19700 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Spatial structure of P33A mutant of non-conventional toxin WTX from Naja kaouthia ; _BMRB_accession_number 19700 _BMRB_flat_file_name bmr19700.str _Entry_type original _Submission_date 2013-12-23 _Accession_date 2013-12-23 _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 Paramonov Alexander S. . 2 Shenkarev Zakhar O. . 3 Lyukmanova Ekaterina N. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 414 "15N chemical shifts" 74 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-12-22 original author . stop_ _Original_release_date 2014-12-22 save_ ############################# # Citation for this entry # ############################# save_citations _Saveframe_category entry_citation _Citation_full . _Citation_title 'Interaction of Weak Toxin from Naja kaouthia with Muscarinic Acetylcholine Receptors: Mutagenesis, NMR and Modeling Study' _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 Paramonov Alexander S. . 2 Shenkarev Zakhar O. . 3 Lyukmanova Ekaterina N. . stop_ _Journal_abbreviation 'To be Published' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'P33A mutant of non-conventional toxin WTX from Naja kaouthia' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'P33A mutant of non-conventional toxin WTX' $P33A_WTX stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_P33A_WTX _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common WTX[P33A] _Molecular_mass 7742.275 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 66 _Mol_residue_sequence ; MLTCLNCPEMFCGKFQICRN GEKICFKKLHQRRALSWRYI RGCADTCPVGKPYEMIECCS TDKCNR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 100 MET 2 101 LEU 3 102 THR 4 103 CYS 5 104 LEU 6 105 ASN 7 106 CYS 8 107 PRO 9 108 GLU 10 109 MET 11 110 PHE 12 111 CYS 13 112 GLY 14 113 LYS 15 114 PHE 16 115 GLN 17 116 ILE 18 117 CYS 19 118 ARG 20 119 ASN 21 120 GLY 22 121 GLU 23 122 LYS 24 123 ILE 25 124 CYS 26 125 PHE 27 126 LYS 28 127 LYS 29 128 LEU 30 129 HIS 31 130 GLN 32 131 ARG 33 132 ARG 34 133 ALA 35 134 LEU 36 135 SER 37 136 TRP 38 137 ARG 39 138 TYR 40 139 ILE 41 140 ARG 42 141 GLY 43 142 CYS 44 143 ALA 45 144 ASP 46 145 THR 47 146 CYS 48 147 PRO 49 148 VAL 50 149 GLY 51 150 LYS 52 151 PRO 53 152 TYR 54 153 GLU 55 154 MET 56 155 ILE 57 156 GLU 58 157 CYS 59 158 CYS 60 159 SER 61 160 THR 62 161 ASP 63 162 LYS 64 163 CYS 65 164 ASN 66 165 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-05 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 