data_36149 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; LPS bound solution structure of WS2-KG18 ; _BMRB_accession_number 36149 _BMRB_flat_file_name bmr36149.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" 100 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 36150 'LPS bound solution NMR structure of WS2-VR18' 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 LYS-ASN-LYS-SER-ARG-VAL-ALA-ARG-GLY-TRP-GLY-ARG-LYS-CYS-PRO-LEU-PHE-GLY _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 LYS-ASN-LYS-SER-ARG-VAL-ALA-ARG-GLY-TRP-GLY-ARG-LYS-CYS-PRO-LEU-PHE-GLY _Molecular_mass 2066.479 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 18 _Mol_residue_sequence ; KNKSRVARGWGRKCPLFG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 LYS 2 2 ASN 3 3 LYS 4 4 SER 5 5 ARG 6 6 VAL 7 7 ALA 8 8 ARG 9 9 GLY 10 10 TRP 11 11 GLY 12 12 ARG 13 13 LYS 14 14 CYS 15 15 PRO 16 16 LEU 17 17 PHE 18 18 GLY 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 LYS-ASN-LYS-SER-ARG-VAL-ALA-ARG-GLY-TRP-GLY-ARG-LYS-CYS-PRO-LEU-PHE-GLY, 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 1 1 LYS HA H 3.722 0.000 1 2 1 1 LYS HB2 H 1.980 0.000 1 3 1 1 LYS HB3 H 1.861 0.000 1 4 1 1 LYS HG2 H 1.358 0.000 2 5 1 1 LYS HG3 H 1.358 0.000 2 6 2 2 ASN H H 8.329 0.014 1 7 2 2 ASN HA H 4.748 0.026 1 8 2 2 ASN HB2 H 2.876 0.004 2 9 2 2 ASN HB3 H 2.876 0.004 2 10 3 3 LYS H H 8.636 0.010 1 11 3 3 LYS HA H 4.340 0.000 1 12 3 3 LYS HB2 H 1.866 0.001 1 13 3 3 LYS HB3 H 1.755 0.003 1 14 3 3 LYS HG2 H 1.468 0.001 2 15 3 3 LYS HG3 H 1.468 0.001 2 16 3 3 LYS HE2 H 3.006 0.001 2 17 3 3 LYS HE3 H 3.006 0.001 2 18 4 4 SER H H 8.404 0.006 1 19 4 4 SER HA H 4.422 0.008 1 20 4 4 SER HB2 H 3.878 0.004 2 21 4 4 SER HB3 H 3.878 0.004 2 22 5 5 ARG H H 8.513 0.006 1 23 5 5 ARG HA H 4.363 0.004 1 24 5 5 ARG HB2 H 1.860 0.005 1 25 5 5 ARG HB3 H 1.743 0.003 1 26 5 5 ARG HG2 H 1.620 0.006 2 27 5 5 ARG HG3 H 1.620 0.006 2 28 5 5 ARG HD2 H 3.188 0.009 2 29 5 5 ARG HD3 H 3.188 0.009 2 30 6 6 VAL H H 8.168 0.014 1 31 6 6 VAL HA H 4.071 0.007 1 32 6 6 VAL HB H 2.030 0.019 1 33 6 6 VAL HG1 H 0.924 0.007 2 34 6 6 VAL HG2 H 0.924 0.007 2 35 7 7 ALA H H 8.392 0.003 1 36 7 7 ALA HA H 4.317 0.000 1 37 7 7 ALA HB H 1.363 0.015 1 38 8 8 ARG H H 8.089 0.014 1 39 8 8 ARG HA H 4.287 0.000 1 40 8 8 ARG HB2 H 1.842 0.000 1 41 8 8 ARG HB3 H 1.720 0.000 1 42 8 8 ARG HG2 H 1.603 0.005 2 43 8 8 ARG HG3 H 1.603 0.005 2 44 8 8 ARG HD2 H 3.006 0.006 2 45 8 8 ARG HD3 H 3.006 0.006 2 46 9 9 GLY H H 8.398 0.007 1 47 9 9 GLY HA2 H 3.913 0.004 2 48 9 9 GLY HA3 H 3.913 0.004 2 49 10 10 TRP H H 8.102 0.001 1 50 10 10 TRP HA H 4.662 0.010 1 51 10 10 TRP HB2 H 3.351 0.001 1 52 10 10 TRP HB3 H 3.252 0.001 1 53 10 10 TRP HD1 H 7.298 0.004 1 54 10 10 TRP HE3 H 7.620 0.002 1 55 10 10 TRP HZ2 H 7.501 0.000 1 56 10 10 TRP HH2 H 7.251 0.004 1 57 11 11 GLY H H 8.346 0.001 1 58 11 11 GLY HA2 H 3.860 0.002 1 59 11 11 GLY HA3 H 3.808 0.006 1 60 12 12 ARG H H 8.326 0.004 1 61 12 12 ARG HA H 4.311 0.000 1 62 12 12 ARG HB2 H 1.737 0.000 2 63 12 12 ARG HB3 H 1.737 0.000 2 64 12 12 ARG HG2 H 1.585 0.004 2 65 12 12 ARG HG3 H 1.585 0.004 2 66 12 12 ARG HD2 H 3.135 0.000 2 67 12 12 ARG HD3 H 3.135 0.000 2 68 13 13 LYS H H 8.451 0.009 1 69 13 13 LYS HA H 4.322 0.000 1 70 13 13 LYS HB2 H 1.833 0.000 1 71 13 13 LYS HB3 H 1.673 0.000 1 72 13 13 LYS HG2 H 1.382 0.000 2 73 13 13 LYS HG3 H 1.382 0.000 2 74 13 13 LYS HE2 H 2.989 0.000 2 75 13 13 LYS HE3 H 2.989 0.000 2 76 14 14 CYS H H 8.450 0.010 1 77 14 14 CYS HA H 4.736 0.001 1 78 14 14 CYS HB2 H 3.199 0.000 1 79 14 14 CYS HB3 H 2.882 0.000 1 80 15 15 PRO HA H 4.360 0.000 1 81 15 15 PRO HB2 H 2.207 0.000 1 82 15 15 PRO HB3 H 1.976 0.001 1 83 15 15 PRO HD2 H 3.727 0.002 2 84 15 15 PRO HD3 H 3.727 0.002 2 85 16 16 LEU H H 8.096 0.004 1 86 16 16 LEU HA H 4.203 0.003 1 87 16 16 LEU HB2 H 1.481 0.000 2 88 16 16 LEU HB3 H 1.481 0.000 2 89 16 16 LEU HG H 1.394 0.007 1 90 16 16 LEU HD1 H 0.854 0.001 2 91 16 16 LEU HD2 H 0.854 0.001 2 92 17 17 PHE H H 8.064 0.020 1 93 17 17 PHE HA H 4.705 0.002 1 94 17 17 PHE HB2 H 3.225 0.004 1 95 17 17 PHE HB3 H 3.017 0.004 1 96 17 17 PHE HE1 H 7.350 0.001 1 97 17 17 PHE HE2 H 7.350 0.001 1 98 18 18 GLY H H 7.932 0.017 1 99 18 18 GLY HA2 H 3.757 0.000 2 100 18 18 GLY HA3 H 3.757 0.000 2 stop_ save_