data_18369 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H and 15N Chemical Shift Assignments for Hen Egg White Lysozyme mutant W111G. ; _BMRB_accession_number 18369 _BMRB_flat_file_name bmr18369.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" 122 "15N chemical shifts" 122 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 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 W111G _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label W111G $W111G 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_W111G _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common W111G _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 129 _Mol_residue_sequence ; KVFGRAELAAAMKRHGLDNY RGYSLGNWVAAAKFESNFNT QATNRNTDGSTDYGILQINS RWWANDGRTPGSRNLANIPA SALLSSDITASVNAAKKIVS DGNGMNAWVAGRNRAKGTDV 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 TRP 109 VAL 110 ALA 111 GLY 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 18368 W108G 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 $W111G 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 $W111G '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 $W111G 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 W111G _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 8.646 0.014 1 2 1 1 LYS N N 124.86 0.380 1 3 2 2 VAL H H 8.176 0.014 1 4 2 2 VAL N N 122.34 0.380 1 5 3 3 PHE H H 8.436 0.014 1 6 3 3 PHE N N 124.86 0.380 1 7 4 4 GLY H H 8.292 0.014 1 8 4 4 GLY N N 110.53 0.380 1 9 5 5 ARG H H 8.236 0.014 1 10 5 5 ARG N N 120.99 0.380 1 11 6 6 ALA H H 8.421 0.014 1 12 6 6 ALA N N 124.13 0.380 1 13 7 7 GLU H H 8.15 0.014 1 14 7 7 GLU N N 119.33 0.380 1 15 8 8 LEU H H 8.093 0.014 1 16 8 8 LEU N N 122.88 0.380 1 17 11 11 ALA H H 8.046 0.014 1 18 11 11 ALA N N 121.79 0.380 1 19 12 12 MET H H 8.022 0.014 1 20 12 12 MET N N 118.16 0.380 1 21 13 13 LYS H H 7.993 0.014 1 22 13 13 LYS N N 121.67 0.380 1 23 14 14 ARG H H 8.111 0.014 1 24 14 14 ARG N N 120.81 0.380 1 25 15 15 HIS H H 8.395 0.014 1 26 15 15 HIS N N 118.8 0.380 1 27 16 16 GLY H H 8.375 0.014 1 28 16 16 GLY N N 109.85 0.380 1 29 17 17 LEU H H 8.168 0.014 1 30 17 17 LEU N N 121.53 0.380 1 31 18 18 ASP H H 8.459 0.014 1 32 18 18 ASP N N 119.04 0.380 1 33 19 19 ASN H H 8.238 0.014 1 34 19 19 ASN N N 118.88 0.380 1 35 20 20 TYR H H 8.015 0.014 1 36 20 20 TYR N N 120.48 0.380 1 37 21 21 ARG H H 8.172 0.014 1 38 21 21 ARG N N 123.2 0.380 1 39 22 22 GLY H H 7.712 0.014 1 40 22 22 GLY N N 108.63 0.380 1 41 23 23 TYR H H 7.884 0.014 1 42 23 23 TYR N N 119.75 0.380 1 43 24 24 SER H H 8.208 0.014 1 44 24 24 SER N N 117.46 0.380 1 45 25 25 LEU H H 8.154 0.014 1 46 25 25 LEU N N 123.88 0.380 1 47 26 26 GLY H H 8.161 0.014 1 48 26 26 GLY N N 108.3 0.380 1 49 27 27 ASN H H 8.131 0.014 1 50 27 27 ASN N N 118.67 0.380 1 51 28 28 TRP H H 8.032 0.014 1 52 28 28 TRP N N 121.68 0.380 1 53 29 29 VAL H H 7.682 0.014 1 54 29 29 VAL N N 121.99 0.380 1 55 30 30 ALA H H 7.972 0.014 1 56 30 30 ALA N N 126.14 0.380 1 57 31 31 ALA H H 8.005 0.014 1 58 31 31 ALA N N 122.4 0.380 1 59 32 32 ALA H H 8.034 