data_5163 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of desulfovibrio gigas zinc rubredoxin, NMR, 20 structures ; _BMRB_accession_number 5163 _BMRB_flat_file_name bmr5163.str _Entry_type original _Submission_date 2001-10-02 _Accession_date 2001-10-02 _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 Lamosa P. . . 2 Brennan L. . . 3 Vis H. . . 4 Turner D. L. . 5 Santos H. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 248 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-02-14 original author . stop_ _Original_release_date 2002-02-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Structure of Desulfovibrio gigas Rubredoxin: a Model for studying Protein Stabilization by Compatible Solutes ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21556002 _PubMed_ID 11699644 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lamosa P. . . 2 Brennan L. . . 3 Vis H. . . 4 Turner D. L. . 5 Santos H. . . stop_ _Journal_abbreviation Extremophiles _Journal_volume 5 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 303 _Page_last 311 _Year 2001 _Details . loop_ _Keyword iron-sulfur-protein zinc-substitution thermostability stop_ save_ ################################## # Molecular system description # ################################## save_system_Rd _Saveframe_category molecular_system _Mol_system_name RUBREDOXIN _Abbreviation_common Rd _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label rubredoxin $rubredoxin 'zinc ion' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_rubredoxin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common RUBREDOXIN _Name_variant none _Abbreviation_common Rd _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 52 _Mol_residue_sequence ; MDIYVCTVCGYEYDPAKGDP DSGIKPGTKFEDLPDDWACP VCGASKDAFEKQ ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 ILE 4 TYR 5 VAL 6 CYS 7 THR 8 VAL 9 CYS 10 GLY 11 TYR 12 GLU 13 TYR 14 ASP 15 PRO 16 ALA 17 LYS 18 GLY 19 ASP 20 PRO 21 ASP 22 SER 23 GLY 24 ILE 25 LYS 26 PRO 27 GLY 28 THR 29 LYS 30 PHE 31 GLU 32 ASP 33 LEU 34 PRO 35 ASP 36 ASP 37 TRP 38 ALA 39 CYS 40 PRO 41 VAL 42 CYS 43 GLY 44 ALA 45 SER 46 LYS 47 ASP 48 ALA 49 PHE 50 GLU 51 LYS 52 GLN stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 SWISS-PROT P00270 'Rubredoxin (Rd)' 100.00 52 100.00 100.00 4.89e-22 GenBank AAK08075 'rubredoxin [Desulfovibrio gigas]' 100.00 52 100.00 100.00 4.89e-22 PDB 2DSX 'Crystal Structure Of Rubredoxin From Desulfovibrio Gigas To Ultra-High 0.68 A Resolution' 100.00 52 100.00 100.00 4.89e-22 PDB 1RDG 'Rubredoxin From Desulfovibrio Gigas. A Molecular Model Of The Oxidized Form At 1.4 Angstroms Resolution' 100.00 52 100.00 100.00 4.89e-22 PDB 1E8J 'Solution Structure Of Desulfovibrio Gigas Zinc Rubredoxin, Nmr, 20 Structures' 100.00 52 100.00 100.00 4.89e-22 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jun 20 12:12:44 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction $rubredoxin 'Desulfovibrio gigas' 879 Bacteria . Desulfovibrio gigas cytoplasm 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 $rubredoxin 'recombinant technology' 'Escherichia coli' Escherichia coli JM109 . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $rubredoxin 2.5 mM . $ZN 2.5 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H NOESY' _Sample_label $sample_1 save_ save_2D_1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H_COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H COSY' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.6 0.2 n/a temperature 308 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 _Indirect_shift_ratio_citation_label _Reference_correction_type _Correction_value_citation_label H2O H 1 protons ppm 4.651 internal direct spherical internal parallel 1 $entry_citation temperature $entry_citation 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name rubredoxin _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 ASP H H 8.132 0.119 . 2 . 2 ASP HA H 4.855 . . 3 . 2 ASP HB2 H 2.819 0.122 . 4 . 2 ASP HB3 H 2.518 . . 5 . 3 ILE H H 8.293 0.135 . 6 . 3 ILE HA H 4.971 0.076 . 7 . 3 ILE HB H 1.891 0.125 . 8 . 3 ILE HG2 H 0.928 0.141 . 9 . 3 ILE HG12 H 1.419 0.131 . 10 . 3 ILE HD1 H 1.050 0.143 . 11 . 4 TYR HB2 H 2.786 0.120 . 12 . 4 TYR HB3 H 2.585 0.121 . 13 . 4 TYR H H 8.747 0.131 . 14 . 4 TYR HA H 5.264 0.116 . 15 . 4 TYR HD1 H 6.698 0.139 . 16 . 4 TYR HD2 H 6.697 0.139 . 17 . 4 TYR HE1 H 6.794 0.139 . 18 . 4 TYR HE2 H 6.804 0.140 . 19 . 5 VAL H H 9.435 0.121 . 20 . 5 VAL HA H 5.317 0.125 . 21 . 5 VAL HB H 2.079 0.095 . 22 . 5 VAL HG2 H 1.003 0.136 . 23 . 6 CYS H H 9.618 0.124 . 24 . 6 CYS HA H 3.043 0.103 . 25 . 6 CYS HB3 H 3.449 0.228 . 26 . 6 CYS HB2 H 3.081 0.279 . 27 . 7 THR H H 8.530 0.126 . 28 . 7 THR HA H 4.348 0.093 . 29 . 7 THR HB H 3.967 . . 30 . 7 THR HG2 H 1.542 0.140 . 31 . 8 VAL H H 9.336 0.130 . 32 . 8 VAL HA H 3.678 0.303 . 33 . 8 VAL HB H 2.854 0.114 . 34 . 8 VAL HG1 H 1.022 0.140 . 35 . 8 VAL HG2 H 1.010 0.140 . 36 . 9 CYS H H 9.287 0.122 . 37 . 9 CYS HA H 5.251 0.103 . 38 . 9 CYS HB2 H 3.536 0.106 . 39 . 9 CYS HB3 H 2.750 0.105 . 40 . 10 GLY H H 8.187 0.114 . 41 . 10 GLY HA2 H 4.564 0.079 . 42 . 10 GLY HA3 H 3.939 0.096 . 43 . 11 TYR H H 9.624 0.118 . 44 . 11 TYR HA H 4.483 0.086 . 45 . 11 TYR HB2 H 3.518 0.218 . 46 . 11 TYR HB3 H 3.323 0.104 . 47 . 11 TYR HD1 H 7.565 0.139 . 48 . 11 TYR HE1 H 7.276 0.140 . 49 . 11 TYR HE2 H 7.277 0.140 . 50 . 11 TYR HD2 H 7.565 0.139 . 51 . 12 GLU H H 7.470 0.116 . 52 . 12 GLU HA H 5.002 0.070 . 53 . 12 GLU HB2 H 2.008 0.108 . 54 . 12 GLU HB3 H 1.862 0.102 . 55 . 12 GLU HG2 H 2.616 0.072 . 56 . 12 GLU HG3 H 2.174 0.108 . 57 . 13 TYR H H 9.868 0.116 . 58 . 13 TYR HA H 4.822 0.086 . 59 . 13 TYR HB2 H 3.392 0.124 . 60 . 13 TYR HB3 H 3.398 0.122 . 61 . 13 TYR HH H 8.813 0.139 . 62 . 13 TYR HD1 H 7.369 0.138 . 63 . 13 TYR HE1 H 6.550 0.139 . 64 . 13 TYR HE2 H 6.550 0.139 . 65 . 13 TYR HD2 H 7.364 0.138 . 66 . 14 ASP H H 8.535 0.115 . 67 . 14 ASP HB2 H 3.293 0.002 . 68 . 14 ASP HB3 H 3.015 0.089 . 69 . 15 PRO HA H 4.300 0.117 . 70 . 15 PRO HB2 H 2.640 0.103 . 71 . 15 PRO HG2 H 1.666 0.018 . 72 . 15 PRO HD3 H 3.703 0.121 . 73 . 15 PRO HD2 H 3.620 0.168 . 74 . 16 ALA H H 8.416 0.108 . 75 . 16 ALA HA H 4.226 0.114 . 76 . 16 ALA HB H 1.546 0.140 . 77 . 17 LYS H H 7.878 0.121 . 78 . 17 LYS HA H 4.583 0.082 . 79 . 17 LYS HB2 H 2.198 0.093 . 80 . 17 LYS HG2 H 1.738 0.059 . 81 . 17 LYS HG3 H 1.641 0.053 . 82 . 17 LYS HD2 H 2.086 0.065 . 83 . 17 LYS HD3 H 2.024 0.073 . 84 . 17 LYS HE2 H 3.350 0.059 . 85 . 18 GLY H H 8.231 0.119 . 86 . 18 GLY HA2 H 4.090 0.117 . 87 . 18 GLY HA3 H 3.820 0.115 . 88 . 19 ASP H H 8.353 0.118 . 89 . 19 ASP HA H 5.539 0.114 . 90 . 19 ASP HB2 H 3.368 0.114 . 91 . 19 ASP HB3 H 3.161 0.124 . 92 . 20 PRO HA H 4.478 0.092 . 93 . 20 PRO HB2 H 2.457 . . 94 . 20 PRO HG2 H 2.145 . . 95 . 20 PRO HD2 H 4.343 0.100 . 96 . 20 PRO HD3 H 4.049 0.120 . 97 . 21 ASP H H 8.208 0.427 . 98 . 21 ASP HA H 4.410 0.117 . 99 . 21 ASP HB2 H 2.078 . . 100 . 21 ASP HB3 H 1.105 . . 101 . 22 SER HA H 4.784 . . 102 . 22 SER HB2 H 3.529 . . 103 . 23 GLY H H 8.056 0.128 . 104 . 23 GLY HA2 H 4.429 0.094 . 105 . 23 GLY HA3 H 4.015 0.107 . 106 . 24 ILE H H 7.917 0.132 . 107 . 24 ILE HA H 4.544 0.100 . 108 . 24 ILE HB H 2.342 0.123 . 109 . 24 ILE HG2 H 1.039 0.140 . 110 . 24 ILE HG12 H 1.846 0.129 . 111 . 24 ILE HG13 H 1.482 0.125 . 112 . 24 ILE HD1 H 0.871 0.140 . 113 . 25 LYS H H 8.781 0.123 . 114 . 25 LYS HA H 4.723 0.051 . 115 . 25 LYS HB2 H 1.921 0.116 . 116 . 25 LYS HB3 H 1.760 0.108 . 117 . 25 LYS HG2 H 2.065 0.097 . 118 . 26 PRO HA H 4.097 0.068 . 119 . 26 PRO HB2 H 2.630 0.084 . 120 . 26 PRO HB3 H 3.219 0.140 . 121 . 27 GLY H H 9.169 0.120 . 122 . 27 GLY HA2 H 4.531 0.062 . 123 . 27 GLY HA3 H 3.668 0.092 . 124 . 28 THR H H 7.458 0.112 . 125 . 28 THR HA H 4.472 0.109 . 126 . 28 THR HB H 4.083 0.121 . 127 . 28 THR HG2 H 1.192 0.140 . 128 . 28 THR HG1 H 6.373 0.139 . 129 . 29 LYS H H 9.469 0.124 . 130 . 29 LYS HA H 4.491 0.097 . 131 . 29 LYS HB2 H 2.374 0.117 . 132 . 29 LYS HG2 H 2.031 0.077 . 133 . 29 LYS HD2 H 1.888 0.088 . 134 . 29 LYS HE2 H 3.319 0.073 . 135 . 30 PHE H H 9.671 0.116 . 136 . 30 PHE HA H 3.425 0.121 . 137 . 30 PHE HB2 H 2.864 0.128 . 138 . 30 PHE HB3 H 2.452 0.130 . 139 . 30 PHE HZ H 7.066 0.125 . 140 . 30 PHE HD1 H 6.220 0.140 . 141 . 30 PHE HE1 H 6.577 0.140 . 142 . 30 PHE HE2 H 6.579 0.140 . 143 . 30 PHE HD2 H 6.221 0.140 . 144 . 31 GLU H H 9.821 0.123 . 145 . 31 GLU HA H 4.034 0.097 . 146 . 31 GLU HB2 H 2.293 0.077 . 147 . 31 GLU HB3 H 2.159 0.077 . 148 . 31 GLU HG2 H 2.617 0.073 . 149 . 31 GLU HG3 H 2.539 0.065 . 150 . 32 ASP H H 7.612 0.108 . 151 . 32 ASP HA H 4.876 0.051 . 152 . 32 ASP HB3 H 3.048 0.100 . 153 . 32 ASP HB2 H 2.730 0.109 . 154 . 33 LEU H H 7.243 0.119 . 155 . 33 LEU HA H 4.037 0.100 . 156 . 33 LEU HB2 H 0.840 0.121 . 157 . 33 LEU HB3 H 0.506 0.126 . 158 . 33 LEU HG H 1.002 0.121 . 159 . 33 LEU HD2 H -0.091 0.139 . 160 . 33 LEU HD1 H -1.507 0.140 . 161 . 34 PRO HA H 4.396 . . 162 . 34 PRO HB2 H 2.377 0.110 . 163 . 34 PRO HB3 H 2.134 0.088 . 164 . 34 PRO HD2 H 3.459 0.117 . 165 . 34 PRO HD3 H 3.938 0.118 . 166 . 35 ASP H H 8.197 0.287 . 167 . 36 ASP H H 8.416 0.110 . 168 . 36 ASP HA H 4.821 0.106 . 169 . 37 TRP H H 7.846 0.105 . 170 . 37 TRP HA H 4.333 0.110 . 171 . 37 TRP HB2 H 3.170 0.110 . 172 . 37 TRP HB3 H 3.092 0.105 . 173 . 37 TRP HD1 H 7.395 0.129 . 174 . 37 TRP HZ2 H 7.476 0.133 . 175 . 37 TRP HE1 H 10.884 0.139 . 176 . 37 TRP HH2 H 7.142 0.129 . 177 . 37 TRP HE3 H 6.839 0.123 . 178 . 37 TRP HZ3 H 6.077 0.128 . 179 . 38 ALA H H 6.708 0.109 . 180 . 38 ALA HA H 4.647 0.088 . 181 . 38 ALA HB H 0.984 0.140 . 182 . 39 CYS H H 9.162 0.124 . 183 . 39 CYS HA H 4.047 0.116 . 184 . 39 CYS HB2 H 3.368 0.125 . 185 . 39 CYS HB3 H 3.297 0.115 . 186 . 40 PRO HA H 4.188 0.142 . 187 . 40 PRO HB2 H 1.605 0.121 . 188 . 40 PRO HB3 H 2.132 0.133 . 189 . 40 PRO HG3 H 2.151 0.124 . 190 . 40 PRO HG2 H 2.475 0.344 . 191 . 40 PRO HD3 H 3.687 0.121 . 192 . 40 PRO HD2 H 3.292 0.123 . 193 . 41 VAL H H 8.864 0.124 . 194 . 41 VAL HA H 3.901 0.138 . 195 . 41 VAL HB H 2.987 0.114 . 196 . 41 VAL HG2 H 1.087 0.140 . 197 . 41 VAL HG1 H 1.071 0.140 . 198 . 42 CYS H H 8.963 0.123 . 199 . 42 CYS HA H 5.164 0.098 . 200 . 42 CYS HB2 H 3.484 0.106 . 201 . 42 CYS HB3 H 2.769 0.088 . 202 . 43 GLY H H 8.155 0.115 . 203 . 43 GLY HA2 H 4.117 0.325 . 204 . 43 GLY HA3 H 3.953 0.138 . 205 . 44 ALA H H 9.373 0.128 . 206 . 44 ALA HA H 4.429 0.117 . 207 . 44 ALA HB H 1.703 0.140 . 208 . 45 SER H H 8.354 0.123 . 209 . 45 SER HA H 4.837 0.076 . 210 . 45 SER HB2 H 4.678 0.065 . 211 . 45 SER HB3 H 4.357 0.106 . 212 . 46 LYS H H 8.970 0.117 . 213 . 46 LYS HA H 4.477 0.108 . 214 . 46 LYS HB3 H 2.191 0.076 . 215 . 46 LYS HB2 H 2.704 0.418 . 216 . 46 LYS HG2 H 2.116 0.076 . 217 . 46 LYS HG3 H 1.405 0.104 . 218 . 46 LYS HD2 H 1.569 0.103 . 219 . 47 ASP H H 8.545 0.105 . 220 . 47 ASP HA H 5.399 0.107 . 221 . 47 ASP HB2 H 2.973 0.120 . 222 . 47 ASP HB3 H 2.596 0.114 . 223 . 48 ALA H H 8.608 0.121 . 224 . 48 ALA HB H 1.823 0.141 . 225 . 49 PHE H H 8.398 0.119 . 226 . 49 PHE HA H 5.617 0.120 . 227 . 49 PHE HZ H 7.932 0.132 . 228 . 49 PHE HB2 H 4.010 0.113 . 229 . 49 PHE HB3 H 2.776 0.123 . 230 . 49 PHE HD1 H 7.586 0.139 . 231 . 49 PHE HE1 H 7.767 0.139 . 232 . 49 PHE HE2 H 7.767 0.139 . 233 . 49 PHE HD2 H 7.587 0.139 . 234 . 50 GLU H H 9.264 0.122 . 235 . 50 GLU HA H 5.079 0.058 . 236 . 50 GLU HB2 H 2.166 0.102 . 237 . 50 GLU HB3 H 2.072 0.084 . 238 . 50 GLU HG2 H 2.536 0.057 . 239 . 51 LYS H H 8.778 0.116 . 240 . 51 LYS HA H 3.624 0.102 . 241 . 51 LYS HB2 H 1.722 0.066 . 242 . 51 LYS HB3 H 1.456 0.106 . 243 . 51 LYS HG2 H 1.049 0.110 . 244 . 51 LYS HD2 H 1.842 0.073 . 245 . 51 LYS HE2 H 3.206 0.065 . 246 . 52 GLN H H 8.539 0.121 . 247 . 52 GLN HB2 H 1.819 . . 248 . 52 GLN HB3 H 1.716 . . stop_ save_