SP P82935 "RecName: Full=Tryptophan-containing weak neurotoxin; Short=WTX; Flags: Precursor" 98.48 86 98.46 98.46 2.82e-39 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $P33A_WTX 'monocled cobra' 8649 Eukaryota Metazoa Naja kaouthia 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 $P33A_WTX 'recombinant technology' . Escherichia coli BL21(DE3) pET22b(+) 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 $P33A_WTX 0.5 mM '[U-99% 15N]' H2O 95 % 'natural abundance' D2O 5 % '[U-100% 2H]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $P33A_WTX 0.5 mM '[U-99% 15N]' D2O 100 % '[U-100% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_2 save_ save_2D_1H-1H_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_2 save_ save_2D_DQF-COSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.01 . M pH 3.0 . pH pressure 1 . atm temperature 313 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D 1H-15N TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'P33A mutant of non-conventional toxin WTX' _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 1 100 1 MET HA H 4.170 0.02 1 2 100 1 MET HB2 H 2.172 0.02 2 3 100 1 MET HB3 H 2.213 0.02 2 4 100 1 MET HG2 H 2.655 0.02 1 5 100 1 MET HG3 H 2.655 0.02 1 6 101 2 LEU H H 8.706 0.02 1 7 101 2 LEU HA H 4.722 0.02 1 8 101 2 LEU HB2 H 1.426 0.02 1 9 101 2 LEU HB3 H 1.550 0.02 1 10 101 2 LEU HG H 1.510 0.02 1 11 101 2 LEU HD1 H 0.745 0.02 2 12 101 2 LEU HD2 H 0.825 0.02 2 13 101 2 LEU N N 128.488 0.10 1 14 102 3 THR H H 7.729 0.02 1 15 102 3 THR HA H 5.198 0.02 1 16 102 3 THR HB H 3.756 0.02 1 17 102 3 THR HG2 H 1.056 0.02 1 18 102 3 THR N N 117.086 0.10 1 19 103 4 CYS H H 8.514 0.02 1 20 103 4 CYS HA H 5.128 0.02 1 21 103 4 CYS HB2 H 2.645 0.02 1 22 103 4 CYS HB3 H 2.892 0.02 1 23 103 4 CYS N N 119.021 0.10 1 24 104 5 LEU H H 9.147 0.02 1 25 104 5 LEU HA H 4.811 0.02 1 26 104 5 LEU HB2 H 1.553 0.02 1 27 104 5 LEU HB3 H 1.553 0.02 1 28 104 5 LEU HG H 1.539 0.02 1 29 104 5 LEU HD1 H 0.863 0.02 2 30 104 5 LEU HD2 H 0.906 0.02 2 31 104 5 LEU N N 123.028 0.10 1 32 105 6 ASN H H 8.611 0.02 1 33 105 6 ASN HA H 4.806 0.02 1 34 105 6 ASN HB2 H 3.059 0.02 2 35 105 6 ASN HB3 H 2.350 0.02 2 36 105 6 ASN HD21 H 7.334 0.02 2 37 105 6 ASN HD22 H 6.455 0.02 2 38 105 6 ASN N N 119.029 0.10 1 39 105 6 ASN ND2 N 108.074 0.10 1 40 106 7 CYS H H 7.210 0.02 1 41 106 7 CYS HA H 5.227 0.02 1 42 106 7 CYS HB2 H 3.857 0.02 1 43 106 7 CYS HB3 H 3.538 0.02 1 44 106 7 CYS N N 117.427 0.10 1 