BMRB Entry 6072

Name: Solution structure of human p53 binding domain of PIAS-1
Published: 2004-08-05

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PDB ID: 1v66
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR6072
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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:

Solution structure of human p53 binding domain of PIAS-1

Deposition date:

2004-01-12

Original release date:

2004-08-05

Authors:

Okubo, S.; Hara, F.; Tsuchida, Y.; Shimotakahara, S.; Suzuki, S.; Hatanaka, H.; Yokoyama, S.; Tanaka, H.; Yasuda, H.; Shindo, H.

Citation:

Citation: Okubo, S.; Hara, F.; Tsuchida, Y.; Shimotakahara, S.; Suzuki, S.; Hatanaka, H.; Yokoyama, S.; Tanaka, H.; Yasuda, H.; Shindo, H.. "NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA ologomers." J. Biol. Chem. 279, 31455-31461 (2004).
PubMed: 15133049

Assembly members:

Assembly members:
PIAS-1, polymer, 65 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PIAS-1: MADSAELKQMVMSLRVSELQ VLLGYAGRNKHGRKHELLTK ALHLLKAGCSPAVQMKIKEL YRRRF

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
13C chemical shifts	295
15N chemical shifts	68
1H chemical shifts	444

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Protein inhibitor of activated STAT protein 1	1

Entities:

Entity 1, Protein inhibitor of activated STAT protein 1 65 residues - Formula weight is not available

1

MET

ALA

ASP

SER

ALA

GLU

LEU

LYS

GLN

MET

2

VAL

MET

SER

LEU

ARG

VAL

SER

GLU

LEU

GLN

3

VAL

LEU

GLY

TYR

ALA

GLY

ARG

ASN

LYS

4

HIS

GLY

ARG

LYS

HIS

GLU

LEU

THR

LYS

5

ALA

LEU

HIS

LEU

LYS

ALA

GLY

CYS

SER

6

PRO

ALA

VAL

GLN

MET

LYS

ILE

LYS

GLU

LEU

7

TYR

ARG

PHE

Samples:

sample_1: PIAS-1

sample_cond_1: pH: 6.0; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions

Software:

CYANA - refinement

NMR spectrometers:

unknown unknown 0 MHz

PDB	1V66
DBJ	BAC35902 BAE00325 BAE32224 BAG37114 BAG52901
EMBL	CAF98368
GB	AAB58488 AAC36701 AAC36702 AAD49722 AAH51417
PIR	JC5517
REF	NP_001026627 NP_001068864 NP_001079161 NP_001100299 NP_001253230
SP	O75925 O88907
TPG	DAA25728
AlphaFold	O75925 O88907