Click here to enlarge.

PDB ID: 9wpr
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36786
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text 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

Please specify the pdb ID.

Name: Solution structure of N-terminal domain of mouse HBS1L protein
Published: 2026-05-07

Title:

Solution structure of N-terminal domain of mouse HBS1L protein

Deposition date:

2025-09-09

Original release date:

2026-05-07

Authors:

He, F.; Hayami, N.; Terada, T.; Inoue, M.; Yabuki, T.; Aoki, M.; Seki, E.; Matsuda, T.; Hirota, H.; Yoshida, M.; Matsuo, Y.; Hayashizaki, Y.; Takahashi, M.; Tsuda, K.; Nagata, T.; Tanaka, A.; Kobayashi, N.; Kigawa, T.; Guntert, P.; Shirouzu, M.; Yokoyama, S.; Muto, Y.; Kuwasako, K.; RIKEN Structural Genomics/Proteomics Initiative (RSGI), RIKEN

Citation:

Citation: He, F.; Nameki, N.; Muto, Y.; Takahashi, M.; Tsuda, K.; Nagata, T.; Tanaka, A.; Kobayashi, N.; Kigawa, T.; Guntert, P.; Shirouzu, M.; Yokoyama, S.; Kuwasako, K.. "Solution structure of mouse HBS1L/SKI7-specific UBA domain in complex with ubiquitin: Implications for stalled ribosome recognition." Plos One ., .-. (2026).

Assembly members:

Assembly members:
HBS1-like protein, polymer, 83 residues, 8975.762 Da.

Natural source:

Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: not available Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Cell-free gateway cloning vector N-term 8xHis pCellFree_G01

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HBS1-like protein: GSSGSSGEYGYEDLRESSNS LLNHQLSEIDQARLYSCLDH MREVLGDAVPDDILTEAILK HKFDVQKALSVVLEQDGSGP SSG

Data sets:

assigned_chemical_shifts
- HBS1

Data type	Count
13C chemical shifts	331
15N chemical shifts	80
1H chemical shifts	532

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 83 residues - 8975.762 Da.

1

GLY

SER

GLY

SER

GLY

GLU

TYR

GLY

2

TYR

GLU

ASP

LEU

ARG

GLU

SER

ASN

SER

3

LEU

ASN

HIS

GLN

LEU

SER

GLU

ILE

ASP

4

GLN

ALA

ARG

LEU

TYR

SER

CYS

LEU

ASP

HIS

5

MET

ARG

GLU

VAL

LEU

GLY

ASP

ALA

VAL

PRO

6

ASP

ILE

LEU

THR

GLU

ALA

ILE

LEU

LYS

7

HIS

LYS

PHE

ASP

VAL

GLN

LYS

ALA

LEU

SER

8

VAL

LEU

GLU

GLN

ASP

GLY

SER

GLY

PRO

9

SER

GLY

Samples:

sample_1: mouse HBS1L N-terminal domain, [U-99% 13C; U-99% 15N], 1.0 mM; NaN3 0.02%; NaCl 100 mM; potassium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D_13C,15N-SEPARATED_NOESY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH, 3D HNCCB	sample_1	isotropic	sample_conditions_1

Software:

Amber v24, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

KUJIRA v0.863, N. Kobayashi, T. Kigawa, S. Yokoyama - chemical shift assignment

NMRView v5.0.4, Johnson, One Moon Scientific - peak picking

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

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

BMRB Entry 36786