BMRB Entry 26526

Name: UBCH10
Published: 2015-06-17

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26526

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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:

UBCH10

Deposition date:

2015-03-02

Original release date:

2015-06-17

Authors:

Grace, Christy; Brown, Nicholus

Citation:

Citation: Brown, Nicholas; VanderLinden, Ryan; Watson, Edmond; Qiao, Renping; Grace, Christy; Yamaguchi, Masaya; Weissmann, Florian; Frye, Jeremiah; Dube, Prakash; Cho, Shein; Actis, Marcelo; Rodrigues, Patrick; Fujii, Naoaki; Peters, Jan-Michael; Stark, Holger; Schulman, Brenda. "RING E3 mechanism for ubiquitin ligation to a disordered substrate visualized for human anaphase-promoting complex" Proc. Natl. Acad. Sci. U. S. A. 17, 5272-5279 (2015).
PubMed: 25825779

Assembly members:

Assembly members:
Molecule_2, polymer, 187 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: prsf1b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Molecule_2: MASQNRDPAATSVAAARKGA EPSGGGARGPVGKRLQQELM TLMMSGDKGISAFPESDNLF KWVGTIHGAAGTVYEDLRYK LSLEFPSGYPYNAPTVKFLT PCYHPNVDTQGNISLDILKE KWSALYDVRTILLSIQSLLG EPNIDSPLNTHAAELWKNPT AFKKYLQETYSKQVTSQEPG SHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	367
15N chemical shifts	135
1H chemical shifts	135

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	molecule_2	1

Entities:

Entity 1, molecule_2 187 residues - Formula weight is not available

1

MET

ALA

SER

GLN

ASN

ARG

ASP

PRO

ALA

2

THR

SER

VAL

ALA

ARG

LYS

GLY

ALA

3

GLU

PRO

SER

GLY

ALA

ARG

GLY

PRO

4

VAL

GLY

LYS

ARG

LEU

GLN

GLU

LEU

MET

5

THR

LEU

MET

SER

GLY

ASP

LYS

GLY

ILE

6

SER

ALA

PHE

PRO

GLU

SER

ASP

ASN

LEU

PHE

7

LYS

TRP

VAL

GLY

THR

ILE

HIS

GLY

ALA

8

GLY

THR

VAL

TYR

GLU

ASP

LEU

ARG

TYR

LYS

9

LEU

SER

LEU

GLU

PHE

PRO

SER

GLY

TYR

PRO

10

TYR

ASN

ALA

PRO

THR

VAL

LYS

PHE

LEU

THR

11

PRO

CYS

TYR

HIS

PRO

ASN

VAL

ASP

THR

GLN

12

GLY

ASN

ILE

SER

LEU

ASP

ILE

LEU

LYS

GLU

13

LYS

TRP

SER

ALA

LEU

TYR

ASP

VAL

ARG

THR

14

ILE

LEU

SER

ILE

GLN

SER

LEU

GLY

15

GLU

PRO

ASN

ILE

ASP

SER

PRO

LEU

ASN

THR

16

HIS

ALA

GLU

LEU

TRP

LYS

ASN

PRO

THR

17

ALA

PHE

LYS

TYR

LEU

GLN

GLU

THR

TYR

18

SER

LYS

GLN

VAL

THR

SER

GLN

GLU

PRO

GLY

19

SER

HIS

Samples:

sample_1: Molecule_2, [U-100% 13C; U-100% 15N], 0.5 mM; DTT 0.01 mM; sodium chloride 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

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