data_30522 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution NMR structure of spider toxin analogue [F5A,M6F,T26L,K28R]GpTx-1 ; _BMRB_accession_number 30522 _BMRB_flat_file_name bmr30522.str _Entry_type original _Submission_date 2018-09-25 _Accession_date 2018-09-25 _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 Schroeder C. I. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 205 "13C chemical shifts" 96 "15N chemical shifts" 36 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-07-09 update BMRB 'update entry citation' 2018-12-13 original author 'original release' stop_ _Original_release_date 2018-09-26 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Peptide-Membrane Interactions Affect the Inhibitory Potency and Selectivity of Spider Toxins ProTx-II and GpTx-1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30507158 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lawrence N. . . 2 Wu B. . . 3 Ligutti J. . . 4 Cheneval O. . . 5 Agwa A. J. . 6 Benfield A. H. . 7 Biswas K. . . 8 Craik D. J. . 9 Miranda L. P. . 10 Henriques S. T. . 11 Schroeder C. I. . stop_ _Journal_abbreviation 'ACS Chem. Biol.' _Journal_name_full 'ACS chemical biology' _Journal_volume 14 _Journal_issue 1 _Journal_ISSN 1554-8937 _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 118 _Page_last 130 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Toxin GTx1-15' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 4068.863 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 34 _Mol_residue_sequence ; DCLGAFRKCIPDNDKCCRPN LVCSRLHRWCKYVF ; loop_ _Residue_seq_code _Residue_label 1 ASP 2 CYS 3 LEU 4 GLY 5 ALA 6 PHE 7 ARG 8 LYS 9 CYS 10 ILE 11 PRO 12 ASP 13 ASN 14 ASP 15 LYS 16 CYS 17 CYS 18 ARG 19 PRO 20 ASN 21 LEU 22 VAL 23 CYS 24 SER 25 ARG 26 LEU 27 HIS 28 ARG 29 TRP 30 CYS 31 LYS 32 TYR 33 VAL 34 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 'Tarantula spider' 1749325 Eukaryota Metazoa Grammostola porteri 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 $entity_1 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '2 mg/mL [AFLR]GpTx-1, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 2 mg/mL 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details '2 mg/mL [AFLR]GpTx-1, 100% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 2 mg/mL 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_software_2 _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'structure calculation' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AvanceIII _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1D_1H_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1D 1H' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_2 save_ save_E._COSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name 'E. 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 . mM pH 3.5 0.5 pH pressure 1 . Pa temperature 298 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0 . mM pH 3.5 0.5 pH pressure 1 . Pa temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 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_assigned_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1D 1H' '2D 1H-1H TOCSY' '2D 1H-1H NOESY' '2D 1H-15N HSQC' '2D 1H-13C HSQC' 'E. COSY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name entity_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 1 ASP HA H 4.396 0.004 . 2 1 1 ASP HB2 H 2.823 0.006 . 3 1 1 ASP HB3 H 2.932 0.001 . 4 1 1 ASP CA C 52.849 0.000 . 5 1 1 ASP CB C 39.224 0.012 . 6 2 2 CYS H H 8.687 0.002 . 7 2 2 CYS HA H 4.975 0.004 . 8 2 2 CYS HB2 H 3.197 0.002 . 9 2 2 CYS HB3 H 3.329 0.002 . 10 2 2 CYS CA C 54.631 0.000 . 11 2 2 CYS CB C 44.070 0.023 . 12 2 2 CYS N N 116.923 0.000 . 13 3 3 LEU H H 8.676 0.003 . 14 3 3 LEU HA H 4.307 0.002 . 15 3 3 LEU HB2 H 1.358 0.003 . 16 3 3 LEU HB3 H 1.777 0.003 . 17 3 3 LEU HG H 1.566 0.003 . 18 3 3 LEU HD1 H 0.944 0.003 . 19 3 3 LEU HD2 H 0.843 0.003 . 20 3 3 LEU CA C 54.512 0.000 . 21 3 3 LEU CB C 44.804 0.000 . 22 3 3 LEU CG C 26.130 0.000 . 23 3 3 LEU CD1 C 26.247 0.000 . 24 3 3 LEU CD2 C 22.207 0.000 . 25 3 3 LEU N N 120.093 0.000 . 26 4 4 GLY H H 7.990 0.003 . 27 4 4 GLY HA2 H 4.044 0.002 . 28 4 4 GLY HA3 H 3.590 0.003 . 29 4 4 GLY CA C 42.863 0.025 . 30 4 4 GLY N N 107.119 0.000 . 31 5 5 ALA H H 8.021 0.002 . 32 5 5 ALA HA H 3.176 0.003 . 33 5 5 ALA HB H 0.884 0.003 . 34 5 5 ALA CA C 53.877 0.000 . 35 5 5 ALA CB C 17.727 0.000 . 36 5 5 ALA N N 119.137 0.000 . 37 6 6 PHE H H 8.965 0.002 . 38 6 6 PHE HA H 3.509 0.003 . 39 6 6 PHE HB2 H 2.845 0.002 . 40 6 6 PHE HB3 H 3.051 0.004 . 41 6 6 PHE HD1 H 6.296 0.002 . 42 6 6 PHE HD2 H 6.296 0.002 . 43 6 6 PHE HE1 H 7.233 0.003 . 44 6 6 PHE HE2 H 7.233 0.003 . 45 6 6 PHE CA C 59.975 0.000 . 46 6 6 PHE CB C 35.534 0.013 . 47 6 6 PHE N N 113.846 0.000 . 48 7 7 ARG H H 7.580 0.002 . 49 7 7 ARG HA H 4.438 0.001 . 50 7 7 ARG HB2 H 1.895 0.005 . 51 7 7 ARG HB3 H 1.971 0.007 . 52 7 7 ARG HG2 H 1.463 0.003 . 53 7 7 ARG HG3 H 1.756 0.002 . 54 7 7 ARG HD2 H 3.227 0.006 . 55 7 7 ARG HD3 H 3.227 0.006 . 56 7 7 ARG HE H 7.280 0.004 . 57 7 7 ARG CA C 54.385 0.000 . 58 7 7 ARG CB C 30.234 0.012 . 59 7 7 ARG CG C 26.786 0.012 . 60 7 7 ARG CD C 42.808 0.000 . 61 7 7 ARG N N 119.927 0.000 . 62 8 8 LYS H H 8.544 0.002 . 63 8 8 LYS HA H 4.821 0.004 . 64 8 8 LYS HB2 H 1.930 0.003 . 65 8 8 LYS HB3 H 1.930 0.003 . 66 8 8 LYS HG2 H 1.679 0.002 . 67 8 8 LYS HG3 H 1.819 0.003 . 68 8 8 LYS HE2 H 3.164 0.000 . 69 8 8 LYS HE3 H 3.164 0.000 . 70 8 8 LYS HZ H 7.652 0.004 . 71 8 8 LYS CA C 57.169 0.000 . 72 8 8 LYS CB C 32.082 0.000 . 73 8 8 LYS CG C 24.876 0.015 . 74 8 8 LYS CD C 28.872 0.000 . 75 8 8 LYS N N 121.770 0.000 . 76 8 8 LYS NZ N 124.166 0.000 . 77 9 9 CYS H H 8.215 0.002 . 78 9 9 CYS HA H 4.903 0.003 . 79 9 9 CYS HB2 H 2.928 0.003 . 80 9 9 CYS HB3 H 3.096 0.004 . 