BMRB Entry 17124

Name: NP_888769.1
Published: 2011-05-04

Click here to enlarge.

PDB ID: 2l25
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17124
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: NP_888769.1 PubMed: 21520320

Deposition date: 2010-08-11 Original release date: 2011-05-04

Authors: Wahab, Atia-tul; Serrano, Pedro; Geralt, Michael; Wilson, Ian; Wuthrich, Kurt

Citation: Wahab, Atia-Tul; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage-related protein family PF13554." Protein Sci. 20, 1137-1144 (2011).

Assembly members:
NP_888769.1, polymer, 141 residues, 15260.356 Da.

Natural source: Common Name: B. bronchiseptica Taxonomy ID: 518 Superkingdom: Bacteria Kingdom: not available Genus/species: Bordetella bronchiseptica

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

Entity Sequences (FASTA):
NP_888769.1: GMSQDLIRAAFEKRLSDWAK ARTPALPVAWQNTKFTPPAA GVYLRAYVMPAATISRDAAG DHRQYRGVFQVNVVMPIGDG SRSAEQVAAELDALFPVNLV MQSGGLAVRVRTPISNGQPT TGDADHTVPISLGYDVQFYP E

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	565
15N chemical shifts	142
1H chemical shifts	947

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NP_888769.1	1

Entities:

Entity 1, NP_888769.1 141 residues - 15260.356 Da.

1

GLY

MET

SER

GLN

ASP

LEU

ILE

ARG

ALA

2

PHE

GLU

LYS

ARG

LEU

SER

ASP

TRP

ALA

LYS

3

ALA

ARG

THR

PRO

ALA

LEU

PRO

VAL

ALA

TRP

4

GLN

ASN

THR

LYS

PHE

THR

PRO

ALA

5

GLY

VAL

TYR

LEU

ARG

ALA

TYR

VAL

MET

PRO

6

ALA

THR

ILE

SER

ARG

ASP

ALA

GLY

7

ASP

HIS

ARG

GLN

TYR

ARG

GLY

VAL

PHE

GLN

8

VAL

ASN

VAL

MET

PRO

ILE

GLY

ASP

GLY

9

SER

ARG

SER

ALA

GLU

GLN

VAL

ALA

GLU

10

LEU

ASP

ALA

LEU

PHE

PRO

VAL

ASN

LEU

VAL

11

MET

GLN

SER

GLY

LEU

ALA

VAL

ARG

VAL

12

ARG

THR

PRO

ILE

SER

ASN

GLY

GLN

PRO

THR

13

THR

GLY

ASP

ALA

ASP

HIS

THR

VAL

PRO

ILE

14

SER

LEU

GLY

TYR

ASP

VAL

GLN

PHE

TYR

PRO

15

GLU

Samples:

sample_1: NP_888769.1, [U-98% 13C; U-98% 15N], 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 4.5 mM; D2O 5%; H2O 95%

sample_conditions_1: ionic strength: 0.11 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 15N-1H HSQC	sample_1	isotropic	sample_conditions_1
4D APSY-HACANH	sample_1	isotropic	sample_conditions_1
5D APSY-HACACONH	sample_1	isotropic	sample_conditions_1
5D APSY-CBCACONH	sample_1	isotropic	sample_conditions_1
15N-resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
13C(aliphatic)-resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
13C(aromatic)-resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1

Software:

UNIO v2.0.0, Torsten Herrmann - chemical shift assignment, peak picking, structure calculation

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

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

Molmol v2K.1, Koradi, Billeter and Wuthrich - analysis and display of molecule

CARA v1.8.4_linux, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2L25
DBJ	BAO70052
EMBL	CAE32722 CAE33988 CCN17196
GB	KAK74699 KCV36321 KCV51124 KDB85184 KDB90075
REF	WP_004566287

Biological Magnetic Resonance Data Bank