data_50153 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Isolation and characterization of antimicrobial peptides with unusual disulfide connectivity from the colonial ascidian Synoicum turgens [Turgencin B(Mox2)] ; _BMRB_accession_number 50153 _BMRB_flat_file_name bmr50153.str _Entry_type original _Submission_date 2020-01-09 _Accession_date 2020-01-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Crude structure calculation of the Turgencin B (Mox2) peptide in water. There is structural heterogeneity in the oxidation state and chirality of the oxidized methionines. There are also signs of fast conformational dynamics, so the helix folds are only partial. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hansen Ida K.O.e. . 2 Isaksson Johan . . 3 Poth Aaron G. . 4 Andersen Aaron J.C. . 5 Hansen Kine O.e. . 6 Richard Celine S. . 7 Blencke Hans-Matti . . 8 Stensvaag Klara . . 9 Craik David J. . 10 Tor Haug . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 185 "13C chemical shifts" 104 "15N chemical shifts" 35 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-06-09 original BMRB . stop_ _Original_release_date 2020-02-04 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Isolation and characterization of antimicrobial peptides with unusual disulfide connectivity from the colonial ascidian Synoicum turgens ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31940927 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hansen Ida . . 2 Isaksson Johan . . 3 Poth Aaron G. . 4 Hansen Kine o. . 5 Andersen Aaron . . 6 Richard Celine . . 7 Blencke Hans-Matti M. . 8 Stensvag Klara . . 9 Craik David J. . 10 Haug Tor . . stop_ _Journal_abbreviation 'Mar. Drugs' _Journal_volume 18 _Journal_issue 1 _Journal_ISSN 1660-3397 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2020 _Details . loop_ _Keyword 'marine; acidian; peptide; antimicrobial; methionine oxidation' stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'Turgencin B (Mox2)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Turgencin B (Mox2)' $entity_1 stop_ _System_molecular_weight 3575 _System_physical_state native _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 'Turgencin B (Mox2)' _Molecular_mass 3575 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 36 _Mol_residue_sequence ; GIKEMLCNMACAQTVCKKSG GPLCDTCQAACKALGX ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ILE 3 LYS 4 GLU 5 MET 6 LEU 7 CYS 8 ASN 9 MET 10 ALA 11 CYS 12 ALA 13 GLN 14 THR 15 VAL 16 CYS 17 LYS 18 LYS 19 SER 20 GLY 21 GLY 22 PRO 23 LEU 24 CYS 25 ASP 26 THR 27 CYS 28 GLN 29 ALA 30 ALA 31 CYS 32 LYS 33 ALA 34 LEU 35 GLY 36 NH2 stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 . 