data_18655 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Arced helix (ArcH) NMR structure of the reovirus p14 fusion-associated small transmembrane (FAST) protein transmembrane domain (TMD) in dodecyl phosphocholine (DPC) micelles ; _BMRB_accession_number 18655 _BMRB_flat_file_name bmr18655.str _Entry_type original _Submission_date 2012-08-10 _Accession_date 2012-08-10 _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 Sarker Muzaddid . . 2 Key Tim . . 3 Duncan Roy . . 4 Rainey Jan K. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 223 "15N chemical shifts" 8 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-09-04 original author . stop_ _Original_release_date 2012-09-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A Cell-Cell Membrane Fusion Module Comprising a Transmembrane Arced Helix (ArcH)' _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 Sarker Muzaddid . . 2 Key Tim . . 3 Rainey Jan K. . 4 Duncan Roy . . 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 'Transmembrane Arced Helix (ArcH)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Transmembrane Arced Helix (ArcH)' $ArcH 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_ArcH _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ArcH _Molecular_mass 3816.708 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 32 _Mol_residue_sequence ; KKHTIWEVIAGLVALLTFLA FGFWLFKYLQKK ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 LYS 3 HIS 4 THR 5 ILE 6 TRP 7 GLU 8 VAL 9 ILE 10 ALA 11 GLY 12 LEU 13 VAL 14 ALA 15 LEU 16 LEU 17 THR 18 PHE 19 LEU 20 ALA 21 PHE 22 GLY 23 PHE 24 TRP 25 LEU 26 PHE 27 LYS 28 TYR 29 LEU 30 GLN 31 LYS 32 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-12 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 2LX0 "Arced Helix (Arch) Nmr Structure Of The Reovirus P14 Fusion-Associated Small Transmembrane (Fast) Protein Transmembrane Domain " 100.00 32 100.00 100.00 3.49e-12 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ArcH 'Reptilian orthoreovirus' 226613 Viruses . Reptilian orthoreovirus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $ArcH 'chemical synthesis' . Reptilian orthoreovirus . 'Not applicable' 'Not applicable' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '0.75 mM p14 TMD peptide, 150 mM deuterated dodecyl phosphocholine (DPC), 0.5 mM sodium 2,2-dimethyl-2-silapentane-5-sulfonate (DSS), 0.2 mM sodium azide, 20 mM sodium acetate, pH 5, 37 degree celcius' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ArcH 0.75 mM 'Partial 15N (8 of 32 amino acids)' DPC 150 mM [U-2H] DSS 0.5 mM 'natural abundance' 'sodium azide' 0.2 mM 'natural abundance' 'sodium acetate' 20 mM [U-2H] H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version 2.18 loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement 'structure solution' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.110 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_Molmol _Saveframe_category software _Name Molmol _Version 2k.2 loop_ _Vendor _Address _Electronic_address 'Koradi, Billeter and Wuthrich' . . stop_ loop_ _Task 'ensemble superposition' 'RMSD calculation' visualization stop_ _Details . save_ save_UCSF_Chimera _Saveframe_category software _Name Chimera _Version 1.6.2 loop_ _Vendor _Address _Electronic_address 'Pettersen, Goddard, Huang, Couch, Greenblatt, Meng, Ferrin' . . stop_ loop_ _Task 'Distance measurement' visualization stop_ _Details . save_ save_ProcheckNMR _Saveframe_category software _Name ProcheckNMR _Version 3.5.4 loop_ _Vendor _Address _Electronic_address 'Laskowski and MacArthur' . . stop_ loop_ _Task 'Ramachandran plot statistics' 'structure validation' stop_ _Details . save_ save_DSSP _Saveframe_category software _Name DSSP _Version . loop_ _Vendor _Address _Electronic_address 'Kabsch, Sander; Joosten, Te Beek, Krieger, Hekkelman, Hooft, Schneider, Sander, Vriend' . . stop_ loop_ _Task 'secondary structure analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details 'TCI 5mm probe' 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_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_3D_1H-15N_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N 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 5 . pH pressure 1 . atm temperature 310 . 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 '2D 1H-15N 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 'Transmembrane Arced Helix (ArcH)' _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 HB2 H 1.832 0.002 2 2 1 1 LYS HB3 H 1.832 0.002 2 3 1 1 LYS HG2 H 1.287 0.000 2 4 1 1 LYS HG3 H 1.287 0.000 2 5 1 1 LYS HD2 H 1.684 0.000 2 6 1 1 LYS HD3 H 1.684 0.000 2 7 1 1 LYS HE2 H 2.974 0.003 2 8 1 1 LYS HE3 H 2.974 0.003 2 9 2 2 LYS HA H 4.300 0.003 1 10 2 2 LYS HB2 H 1.745 0.004 2 11 2 2 LYS HB3 H 1.745 0.004 2 12 2 2 LYS HG2 H 1.398 0.006 2 13 2 2 LYS HG3 H 1.398 0.006 2 14 2 2 LYS HD2 H 1.682 0.002 2 15 2 2 LYS HD3 H 1.682 0.002 2 16 2 2 LYS HE2 H 2.977 0.001 2 17 2 2 LYS HE3 H 2.977 0.001 2 18 3 3 HIS H H 8.759 0.003 1 19 3 3 HIS HA H 4.999 0.002 1 20 3 3 HIS HB2 H 3.153 0.005 2 21 3 3 HIS HB3 H 3.041 0.003 2 22 3 3 HIS HD1 H 11.126 0.003 1 23 3 3 HIS HD2 H 7.319 0.002 1 24 3 3 HIS HE1 H 7.401 0.004 1 25 4 4 THR H H 8.240 0.003 1 26 4 4 THR HA H 4.578 0.002 1 27 4 4 THR HG2 H 1.331 0.002 1 28 5 5 ILE H H 8.947 0.003 1 29 5 5 ILE HA H 3.866 0.002 1 30 5 5 ILE HB H 1.806 0.004 1 31 5 5 ILE HG12 H 1.300 0.006 2 32 5 5 ILE HG13 H 1.084 0.005 2 33 5 5 ILE HG2 H 0.798 0.003 1 34 5 5 ILE HD1 H 0.518 0.001 1 35 6 6 TRP H H 7.389 0.004 1 36 6 6 TRP HA H 4.383 0.002 1 37 6 6 TRP HB2 H 3.320 0.005 2 38 6 6 TRP HB3 H 3.259 0.003 2 39 6 6 TRP HD1 H 7.403 0.003 1 40 6 6 TRP HE1 H 10.631 0.003 1 41 6 6 TRP HE3 H 7.457 0.003 1 42 6 6 TRP HZ2 H 7.512 0.003 1 43 6 6 TRP HZ3 H 6.919 0.003 1 44 6 6 TRP HH2 H 7.092 0.003 1 45 7 7 GLU H H 7.642 0.002 1 46 7 7 GLU HA H 3.898 0.003 1 47 7 7 GLU HB2 H 2.240 0.004 2 48 7 7 GLU HB3 H 2.075 0.004 2 49 7 7 GLU HG2 H 2.480 0.003 2 50 7 7 GLU HG3 H 2.431 0.005 2 51 8 8 VAL H H 7.560 0.003 1 52 8 8 VAL HA H 3.549 0.002 1 53 8 8 VAL HB H 2.261 0.003 1 54 8 8 VAL HG1 H 1.009 0.002 2 55 8 8 VAL HG2 H 0.883 0.004 2 56 9 9 ILE H H 8.276 0.004 1 57 9 9 ILE HA H 3.553 0.005 1 58 9 9 ILE HB H 1.949 0.002 1 59 9 9 ILE HG12 H 1.004 0.004 2 60 9 9 ILE HG13 H 1.004 0.004 2 61 9 9 ILE HG2 H 0.903 0.003 1 62 9 9 ILE HD1 H 0.571 0.003 1 63 10 10 ALA H H 8.386 0.003 1 64 10 10 ALA HA H 3.905 0.002 1 65 10 10 ALA HB H 1.471 0.004 1 66 10 10 ALA N N 120.595 0.000 1 67 11 11 GLY H H 8.272 0.005 1 68 11 11 GLY HA2 H 3.644 0.005 2 69 11 11 GLY HA3 H 3.644 0.005 2 70 12 12 LEU H H 8.401 0.003 1 71 12 12 LEU HA H 4.050 0.003 1 72 12 12 LEU HB2 H 1.817 0.003 2 73 12 12 LEU HB3 H 1.656 0.004 2 74 12 12 LEU HG H 1.754 0.002 1 75 12 12 LEU HD1 H 0.822 0.003 2 76 12 12 LEU HD2 H 0.793 0.004 2 77 12 12 LEU N N 121.657 0.000 1 78 13 13 VAL H H 8.590 0.003 1 79 13 13 VAL HA H 3.474 0.003 1 80 13 13 VAL HB H 2.194 0.005 1 81 13 13 VAL HG1 H 1.000 0.002 2 82 13 13 VAL HG2 H 0.833 0.002 2 83 14 14 ALA H H 8.524 0.003 1 84 14 14 ALA HA H 3.863 0.003 1 85 14 14 ALA HB H 1.432 0.002 1 86 14 14 ALA N N 124.024 0.000 1 87 15 15 LEU H H 8.309 0.003 1 88 15 15 LEU HA H 4.017 0.003 1 89 15 15 LEU HB2 H 1.902 0.003 2 90 15 15 LEU HB3 H 1.902 0.003 2 91 15 15 LEU HG H 1.672 0.003 1 92 15 15 LEU HD1 H 0.886 0.003 2 93 15 15 LEU HD2 H 0.830 0.003 2 94 16 16 LEU H H 8.523 0.002 1 95 16 16 LEU HA H 3.964 0.005 1 96 16 16 LEU HB2 H 1.894 0.005 2 97 16 16 LEU HB3 H 1.894 0.005 2 98 16 16 LEU HG H 1.429 0.004 1 99 16 16 LEU HD1 H 0.777 0.003 2 100 16 16 LEU HD2 H 0.777 0.003 2 101 16 16 LEU N N 117.442 0.000 1 102 17 17 THR H H 8.194 0.004 1 103 17 17 THR HA H 3.690 0.003 1 104 17 17 THR HB H 4.172 0.004 1 105 17 17 THR HG2 H 0.995 0.002 1 106 18 18 PHE H H 8.372 0.003 1 107 18 18 PHE HA H 4.254 0.004 1 108 18 18 PHE HB2 H 3.232 0.002 2 109 18 18 PHE HB3 H 3.208 0.003 2 110 18 18 PHE HD1 H 7.106 0.004 3 111 18 18 PHE HD2 H 7.106 0.004 3 112 18 18 PHE HE1 H 7.042 0.003 3 113 18 18 PHE HE2 H 7.042 0.003 3 114 18 18 PHE HZ H 6.987 0.002 1 115 18 18 PHE N N 121.022 0.000 1 116 19 19 LEU H H 8.521 0.002 1 117 19 19 LEU HA H 3.968 0.004 1 118 19 19 LEU HB2 H 2.053 0.005 2 119 19 19 LEU HB3 H 2.017 0.003 2 120 19 19 LEU HG H 1.410 0.006 1 121 19 19 LEU HD1 H 0.838 0.003 2 122 19 19 LEU HD2 H 0.838 0.003 2 123 20 20 ALA H H 8.517 0.003 1 124 20 20 ALA HA H 4.053 0.003 1 125 20 20 ALA HB H 1.484 0.003 1 126 20 20 ALA N N 121.004 0.000 1 127 21 21 PHE H H 8.659 0.004 1 128 21 21 PHE HA H 4.428 0.003 1 129 21 21 PHE HB2 H 3.204 0.002 2 130 21 21 PHE HB3 H 3.204 0.002 2 131 21 21 PHE HD1 H 7.142 0.002 3 132 21 21 PHE HD2 H 7.142 0.002 3 133 21 21 PHE HE1 H 7.115 0.002 3 134 21 21 PHE HE2 H 7.115 0.002 3 135 21 21 PHE HZ H 7.300 0.002 1 136 22 22 GLY H H 8.887 0.002 1 137 22 22 GLY HA2 H 3.538 0.004 2 138 22 22 GLY HA3 H 3.538 0.004 2 139 22 22 GLY N N 107.120 0.000 1 140 23 23 PHE H H 8.733 0.002 1 141 23 23 PHE HA H 4.256 0.003 1 142 23 23 PHE HB2 H 3.283 0.003 2 143 23 