BMRB Entry 52980

Name: Peptidylprolyl Isomerase Like 1 (PPIL1)
Published: 2025-04-02

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52980

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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:

Peptidylprolyl Isomerase Like 1 (PPIL1)

Deposition date:

2025-03-24

Original release date:

2025-04-02

Authors:

Parra, George; Xiaoping, Xu; Libich, David

Citation:

Citation: Parra, George; Sohn, Erich; Xiaoping, Xu; Libich, David. "The spliceosomal peptidyl prolyl isomerase L1 interacts with the low-complexity domain of the RNA binding protein EWS modulating its phase separation behavior." Biochemistry ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 166 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pAG8Ha

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAAIPPDSWQPPNVYLETSM GIIVLELYWKHAPKTCKNFA ELARRGYYNGTKFHRIIKDF MIQGGDPTGTGRGGASIYGK QFEDELHPDLKFTGAGILAM ANAGPDTNGSQFFVTLAPTQ WLDGKHTIFGRVCQGIGMVN RVGMVETNSQDRPVDDVKII KAYPSG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	411
15N chemical shifts	150
1H chemical shifts	151

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PPIL1	1

Entities:

Entity 1, PPIL1 166 residues - Formula weight is not available

1

MET

ALA

ILE

PRO

ASP

SER

TRP

GLN

2

PRO

ASN

VAL

TYR

LEU

GLU

THR

SER

MET

3

GLY

ILE

VAL

LEU

GLU

LEU

TYR

TRP

LYS

4

HIS

ALA

PRO

LYS

THR

CYS

LYS

ASN

PHE

ALA

5

GLU

LEU

ALA

ARG

GLY

TYR

ASN

GLY

6

THR

LYS

PHE

HIS

ARG

ILE

LYS

ASP

PHE

7

MET

ILE

GLN

GLY

ASP

PRO

THR

GLY

THR

8

GLY

ARG

GLY

ALA

SER

ILE

TYR

GLY

LYS

9

GLN

PHE

GLU

ASP

GLU

LEU

HIS

PRO

ASP

LEU

10

LYS

PHE

THR

GLY

ALA

GLY

ILE

LEU

ALA

MET

11

ALA

ASN

ALA

GLY

PRO

ASP

THR

ASN

GLY

SER

12

GLN

PHE

VAL

THR

LEU

ALA

PRO

THR

GLN

13

TRP

LEU

ASP

GLY

LYS

HIS

THR

ILE

PHE

GLY

14

ARG

VAL

CYS

GLN

GLY

ILE

GLY

MET

VAL

ASN

15

ARG

VAL

GLY

MET

VAL

GLU

THR

ASN

SER

GLN

16

ASP

ARG

PRO

VAL

ASP

VAL

LYS

ILE

17

LYS

ALA

TYR

PRO

SER

GLY

Samples:

sample_1: Peptidylprolyl Isomerase Like-1, [U-99% 13C; U-99% 15N], 100 uM; D2O, [U-99% 2H], 5%; PMSF 1 mM; TCEP 1 mM; MES 20 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR - chemical shift assignment

TOPSPIN - collection

NMRDraw - refinement

NMRPipe - processing

NMR spectrometers:

Bruker Avance 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks