BMRB Entry 25536

Name: MDMX-057
Published: 2016-01-25

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PDB ID: 2n0u
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25536
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-057

Deposition date: 2015-03-17 Original release date: 2016-01-25

Authors: Grace, Christy; Kriwacki, Richard

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

Assembly members:
entity_1, polymer, 89 residues, 10160.976 Da.
entity_CM7, non-polymer, 628.705 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	413
15N chemical shifts	95
1H chemical shifts	704

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.

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 - C32 H35 F3 N4 O4 S - 628.705 Da.

1

CM7

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.5 mM; entity_2 0.6 mM; NaCl 200 mM

sample_conditions_1: ionic strength: 200 mM; 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
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCA	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 C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts