BMRB Entry 6002

Name: Structure of the C-terminal domain of p63
Published: 2007-03-22

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PDB ID: 1rg6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6002
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Structure of the C-terminal domain of p63

Deposition date:

2003-11-11

Original release date:

2007-03-22

Authors:

Cadot, Bruno; Candi, Eleonora; Cicero, Daniel; Desideri, Alesssandro; Mele, Sonia; Melino, Gerry; Paci, Maurizio

Citation:

Citation: Cicero, Daniel; Falconi, M.; Candi, Eleonora; Mele, Sonia; Cadot, Bruno; Di Venere, A.; Rufini, S.; Melino, Gerry; Desideri, Alessandro. "NMR structure of the p63 SAM domain and dynamical properties of G534V and T537P pathological mutants, identified in the AEC syndrome" Cell Biochem. Biophys. 44, 475-489 (2006).
PubMed: 16679535

Assembly members:

Assembly members:
polymer, polymer, 75 residues, 8379 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: pGEXsx2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
polymer: PPPYPTDCSIVSFLARLGCS SCLDYFTTQGLTTIYQIEHY SMDDLASLKIPEQFRHAIWK GILDHRQLHEFAAAS

Data sets:

assigned_chemical_shifts
- chemical_shifts

Data type	Count
13C chemical shifts	337
15N chemical shifts	81
1H chemical shifts	507

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p63 monomer	1

Entities:

Entity 1, p63 monomer 75 residues - 8379 Da.

1

PRO

TYR

PRO

THR

ASP

CYS

SER

ILE

2

VAL

SER

PHE

LEU

ALA

ARG

LEU

GLY

CYS

SER

3

SER

CYS

LEU

ASP

TYR

PHE

THR

GLN

GLY

4

LEU

THR

ILE

TYR

GLN

ILE

GLU

HIS

TYR

5

SER

MET

ASP

LEU

ALA

SER

LEU

LYS

ILE

6

PRO

GLU

GLN

PHE

ARG

HIS

ALA

ILE

TRP

LYS

7

GLY

ILE

LEU

ASP

HIS

ARG

GLN

LEU

HIS

GLU

8

PHE

ALA

SER

Samples:

sample_1: polymer, [U-15N], 0.75 mM; sodium posphate 25 mM; sodium chloride 150 mM; AEBSF 1 mM; DTT 3 mM

sample_2: polymer, [U-13C; U-15N], 0.25 mM; sodium posphate 25 mM; sodium chloride 150 mM; AEBSF 1 mM; DTT 3 mM

Exp-cond_1: pH: 6.0; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	not available	not available	not available
3D 1H-1H-15N TOCSY	not available	not available	not available
3D 1H-1H-15N NOESY	not available	not available	not available
3D HNHA	not available	not available	not available
3D HNCA	not available	not available	not available
3D HNCO	not available	not available	not available
3D CBCA(co)NH	not available	not available	not available
3D CBCANH	not available	not available	not available
3D HBHA(co)NH	not available	not available	not available
3D HACACO	not available	not available	not available
2D HACA	not available	not available	not available
3D hCCH TOCSY	not available	not available	not available
3D HcCH TOCSY	not available	not available	not available
3D HcCH COSY	not available	not available	not available
3D hCCH COSY	not available	not available	not available
3D C13,N15 edited NOESY	not available	not available	not available
2D 1H-13C HSQC	not available	not available	not available

Software:

NMRView v5 - peak-picking analysis of processed data

InsightII - graphic processing

X-PLOR v3.8 - Structure calculation

Procheck NMR - Structure validation

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 400 MHz

PDB	1RG6 2Y9U
GB	ELW50906
REF	XP_006156783 XP_006156784