data_15140 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Proton chemical shifts of mytilin ; _BMRB_accession_number 15140 _BMRB_flat_file_name bmr15140.str _Entry_type original _Submission_date 2007-02-22 _Accession_date 2007-02-22 _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 Roch Philippe . . 2 Yang Yinshan . . 3 Aumelas Andre . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 204 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-02 update BMRB 'complete entry citation' 2007-10-24 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_Citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR structure of mussel mytilin, and antiviral-antibacterial activities of derived synthetic peptides.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17628674 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Roch Philippe . Dr. 2 Yang Yinshan . Dr. 3 Toubianaa Mylene . Dr. 4 Aumelas Andre . Dr. stop_ _Journal_abbreviation 'Dev. Comp. Immunol.' _Journal_volume 32 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 227 _Page_last 238 _Year 2007 _Details . loop_ _Keyword 'antimicrobial peptide' antiviral 'Disulfide bond' mussel mytilin stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name mytilin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Mytilin structure' $mytilin 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_mytilin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common mytilin _Molecular_mass . _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function Antiviral Antmicrobial stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 34 _Mol_residue_sequence ; SCASRCKGHCRARRCGYYVS VLYRGRCYCKCLRC ; loop_ _Residue_seq_code _Residue_label 1 SER 2 CYS 3 ALA 4 SER 5 ARG 6 CYS 7 LYS 8 GLY 9 HIS 10 CYS 11 ARG 12 ALA 13 ARG 14 ARG 15 CYS 16 GLY 17 TYR 18 TYR 19 VAL 20 SER 21 VAL 22 LEU 23 TYR 24 ARG 25 GLY 26 ARG 27 CYS 28 TYR 29 CYS 30 LYS 31 CYS 32 LEU 33 ARG 34 CYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 2EEM "Solution Structure Of The Synthetic Mytilin" 100.00 34 100.00 100.00 4.32e-12 GB AAD45013 "mytilin B antimicrobial peptide precursor [Mytilus galloprovincialis]" 100.00 103 100.00 100.00 3.33e-14 GB AAD52661 "mytilin B precursor [Mytilus galloprovincialis]" 100.00 103 100.00 100.00 3.33e-14 GB AEE60903 "mytilin [Mytilus chilensis]" 100.00 100 100.00 100.00 3.13e-14 SP P81613 "RecName: Full=Mytilin-B" 100.00 34 100.00 100.00 4.32e-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 $mytilin 'Mediterranean mussel' 29158 Eukaryota Metazoa Mytilus galloprovincialis 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 $mytilin 'chemical synthesis' . Synthetic Synthetic . . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $mytilin . mM 0.8 1.0 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version 3.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_GIFA _Saveframe_category software _Name GIFA _Version . loop_ _Vendor _Address _Electronic_address Delsuc . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version . loop_ _Vendor _Address _Electronic_address Brunger . . stop_ loop_ _Task 'geometry optimization' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_nmr_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _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' . . M pH 3.3 . pH pressure 1 . atm temperature 295 . 