data_15245 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR SOLUTION STRUCTURE OF THE VILLIN HEADPIECE MUTANT G34L ; _BMRB_accession_number 15245 _BMRB_flat_file_name bmr15245.str _Entry_type original _Submission_date 2007-05-10 _Accession_date 2007-05-10 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Residues 2 - 36 of our fragment containing the mutation G34L correspond to residues 792 - 826 of intact chicken villin and to residues 42 - 76 of the C-terminal 76-amino acid chicken villin headpiece domain. Residue Met1 of our fragment is not from villin but was included to compare our fragment with the corresponding structure 1VII.pdb where it is also included. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gronwald Wolfram . . 2 Hohm Tim . . 3 Hoffmann Daniel . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 187 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-02 update BMRB 'complete entry citation' 2007-05-14 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Evolutionary Pareto-optimization of stably folding peptides' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18284690 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gronwald Wolfram . . 2 Hohm Tim . . 3 Hoffmann Daniel . . stop_ _Journal_abbreviation 'BMC Bioinformatics.' _Journal_volume 9 _Journal_issue 109 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'villin_G34L monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'villin_G34L monomer' $villin_G34L stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_villin_G34L _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common villin_G34L _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'f-actin binding' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 36 _Mol_residue_sequence ; MLSDEDFKAVFGMTRSAFAN LPLWKQQNLKKEKLLF ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 SER 4 ASP 5 GLU 6 ASP 7 PHE 8 LYS 9 ALA 10 VAL 11 PHE 12 GLY 13 MET 14 THR 15 ARG 16 SER 17 ALA 18 PHE 19 ALA 20 ASN 21 LEU 22 PRO 23 LEU 24 TRP 25 LYS 26 GLN 27 GLN 28 ASN 29 LEU 30 LYS 31 LYS 32 GLU 33 LYS 34 LEU 35 LEU 36 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 11519 protein 100.00 36 97.22 97.22 5.60e-15 BMRB 11520 protein 100.00 36 97.22 97.22 5.60e-15 BMRB 11521 protein 100.00 36 97.22 97.22 5.60e-15 BMRB 15097 D6-HP 97.22 208 97.14 97.14 2.89e-13 BMRB 17698 HP67_H41F 97.22 67 97.14 97.14 4.46e-14 BMRB 4428 "HEADPIECE DOMAIN FROM CHICKEN VILLIN" 97.22 67 97.14 97.14 3.45e-14 PDB 1QQV "Solution Structure Of The Headpiece Domain Of Chicken Villin" 97.22 67 97.14 97.14 3.45e-14 PDB 1VII "Thermostable Subdomain From Chicken Villin Headpiece, Nmr, Minimized Average Structure" 100.00 36 97.22 97.22 5.60e-15 PDB 1YU5 "Crystal Structure Of The Headpiece Domain Of Chicken Villin" 97.22 67 97.14 97.14 3.45e-14 PDB 1YU8 "Crystal Structure Of The R37a Mutant Of Villin Headpiece" 97.22 67 97.14 97.14 3.31e-14 PDB 2PPZ "Nmr Solution Structure Of The Villin Headpiece Mutant G34l" 100.00 36 100.00 100.00 5.83e-16 PDB 2RJV "Crystal Structure Of The H41y Mutant Of Villin Headpiece, P 21 21 21 Space Group" 97.22 67 97.14 97.14 3.56e-14 PDB 2RJW "The Crystal Structure Of The H41y Mutant Of Villin Headpiece, P61 Space Group" 97.22 67 97.14 97.14 3.56e-14 PDB 2RJX "Crystal Structure Of The Headpiece Domain Of Chicken Villin, P61 Space Group" 97.22 67 97.14 97.14 3.45e-14 PDB 2RJY "Crystal Structure Of Villin Headpiece, P21 21 21 Space Group" 97.22 67 97.14 97.14 3.45e-14 PDB 3MYA "Crystal Structure Of Hp67 H41f - P61" 97.22 67 97.14 97.14 4.46e-14 PDB 3MYC "Crystal Structure Of Hp67 H41f - P212121" 97.22 67 97.14 97.14 4.46e-14 GB AAA49133 "villin [Gallus gallus]" 97.22 826 97.14 97.14 9.40e-13 REF NP_990773 "villin-1 [Gallus gallus]" 97.22 826 97.14 97.14 9.40e-13 REF XP_003207697 "PREDICTED: villin-1 [Meleagris gallopavo]" 97.22 826 97.14 97.14 9.49e-13 REF XP_010711916 "PREDICTED: villin-1 [Meleagris gallopavo]" 97.22 826 97.14 97.14 9.49e-13 REF XP_010711917 "PREDICTED: villin-1 [Meleagris gallopavo]" 97.22 826 97.14 97.14 9.49e-13 SP P02640 "RecName: Full=Villin-1" 97.22 826 97.14 97.14 9.40e-13 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $villin_G34L chicken 9031 Eukaryota Metazoa Gallus gallus 'residues 792 - 826' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $villin_G34L 'chemical synthesis' . none none . none none stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'pH 5.0' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $villin_G34L 4.3 mg 'natural abundance' H2O 90 'v/v %' 'natural abundance' D2O 10 'v/v %' 'natural abundance' DSS 0.1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Auremol _Saveframe_category software _Name AUREMOL _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . www.auremol.de stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details 'spectra assignment and restraint generation' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _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_ ####################### # 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 . M pH 5.0 . pH pressure 1 . atm temperature 298 . 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_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H 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 'villin_G34L monomer' _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 LEU H H 8.85000 0.05000 1 2 2 2 LEU HA H 4.67100 0.05000 1 3 2 2 LEU HB2 H 1.83400 0.05000 2 4 2 2 LEU HB3 H 1.83400 0.05000 2 5 2 2 LEU HD1 H 0.90800 0.05000 1 6 2 2 LEU HD2 H 0.90800 0.05000 1 7 2 2 LEU HG H 1.69000 0.05000 1 8 3 3 SER H H 9.55200 0.05000 1 9 3 3 SER HA H 4.51900 0.05000 1 10 3 3 SER HB2 H 4.41700 0.05000 2 11 3 3 SER HB3 H 4.15100 0.05000 2 12 4 4 ASP H H 9.16500 0.05000 1 13 4 4 ASP HA H 4.39800 0.05000 1 14 4 4 ASP HB2 H 2.72600 0.05000 1 15 4 4 ASP HB3 H 2.72600 0.05000 1 16 5 5 GLU H H 8.78200 0.05000 1 17 5 5 GLU HA H 4.12600 0.05000 1 18 5 5 GLU HB2 H 2.02200 0.05000 1 19 5 5 GLU HB3 H 2.02200 0.05000 1 20 5 5 GLU HG2 H 2.40500 0.05000 2 21 5 5 GLU HG3 H 2.34800 0.05000 2 22 6 6 ASP H H 8.04400 0.05000 