data_36150 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; LPS bound solution NMR structure of WS2-VR18 ; _BMRB_accession_number 36150 _BMRB_flat_file_name bmr36150.str _Entry_type original _Submission_date 2018-01-05 _Accession_date 2018-06-27 _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 Bhunia A. . . 2 Mohid S. A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 88 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-03-06 update BMRB 'update entry citation' 2019-02-04 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 36149 'LPS bound solution structure of WS2-KG18' stop_ _Original_release_date 2018-06-27 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Application of tungsten disulfide quantum dot-conjugated antimicrobial peptides in bio-imaging and antimicrobial therapy. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30658284 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mohid 'Sk Abdul' A. . 2 Ghorai Arup . . 3 Ilyas Humaira . . 4 Mroue Kamal H. . 5 Narayanan Gomathy . . 6 Sarkar Abhisek . . 7 Ray Samit K. . 8 Biswas Kaushik . . 9 Bera 'Amal Kanti' K. . 10 Malmsten Martin . . 11 Midya Anupam . . 12 Bhunia Anirban . . stop_ _Journal_abbreviation 'Colloids Surf. B Biointerfaces' _Journal_name_full 'Colloids and surfaces. B, Biointerfaces' _Journal_volume 176 _Journal_issue . _Journal_ISSN 1873-4367 _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 360 _Page_last 370 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name VAL-ALA-ARG-GLY-TRP-GLY-ARG-LYS-CYS-PRO-LEU-PHE-GLY-LYS-ASN-LYS-SER-ARG _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common VAL-ALA-ARG-GLY-TRP-GLY-ARG-LYS-CYS-PRO-LEU-PHE-GLY-LYS-ASN-LYS-SER-ARG _Molecular_mass 2066.479 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 18 _Mol_residue_sequence ; VARGWGRKCPLFGKNKSR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 VAL 2 2 ALA 3 3 ARG 4 4 GLY 5 5 TRP 6 6 GLY 7 7 ARG 8 8 LYS 9 9 CYS 10 10 PRO 11 11 LEU 12 12 PHE 13 13 GLY 14 14 LYS 15 15 ASN 16 16 LYS 17 17 SER 18 18 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 . 32630 . . . . 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 $entity_1 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details '0.5 mM VAL-ALA-ARG-GLY-TRP-GLY-ARG-LYS-CYS-PRO-LEU-PHE-GLY-LYS-ASN-LYS-SER-ARG, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.5 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_software_2 _Saveframe_category software _Name SPARKY _Version 3.114 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name TOPSPIN _Version 3.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AvanceIII _Field_strength 700 _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_trNOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D trNOESY' _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 . mM pH 4.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 TSP H 1 protons ppm 0 external direct . . . 