data_1635 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Conformation of a Peptide Fragment Representing a Proposed RNA-Binding Site of a Viral Coat Protein Studied by Two-Dimensional NMR ; _BMRB_accession_number 1635 _BMRB_flat_file_name bmr1635.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-13 _Entry_origination BMRB _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 'van der Graaf' Marinette . . 2 'van Mierlo' Carlo P.M. . 3 Hemminga Marcus A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 144 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-15 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; van der Graaf, Marinette, van Mierlo, Carlo P.M., Hemminga, Marcus A., "Solution Conformation of a Peptide Fragment Representing a Proposed RNA-Binding Site of a Viral Coat Protein Studied by Two-Dimensional NMR," Biochemistry 30, 5722-5727 (1991). ; _Citation_title ; Solution Conformation of a Peptide Fragment Representing a Proposed RNA-Binding Site of a Viral Coat Protein Studied by Two-Dimensional NMR ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 'van der Graaf' Marinette . . 2 'van Mierlo' Carlo P.M. . 3 Hemminga Marcus A. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 30 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5722 _Page_last 5727 _Year 1991 _Details . save_ ################################## # Molecular system description # ################################## save_system_viral_coat_protein _Saveframe_category molecular_system _Mol_system_name 'viral coat protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'viral coat protein' $viral_coat_protein stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_viral_coat_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'viral coat protein' _Name_variant 'RNA-binding fragment' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 24 _Mol_residue_sequence ; XTVGTGKLTRAQRRAAARKN KRNT ; loop_ _Residue_seq_code _Residue_label 1 X 2 THR 3 VAL 4 GLY 5 THR 6 GLY 7 LYS 8 LEU 9 THR 10 ARG 11 ALA 12 GLN 13 ARG 14 ARG 15 ALA 16 ALA 17 ALA 18 ARG 19 LYS 20 ASN 21 LYS 22 ARG 23 ASN 24 THR 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 1998 "viral coat protein" 95.83 24 100.00 100.00 1.78e-04 BMRB 1999 "viral coat protein" 95.83 24 100.00 100.00 1.78e-04 BMRB 2000 "viral coat protein" 95.83 24 100.00 100.00 1.78e-04 BMRB 2001 "viral coat protein" 95.83 24 100.00 100.00 1.78e-04 BMRB 2002 "viral coat protein" 95.83 24 100.00 100.00 1.78e-04 BMRB 2003 "viral coat protein" 95.83 24 100.00 100.00 1.78e-04 PDB 1CWP "Structures Of The Native And Swollen Forms Of Cowpea Chlorotic Mottle Virus Determined By X-Ray Crystallography And Cryo-Electr" 95.83 190 100.00 100.00 6.57e-05 GB AAA46370 "viral coat protein [Cowpea chlorotic mottle virus]" 95.83 190 100.00 100.00 6.57e-05 GB AAA46373 "coat protein [Cowpea chlorotic mottle virus]" 95.83 190 100.00 100.00 6.57e-05 GB AAM64087 "coat protein [Cowpea chlorotic mottle virus]" 95.83 190 100.00 100.00 6.37e-05 GB AAN37634 "coat protein [Cowpea chlorotic mottle virus]" 95.83 190 100.00 100.00 6.78e-05 GB AAN37638 "coat protein [Cowpea chlorotic mottle virus]" 95.83 190 100.00 100.00 6.57e-05 PRF 0808330A "protein,coat [Cowpea chlorotic mottle virus]" 95.83 190 100.00 100.00 5.73e-05 REF NP_613277 "coat protein [Cowpea chlorotic mottle virus]" 95.83 190 100.00 100.00 6.57e-05 SP P03601 "RecName: Full=Capsid protein; Short=CP; AltName: Full=Coat protein" 95.83 190 100.00 100.00 6.57e-05 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _ICTVdb_decimal_code _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $viral_coat_protein 'cowpea chlorotic mottle virus' Virus 12300 . bromovirus . . 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 $viral_coat_protein 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4 . na temperature 283 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label TSP H . . ppm 0 . . . . . $entry_citation $entry_citation 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'viral coat protein' _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 THR H H 8.41 . 1 2 . 2 THR HA H 4.45 . 1 3 . 2 THR HB H 4.3 . 1 4 . 2 THR HG2 H 1.21 . 1 5 . 3 VAL H H 8.21 . 1 6 . 3 VAL HA H 4.14 . 1 7 . 3 VAL HB H 2.1 . 1 8 . 3 VAL HG1 H .97 . 1 9 . 3 VAL HG2 H .97 . 1 10 . 4 GLY H H 8.63 . 1 11 . 4 GLY HA2 H 4.05 . 1 12 . 4 GLY HA3 H 4.05 . 1 13 . 5 THR H H 8.22 . 1 14 . 5 THR HA H 4.36 . 1 15 . 5 THR HB H 4.31 . 1 16 . 5 THR HG2 H 1.23 . 1 17 . 6 GLY H H 8.59 . 1 18 . 6 GLY HA2 H 3.98 . 1 19 . 6 GLY HA3 H 3.98 . 1 20 . 7 LYS H H 8.23 . 1 21 . 7 LYS HA H 4.32 . 1 22 . 7 LYS HB2 H 1.75 . 2 23 . 7 LYS HB3 H 1.83 . 2 24 . 7 LYS HG2 H 1.39 . 2 25 . 7 LYS HG3 H 1.44 . 2 26 . 7 LYS HD2 H 1.68 . 1 27 . 7 LYS HD3 H 1.68 . 1 28 . 7 LYS HE2 H 3.01 . 1 29 . 7 LYS HE3 H 3.01 . 1 30 . 7 LYS HZ H 7.61 . 1 31 . 8 LEU H H 8.29 . 1 32 . 8 LEU HA H 4.56 . 1 33 . 8 LEU HB2 H 1.67 . 2 34 . 8 LEU HB3 H 1.57 . 2 35 . 8 LEU HG H 1.68 . 1 36 . 8 LEU HD1 H .84 . 2 37 . 8 LEU HD2 H .89 . 2 38 . 9 THR H H 8.57 . 1 39 . 9 THR HA H 4.39 . 1 40 . 9 THR HB H 4.56 . 1 41 . 9 THR HG2 H 1.3 . 1 42 . 10 ARG H H 8.84 . 1 43 . 10 ARG HA H 4.05 . 1 44 . 10 ARG HB2 H 1.89 . 1 45 . 10 ARG HB3 H 1.89 . 1 46 . 10 ARG HG2 H 1.63 . 2 47 . 10 ARG HG3 H 1.77 . 2 48 . 10 ARG HD2 H 3.24 . 1 49 . 10 ARG HD3 H 3.24 . 1 50 . 10 ARG HE H 7.38 . 1 51 . 11 ALA H H 8.52 . 1 52 . 11 ALA HA H 4.16 . 1 53 . 11 ALA HB H 1.43 . 1 54 . 12 GLN H H 8.1 . 1 55 . 12 GLN HA H 4.16 . 1 56 . 12 GLN HB2 H 2.04 . 2 57 . 12 GLN HB3 H 2.27 . 2 58 . 12 GLN HG2 H 2.44 . 1 59 . 12 GLN HG3 H 2.44 . 1 60 . 12 GLN HE21 H 6.89 . 2 61 . 12 GLN HE22 H 7.6 . 2 62 . 13 ARG H H 8.59 . 1 63 . 13 ARG HA H 4.12 . 1 64 . 13 ARG HB2 H 1.9 . 1 65 . 13 ARG HB3 H 1.9 . 1 66 . 13 ARG HG2 H 1.63 . 2 67 . 13 ARG HG3 H 1.77 . 2 68 . 13 ARG HD2 H 3.19 . 2 69 . 13 ARG HD3 H 3.25 . 2 70 . 13 ARG HE H 7.23 . 1 71 . 14 ARG H H 8.33 . 1 72 . 14 ARG HA H 4.18 . 1 73 . 14 ARG HB2 H 1.89 . 1 74 . 14 ARG HB3 H 1.89 . 1 75 . 14 ARG HG2 H 1.64 . 2 76 . 14 ARG HG3 H 1.78 . 2 77 . 14 ARG HD2 H 3.22 . 1 78 . 14 ARG HD3 H 3.22 . 1 79 . 14 ARG HE H 7.35 . 1 80 . 15 ALA H H 8.08 . 1 81 . 15 ALA HA H 4.19 . 1 82 . 15 ALA HB H 1.47 . 1 83 . 16 ALA H H 8.06 . 1 84 . 16 ALA HA H 4.2 . 1 85 . 16 ALA HB H 1.45 . 1 86 . 17 ALA H H 7.96 . 1 87 . 17 ALA HA H 4.26 . 1 88 . 17 ALA HB H 1.47 . 1 89 . 18 ARG H H 7.99 . 1 90 . 18 ARG HA H 4.25 . 1 91 . 18 ARG HB2 H 1.85 . 2 92 . 18 ARG HB3 H 1.91 . 2 93 . 18 ARG HG2 H 1.67 . 2 94 . 18 ARG HG3 H 1.76 . 2 95 . 18 ARG HD2 H 3.23 . 1 96 . 18 ARG HD3 H 3.23 . 1 97 . 18 ARG HE H 7.32 . 1 98 . 19 LYS H H 8.12 . 1 99 . 19 LYS HA H 4.25 . 1 100 . 19 LYS HB2 H 1.82 . 2 101 . 19 LYS HB3 H 1.87 . 2 102 . 19 LYS HG2 H 1.51 . 2 103 . 19 LYS HG3 H 1.43 . 2 104 . 19 LYS HD2 H 1.71 . 1 105 . 19 LYS HD3 H 1.71 . 1 106 . 19 LYS HE2 H 3.01 . 1 107 . 19 LYS HE3 H 3.01 . 1 108 . 19 LYS HZ H 7.61 . 1 109 . 20 ASN H H 8.34 . 1 110 . 20 ASN HA H 4.69 . 1 111 . 20 ASN HB2 H 2.8 . 2 112 . 20 ASN HB3 H 2.87 . 2 113 . 20 ASN HD21 H 7.7 . 2 114 . 20 ASN HD22 H 7.01 . 2 115 . 21 LYS H H 8.29 . 1 116 . 21 LYS HA H 4.3 . 1 117 . 21 LYS HB2 H 1.8 . 2 118 . 21 LYS HB3 H 1.88 . 2 119 . 21 LYS HG2 H 1.44 . 2 120 . 21 LYS HG3 H 1.47 . 2 121 . 21 LYS HD2 H 1.7 . 1 122 . 21 LYS HD3 H 1.7 . 1 123 . 21 LYS HE2 H 3.02 . 1 124 . 21 LYS HE3 H 3.02 . 1 125 . 21 LYS HZ H 7.61 . 1 126 . 22 ARG H H 8.41 . 1 127 . 22 ARG HA H 4.31 . 1 128 . 22 ARG HB2 H 1.81 . 2 129 . 22 ARG HB3 H 1.88 . 2 130 . 22 ARG HG2 H 1.68 . 2 131 . 22 ARG HG3 H 1.63 . 2 132 . 22 ARG HD2 H 3.22 . 1 133 . 22 ARG HD3 H 3.22 . 1 134 . 22 ARG HE H 7.28 . 1 135 . 23 ASN H H 8.58 . 1 136 . 23 ASN HA H 4.8 . 1 137 . 23 ASN HB2 H 2.82 . 2 138 . 23 ASN HB3 H 2.9 . 2 139 . 23 ASN HD21 H 6.99 . 2 140 . 23 ASN HD22 H 7.72 . 2 141 . 24 THR H H 8.25 . 1 142 . 24 THR HA H 4.34 . 1 143 . 24 THR HB H 4.27 . 1 144 . 24 THR HG2 H 1.21 . 1 stop_ save_