BMRB Entry 16406

Name: Solution structure of peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei. Seattle Structure Genomics Center for Infectious Disease (SSGCID)
Published: 2009-07-23

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16406

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:

Solution structure of peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei. Seattle Structure Genomics Center for Infectious Disease (SSGCID)

Deposition date:

2009-07-13

Original release date:

2009-07-23

Authors:

Zheng, Suxin; Leeper, Thomas; Varani, Gabriele

Citation:

Citation: Zheng, Suxin; Leeper, Thomas; Varani, Gabriele. "Null" To be Published ., .-..

Assembly members:

Assembly members:
peptidyl-prolyl cis-trans isomerase, polymer, 117 residues, 12239.810 Da.

Natural source:

Natural source: Common Name: Burkholderia pseudomallei Taxonomy ID: 28450 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia pseudomallei

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
peptidyl-prolyl cis-trans isomerase: GPGSMTVVTTESGLKYEDLT EGSGAEARAGQTVSVHYTGW LTDGQKFDSSKDRNDPFAFV LGGGMVIKGWDEGVQGMKVG GVRRLTIPPQLGYGARGAGG VIPPNATLVFEVELLDV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	322
15N chemical shifts	109
1H chemical shifts	748

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	peptidyl-prolyl cis-trans isomerase	1

Entities:

Entity 1, peptidyl-prolyl cis-trans isomerase 117 residues - 12239.810 Da.

1

GLY

PRO

GLY

SER

MET

THR

VAL

THR

2

GLU

SER

GLY

LEU

LYS

TYR

GLU

ASP

LEU

THR

3

GLU

GLY

SER

GLY

ALA

GLU

ALA

ARG

ALA

GLY

4

GLN

THR

VAL

SER

VAL

HIS

TYR

THR

GLY

TRP

5

LEU

THR

ASP

GLY

GLN

LYS

PHE

ASP

SER

6

LYS

ASP

ARG

ASN

ASP

PRO

PHE

ALA

PHE

VAL

7

LEU

GLY

MET

VAL

ILE

LYS

GLY

TRP

8

ASP

GLU

GLY

VAL

GLN

GLY

MET

LYS

VAL

GLY

9

GLY

VAL

ARG

LEU

THR

ILE

PRO

GLN

10

LEU

GLY

TYR

GLY

ALA

ARG

GLY

ALA

GLY

11

VAL

ILE

PRO

ASN

ALA

THR

LEU

VAL

PHE

12

GLU

VAL

GLU

LEU

ASP

VAL

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	C13_N15-labeled	isotropic	sample_conditions_1
3D HNCACB	C13_N15-labeled	isotropic	sample_conditions_1
3D HNCA	C13_N15-labeled	isotropic	sample_conditions_1
3D HN(CO)CA	C13_N15-labeled	isotropic	sample_conditions_1
3D HCCH-TOCSY	C13_N15-labeled	isotropic	sample_conditions_1
3D 1H-13C NOESY	C13_N15-labeled	isotropic	sample_conditions_1
2D 1H-15N HSQC	N15-labeled	isotropic	sample_conditions_1
3D 1H-15N NOESY	N15-labeled	isotropic	sample_conditions_1
2D 1H-15N HSQC	N15-labeled_2	isotropic	sample_conditions_1
2D 1H-1H TOCSY	N15-labeled_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	N15-labeled_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	N15-labeled	isotropic	sample_conditions_1

BMRB	16491 17151
PDB	2KE0 2KO7 2L2S 2Y78 3UF8 3UQA 3UQB 3VAW 4DZ2 4DZ3 4FN2 4G50 4GGQ 4GIV
EMBL	CAH39299 CDU31864 CFB51428 CFD89802 CFD92609
GB	ABA51599 ABC34056 ABN85861 ABN94560 AFI70186
REF	WP_004525093 WP_004537279 WP_009895623 WP_010110204 WP_010120234

BMRB Entry 16406

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: