BMRB Entry 19111

Name: USP25
Published: 2013-08-16

Click here to enlarge.

PDB ID: 2mux
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19111
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:

USP25

Deposition date:

2013-03-27

Original release date:

2013-08-16

Authors:

Shi, Li; Zhang, Naixia; Wen, Yi

Citation:

Citation: Shi, Li; Wen, Yi; Zhang, Naixia. "(1)H, (13)C and (15)N backbone and side-chain resonance assignments of the N-terminal ubiquitin-binding domains of USP25." Biomol. NMR Assignments ., .-. (2013).
PubMed: 23754700

Assembly members:

Assembly members:
USP25, polymer, 166 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
USP25: MGSSHHHHHHSSGLVPRGSH MTVEQNVLQQSAAQKHQQTF LNQLREITGINDTQILQQAL KDSNGNLELAVAFLTAKNAK TPQQEETTYYQTALPGNDRY ISVGSQADTNVIDLTGDDKD DLQRAIALSLAESNRAFRET GITDEEQAISRVLEASIAEN KACLKR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	603
15N chemical shifts	162
1H chemical shifts	967

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	USP25	1

Entities:

Entity 1, USP25 166 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

THR

VAL

GLU

GLN

ASN

VAL

LEU

GLN

4

SER

ALA

GLN

LYS

HIS

GLN

THR

PHE

5

LEU

ASN

GLN

LEU

ARG

GLU

ILE

THR

GLY

ILE

6

ASN

ASP

THR

GLN

ILE

LEU

GLN

ALA

LEU

7

LYS

ASP

SER

ASN

GLY

ASN

LEU

GLU

LEU

ALA

8

VAL

ALA

PHE

LEU

THR

ALA

LYS

ASN

ALA

LYS

9

THR

PRO

GLN

GLU

THR

TYR

10

GLN

THR

ALA

LEU

PRO

GLY

ASN

ASP

ARG

TYR

11

ILE

SER

VAL

GLY

SER

GLN

ALA

ASP

THR

ASN

12

VAL

ILE

ASP

LEU

THR

GLY

ASP

LYS

ASP

13

ASP

LEU

GLN

ARG

ALA

ILE

ALA

LEU

SER

LEU

14

ALA

GLU

SER

ASN

ARG

ALA

PHE

ARG

GLU

THR

15

GLY

ILE

THR

ASP

GLU

GLN

ALA

ILE

SER

16

ARG

VAL

LEU

GLU

ALA

SER

ILE

ALA

GLU

ASN

17

LYS

ALA

CYS

LEU

LYS

ARG

Samples:

sample_1: USP25, [U-99% 13C; U-99% 15N], 0.6 mM; H2O 90%; D2O 10%

sample_2: USP25, [U-99% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_3: USP25, [U-99% 13C], 0.8 mM; D2O 100%

sample_conditions_1: ionic strength: 150 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_3	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
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D HCCH-COSY	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_3	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

DBJ	BAB27849 BAC29438
GB	AAF24998 AAF32263 AAF32264 AAH15930 AAH48171
REF	NP_001269970 NP_001269971 NP_037528 NP_038946 XP_001155737
SP	P57080 Q9UHP3
TPG	DAA33643
AlphaFold	P57080 Q9UHP3