1 23 6 6 ASP HA H 4.51900 0.05000 1 24 6 6 ASP HB2 H 2.83800 0.05000 2 25 6 6 ASP HB3 H 2.64600 0.05000 2 26 7 7 PHE H H 9.05000 0.05000 1 27 7 7 PHE HA H 3.87100 0.05000 1 28 7 7 PHE HB2 H 3.35200 0.05000 2 29 7 7 PHE HB3 H 2.98400 0.05000 2 30 7 7 PHE HD1 H 7.15300 0.05000 1 31 7 7 PHE HD2 H 7.15300 0.05000 1 32 7 7 PHE HE1 H 6.50200 0.05000 1 33 7 7 PHE HE2 H 6.50200 0.05000 1 34 8 8 LYS H H 7.86800 0.05000 1 35 8 8 LYS HA H 4.36900 0.05000 1 36 8 8 LYS HB2 H 1.89600 0.05000 1 37 8 8 LYS HB3 H 1.89600 0.05000 1 38 9 9 ALA H H 7.69700 0.05000 1 39 9 9 ALA HA H 4.09000 0.05000 1 40 9 9 ALA HB H 1.56600 0.05000 1 41 10 10 VAL H H 7.91700 0.05000 1 42 10 10 VAL HA H 3.54700 0.05000 1 43 10 10 VAL HB H 1.50500 0.05000 1 44 10 10 VAL HG1 H -0.10900 0.05000 2 45 10 10 VAL HG2 H 0.80900 0.05000 2 46 11 11 PHE H H 8.46000 0.05000 1 47 11 11 PHE HA H 4.19400 0.05000 1 48 11 11 PHE HB2 H 2.88600 0.05000 2 49 11 11 PHE HB3 H 2.40500 0.05000 2 50 11 11 PHE HD1 H 6.33300 0.05000 1 51 11 11 PHE HD2 H 6.33300 0.05000 1 52 11 11 PHE HE1 H 6.63200 0.05000 1 53 11 11 PHE HE2 H 6.63200 0.05000 1 54 11 11 PHE HZ H 6.79500 0.05000 1 55 12 12 GLY H H 8.19900 0.05000 1 56 12 12 GLY HA2 H 4.04500 0.05000 2 57 12 12 GLY HA3 H 3.91800 0.05000 2 58 13 13 MET H H 7.59600 0.05000 1 59 13 13 MET HA H 4.82300 0.05000 1 60 13 13 MET HB2 H 2.35400 0.05000 2 61 13 13 MET HB3 H 2.13700 0.05000 2 62 13 13 MET HG2 H 2.80700 0.05000 1 63 13 13 MET HG3 H 2.80700 0.05000 1 64 14 14 THR H H 8.19900 0.05000 1 65 14 14 THR HA H 4.54400 0.05000 1 66 14 14 THR HG2 H 1.40000 0.05000 1 67 15 15 ARG H H 8.77900 0.05000 1 68 15 15 ARG HA H 3.25200 0.05000 1 69 15 15 ARG HB2 H 1.31200 0.05000 2 70 15 15 ARG HB3 H 1.19100 0.05000 2 71 15 15 ARG HD2 H 2.90800 0.05000 2 72 15 15 ARG HD3 H 2.73300 0.05000 2 73 15 15 ARG HE H 7.06300 0.05000 1 74 15 15 ARG HG2 H 0.82100 0.05000 2 75 15 15 ARG HG3 H 0.37600 0.05000 2 76 16 16 SER H H 8.19700 0.05000 1 77 16 16 SER HA H 4.08800 0.05000 1 78 16 16 SER HB2 H 3.77400 0.05000 1 79 16 16 SER HB3 H 3.77400 0.05000 1 80 17 17 ALA H H 7.61500 0.05000 1 81 17 17 ALA HA H 4.09900 0.05000 1 82 17 17 ALA HB H 1.48000 0.05000 1 83 18 18 PHE H H 8.43100 0.05000 1 84 18 18 PHE HA H 4.11100 0.05000 1 85 18 18 PHE HB2 H 3.16200 0.05000 2 86 18 18 PHE HB3 H 3.02100 0.05000 2 87 18 18 PHE HD1 H 7.06700 0.05000 1 88 18 18 PHE HD2 H 7.06700 0.05000 1 89 19 19 ALA H H 7.83500 0.05000 1 90 19 19 ALA HA H 3.94500 0.05000 1 91 19 19 ALA HB H 1.44200 0.05000 1 92 20 20 ASN H H 7.16400 0.05000 1 93 20 20 ASN HA H 4.67100 0.05000 1 94 20 20 ASN HB2 H 2.87700 0.05000 2 95 20 20 ASN HB3 H 2.65500 0.05000 2 96 20 20 ASN HD21 H 6.81200 0.05000 2 97 20 20 ASN HD22 H 7.47500 0.05000 2 98 21 21 LEU H H 7.40300 0.05000 1 99 21 21 LEU HA H 4.32800 0.05000 1 100 21 21 LEU HB2 H 1.84300 0.05000 2 101 21 21 LEU HB3 H 1.60000 0.05000 2 102 21 21 LEU HD1 H 0.71700 0.05000 2 103 21 21 LEU HD2 H 0.83200 0.05000 2 104 21 21 LEU HG H 1.46400 0.05000 1 105 22 22 PRO HA H 4.34900 0.05000 1 106 23 23 LEU H H 8.81900 0.05000 1 107 23 23 