81 9 9 CYS CA C 53.491 0.000 . 82 9 9 CYS CB C 46.344 0.000 . 83 9 9 CYS N N 118.699 0.000 . 84 10 10 ILE H H 9.003 0.003 . 85 10 10 ILE HA H 4.506 0.003 . 86 10 10 ILE HB H 1.871 0.003 . 87 10 10 ILE HG12 H 1.129 0.004 . 88 10 10 ILE HG13 H 1.548 0.001 . 89 10 10 ILE HD1 H 0.891 0.001 . 90 10 10 ILE CA C 57.086 0.000 . 91 10 10 ILE CB C 39.104 0.000 . 92 10 10 ILE CG1 C 26.862 0.000 . 93 10 10 ILE CD1 C 20.928 0.000 . 94 10 10 ILE N N 122.753 0.000 . 95 11 11 PRO HA H 3.697 0.003 . 96 11 11 PRO HB2 H 1.920 0.003 . 97 11 11 PRO HB3 H 2.113 0.001 . 98 11 11 PRO HG2 H 1.756 0.003 . 99 11 11 PRO HG3 H 2.107 0.005 . 100 11 11 PRO HD2 H 3.854 0.008 . 101 11 11 PRO HD3 H 3.905 0.007 . 102 11 11 PRO CA C 66.350 0.000 . 103 11 11 PRO CB C 31.700 0.017 . 104 11 11 PRO CG C 27.975 0.034 . 105 11 11 PRO CD C 50.596 0.019 . 106 12 12 ASP H H 8.075 0.001 . 107 12 12 ASP HA H 4.686 0.004 . 108 12 12 ASP HB2 H 2.734 0.004 . 109 12 12 ASP HB3 H 2.858 0.002 . 110 12 12 ASP CA C 53.453 0.000 . 111 12 12 ASP CB C 38.526 0.000 . 112 12 12 ASP N N 111.205 0.000 . 113 13 13 ASN H H 7.738 0.002 . 114 13 13 ASN HA H 4.724 0.001 . 115 13 13 ASN HB2 H 2.654 0.006 . 116 13 13 ASN HB3 H 2.539 0.004 . 117 13 13 ASN HD21 H 7.353 0.001 . 118 13 13 ASN HD22 H 6.796 0.001 . 119 13 13 ASN CA C 52.526 0.000 . 120 13 13 ASN CB C 37.308 0.015 . 121 13 13 ASN N N 120.741 0.000 . 122 13 13 ASN ND2 N 109.700 0.000 . 123 14 14 ASP H H 8.408 0.002 . 124 14 14 ASP HA H 4.174 0.003 . 125 14 14 ASP HB2 H 2.751 0.004 . 126 14 14 ASP HB3 H 3.006 0.003 . 127 14 14 ASP CA C 55.245 0.000 . 128 14 14 ASP CB C 41.610 0.015 . 129 14 14 ASP N N 122.776 0.000 . 130 15 15 LYS H H 8.095 0.004 . 131 15 15 LYS HA H 4.669 0.004 . 132 15 15 LYS HB2 H 1.624 0.004 . 133 15 15 LYS HB3 H 2.393 0.004 . 134 15 15 LYS HG2 H 1.400 0.002 . 135 15 15 LYS HG3 H 1.502 0.003 . 136 15 15 LYS HE2 H 2.861 0.000 . 137 15 15 LYS HE3 H 2.944 0.000 . 138 15 15 LYS HZ H 7.481 0.000 . 139 15 15 LYS CA C 54.194 0.000 . 140 15 15 LYS CB C 31.257 0.026 . 141 15 15 LYS CG C 24.448 0.026 . 142 15 15 LYS CE C 42.069 0.000 . 143 15 15 LYS N N 127.209 0.000 . 144 15 15 LYS NZ N 108.545 0.000 . 145 16 16 CYS H H 9.221 0.002 . 146 16 16 CYS HA H 4.935 0.004 . 147 16 16 CYS HB2 H 2.618 0.002 . 148 16 16 CYS HB3 H 2.618 0.002 . 149 16 16 CYS CA C 56.409 0.000 . 150 16 16 CYS CB C 38.483 0.000 . 151 16 16 CYS N N 122.131 0.000 . 152 17 17 CYS H H 9.303 0.002 . 153 17 17 CYS HA H 4.429 0.001 . 154 17 17 CYS HB2 H 2.718 0.002 . 155 17 17 CYS HB3 H 3.172 0.006 . 156 17 17 CYS CA C 56.085 0.000 . 157 17 17 CYS CB C 41.794 0.012 . 158 17 17 CYS N N 122.222 0.000 . 159 18 18 ARG H H 8.769 0.002 . 160 18 18 ARG HA H 4.370 0.004 . 161 18 18 ARG HB2 H 1.834 0.000 . 162 18 18 ARG HB3 H 1.967 0.008 . 163 18 18 ARG HD2 H 3.169 0.001 . 164 18 18 ARG HD3 H 3.284 0.001 . 165 18 18 ARG HE H 7.159 0.004 . 166 18 18 ARG CA C 57.418 0.000 . 