45 107 8 PRO HA H 5.064 0.02 1 46 107 8 PRO HB2 H 2.328 0.02 1 47 107 8 PRO HB3 H 2.328 0.02 1 48 107 8 PRO HG2 H 2.173 0.02 1 49 107 8 PRO HG3 H 2.173 0.02 1 50 107 8 PRO HD2 H 3.954 0.02 2 51 107 8 PRO HD3 H 3.760 0.02 2 52 108 9 GLU H H 7.777 0.02 1 53 108 9 GLU HA H 4.576 0.02 1 54 108 9 GLU HB2 H 1.963 0.02 1 55 108 9 GLU HB3 H 2.356 0.02 1 56 108 9 GLU HG2 H 2.479 0.02 1 57 108 9 GLU HG3 H 2.479 0.02 1 58 108 9 GLU N N 119.996 0.10 1 59 109 10 MET H H 8.954 0.02 1 60 109 10 MET HA H 3.879 0.02 1 61 109 10 MET HB2 H 2.097 0.02 2 62 109 10 MET HB3 H 1.979 0.02 2 63 109 10 MET HG2 H 2.147 0.02 1 64 109 10 MET HG3 H 2.147 0.02 1 65 109 10 MET N N 121.587 0.10 1 66 110 11 PHE H H 7.943 0.02 1 67 110 11 PHE HA H 4.947 0.02 1 68 110 11 PHE HB2 H 2.903 0.02 1 69 110 11 PHE HB3 H 3.153 0.02 1 70 110 11 PHE HD1 H 7.314 0.02 1 71 110 11 PHE HD2 H 7.314 0.02 1 72 110 11 PHE HE1 H 7.385 0.02 1 73 110 11 PHE HE2 H 7.385 0.02 1 74 110 11 PHE N N 114.224 0.10 1 75 111 12 CYS H H 8.141 0.02 1 76 111 12 CYS HA H 4.853 0.02 1 77 111 12 CYS HB2 H 3.407 0.02 1 78 111 12 CYS HB3 H 4.010 0.02 1 79 111 12 CYS N N 117.718 0.10 1 80 112 13 GLY H H 8.738 0.02 1 81 112 13 GLY HA2 H 4.652 0.02 1 82 112 13 GLY HA3 H 3.710 0.02 1 83 112 13 GLY N N 106.232 0.10 1 84 113 14 LYS H H 7.064 0.02 1 85 113 14 LYS HA H 4.391 0.02 1 86 113 14 LYS HB2 H 1.671 0.02 1 87 113 14 LYS HB3 H 1.904 0.02 1 88 113 14 LYS HG2 H 1.527 0.02 2 89 113 14 LYS HG3 H 1.616 0.02 2 90 113 14 LYS HD2 H 1.751 0.02 1 91 113 14 LYS HD3 H 1.751 0.02 1 92 113 14 LYS HE2 H 3.080 0.02 1 93 113 14 LYS HE3 H 3.080 0.02 1 94 113 14 LYS N N 123.354 0.10 1 95 114 15 PHE H H 7.823 0.02 1 96 114 15 PHE HA H 5.344 0.02 1 97 114 15 PHE HB2 H 2.842 0.02 1 98 114 15 PHE HB3 H 2.643 0.02 1 99 114 15 PHE HD1 H 7.077 0.02 1 100 114 15 PHE HD2 H 7.077 0.02 1 101 114 15 PHE HE1 H 7.412 0.02 1 102 114 15 PHE HE2 H 7.412 0.02 1 103 114 15 PHE N N 117.507 0.10 1 104 115 16 GLN H H 9.044 0.02 1 105 115 16 GLN HA H 4.788 0.02 1 106 115 16 GLN HB2 H 1.993 0.02 2 107 115 16 GLN HB3 H 2.103 0.02 2 108 115 16 GLN HG2 H 2.176 0.02 2 109 115 16 GLN HG3 H 2.302 0.02 2 110 115 16 GLN HE21 H 7.035 0.02 2 111 115 16 GLN HE22 H 7.304 0.02 2 112 115 16 GLN N N 117.426 0.10 1 113 115 16 GLN NE2 N 111.344 0.10 1 114 116 17 ILE H H 8.705 0.02 1 115 116 17 ILE HA H 4.367 0.02 1 116 116 17 ILE HB H 1.830 0.02 1 117 116 17 ILE HG12 H 1.261 0.02 2 118 116 17 ILE HG13 H 1.755 0.02 2 119 116 17 ILE HG2 H 1.048 0.02 1 120 116 17 ILE HD1 H 