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 15055

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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/BMR15055
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Title: Structure for the N-terminus of chromosomal replication initiation protein dnaA from M. genitalium   PubMed: 17680349

Deposition date: 2006-11-27 Original release date: 2007-10-16

Authors: Lowery, Thomas; Pelton, Jeffrey; Wemmer, David

Citation: Lowery, Thomas; Pelton, Jeffrey; Chandonia, John-Marc; Kim, Rosalind; Yokota, Hisao; Wemmer, David. "NMR Structure of the N-terminal domain of the replication initiator protein DnaA"  J. Struct. Funct. Genomics 8, 11-17 (2007).

Assembly members:
N_dnaA, polymer, 100 residues, 11870.441 Da.

Natural source:   Common Name: Mycoplasma genitalium   Taxonomy ID: 2097   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycoplasma genitalium

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

Entity Sequences (FASTA):
N_dnaA: MEQFNAFKSLLKKHYEKTIG FHDKYIKDINRFVFKNNVLL ILLENEFARNSLNDNSEIIH LAESLYEGIKSVNFVNEQDF FFNLAKLEENSRDTLYQNSG

Data sets:
Data typeCount
13C chemical shifts403
15N chemical shifts99
1H chemical shifts602

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N_dnaA1

Entities:

Entity 1, N_dnaA 100 residues - 11870.441 Da.

1   METGLUGLNPHEASNALAPHELYSSERLEU
2   LEULYSLYSHISTYRGLULYSTHRILEGLY
3   PHEHISASPLYSTYRILELYSASPILEASN
4   ARGPHEVALPHELYSASNASNVALLEULEU
5   ILELEULEUGLUASNGLUPHEALAARGASN
6   SERLEUASNASPASNSERGLUILEILEHIS
7   LEUALAGLUSERLEUTYRGLUGLYILELYS
8   SERVALASNPHEVALASNGLUGLNASPPHE
9   PHEPHEASNLEUALALYSLEUGLUGLUASN
10   SERARGASPTHRLEUTYRGLNASNSERGLY

Samples:

sample_1: N_dnaA, [U-100% 15N], 0.75 ± 0.2 mM; sodium phosphate 50 ± 10 mM; sodium chloride 100 ± 10 mM; EDTA 2 ± 1 mM; sodium azide 0.05 ± 0.01 %

sample_2: N_dnaA, [U-98% 13C; U-98% 15N], 0.75 ± 0.2 mM; sodium phosphate 50 ± 10 mM; sodium chloride 100 ± 10 mM; EDTA 2 ± 1 mM; sodium azide 0.05 ± 0.01 %

sample_3: N_dnaA 0.75 ± 0.2 mM; sodium phosphate 50 ± 10 mM; sodium chloride 100 ± 10 mM; EDTA 2 ± 1 mM; sodium azide 0.05 ± 0.01 %

sample_4: N_dnaA, [U-98% 13C; U-98% 15N], 0.75 ± 0.2 mM; sodium phosphate 50 ± 10 mM; sodium chloride 100 ± 10 mM; EDTA 2 ± 1 mM; sodium azide 0.05 ± 0.01 %

sample_5: N_dnaA, [10% 13C], 0.75 ± 0.2 mM; sodium phosphate 50 ± 10 mM; sodium chloride 100 ± 10 mM; EDTA 2 ± 1 mM; sodium azide 0.05 ± 0.01 %

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3d HN(CA)COsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_4isotropicsample_conditions_1
3D 1H-13C NOESYsample_4isotropicsample_conditions_1
4D HCCH NOESYsample_4isotropicsample_conditions_1
2D 1H-13C HSQCsample_5isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
2D DQF-COSYsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1

Software:

NMRPipe v2.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing

CARA v1.5.5, Rochus Keller & Datonal AG - chemical shift assignment

X-PLOR NIH v2.11.2, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker DMX 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
GB AAC72490 ABY79668 AFQ03308 AFQ03792 AFQ04301
REF WP_010869493 WP_014894707
SP P35888

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