data_25835 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of OtTx1a - AMP in DPC micelles ; _BMRB_accession_number 25835 _BMRB_flat_file_name bmr25835.str _Entry_type original _Submission_date 2015-10-05 _Accession_date 2015-10-05 _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 Nadezhdin Kirill . . 2 Romanovskaya Daria . . 3 Sachkova Maria . . 4 Vassilevski Alexander . . 5 Grishin Evgeny . . 6 Kovalchuk Sergey . . 7 Arseniev Alexander . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 287 "13C chemical shifts" 125 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-09-29 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 25836 'OtTx1a - ICK' stop_ _Original_release_date 2016-09-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR structure of OtTx1a - AMP in DPC micelles ; _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 Nadezhdin Kirill . . 2 Romanovskaya Daria . . 3 Sachkova Maria . . 4 Vassilevski Alexander . . 5 Grishin Evgeny . . 6 Kovalchuk Sergey . . 7 Arseniev Alexander . . stop_ _Journal_abbreviation 'Not known' _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 'OtTx1a - AMP in DPC micelles' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $entity 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_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 4832.061 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 41 _Mol_residue_sequence ; KFKWGKLFSTAKKLYKKGKK LSKNKNFKKALKFGKQLAKN L ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 LYS 2 2 PHE 3 3 LYS 4 4 TRP 5 5 GLY 6 6 LYS 7 7 LEU 8 8 PHE 9 9 SER 10 10 THR 11 11 ALA 12 12 LYS 13 13 LYS 14 14 LEU 15 15 TYR 16 16 LYS 17 17 LYS 18 18 GLY 19 19 LYS 20 20 LYS 21 21 LEU 22 22 SER 23 23 LYS 24 24 ASN 25 25 LYS 26 26 ASN 27 27 PHE 28 28 LYS 29 29 LYS 30 30 ALA 31 31 LEU 32 32 LYS 33 33 PHE 34 34 GLY 35 35 LYS 36 36 GLN 37 37 LEU 38 38 ALA 39 39 LYS 40 40 ASN 41 41 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 UNP P86716 SPN1A_OXYTA . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $entity spiders 666126 Eukaryota Metazoa Oxyopes Takobius 'spider 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 $entity 'chemical synthesis' . . . . none stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type micelle _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 0.6 mM 'natural abundance' DPC 60 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Molmol _Saveframe_category software _Name Molmol _Version . loop_ _Vendor _Address _Electronic_address 'Koradi, Billeter