data_18368 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H and 15N Chemical Shift Assignments for Hen Egg White Lysozyme mutant W108G. ; _BMRB_accession_number 18368 _BMRB_flat_file_name bmr18368.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" 121 "15N chemical shifts" 121 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 18369 W111G 18370 W123G 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 W108G _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label W108G $W108G 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_W108G _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common W108G _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 129 _Mol_residue_sequence ; KVFGRAELAAAMKRHGLDNY RGYSLGNWVAAAKFESNFNT QATNRNTDGSTDYGILQINS RWWANDGRTPGSRNLANIPA SALLSSDITASVNAAKKIVS DGNGMNAGVAWRNRAKGTDV QAWIRGARL ; 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 GLY 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 TRP 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 18369 W111G 100.00 129 98.45 98.45 3.22e-82 BMRB 18370 W123G 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 $W108G 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 $W108G '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 $W108G 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 W108G _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 8.71 0.014 1 2 1 1 LYS N N 126.22 0.380 1 3 2 2 VAL H H 8.24 0.014 1 4 2 2 VAL N N 123.67 0.380 1 5 3 3 PHE H H 8.49 0.014 1 6 3 3 PHE N N 126.13 0.380 1 7 4 4 GLY H H 8.34 0.014 1 8 4 4 GLY N N 111.87 0.380 1 9 5 5 ARG H H 8.31 0.014 1 10 5 5 ARG N N 122.35 0.380 1 11 6 6 ALA H H 8.49 0.014 1 12 6 6 ALA N N 125.31 0.380 1 13 7 7 GLU H H 8.19 0.014 1 14 7 7 GLU N N 120.61 0.380 1 15 8 8 LEU H H 8.15 0.014 1 16 8 8 LEU N N 124.12 0.380 1 17 10 10 ALA H H 8.09 0.014 1 18 10 10 ALA N N 123 0.380 1 19 12 12 MET H H 8.09 0.014 1 20 12 12 MET N N 119.39 0.380 1 21 14 14 ARG H H 8.15 0.014 1 22 14 14 ARG N N 122.43 0.380 1 23 15 15 HIS H H 8.42 0.014 1 24 15 15 HIS N N 119.93 0.380 1 25 16 16 GLY H H 8.39 0.014 1 26 16 16 GLY N N 111.01 0.380 1 27 17 17 LEU H H 8.19 0.014 1 28 17 17 LEU N N 122.78 0.380 1 29 18 18 ASP H H 8.53 0.014 1 30 18 18 ASP N N 120.27 0.380 1 31 19 19 ASN H H 8.28 0.014 1 32 19 19 ASN N N 120.14 0.380 1 33 20 20 TYR H H 8.08 0.014 1 34 20 20 TYR N N 121.76 0.380 1 35 21 21 ARG H H 8.24 0.014 1 36 21 21 ARG N N 124.47 0.380 1 37 22 22 GLY H H 7.79 0.014 1 38 22 22 GLY N N 109.91 0.380 1 39 23 23 TYR H H 7.94 0.014 1 40 23 23 TYR N N 121.08 0.380 1 41 24 24 SER H H 8.27 0.014 1 42 24 24 SER N N 118.74 0.380 1 43 25 25 LEU H H 8.22 0.014 1 44 25 25 LEU N N 125.19 0.380 1 45 26 26 GLY H H 8.23 0.014 1 46 26 26 GLY N N 109.58 0.380 1 47 27 27 ASN H H 8.17 0.014 1 48 27 27 ASN N N 119.71 0.380 1 49 28 28 TRP H H 8.05 0.014 1 50 28 28 TRP N N 122.93 0.380 1 51 29 29 VAL H H 7.76 0.014 1 52 29 29 VAL N N 123.22 0.380 1 53 30 30 ALA H H 8.02 0.014 1 54 30 30 ALA N N 127.27 0.380 1 55 32 32 ALA H H 8.08 0.014 1 56 32 32 ALA N N 123.57 0.380 1 57 33 33 LYS H H 8.05 0.014 1 58 33 33 LYS N N 120.51 0.380 1 59 34 34 PHE H H 8.08 0.014 1 60 34 34 PHE N N 121.39 0.380 1 61 36 36 SER H H 8.25 0.014 1 62 36 36 SER N N 117.67 0.380 1 63 37 37 ASN H H 8.32 0.014 1 64 37 37 ASN N N 121.25 0.380 1 65 38 38 PHE H H 8.14 0.014 1 66 38 38 PHE N N 121.45 0.380 1 67 39 39 ASN H H 8.34 0.014 1 68 39 39 ASN N N 121.23 0.380 1 69 40 40 THR H H 8.12 0.014 1 70 40 40 THR N N 115.58 0.380 1 71 41 41 GLN H H 8.33 0.014 1 72 41 41 GLN N N 123.17 0.380 1 73 42 42 ALA H H 8.27 0.014 1 74 42 42 ALA N N 125.93 0.380 1 75 43 43 THR H H 8.09 0.014 1 76 43 43 THR N N 113.82 0.380 1 77 44 44 ASN H H 8.37 0.014 1 78 44 44 ASN N N 122.05 0.380 1 79 45 45 ARG H H 8.32 0.014 1 80 45 45 ARG N N 122.51 0.380 1 81 46 46 ASN H H 8.5 0.014 1 82 46 46 ASN N N 120.72 0.380 1 83 47 47 THR H H 8.17 0.014 1 84 47 47 THR N N 115.19 0.380 1 85 48 48 ASP H H 8.52 0.014 1 86 48 48 ASP N N 121.97 0.380 1 87 49 49 GLY H H 8.39 0.014 1 88 49 49 GLY N N 110.67 0.380 1 89 50 50 SER H H 8.17 0.014 1 90 50 50 SER N N 116.71 0.380 1 91 51 51 THR H H 8.21 0.014 1 92 51 51 THR N N 116.8 0.380 1 93 52 52 ASP H H 8.39 0.014 1 94 52 52 ASP N N 122.13 0.380 1 95 53 53 TYR H H 8.13 0.014 1 96 53 53 TYR N N 122 0.380 1 97 54 54 GLY H H 8.28 0.014 1 98 54 54 GLY N N 110.93 0.380 1 99 55 55 ILE H H 7.85 0.014 1 100 55 55 ILE N N 120.88 0.380 1 101 56 56 LEU H H 8.24 0.014 1 102 56 56 LEU N N 125.92 0.380 1 103 57 57 GLN H H 8.27 0.014 1 104 57 57 GLN N N 122.41 0.380 1 105 58 58 ILE H H 8.09 0.014 1 106 58 58 ILE N N 122.53 0.380 1 107 59 59 ASN H H 8.35 0.014 1 108 59 59 ASN N N 122.73 0.380 1 109 60 60 SER H H 8.2 0.014 1 110 60 60 SER N N 117.48 0.380 1 111 61 61 ARG H H 8.24 0.014 1 112 61 61 ARG N N 123.4 0.380 1 113 62 62 TRP H H 7.82 0.014 1 114 62 62 TRP N N 121.83 0.380 1 115 63 63 TRP H H 7.39 0.014 1 116 63 63 TRP N N 121.77 0.380 1 117 64 64 ALA H H 7.72 0.014 1 118 64 64 ALA N N 125.24 0.380 1 119 65 65 ASN H H 8.12 0.014 1 120 65 65 ASN N N 118.2 0.380 1 121 66 66 ASP H H 8.34 0.014 1 122 66 66 ASP N N 119.59 0.380 1 123 67 67 GLY H H 8.32 0.014 1 124 67 67 GLY N N 109.55 0.380 1 125 68 68 ARG H H 7.96 0.014 1 126 68 68 ARG N N 121.09 0.380 1 127 69 69 THR H H 8.24 0.014 1 128 69 69 THR N N 118.23 0.380 1 129 71 71 GLY H H 8.13 0.014 1 130 71 71 GLY N N 116.72 0.380 1 131 72 72 SER H H 8.41 0.014 1 132 72 72 SER N N 123.79 0.380 1 133 73 73 ARG H H 8.44 0.014 1 134 73 73 ARG N N 120.84 0.380 1 135 74 74 ASN H H 8.18 0.014 1 136 74 74 ASN N N 122.72 0.380 1 137 75 75 LEU H H 8.25 0.014 1 138 75 75 LEU N N 124.26 0.380 1 139 76 76 ALA H H 8.19 0.014 1 140 76 76 ALA N N 124.54 0.380 1 141 77 77 ASN H H 8.27 0.014 1 142 77 77 ASN N N 118.41 0.380 1 143 78 78 ILE H H 8 0.014 1 144 78 78 ILE N N 123.88 0.380 1 145 80 80 ALA H H 8.49 0.014 1 146 80 80 ALA N N 125.71 0.380 1 147 81 81 SER H H 8.25 0.014 1 148 81 81 SER N N 114.85 0.380 1 149 82 82 ALA H H 8.21 0.014 1 150 82 82 ALA N N 126.94 0.380 1 151 83 83 LEU H H 7.96 0.014 1 152 83 83 LEU N N 121.44 0.380 1 153 84 84 LEU H H 8.03 0.014 1 154 84 84 LEU N N 123.08 0.380 1 155 85 85 SER H H 8.22 0.014 1 156 85 85 SER N N 117.11 0.380 1 157 86 86 SER H H 8.25 0.014 1 158 86 86 SER N N 118.35 0.380 1 159 87 87 ASP H H 8.41 0.014 1 160 87 87 ASP N N 121.97 0.380 1 161 88 88 ILE H H 8.08 0.014 1 162 88 88 ILE N N 122.48 0.380 1 163 89 89 THR H H 8.16 0.014 1 164 89 89 THR N N 119.13 0.380 1 165 90 90 ALA H H 8.26 0.014 1 166 90 90 ALA N N 127.38 0.380 1 167 91 91 SER H H 8.28 0.014 1 168 91 91 SER N N 116.58 0.380 1 169 92 92 VAL H H 8.17 0.014 1 170 92 92 VAL N N 123.17 0.380 1 171 93 93 ASN H H 8.43 0.014 1 172 93 93 ASN N N 122.68 0.380 1 173 94 94 ALA H H 8.21 0.014 1 174 94 94 ALA N N 125.87 0.380 1 175 95 95 ALA H H 8.16 0.014 1 176 95 95 ALA N N 123.7 0.380 1 177 96 96 LYS H H 8.11 0.014 1 178 96 96 LYS N N 121.32 0.380 1 179 97 97 LYS H H 8.22 0.014 1 180 97 97 LYS N N 123.95 0.380 1 181 98 98 ILE H H 8.23 0.014 1 182 98 98 ILE N N 124.45 0.380 1 183 99 99 VAL H H 8.32 0.014 1 184 99 99 VAL N N 126.33 0.380 1 185 100 100 SER H H 8.45 0.014 1 186 100 100 SER N N 120.92 0.380 1 187 101 101 ASP H H 8.59 0.014 1 188 101 101 ASP N N 122.61 0.380 1 189 102 102 GLY H H 8.42 0.014 1 190 102 102 GLY N N 110.57 0.380 1 191 103 103 ASN H H 8.36 0.014 1 192 103 103 ASN N N 119.8 0.380 1 193 104 104 GLY H H 8.48 0.014 1 194 104 104 GLY N N 110.47 0.380 1 195 105 105 MET H H 8.21 0.014 1 196 105 105 MET N N 120.88 0.380 1 197 106 106 ASN H H 8.19 0.014 1 198 106 106 ASN N N 120.01 0.380 1 199 107 107 ALA H H 8.21 0.014 1 200 107 107 ALA N N 124.72 0.380 1 201 108 108 GLY H H 8.4 0.014 1 202 108 108 GLY N N 109.01 0.380 1 203 109 109 VAL H H 7.89 0.014 1 204 109 109 VAL N N 122.57 0.380 1 205 110 110 ALA H H 8.36 0.014 1 206 110 110 ALA N N 127.53 0.380 1 207 111 111 TRP H H 7.94 0.014 1 208 111 111 TRP N N 120.28 0.380 1 209 112 112 ARG H H 8.04 0.014 1 210 112 112 ARG N N 122.54 0.380 1 211 113 113 ASN H H 8.03 0.014 1 212 113 113 ASN N N 122.52 0.380 1 213 114 114 ARG H H 8.18 0.014 1 214 114 114 ARG N N 125.62 0.380 1 215 115 115 ALA H H 8.26 0.014 1 216 115 115 ALA N N 121.83 0.380 1 217 116 116 LYS H H 8.4 0.014 1 218 116 116 LYS N N 111.08 0.380 1 219 117 117 GLY H H 8.4 0.014 1 220 117 117 GLY N N 111.08 0.380 1 221 118 118 THR H H 8.08 0.014 1 222 118 118 THR N N 114.45 0.380 1 223 119 119 ASP H H 8.59 0.014 1 224 119 119 ASP N N 122.66 0.380 1 225 120 120 VAL H H 8.1 0.014 1 226 120 120 VAL N N 122.02 0.380 1 227 121 121 GLN H H 8.37 0.014 1 228 121 121 GLN N N 124.53 0.380 1 229 123 123 TRP H H 8 0.014 1 230 123 123 TRP N N 120.84 0.380 1 231 124 124 ILE H H 7.88 0.014 1 232 124 124 ILE N N 124.14 0.380 1 233 125 125 ARG H H 8.2 0.014 1 234 125 125 ARG N N 125.72 0.380 1 235 126 126 GLY H H 8.34 0.014 1 236 126 126 GLY N N 111.29 0.380 1 237 127 127 ALA H H 8.08 0.014 1 238 127 127 ALA N N 124.93 0.380 1 239 128 128 ARG H H 8.3 0.014 1 240 128 128 ARG N N 121.55 0.380 1 241 129 129 LEU H H 8.4 0.014 1 242 129 129 LEU N N 125.69 0.380 1 stop_ save_