BMRB Entry 17734

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17734
MolProbity Validation Chart

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Title:
Solution NMR structure of N-terminal domain of Salmonella effector protein PipB2. Northeast structural genomics consortium (NESG) target stt318a
Deposition date:
2011-06-27
Original release date:
2011-07-18
Authors:
Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Garcia, Maite; Daniels, Craig; Savchenko, Alexei; Arrowsmith, Cheryl
Citation:

Citation: Lemak, Alexander; Yee, Adelinda; Houliston, Scott; Garcia, Maite; Daniels, Craig; Savchenko, Alexei; Arrowsmith, Cheryl. "NMR solution structure of N-terminal domain of Salmonella effector protein PipB2"  .

Assembly members:

Assembly members:
PipB2, polymer, 145 residues, 13410.311 Da.

Natural source:

Natural source:   Common Name: Salmonella typhimurium   Taxonomy ID: 99287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salmonella typhimurium

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: p15Tv lic

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PipB2: GAGTSAAMRQATSPKTILEY IINFFTCGGIRRRNETQYQE LIETMAETLKSTMPDRGAPL PENIILDDMDGCRVEFNLPG ENNEAGQVIVRVSKGDHSET REIPLASFEKICRALLFRCE FSLPQDSVILTAQGGMNLKG AVLTG

Data sets:
Data typeCount
13C chemical shifts575
15N chemical shifts133
1H chemical shifts937

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PipB21

Entities:

Entity 1, PipB2 145 residues - 13410.311 Da.

1   GLYALAGLYTHRSERALAALAMETARGGLN
2   ALATHRSERPROLYSTHRILELEUGLUTYR
3   ILEILEASNPHEPHETHRCYSGLYGLYILE
4   ARGARGARGASNGLUTHRGLNTYRGLNGLU
5   LEUILEGLUTHRMETALAGLUTHRLEULYS
6   SERTHRMETPROASPARGGLYALAPROLEU
7   PROGLUASNILEILELEUASPASPMETASP
8   GLYCYSARGVALGLUPHEASNLEUPROGLY
9   GLUASNASNGLUALAGLYGLNVALILEVAL
10   ARGVALSERLYSGLYASPHISSERGLUTHR
11   ARGGLUILEPROLEUALASERPHEGLULYS
12   ILECYSARGALALEULEUPHEARGCYSGLU
13   PHESERLEUPROGLNASPSERVALILELEU
14   THRALAGLNGLYGLYMETASNLEULYSGLY
15   ALAVALLEUTHRGLY

Samples:

sample_1: PipB2, [U-13C; U-15N], 0.5 mM; TRIS 10 mM; sodium chloride 300 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 300 mM; pH: 7.0; pressure: ambient atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - peak picking

FMC, Lemak,Steren,Llinas, Arrowsmith - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

PSVS, Bhattacharya and Montelione - validation

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAJ37775 BAP08680
EMBL CAR34204 CAR60691 CBG25753 CBW18862 CCW75481
GB AAL21665 AAS66036 AAV78500 AAX66616 ABX68796
REF NP_461706 WP_000442272 WP_001540738 WP_001667622 WP_001670212
SP Q57KZ6 Q5PEX4 Q8ZMM8
AlphaFold Q57KZ6 Q5PEX4 Q8ZMM8

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks