BMRB Entry 25825

Name: UBL protein
Published: 2016-07-18

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PDB ID: 2nbw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25825
MolProbity Validation Chart

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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:

UBL protein

Deposition date:

2015-09-23

Original release date:

2016-07-18

Authors:

Chen, Xiang; Walters, Kylie

Citation:

Citation: Chen, Xiang; Walters, Kylie. "UBL protein" .

Assembly members:

Assembly members:
UBL_protein, polymer, 99 residues, Formula weight is not available

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET23a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UBL_protein: MVSLTFKNFKKEKVPLDLEP SNTILETKTKLAQSISCEES QIKLIYSGKVLQDSKTVSEC GLKDGDQVVFMVSQKKSTDP NSSSVDKLAAALEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	404
15N chemical shifts	98
1H chemical shifts	675

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	UBL protein, 1	1
2	UBL protein, 2	1

Entities:

Entity 1, UBL protein, 1 99 residues - Formula weight is not available

1

MET

VAL

SER

LEU

THR

PHE

LYS

ASN

PHE

LYS

2

LYS

GLU

LYS

VAL

PRO

LEU

ASP

LEU

GLU

PRO

3

SER

ASN

THR

ILE

LEU

GLU

THR

LYS

THR

LYS

4

LEU

ALA

GLN

SER

ILE

SER

CYS

GLU

SER

5

GLN

ILE

LYS

LEU

ILE

TYR

SER

GLY

LYS

VAL

6

LEU

GLN

ASP

SER

LYS

THR

VAL

SER

GLU

CYS

7

GLY

LEU

LYS

ASP

GLY

ASP

GLN

VAL

PHE

8

MET

VAL

SER

GLN

LYS

SER

THR

ASP

PRO

9

ASN

SER

VAL

ASP

LYS

LEU

ALA

10

ALA

LEU

GLU

HIS

Samples:

sample_1: UBL protein, [U-100% 13C; U-100% 15N], 0.7 mM; potassium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%

sample_2: UBL protein, [U-100% 13C; U-100% 15N], 0.7 mM; potassium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%

sample_conditions_1: ionic strength: 50 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
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D HCCH-TCOSY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 700 MHz

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