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 19198

Title: NMR Structure of the protein NP_346341.1 from Streptococcus pneumoniae

Deposition date: 2013-04-29 Original release date: 2013-05-13

Authors: Proudfoot, Andrew; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation: Proudfoot, Andrew; Wuthrich, Kurt. "NMR Structure of the protein NP_346341.1 from Streptococcus pneumoniae"  Not known ., .-..

Assembly members:
entity, polymer, 70 residues, 8188.046 Da.

Natural source:   Common Name: Streptococcus pneumoniae   Taxonomy ID: 1313   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus pneumoniae

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

Entity Sequences (FASTA):
entity: GDDRKLMKTQEELTEIVRDH FSDMGEIATLYVQVYESSLE SLVGGVIFEDGRHYTFVYEN EDLVYEEEVL

Data sets:
Data typeCount
13C chemical shifts233
15N chemical shifts70
1H chemical shifts475

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SP18156A1

Entities:

Entity 1, SP18156A 70 residues - 8188.046 Da.

1   GLYASPASPARGLYSLEUMETLYSTHRGLN
2   GLUGLULEUTHRGLUILEVALARGASPHIS
3   PHESERASPMETGLYGLUILEALATHRLEU
4   TYRVALGLNVALTYRGLUSERSERLEUGLU
5   SERLEUVALGLYGLYVALILEPHEGLUASP
6   GLYARGHISTYRTHRPHEVALTYRGLUASN
7   GLUASPLEUVALTYRGLUGLUGLUVALLEU

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM

sample_conditions_1: ionic strength: 0.220 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
APSY 4D-HACANHsample_1isotropicsample_conditions_1
APSY 5D-CBCACONHsample_1isotropicsample_conditions_1
APSY 5D-HACACONHsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

TOPSPIN, Bruker Biospin - collection, processing

UNIO, Herrmann and Wuthrich - chemical shift assignment, structure solution

Opalp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CAR69689 CBJ21675 CBW33335 CBW35367 CBW37330
GB AAK75981 AAL00531 ABJ54543 ACA37339 ACB91139
REF NP_359320 WP_000266833 WP_001013971 WP_001013972 WP_001013973

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