1 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H TOCSY' '2D trNOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name entity_1 _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 ALA H H 8.664 0.006 1 2 2 2 ALA HA H 4.390 0.002 1 3 2 2 ALA HB H 1.385 0.004 1 4 3 3 ARG H H 8.511 0.015 1 5 3 3 ARG HA H 4.255 0.002 1 6 3 3 ARG HB2 H 1.743 0.000 2 7 3 3 ARG HB3 H 1.743 0.000 2 8 3 3 ARG HG2 H 1.601 0.000 2 9 3 3 ARG HG3 H 1.601 0.000 2 10 3 3 ARG HD2 H 3.158 0.000 2 11 3 3 ARG HD3 H 3.158 0.000 2 12 4 4 GLY H H 8.457 0.016 1 13 4 4 GLY HA2 H 3.908 0.000 2 14 4 4 GLY HA3 H 3.908 0.000 2 15 5 5 TRP H H 8.103 0.015 1 16 5 5 TRP HA H 4.661 0.001 1 17 5 5 TRP HB2 H 3.349 0.001 1 18 5 5 TRP HB3 H 3.256 0.000 1 19 5 5 TRP HE3 H 7.628 0.000 1 20 5 5 TRP HZ3 H 7.195 0.001 1 21 5 5 TRP HH2 H 7.259 0.004 1 22 6 6 GLY H H 8.342 0.013 1 23 6 6 GLY HA2 H 3.824 0.000 2 24 6 6 GLY HA3 H 3.824 0.000 2 25 7 7 ARG H H 8.098 0.012 1 26 7 7 ARG HA H 4.270 0.001 1 27 7 7 ARG HB2 H 1.829 0.000 1 28 7 7 ARG HB3 H 1.716 0.001 1 29 7 7 ARG HG2 H 1.598 0.001 2 30 7 7 ARG HG3 H 1.598 0.001 2 31 8 8 LYS H H 8.453 0.014 1 32 8 8 LYS HA H 4.334 0.000 1 33 8 8 LYS HB2 H 1.821 0.000 1 34 8 8 LYS HB3 H 1.743 0.000 1 35 8 8 LYS HG2 H 1.433 0.000 2 36 8 8 LYS HG3 H 1.433 0.000 2 37 9 9 CYS H H 8.381 0.013 1 38 9 9 CYS HA H 4.747 0.001 1 39 9 9 CYS HB2 H 2.878 0.000 2 40 9 9 CYS HB3 H 2.878 0.000 2 41 10 10 PRO HA H 4.364 0.000 1 42 10 10 PRO HB2 H 2.204 0.117 1 43 10 10 PRO HB3 H 1.970 0.117 1 44 10 10 PRO HD2 H 3.719 0.000 2 45 10 10 PRO HD3 H 3.719 0.000 2 46 11 11 LEU H H 8.175 0.016 1 47 11 11 LEU HA H 4.267 0.002 1 48 11 11 LEU HB2 H 1.529 0.007 2 49 11 11 LEU HB3 H 1.529 0.007 2 50 11 11 LEU HG H 1.439 0.001 1 51 11 11 LEU HD1 H 0.857 0.014 2 52 11 11 LEU HD2 H 0.857 0.014 2 53 12 12 PHE H H 8.165 0.014 1 54 12 12 PHE HA H 4.640 0.003 1 55 12 12 PHE HB2 H 3.167 0.002 1 56 12 12 PHE HB3 H 3.040 0.002 1 57 12 12 PHE HE1 H 7.356 0.001 1 58 12 12 PHE HE2 H 7.356 0.001 1 59 12 12 PHE HZ H 7.310 0.000 1 60 13 13 GLY H H 8.361 0.010 1 61 13 13 GLY HA2 H 3.908 0.001 2 62 13 13 GLY HA3 H 3.908 0.001 2 63 14 14 LYS H H 8.232 0.020 1 64 14 14 LYS HA H 4.312 0.000 1 65 14 14 LYS HB2 H 1.843 0.000 1 66 14 14 LYS HB3 H 1.751 0.000 1 67 14 14 LYS HG2 H 1.434 0.000 2 68 14 14 LYS HG3 H 1.434 0.000 2 69 15 15 ASN H H 8.508 0.010 1 70 15 15 ASN HA H 4.683 0.000 1 71 15 15 ASN HB2 H 2.851 0.001 1 72 15 15 ASN HB3 H 2.776 0.002 1 73 16 16 LYS H H 8.321 0.014 1 74 16 16 LYS HA H 4.359 0.000 1 75 16 16 LYS HB2 H 1.875 0.000 1 76 16 16 LYS HB3 H 1.763 0.000 1 77 16 16 LYS HG2 H 1.437 0.000 2 78 16 16 LYS HG3 H 1.437 0.000 2 79 17 17 SER H H 8.404 0.009 1 80 17 17 SER HA H 4.439 0.000 1 81 17 17 SER HB2 H 3.889 0.000 2 82 17 17 SER HB3 H 3.889 0.000 2 83 18 18 ARG H H 7.995 0.017 1 84 18 18 ARG HA H 4.177 0.000 1 85 18 18 ARG HB2 H 1.860 0.000 1 86 18 18 ARG HB3 H 1.738 0.000 1 87 18 18 ARG HG2 H 1.621 0.000 2 88 18 18 ARG HG3 H 1.621 0.000 2 stop_ save_