data_27730 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure determination of transmembrane- C-terminal fragment of UL49.5 protein from bovine herpesvirus 1 by NMR spectroscopy and molecular dynamics ; _BMRB_accession_number 27730 _BMRB_flat_file_name bmr27730.str _Entry_type original _Submission_date 2018-12-16 _Accession_date 2018-12-16 _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 Karska Natalia . . 2 Graul Malgorzata . . 3 Sikorska Emilia . . 4 Zhukov Igor . . 5 Slusarz Magdalena . . 6 Kasprzykowski Franciszek . . 7 Lipinska Andrea . . 8 Rodziewicz-Motowidlo Sylwia . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 216 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-02-25 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 27728 N.BHV stop_ _Original_release_date 2018-12-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure determination of UL49.5 transmembrane protein from bovine herpesvirus 1 by NMR spectroscopy and molecular dynamics. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30772281 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Karska Natalia . . 2 Graul Malgorzata . . 3 Sikorska Emilia . . 4 Zhukov Igor . . 5 Slusarz Magdalena J. . 6 Kasprzykowski Franciszek . . 7 Lipinska Andrea D. . 8 Rodziewicz-Motowidlo Sylwia . . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta Biomembr.' _Journal_name_full 'Biochimica et biophysica acta. Biomembranes' _Journal_volume 1861 _Journal_issue 5 _Journal_ISSN 1879-2642 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 926 _Page_last 938 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name TMC.BHV _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TMC.BHV $TMC.BHV stop_ _System_molecular_weight 4209 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TMC.BHV _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TMC.BHV _Molecular_mass 4209 _Mol_thiol_state 'not present' loop_ _Biological_function ; UL49.5 protein blocks the transporter associated with antigen processing (TAP). The interaction of the UL49.5 protein with the TAP complex blocks conformational rearrangements in TAP required for peptide translocation into the endoplasmic reticulum (ER). In addition, UL49.5 induces degradation of the transporter and the UL49.5 protein itself (18). A truncated form of the UL49.5 protein lacking the cytoplasmic tail can still block the translocation of peptides, but it fails to trigger degradation of the TAP complex. ; stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 40 _Mol_residue_sequence ; VVFYVALTAVXVAVALYAYG LXFRLXGASGPNKKESRGRG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 VAL 2 2 VAL 3 3 PHE 4 4 TYR 5 5 VAL 6 6 ALA 7 7 LEU 8 8 THR 9 9 ALA 10 10 VAL 11 11 NLE 12 12 VAL 13 13 ALA 14 14 VAL 15 15 ALA 16 16 LEU 17 17 TYR 18 18 ALA 19 19 TYR 20 20 GLY 21 21 LEU 22 22 ABA 23 23 PHE 24 24 ARG 25 25 LEU 26 26 NLE 27 27 GLY 28 28 ALA 29 29 SER 30 30 GLY 31 31 PRO 32 32 ASN 33 33 LYS 34 34 LYS 35 35 GLU 36 36 SER 37 37 ARG 38 38 GLY 39 39 ARG 40 40 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_ABA _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common 'ALPHA-AMINOBUTYRIC ACID' _BMRB_code ABA _PDB_code ABA _Standard_residue_derivative . _Molecular_mass 103.120 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HN2 HN2 H . 