LEU HA H 3.76800 0.05000 1 108 23 23 LEU HB2 H 1.70900 0.05000 1 109 23 23 LEU HB3 H 1.70900 0.05000 1 110 24 24 TRP H H 7.94300 0.05000 1 111 24 24 TRP HA H 4.39200 0.05000 1 112 24 24 TRP HB2 H 3.48500 0.05000 2 113 24 24 TRP HB3 H 3.23400 0.05000 2 114 24 24 TRP HD1 H 7.55500 0.05000 1 115 24 24 TRP HE1 H 10.49400 0.05000 1 116 24 24 TRP HE3 H 7.39100 0.05000 1 117 24 24 TRP HZ3 H 7.08000 0.05000 1 118 25 25 LYS H H 6.07400 0.05000 1 119 25 25 LYS HA H 3.66900 0.05000 1 120 25 25 LYS HB2 H 1.43400 0.05000 2 121 25 25 LYS HB3 H 1.27800 0.05000 2 122 25 25 LYS HD2 H 0.89800 0.05000 1 123 25 25 LYS HD3 H 0.89800 0.05000 1 124 25 25 LYS HG2 H 0.70500 0.05000 2 125 25 25 LYS HG3 H 0.34900 0.05000 2 126 26 26 GLN H H 7.60800 0.05000 1 127 26 26 GLN HA H 3.44900 0.05000 1 128 26 26 GLN HB2 H 1.91400 0.05000 2 129 26 26 GLN HB3 H 1.79600 0.05000 2 130 26 26 GLN HG2 H 2.04800 0.05000 1 131 26 26 GLN HG3 H 2.04800 0.05000 1 132 27 27 GLN H H 8.22300 0.05000 1 133 27 27 GLN HA H 4.06100 0.05000 1 134 27 27 GLN HB2 H 2.25900 0.05000 2 135 27 27 GLN HB3 H 2.16000 0.05000 2 136 27 27 GLN HE21 H 6.93400 0.05000 2 137 27 27 GLN HE22 H 7.42400 0.05000 2 138 27 27 GLN HG2 H 2.57100 0.05000 2 139 27 27 GLN HG3 H 2.47200 0.05000 2 140 28 28 ASN H H 7.93400 0.05000 1 141 28 28 ASN HA H 4.53700 0.05000 1 142 28 28 ASN HB2 H 2.98900 0.05000 1 143 28 28 ASN HB3 H 2.98900 0.05000 1 144 29 29 LEU H H 8.44100 0.05000 1 145 29 29 LEU HA H 4.28500 0.05000 1 146 29 29 LEU HB2 H 2.18300 0.05000 2 147 29 29 LEU HB3 H 1.69800 0.05000 2 148 29 29 LEU HD1 H 0.96900 0.05000 2 149 29 29 LEU HD2 H 1.07400 0.05000 2 150 29 29 LEU HG H 1.88300 0.05000 1 151 30 30 LYS H H 8.28800 0.05000 1 152 30 30 LYS HA H 4.07300 0.05000 1 153 30 30 LYS HB2 H 1.80800 0.05000 1 154 30 30 LYS HB3 H 1.80800 0.05000 1 155 30 30 LYS HG2 H 1.45000 0.05000 1 156 30 30 LYS HG3 H 1.45000 0.05000 1 157 31 31 LYS H H 7.87100 0.05000 1 158 31 31 LYS HA H 4.08800 0.05000 1 159 31 31 LYS HB2 H 1.73400 0.05000 2 160 31 31 LYS HB3 H 1.58800 0.05000 2 161 31 31 LYS HD2 H 1.45900 0.05000 1 162 31 31 LYS HD3 H 1.45900 0.05000 1 163 32 32 GLU H H 8.05800 0.05000 1 164 32 32 GLU HA H 4.12600 0.05000 1 165 32 32 GLU HB2 H 2.24400 0.05000 2 166 32 32 GLU HB3 H 2.17500 0.05000 2 167 32 32 GLU HG2 H 2.45500 0.05000 1 168 32 32 GLU HG3 H 2.45500 0.05000 1 169 33 33 LYS H H 7.76500 0.05000 1 170 33 33 LYS HA H 4.29000 0.05000 1 171 33 33 LYS HB2 H 1.81600 0.05000 1 172 33 33 LYS HB3 H 1.81600 0.05000 1 173 33 33 LYS HD2 H 1.57900 0.05000 1 174 33 33 LYS HD3 H 1.57900 0.05000 1 175 33 33 LYS HG2 H 1.44600 0.05000 1 176 33 33 LYS HG3 H 1.44600 0.05000 1 177 34 34 LEU H H 8.05200 0.05000 1 178 34 34 LEU HA H 4.27400 0.05000 1 179 34 34 LEU HD1 H 0.79900 0.05000 2 180 34 34 LEU HD2 H 0.90600 0.05000 2 181 34 34 LEU HG H 1.49400 0.05000 1 182 35 35 LEU H H 7.76100 0.05000 1 183 35 35 LEU HA H 4.26400 0.05000 1 184 35 35 LEU HD1 H 0.87100 0.05000 1 185 35 35 LEU HD2 H 0.87100 0.05000 1 186 36 36 PHE H H 7.89700 0.05000 1 187 36 36 PHE HA H 4.56600 0.05000 1 stop_ save_