BMRB Entry 25150

Name: Solution structure of the human ubiquitin conjugating enzyme Ube2w
Published: 2014-11-24

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PDB ID: 2mt6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25150
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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 the human ubiquitin conjugating enzyme Ube2w

Deposition date:

2014-08-14

Original release date:

2014-11-24

Authors:

Vittal, Vinayak; Shi, Lei; Wenzel, Dawn; Brzovic, Peter; Klevit, Rachel

Citation:

Citation: Vittal, Vinayak; Shi, Lei; Wenzel, Dawn; Scaglione, K. Matthew; Duncan, Emily; Basrur, Venkatesha; Elenitoba-Johnson, Kojo; Baker, David; Paulson, Henry; Brzovic, Peter; Klevit, Rachel. "Intrinsic disorder drives N-terminal ubiquitination by Ube2w" Nat. Chem. Biol. 11, 83-89 (2015).
PubMed: 25436519

Assembly members:

Assembly members:
entity, polymer, 151 residues, 17350.973 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: pET24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MASMQKRLQKELLALQNDPP PGMTLNEKSVQNSITQWIVD MEGAPGTLYEGEKFQLLFKF SSRYPFDSPQVMFTGENIPV HPHVYSNGHICLSILTEDWS PALSVQSVCLSIISMLSSCK EKRRPPDNSFYVRTCNKNPK KTKWWYHDDTC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	367
15N chemical shifts	113
1H chemical shifts	230

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 151 residues - 17350.973 Da.

1

MET

ALA

SER

MET

GLN

LYS

ARG

LEU

GLN

LYS

2

GLU

LEU

ALA

LEU

GLN

ASN

ASP

PRO

3

PRO

GLY

MET

THR

LEU

ASN

GLU

LYS

SER

VAL

4

GLN

ASN

SER

ILE

THR

GLN

TRP

ILE

VAL

ASP

5

MET

GLU

GLY

ALA

PRO

GLY

THR

LEU

TYR

GLU

6

GLY

GLU

LYS

PHE

GLN

LEU

PHE

LYS

PHE

7

SER

ARG

TYR

PRO

PHE

ASP

SER

PRO

GLN

8

VAL

MET

PHE

THR

GLY

GLU

ASN

ILE

PRO

VAL

9

HIS

PRO

HIS

VAL

TYR

SER

ASN

GLY

HIS

ILE

10

CYS

LEU

SER

ILE

LEU

THR

GLU

ASP

TRP

SER

11

PRO

ALA

LEU

SER

VAL

GLN

SER

VAL

CYS

LEU

12

SER

ILE

SER

MET

LEU

SER

CYS

LYS

13

GLU

LYS

ARG

PRO

ASP

ASN

SER

PHE

14

TYR

VAL

ARG

THR

CYS

ASN

LYS

ASN

PRO

LYS

15

LYS

THR

LYS

TRP

TYR

HIS

ASP

THR

16

CYS

Samples:

sample_1: Ube2w, [U-100% 13C; U-100% 15N], 200 – 400 uM; H20 90%; D20 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CS-ROSETTA, Shen, Vernon, Baker and Bax - refinement, structure solution

NMR spectrometers:

Bruker DMX 500 MHz
Bruker INOVA 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks