BMRB Entry 16893

Name: MDM4 binds ligands via an induced fit mechanism in which disordered regions become structured
Published: 2010-06-16

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16893

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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:

MDM4 binds ligands via an induced fit mechanism in which disordered regions become structured

Deposition date:

2010-04-22

Original release date:

2010-06-16

Authors:

Sanchez, Maria; Renshaw, Jonathan; Davies, Gareth; Barlow, Paul; Vogtherr, Martin

Citation:

Citation: Sanchez, Maria; Renshaw, Jonathan; Davies, Gareth; Barlow, Paul; Vogtherr, Martin. "MDM4 binds ligands via a mechanism in which disordered regions become structured." FEBS Lett. 584, 3035-3041 (2010).
PubMed: 20515689

Assembly members:

Assembly members:
MDM4 N-terminal domain, polymer, 102 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: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MDM4 N-terminal domain: GSHMDSASRISPGQINQVRP KLPLLKILHAAGAQGEMFTV KEVMHYLGQYIMVKQLYDQQ EQHMVYCGGDLLGELLGRQS FSVKDPSPLYDMLRKNLVTL AT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	215
15N chemical shifts	66
1H chemical shifts	66

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MDM4	1

Entities:

Entity 1, MDM4 102 residues - Formula weight is not available

1

GLY

SER

HIS

MET

ASP

SER

ALA

SER

ARG

ILE

2

SER

PRO

GLY

GLN

ILE

ASN

GLN

VAL

ARG

PRO

3

LYS

LEU

PRO

LEU

LYS

ILE

LEU

HIS

ALA

4

ALA

GLY

ALA

GLN

GLY

GLU

MET

PHE

THR

VAL

5

LYS

GLU

VAL

MET

HIS

TYR

LEU

GLY

GLN

TYR

6

ILE

MET

VAL

LYS

GLN

LEU

TYR

ASP

GLN

7

GLU

GLN

HIS

MET

VAL

TYR

CYS

GLY

ASP

8

LEU

GLY

GLU

LEU

GLY

ARG

GLN

SER

9

PHE

SER

VAL

LYS

ASP

PRO

SER

PRO

LEU

TYR

10

ASP

MET

LEU

ARG

LYS

ASN

LEU

VAL

THR

LEU

11

ALA

THR

Samples:

sample_1: MDM4 N-terminal domain, [U-100% 13C; U-100% 15N], 0.1 mM; sodium chloride 100 mM; TCEP 2 mM; EDTA 0.1 mM; BisTris 50 mM; sodium azide 0.1%; H2O 99%; DMSO 1%

sample_conditions_1: ionic strength: 0.2 M; 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.5.5, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

BMRB	16894 16900
PDB	2VYR 3DAB 3FDO 3FE7 3FEA 3JZO 3JZP 3JZQ 3LBJ 3U15 4RXZ
DBJ	BAD96948 BAG64634 BAG65468 BAK62829
EMBL	CAE45961 CAH18300
GB	AAH67299 AAI05107 AAO13494 AGJ70143 AGZ93683
REF	NP_001191100 NP_001265445 NP_001265447 NP_001267305 NP_002384
SP	O15151
AlphaFold	O15151