BMRB Entry 5298

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PDB ID: 1l1p
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5298
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, and 15N Chemical Shift Assignments for the PPIase domain from E. coli trigger factor

Deposition date:

2002-02-20

Original release date:

2003-06-25

Authors:

Kozlov, Guennadi; Trempe, Jean-Francois; Perreault, Audry; Wong, Molly; Denisov, Aleksej; Ghandi, Shaifali; Gehring, Kalle; Ekiel, Irena

Citation:

Citation: Kozlov, Guennadi; Trempe, Jean-Francois; Perreault, Audry; Wong, Molly; Denisov, Aleksej; Ghandi, Shaifali; Gehring, Kalle; Ekiel, Irena. "Solution structure of the closed form of a peptidyl-prolyl isomerase reveals the mechanism of protein folding " .

Assembly members:

Assembly members:
peptidyl-prolyl isomerase, polymer, 106 residues, 11647 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
peptidyl-prolyl isomerase: GSHMQATWKEKDGAVEAEDR VTIDFTGSVDGEEFEGGKAS DFVLAMGQGRMIPGFEDGIK GHKAGEEFTIDVTFPEEYHA ENLKGKAAKFAINLKKVEER ELPELT

Data sets:

assigned_chemical_shifts
- shift_set_1
coupling_constants
- J_values_set_1

Data type	Count
1H chemical shifts	536
13C chemical shifts	187
15N chemical shifts	98
coupling constants	82

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PPIase	1

Entities:

Entity 1, PPIase 106 residues - 11647 Da.

1

GLY

SER

HIS

MET

GLN

ALA

THR

TRP

LYS

GLU

2

LYS

ASP

GLY

ALA

VAL

GLU

ALA

GLU

ASP

ARG

3

VAL

THR

ILE

ASP

PHE

THR

GLY

SER

VAL

ASP

4

GLY

GLU

PHE

GLU

GLY

LYS

ALA

SER

5

ASP

PHE

VAL

LEU

ALA

MET

GLY

GLN

GLY

ARG

6

MET

ILE

PRO

GLY

PHE

GLU

ASP

GLY

ILE

LYS

7

GLY

HIS

LYS

ALA

GLY

GLU

PHE

THR

ILE

8

ASP

VAL

THR

PHE

PRO

GLU

TYR

HIS

ALA

9

GLU

ASN

LEU

LYS

GLY

LYS

ALA

LYS

PHE

10

ALA

ILE

ASN

LEU

LYS

VAL

GLU

ARG

11

GLU

LEU

PRO

GLU

LEU

THR

Samples:

sample_1: peptidyl-prolyl isomerase2.0 – 3.0 mM; NaCl 100 mM

sample_2: peptidyl-prolyl isomerase, [U-15N], 2.0 – 3.0 mM; NaCl 100 mM

sample_3: peptidyl-prolyl isomerase, [U-13C; U-15N], 2.0 – 3.0 mM; NaCl 100 mM

conditions_1: pH: 6.8; temperature: 303 K; ionic strength: 0.1 M; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	not available	not available	not available
3D 1H-1H-15N NOESY	not available	not available	not available
3D 1H-1H-15N TOCSY	not available	not available	not available
3D HNHA	not available	not available	not available
3D CBCA(CO)NH	not available	not available	not available
3D HNCACB	not available	not available	not available

Software:

XWINNMR v2.1 - data collection

GIFA v4.31 - data processing

XEASY v1.3.13 - peak assignments

NMR spectrometers:

Bruker DRX 500 MHz

BMRB	19835 19836 19837
PDB	1L1P 1W26 2MLX 2MLY 2MLZ 2VRH
DBJ	BAB33913 BAD98926 BAE76216 BAG75986 BAH62052
EMBL	CAP74970 CAQ30908 CAQ90076 CAQ97312 CAR01780
GB	AAA62791 AAB40192 AAC73539 AAG54786 AAN42037
REF	NP_286178 NP_308517 NP_414970 NP_706330 NP_752485
SP	A1A8A5 A6T5H9 A7ZIJ4 A7ZX94 A8AK17
AlphaFold	A1A8A5 A6T5H9 A7ZIJ4 A7ZX94 A8AK17