1.006 0.02 1 121 116 17 ILE N N 124.941 0.10 1 122 117 18 CYS H H 9.103 0.02 1 123 117 18 CYS HA H 4.848 0.02 1 124 117 18 CYS HB2 H 2.885 0.02 1 125 117 18 CYS HB3 H 3.701 0.02 1 126 117 18 CYS N N 127.674 0.10 1 127 118 19 ARG H H 8.396 0.02 1 128 118 19 ARG HA H 4.512 0.02 1 129 118 19 ARG HB2 H 1.700 0.02 2 130 118 19 ARG HB3 H 1.980 0.02 2 131 118 19 ARG HG2 H 1.660 0.02 2 132 118 19 ARG HG3 H 1.802 0.02 2 133 118 19 ARG HD2 H 3.292 0.02 1 134 118 19 ARG HD3 H 3.292 0.02 1 135 118 19 ARG HE H 7.216 0.02 1 136 118 19 ARG N N 120.976 0.10 1 137 118 19 ARG NE N 84.951 0.10 1 138 119 20 ASN H H 8.836 0.02 1 139 119 20 ASN HA H 4.560 0.02 1 140 119 20 ASN HB2 H 2.827 0.02 2 141 119 20 ASN HB3 H 2.886 0.02 2 142 119 20 ASN HD21 H 7.669 0.02 2 143 119 20 ASN HD22 H 6.985 0.02 2 144 119 20 ASN N N 119.240 0.10 1 145 119 20 ASN ND2 N 113.103 0.10 1 146 120 21 GLY H H 8.755 0.02 1 147 120 21 GLY HA2 H 4.258 0.02 1 148 120 21 GLY HA3 H 3.733 0.02 1 149 120 21 GLY N N 111.230 0.10 1 150 121 22 GLU H H 8.158 0.02 1 151 121 22 GLU HA H 4.250 0.02 1 152 121 22 GLU HB2 H 2.464 0.02 1 153 121 22 GLU HB3 H 1.846 0.02 1 154 121 22 GLU HG2 H 2.427 0.02 2 155 121 22 GLU HG3 H 2.134 0.02 2 156 121 22 GLU N N 119.650 0.10 1 157 122 23 LYS H H 7.622 0.02 1 158 122 23 LYS HA H 4.559 0.02 1 159 122 23 LYS HB2 H 1.847 0.02 1 160 122 23 LYS HB3 H 2.070 0.02 1 161 122 23 LYS HG2 H 1.482 0.02 1 162 122 23 LYS HG3 H 1.482 0.02 1 163 122 23 LYS HD2 H 1.784 0.02 1 164 122 23 LYS HD3 H 1.784 0.02 1 165 122 23 LYS HE2 H 3.104 0.02 1 166 122 23 LYS HE3 H 3.104 0.02 1 167 122 23 LYS N N 120.471 0.10 1 168 123 24 ILE H H 8.142 0.02 1 169 123 24 ILE HA H 4.756 0.02 1 170 123 24 ILE HB H 1.902 0.02 1 171 123 24 ILE HG12 H 1.093 0.02 2 172 123 24 ILE HG13 H 1.286 0.02 2 173 123 24 ILE HG2 H 0.924 0.02 1 174 123 24 ILE HD1 H 0.859 0.02 1 175 123 24 ILE N N 118.223 0.10 1 176 124 25 CYS H H 9.196 0.02 1 177 124 25 CYS HA H 5.985 0.02 1 178 124 25 CYS HB2 H 2.987 0.02 1 179 124 25 CYS HB3 H 2.987 0.02 1 180 124 25 CYS N N 118.872 0.10 1 181 125 26 PHE H H 8.958 0.02 1 182 125 26 PHE HA H 6.317 0.02 1 183 125 26 PHE HB2 H 3.104 0.02 1 184 125 26 PHE HB3 H 2.835 0.02 1 185 125 26 PHE HD1 H 6.849 0.02 1 186 125 26 PHE HD2 H 6.849 0.02 1 187 125 26 PHE HE1 H 7.093 0.02 1 188 125 26 PHE HE2 H 7.093 0.02 1 189 125 26 PHE HZ H 7.241 0.02 1 190 125 26 PHE N N 116.458 0.10 1 191 126 27 LYS H H 9.109 0.02 1 192 126 27 LYS HA H 5.151 0.02 1 193 126 27 LYS HB2 H 1.555 0.02 1 194 126 27 LYS HB3 H 1.769 0.02 1 195 126 27 LYS HG2 H 1.057 0.02 1 196 126 27 LYS HG3 H 1.057 0.02 1 197 126 27 LYS HD2 H 0.837 0.02 2 198 126 27 LYS HD3 H 1.170 0.02 2 199 126 27 LYS HE2 H 2.202 0.02 2 200 126 27 LYS HE3 H 2.466 0.02 2 201 126 27 LYS N N 125.559 0.10 1 202 127 28 LYS H H 9.498 0.02 1 203 127 28 LYS HA H 5.217 0.02 1 204 127 28 LYS HB2 H 1.977 0.02 1 205 127 28 LYS HB3 H 1.977 0.02 1 206 127 28 LYS HG2 H 1.480 0.02 1 207 127 28 LYS HG3 H 1.480 0.02 1 208 127 28 LYS HD2 H 1.595 0.02 1 209 127 28 LYS HD3 H 1.595 0.02 1 210 127 28 LYS HE2 H 2.866 0.02 2 211 127 28 LYS HE3 H 2.810 0.02 2 212 127 28 LYS N N 124.796 0.10 1 213 128 29 LEU H H 9.105 0.02 1 214 128 29 LEU HA H 4.441 0.02 1 215 128 29 LEU HB2 H 1.612 0.02 2 216 128 29 LEU HB3 H 1.823 0.02 2 217 128 29 LEU HG H 1.468 0.02 1 218 128 29 LEU HD1 H 0.700 0.02 2 219 128 29 LEU HD2 H 0.754 0.02 2 220 128 29 LEU N N 126.430 0.10 1 221 129 30 HIS H H 9.123 0.02 1 222 129 30 HIS HA H 4.930 0.02 1 223 129 30 HIS HB2 H 2.946 0.02 1 224 129 30 HIS HB3 H 3.149 0.02 1 225 129 30 HIS HD2 H 7.272 0.02 1 226 129 30 HIS HE1 H 8.669 0.02 1 227 129 30 HIS N N 124.315 0.10 1 228 130 31 GLN H H 8.246 0.02 1 229 130 31 GLN HA H 4.384 0.02 1 230 130 31 GLN HB2 H 1.822 0.02 2 231 130 31 GLN HB3 H 1.955 0.02 2 232 130 31 GLN HG2 H 2.095 0.02 1 233 130 31 GLN HG3 H 2.095 0.02 1 234 130 31 GLN HE21 H 7.321 0.02 2 235 130 31 GLN HE22 H 6.757 0.02 2 236 130 31 GLN N N 120.311 0.10 1 237 130 31 GLN NE2 N 111.337 0.10 1 238 131 32 ARG H H 8.510 0.02 1 239 131 32 ARG HA H 4.290 0.02 1 240 131 32 ARG HB2 H 1.577 0.02 2 241 131 32 ARG HB3 H 1.729 0.02 2 242 131 32 ARG HG2 H 1.328 0.02 1 243 131 32 ARG HG3 H 1.328 0.02 1 244 131 32 ARG HD2 H 2.960 0.02 1 245 131 32 ARG HD3 H 2.960 0.02 1 246 131 32 ARG HE H 7.006 0.02 1 247 131 32 ARG N N 123.995 0.10 1 248 131 32 ARG NE N 84.583 0.10 1 249 132 33 ARG H H 8.183 0.02 1 250 132 33 ARG HA H 4.308 0.02 1 251 132 33 ARG HB2 H 1.766 0.02 2 252 132 33 ARG HB3 H 1.893 0.02 2 253 132 33 ARG HG2 H 1.590 0.02 2 254 132 33 ARG HG3 H 1.628 0.02 2 255 132 33 ARG HD2 H 3.201 0.02 1 256 132 33 ARG HD3 H 3.201 0.02 1 257 132 33 ARG HE H 7.162 0.02 1 258 132 33 ARG N N 121.592 0.10 1 259 132 33 ARG NE N 84.589 0.10 1 260 133 34 ALA H H 8.249 0.02 1 261 133 34 ALA HA H 4.236 0.02 1 262 133 34 ALA HB H 1.410 0.02 1 263 133 34 ALA N N 124.315 0.10 1 264 134 35 LEU H H 8.146 0.02 1 265 134 35 LEU HA H 4.265 0.02 1 266 134 35 LEU HB2 H 1.724 0.02 1 267 134 35 LEU HB3 H 1.651 0.02 1 