BMRB Entry 18152

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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/BMR18152
MolProbity Validation Chart

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the catalytic domain of B. anthracis SrtD
Deposition date:
2011-12-19
Original release date:
2012-09-19
Authors:
Robson, Scott; Weiner, Ethan; Clubb, Robert
Citation:

Citation: Robson, Scott; Jacobitz, Alex; Phillips, Martin; Clubb, Robert. "Solution structure of the sortase required for efficient production of infectious Bacillus anthracis spores."  Biochemistry 51, 7953-7963 (2012).
PubMed: 22974341

Assembly members:

Assembly members:
entity, polymer, 147 residues, 16547.906 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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GSHMSSQTEHKEGEKVAMLN IPKLKKKFSIYWGADDATLK KGVGMFVSDVTTTPSGGGHT VLSGHRDTVFTDLGQLKEKD TLVLEYDNKTYTYEIQKIWI THADDRTVIIKKEEPILTLT TCYPFDYIGDAPDRYIIEAK LTGSYSK

Data sets:
Data typeCount
13C chemical shifts525
15N chemical shifts121
1H chemical shifts785

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BA_SrtD1

Entities:

Entity 1, BA_SrtD 147 residues - 16547.906 Da.

1   GLYSERHISMETSERSERGLNTHRGLUHIS
2   LYSGLUGLYGLULYSVALALAMETLEUASN
3   ILEPROLYSLEULYSLYSLYSPHESERILE
4   TYRTRPGLYALAASPASPALATHRLEULYS
5   LYSGLYVALGLYMETPHEVALSERASPVAL
6   THRTHRTHRPROSERGLYGLYGLYHISTHR
7   VALLEUSERGLYHISARGASPTHRVALPHE
8   THRASPLEUGLYGLNLEULYSGLULYSASP
9   THRLEUVALLEUGLUTYRASPASNLYSTHR
10   TYRTHRTYRGLUILEGLNLYSILETRPILE
11   THRHISALAASPASPARGTHRVALILEILE
12   LYSLYSGLUGLUPROILELEUTHRLEUTHR
13   THRCYSTYRPROPHEASPTYRILEGLYASP
14   ALAPROASPARGTYRILEILEGLUALALYS
15   LEUTHRGLYSERTYRSERLYS

Samples:

sample_1: HEPES 20 mM; H2O 93%; D20 7%

sample_2: HEPES 20 mM; D2O 100%

sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_2isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

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

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 17109
PDB
DBJ BAR74314 GAF00419 GAO61843 GAO67625
EMBL COE74822 CUB43016 CUB56473
GB AAP28746 AAT34193 AAT57002 AAT63578 ABK87585
REF NP_847260 WP_000771569 WP_000771599 WP_000771600 WP_000771601

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