0 . ? HA HA H . 0 . ? HB3 HB3 H . 0 . ? HB2 HB2 H . 0 . ? HG1 HG1 H . 0 . ? HG3 HG3 H . 0 . ? HG2 HG2 H . 0 . ? HXT HXT H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N HN2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING CB CG ? ? SING CB HB3 ? ? SING CB HB2 ? ? SING CG HG1 ? ? SING CG HG3 ? ? SING CG HG2 ? ? SING OXT HXT ? ? stop_ save_ save_chem_comp_NLE _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common NORLEUCINE _BMRB_code NLE _PDB_code NLE _Standard_residue_derivative . _Molecular_mass 131.173 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? CE CE C . 0 . ? H H H . 0 . ? HN2 HN2 H . 0 . ? HA HA H . 0 . ? HXT HXT H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HD2 HD2 H . 0 . ? HD3 HD3 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HE3 HE3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N HN2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG HG2 ? ? SING CG HG3 ? ? SING CD CE ? ? SING CD HD2 ? ? SING CD HD3 ? ? SING CE HE1 ? ? SING CE HE2 ? ? SING CE HE3 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $TMC.BHV BHV-1 10320 Viruses . Varicellovirus BHV-1 UL49.5 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 $TMC.BHV 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'NMR experiments were performed using 100 mM DPC-d38 in water (90%:10% H2O:D2O).' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TMC.BHV 2.7 mM 'natural abundance' DPC 100 mM 'natural abundance' 'Acetic Acid-d4' 0.01 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'chemical shift calculation' 'peak picking' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'data analysis' 'structure solution' stop_ _Details . save_ save_AMBER _Saveframe_category software _Name AMBER _Version 15 loop_ _Vendor _Address _Electronic_address 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman' . . stop_ loop_ _Task 'geometry optimization' refinement '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_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Agilent _Model 'Uniform NMR System' _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_ROESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H ROESY' _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 'ionic strength' 0.05 . M pH 5 . pH pressure 1 . atm temperature 303 . 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 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_ _Software_label $SPARKY stop_ loop_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H NOESY' '2D 1H-1H ROESY' 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 TMC.BHV _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 2 2 VAL H H 9.06 0.02 1 2 2 2 VAL HA H 3.91 0.02 1 3 2 2 VAL HB H 2.25 0.02 1 4 2 2 VAL HG1 H 1.10 0.02 2 5 2 2 VAL HG2 H 1.01 0.02 2 6 3 3 PHE H H 7.60 0.02 1 7 3 3 PHE HA H 4.12 0.02 1 8 3 3 PHE HB2 H 3.29 0.02 1 9 3 3 PHE HB3 H 2.82 0.02 1 10 3 3 PHE HD1 H 6.84 0.02 3 11 3 3 PHE HD2 H 6.84 0.02 3 12 3 3 PHE HE1 H 6.84 0.02 3 13 3 3 PHE HE2 H 6.84 0.02 3 14 4 4 TYR H H 8.08 0.02 1 15 4 4 TYR HA H 4.12 0.02 1 16 4 4 TYR HB2 H 3.07 0.02 1 17 4 4 TYR HB3 H 2.96 0.02 1 18 4 4 TYR HD1 H 7.06 0.02 3 19 4 4 TYR HD2 H 7.06 0.02 3 20 4 4 TYR HE1 H 7.44 0.02 3 21 4 4 TYR HE2 H 7.44 0.02 3 22 5 5 VAL H H 8.31 0.02 1 23 5 5 VAL HA H 3.47 0.02 1 24 5 5 VAL HB H 2.19 0.02 1 25 5 5 VAL HG1 H 0.99 0.02 2 26 5 5 VAL HG2 H 0.84 0.02 2 27 6 6 ALA H H 8.12 0.02 1 28 6 6 ALA HA H 3.82 0.02 1 29 6 6 ALA HB H 1.41 0.02 1 30 7 7 LEU H H 7.89 0.02 1 31 7 7 LEU HA H 3.82 0.02 1 32 7 7 LEU HB2 H 1.49 0.02 2 33 7 7 LEU HB3 H 1.49 0.02 2 34 7 7 LEU HG H 1.41 0.02 1 35 7 7 LEU HD1 H 1.00 0.02 2 36 7 7 LEU HD2 H 0.84 0.02 2 37 8 8 THR H H 8.41 0.02 1 38 9 9 ALA H H 8.08 0.02 1 39 9 9 ALA HA H 3.90 0.02 1 40 9 9 ALA HB H 1.35 0.02 1 41 10 10 VAL H H 8.41 0.02 1 42 10 10 VAL HA H 3.86 0.02 1 43 10 10 VAL HB H 2.35 0.02 1 44 10 10 VAL HG1 H 1.17 0.02 2 45 10 10 VAL HG2 H 1.05 0.02 2 46 11 11 NLE H H 7.76 0.02 1 47 11 11 NLE HA H 4.23 0.02 1 48 11 11 NLE HE1 H 0.78 0.02 2 49 11 11 NLE HE2 H 0.78 0.02 2 50 11 11 NLE HE3 H 0.78 0.02 2 51 11 11 NLE HG2 H 1.09 0.02 2 52 11 11 NLE HG3 H 1.09 0.02 2 53 12 12 VAL H H 8.38 0.02 1 54 12 12 VAL HA H 3.79 0.02 1 55 12 12 VAL HB H 2.39 0.02 1 56 12 12 VAL HG1 H 1.21 0.02 2 57 12 12 VAL HG2 H 1.06 0.02 2 58 13 13 ALA H H 8.31 0.02 1 59 13 13 ALA HA H 3.96 0.02 1 60 13 13 ALA HB H 1.49 0.02 1 61 14 14 VAL H H 8.57 0.02 1 62 14 14 VAL HA H 3.60 0.02 1 63 14 14 VAL HB H 2.27 0.02 1 64 14 14 VAL HG1 H 1.07 0.02 2 65 14 14 VAL HG2 H 0.97 0.02 2 66 15 15 ALA H H 8.49 0.02 1 67 15 15 ALA HA H 4.07 0.02 1 68 15 15 ALA HB H 1.55 0.02 1 69 16 16 LEU H H 8.73 0.02 1 70 16 16 LEU HA H 4.06 0.02 1 71 16 16 LEU HB2 H 2.10 0.02 2 72 16 16 LEU HB3 H 2.10 0.02 2 73 16 16 LEU HG H 2.05 0.02 1 74 16 16 LEU HD1 H 0.82 0.02 2 75 17 17 TYR H H 8.49 0.02 1 76 17 17 TYR HA H 4.24 0.02 1 77 17 17 TYR HB2 H 3.27 0.02 1 78 17 17 TYR HB3 H 3.07 0.02 1 79 17 17 TYR HD1 H 6.95 0.02 3 80 17 17 TYR HD2 H 6.95 0.02 3 81 17 17 TYR HE1 H 6.79 0.02 3 82 17 17 TYR HE2 H 6.79 0.02 3 83 18 18 ALA H H 9.19 0.02 1 84 18 18 ALA HA H 3.87 0.02 1 85 18 18 ALA HB H 1.48 0.02 1 86 19 19 TYR H H 8.25 0.02 1 87 19 19 TYR HA H 4.07 0.02 1 88 19 19 TYR HB2 H 3.27 0.02 1 89 19 19 TYR HB3 H 2.99 0.02 1 90 19 19 TYR HD1 H 7.15 0.02 3 91 19 19 TYR HD2 H 7.15 0.02 3 92 19 19 TYR HE1 H 6.71 0.02 3 93 19 19 TYR HE2 H 6.71 0.02 3 94 20 20 GLY H H 8.73 0.02 1 95 20 20 GLY HA2 H 3.95 0.02 2 96 20 20 GLY HA3 H 3.95 0.02 2 97 21 21 LEU H H 8.49 0.02 1 98 21 21 LEU HA H 3.47 0.02 1 99 21 21 LEU HG H 1.31 0.02 1 100 22 22 ABA H H 8.09 0.02 1 101 22 22 ABA HA H 3.86 0.02 1 102 22 22 ABA HB2 H 1.72 0.02 2 103 22 22 ABA HB3 H 1.72 0.02 2 104 22 22 ABA HG1 H 0.80 0.02 2 105 22 22 ABA HG2 H 0.80 0.02 2 106 22 22 ABA HG3 H 0.80 0.02 2 107 23 23 PHE H H 8.00 0.02 1 108 23 23 PHE HA H 4.29 0.02 1 109 23 23 PHE HB2 H 3.20 0.02 1 110 23 23 PHE HB3 H 3.00 0.02 1 111 23 23 PHE HD1 H 7.25 0.02 3 112 23 23 PHE HD2 H 7.25 0.02 3 113 23 23 PHE HE1 H 7.33 0.02 3 114 23 23 PHE HE2 H 7.33 0.02 3 115 24 24 ARG H H 7.81 0.02 1 116 24 24 ARG HA H 4.15 0.02 1 117 24 24 ARG HB2 H 1.95 0.02 