BMRB Entry 19198

Name: NMR Structure of the protein NP_346341.1 from Streptococcus pneumoniae
Published: 2013-05-13

Click here to enlarge.

PDB ID: 2m7o
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19198
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

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:

Citation: Proudfoot, Andrew; Wuthrich, Kurt. "NMR Structure of the protein NP_346341.1 from Streptococcus pneumoniae" .

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	233
15N chemical shifts	70
1H chemical shifts	475

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SP18156A	1

Entities:

Entity 1, SP18156A 70 residues - 8188.046 Da.

1	GLY	ASP	ASP	ARG	LYS	LEU	MET	LYS	THR	GLN
2	GLU	GLU	LEU	THR	GLU	ILE	VAL	ARG	ASP	HIS
3	PHE	SER	ASP	MET	GLY	GLU	ILE	ALA	THR	LEU
4	TYR	VAL	GLN	VAL	TYR	GLU	SER	SER	LEU	GLU
5	SER	LEU	VAL	GLY	GLY	VAL	ILE	PHE	GLU	ASP
6	GLY	ARG	HIS	TYR	THR	PHE	VAL	TYR	GLU	ASN
7	GLU	ASP	LEU	VAL	TYR	GLU	GLU	GLU	VAL	LEU

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
APSY 4D-HACANH	sample_1	isotropic	sample_conditions_1
APSY 5D-CBCACONH	sample_1	isotropic	sample_conditions_1
APSY 5D-HACACONH	sample_1	isotropic	sample_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

PDB	2M7O
EMBL	CAR69689 CBJ21675 CBW33335 CBW35367 CBW37330
GB	AAK75981 AAL00531 ABJ54543 ACA37339 ACB91139
REF	NP_359320 WP_000266833 WP_001013971 WP_001013972 WP_001013973

1	GLY	ASP	ASP	ARG	LYS	LEU	MET	LYS	THR	GLN
2	GLU	GLU	LEU	THR	GLU	ILE	VAL	ARG	ASP	HIS
3	PHE	SER	ASP	MET	GLY	GLU	ILE	ALA	THR	LEU
4	TYR	VAL	GLN	VAL	TYR	GLU	SER	SER	LEU	GLU
5	SER	LEU	VAL	GLY	GLY	VAL	ILE	PHE	GLU	ASP
6	GLY	ARG	HIS	TYR	THR	PHE	VAL	TYR	GLU	ASN
7	GLU	ASP	LEU	VAL	TYR	GLU	GLU	GLU	VAL	LEU

1	GLY	ASP	ASP	ARG	LYS	LEU	MET	LYS	THR	GLN
2	GLU	GLU	LEU	THR	GLU	ILE	VAL	ARG	ASP	HIS
3	PHE	SER	ASP	MET	GLY	GLU	ILE	ALA	THR	LEU
4	TYR	VAL	GLN	VAL	TYR	GLU	SER	SER	LEU	GLU
5	SER	LEU	VAL	GLY	GLY	VAL	ILE	PHE	GLU	ASP
6	GLY	ARG	HIS	TYR	THR	PHE	VAL	TYR	GLU	ASN
7	GLU	ASP	LEU	VAL	TYR	GLU	GLU	GLU	VAL	LEU