BMRB Entry 25377

Name: MDMX-P53
Published: 2016-01-25

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PDB ID: 2mwy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25377
MolProbity Validation Chart

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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:

MDMX-P53

Deposition date:

2014-12-03

Original release date:

2016-01-25

Authors:

Grace, Christy

Citation:

Citation: Grace, Christy; Kriwacki, Richard; Ban, David. "Monitoring ligand induced protein ordering in drug discovery" J. Mol. Biol. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 89 residues, 10160.976 Da.
entity_2, polymer, 15 residues, 1807.993 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: BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: QINQVRPKLPLLKILHAAGA QGEMFTVKEVMHYLGQYIMV KQLYDQQEQHMVYCGGDLLG ELLGRQSFSVKDPSPLYDML RKNLVTLAT
entity_2: SQETFSDLWKLLPEN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	585

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 89 residues - 10160.976 Da.

Residue 1 corresponds to 23 in MDMX

1

GLN

ILE

ASN

GLN

VAL

ARG

PRO

LYS

LEU

PRO

2

LEU

LYS

ILE

LEU

HIS

ALA

GLY

ALA

3

GLN

GLY

GLU

MET

PHE

THR

VAL

LYS

GLU

VAL

4

MET

HIS

TYR

LEU

GLY

GLN

TYR

ILE

MET

VAL

5

LYS

GLN

LEU

TYR

ASP

GLN

GLU

GLN

HIS

6

MET

VAL

TYR

CYS

GLY

ASP

LEU

GLY

7

GLU

LEU

GLY

ARG

GLN

SER

PHE

SER

VAL

8

LYS

ASP

PRO

SER

PRO

LEU

TYR

ASP

MET

LEU

9

ARG

LYS

ASN

LEU

VAL

THR

LEU

ALA

THR

Entity 2, entity_2 15 residues - 1807.993 Da.

Peptide is TAD of p53 from 15 to 29

1

SER

GLN

GLU

THR

PHE

SER

ASP

LEU

TRP

LYS

2

LEU

PRO

GLU

ASN

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 1.0 mM; entity_2 1.2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 200 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, G??ntert P. - refinement

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz