BMRB Entry 26026

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26026
MolProbity Validation Chart

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Title:
Solution Structure of the PriC DNA replication restart protein
Deposition date:
2016-04-07
Original release date:
2016-07-05
Authors:
Cornilescu, Claudia; Cornilescu, Gabriel; Wessel, Sarah; Keck, James; Markley, John
Citation:

Citation: Wessel, Sarah; Cornilescu, Claudia; Cornilescu, Gabriel; Hu, Kaifeng; Sandler, Steven; Markley, John; Keck, James. "Structure and Function of the PriC DNA Replication Restart Protein"  J. Biol. Chem. 291, 18384-18396 (2016).
PubMed: 27382050

Assembly members:

Assembly members:
PriC, polymer, 171 residues, 19733.648 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: T7-inducible overexpression

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PriC: MRTPLLLQSLKTRVAALHTL IGPLASQRHFSPRFDRQLFA CRGARLGDYLTEAEESLTHL EAAVNQGDATRVAWLAERLA AQIEALQREAATATLRRHEN AHLPGGRLHARLAEYQEYER RLLAMKNEREQRYAERHDPQ LAREITALDERLTRCRTAIA RTERALERITR

Data sets:
Data typeCount
13C chemical shifts568
15N chemical shifts134
1H chemical shifts794

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PriC DNA replication restart protein1

Entities:

Entity 1, PriC DNA replication restart protein 171 residues - 19733.648 Da.

1   METARGTHRPROLEULEULEUGLNSERLEU
2   LYSTHRARGVALALAALALEUHISTHRLEU
3   ILEGLYPROLEUALASERGLNARGHISPHE
4   SERPROARGPHEASPARGGLNLEUPHEALA
5   CYSARGGLYALAARGLEUGLYASPTYRLEU
6   THRGLUALAGLUGLUSERLEUTHRHISLEU
7   GLUALAALAVALASNGLNGLYASPALATHR
8   ARGVALALATRPLEUALAGLUARGLEUALA
9   ALAGLNILEGLUALALEUGLNARGGLUALA
10   ALATHRALATHRLEUARGARGHISGLUASN
11   ALAHISLEUPROGLYGLYARGLEUHISALA
12   ARGLEUALAGLUTYRGLNGLUTYRGLUARG
13   ARGLEULEUALAMETLYSASNGLUARGGLU
14   GLNARGTYRALAGLUARGHISASPPROGLN
15   LEUALAARGGLUILETHRALALEUASPGLU
16   ARGLEUTHRARGCYSARGTHRALAILEALA
17   ARGTHRGLUARGALALEUGLUARGILETHR
18   ARG

Samples:

sample_PriC: PriC, [U-13C; U-15N], 0.5 mM; MES 20 mM; DTT 5 mM; EDTA 1 mM

aligned-PriC: PriC, [U-13C; U-15N], 0.5 mM

MES: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_PriCisotropicMES
3D HNCOsample_PriCisotropicMES
3D CBCA(CO)NHsample_PriCisotropicMES
3D HNCACBsample_PriCisotropicMES
3D C(CO)NHsample_PriCisotropicMES
3D H(CCO)NHsample_PriCisotropicMES
3D HBHA(CO)NHsample_PriCisotropicMES
3D HCCH-TOCSYsample_PriCisotropicMES
3D 1H-15N NOESYsample_PriCisotropicMES
3D 1H-13C NOESY aliphaticsample_PriCisotropicMES
3D 1H-13C NOESY aromaticsample_PriCisotropicMES
(HB)CB(CGCD)HDsample_PriCisotropicMES
(HB)CB(CGCDCE)HEsample_PriCisotropicMES
2D 1H-13C HSQC aliphaticsample_PriCisotropicMES
2D ARTSYsample_PriCisotropicMES
2D ARTSYaligned-PriCanisotropicMES
3D HCA(CO)Nsample_PriCisotropicMES
3D HCA(CO)Naligned-PriCanisotropicMES

Software:

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

PIPP, Garrett - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - dihedral angle prediction

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinement, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz
  • Bruker Avance 750 MHz
  • Varian INOVA 900 MHz

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