BMRB Entry 27573

Name: Backbone and side chain chemical shifts assignments of uniformly labeled 13C, 15N SUMO1-F64L
Published: 2019-03-01

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27573

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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:

Backbone and side chain chemical shifts assignments of uniformly labeled 13C, 15N SUMO1-F64L

Deposition date:

2018-08-08

Original release date:

2019-03-01

Authors:

Das, Ranabir; Chatterjee, Kiran Sankar

Citation:

Citation: Chatterjee, Kiran Sankar; Tripathi, Vasvi; Das, Ranabir. "A conserved and buried edge-to-face aromatic interaction in small ubiquitin-like modifier (SUMO) has a role in SUMO stability and function" J. Biol. Chem. 294, 6772-6784 (2019).
PubMed: 30824543

Assembly members:

Assembly members:
SUMO1_F64L, polymer, 109 residues, 12497 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pQE-80L

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SUMO1_F64L: MRGSHHHHHHGSMSDQEAKP STEDLGDKKEGEYIKLKVIG QDSSEIHFKVKMTTHLKKLK ESYCQRQGVPMNSLRLLFEG QRIADNHTPKELGMEEEDVI EVYQEQTGG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	197
15N chemical shifts	86
1H chemical shifts	472

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SUMO1 F64L	1

Entities:

Entity 1, SUMO1 F64L 109 residues - 12497 Da.

residue 1 to 12 is His affinity tag

1

MET

ARG

GLY

SER

HIS

2

GLY

SER

MET

SER

ASP

GLN

GLU

ALA

LYS

PRO

3

SER

THR

GLU

ASP

LEU

GLY

ASP

LYS

GLU

4

GLY

GLU

TYR

ILE

LYS

LEU

LYS

VAL

ILE

GLY

5

GLN

ASP

SER

GLU

ILE

HIS

PHE

LYS

VAL

6

LYS

MET

THR

HIS

LEU

LYS

LEU

LYS

7

GLU

SER

TYR

CYS

GLN

ARG

GLN

GLY

VAL

PRO

8

MET

ASN

SER

LEU

ARG

LEU

PHE

GLU

GLY

9

GLN

ARG

ILE

ALA

ASP

ASN

HIS

THR

PRO

LYS

10

GLU

LEU

GLY

MET

GLU

ASP

VAL

ILE

11

GLU

VAL

TYR

GLN

GLU

GLN

THR

GLY

Samples:

sample_1: SUMO1 F64L, [U-100% 13C; U-100% 15N], 225 uM; DTT 2 mM; Phosphate buffer 25 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	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 H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

NMRDraw, Bahrami, Markley, Assadi, and Eghbalnia, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - chemical shift assignment, processing

NMR spectrometers:

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