and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_TALOS _Saveframe_category software _Name TALOS _Version . loop_ _Vendor _Address _Electronic_address 'Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task 'angle prediction' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection 'data analysis' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-13C_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.3 . 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 C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 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 '2D 1H-13C HSQC' '2D 1H-1H TOCSY' '2D 1H-1H NOESY' 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 entity _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 LYS HA H 4.049 . . 2 1 1 LYS HB2 H 1.894 . . 3 1 1 LYS HB3 H 1.457 . . 4 1 1 LYS HD2 H 1.723 . . 5 1 1 LYS HD3 H 1.723 . . 6 1 1 LYS HE2 H 2.960 . . 7 1 1 LYS HE3 H 3.028 . . 8 1 1 LYS H H 9.104 . . 9 1 1 LYS CA C 54.588 . . 10 2 2 PHE H H 9.104 . . 11 2 2 PHE HA H 4.353 . . 12 2 2 PHE HB2 H 2.785 . . 13 2 2 PHE HB3 H 2.445 . . 14 2 2 PHE HD1 H 6.612 . . 15 2 2 PHE HD2 H 6.612 . . 16 2 2 PHE HE1 H 6.774 . . 17 2 2 PHE HE2 H 6.774 . . 18 2 2 PHE CA C 57.364 . . 19 2 2 PHE CB C 38.971 . . 20 3 3 LYS H H 7.826 . . 21 3 3 LYS HA H 4.325 . . 22 3 3 LYS HB2 H 1.505 . . 23 3 3 LYS HB3 H 1.585 . . 24 3 3 LYS HG2 H 1.340 . . 25 3 3 LYS HG3 H 1.340 . . 26 3 3 LYS HD2 H 1.683 . . 27 3 3 LYS HD3 H 1.683 . . 28 3 3 LYS CA C 54.103 . . 29 3 3 LYS CB C 30.844 . . 30 3 3 LYS CG C 24.636 . . 31 3 3 LYS CD C 28.197 . . 32 4 4 TRP H H 7.838 . . 33 4 4 TRP HA H 4.201 . . 34 4 4 TRP HB2 H 3.238 . . 35 4 4 TRP HB3 H 3.061 . . 36 4 4 TRP HD1 H 7.441 . . 37 4 4 TRP HE3 H 7.479 . . 38 4 4 TRP HZ2 H 6.954 . . 39 4 4 TRP HZ3 H 6.885 . . 40 4 4 TRP HH2 H 7.382 . . 41 4 4 TRP CA C 58.893 . . 42 4 4 TRP CB C 28.804 . . 43 5 5 GLY H H 8.877 . . 44 5 5 GLY HA2 H 3.992 . . 45 5 5 GLY HA3 H 3.827 . . 46 5 5 GLY CA C 46.488 . . 47 6 6 LYS H H 7.740 . . 48 6 6 LYS HA H 4.300 . . 49 6 6 LYS HB2 H 1.854 . . 50 6 6 LYS HB3 H 1.854 . . 51 6 6 LYS HG2 H 1.427 . . 52 6 6 LYS HG3 H 1.427 . . 53 6 6 LYS HD2 H 1.675 . . 54 6 6 LYS HD3 H 1.675 . . 55 6 6 LYS CA C 57.358 . . 56 6 6 LYS CB C 31.401 . . 57 6 6 LYS CG C 24.025 . . 58 6 6 LYS CD C 28.661 . . 59 7 7 LEU H H 7.839 . . 60 7 7 LEU HA H 4.154 . . 61 7 7 LEU HB2 H 1.933 . . 62 7 7 LEU HB3 H 1.842 . . 63 7 7 LEU HG H 1.768 . . 64 7 7 LEU HD1 H 0.994 . . 65 7 7 LEU HD2 H 0.994 . . 66 7 7 LEU CA C 57.363 . . 67 7 7 LEU CB C 40.803 . . 68 7 7 LEU CG C 26.848 . . 69 7 7 LEU CD1 C 24.168 . . 70 8 8 PHE H H 8.404 . . 71 8 8 PHE HA H 4.357 . . 72 8 8 PHE HB2 H 3.290 . . 73 8 8 PHE HB3 H 3.290 . . 74 8 8 PHE HD1 H 7.284 . . 75 8 8 PHE HD2 H 7.284 . . 76 8 8 PHE CA C 59.586 . . 77 8 8 PHE CB C 37.549 . . 78 9 9 SER H H 8.415 . . 79 9 9 SER HA H 4.083 . . 80 9 9 SER HB2 H 4.050 . . 81 9 9 SER HB3 H 4.024 . . 82 9 9 SER CA C 61.080 . . 83 9 9 SER CB C 61.641 . . 84 10 10 THR H H 8.018 . . 85 10 10 THR HA H 3.917 . . 86 10 10 THR HB H 4.283 . . 87 10 10 THR HG2 H 1.235 . . 88 10 10 THR CA C 66.484 . . 89 10 10 THR CB C 67.412 . . 90 10 10 THR CG2 C 21.005 . . 91 11 11 ALA H H 8.542 . . 92 11 11 ALA HA H 3.934 . . 93 11 11 ALA HB H 1.514 . . 94 11 11 ALA CA C 55.007 . . 95 11 11 ALA CB C 17.260 . . 96 12 12 LYS H H 8.133 . . 97 12 12 LYS HA H 3.881 . . 98 12 12 LYS HB2 H 1.837 . . 99 12 12 LYS HB3 H 1.764 . . 100 12 12 LYS HG2 H 1.441 . . 101 12 12 LYS HG3 H 1.290 . . 102 12 12 LYS HD2 H 1.621 . . 103 12 12 LYS HD3 H 1.621 . . 104 12 12 LYS HE2 H 2.754 . . 105 12 12 LYS HE3 H 2.699 . . 106 12 12 LYS CA C 59.642 . . 107 12 12 LYS CB C 31.467 . . 108 12 12 LYS CG C 24.835 . . 109 12 12 LYS CD C 28.203 . . 110 12 12 LYS CE C 40.896 . . 111 13 13 LYS H H 7.631 . . 112 13 13 LYS HA H 4.031 . . 113 13 13 LYS HB2 H 2.054 . . 114 13 13 LYS HB3 H 1.938 . . 115 13 13 LYS HG2 H 1.464 . . 116 13 13 LYS HG3 H 1.464 . . 117 13 13 LYS HD2 H 1.672 . . 118 13 13 LYS HD3 H 1.672 . . 119 13 13 LYS CA C 58.983 . . 120 13 13 LYS CB C 31.582 . . 121 13 13 LYS CG C 23.126 . . 122 13 13 LYS CD C 28.270 . . 123 14 14 LEU H H 8.232 . . 124 14 14 LEU HA H 4.017 . . 125 14 14 LEU HB2 H 1.954 . . 126 14 14 LEU HB3 H 1.494 . . 127 14 14 LEU HG H 1.894 . . 128 14 14 LEU HD1 H 0.868 . . 129 14 14 LEU HD2 H 0.858 . . 130 14 14 LEU CA C 56.984 . . 131 14 14 LEU CB C 40.832 . . 132 14 14 LEU CG C 25.972 . . 133 14 14 LEU CD1 C 24.799 . . 134 14 14 LEU CD2 C 22.490 . . 135 15 15 TYR H H 8.489 . . 136 15 15 TYR HA H 4.070 . . 137 15 15 TYR HB2 H 3.195 . . 138 15 15 TYR HB3 H 3.062 . . 139 15 15 TYR HD1 H 6.751 . . 140 15 15 TYR HD2 H 6.751 . . 141 15 15 TYR HE1 H 6.925 . . 142 15 15 TYR HE2 H 6.925 . . 143 15 15 TYR HH H 7.286 . . 144 15 15 TYR CA C 60.638 . . 145 15 15 TYR CB C 37.784 . . 146 16 16 LYS H H 7.959 . . 147 16 16 LYS HA H 3.693 . . 148 16 16 LYS HB2 H 1.954 . . 149 16 16 LYS HB3 H 1.883 . . 150 16 16 LYS HG2 H 1.481 . . 151 16 16 LYS HG3 H 1.481 . . 152 16 16 LYS HD2 H 1.715 . . 153 16 16 LYS HD3 H 1.715 . . 154 16 16 LYS CA C 58.894 . . 155 16 16 LYS CB C 31.410 . . 156 16 16 LYS CG C 24.251 . . 157 16 16 LYS CD C 28.347 . . 158 17 17 LYS H H 7.862 . . 159 17 17 LYS HA H 4.075 . . 160 17 17 LYS HB2 H 1.951 . . 161 17 17 LYS HB3 H 1.851 . . 162 17 17 LYS HG2 H 1.432 . . 163 17 17 LYS HG3 H 1.432 . . 164 17 17 LYS HD2 H 1.669 . . 165 17 17 LYS HD3 H 1.669 . . 166 17 17 LYS CA C 57.774 . . 167 17 17 LYS CB C 31.147 . . 168 17 17 LYS CG C 24.028 . . 169 17 17 LYS CD C 28.309 . . 170 18 18 GLY H H 8.651 . . 171 18 18 GLY HA2 H 3.649 . . 172 18 18 GLY HA3 H 3.528 . . 173 18 18 GLY CA C 46.154 . . 174 19 19 LYS H H 8.271 . . 175 19 19 LYS HA H 3.785 . . 176 19 19 LYS HB2 H 1.657 . . 177 19 19 LYS HB3 H 1.597 . . 178 19 19 LYS HG2 H 1.235 . . 179 19 19 LYS HG3 H 1.209 . . 180 19 19 LYS HD2 H 1.527 . . 181 19 19 LYS HD3 H 1.527 . . 182 19 19 LYS HE2 H 2.820 . . 183 19 19 LYS HE3 H 2.820 . . 184 19 19 LYS CA C 58.338 . . 185 19 19 LYS CB C 30.830 . . 186 19 19 LYS CG C 23.776 . . 187 19 19 LYS CD C 28.182 . . 188 20 20 LYS H H 7.559 . . 189 20 20 LYS HA H 4.050 . . 190 20 20 LYS HB2 H 1.906 . . 191 20 20 LYS HB3 H 1.872 . . 192 20 20 LYS HG2 H 1.336 . . 193 20 20 LYS HG3 H 1.336 . . 194 20 20 LYS HD2 H 1.737 . . 195 20 20 LYS HD3 H 1.737 . . 196 20 20 LYS CA C 57.838 . . 197 20 20 LYS CB C 32.276 . . 198 20 20 LYS CG C 23.648 . . 199 20 20 LYS CD C 28.217 . . 200 21 21 LEU H H 7.925 . . 201 21 21 LEU HA H 4.086 . . 202 21 21 LEU HB2 H 1.713 . . 203 21 21 LEU HB3 H 1.400 . . 204 21 21 LEU HG H 1.692 . . 205 21 21 LEU HD1 H 0.843 . . 206 21 21 LEU HD2 H 0.826 . . 207 21 21 LEU CA C 55.837 . . 208 21 21 LEU CB C 41.056 . . 209 21 21 LEU CG C 25.947 . . 210 21 21 LEU CD1 C 24.521 . . 211 21 21 LEU CD2 C 22.792 . . 212 22 22 SER H H 7.693 . . 213 22 22 SER HA H 3.621 . . 214 22 22 SER HB2 H 3.749 . . 215 22 22 SER HB3 H 3.649 . . 216 22 22 SER CA C 59.577 . . 217 22 22 SER CB C 62.318 . . 218 23 23 LYS H H 7.301 . . 219 23 23 LYS HA H 4.264 . . 220 23 23 LYS HB2 H 1.948 . . 221 23 23 LYS HB3 H 1.761 . . 222 23 23 LYS HG2 H 1.477 . . 223 23 23 LYS HG3 H 1.407 . . 224 23 23 LYS HD2 H 1.642 . . 225 23 23 LYS HD3 H 1.629 . . 226 23 23 LYS CA C 55.364 . . 227 23 23 LYS CB C 31.593 . . 228 23 23 LYS CG C 24.169 . . 229 23 23 LYS CD C 28.724 . . 230 24 24 ASN H H 8.064 . . 231 24 24 ASN HA H 4.616 . . 232 24 24 ASN HB2 H 2.997 . . 233 24 24 ASN HB3 H 2.905 . . 234 24 24 ASN HD21 H 7.370 . . 235 24 24 ASN HD22 H 7.847 . . 236 24 24 ASN CB C 39.031 . . 237 25 25 LYS H H 8.776 . . 238 25 25 LYS HA H 4.124 . . 239 25 25 LYS HB2 H 1.841 . . 240 25 25 LYS HB3 H 1.772 . . 241 25 25 LYS HG2 H 1.430 . . 242 25 25 LYS HG3 H 1.430 . . 243 25 25 LYS HD2 H 1.677 . . 244 25 25 LYS HD3 H 1.677 . . 245 25 25 LYS CA C 57.639 . . 246 25 25 LYS CB C 31.461 . . 247 25 25 LYS CG C 23.812 . . 248 25 25 LYS CD C 28.525 . . 249 26 26 ASN H H 8.638 . . 250 26 26 ASN HA H 4.729 . . 251 26 26 ASN HB2 H 2.877 . . 252 26 26 ASN HB3 H 2.717 . . 253 26 26 ASN HD21 H 7.092 . . 254 26 26 ASN HD22 H 7.813 . . 255 26 26 ASN CB C 37.573 . . 256 27 27 PHE H H 8.384 . . 257 27 27 PHE HA H 4.218 . . 258 27 27 PHE HB2 H 3.333 . . 259 27 27 PHE HB3 H 3.147 . . 260 27 27 PHE HD1 H 7.141 . . 261 27 27 PHE HD2 H 7.141 . . 262 27 27 PHE HE1 H 7.183 . . 263 27 27 PHE HE2 H 7.183 . . 264 27 27 PHE HZ H 7.098 . . 265 27 27 PHE CA C 60.324 . . 266 27 27 PHE CB C 38.388 . . 267 28 28 LYS H H 8.193 . . 268 28 28 LYS HA H 3.827 . . 269 28 28 LYS HB2 H 1.948 . . 270 28 28 LYS HB3 H 1.864 . . 271 28 28 LYS HG2 H 1.477 . . 272 28 28 LYS HG3 H 1.477 . . 273 28 28 LYS HD2 H 1.727 . . 274 28 28 LYS HD3 H 1.727 . . 275 28 28 LYS HE2 H 3.009 . . 276 28 28 LYS HE3 H 3.009 . . 277 28 28 LYS CA C 59.201 . . 278 28 28 LYS CB C 31.714 . . 279 28 28 LYS CG C 24.735 . . 280 28 28 LYS CD C 28.283 . . 281 29 29 LYS H H 7.824 . . 282 29 29 LYS HA H 3.993 . . 283 29 29 LYS HB2 H 1.932 . . 284 29 29 LYS HB3 H 1.856 . . 285 29 29 LYS HG2 H 1.725 . . 286 29 29 LYS HG3 H 1.725 . . 287 29 29 LYS HD2 H 1.576 . . 288 29 29 LYS HD3 H 1.576 . . 289 29 29 LYS HE2 H 2.942 . . 290 29 29 LYS HE3 H 2.942 . . 291 29 29 LYS CA C 58.571 . . 292 29 29 LYS CB C 31.191 . . 293 29 29 LYS CG C 24.759 . . 294 29 29 LYS CD C 28.261 . . 295 30 30 ALA H H 7.860 . . 296 30 30 ALA HA H 4.074 . . 297 30 30 ALA HB H 1.426 . . 298 30 30 ALA CA C 54.300 . . 299 30 30 ALA CB C 17.348 . . 300 31 31 LEU H H 7.932 . . 301 31 31 LEU HA H 3.970 . . 302 31 31 LEU HB2 H 1.477 . . 303 31 31 LEU HB3 H 1.688 . . 304 31 31 LEU HG H 1.530 . . 305 31 31 LEU HD1 H 0.779 . . 306 31 31 LEU HD2 H 0.778 . . 307 31 31 LEU CA C 56.494 . . 308 31 31 LEU CB C 41.107 . . 309 31 31 LEU CG C 25.848 . . 310 31 31 LEU CD1 C 23.080 . . 311 31 31 LEU CD2 C 24.388 . . 312 32 32 LYS H H 7.747 . . 313 32 32 LYS HA H 3.905 . . 314 32 32 LYS HB2 H 1.504 . . 315 32 32 LYS HB3 H 1.879 . . 316 32 32 LYS HG2 H 1.318 . . 317 32 32 LYS HG3 H 1.318 . . 318 32 32 LYS HD2 H 1.731 . . 319 32 32 LYS HD3 H 1.731 . . 320 32 32 LYS HE2 H 2.904 . . 321 32 32 LYS HE3 H 2.904 . . 322 32 32 LYS CA C 58.880 . . 323 32 32 LYS CB C 31.519 . . 324 32 32 LYS CG C 24.135 . . 325 32 32 LYS CD C 28.649 . . 326 33 33 PHE H H 7.981 . . 327 33 33 PHE HA H 4.389 . . 328 33 33 PHE HB2 H 3.216 . . 329 33 33 PHE HB3 H 3.154 . . 330 33 33 PHE HD1 H 7.216 . . 331 33 33 PHE HD2 H 7.216 . . 332 33 33 PHE HE1 H 7.278 . . 333 33 33 PHE HE2 H 7.278 . . 334 33 33 PHE CA C 59.657 . . 335 33 33 PHE CB C 38.310 . . 336 34 34 GLY H H 8.838 . . 337 34 34 GLY HA2 H 3.593 . . 338 34 34 GLY HA3 H 3.593 . . 339 34 34 GLY CA C 46.646 . . 340 35 35 LYS H H 8.331 . . 341 35 35 LYS HA H 3.861 . . 342 35 35 LYS HB2 H 1.864 . . 343 35 35 LYS HB3 H 1.595 . . 344 35 35 LYS HG2 H 1.372 . . 345 35 35 LYS HG3 H 1.372 . . 346 35 35 LYS HD2 H 1.681 . . 347 35 35 LYS HD3 H 1.681 . . 348 35 35 LYS HE2 H 2.873 . . 349 35 35 LYS HE3 H 2.873 . . 350 35 35 LYS CA C 59.239 . . 351 35 35 LYS CB C 30.845 . . 352 35 35 LYS CG C 25.053 . . 353 35 35 LYS CD C 28.695 . . 354 36 36 GLN H H 7.578 . . 355 36 36 GLN HA H 3.986 . . 356 36 36 GLN HB2 H 2.176 . . 357 36 36 GLN HB3 H 2.086 . . 358 36 36 GLN HG2 H 2.438 . . 359 36 36 GLN HG3 H 2.351 . . 360 36 36 GLN HE21 H 6.848 . . 361 36 36 GLN HE22 H 7.406 . . 362 36 36 GLN CA C 57.558 . . 363 36 36 GLN CB C 27.359 . . 364 36 36 GLN CG C 32.903 . . 365 37 37 LEU H H 7.993 . . 366 37 37 LEU HA H 3.892 . . 367 37 37 LEU HB2 H 1.550 . . 368 37 37 LEU HB3 H 1.550 . . 369 37 37 LEU HG H 1.580 . . 370 37 37 LEU HD1 H 0.793 . . 371 37 37 LEU HD2 H 0.816 . . 372 37 37 LEU CA C 57.057 . . 373 37 37 LEU CB C 40.606 . . 374 37 37 LEU CG C 24.568 . . 375 37 37 LEU CD1 C 23.192 . . 376 37 37 LEU CD2 C 23.964 . . 377 38 38 ALA H H 7.994 . . 378 38 38 ALA HA H 3.948 . . 379 38 38 ALA HB H 1.429 . . 380 38 38 ALA CA C 53.266 . . 381 38 38 ALA CB C 17.604 . . 382 39 39 LYS H H 7.355 . . 383 39 39 LYS HA H 4.044 . . 384 39 39 LYS HB2 H 1.871 . . 385 39 39 LYS HB3 H 1.871 . . 386 39 39 LYS HG2 H 1.512 . . 387 39 39 LYS HG3 H 1.512 . . 388 39 39 LYS HD2 H 1.670 . . 389 39 39 LYS HD3 H 1.670 . . 390 39 39 LYS CA C 57.467 . . 391 39 39 LYS CB C 32.274 . . 392 39 39 LYS CG C 23.750 . . 393 39 39 LYS CD C 28.297 . . 394 40 40 ASN H H 7.816 . . 395 40 40 ASN HA H 4.746 . . 396 40 40 ASN HB2 H 2.890 . . 397 40 40 ASN HB3 H 2.633 . . 398 40 40 ASN HD21 H 7.075 . . 399 40 40 ASN HD22 H 7.582 . . 400 40 40 ASN CB C 39.205 . . 401 41 41 LEU H H 7.472 . . 402 41 41 LEU HA H 4.279 . . 403 41 41 LEU HB2 H 1.799 . . 404 41 41 LEU HB3 H 1.580 . . 405 41 41 LEU HG H 1.816 . . 406 41 41 LEU HD1 H 0.852 . . 407 41 41 LEU HD2 H 0.894 . . 408 41 41 LEU CA C 53.251 . . 409 41 41 LEU CB C 41.284 . . 410 41 41 LEU CG C 26.001 . . 411 41 41 LEU CD1 C 22.559 . . 412 41 41 LEU CD2 C 24.799 . . stop_ save_