data_4557 #Corrected using PDB structure: 1QLOA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 16 V HA 4.20 3.25 # 23 D HA 4.47 5.20 # 26 D HA 4.44 5.32 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.02 N/A N/A N/A N/A 0.01 # #bmr4557.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4557.str file): #HA CA CB CO N HN #N/A N/A N/A N/A N/A N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.05 N/A N/A N/A N/A +/-0.09 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.649 N/A N/A N/A N/A 0.347 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.141 N/A N/A N/A N/A 0.235 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscop ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pfaender R. . . 2 Neumann L. . . 3 Zweckstetter M. . . 4 Seger C. . . 5 Holak T. A. . 6 Tampe R. . . stop_ _BMRB_accession_number 4557 _BMRB_flat_file_name bmr4557.str _Entry_type new _Submission_date 1999-12-11 _Accession_date 1999-12-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 151 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; The structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscop ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 10521276 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pfaender R. . . 2 Neumann L. . . 3 Zweckstetter M. . . 4 Seger C. . . 5 Holak T. A. . 6 Tampe R. . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full . _Journal_volume 38 _Journal_issue 41 _Page_first 13692 _Page_last 13698 _Year 1999 loop_ _Keyword "membrane proteins" structure NMR "herpes simplex virus protein ICP47" stop_ save_ ################################## # Molecular system description # ################################## save_system_ICP47 _Saveframe_category molecular_system _Mol_system_name "herpes simplex virus protein ICP47" _Abbreviation_common ICP47 loop_ _Mol_system_component_name _Mol_label "ICP47 domain 2-34" $ICP47 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1QLO ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_ICP47 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "herpes simplex virus protein ICP47" _Abbreviation_common ICP47 _Mol_thiol_state 'not present' ############################## # Polymer residue sequence # ############################## _Residue_count 33 _Mol_residue_sequence ; SWALEMADTFLDNMRVGPRT YADVRDEINKRGR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 SER 2 3 TRP 3 4 ALA 4 5 LEU 5 6 GLU 6 7 MET 7 8 ALA 8 9 ASP 9 10 THR 10 11 PHE 11 12 LEU 12 13 ASP 13 14 ASN 14 15 MET 15 16 ARG 16 17 VAL 17 18 GLY 18 19 PRO 19 20 ARG 20 21 THR 21 22 TYR 22 23 ALA 23 24 ASP 24 25 VAL 25 26 ARG 26 27 ASP 27 28 GLU 28 29 ILE 29 30 ASN 30 31 LYS 31 32 ARG 32 33 GLY 33 34 ARG stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-04-29 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 PDB 1QLO "A Chain A, Structure Of The Active Domain OfThe Herpes Simplex Virus Protein Icp47 In WaterSODIUMDODECYL SULFATE SOLUTION Determined By Nuclear MagneticResonance Spectroscopy" 97.06 34 100 100 3e-12 EMBL CAA23737.1 "unnamed protein product [Humanherpesvirus 1]" 60.00 55 100 100 3e-12 GenBank AAA45795.1 "IE mRNA-5 protein" 37.50 88 100 100 3e-12 PIR EDBE51 "immediate-early-5 protein - humanherpesvirus 1" 37.50 88 100 100 3e-12 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $ICP47 "herpes simplex virus" . . . . . . 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 $ICP47 "chemically synthesized" . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ICP47 4.7 mM . SDS 560 mM [U-2H] H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ICP47 4.7 mM . SDS 560 mM [U-2H] D2O 100 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 save_ save_NMR_spectrometer3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 save_ save_NMR_spectrometer4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 save_ save_NMR_spectrometer5 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; NOESY TOCSY COSY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 0.1 n/a temperature 307 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref _Saveframe_category chemical_shift_reference 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 0.0 internal direct . . . 1.0 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_ref _Mol_system_component_name "ICP47 domain 2-34" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 TRP H H 8.66 . . 2 2 TRP HA H 4.59 . . 3 2 TRP HB2 H 3.30 . . 4 2 TRP HB3 H 3.30 . . 5 3 ALA H H 7.59 . . 6 3 ALA HA H 3.79 . . 7 3 ALA HB H 1.13 . . 8 4 LEU H H 7.40 . . 9 4 LEU HA H 4.02 . . 10 4 LEU HB2 H 1.59 . . 11 4 LEU HB3 H 1.59 . . 12 4 LEU HG H 0.88 . . 13 4 LEU HD1 H 0.81 . . 14 4 LEU HD2 H 0.81 . . 15 5 GLU H H 7.97 . . 16 5 GLU HA H 4.07 . . 17 5 GLU HB2 H 1.99 . . 18 5 GLU HB3 H 1.99 . . 19 5 GLU HG2 H 2.31 . . 20 5 GLU HG3 H 2.22 . . 21 6 MET H H 8.07 . . 22 6 MET HA H 4.23 . . 23 6 MET HB2 H 2.21 . . 24 6 MET HB3 H 2.21 . . 25 6 MET HG2 H 1.91 . . 26 6 MET HG3 H 1.82 . . 27 6 MET HE H 1.23 . . 28 7 ALA H H 8.07 . . 29 7 ALA HA H 4.04 . . 30 7 ALA HB H 1.42 . . 31 8 ASP H H 8.16 . . 32 8 ASP HA H 4.35 . . 33 8 ASP HB2 H 2.75 . . 34 8 ASP HB3 H 2.69 . . 35 9 THR H H 7.80 . . 36 9 THR HA H 4.01 . . 37 9 THR HB H 4.20 . . 38 9 THR HG2 H 1.10 . . 39 10 PHE H H 8.00 . . 40 10 PHE HA H 4.35 . . 41 10 PHE HB2 H 3.12 . . 42 10 PHE HB3 H 3.12 . . 43 11 LEU H H 8.29 . . 44 11 LEU HA H 3.96 . . 45 11 LEU HB2 H 1.80 . . 46 11 LEU HB3 H 1.75 . . 47 11 LEU HG H 1.50 . . 48 11 LEU HD1 H 0.87 . . 49 11 LEU HD2 H 0.87 . . 50 12 ASP H H 7.59 . . 51 12 ASP HA H 4.14 . . 52 12 ASP HB2 H 2.72 . . 53 12 ASP HB3 H 2.60 . . 54 13 ASN H H 7.83 . . 55 13 ASN HA H 4.55 . . 56 13 ASN HB2 H 2.74 . . 57 13 ASN HB3 H 2.74 . . 58 14 MET H H 7.78 . . 59 14 MET HA H 4.29 . . 60 14 MET HB2 H 1.94 . . 61 14 MET HB3 H 1.94 . . 62 14 MET HG2 H 2.38 . . 63 14 MET HG3 H 2.32 . . 64 15 ARG H H 7.93 . . 65 15 ARG HA H 4.25 . . 66 15 ARG HB2 H 1.90 . . 67 15 ARG HB3 H 1.90 . . 68 15 ARG HG2 H 1.80 . . 69 15 ARG HG3 H 1.80 . . 70 15 ARG HD2 H 2.07 . . 71 15 ARG HD3 H 2.07 . . 72 16 VAL H H 7.63 . . 73 16 VAL HA H 4.18 . . 74 16 VAL HB H 2.12 . . 75 16 VAL HG1 H 0.88 . . 76 16 VAL HG2 H 0.88 . . 77 17 GLY H H 7.91 . . 78 17 GLY HA2 H 4.08 . . 79 17 GLY HA3 H 4.08 . . 80 20 THR H H 8.03 . . 81 20 THR HA H 4.38 . . 82 21 TYR H H 8.11 . . 83 21 TYR HA H 4.27 . . 84 21 TYR HB2 H 3.04 . . 85 21 TYR HB3 H 2.94 . . 86 22 ALA H H 7.88 . . 87 22 ALA HA H 3.92 . . 88 22 ALA HB H 1.33 . . 89 23 ASP H H 7.88 . . 90 23 ASP HA H 4.45 . . 91 23 ASP HB2 H 2.75 . . 92 24 VAL H H 7.78 . . 93 24 VAL HA H 3.70 . . 94 24 VAL HB H 2.17 . . 95 24 VAL HG1 H 0.98 . . 96 24 VAL HG2 H 0.89 . . 97 25 ARG H H 8.13 . . 98 25 ARG HA H 3.82 . . 99 25 ARG HB2 H 1.83 . . 100 25 ARG HB3 H 1.73 . . 101 25 ARG HG2 H 1.65 . . 102 25 ARG HG3 H 1.58 . . 103 25 ARG HD2 H 3.11 . . 104 25 ARG HD3 H 3.11 . . 105 26 ASP H H 7.92 . . 106 26 ASP HA H 4.42 . . 107 26 ASP HB2 H 2.72 . . 108 26 ASP HB3 H 2.64 . . 109 27 GLU H H 7.81 . . 110 27 GLU HA H 4.11 . . 111 27 GLU HB2 H 2.38 . . 112 27 GLU HB3 H 2.38 . . 113 27 GLU HG2 H 2.27 . . 114 27 GLU HG3 H 1.95 . . 115 28 ILE H H 7.94 . . 116 28 ILE HA H 3.76 . . 117 28 ILE HB H 1.66 . . 118 28 ILE HG12 H 0.87 . . 119 28 ILE HG13 H 0.87 . . 120 28 ILE HG2 H 0.78 . . 121 29 ASN H H 8.04 . . 122 29 ASN HA H 4.58 . . 123 29 ASN HB2 H 2.81 . . 124 29 ASN HB3 H 2.81 . . 125 30 LYS H H 7.85 . . 126 30 LYS HA H 4.15 . . 127 30 LYS HB2 H 1.81 . . 128 30 LYS HB3 H 1.81 . . 129 30 LYS HG2 H 1.49 . . 130 30 LYS HG3 H 1.49 . . 131 30 LYS HD2 H 1.39 . . 132 30 LYS HD3 H 1.39 . . 133 30 LYS HE2 H 3.09 . . 134 30 LYS HE3 H 3.09 . . 135 31 ARG H H 7.76 . . 136 31 ARG HA H 4.23 . . 137 31 ARG HB2 H 1.81 . . 138 31 ARG HB3 H 1.81 . . 139 31 ARG HG2 H 1.68 . . 140 31 ARG HG3 H 1.68 . . 141 32 GLY H H 8.01 . . 142 32 GLY HA2 H 3.91 . . 143 32 GLY HA3 H 3.91 . . 144 33 ARG H H 7.68 . . 145 33 ARG HA H 4.11 . . 146 33 ARG HB2 H 1.81 . . 147 33 ARG HB3 H 1.67 . . 148 33 ARG HG2 H 1.56 . . 149 33 ARG HG3 H 1.56 . . 150 33 ARG HD2 H 3.12 . . 151 33 ARG HD3 H 3.12 . . stop_ save_