562744 Eukaryota Metazoa Synoicum turgens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $entity_1 'purified from the natural source' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 2 mg 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1_Bruker_Avance_III_HD _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'TCI cryoprobe - enhanced for 1H, 2H and 13C' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1_1 save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1_1 save_ save_2D_1H-1H_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1_1 save_ save_2D_1H-13C_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1_1 save_ save_2D_1H-1H_COSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H COSY' _Sample_label $sample_1_1 save_ save_2D_1H-13C_HMBC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HMBC' _Sample_label $sample_1_1 save_ save_2D_1H-13C_TOCSYHSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C TOCSYHSQC' _Sample_label $sample_1_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_1_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 water H 1 protons ppm 4.700 internal direct . . . 1 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1_1 stop_ _Sample_conditions_label $sample_conditions_1_1 _Chem_shift_reference_set_label $chem_shift_reference_1_1 _Mol_system_component_name 'Turgencin B (Mox2)' _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 GLY H H 7.631 . 1 2 1 1 GLY HA2 H 3.649 . 2 3 1 1 GLY HA3 H 3.771 . 2 4 1 1 GLY N N 106.300 . 1 5 2 2 ILE H H 8.651 . 1 6 2 2 ILE HA H 3.945 . 1 7 2 2 ILE HB H 1.789 . 1 8 2 2 ILE HG12 H 1.192 . 2 9 2 2 ILE HG13 H 1.416 . 2 10 2 2 ILE HG2 H 0.857 . 1 11 2 2 ILE HD1 H 0.806 . 1 12 2 2 ILE CA C 60.816 . 1 13 2 2 ILE CB C 35.455 . 1 14 2 2 ILE CG1 C 25.640 . 1 15 2 2 ILE CG2 C 14.678 . 1 16 2 2 ILE CD1 C 10.319 . 1 17 2 2 ILE N N 122.148 . 1 18 3 3 LYS H H 8.426 . 1 19 3 3 LYS HA H 3.881 . 1 20 3 3 LYS HB2 H 1.762 . 2 21 3 3 LYS HB3 H 1.670 . 2 22 3 3 LYS HG2 H 1.321 . 2 23 3 3 LYS HG3 H 1.470 . 2 24 3 3 LYS HD2 H 1.602 . 1 25 3 3 LYS HD3 H 1.602 . 1 26 3 3 LYS HE2 H 2.887 . 1 27 3 3 LYS HE3 H 2.887 . 1 28 3 3 LYS CA C 57.241 . 1 29 3 3 LYS CB C 29.275 . 1 30 3 3 LYS CG C 22.649 . 1 31 3 3 LYS CD C 26.375 . 1 32 3 3 LYS CE C 39.276 . 1 33 3 3 LYS N N 120.823 . 1 34 4 4 GLU H H 8.415 . 1 35 4 4 GLU HA H 3.827 . 1 36 4 4 GLU HB2 H 1.979 . 2 37 4 4 GLU HB3 H 1.943 . 2 38 4 4 GLU HG2 H 2.253 . 2 39 4 4 GLU HG3 H 2.172 . 2 40 4 4 GLU CA C 57.433 . 1 41 4 4 GLU CB C 26.152 . 1 42 4 4 GLU CG C 33.184 . 1 43 4 4 GLU N N 120.898 . 1 44 5 5 MET H H 8.009 . 1 45 5 5 MET HA H 4.202 . 1 46 5 5 MET HB2 H 2.280 . 2 47 5 5 MET HB3 H 2.213 . 2 48 5 5 MET HG2 H 3.010 . 2 49 5 5 MET HG3 H 2.841 . 2 50 5 5 MET HE H 2.580 . 1 51 5 5 MET CA C 55.764 . 1 52 5 5 MET CB C 23.130 . 1 53 5 5 MET CG C 48.728 . 1 54 5 5 MET CE C 36.565 . 1 55 5 5 MET N N 118.829 . 1 56 6 6 LEU H H 8.504 . 1 57 6 6 LEU HA H 3.971 . 1 58 6 6 LEU HB2 H 1.749 . 2 59 6 6 LEU HB3 H 1.420 . 2 60 6 6 LEU HG H 1.752 . 1 61 6 6 LEU HD1 H 0.774 . 1 62 6 6 LEU HD2 H 0.758 . 1 63 6 6 LEU CA C 55.313 . 1 64 6 6 LEU CB C 38.679 . 1 65 6 6 LEU CG C 23.924 . 1 66 6 6 LEU CD1 C 22.684 . 1 67 6 6 LEU CD2 C 19.855 . 1 68 6 6 LEU N N 121.066 . 1 69 7 7 CYS H H 7.834 . 1 70 7 7 CYS HA H 4.196 . 1 71 7 7 CYS HB2 H 3.254 . 2 72 7 7 CYS HB3 H 2.820 . 2 73 7 7 CYS CA C 57.188 . 1 74 7 7 CYS CB C 32.111 . 1 75 7 7 CYS N N 121.224 . 1 76 8 8 ASN H H 8.574 . 1 77 8 8 ASN HA H 4.203 . 1 78 8 8 ASN HB2 H 2.748 . 2 79 8 8 ASN HB3 H 2.701 . 2 80 8 8 ASN CA C 54.040 . 1 81 8 8 ASN CB C 35.911 . 1 82 8 8 ASN N N 120.641 . 1 83 9 9 MET H H 8.217 . 1 84 9 9 MET HA H 4.144 . 1 85 9 9 MET HB2 H 2.236 . 2 86 9 9 MET HB3 H 2.263 . 2 87 9 9 MET HG2 H 3.021 . 2 88 9 9 MET HG3 H 2.733 . 2 89 9 9 MET HE H 2.567 . 1 90 9 9 MET CA C 55.598 . 1 91 9 9 MET CB C 22.931 . 1 92 9 9 MET CG C 47.838 . 1 93 9 9 MET CE C 36.547 . 1 94 9 9 MET N N 120.493 . 1 95 10 10 ALA H H 7.856 . 1 96 10 10 ALA HA H 4.211 . 1 97 10 10 ALA HB H 1.481 . 1 98 10 10 ALA CA C 52.643 . 1 99 10 10 ALA CB C 14.449 . 1 100 10 10 ALA N N 122.843 . 1 101 11 11 CYS H H 8.006 . 1 102 11 11 CYS HA H 4.265 . 1 103 11 11 CYS HB2 H 3.067 . 2 104 11 11 CYS HB3 H 3.045 . 2 105 11 11 CYS CA C 54.799 . 1 106 11 11 CYS CB C 35.199 . 1 107 11 11 CYS N N 116.927 . 1 108 12 12 ALA H H 8.222 . 1 109 12 12 ALA HA H 3.731 . 1 110 12 12 ALA HB H 1.423 . 1 111 12 12 ALA CA C 52.694 . 1 112 12 12 ALA CB C 15.504 . 1 113 12 12 ALA N N 123.914 . 1 114 13 13 GLN H H 7.553 . 1 115 13 13 GLN HA H 4.185 . 1 116 13 13 GLN HB2 H 2.200 . 2 117 13 13 GLN HB3 H 2.062 . 2 118 13 13 GLN HG2 H 2.471 . 2 119 13 13 GLN HG3 H 2.405 . 2 120 13 13 GLN HE21 H 7.315 . 1 121 13 13 GLN HE22 H 6.852 . 1 122 13 13 GLN CA C 53.473 . 1 123 13 13 GLN CB C 27.030 . 1 124 13 13 GLN CG C 31.248 . 1 125 13 13 GLN CD C 177.405 . 1 126 13 13 GLN N N 111.924 . 1 127 13 13 GLN NE2 N 111.168 . 1 128 14 14 THR H H 7.432 . 1 129 14 14 THR HA H 4.495 . 1 130 14 14 THR HB H 4.264 . 1 131 14 14 THR HG2 H 1.158 . 1 132 14 14 THR CA C 57.095 . 1 133 14 14 THR CB C 67.655 . 1 134 14 14 THR CG2 C 18.380 . 1 135 14 14 THR N N 108.632 . 1 136 15 15 VAL H H 8.809 . 1 137 15 15 VAL HA H 4.087 . 1 138 15 15 VAL HB H 2.085 . 1 139 15 15 VAL HG1 H 1.044 . 1 140 15 15 VAL HG2 H 0.979 . 1 141 15 15 VAL CA C 61.243 . 1 142 15 15 VAL CB C 29.559 . 1 143 15 15 VAL CG1 C 17.419 . 1 144 15 15 VAL CG2 C 19.534 . 1 145 15 15 VAL N N 118.305 . 1 146 16 16 CYS H H 8.132 . 1 147 16 16 CYS HA H 4.891 . 1 148 16 16 CYS HB2 H 3.313 . 2 149 16 16 CYS HB3 H 2.763 . 2 150 16 16 CYS CA C 52.910 . 1 151 16 16 CYS CB C 41.124 . 1 152 16 16 CYS N N 116.073 . 1 153 17 17 LYS H H 7.227 . 1 154 17 17 LYS HA H 3.988 . 1 155 17 17 LYS HB2 H 1.696 . 1 156 17 17 LYS HB3 H 1.696 . 1 157 17 17 LYS HG2 H 1.299 . 1 158 17 17 LYS HG3 H 1.299 . 1 159 17 17 LYS HD2 H 1.595 . 1 160 17 17 LYS HD3 H 1.595 . 1 161 17 17 LYS HE2 H 2.896 . 1 162 17 17 LYS HE3 H 2.896 . 1 163 17 17 LYS CA C 56.094 . 1 164 17 17 LYS CB C 30.063 . 1 165 17 17 LYS CG C 22.133 . 1 166 17 17 LYS CD C 26.346 . 1 167 17 17 LYS CE C 39.322 . 1 168 17 17 LYS N N 120.889 . 1 169 18 18 LYS H H 8.132 . 1 170 18 18 LYS HA H 4.172 . 1 171 18 18 LYS HB2 H 1.805 . 2 172 18 18 LYS HB3 H 1.700 . 2 173 18 18 LYS HG2 H 1.305 . 1 174 18 18 LYS HG3 H 1.305 . 1 175 18 18 LYS HD2 H 1.595 . 1 176 18 18 LYS HD3 H 1.595 . 1 177 18 18 LYS HE2 H 2.888 . 1 178 18 18 LYS HE3 H 2.888 . 1 179 18 18 LYS C C 174.119 . 1 180 18 18 LYS CA C 54.219 . 1 181 18 18 LYS CB C 29.953 . 1 182 18 18 LYS CG C 22.175 . 1 183 18 18 LYS CD C 26.345 . 1 184 18 18 LYS CE C 39.294 . 1 185 18 18 LYS N N 117.661 . 1 186 19 19 SER H H 7.765 . 1 187 19 19 SER HA H 4.373 . 1 188 19 19 SER HB2 H 3.830 . 2 189 19 19 SER HB3 H 3.765 . 2 190 19 19 SER CA C 55.417 . 1 191 19 19 SER CB C 61.546 . 1 192 19 19 SER N N 113.189 . 1 193 20 20 GLY H H 8.177 . 1 194 20 20 GLY HA2 H 4.117 . 2 195 20 20 GLY HA3 H 3.820 . 2 196 20 20 GLY CA C 42.222 . 1 197 20 20 GLY N N 108.859 . 1 198 21 21 GLY H H 8.617 . 1 199 21 21 GLY HA2 H 4.437 . 2 200 21 21 GLY HA3 H 3.853 . 2 201 21 21 GLY CA C 42.040 . 1 202 21 21 GLY N N 110.511 . 1 203 22 22 PRO HA H 4.255 . 1 204 22 22 PRO HB2 H 1.869 . 2 205 22 22 PRO HB3 H 2.298 . 2 206 22 22 PRO HG2 H 1.902 . 2 207 22 22 PRO HG3 H 1.983 . 2 208 22 22 PRO HD2 H 3.545 . 2 209 22 22 PRO HD3 H 3.676 . 2 210 22 22 PRO CA C 62.765 . 1 211 22 22 PRO CB C 29.457 . 1 212 22 22 PRO CG C 24.590 . 1 213 22 22 PRO CD C 47.001 . 1 214 23 23 LEU H H 8.458 . 1 215 23 23 LEU HA H 4.090 . 1 216 23 23 LEU HB2 H 1.336 . 2 217 23 23 LEU HB3 H 1.699 . 2 218 23 23 LEU HG H 1.598 . 1 219 23 23 LEU HD1 H 0.843 . 1 220 23 23 LEU HD2 H 0.796 . 1 221 23 23 LEU CA C 55.077 . 1 222 23 23 LEU CB C 38.438 . 1 223 23 23 LEU CG C 24.450 . 1 224 23 23 LEU CD1 C 22.084 . 1 225 23 23 LEU CD2 C 20.314 . 1 226 23 23 LEU N N 117.915 . 1 227 24 24 CYS H H 7.495 . 1 228 24 24 CYS HA H 4.192 . 1 229 24 24 CYS HB2 H 3.210 . 2 230 24 24 CYS HB3 H 3.163 . 2 231 24 24 CYS CA C 55.876 . 1 232 24 24 CYS CB C 36.379 . 1 233 24 24 CYS N N 119.229 . 1 234 25 25 ASP H H 8.394 . 1 235 25 25 ASP HA H 4.253 . 1 236 25 25 ASP HB2 H 2.670 . 2 237 25 25 ASP HB3 H 2.621 . 2 238 25 25 ASP CA C 54.793 . 1 239 25 25 ASP CB C 36.900 . 1 240 25 25 ASP N N 120.777 . 1 241 26 26 THR H H 8.335 . 1 242 26 26 THR HA H 3.860 . 1 243 26 26 THR HB H 4.079 . 1 244 26 26 THR HG2 H 1.171 . 1 245 26 26 THR CA C 63.816 . 1 246 26 26 THR CB C 66.015 . 1 247 26 26 THR CG2 C 18.781 . 1 248 26 26 THR N N 116.552 . 1 249 27 27 CYS H H 7.555 . 1 250 27 27 CYS HA H 4.155 . 1 251 27 27 CYS HB2 H 3.357 . 2 252 27 27 CYS HB3 H 3.006 . 2 253 27 27 CYS CA C 58.413 . 1 254 27 27 CYS CB C 35.903 . 1 255 27 27 CYS N N 123.341 . 1 256 28 28 GLN H H 8.290 . 1 257 28 28 GLN HA H 3.924 . 1 258 28 28 GLN HB2 H 2.033 . 2 259 28 28 GLN HB3 H 1.991 . 2 260 28 28 GLN HG2 H 2.620 . 2 261 28 28 GLN HG3 H 2.219 . 2 262 28 28 GLN CA C 56.491 . 1 263 28 28 GLN CB C 25.720 . 1 264 28 28 GLN CG C 31.999 . 1 265 28 28 GLN N N 116.812 . 1 266 29 29 ALA H H 8.374 . 1 267 29 29 ALA HA H 4.019 . 1 268 29 29 ALA HB H 1.405 . 1 269 29 29 ALA CA C 52.243 . 1 270 29 29 ALA CB C 15.109 . 1 271 29 29 ALA N N 123.116 . 1 272 30 30 ALA H H 7.640 . 1 273 30 30 ALA HA H 4.148 . 1 274 30 30 ALA HB H 1.457 . 1 275 30 30 ALA CA C 51.882 . 1 276 30 30 ALA CB C 14.648 . 1 277 30 30 ALA N N 121.609 . 1 278 31 31 CYS H H 7.488 . 1 279 31 31 CYS HA H 4.549 . 1 280 31 31 CYS HB2 H 3.081 . 2 281 31 31 CYS HB3 H 3.003 . 2 282 31 31 CYS CA C 52.015 . 1 283 31 31 CYS CB C 32.631 . 1 284 31 31 CYS N N 115.487 . 1 285 32 32 LYS H H 7.632 . 1 286 32 32 LYS HA H 4.034 . 1 287 32 32 LYS HB2 H 1.847 . 2 288 32 32 LYS HB3 H 1.795 . 2 289 32 32 LYS HG2 H 1.490 . 2 290 32 32 LYS HG3 H 1.363 . 2 291 32 32 LYS HD2 H 1.592 . 1 292 32 32 LYS HD3 H 1.592 . 1 293 32 32 LYS HE2 H 2.864 . 1 294 32 32 LYS HE3 H 2.864 . 1 295 32 32 LYS CA C 55.407 . 1 296 32 32 LYS CB C 29.823 . 1 297 32 32 LYS CG C 22.314 . 1 298 32 32 LYS CD C 26.238 . 1 299 32 32 LYS CE C 39.205 . 1 300 32 32 LYS N N 119.508 . 1 301 33 33 ALA H H 7.572 . 1 302 33 33 ALA HA H 4.205 . 1 303 33 33 ALA HB H 1.372 . 1 304 33 33 ALA CA C 50.368 . 1 305 33 33 ALA CB C 15.707 . 1 306 33 33 ALA N N 121.344 . 1 307 34 34 LEU H H 7.605 . 1 308 34 34 LEU HA H 4.153 . 1 309 34 34 LEU HB2 H 1.452 . 2 310 34 34 LEU HB3 H 1.747 . 2 311 34 34 LEU HG H 1.778 . 1 312 34 34 LEU HD1 H 0.824 . 1 313 34 34 LEU HD2 H 0.783 . 1 314 34 34 LEU CA C 53.191 . 1 315 34 34 LEU CB C 39.373 . 1 316 34 34 LEU CG C 23.837 . 1 317 34 34 LEU CD1 C 23.078 . 1 318 34 34 LEU CD2 C 20.261 . 1 319 34 34 LEU N N 118.716 . 1 320 35 35 GLY H H 7.926 . 1 321 35 35 GLY HA2 H 3.867 . 2 322 35 35 GLY HA3 H 3.780 . 2 323 35 35 GLY CA C 42.357 . 1 324 35 35 GLY N N 108.316 . 1 stop_ save_