268 134 35 LEU HG H 1.710 0.02 1 269 134 35 LEU HD1 H 0.922 0.02 1 270 134 35 LEU HD2 H 0.922 0.02 1 271 134 35 LEU N N 119.576 0.10 1 272 135 36 SER H H 7.980 0.02 1 273 135 36 SER HA H 4.504 0.02 1 274 135 36 SER HB2 H 3.859 0.02 1 275 135 36 SER HB3 H 3.859 0.02 1 276 135 36 SER N N 113.103 0.10 1 277 136 37 TRP H H 8.027 0.02 1 278 136 37 TRP HA H 4.853 0.02 1 279 136 37 TRP HB2 H 3.128 0.02 2 280 136 37 TRP HB3 H 3.181 0.02 2 281 136 37 TRP HD1 H 7.185 0.02 1 282 136 37 TRP HE1 H 10.035 0.02 1 283 136 37 TRP HE3 H 7.596 0.02 1 284 136 37 TRP HZ2 H 7.537 0.02 1 285 136 37 TRP HZ3 H 7.137 0.02 1 286 136 37 TRP HH2 H 7.285 0.02 1 287 136 37 TRP N N 123.354 0.10 1 288 136 37 TRP NE1 N 128.640 0.10 1 289 137 38 ARG H H 7.991 0.02 1 290 137 38 ARG HA H 4.674 0.02 1 291 137 38 ARG HB2 H 1.723 0.02 1 292 137 38 ARG HB3 H 1.723 0.02 1 293 137 38 ARG HG2 H 1.398 0.02 1 294 137 38 ARG HG3 H 1.398 0.02 1 295 137 38 ARG HD2 H 3.178 0.02 1 296 137 38 ARG HD3 H 3.178 0.02 1 297 137 38 ARG HE H 7.180 0.02 1 298 137 38 ARG N N 120.614 0.10 1 299 137 38 ARG NE N 84.270 0.10 1 300 138 39 TYR H H 9.191 0.02 1 301 138 39 TYR HA H 5.414 0.02 1 302 138 39 TYR HB2 H 2.622 0.02 1 303 138 39 TYR HB3 H 2.915 0.02 1 304 138 39 TYR HD1 H 6.950 0.02 1 305 138 39 TYR HD2 H 6.950 0.02 1 306 138 39 TYR HE1 H 6.866 0.02 1 307 138 39 TYR HE2 H 6.866 0.02 1 308 138 39 TYR N N 119.354 0.10 1 309 139 40 ILE H H 9.104 0.02 1 310 139 40 ILE HA H 4.318 0.02 1 311 139 40 ILE HB H 1.699 0.02 1 312 139 40 ILE HG12 H 1.148 0.02 2 313 139 40 ILE HG13 H 1.514 0.02 2 314 139 40 ILE HG2 H 1.068 0.02 1 315 139 40 ILE HD1 H 0.734 0.02 1 316 139 40 ILE N N 119.510 0.10 1 317 140 41 ARG H H 8.393 0.02 1 318 140 41 ARG HA H 4.816 0.02 1 319 140 41 ARG HB2 H 1.352 0.02 2 320 140 41 ARG HB3 H 1.447 0.02 2 321 140 41 ARG HG2 H 1.765 0.02 1 322 140 41 ARG HG3 H 1.765 0.02 1 323 140 41 ARG HD2 H 3.209 0.02 1 324 140 41 ARG HD3 H 3.209 0.02 1 325 140 41 ARG HE H 6.627 0.02 1 326 140 41 ARG N N 125.596 0.10 1 327 140 41 ARG NE N 80.743 0.10 1 328 141 42 GLY H H 6.307 0.02 1 329 141 42 GLY HA2 H 3.915 0.02 2 330 141 42 GLY HA3 H 4.012 0.02 2 331 141 42 GLY N N 103.964 0.10 1 332 142 43 CYS H H 8.184 0.02 1 333 142 43 CYS HA H 5.756 0.02 1 334 142 43 CYS HB2 H 3.298 0.02 1 335 142 43 CYS HB3 H 2.804 0.02 1 336 142 43 CYS N N 117.908 0.10 1 337 143 44 ALA H H 9.508 0.02 1 338 143 44 ALA HA H 4.795 0.02 1 339 143 44 ALA HB H 1.571 0.02 1 340 143 44 ALA N N 121.268 0.10 1 341 144 45 ASP H H 9.030 