BMRB Entry 15746

Name: Bpp3783_115-220
Published: 2009-11-11

Click here to enlarge.

PDB ID: 2jpf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: LACS
BMRB Entry DOI: doi:10.13018/BMR15746
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:

Bpp3783_115-220

Deposition date:

2008-04-29

Original release date:

2009-11-11

Authors:

Shaw, Gary; Revington, Matthew; Savichenko, Alexei; Arrowsmith, Cheryl

Citation:

Citation: Revington, Matthew; Shaw, Gary; Savichenko, Alexei; Arrowsmith, Cheryl. "Solution structure of a domain of a type three secretion system secretory protein BPP 3783 from Bordetella pertusis" .

Assembly members:

Assembly members:
BPP3783_115-120, polymer, 106 residues, 12116.664 Da.

Natural source:

Natural source: Common Name: Bordetella Parapertussis Taxonomy ID: 519 Superkingdom: Bacteria Kingdom: not available Genus/species: Bordetella Parapertussis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BPP3783_115-120: KQQLQEHAPSHANLDVKWLD GLRAGSMALQGDVKVWMQNL EDLHTRRPDEFTARLQQSTD ALYSHLEAQWAKQHGTPPTA SDVVGMPQWQEYTAMLRERF AGLDTI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	359
15N chemical shifts	94
1H chemical shifts	566

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BPP3783_115-120	1

Entities:

Entity 1, BPP3783_115-120 106 residues - 12116.664 Da.

1

LYS

GLN

LEU

GLN

GLU

HIS

ALA

PRO

SER

2

HIS

ALA

ASN

LEU

ASP

VAL

LYS

TRP

LEU

ASP

3

GLY

LEU

ARG

ALA

GLY

SER

MET

ALA

LEU

GLN

4

GLY

ASP

VAL

LYS

VAL

TRP

MET

GLN

ASN

LEU

5

GLU

ASP

LEU

HIS

THR

ARG

PRO

ASP

GLU

6

PHE

THR

ALA

ARG

LEU

GLN

SER

THR

ASP

7

ALA

LEU

TYR

SER

HIS

LEU

GLU

ALA

GLN

TRP

8

ALA

LYS

GLN

HIS

GLY

THR

PRO

THR

ALA

9

SER

ASP

VAL

GLY

MET

PRO

GLN

TRP

GLN

10

GLU

TYR

THR

ALA

MET

LEU

ARG

GLU

ARG

PHE

11

ALA

GLY

LEU

ASP

THR

ILE

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.5 ± 0.2 mM; NaCl 500 ± 10 mM; TRIS 10 ± 1 mM; Zn++ 10 ± 1 uM; Benzamidine 1 ± 0.2 mM; NaN3 0.01 ± 0.01 %

sample_conditions_1: ionic strength: 1 M; pH: 7.7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDCEHE	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe vv2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.2.2, Johnson, One Moon Scientific - data analysis

CYANA v2, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

VNMR v6.1c, Varian - collection

NMR spectrometers:

Varian INOVA 600 MHz

PDB	2JPF
EMBL	CAE39066 CCJ60666 CCK33761 CCN05630 CCN18924
GB	KAK50548 KAK74290 KAK75306 KCV30400 KCV45728
REF	WP_003820735 WP_004567631 WP_010929242 WP_033450554 WP_033453212