2 118 24 24 ARG HB3 H 1.95 0.02 2 119 24 24 ARG HG2 H 1.73 0.02 1 120 24 24 ARG HG3 H 1.64 0.02 1 121 24 24 ARG HD2 H 3.21 0.02 2 122 24 24 ARG HD3 H 3.21 0.02 2 123 24 24 ARG HE H 7.47 0.02 1 124 25 25 LEU H H 7.98 0.02 1 125 25 25 LEU HA H 4.23 0.02 1 126 25 25 LEU HB2 H 1.78 0.02 2 127 25 25 LEU HB3 H 1.78 0.02 2 128 25 25 LEU HG H 1.62 0.02 1 129 25 25 LEU HD1 H 0.91 0.02 2 130 26 26 NLE H H 8.10 0.02 1 131 26 26 NLE HA H 3.77 0.02 1 132 26 26 NLE HB2 H 1.72 0.02 2 133 26 26 NLE HB3 H 1.72 0.02 2 134 26 26 NLE HD2 H 1.24 0.02 2 135 26 26 NLE HD3 H 1.24 0.02 2 136 26 26 NLE HE1 H 0.81 0.02 2 137 26 26 NLE HE2 H 0.81 0.02 2 138 26 26 NLE HE3 H 0.81 0.02 2 139 26 26 NLE HG2 H 1.56 0.02 2 140 26 26 NLE HG3 H 1.56 0.02 2 141 27 27 GLY H H 7.99 0.02 1 142 27 27 GLY HA2 H 3.94 0.02 1 143 27 27 GLY HA3 H 3.90 0.02 1 144 28 28 ALA H H 8.05 0.02 1 145 28 28 ALA HA H 4.39 0.02 1 146 28 28 ALA HB H 1.41 0.02 1 147 29 29 SER H H 8.26 0.02 1 148 29 29 SER HA H 4.49 0.02 1 149 29 29 SER HB2 H 3.89 0.02 2 150 29 29 SER HB3 H 3.89 0.02 2 151 30 30 GLY H H 8.23 0.02 1 152 30 30 GLY HA2 H 4.10 0.02 2 153 30 30 GLY HA3 H 4.10 0.02 2 154 31 31 PRO HA H 4.44 0.02 1 155 31 31 PRO HB2 H 2.27 0.02 2 156 31 31 PRO HB3 H 2.27 0.02 2 157 31 31 PRO HG2 H 2.01 0.02 1 158 31 31 PRO HG3 H 1.94 0.02 1 159 31 31 PRO HD2 H 3.65 0.02 1 160 31 31 PRO HD3 H 3.61 0.02 1 161 32 32 ASN H H 8.49 0.02 1 162 32 32 ASN HA H 4.68 0.02 1 163 32 32 ASN HB2 H 2.84 0.02 1 164 32 32 ASN HB3 H 2.78 0.02 1 165 32 32 ASN HD21 H 7.62 0.02 1 166 32 32 ASN HD22 H 6.94 0.02 1 167 33 33 LYS H H 8.24 0.02 1 168 33 33 LYS HA H 4.28 0.02 1 169 33 33 LYS HB2 H 1.86 0.02 2 170 33 33 LYS HB3 H 1.86 0.02 2 171 33 33 LYS HG2 H 1.76 0.02 1 172 33 33 LYS HG3 H 1.69 0.02 1 173 33 33 LYS HD2 H 1.45 0.02 1 174 33 33 LYS HD3 H 1.41 0.02 1 175 34 34 LYS H H 8.30 0.02 1 176 34 34 LYS HA H 4.29 0.02 1 177 34 34 LYS HB2 H 1.84 0.02 2 178 34 34 LYS HB3 H 1.84 0.02 2 179 34 34 LYS HG2 H 1.77 0.02 1 180 34 34 LYS HG3 H 1.69 0.02 1 181 34 34 LYS HD2 H 1.46 0.02 1 182 34 34 LYS HD3 H 1.40 0.02 1 183 34 34 LYS HE2 H 3.00 0.02 2 184 34 34 LYS HE3 H 3.00 0.02 2 185 35 35 GLU H H 8.34 0.02 1 186 35 35 GLU HA H 4.38 0.02 1 187 35 35 GLU HB2 H 2.10 0.02 1 188 35 35 GLU HB3 H 1.98 0.02 1 189 35 35 GLU HG2 H 2.39 0.02 2 190 35 35 GLU HG3 H 2.39 0.02 2 191 36 36 SER H H 8.35 0.02 1 192 36 36 SER HA H 4.46 0.02 1 193 36 36 SER HB2 H 3.87 0.02 2 194 36 36 SER HB3 H 3.87 0.02 2 195 37 37 ARG H H 8.42 0.02 1 196 37 37 ARG HA H 4.38 0.02 1 197 37 37 ARG HB2 H 1.91 0.02 1 198 37 37 ARG HB3 H 1.80 0.02 1 199 37 37 ARG HG2 H 1.68 0.02 2 200 37 37 ARG HG3 H 1.68 0.02 2 201 37 37 ARG HD2 H 3.21 0.02 2 202 37 37 ARG HD3 H 3.21 0.02 2 203 38 38 GLY H H 8.42 0.02 1 204 38 38 GLY HA2 H 3.98 0.02 2 205 38 38 GLY HA3 H 3.98 0.02 2 206 39 39 ARG H H 8.34 0.02 1 207 39 39 ARG HA H 4.34 0.02 1 208 39 39 ARG HB2 H 1.91 0.02 1 209 39 39 ARG HB3 H 1.79 0.02 1 210 39 39 ARG HG2 H 1.67 0.02 2 211 39 39 ARG HG3 H 1.67 0.02 2 212 39 39 ARG HD2 H 3.22 0.02 2 213 39 39 ARG HD3 H 3.22 0.02 2 214 40 40 GLY H H 8.48 0.02 1 215 40 40 GLY HA2 H 3.92 0.02 2 216 40 40 GLY HA3 H 3.92 0.02 2 stop_ save_