BMRB Entry 25545

Name: Complex structure of MyUb (1080-1122) of human Myosin VI with K63-diUb
Published: 2016-03-07

Click here to enlarge.

PDB ID: 2n13
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25545
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Complex structure of MyUb (1080-1122) of human Myosin VI with K63-diUb

Deposition date:

2015-03-20

Original release date:

2016-03-07

Authors:

He, Fahu; Walters, Kylie

Citation:

Citation: He, Fahu; Wollscheid, Hans-Peter; Nowicka, Urszula; Biancospino, Matteo; Valentini, Eleonora; Ehlinger, Aaron; Acconcia, Filippo; Magistrati, Elisa; Polo, Simona; Walters, Kylie. "Myosin VI Contains a Compact Structural Motif that Binds to Ubiquitin Chains" Cell Rep. 14, 2683-2694 (2016).
PubMed: 26971995

Assembly members:

Assembly members:
entity_1, polymer, 43 residues, Formula weight is not available
entity_2, polymer, 76 residues, Formula weight is not available
entity_3, polymer, 76 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: pGEX6p

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GTKKYDLSKWKYAELRDTIN TSCDIELLAACREEFHRRLK VYH
entity_2: MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQRESTLHLVLRLRGG
entity_3: MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	698
15N chemical shifts	156
1H chemical shifts	1145

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, 1	1
2	entity_2	2
3	entity_3	3
4	entity_1, 2	1

Entities:

Entity 1, entity_1, 1 43 residues - Formula weight is not available

1

GLY

THR

LYS

TYR

ASP

LEU

SER

LYS

TRP

2

LYS

TYR

ALA

GLU

LEU

ARG

ASP

THR

ILE

ASN

3

THR

SER

CYS

ASP

ILE

GLU

LEU

ALA

4

CYS

ARG

GLU

PHE

HIS

ARG

LEU

LYS

5

VAL

TYR

HIS

Entity 2, entity_2 76 residues - Formula weight is not available

1

MET

GLN

ILE

PHE

VAL

LYS

THR

LEU

THR

GLY

2

LYS

THR

ILE

THR

LEU

GLU

VAL

GLU

PRO

SER

3

ASP

THR

ILE

GLU

ASN

VAL

LYS

ALA

LYS

ILE

4

GLN

ASP

LYS

GLU

GLY

ILE

PRO

ASP

GLN

5

GLN

ARG

LEU

ILE

PHE

ALA

GLY

LYS

GLN

LEU

6

GLU

ASP

GLY

ARG

THR

LEU

SER

ASP

TYR

ASN

7

ILE

GLN

ARG

GLU

SER

THR

LEU

HIS

LEU

VAL

8

LEU

ARG

LEU

ARG

GLY

Entity 3, entity_3 76 residues - Formula weight is not available

1

MET

GLN

ILE

PHE

VAL

LYS

THR

LEU

THR

GLY

2

LYS

THR

ILE

THR

LEU

GLU

VAL

GLU

PRO

SER

3

ASP

THR

ILE

GLU

ASN

VAL

LYS

ALA

LYS

ILE

4

GLN

ASP

LYS

GLU

GLY

ILE

PRO

ASP

GLN

5

GLN

ARG

LEU

ILE

PHE

ALA

GLY

LYS

GLN

LEU

6

GLU

ASP

GLY

ARG

THR

LEU

SER

ASP

TYR

ASN

7

ILE

GLN

LYS

GLU

SER

THR

LEU

HIS

LEU

VAL

8

LEU

ARG

LEU

ARG

GLY

CYS

Samples:

sample_1: entity_1, [U-13C; U-15N], 0.5 mM; entity_2, [U-13C; U-15N], 0.5 mM; entity_3, [U-13C; U-15N], 0.5 mM; sodium phosphate 20 mM; NaCl 50 mM; DTT 2 mM; NaN3 0.1%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D half-filter NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Kujira, Naohiro Kobayashi - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Bruker Avance 900 MHz

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