167 18 18 ARG CB C 27.514 0.012 . 168 18 18 ARG CD C 42.713 0.000 . 169 18 18 ARG N N 125.867 0.000 . 170 19 19 PRO HA H 4.567 0.003 . 171 19 19 PRO HB2 H 2.271 0.003 . 172 19 19 PRO HB3 H 2.351 0.003 . 173 19 19 PRO HG2 H 1.763 0.002 . 174 19 19 PRO HG3 H 2.027 0.002 . 175 19 19 PRO HD2 H 3.571 0.002 . 176 19 19 PRO HD3 H 3.571 0.002 . 177 19 19 PRO CA C 63.636 0.000 . 178 19 19 PRO CB C 34.908 0.023 . 179 19 19 PRO CG C 23.836 0.012 . 180 19 19 PRO CD C 50.113 0.000 . 181 20 20 ASN H H 8.449 0.002 . 182 20 20 ASN HA H 4.805 0.009 . 183 20 20 ASN HB2 H 2.917 0.002 . 184 20 20 ASN HB3 H 3.019 0.003 . 185 20 20 ASN HD21 H 7.610 0.001 . 186 20 20 ASN HD22 H 7.117 0.004 . 187 20 20 ASN CA C 55.731 0.000 . 188 20 20 ASN CB C 39.165 0.007 . 189 20 20 ASN N N 118.938 0.000 . 190 20 20 ASN ND2 N 112.576 0.023 . 191 21 21 LEU H H 7.785 0.002 . 192 21 21 LEU HA H 5.434 0.002 . 193 21 21 LEU HB2 H 0.779 0.002 . 194 21 21 LEU HB3 H 2.155 0.003 . 195 21 21 LEU HG H 1.294 0.002 . 196 21 21 LEU HD2 H 0.014 0.002 . 197 21 21 LEU CA C 53.258 0.000 . 198 21 21 LEU CB C 46.275 0.013 . 199 21 21 LEU CG C 26.564 0.000 . 200 21 21 LEU CD2 C 23.719 0.000 . 201 21 21 LEU N N 118.092 0.000 . 202 22 22 VAL H H 8.619 0.002 . 203 22 22 VAL HA H 4.259 0.002 . 204 22 22 VAL HB H 1.836 0.001 . 205 22 22 VAL HG1 H 0.891 0.002 . 206 22 22 VAL HG2 H 0.706 0.003 . 207 22 22 VAL CA C 59.615 0.000 . 208 22 22 VAL CB C 30.215 0.000 . 209 22 22 VAL CG2 C 20.140 0.000 . 210 22 22 VAL N N 115.266 0.000 . 211 23 23 CYS H H 9.490 0.002 . 212 23 23 CYS HA H 4.584 0.002 . 213 23 23 CYS HB2 H 2.593 0.003 . 214 23 23 CYS HB3 H 3.146 0.002 . 215 23 23 CYS CA C 56.021 0.000 . 216 23 23 CYS CB C 37.735 0.014 . 217 23 23 CYS N N 125.591 0.000 . 218 24 24 SER H H 8.277 0.001 . 219 24 24 SER HA H 4.378 0.006 . 220 24 24 SER HB2 H 3.825 0.003 . 221 24 24 SER HB3 H 4.021 0.004 . 222 24 24 SER CA C 53.477 0.000 . 223 24 24 SER CB C 63.680 0.014 . 224 24 24 SER N N 123.472 0.000 . 225 25 25 ARG H H 9.007 0.002 . 226 25 25 ARG HA H 3.815 0.003 . 227 25 25 ARG HB2 H 1.814 0.002 . 228 25 25 ARG HB3 H 1.814 0.002 . 229 25 25 ARG HG2 H 1.570 0.005 . 230 25 25 ARG HG3 H 1.706 0.001 . 231 25 25 ARG HD2 H 3.204 0.004 . 232 25 25 ARG HD3 H 3.204 0.004 . 233 25 25 ARG HE H 7.306 0.003 . 234 25 25 ARG CA C 59.263 0.000 . 235 25 25 ARG CB C 29.621 0.000 . 236 25 25 ARG CG C 28.492 0.000 . 237 25 25 ARG CD C 43.642 0.000 . 238 25 25 ARG N N 131.161 0.000 . 239 26 26 LEU H H 7.491 0.005 . 240 26 26 LEU HA H 4.053 0.002 . 241 26 26 LEU HB2 H 0.948 0.000 . 242 26 26 LEU HB3 H 1.267 0.002 . 243 26 26 LEU HG H 0.794 0.008 . 244 26 26 LEU HD1 H 0.748 0.002 . 245 26 26 LEU HD2 H 0.629 0.002 . 246 26 26 LEU CA C 56.444 0.000 . 247 26 26 LEU CB C 42.816 0.000 . 248 26 26 LEU CG C 26.870 0.000 . 249 26 26 LEU CD1 C 23.230 0.000 . 250 26 26 LEU CD2 C 24.302 0.000 . 251 26 26 LEU N N 116.760 0.000 . 252 27 27 HIS H H 7.419 0.002 . 253 27 27 HIS HA H 4.195 0.001 . 254 27 27 HIS HB2 H 1.044 0.003 . 255 27 27 HIS HB3 H 1.227 0.004 . 256 27 27 HIS HD2 H 6.991 0.003 . 257 27 27 HIS HE1 H 8.658 0.001 . 258 27 27 HIS CA C 54.585 0.000 . 259 27 27 HIS CB C 27.167 0.014 . 260 27 27 HIS N N 111.299 0.000 . 261 28 28 ARG H H 8.200 0.003 . 262 28 28 ARG HA H 3.768 0.004 . 263 28 28 ARG HB2 H 1.284 0.002 . 264 28 28 ARG HB3 H 1.448 0.005 . 265 28 28 ARG HG2 H 2.032 0.001 . 266 28 28 ARG HG3 H 2.356 0.002 . 267 28 28 ARG HD2 H 3.215 0.002 . 268 28 28 ARG HD3 H 3.215 0.002 . 269 28 28 ARG HE H 7.300 0.004 . 270 28 28 ARG CA C 57.407 0.000 . 271 28 28 ARG CB C 28.282 0.000 . 272 28 28 ARG CG C 26.207 0.014 . 273 28 28 ARG N N 114.938 0.000 . 274 29 29 TRP H H 6.784 0.004 . 275 29 29 TRP HA H 5.733 0.003 . 276 29 29 TRP HB2 H 3.224 0.004 . 277 29 29 TRP HB3 H 2.713 0.005 . 278 29 29 TRP HD1 H 6.842 0.003 . 279 29 29 TRP HE1 H 10.551 0.003 . 280 29 29 TRP HE3 H 7.577 0.000 . 281 29 29 TRP HZ2 H 7.004 0.002 . 282 29 29 TRP HZ3 H 7.576 0.002 . 283 29 29 TRP HH2 H 7.188 0.005 . 284 29 29 TRP CA C 54.672 0.000 . 285 29 29 TRP CB C 31.002 0.030 . 286 29 29 TRP N N 110.709 0.000 . 287 29 29 TRP NE1 N 129.424 0.000 . 288 30 30 CYS H H 8.665 0.017 . 289 30 30 CYS HA H 4.930 0.004 . 290 30 30 CYS HB2 H 2.493 0.002 . 291 30 30 CYS HB3 H 3.168 0.002 . 292 30 30 CYS CA C 54.697 0.000 . 293 30 30 CYS CB C 39.085 0.012 . 294 30 30 CYS N N 121.565 0.000 . 295 31 31 LYS H H 9.665 0.002 . 296 31 31 LYS HA H 4.697 0.003 . 297 31 31 LYS HB2 H 1.831 0.004 . 298 31 31 LYS HB3 H 2.102 0.003 . 299 31 31 LYS HG2 H 1.399 0.002 . 300 31 31 LYS HG3 H 1.614 0.004 . 301 31 31 LYS HD2 H 1.756 0.002 . 302 31 31 LYS HD3 H 1.756 0.002 . 303 31 31 LYS CA C 53.376 0.000 . 304 31 31 LYS CB C 35.776 0.031 . 305 31 31 LYS CG C 23.651 0.008 . 306 31 31 LYS CD C 29.381 0.000 . 307 31 31 LYS N N 126.467 0.000 . 308 32 32 TYR H H 7.987 0.003 . 309 32 32 TYR HA H 4.855 0.005 . 310 32 32 TYR HB2 H 2.976 0.005 . 311 32 32 TYR HB3 H 2.725 0.003 . 312 32 32 TYR HD1 H 7.178 0.004 . 313 32 32 TYR HD2 H 7.178 0.004 . 314 32 32 TYR HE1 H 6.767 0.002 . 315 32 32 TYR HE2 H 6.767 0.002 . 316 32 32 TYR CA C 58.832 0.000 . 317 32 32 TYR CB C 38.459 0.010 . 318 32 32 TYR N N 120.184 0.000 . 319 33 33 VAL H H 8.374 0.001 . 320 33 33 VAL HA H 3.834 0.003 . 321 33 33 VAL HB H 1.874 0.002 . 322 33 33 VAL HG1 H 0.804 0.001 . 323 33 33 VAL HG2 H 0.675 0.001 . 324 33 33 VAL CA C 63.504 0.000 . 325 33 33 VAL CB C 32.933 0.000 . 326 33 33 VAL CG1 C 21.072 0.000 . 327 33 33 VAL CG2 C 21.092 0.000 . 328 33 33 VAL N N 122.844 0.000 . 329 34 34 PHE H H 8.024 0.001 . 330 34 34 PHE HA H 4.735 0.001 . 331 34 34 PHE HB2 H 3.003 0.006 . 332 34 34 PHE HB3 H 3.218 0.006 . 333 34 34 PHE HD1 H 7.326 0.003 . 334 34 34 PHE HD2 H 7.326 0.003 . 335 34 34 PHE CA C 56.554 0.000 . 336 34 34 PHE CB C 39.780 0.024 . 337 34 34 PHE N N 120.725 0.000 . stop_ save_