BMRB Entry 10027

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10027
MolProbity Validation Chart

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Title:
chemical shift assignment of DnaA domain I-II
Deposition date:
2006-10-05
Original release date:
2007-06-26
Authors:
Abe, Yoshito; Watanabe, Noriko; Yoshida, Yuichiro; Katayama, Tsutomu; Ueda, Tadashi
Citation:

Citation: Yoshito, Abe; Noriko, Watanabe; Yuichiro, Yoshida; Fumi, Ebata; Tsutomu, Katayama; Tadashi, Ueda. "Assignment of 1H, 13C and 15N resonances of N-terminal domain of DnaA protein"  Biomol. NMR Assignments 1, 57-59 (2007).
PubMed: 19636826

Assembly members:

Assembly members:
N-terminal domain of DnaA, polymer, 107 residues, 11000 Da.

Natural source:

Natural source:   Common Name: Bacterium coli   Taxonomy ID: 83333   Superkingdom: Eubacteria   Kingdom: Protista   Genus/species: Escherichia Coli

Experimental source:

Experimental source:   Production method: recombinant technology   Vector: pET-22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N-terminal domain of DnaA: SLSLWQQCLARLQDELPATE FSMWIRPLQAELSDNTLALY APNRFVLDWVRDKYLNNING LLTSFCGADAPQLRFEVGTK PVTQTPQAAVTSNVAAPAQV AQTQPQR

Data sets:
  • assigned_chemical_shifts
Data typeCount
13C chemical shifts519
15N chemical shifts126
1H chemical shifts830

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal domain of DnaA1

Entities:

Entity 1, N-terminal domain of DnaA 107 residues - 11000 Da.

1   SERLEUSERLEUTRPGLNGLNCYSLEUALA
2   ARGLEUGLNASPGLULEUPROALATHRGLU
3   PHESERMETTRPILEARGPROLEUGLNALA
4   GLULEUSERASPASNTHRLEUALALEUTYR
5   ALAPROASNARGPHEVALLEUASPTRPVAL
6   ARGASPLYSTYRLEUASNASNILEASNGLY
7   LEULEUTHRSERPHECYSGLYALAASPALA
8   PROGLNLEUARGPHEGLUVALGLYTHRLYS
9   PROVALTHRGLNTHRPROGLNALAALAVAL
10   THRSERASNVALALAALAPROALAGLNVAL
11   ALAGLNTHRGLNPROGLNARG

Samples:

sample_1: N-terminal domain of DnaA, [U-13C; U-15N], 0.5 ± 0.2 mM; sodium phosphate 50 mM; ethylenediaminetetracetic acid 1 mM; sodium chloride 40 mM; Dithiothreitol 2 mM; sucrose 10%

condition_1: pH: 6.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCsample_1not availablecondition_1
1H-13C HSQCsample_1not availablecondition_1
HNCAsample_1not availablecondition_1
HNCOCAsample_1not availablecondition_1
HNCACOsample_1not availablecondition_1
HNCOsample_1not availablecondition_1
CBCACONHsample_1not availablecondition_1
HNCACBsample_1not availablecondition_1
15N 3D TOCSYsample_1not availablecondition_1
15N enhanced NOESYsample_1not availablecondition_1
HCCH TOCSYsample_1not availablecondition_1
HCCH COSYsample_1not availablecondition_1
13C enhanced NOESYsample_1not availablecondition_1
1H NOESYsample_1not availablecondition_1
1H TOCSYsample_1not availablecondition_1

Software:

NMRPipe v2.5, Dlaglio, F - Fourier Transfer

Olivia v1.13.0, hokkaido University - chemical shift assignment

NMR spectrometers:

  • Varian Inova 600 600 MHz

Related Database Links:

PDB
DBJ BAB38060 BAE77592 BAG79512 BAI28038 BAI33157
EMBL CAP78161 CAQ34046 CAR00675 CAR05331 CAR10518
GB AAA62053 AAB59149 AAC76725 AAG58899 AAN45205
REF NP_312664 NP_418157 WP_000059087 WP_000059101 WP_000059102
SP A7ZTQ8 A8A6G3 B1IYP2 B1LL27 B2TUS6
AlphaFold A7ZTQ8 A8A6G3 B1IYP2 B1LL27 B2TUS6

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