0.02 1 342 144 45 ASP HA H 4.892 0.02 1 343 144 45 ASP HB2 H 2.972 0.02 1 344 144 45 ASP HB3 H 2.972 0.02 1 345 144 45 ASP N N 118.068 0.10 1 346 145 46 THR H H 7.401 0.02 1 347 145 46 THR HA H 4.422 0.02 1 348 145 46 THR HB H 4.074 0.02 1 349 145 46 THR HG2 H 1.124 0.02 1 350 145 46 THR N N 108.476 0.10 1 351 146 47 CYS H H 8.850 0.02 1 352 146 47 CYS HA H 4.713 0.02 1 353 146 47 CYS HB2 H 3.073 0.02 1 354 146 47 CYS HB3 H 2.956 0.02 1 355 146 47 CYS N N 123.516 0.10 1 356 147 48 PRO HA H 4.256 0.02 1 357 147 48 PRO HB2 H 2.035 0.02 1 358 147 48 PRO HB3 H 1.558 0.02 1 359 147 48 PRO HG2 H 1.225 0.02 2 360 147 48 PRO HG3 H 1.135 0.02 2 361 147 48 PRO HD2 H 3.337 0.02 2 362 147 48 PRO HD3 H 3.651 0.02 2 363 148 49 VAL H H 7.857 0.02 1 364 148 49 VAL HA H 4.086 0.02 1 365 148 49 VAL HB H 1.983 0.02 1 366 148 49 VAL HG1 H 0.957 0.02 1 367 148 49 VAL HG2 H 0.957 0.02 1 368 148 49 VAL N N 118.686 0.10 1 369 149 50 GLY H H 8.357 0.02 1 370 149 50 GLY HA2 H 3.757 0.02 2 371 149 50 GLY HA3 H 4.301 0.02 2 372 149 50 GLY N N 113.423 0.10 1 373 150 51 LYS H H 8.574 0.02 1 374 150 51 LYS HA H 4.627 0.02 1 375 150 51 LYS HB2 H 1.191 0.02 1 376 150 51 LYS HB3 H 1.633 0.02 1 377 150 51 LYS HG2 H 1.537 0.02 1 378 150 51 LYS HG3 H 1.537 0.02 1 379 150 51 LYS HD2 H 1.745 0.02 2 380 150 51 LYS HD3 H 1.809 0.02 2 381 150 51 LYS HE2 H 3.099 0.02 1 382 150 51 LYS HE3 H 3.099 0.02 1 383 150 51 LYS N N 121.492 0.10 1 384 151 52 PRO HA H 4.342 0.02 1 385 151 52 PRO HB2 H 2.237 0.02 1 386 151 52 PRO HB3 H 2.432 0.02 1 387 151 52 PRO HG2 H 2.124 0.02 1 388 151 52 PRO HG3 H 2.001 0.02 1 389 151 52 PRO HD2 H 3.736 0.02 1 390 151 52 PRO HD3 H 3.945 0.02 1 391 152 53 TYR H H 7.127 0.02 1 392 152 53 TYR HA H 4.524 0.02 1 393 152 53 TYR HB2 H 3.082 0.02 1 394 152 53 TYR HB3 H 3.359 0.02 1 395 152 53 TYR HD1 H 7.116 0.02 1 396 152 53 TYR HD2 H 7.116 0.02 1 397 152 53 TYR HE1 H 6.914 0.02 1 398 152 53 TYR HE2 H 6.914 0.02 1 399 152 53 TYR N N 111.257 0.10 1 400 153 54 GLU H H 7.603 0.02 1 401 153 54 GLU HA H 4.407 0.02 1 402 153 54 GLU HB2 H 2.129 0.02 1 403 153 54 GLU HB3 H 2.129 0.02 1 404 153 54 GLU HG2 H 1.945 0.02 2 405 153 54 GLU HG3 H 2.210 0.02 2 406 153 54 GLU N N 119.670 0.10 1 407 154 55 MET H H 8.052 0.02 1 408 154 55 MET HA H 4.335 0.02 1 409 154 55 MET HB2 H 2.142 0.02 1 410 154 55 MET HB3 H 2.236 0.02 1 411 154 55 MET HG2 H 2.594 0.02 2 412 154 55 MET HG3 H 2.693 0.02 2 413 154 55 MET N N 117.748 0.10 1 414 155 56 ILE H H 8.393 0.02 1 415 155 56 ILE HA H 