BMRB Entry 16211

Name: Solution structure of putative prolyl isomerase PpiD from E.Coli
Published: 2009-11-05

Click here to enlarge.

PDB ID: 2kgj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16211
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:

Solution structure of putative prolyl isomerase PpiD from E.Coli

Deposition date:

2009-03-12

Original release date:

2009-11-05

Authors:

Weininger, Ulrich; Jakob, Roman

Citation:

Citation: Weininger, Ulrich; Jakob, Roman; Kovermann, Michael; Balbach, Jochen; Schmid, Franz. "The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity." Protein Sci. 19, 6-18 (2010).
PubMed: 19866485

Assembly members:

Assembly members:
prolyl isomerase domain, polymer, 102 residues, 11173.603 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
prolyl isomerase domain: TQPQRTRYSIIQTKTEDEAK AVLDELNKGGDFAALAKEKS ADIISARNGGDMGWLEDATI PDELKNAGLKEKGQLSGVIK SSVGFLIVRLDDIQAAHHHH HH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	108
1H chemical shifts	690

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	prolyl isomerase domain	1

Entities:

Entity 1, prolyl isomerase domain 102 residues - 11173.603 Da.

1

THR

GLN

PRO

GLN

ARG

THR

ARG

TYR

SER

ILE

2

ILE

GLN

THR

LYS

THR

GLU

ASP

GLU

ALA

LYS

3

ALA

VAL

LEU

ASP

GLU

LEU

ASN

LYS

GLY

4

ASP

PHE

ALA

LEU

ALA

LYS

GLU

LYS

SER

5

ALA

ASP

ILE

SER

ALA

ARG

ASN

GLY

6

ASP

MET

GLY

TRP

LEU

GLU

ASP

ALA

THR

ILE

7

PRO

ASP

GLU

LEU

LYS

ASN

ALA

GLY

LEU

LYS

8

GLU

LYS

GLY

GLN

LEU

SER

GLY

VAL

ILE

LYS

9

SER

VAL

GLY

PHE

LEU

ILE

VAL

ARG

LEU

10

ASP

ILE

GLN

ALA

HIS

11

HIS

Samples:

sample_1: potassium phosphate 100 mM; entity, [U-15N], 5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; 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-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

ARIA v2.0, Linge, O'Donoghue and Nilges - chemical shift assignment, structure solution

NMR spectrometers:

Bruker Avance 800 MHz

PDB	2KGJ
DBJ	BAA11645 BAB33918 BAE76221 BAG75991 BAI23815
EMBL	CAP74975 CAQ30914 CAQ97317 CAR01785 CAR06675
GB	AAB40197 AAC73544 AAG54791 AAN42042 AAN79035
REF	NP_308522 NP_414975 NP_706335 WP_000969091 WP_000969347
SP	P0ADY1 P0ADY2
AlphaFold	P0ADY1 P0ADY2