BMRB Entry 25569

Name: PIN1 WW domain in complex with a phosphorylated CPEB1 derived peptide
Published: 2015-10-26

Click here to enlarge.

PDB ID: 2n1o
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25569
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:

PIN1 WW domain in complex with a phosphorylated CPEB1 derived peptide

Deposition date:

2015-04-13

Original release date:

2015-10-26

Authors:

Schelhorn, Constanze; Macias, Maria J.; Martin-Malpartida, Pau

Citation:

Citation: Schelhorn, Constanze; Martin-Malpartida, Pau; Sunol, David; Macias, Maria J.. "Structural Analysis of the Pin1-CPEB1 interaction and its potential role in CPEB1 degradation" Sci. Rep. 5, 14990-14990 (2015).
PubMed: 26456073

Assembly members:

Assembly members:
Pin1, polymer, 33 residues, 3901.367 Da.
CPEB1, polymer, 8 residues, 1007.111 Da.

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: pETM30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Pin1: LPPGWEKRMSRSSGRVYYFN HITNASQWERPSG
CPEB1: RIXPPLPF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	235

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Pin1	1
2	CPEB1	2

Entities:

Entity 1, Pin1 33 residues - 3901.367 Da.

1

LEU

PRO

GLY

TRP

GLU

LYS

ARG

MET

SER

2

ARG

SER

GLY

ARG

VAL

TYR

PHE

ASN

3

HIS

ILE

THR

ASN

ALA

SER

GLN

TRP

GLU

ARG

4

PRO

SER

GLY

Entity 2, CPEB1 8 residues - 1007.111 Da.

1

ARG

ILE

SEP

PRO

LEU

PRO

PHE

Samples:

sample_1: Pin1 1 mM; CPEB1 3 mM; D2O, [U-100% 2H], 10%; TRIS, [U-100% 2H], 20 mM; sodium chloride 130 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 285 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1

Software:

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

XEASY, Bartels et al. - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance 600 MHz

UNP	Q13526 Q91572
BMRB	16070 16088 17545 19258 19259
PDB	1F8A 1I6C 1I8G 1I8H 1NMV 1PIN 2ITK 2KCF 2LB3 2M8I 2M8J 2Q5A 2XP3 2XP4 2XP5 2XP6 2XP7 2XP8 2XP9 2XPA 2XPB 2ZQS 2ZQT 2ZQU 2ZQV 2ZR4 2ZR5 2ZR6 3KAB 3KAD 3KAF 3KAG 3KAH 3KAI 3KCE 3NTP 3ODK 3OOB 3TC5 3TCZ 3TDB 3WH0 4GWT 4GWV 4QIB 4U84 4U85 4U86
DBJ	BAA87037 BAA87038 BAB22270 BAB22743 BAC35631
EMBL	CAG28582
GB	AAC50492 AAH02899 AAH38254 AAH59553 AAI12584
PRF	2209428A
REF	NP_001029804 NP_001100171 NP_001231300 NP_001270625 NP_006212
SP	Q13526 Q4R383 Q5BIN5 Q9QUR7
TPG	DAA28013
AlphaFold	Q53X75 Q13526 Q4R383 Q5BIN5 Q9QUR7 B7ZRZ4