BMRB Entry 36226

Name: Solution structure of Ufm1 protein from Trypanosoma brucei
Published: 2025-09-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36226

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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 Ufm1 protein from Trypanosoma brucei

Deposition date:

2018-12-19

Original release date:

2025-09-27

Authors:

Diwu, Y.; Tu, X.

Citation:

Citation: Diwu, Yating; Zhang, Jiahai; Li, Mingwei; Yang, Xiao; Shan, Fangzhen; Ma, Haoyu; Zhang, Xuecheng; Liao, Shanhui; Tu, Xiaoming. "Solution structure of TbUfm1 from Trypanosoma brucei and its binding to TbUba5." J. Struct. Biol. 212, 107580-107580 (2020).
PubMed: 32693018

Assembly members:

Assembly members:
Ubiquitin-fold modifier 1, polymer, 95 residues, 10225.549 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 185431 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma brucei

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ubiquitin-fold modifier 1: MSQNEEAPARSGGKVTFRII LTSERSQPFRVISIAEEAPL TAALRFAAEEFGIASVDSMA ATTKDGTGINPAQTAGNVFM KYGQEIRLIPRDRVG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	336
15N chemical shifts	86
1H chemical shifts	533

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 95 residues - 10225.549 Da.

1

MET

SER

GLN

ASN

GLU

ALA

PRO

ALA

ARG

2

SER

GLY

LYS

VAL

THR

PHE

ARG

ILE

3

LEU

THR

SER

GLU

ARG

SER

GLN

PRO

PHE

ARG

4

VAL

ILE

SER

ILE

ALA

GLU

ALA

PRO

LEU

5

THR

ALA

LEU

ARG

PHE

ALA

GLU

6

PHE

GLY

ILE

ALA

SER

VAL

ASP

SER

MET

ALA

7

ALA

THR

LYS

ASP

GLY

THR

GLY

ILE

ASN

8

PRO

ALA

GLN

THR

ALA

GLY

ASN

VAL

PHE

MET

9

LYS

TYR

GLY

GLN

GLU

ILE

ARG

LEU

ILE

PRO

10

ARG

ASP

ARG

VAL

GLY

Samples:

13C-15N: Ubiquitin-fold modifier 1, [U-13C; U-15N], mM; DTT 2 mM; EDTA 2 mM; sodium chloride 150 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	13C-15N	isotropic	sample_conditions_1
2D NOESY	13C-15N	isotropic	sample_conditions_1

Software:

CYANA, Guntert P. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Sparky, Goddard - chemical shift assignment

Sparky, Goddard - peak picking

NMR spectrometers:

Bruker DMX 600 MHz

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