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 COSY' '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 'Mytilin structure' _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 SER HA H 4.24 0.01 1 2 1 1 SER HB2 H 4.32 0.01 2 3 1 1 SER HB3 H 4.07 0.01 2 4 2 2 CYS H H 9.39 0.01 1 5 2 2 CYS HA H 4.47 0.01 1 6 2 2 CYS HB2 H 3.23 0.01 1 7 2 2 CYS HB3 H 2.81 0.01 1 8 3 3 ALA H H 8.35 0.01 1 9 3 3 ALA HA H 4.10 0.01 1 10 3 3 ALA HB H 1.41 0.01 1 11 4 4 SER H H 8.27 0.01 1 12 4 4 SER HA H 3.86 0.01 1 13 4 4 SER HB2 H 3.86 0.01 2 14 4 4 SER HB3 H 3.73 0.01 2 15 5 5 ARG H H 8.28 0.01 1 16 5 5 ARG HA H 4.02 0.01 1 17 5 5 ARG HB2 H 1.86 0.01 2 18 5 5 ARG HB3 H 1.77 0.01 2 19 5 5 ARG HG2 H 1.49 0.01 1 20 5 5 ARG HG3 H 1.49 0.01 1 21 5 5 ARG HD2 H 3.09 0.01 1 22 5 5 ARG HD3 H 3.09 0.01 1 23 5 5 ARG HE H 7.11 0.01 1 24 6 6 CYS H H 8.30 0.01 1 25 6 6 CYS HA H 4.55 0.01 1 26 6 6 CYS HB2 H 2.60 0.01 1 27 6 6 CYS HB3 H 3.13 0.01 1 28 7 7 LYS H H 8.17 0.01 1 29 7 7 LYS HA H 2.77 0.01 1 30 7 7 LYS HB2 H 1.41 0.01 2 31 7 7 LYS HB3 H 0.95 0.01 2 32 7 7 LYS HG2 H 1.06 0.01 1 33 7 7 LYS HG3 H 1.06 0.01 1 34 7 7 LYS HD2 H 1.53 0.01 1 35 7 7 LYS HD3 H 1.53 0.01 1 36 7 7 LYS HE2 H 2.87 0.01 1 37 7 7 LYS HE3 H 2.87 0.01 1 38 8 8 GLY H H 7.59 0.01 1 39 8 8 GLY HA2 H 3.85 0.01 2 40 8 8 GLY HA3 H 3.69 0.01 2 41 9 9 HIS H H 8.26 0.01 1 42 9 9 HIS HA H 4.33 0.01 1 43 9 9 HIS HB2 H 3.42 0.01 1 44 9 9 HIS HB3 H 3.22 0.01 1 45 9 9 HIS HD2 H 6.88 0.01 1 46 9 9 HIS HE1 H 8.34 0.01 1 47 10 10 CYS H H 8.85 0.01 1 48 10 10 CYS HA H 4.37 0.01 1 49 10 10 CYS HB2 H 2.81 0.01 1 50 10 10 CYS HB3 H 2.54 0.01 1 51 11 11 ARG H H 8.42 0.01 1 52 11 11 ARG HA H 4.17 0.01 1 53 11 11 ARG HB2 H 1.88 0.01 1 54 11 11 ARG HB3 H 1.88 0.01 1 55 11 11 ARG HG2 H 1.69 0.01 2 56 11 11 ARG HG3 H 1.59 0.01 2 57 11 11 ARG HD2 H 3.14 0.01 1 58 11 11 ARG HD3 H 3.14 0.01 1 59 11 11 ARG HE H 7.19 0.01 1 60 12 12 ALA H H 7.82 0.01 1 61 12 12 ALA HA H 4.12 0.01 1 62 12 12 ALA HB H 1.47 0.01 1 63 13 13 ARG H H 7.06 0.01 1 64 13 13 ARG HA H 4.20 0.01 1 65 13 13 ARG HB2 H 2.11 0.01 2 66 13 13 ARG HB3 H 1.69 0.01 2 67 13 13 ARG HG2 H 1.51 0.01 1 68 13 13 ARG HG3 H 1.51 0.01 1 69 13 13 ARG HD2 H 3.00 0.01 2 70 13 13 ARG HD3 H 2.93 0.01 2 71 13 13 ARG HE H 7.12 0.01 1 72 14 14 ARG H H 7.95 0.01 1 73 14 14 ARG HA H 3.85 0.01 1 74 14 14 ARG HB2 H 2.15 0.01 2 75 14 14 ARG HB3 H 1.96 0.01 2 76 14 14 ARG HG2 H 1.51 0.01 1 77 14 14 ARG HG3 H 1.51 0.01 1 78 14 14 ARG HD2 H 3.17 0.01 1 79 14 14 ARG HD3 H 3.17 0.01 1 80 14 14 ARG HE H 7.14 0.01 1 81 15 15 CYS H H 7.88 0.01 1 82 15 15 CYS HA H 5.08 0.01 1 83 15 15 CYS HB2 H 2.96 0.01 1 84 15 15 CYS HB3 H 3.34 0.01 1 85 16 16 GLY H H 8.48 0.01 1 86 16 16 GLY HA2 H 4.01 0.01 1 87 16 16 GLY HA3 H 3.76 0.01 1 88 17 17 TYR H H 8.18 0.01 1 89 17 17 TYR HA H 4.83 0.01 1 90 17 17 TYR HB2 H 2.87 0.01 2 91 17 17 TYR HB3 H 2.62 0.01 2 92 17 17 TYR HD1 H 7.06 0.01 1 93 17 17 TYR HD2 H 7.06 0.01 1 94 17 17 TYR HE1 H 6.71 0.01 1 95 17 17 TYR HE2 H 6.71 0.01 1 96 18 18 TYR H H 6.89 0.01 1 97 18 18 TYR HA H 5.40 0.01 1 98 18 18 TYR HB2 H 3.07 0.01 2 99 18 18 TYR HB3 H 2.76 0.01 2 100 18 18 TYR HD1 H 6.60 0.01 1 101 18 18 TYR HD2 H 6.60 0.01 