23 PHE HB3 H 3.183 0.003 2 144 23 23 PHE HD1 H 7.120 0.005 3 145 23 23 PHE HD2 H 7.120 0.005 3 146 23 23 PHE HE1 H 7.236 0.003 3 147 23 23 PHE HE2 H 7.236 0.003 3 148 23 23 PHE HZ H 7.316 0.003 1 149 24 24 TRP H H 8.592 0.003 1 150 24 24 TRP HA H 3.985 0.003 1 151 24 24 TRP HB2 H 3.592 0.002 2 152 24 24 TRP HB3 H 3.296 0.005 2 153 24 24 TRP HD1 H 7.143 0.006 1 154 24 24 TRP HE1 H 10.342 0.003 1 155 24 24 TRP HE3 H 7.301 0.004 1 156 24 24 TRP HZ2 H 7.158 0.003 1 157 24 24 TRP HZ3 H 6.717 0.004 1 158 24 24 TRP HH2 H 6.640 0.003 1 159 25 25 LEU H H 8.925 0.003 1 160 25 25 LEU HA H 3.635 0.003 1 161 25 25 LEU HB2 H 1.666 0.004 2 162 25 25 LEU HB3 H 1.471 0.006 2 163 25 25 LEU HG H 1.577 0.005 1 164 25 25 LEU HD1 H 0.851 0.004 2 165 25 25 LEU HD2 H 0.851 0.004 2 166 26 26 PHE H H 8.458 0.003 1 167 26 26 PHE HA H 3.990 0.002 1 168 26 26 PHE HB2 H 3.233 0.003 2 169 26 26 PHE HB3 H 3.113 0.003 2 170 26 26 PHE HD1 H 7.022 0.003 3 171 26 26 PHE HD2 H 7.022 0.003 3 172 26 26 PHE HE1 H 7.243 0.002 3 173 26 26 PHE HE2 H 7.243 0.002 3 174 26 26 PHE HZ H 7.118 0.005 1 175 27 27 LYS H H 7.788 0.003 1 176 27 27 LYS HA H 3.669 0.003 1 177 27 27 LYS HB2 H 1.695 0.005 2 178 27 27 LYS HB3 H 1.534 0.006 2 179 27 27 LYS HG2 H 1.124 0.002 2 180 27 27 LYS HG3 H 1.124 0.002 2 181 27 27 LYS HD2 H 1.478 0.002 2 182 27 27 LYS HD3 H 1.431 0.003 2 183 27 27 LYS HE2 H 2.846 0.003 2 184 27 27 LYS HE3 H 2.717 0.003 2 185 27 27 LYS HZ H 7.241 0.002 1 186 28 28 TYR H H 8.303 0.003 1 187 28 28 TYR HA H 3.901 0.002 1 188 28 28 TYR HB2 H 2.670 0.003 2 189 28 28 TYR HB3 H 2.269 0.004 2 190 28 28 TYR HD1 H 6.831 0.003 3 191 28 28 TYR HD2 H 6.831 0.003 3 192 28 28 TYR HE1 H 6.764 0.002 3 193 28 28 TYR HE2 H 6.764 0.002 3 194 29 29 LEU H H 8.039 0.003 1 195 29 29 LEU HA H 3.869 0.006 1 196 29 29 LEU HB2 H 1.907 0.002 2 197 29 29 LEU HB3 H 1.688 0.005 2 198 29 29 LEU HG H 1.414 0.001 1 199 29 29 LEU HD1 H 0.855 0.003 2 200 29 29 LEU HD2 H 0.855 0.003 2 201 29 29 LEU N N 116.640 0.000 1 202 30 30 GLN H H 7.346 0.004 1 203 30 30 GLN HA H 3.993 0.002 1 204 30 30 GLN HB2 H 1.913 0.003 2 205 30 30 GLN HB3 H 1.759 0.002 2 206 30 30 GLN HG2 H 2.107 0.006 2 207 30 30 GLN HG3 H 2.082 0.004 2 208 30 30 GLN HE21 H 6.873 0.003 2 209 30 30 GLN HE22 H 6.659 0.002 2 210 31 31 LYS H H 7.559 0.003 1 211 31 31 LYS HA H 4.129 0.002 1 212 31 31 LYS HB2 H 1.753 0.004 2 213 31 31 LYS HB3 H 1.680 0.005 2 214 31 31 LYS HG2 H 1.399 0.006 2 215 31 31 LYS HG3 H 1.337 0.005 2 216 31 31 LYS HD2 H 1.584 0.005 2 217 31 31 LYS HD3 H 1.584 0.005 2 218 31 31 LYS HE2 H 2.911 0.003 2 219 31 31 LYS HE3 H 2.911 0.003 2 220 31 31 LYS HZ H 6.832 0.004 1 221 32 32 LYS H H 7.686 0.003 1 222 32 32 LYS HA H 4.059 0.002 1 223 32 32 LYS HB2 H 1.743 0.006 2 224 32 32 LYS HB3 H 1.613 0.004 2 225 32 32 LYS HG2 H 1.321 0.004 2 226 32 32 LYS HG3 H 1.321 0.004 2 227 32 32 LYS HD2 H 1.588 0.004 2 228 32 32 LYS HD3 H 1.588 0.004 2 229 32 32 LYS HE2 H 2.913 0.004 2 230 32 32 LYS HE3 H 2.913 0.004 2 231 32 32 LYS HZ H 6.761 0.000 1 stop_ save_