BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19422

Title: Structural Basis of a Thiopeptide Antibiotic Multidrug Resistance System from Streptomyces lividans:Nosiheptide in Complex with TipAS

Deposition date: 2013-08-12 Original release date: 2014-12-08

Authors: Habazettl, Judith; Allan, Martin; Jensen, Pernille; Sass, Hans-Juergen; Grzesiek, Stephan

Citation: Habazettl, Judith; Allan, Martin; Jensen, Pernille; Sass, J rgen; Grzesiek, Stephan. "Structural Basis of a Thiopeptide Antibiotic Multidrug Resistance System from Streptomyces lividans"  Not known ., .-..

Assembly members:
TipAS, polymer, 144 residues, 16453.025 Da.
nosiheptide, polymer, 14 residues, 1050.172 Da.

Natural source:   Common Name: Streptomyces lividans   Taxonomy ID: 1916   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptomyces lividans

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
TipAS: MGINLTPEEKFEVFGDFDPD QYEEEVRERWGNTDAYRQSK EKTASYTKEDWQRIQDEADE LTRRFVALMDAGEPADSEGA MDAAEDHRQGIARNHYDCGY EMHTCLGEMYVSDERFTRNI DAAKPGLAAYMRDAILANAV RHTP
nosiheptide: SXTXXXXCXXXXXX

Data sets:
Data typeCount
13C chemical shifts600
15N chemical shifts153
1H chemical shifts983

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1TipAS1
2nosiheptide2

Entities:

Entity 1, TipAS 144 residues - 16453.025 Da.

TipAS is the short isoform of TipA. It is the C terminal domain from residue M110 to P253.

1   METGLYILEASNLEUTHRPROGLUGLULYS
2   PHEGLUVALPHEGLYASPPHEASPPROASP
3   GLNTYRGLUGLUGLUVALARGGLUARGTRP
4   GLYASNTHRASPALATYRARGGLNSERLYS
5   GLULYSTHRALASERTYRTHRLYSGLUASP
6   TRPGLNARGILEGLNASPGLUALAASPGLU
7   LEUTHRARGARGPHEVALALALEUMETASP
8   ALAGLYGLUPROALAASPSERGLUGLYALA
9   METASPALAALAGLUASPHISARGGLNGLY
10   ILEALAARGASNHISTYRASPCYSGLYTYR
11   GLUMETHISTHRCYSLEUGLYGLUMETTYR
12   VALSERASPGLUARGPHETHRARGASNILE
13   ASPALAALALYSPROGLYLEUALAALATYR
14   METARGASPALAILELEUALAASNALAVAL
15   ARGHISTHRPRO

Entity 2, nosiheptide 14 residues - 1050.172 Da.

1   SERBB9THRDBUBB93GLBB9CYSBB9MH6
2   BB9DHANH2NO1

Samples:

sample_1: TipAS, [U-98% 15N], 1 mM; nosiheptide 2 mM; potassium phosphate 50 mM; sodium azide 0.02 w/v; H2O 95%; D2O 5%

sample_2: TipAS, [U-99% 13C; U-99% 15N], 1 mM; nosiheptide 2 mM; potassium phosphate 50 mM; sodium azide 0.02 w/v; H2O 95%; D2O 5%

sample_3: TipAS, [U-99% 13C; U-99% 15N], 1 mM; nosiheptide 2 mM; potassium phosphate 50 mM; sodium azide 0.02 w/v; D2O 100%

sample_4: TipAS, [U-99% 13C; U-99% 15N], 0.8 mM; nosiheptide 1.6 mM; potassium phosphate 10 mM; Pf1 phage 10 mg/mL; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.055 M; pH: 5.9; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.055 M; pH: 5.9; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 0.055 M; pD: 5.9; pressure: 1 atm; temperature: 298 K

sample_conditions_4: ionic strength: 0.011 M; pH: 5.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_3
3D HNCOsample_2isotropicsample_conditions_2
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D C(CO)NHsample_2isotropicsample_conditions_2
3D HBHA(CO)NHsample_2isotropicsample_conditions_2
3D HC(CO)NH TOCSYsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_3isotropicsample_conditions_3
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_3
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_3
2D 1H-1H NOESY/filter against 13C-15Nsample_3isotropicsample_conditions_3
2D 1H-1H NOESY/filter against 13C-15Nsample_2isotropicsample_conditions_2
2D 1H-1H TOCSY/filter against 13C-15Nsample_3isotropicsample_conditions_3
Doublet-separated 2D 1H-15N HSQCsample_2isotropicsample_conditions_2
Doublet-separated 2D 1H-15N HSQCsample_4isotropicsample_conditions_4
J-resolved ct 13C-HSQCsample_2isotropicsample_conditions_2
J-resolved ct 13C-HSQCsample_4isotropicsample_conditions_4
3D CBCANHsample_2isotropicsample_conditions_2

Software:

X-PLOR NIH v2.30, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMRPipe v2012, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY v3.115, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - experiment/data collection

PIPP, Garrett - peak picking

XEASY, Bartels et al. - chemical shift assignment

TALOS vTALOS+, Cornilescu, Delaglio and Bax - dihedral angle prediction

ProcheckNMR, Laskowski and MacArthur - structure analysis

xwinnmr, Bruker Biospin - experiment/data collection

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

BMRB 19421
PDB
DBJ BAD11210 BAD11216 BAD11222 BAD11228 BAD11234
EMBL CAB42766
GB AAB27737 AAC13653 AIJ15084 AIV35032 EFD68501
REF NP_627619 WP_003975420 WP_007452041 WP_052836374
SP P0A4T8 P0A4T9

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts