BMRB Entry 34638

Name: Structure of the human UFC1 protein in complex with the UBA5 C-terminal UFC1-binding motif.
Published: 2021-08-02

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PDB ID: 7ovc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34638
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Structure of the human UFC1 protein in complex with the UBA5 C-terminal UFC1-binding motif. PubMed: 34299007

Deposition date: 2021-06-14 Original release date: 2021-08-02

Authors: Wesch, W.; Loehr, F.; Rogova, N.; Doetsch, V.; Rogov, V.

Citation: Wesch, W.; Loehr, F.; Rogova, N.; Doetsch, V.; Rogov, V.. "A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1" Int. J. Mol. Sci. 22, 7390-7390 (2021).

Assembly members:
entity_1, polymer, 167 residues, 19486.395 Da.
entity_2, polymer, 27 residues, 3034.459 Da.

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET39_Ub19

Entity Sequences (FASTA):
entity_1: MADEATRRVVSEIPVLKTNA GPRDRELWVQRLKEEYQSLI RYVENNKNADNDWFRLESNK EGTRWFGKCWYIHDLLKYEF DIEFDIPITYPTTAPEIAVP ELDGKTAKMYRGGKICLTDH FKPLWARNVPKFGLAHLMAL GLGPWLAVEIPDLIQKGVIQ HKEKCNQ
entity_2: GMSVTELTVEDSGESLEDLM AKMKNMW

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	676
15N chemical shifts	196
1H chemical shifts	1396

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2

Entities:

Entity 1, unit_1 167 residues - 19486.395 Da.

1

MET

ALA

ASP

GLU

ALA

THR

ARG

VAL

2

SER

GLU

ILE

PRO

VAL

LEU

LYS

THR

ASN

ALA

3

GLY

PRO

ARG

ASP

ARG

GLU

LEU

TRP

VAL

GLN

4

ARG

LEU

LYS

GLU

TYR

GLN

SER

LEU

ILE

5

ARG

TYR

VAL

GLU

ASN

LYS

ASN

ALA

ASP

6

ASN

ASP

TRP

PHE

ARG

LEU

GLU

SER

ASN

LYS

7

GLU

GLY

THR

ARG

TRP

PHE

GLY

LYS

CYS

TRP

8

TYR

ILE

HIS

ASP

LEU

LYS

TYR

GLU

PHE

9

ASP

ILE

GLU

PHE

ASP

ILE

PRO

ILE

THR

TYR

10

PRO

THR

ALA

PRO

GLU

ILE

ALA

VAL

PRO

11

GLU

LEU

ASP

GLY

LYS

THR

ALA

LYS

MET

TYR

12

ARG

GLY

LYS

ILE

CYS

LEU

THR

ASP

HIS

13

PHE

LYS

PRO

LEU

TRP

ALA

ARG

ASN

VAL

PRO

14

LYS

PHE

GLY

LEU

ALA

HIS

LEU

MET

ALA

LEU

15

GLY

LEU

GLY

PRO

TRP

LEU

ALA

VAL

GLU

ILE

16

PRO

ASP

LEU

ILE

GLN

LYS

GLY

VAL

ILE

GLN

17

HIS

LYS

GLU

LYS

CYS

ASN

GLN

Entity 2, unit_2 27 residues - 3034.459 Da.

1

GLY

MET

SER

VAL

THR

GLU

LEU

THR

VAL

GLU

2

ASP

SER

GLY

GLU

SER

LEU

GLU

ASP

LEU

MET

3

ALA

LYS

MET

LYS

ASN

MET

TRP

Samples:

sample_1: Ubiquitin-fold modifier-conjugating enzyme 1, [U-100% 13C; U-100% 15N], 1.0 ± 0.05 mM; Ubiquitin-like modifier-activating enzyme 5 1.0 ± 0.05 mM; TRIS 50 ± 1 mM; sodium chloride 100 ± 1 mM; TCEP 2 ± 0.1 mM; AEBSF protease inhibitor 5 ± 0.1 mM; DSS 0.15 ± 0.01 mM

sample_2: Ubiquitin-fold modifier-conjugating enzyme 1 1.2 ± 0.05 mM; Ubiquitin-like modifier-activating enzyme 5, [U-100% 13C; U-100% 15N], 0.3 ± 0.05 mM; TRIS 50 ± 1 mM; sodium chloride 100 ± 1 mM; TCEP 2 ± 0.1 mM; AEBSF protease inhibitor 5 ± 0.1 mM; DSS 0.15 ± 0.01 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D [15N,1H]-TROSY-(H)C(CC)(CO)NH-TOCSY	sample_1	isotropic	sample_conditions_1
3D [15N,1H]-TROSY-H(C)(CC)(CO)NH-TOCSY	sample_1	isotropic	sample_conditions_1
3D BEST-[15N,1H]-TROSY-HNCACB	sample_1	isotropic	sample_conditions_1
3D F1-13C/15N-filtered NOESY-[13C,1H]-HSQC	sample_1	isotropic	sample_conditions_1
3D F1-13C/15N-filtered NOESY-[15N,1H]-SOFAST-HMQC	sample_1	isotropic	sample_conditions_1
3D F1-13C/15N-filtered NOESY-[13C,1H]-SOFAST-HMQC (aro)	sample_1	isotropic	sample_conditions_1
3D NOESY-[13C,1H]-SOFAST-HMQC (aro)	sample_1	isotropic	sample_conditions_1
3D NOESY-[13C,1H]-HSQC (aliphatic region)	sample_1	isotropic	sample_conditions_1
3D NOESY-BEST-[15N,1H]-TROSY	sample_1	isotropic	sample_conditions_1
3D BEST-[15N,1H]-TROSY-HNCA	sample_2	isotropic	sample_conditions_1
3D BEST-[15N,1H]-TROSY-HNCACB	sample_2	isotropic	sample_conditions_1
3D F1-13C/15N-filtered NOESY-[13C,1H]-HSQC	sample_2	isotropic	sample_conditions_1
3D [15N,1H]-TROSY-(H)C(CC)(CO)NH-TOCSY	sample_2	isotropic	sample_conditions_1
3D NOESY [13C,1H]-HSQC	sample_2	isotropic	sample_conditions_1
3D [15N,1H]-TROSY-H(CC)(CO)NH-TOCSY	sample_2	isotropic	sample_conditions_1
3D NOESY-[15N,1H]-SOFAST-HMQC	sample_2	isotropic	sample_conditions_1

Software:

TopSpin v3.6.2, Bruker Biospin - collection

Sparky v3.114, Goddard - chemical shift assignment, peak picking

CYANA v3.98, Guntert, Mumenthaler and Wuthrich - structure calculation

OPALp v1.4, Koradi, R., Billeter, M. and Guentert, P - refinement

NMR spectrometers:

Bruker AVANCE III HD 700 MHz
Bruker AVANCE III HD 800 MHz
Bruker AVANCE NEO 900 MHz
Bruker AVANCE III 950 MHz
Bruker AVANCE II 600 MHz

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