4.544 0.02 1 416 155 56 ILE HB H 1.718 0.02 1 417 155 56 ILE HG12 H 0.960 0.02 2 418 155 56 ILE HG13 H 1.616 0.02 2 419 155 56 ILE HG2 H 0.940 0.02 1 420 155 56 ILE HD1 H 0.722 0.02 1 421 155 56 ILE N N 121.057 0.10 1 422 156 57 GLU H H 8.994 0.02 1 423 156 57 GLU HA H 4.872 0.02 1 424 156 57 GLU HB2 H 2.067 0.02 2 425 156 57 GLU HB3 H 2.153 0.02 2 426 156 57 GLU HG2 H 2.522 0.02 2 427 156 57 GLU HG3 H 2.283 0.02 2 428 156 57 GLU N N 127.999 0.10 1 429 157 58 CYS H H 9.029 0.02 1 430 157 58 CYS HA H 5.518 0.02 1 431 157 58 CYS HB2 H 3.011 0.02 1 432 157 58 CYS HB3 H 3.775 0.02 1 433 157 58 CYS N N 123.034 0.10 1 434 158 59 CYS H H 9.344 0.02 1 435 158 59 CYS HA H 5.171 0.02 1 436 158 59 CYS HB2 H 3.637 0.02 1 437 158 59 CYS HB3 H 3.545 0.02 1 438 158 59 CYS N N 119.670 0.10 1 439 159 60 SER H H 9.064 0.02 1 440 159 60 SER HA H 5.112 0.02 1 441 159 60 SER HB2 H 4.032 0.02 2 442 159 60 SER HB3 H 4.212 0.02 2 443 159 60 SER N N 114.684 0.10 1 444 160 61 THR H H 7.626 0.02 1 445 160 61 THR HA H 4.784 0.02 1 446 160 61 THR HB H 4.374 0.02 1 447 160 61 THR HG2 H 1.241 0.02 1 448 160 61 THR N N 111.828 0.10 1 449 161 62 ASP H H 8.332 0.02 1 450 161 62 ASP HA H 4.856 0.02 1 451 161 62 ASP HB2 H 2.626 0.02 1 452 161 62 ASP HB3 H 2.412 0.02 1 453 161 62 ASP N N 118.279 0.10 1 454 162 63 LYS H H 9.460 0.02 1 455 162 63 LYS HA H 3.452 0.02 1 456 162 63 LYS HB2 H 1.793 0.02 1 457 162 63 LYS HB3 H 1.879 0.02 1 458 162 63 LYS HG2 H 1.107 0.02 2 459 162 63 LYS HG3 H 0.691 0.02 2 460 162 63 LYS HD2 H 1.264 0.02 1 461 162 63 LYS HD3 H 1.264 0.02 1 462 162 63 LYS HE2 H 2.339 0.02 1 463 162 63 LYS HE3 H 2.339 0.02 1 464 162 63 LYS N N 116.091 0.10 1 465 163 64 CYS H H 7.751 0.02 1 466 163 64 CYS HA H 4.416 0.02 1 467 163 64 CYS HB2 H 3.357 0.02 1 468 163 64 CYS HB3 H 3.760 0.02 1 469 163 64 CYS N N 111.859 0.10 1 470 164 65 ASN H H 9.396 0.02 1 471 164 65 ASN HA H 4.684 0.02 1 472 164 65 ASN HB2 H 2.579 0.02 1 473 164 65 ASN HB3 H 2.188 0.02 1 474 164 65 ASN HD21 H 7.777 0.02 1 475 164 65 ASN HD22 H 7.833 0.02 1 476 164 65 ASN N N 122.713 0.10 1 477 164 65 ASN ND2 N 114.224 0.10 1 478 165 66 ARG H H 7.512 0.02 1 479 165 66 ARG HA H 3.740 0.02 1 480 165 66 ARG HB2 H 1.849 0.02 1 481 165 66 ARG HB3 H 1.770 0.02 1 482 165 66 ARG HG2 H 1.710 0.02 1 483 165 66 ARG HG3 H 1.710 0.02 1 484 165 66 ARG HD2 H 3.337 0.02 1 485 165 66 ARG HD3 H 3.337 0.02 1 486 165 66 ARG HE H 7.276 0.02 1 487 165 66 ARG N N 124.772 0.10 1 488 165 66 ARG NE N 84.909 0.10 1 stop_ save_