1 102 18 18 TYR HE1 H 6.63 0.01 1 103 18 18 TYR HE2 H 6.63 0.01 1 104 19 19 VAL H H 8.92 0.01 1 105 19 19 VAL HA H 3.99 0.01 1 106 19 19 VAL HB H 1.83 0.01 1 107 19 19 VAL HG1 H 0.82 0.01 1 108 19 19 VAL HG2 H 0.82 0.01 1 109 20 20 SER H H 8.72 0.01 1 110 20 20 SER HA H 5.67 0.01 1 111 20 20 SER HB2 H 4.11 0.01 1 112 20 20 SER HB3 H 3.68 0.01 1 113 21 21 VAL H H 8.67 0.01 1 114 21 21 VAL HA H 4.29 0.01 1 115 21 21 VAL HB H 2.00 0.01 1 116 21 21 VAL HG1 H 0.85 0.01 1 117 21 21 VAL HG2 H 0.85 0.01 1 118 22 22 LEU H H 8.47 0.01 1 119 22 22 LEU HA H 5.29 0.01 1 120 22 22 LEU HB2 H 1.72 0.01 2 121 22 22 LEU HB3 H 1.36 0.01 2 122 22 22 LEU HG H 1.39 0.01 1 123 22 22 LEU HD1 H 0.82 0.01 2 124 22 22 LEU HD2 H 0.71 0.01 2 125 23 23 TYR H H 9.22 0.01 1 126 23 23 TYR HA H 4.87 0.01 1 127 23 23 TYR HB2 H 2.85 0.01 1 128 23 23 TYR HB3 H 2.85 0.01 1 129 23 23 TYR HD1 H 7.10 0.01 1 130 23 23 TYR HD2 H 7.10 0.01 1 131 23 23 TYR HE1 H 6.76 0.01 1 132 23 23 TYR HE2 H 6.76 0.01 1 133 24 24 ARG H H 9.33 0.01 1 134 24 24 ARG HA H 3.58 0.01 1 135 24 24 ARG HB2 H 0.49 0.01 1 136 24 24 ARG HB3 H 0.97 0.01 1 137 24 24 ARG HG2 H 1.73 0.01 2 138 24 24 ARG HG3 H 1.34 0.01 2 139 24 24 ARG HD2 H 2.86 0.01 1 140 24 24 ARG HD3 H 2.86 0.01 1 141 24 24 ARG HE H 6.86 0.01 1 142 25 25 GLY H H 8.48 0.01 1 143 25 25 GLY HA2 H 4.04 0.01 2 144 25 25 GLY HA3 H 3.46 0.01 1 145 26 26 ARG H H 7.89 0.01 1 146 26 26 ARG HA H 4.45 0.01 1 147 26 26 ARG HB2 H 1.77 0.01 2 148 26 26 ARG HB3 H 1.64 0.01 2 149 26 26 ARG HG2 H 1.50 0.01 2 150 26 26 ARG HG3 H 1.21 0.01 2 151 26 26 ARG HD2 H 3.07 0.01 1 152 26 26 ARG HD3 H 3.07 0.01 1 153 26 26 ARG HE H 6.97 0.01 1 154 27 27 CYS H H 8.58 0.01 1 155 27 27 CYS HA H 5.10 0.01 1 156 27 27 CYS HB2 H 2.86 0.01 1 157 27 27 CYS HB3 H 2.74 0.01 1 158 28 28 TYR H H 9.61 0.01 1 159 28 28 TYR HA H 4.57 0.01 1 160 28 28 TYR HB2 H 2.99 0.01 2 161 28 28 TYR HB3 H 2.94 0.01 2 162 28 28 TYR HD1 H 7.18 0.01 1 163 28 28 TYR HD2 H 7.18 0.01 1 164 28 28 TYR HE1 H 6.91 0.01 1 165 28 28 TYR HE2 H 6.91 0.01 1 166 29 29 CYS H H 8.68 0.01 1 167 29 29 CYS HA H 5.30 0.01 1 168 29 29 CYS HB2 H 2.52 0.01 1 169 29 29 CYS HB3 H 2.72 0.01 1 170 30 30 LYS H H 9.05 0.01 1 171 30 30 LYS HA H 4.68 0.01 1 172 30 30 LYS HB2 H 1.78 0.01 2 173 30 30 LYS HB3 H 1.66 0.01 2 174 30 30 LYS HG2 H 1.33 0.01 2 175 30 30 LYS HG3 H 1.30 0.01 2 176 30 30 LYS HD2 H 1.62 0.01 1 177 30 30 LYS HD3 H 1.62 0.01 1 178 30 30 LYS HE2 H 2.86 0.01 1 179 30 30 LYS HE3 H 2.86 0.01 1 180 30 30 LYS HZ H 7.54 0.01 1 181 31 31 CYS H H 8.85 0.01 1 182 31 31 CYS HA H 4.37 0.01 1 183 31 31 CYS HB2 H 3.16 0.01 2 184 31 31 CYS HB3 H 2.66 0.01 2 185 32 32 LEU H H 8.39 0.01 1 186 32 32 LEU HA H 4.68 0.01 1 187 32 32 LEU HB2 H 1.57 0.01 2 188 32 32 LEU HB3 H 1.26 0.01 2 189 32 32 LEU HG H 1.40 0.01 1 190 32 32 LEU HD1 H 0.84 0.01 2 191 32 32 LEU HD2 H 0.76 0.01 2 192 33 33 ARG H H 8.99 0.01 1 193 33 33 ARG HA H 3.92 0.01 1 194 33 33 ARG HB2 H 1.94 0.01 2 195 33 33 ARG HB3 H 1.84 0.01 1 196 33 33 ARG HG2 H 1.55 0.01 2 197 33 33 ARG HG3 H 1.52 0.01 2 198 33 33 ARG HD2 H 3.11 0.01 2 199 33 33 ARG HD3 H 3.02 0.01 2 200 33 33 ARG HE H 7.17 0.01 1 201 34 34 CYS H H 8.80 0.01 1 202 34 34 CYS HA H 4.71 0.01 1 203 34 34 CYS HB2 H 2.89 0.01 1 204 34 34 CYS HB3 H 3.17 0.01 1 stop_ save_