BMRB Entry 17512

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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/BMR17512
MolProbity Validation Chart

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Title:
1H, 13C, and 15N resonance assignments for S. aureus primase C-terminal domain
Deposition date:
2011-03-07
Original release date:
2011-06-07
Authors:
Shortridge, Matthew; Griep, Mark; Powers, Robert
Citation:

Citation: Shortridge, Matthew; Griep, Mark; Powers, Robert. "(1)H, (13)C, and (15)N NMR assignments for the helicase interaction domain of Staphylococcus aureus DnaG primase."  Biomol. NMR Assignments 6, 35-38 (2012).
PubMed: 21644056

Assembly members:

Assembly members:
primase_CTD, polymer, 143 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: n/a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
primase_CTD: FDNLSRQEKAERAFLKHLMR DKDTFLNYYESVDKDNFTNQ HFKYVFEVLHDFYAENDQYN ISDAVQYVNSNELRETLISL EQYNLNDEPYENEIDDYVNV INEKGQETIESLNHKLREAT RIGDVELQKYYLQQIVAKNK ERM

Data sets:
Data typeCount
13C chemical shifts565
15N chemical shifts135
1H chemical shifts849

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1c-terminal domain1

Entities:

Entity 1, c-terminal domain 143 residues - Formula weight is not available

1   PHEASPASNLEUSERARGGLNGLULYSALA
2   GLUARGALAPHELEULYSHISLEUMETARG
3   ASPLYSASPTHRPHELEUASNTYRTYRGLU
4   SERVALASPLYSASPASNPHETHRASNGLN
5   HISPHELYSTYRVALPHEGLUVALLEUHIS
6   ASPPHETYRALAGLUASNASPGLNTYRASN
7   ILESERASPALAVALGLNTYRVALASNSER
8   ASNGLULEUARGGLUTHRLEUILESERLEU
9   GLUGLNTYRASNLEUASNASPGLUPROTYR
10   GLUASNGLUILEASPASPTYRVALASNVAL
11   ILEASNGLULYSGLYGLNGLUTHRILEGLU
12   SERLEUASNHISLYSLEUARGGLUALATHR
13   ARGILEGLYASPVALGLULEUGLNLYSTYR
14   TYRLEUGLNGLNILEVALALALYSASNLYS
15   GLUARGMET

Samples:

sample_1: primase CTD, [U-100% 13C; U-100% 15N], 1.4 mM

sample_conditions_1: pH: 6.6; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_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
3D HNHAsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
DBJ BAA19493 BAB42654 BAB57724 BAB95379 BAF67737
EMBL CAG40634 CAG43301 CAI81123 CAQ50051 CBI49436
GB AAW38235 ABD22184 ABD30738 ABQ49413 ABR52502
REF WP_000320523 WP_001217234 WP_001217235 WP_001217236 WP_001217237
SP O05338 P63964 P63965 Q5HFJ8 Q6G904
AlphaFold O05338 P63964 P63965 Q5HFJ8 Q6G904

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