0.014 1 60 32 32 ALA N N 122.37 0.380 1 61 33 33 LYS H H 7.998 0.014 1 62 33 33 LYS N N 119.28 0.380 1 63 34 34 PHE H H 8.051 0.014 1 64 34 34 PHE N N 120.09 0.380 1 65 35 35 GLU H H 8.133 0.014 1 66 35 35 GLU N N 121.47 0.380 1 67 36 36 SER H H 8.207 0.014 1 68 36 36 SER N N 116.42 0.380 1 69 37 37 ASN H H 8.294 0.014 1 70 37 37 ASN N N 119.96 0.380 1 71 38 38 PHE H H 8.091 0.014 1 72 38 38 PHE N N 120.16 0.380 1 73 39 39 ASN H H 8.284 0.014 1 74 39 39 ASN N N 119.95 0.380 1 75 40 40 THR H H 8.059 0.014 1 76 40 40 THR N N 114.28 0.380 1 77 41 41 GLN H H 8.273 0.014 1 78 41 41 GLN N N 121.87 0.380 1 79 42 42 ALA H H 8.207 0.014 1 80 42 42 ALA N N 124.65 0.380 1 81 43 43 THR H H 8.039 0.014 1 82 43 43 THR N N 112.53 0.380 1 83 44 44 ASN H H 8.319 0.014 1 84 44 44 ASN N N 120.76 0.380 1 85 45 45 ARG H H 8.271 0.014 1 86 45 45 ARG N N 121.21 0.380 1 87 46 46 ASN H H 8.449 0.014 1 88 46 46 ASN N N 119.43 0.380 1 89 47 47 THR H H 8.116 0.014 1 90 47 47 THR N N 113.88 0.380 1 91 48 48 ASP H H 8.436 0.014 1 92 48 48 ASP N N 120.66 0.380 1 93 49 49 GLY H H 8.318 0.014 1 94 49 49 GLY N N 109.33 0.380 1 95 50 50 SER H H 8.113 0.014 1 96 50 50 SER N N 115.37 0.380 1 97 51 51 THR H H 8.148 0.014 1 98 51 51 THR N N 115.46 0.380 1 99 52 52 ASP H H 8.337 0.014 1 100 52 52 ASP N N 120.83 0.380 1 101 53 53 TYR H H 8.07 0.014 1 102 53 53 TYR N N 120.7 0.380 1 103 54 54 GLY H H 8.215 0.014 1 104 54 54 GLY N N 109.61 0.380 1 105 55 55 ILE H H 7.779 0.014 1 106 55 55 ILE N N 119.53 0.380 1 107 56 56 LEU H H 8.152 0.014 1 108 56 56 LEU N N 124.72 0.380 1 109 57 57 GLN H H 8.21 0.014 1 110 57 57 GLN N N 121.13 0.380 1 111 58 58 ILE H H 8.035 0.014 1 112 58 58 ILE N N 121.25 0.380 1 113 59 59 ASN H H 8.309 0.014 1 114 59 59 ASN N N 121.41 0.380 1 115 60 60 SER H H 8.133 0.014 1 116 60 60 SER N N 116.14 0.380 1 117 61 61 ARG H H 8.16 0.014 1 118 61 61 ARG N N 122.04 0.380 1 119 62 62 TRP H H 7.75 0.014 1 120 62 62 TRP N N 120.53 0.380 1 121 63 63 TRP H H 7.327 0.014 1 122 63 63 TRP N N 120.56 0.380 1 123 64 64 ALA H H 7.652 0.014 1 124 64 64 ALA N N 123.95 0.380 1 125 65 65 ASN H H 8.052 0.014 1 126 65 65 ASN N N 116.88 0.380 1 127 66 66 ASP H H 8.265 0.014 1 128 66 66 ASP N N 118.27 0.380 1 129 67 67 GLY H H 8.26 0.014 1 130 67 67 GLY N N 108.23 0.380 1 131 68 68 ARG H H 7.908 0.014 1 132 68 68 ARG N N 119.76 0.380 1 133 69 69 THR H H 8.173 0.014 1 134 69 69 THR N N 116.9 0.380 1 135 71 71 GLY H H 8.429 0.014 1 136 71 71 GLY N N 109.25 0.380 1 137 72 72 SER H H 8.061 0.014 1 138 72 72 SER N N 115.37 0.380 1 139 73 73 ARG H H 8.345 0.014 1 140 73 73 ARG N N 122.45 0.380 1 141 74 74 ASN H H 8.371 0.014 1 142 74 74 ASN N N 119.53 0.380 1 143 75 75 LEU H H 8.191 0.014 1 144 75 75 LEU N N 122.96 0.380 1 145 76 76 ALA H H 8.122 0.014 1 146 76 76 ALA N N 123.3 0.380 1 147 77 77 ASN H H 8.21 0.014 1 148 77 77 ASN N N 117.12 0.380 1 149 78 78 ILE H H 7.944 0.014 1 150 78 78 ILE N N 122.57 0.380 1 151 80 80 ALA H H 8.422 0.014 1 152 80 80 ALA N N 124.37 0.380 1 153 81 81 SER H H 8.18 0.014 1 154 81 81 SER N N 113.56 0.380 