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BMRB Entry 19421

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19421
MolProbity Validation Chart

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

Deposition date: 2013-08-12 Original release date: 2015-07-24

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

Citation: Habazettl, Judith; Allan, Martin; Jensen, Pernille; Sass, Hans-Juergen; 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.
promothiocin_A, polymer, 12 residues, 605.680 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
promothiocin_A: SXVGXAXAXXXX

Data sets:
Data typeCount
13C chemical shifts600
15N chemical shifts157
1H chemical shifts980

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TipAS1
2Promothiocin A2

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, Promothiocin A 12 residues - 605.680 Da.

1   SERBB9VALGLYMOZALABB9ALAMOZMH7
2   DHANH2

Samples:

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

sample_2: TipAS, [U-100% 13C; U-100% 15N], 1 mM; promothiocin A 2 mM; potassium phosphate 50 mM; sodium azide 0.02 w/v; H2O 95%; D2O 5%

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

sample_4: TipAS, [U-100% 13C; U-100% 15N], 0.8 mM; promothiocin A 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; pH: 5.9; pressure: 1 atm; temperature: 298 K

sample_conditions_4: ionic strength: 0.055 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)NH TOCSYsample_2isotropicsample_conditions_2
3D HBHA(CO)NHsample_2isotropicsample_conditions_2
3D H(CCO)NH TOCSYsample_2isotropicsample_conditions_2
3D HCCH-TOCSY aliphaticsample_3isotropicsample_conditions_3
3D HNHAsample_2isotropicsample_conditions_2
HAHBsample_3isotropicsample_conditions_3
CBCANHsample_2isotropicsample_conditions_2
13C'-{13C } spin-echo difference 1H-15N HSQCsample_2isotropicsample_conditions_2
15N-{13C } spin-echo difference 1H-15N HSQCsample_2isotropicsample_conditions_2
13C'-{13C } spin-echo difference 1H-13C HSQCsample_2isotropicsample_conditions_2
15N-{13C } spin-echo difference 1H-13C HSQCsample_2isotropicsample_conditions_2
3D 1H-15N ROESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_3
4D 13C-13C-NOESY-HMQCsample_3isotropicsample_conditions_3
2D NOESY filtered against 1H bound to 13C or 15Nsample_3isotropicsample_conditions_3
2D NOESY filtered against 1H bound to 13C or 15Nsample_2isotropicsample_conditions_2
2D HOHAHA filtered against 1H bound to 13C or 15Nsample_3isotropicsample_conditions_3
Doublet-separated sensitivity-enhanced 1H-15N HSQCsample_2isotropicsample_conditions_2
Doublet-separated sensitivity-enhanced 1H-15N HSQCsample_4isotropicsample_conditions_4
J-resolved constant-time 13C-HSQCsample_2isotropicsample_conditions_2
J-resolved constant-time 13C-HSQCsample_4isotropicsample_conditions_4
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_3

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

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

TOPSPIN, Bruker Biospin - experiment/data collection

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

BMRB 19422
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