data_18370 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H and 15N Chemical Shift Assignments for Hen Egg White Lysozyme mutant W123G. ; _BMRB_accession_number 18370 _BMRB_flat_file_name bmr18370.str _Entry_type original _Submission_date 2012-03-29 _Accession_date 2012-03-29 _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 Sziegat Friederike . . 2 Silvers Robert . . 3 Haehnke Martin . . 4 Jensen Malene R. . 5 Blackledge Martin . . 6 Wirmer-Bartoschek Julia . . 7 Schwalbe Harald . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 125 "15N chemical shifts" 125 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-11 update BMRB 'update entry citation' 2012-04-18 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 18365 WT-ALA 18366 W28G 18367 W62G 18368 W108G 18369 W111G stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Disentangling the coil: modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22468860 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sziegat Friederike . . 2 Silvers Robert . . 3 Hahnke Martin . . 4 Jensen 'Malene Ringkjbing' . . 5 Blackledge Martin . . 6 Wirmer-Bartoschek Julia . . 7 Schwalbe Harald . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 51 _Journal_issue 16 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3361 _Page_last 3372 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name W123G _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label W123G $W123G stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_W123G _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common W123G _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 129 _Mol_residue_sequence ; KVFGRAELAAAMKRHGLDNY RGYSLGNWVAAAKFESNFNT QATNRNTDGSTDYGILQINS RWWANDGRTPGSRNLANIPA SALLSSDITASVNAAKKIVS DGNGMNAWVAWRNRAKGTDV QAGIRGARL ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 VAL 3 PHE 4 GLY 5 ARG 6 ALA 7 GLU 8 LEU 9 ALA 10 ALA 11 ALA 12 MET 13 LYS 14 ARG 15 HIS 16 GLY 17 LEU 18 ASP 19 ASN 20 TYR 21 ARG 22 GLY 23 TYR 24 SER 25 LEU 26 GLY 27 ASN 28 TRP 29 VAL 30 ALA 31 ALA 32 ALA 33 LYS 34 PHE 35 GLU 36 SER 37 ASN 38 PHE 39 ASN 40 THR 41 GLN 42 ALA 43 THR 44 ASN 45 ARG 46 ASN 47 THR 48 ASP 49 GLY 50 SER 51 THR 52 ASP 53 TYR 54 GLY 55 ILE 56 LEU 57 GLN 58 ILE 59 ASN 60 SER 61 ARG 62 TRP 63 TRP 64 ALA 65 ASN 66 ASP 67 GLY 68 ARG 69 THR 70 PRO 71 GLY 72 SER 73 ARG 74 ASN 75 LEU 76 ALA 77 ASN 78 ILE 79 PRO 80 ALA 81 SER 82 ALA 83 LEU 84 LEU 85 SER 86 SER 87 ASP 88 ILE 89 THR 90 ALA 91 SER 92 VAL 93 ASN 94 ALA 95 ALA 96 LYS 97 LYS 98 ILE 99 VAL 100 SER 101 ASP 102 GLY 103 ASN 104 GLY 105 MET 106 ASN 107 ALA 108 TRP 109 VAL 110 ALA 111 TRP 112 ARG 113 ASN 114 ARG 115 ALA 116 LYS 117 GLY 118 THR 119 ASP 120 VAL 121 GLN 122 ALA 123 GLY 124 ILE 125 ARG 126 GLY 127 ALA 128 ARG 129 LEU 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 BMRB 11051 0SS-variant 100.00 130 98.45 99.22 1.17e-83 BMRB 11459 1SS[6-127] 100.00 130 97.67 97.67 2.30e-83 BMRB 11460 1SS[30-115] 100.00 130 96.90 97.67 6.34e-83 BMRB 11461 1SS[64-80] 100.00 130 96.90 97.67 6.34e-83 BMRB 11462 1SS[76-94] 100.00 130 96.90 97.67 6.34e-83 BMRB 15198 all-Ala-Hen_egg_white_lysoyzme 100.00 130 99.22 99.22 4.23e-84 BMRB 18365 WT-ALA 100.00 129 99.22 99.22 4.82e-84 BMRB 18366 W28G 100.00 129 98.45 98.45 3.22e-82 BMRB 18367 W62G 100.00 129 98.45 98.45 3.22e-82 BMRB 18368 W108G 100.00 129 98.45 98.45 3.22e-82 BMRB 18369 W111G 100.00 129 98.45 98.45 3.22e-82 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $W123G Chicken 9031 Eukaryota Metazoa Gallus gallus 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 $W123G 'recombinant technology' . Escherichia coli . pET11a 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 $W123G 300 uM '[U-99% 15N]' H2O 49.95 M 'natural abundance' D2O 5.55 M [U-2H] stop_ save_ ############################ # Computer software used # ############################ 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_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . 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_3D_1H-15N_NOESY_2 _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 2.0 . pH pressure 1 . atm temperature 293 . 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' '3D 1H-15N 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 W123G _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 H H 8.567 0.014 1 2 1 1 LYS N N 124.83 0.380 1 3 2 2 VAL H H 8.103 0.014 1 4 2 2 VAL N N 122.39 0.380 1 5 3 3 PHE H H 8.36 0.014 1 6 3 3 PHE N N 124.91 0.380 1 7 4 4 GLY H H 8.218 0.014 1 8 4 4 GLY N N 110.54 0.380 1 9 5 5 ARG H H 8.163 0.014 1 10 5 5 ARG N N 120.97 0.380 1 11 6 6 ALA H H 8.344 0.014 1 12 6 6 ALA N N 124.21 0.380 1 13 7 7 GLU H H 8.082 0.014 1 14 7 7 GLU N N 119.4 0.380 1 15 8 8 LEU H H 8.025 0.014 1 16 8 8 LEU N N 122.94 0.380 1 17 10 10 ALA H H 7.908 0.014 1 18 10 10 ALA N N 121.56 0.380 1 19 11 11 ALA H H 7.965 0.014 1 20 11 11 ALA N N 121.88 0.380 1 21 12 12 MET H H 7.954 0.014 1 22 12 12 MET N N 118.23 0.380 1 23 13 13 LYS H H 7.926 0.014 1 24 13 13 LYS N N 121.53 0.380 1 25 14 14 ARG H H 8.003 0.014 1 26 14 14 ARG N N 120.89 0.380 1 27 15 15 HIS H H 8.331 0.014 1 28 15 15 HIS N N 118.93 0.380 1 29 16 16 GLY H H 8.292 0.014 1 30 16 16 GLY N N 109.87 0.380 1 31 17 17 LEU H H 8.061 0.014 1 32 17 17 LEU N N 121.48 0.380 1 33 18 18 ASP H H 8.388 0.014 1 34 18 18 ASP N N 119.12 0.380 1 35 19 19 ASN H H 8.162 0.014 1 36 19 19 ASN N N 118.91 0.380 1 37 20 20 TYR H H 7.931 0.014 1 38 20 20 TYR N N 120.49 0.380 1 39 21 21 ARG H H 8.102 0.014 1 40 21 21 ARG N N 123.24 0.380 1 41 22 22 GLY H H 7.647 0.014 1 42 22 22 GLY N N 108.64 0.380 1 43 23 23 TYR H H 7.816 0.014 1 44 23 23 TYR N N 119.76 0.380 1 45 24 24 SER H H 8.13 0.014 1 46 24 24 SER N N 117.48 0.380 1 47 25 25 LEU H H 8.077 0.014 1 48 25 25 LEU N N 123.89 0.380 1 49 26 26 GLY H H 8.09 0.014 1 50 26 26 GLY N N 108.34 0.380 1 51 27 27 ASN H H 8.056 0.014 1 52 27 27 ASN N N 118.68 0.380 1 53 28 28 TRP H H 7.939 0.014 1 54 28 28 TRP N N 121.7 0.380 1 55 29 29 VAL H H 7.606 0.014 1 56 29 29 VAL N N 122.1 0.380 1 57 30 30 ALA H H 7.896 0.014 1 58 30 30 ALA N N 126.28 0.380 1 59 31 31 ALA H H 7.939 0.014 1 60 31 31 ALA N N 122.47 0.380 1 61 32 32 ALA H H 7.962 0.014 1 62 32 32 ALA N N 122.46 0.380 1 63 33 33 LYS H H 7.925 0.014 1 64 33 33 LYS N N 119.39 0.380 1 65 34 34 PHE H H 7.955 0.014 1 66 34 34 PHE N N 120.23 0.380 1 67 35 35 GLU H H 8.013 0.014 1 68 35 35 GLU N N 121.41 0.380 1 69 36 36 SER H H 8.132 0.014 1 70 36 36 SER N N 116.48 0.380 1 71 37 37 ASN H H 8.222 0.014 1 72 37 37 ASN N N 120 0.380 1 73 38 38 PHE H H 8.013 0.014 1 74 38 38 PHE N N 120.2 0.380 1 75 39 39 ASN H H 8.21 0.014 1 76 39 39 ASN N N 120 0.380 1 77 40 40 THR H H 7.98 0.014 1 78 40 40 THR N N 114.32 0.380 1 79 41 41 GLN H H 8.198 0.014 1 80 41 41 GLN N N 121.93 0.380 1 81 42 42 ALA H H 8.141 0.014 1 82 42 42 ALA N N 124.67 0.380 1 83 43 43 THR H H 7.957 0.014 1 84 43 43 THR N N 112.55 0.380 1 85 44 44 ASN H H 8.232 0.014 1 86 44 44 ASN N N 120.78 0.380 1 87 45 45 ARG H H 8.195 0.014 1 88 45 45 ARG N N 121.25 0.380 1 89 46 46 ASN H H 8.364 0.014 1 90 46 46 ASN N N 119.46 0.380 1 91 47 47 THR H H 8.038 0.014 1 92 47 47 THR N N 113.89 0.380 1 93 48 48 ASP H H 8.371 0.014 1 94 48 48 ASP N N 120.71 0.380 1 95 49 49 GLY H H 8.251 0.014 1 96 49 49 GLY N N 109.35 0.380 1 97 50 50 SER H H 8.041 0.014 1 98 50 50 SER N N 115.38 0.380 1 99 51 51 THR H H 8.071 0.014 1 100 51 51 THR N N 115.47 0.380 1 101 52 52 ASP H H 8.249 0.014 1 102 52 52 ASP N N 120.83 0.380 1 103 53 53 TYR H H 7.989 0.014 1 104 53 53 TYR N N 120.72 0.380 1 105 54 54 GLY H H 8.143 0.014 1 106 54 54 GLY N N 109.63 0.380 1 107 55 55 ILE H H 7.705 0.014 1 108 55 55 ILE N N 119.56 0.380 1 109 56 56 LEU H H 8.075 0.014 1 110 56 56 LEU N N 124.73 0.380 1 111 57 57 GLN H H 8.133 0.014 1 112 57 57 GLN N N 121.16 0.380 1 113 58 58 ILE H H 7.948 0.014 1 114 58 58 ILE N N 121.3 0.380 1 115 59 59 ASN H H 8.223 0.014 1 116 59 59 ASN N N 121.44 0.380 1 117 60 60 SER H H 8.061 0.014 1 118 60 60 SER N N 116.15 0.380 1 119 61 61 ARG H H 8.094 0.014 1 120 61 61 ARG N N 122.07 0.380 1 121 62 62 TRP H H 7.684 0.014 1 122 62 62 TRP N N 120.53 0.380 1 123 63 63 TRP H H 7.26 0.014 1 124 63 63 TRP N N 120.63 0.380 1 125 64 64 ALA H H 7.589 0.014 1 126 64 64 ALA N N 123.98 0.380 1 127 65 65 ASN H H 7.973 0.014 1 128 65 65 ASN N N 116.88 0.380 1 129 66 66 ASP H H 8.198 0.014 1 130 66 66 ASP N N 118.31 0.380 1 131 67 67 GLY H H 8.187 0.014 1 132 67 67 GLY N N 108.24 0.380 1 133 68 68 ARG H H 7.836 0.014 1 134 68 68 ARG N N 119.75 0.380 1 135 69 69 THR H H 8.097 0.014 1 136 69 69 THR N N 116.94 0.380 1 137 71 71 GLY H H 8.34 0.014 1 138 71 71 GLY N N 109.19 0.380 1 139 72 72 SER H H 7.991 0.014 1 140 72 72 SER N N 115.37 0.380 1 141 73 73 ARG H H 8.28 0.014 1 142 73 73 ARG N N 122.47 0.380 1 143 74 74 ASN H H 8.298 0.014 1 144 74 74 ASN N N 119.56 0.380 1 145 75 75 LEU H H 8.119 0.014 1 146 75 75 LEU N N 122.99 0.380 1 147 76 76 ALA H H 8.049 0.014 1 148 76 76 ALA N N 123.32 0.380 1 149 77 77 ASN H H 8.137 0.014 1 150 77 77 ASN N N 117.16 0.380 1 151 78 78 ILE H H 7.87 0.014 1 152 78 78 ILE N N 122.62 0.380 1 153 80 80 ALA H H 8.348 0.014 1 154 80 80 ALA N N 124.37 0.380 1 155 81 81 SER H H 8.111 0.014 1 156 81 81 SER N N 113.63 0.380 1 157 82 82 ALA H H 8.09 0.014 1 158 82 82 ALA N N 125.68 0.380 1 159 83 83 LEU H H 7.839 0.014 1 160 83 83 LEU N N 120.17 0.380 1 161 84 84 LEU H H 7.898 0.014 1 162 84 84 LEU N N 121.9 0.380 1 163 85 85 SER H H 8.088 0.014 1 164 85 85 SER N N 115.85 0.380 1 165 86 86 SER H H 8.117 0.014 1 166 86 86 SER N N 117.05 0.380 1 167 87 87 ASP H H 8.275 0.014 1 168 87 87 ASP N N 120.68 0.380 1 169 88 88 ILE H H 7.938 0.014 1 170 88 88 ILE N N 121.16 0.380 1 171 89 89 THR H H 8.02 0.014 1 172 89 89 THR N N 117.83 0.380 1 173 90 90 ALA H H 8.117 0.014 1 174 90 90 ALA N N 126.08 0.380 1 175 91 91 SER H H 8.138 0.014 1 176 91 91 SER N N 115.22 0.380 1 177 92 92 VAL H H 8.029 0.014 1 178 92 92 VAL N N 121.86 0.380 1 179 93 93 ASN H H 8.285 0.014 1 180 93 93 ASN N N 121.36 0.380 1 181 94 94 ALA H H 8.078 0.014 1 182 94 94 ALA N N 124.48 0.380 1 183 95 95 ALA H H 8.01 0.014 1 184 95 95 ALA N N 122.36 0.380 1 185 96 96 LYS H H 7.963 0.014 1 186 96 96 LYS N N 119.96 0.380 1 187 97 97 LYS H H 8.079 0.014 1 188 97 97 LYS N N 122.59 0.380 1 189 98 98 ILE H H 8.093 0.014 1 190 98 98 ILE N N 123.17 0.380 1 191 99 99 VAL H H 8.172 0.014 1 192 99 99 VAL N N 125.26 0.380 1 193 100 100 SER H H 8.312 0.014 1 194 100 100 SER N N 119.56 0.380 1 195 101 101 ASP H H 8.442 0.014 1 196 101 101 ASP N N 121.31 0.380 1 197 102 102 GLY H H 8.282 0.014 1 198 102 102 GLY N N 109.21 0.380 1 199 103 103 ASN H H 8.225 0.014 1 200 103 103 ASN N N 118.48 0.380 1 201 104 104 GLY H H 8.352 0.014 1 202 104 104 GLY N N 109.16 0.380 1 203 105 105 MET H H 8.079 0.014 1 204 105 105 MET N N 119.72 0.380 1 205 106 106 ASN H H 8.272 0.014 1 206 106 106 ASN N N 119.22 0.380 1 207 107 107 ALA H H 8.071 0.014 1 208 107 107 ALA N N 123.7 0.380 1 209 108 108 TRP H H 7.911 0.014 1 210 108 108 TRP N N 119.63 0.380 1 211 109 109 VAL H H 7.604 0.014 1 212 109 109 VAL N N 121.12 0.380 1 213 110 110 ALA H H 7.9 0.014 1 214 110 110 ALA N N 124.75 0.380 1 215 111 111 TRP H H 7.762 0.014 1 216 111 111 TRP N N 119 0.380 1 217 112 112 ARG H H 7.822 0.014 1 218 112 112 ARG N N 120.99 0.380 1 219 113 113 ASN H H 7.983 0.014 1 220 113 113 ASN N N 118.06 0.380 1 221 114 114 ARG H H 7.814 0.014 1 222 114 114 ARG N N 120.99 0.380 1 223 115 115 ALA H H 8.064 0.014 1 224 115 115 ALA N N 124.48 0.380 1 225 116 116 LYS H H 8.105 0.014 1 226 116 116 LYS N N 120.42 0.380 1 227 117 117 GLY H H 8.239 0.014 1 228 117 117 GLY N N 109.68 0.380 1 229 118 118 THR H H 7.939 0.014 1 230 118 118 THR N N 113.18 0.380 1 231 119 119 ASP H H 8.456 0.014 1 232 119 119 ASP N N 121.46 0.380 1 233 120 120 VAL H H 7.86 0.014 1 234 120 120 VAL N N 120.14 0.380 1 235 121 121 GLN H H 8.324 0.014 1 236 121 121 GLN N N 123.88 0.380 1 237 123 123 GLY H H 8.209 0.014 1 238 123 123 GLY N N 107.86 0.380 1 239 124 124 ILE H H 8.178 0.014 1 240 124 124 ILE N N 125 0.380 1 241 125 125 ARG H H 8.372 0.014 1 242 125 125 ARG N N 125.14 0.380 1 243 126 126 GLY H H 8.269 0.014 1 244 126 126 GLY N N 110.25 0.380 1 245 127 127 ALA H H 7.977 0.014 1 246 127 127 ALA N N 123.62 0.380 1 247 128 128 ARG H H 8.212 0.014 1 248 128 128 ARG N N 120.36 0.380 1 249 129 129 LEU H H 8.29 0.014 1 250 129 129 LEU N N 124.63 0.380 1 stop_ save_