BMRB Entry 17501

Title:
The NMR structure of the protein NP_344798.1 reveals a CCA-adding enzyme head domain
Deposition date:
2011-03-01
Original release date:
2011-03-25
Authors:
MOHANTY, BISWARANJAN; SERRANO, PEDRO; GERALT, MICHAEL; HORST, RETO; WUTHRICH, KURT
Citation:

Citation: MOHANTY, BISWARANJAN; SERRANO, PEDRO; GERALT, MICHAEL; HORST, RETO; WUTHRICH, KURT. "Solution NMR structure of the protein NP_344798.1"  .

Assembly members:

Assembly members:
NP_344798.1, polymer, 191 residues, 22835.953 Da.

Natural source:

Natural source:   Common Name: Streptococcus pneumoniae TIGR4   Taxonomy ID: 170187   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus pneumoniae

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts834
15N chemical shifts208
1H chemical shifts1393

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NP_344798.11

Entities:

Entity 1, NP_344798.1 191 residues - 22835.953 Da.

1   GLYMETASNTHRVALLYSASNLYSGLNGLU
2   ILELEUGLUALAPHEARGGLUSERPROASP
3   METMETALAILELEUTHRILEILEARGASP
4   LEUGLYLEULYSASPSERTRPLEUALAALA
5   GLYSERVALARGASNPHEILETRPASNLEU
6   LEUSERASPLYSSERPROPHEASPHISGLU
7   THRASPILEASPVALILEPHEPHEASPPRO
8   ASPPHESERTYRGLUGLUTHRLEULEULEU
9   GLULYSLYSLEUARGGLUASPPHEPROGLN
10   TYRGLNTRPGLULEULYSASNGLNVALTYR
11   METHISGLNHISSERPROHISTHRALASER
12   TYRTHRSERSERARGASPALAMETSERLYS
13   TYRPROGLUARGCYSTHRALAVALGLYLEU
14   ARGLEUASNGLUGLULEUASPPHEGLULEU
15   TYRVALPROTYRGLYLEUGLUASPILELEU
16   ASNPHEGLNVALARGPROTHRPROHISPHE
17   LEUGLUASNGLUASPARGMETGLULEUTYR
18   GLNTHRARGLEUSERLYSLYSASNTRPGLN
19   GLULYSTRPLYSASNLEUILEPHELYSASN
20   THR

Samples:

sample_1: NP_344798.1, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 4.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.113 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
4D APSY - HACANHsample_1isotropicsample_conditions_1
5D APSY - HACACONHsample_1isotropicsample_conditions_1
5D APSY - CBCACONHsample_1isotropicsample_conditions_1
15N resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
13Cali resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
13Caro resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

UNIO v2.0.0, Herrmann and Wuthrich - chemical shift assignment, noe assignment, peak picking, structure solution

CARA v1.5.3, Keller and Wuthrich - chemical shift assignment

TOPSPIN v1.3, Bruker Biospin - data collection, processing

OPALp v1.2, Koradi,Billeter and Guntert - energy refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CAR68108 CBW33875 CBW35903 CEO61672 CEO63344
GB AAK74438 AAK99043 ABJ54676 ACO17445 ACO19518
REF NP_357833 WP_001098892 WP_001098893 WP_001098894 WP_001098895

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