1 155 82 82 ALA H H 8.157 0.014 1 156 82 82 ALA N N 125.63 0.380 1 157 83 83 LEU H H 7.905 0.014 1 158 83 83 LEU N N 120.16 0.380 1 159 84 84 LEU H H 7.971 0.014 1 160 84 84 LEU N N 121.83 0.380 1 161 85 85 SER H H 8.162 0.014 1 162 85 85 SER N N 115.81 0.380 1 163 86 86 SER H H 8.189 0.014 1 164 86 86 SER N N 117.03 0.380 1 165 87 87 ASP H H 8.347 0.014 1 166 87 87 ASP N N 120.66 0.380 1 167 88 88 ILE H H 8.012 0.014 1 168 88 88 ILE N N 121.12 0.380 1 169 89 89 THR H H 8.099 0.014 1 170 89 89 THR N N 117.81 0.380 1 171 90 90 ALA H H 8.187 0.014 1 172 90 90 ALA N N 126.06 0.380 1 173 91 91 SER H H 8.211 0.014 1 174 91 91 SER N N 115.23 0.380 1 175 92 92 VAL H H 8.099 0.014 1 176 92 92 VAL N N 121.82 0.380 1 177 93 93 ASN H H 8.355 0.014 1 178 93 93 ASN N N 121.34 0.380 1 179 94 94 ALA H H 8.153 0.014 1 180 94 94 ALA N N 124.53 0.380 1 181 95 95 ALA H H 8.082 0.014 1 182 95 95 ALA N N 122.37 0.380 1 183 96 96 LYS H H 8.037 0.014 1 184 96 96 LYS N N 119.99 0.380 1 185 97 97 LYS H H 8.154 0.014 1 186 97 97 LYS N N 122.63 0.380 1 187 98 98 ILE H H 8.155 0.014 1 188 98 98 ILE N N 123.11 0.380 1 189 99 99 VAL H H 8.255 0.014 1 190 99 99 VAL N N 125.01 0.380 1 191 100 100 SER H H 8.384 0.014 1 192 100 100 SER N N 119.56 0.380 1 193 101 101 ASP H H 8.524 0.014 1 194 101 101 ASP N N 121.27 0.380 1 195 102 102 GLY H H 8.354 0.014 1 196 102 102 GLY N N 109.23 0.380 1 197 103 103 ASN H H 8.294 0.014 1 198 103 103 ASN N N 118.49 0.380 1 199 104 104 GLY H H 8.412 0.014 1 200 104 104 GLY N N 109.17 0.380 1 201 105 105 MET H H 8.14 0.014 1 202 105 105 MET N N 119.62 0.380 1 203 106 106 ASN H H 8.346 0.014 1 204 106 106 ASN N N 119.29 0.380 1 205 107 107 ALA H H 8.144 0.014 1 206 107 107 ALA N N 123.55 0.380 1 207 108 108 TRP H H 7.983 0.014 1 208 108 108 TRP N N 120.21 0.380 1 209 109 109 VAL H H 7.693 0.014 1 210 109 109 VAL N N 122.03 0.380 1 211 110 110 ALA H H 8.112 0.014 1 212 110 110 ALA N N 126.39 0.380 1 213 111 111 GLY H H 8.188 0.014 1 214 111 111 GLY N N 107.4 0.380 1 215 113 113 ASN H H 8.369 0.014 1 216 113 113 ASN N N 119.14 0.380 1 217 115 115 ALA H H 8.114 0.014 1 218 115 115 ALA N N 124.41 0.380 1 219 116 116 LYS H H 8.252 0.014 1 220 116 116 LYS N N 120.73 0.380 1 221 117 117 GLY H H 8.355 0.014 1 222 117 117 GLY N N 109.81 0.380 1 223 118 118 THR H H 8.023 0.014 1 224 118 118 THR N N 121.44 0.380 1 225 119 119 ASP H H 8.513 0.014 1 226 119 119 ASP N N 113.16 0.380 1 227 120 120 VAL H H 8.039 0.014 1 228 120 120 VAL N N 120.75 0.380 1 229 121 121 GLN H H 8.305 0.014 1 230 122 122 ALA N N 123.34 0.380 1 231 123 123 TRP H H 7.937 0.014 1 232 123 123 TRP N N 119.64 0.380 1 233 124 124 ILE H H 7.803 0.014 1 234 124 124 ILE N N 122.88 0.380 1 235 125 125 ARG H H 8.134 0.014 1 236 125 125 ARG N N 124.42 0.380 1 237 126 126 GLY H H 8.278 0.014 1 238 126 126 GLY N N 109.99 0.380 1 239 127 127 ALA H H 8.012 0.014 1 240 127 127 ALA N N 123.59 0.380 1 241 128 128 ARG H H 8.239 0.014 1 242 128 128 ARG N N 120.23 0.380 1 243 129 129 LEU H H 8.303 0.014 1 244 129 129 LEU N N 124.44 0.380 1 stop_ save_