BMRB Entry 36096

Name: NMR solution structure of SMO1, Sumo homologue in Caenorhabditis elegans
Published: 2019-08-21

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PDB ID: 5xqm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36096
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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:

NMR solution structure of SMO1, Sumo homologue in Caenorhabditis elegans

Deposition date:

2017-06-07

Original release date:

2019-08-21

Authors:

Gowda, C.; Surana, P.; Das, R.

Citation:

Citation: Surana, Parag; Gowda, Chandrakala; Tripathi, Vasvi; Broday, Limor; Das, Ranabir. "Structural and functional analysis of SMO-1, the SUMO homolog in Caenorhabditis elegans" PLoS One 12, e0186622-e0186622 (2017).
PubMed: 29045470

Assembly members:

Assembly members:
Small ubiquitin-related modifier, polymer, 97 residues, 11048.223 Da.

Natural source:

Natural source: Common Name: C. elegans Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Small ubiquitin-related modifier: MHHHHHHMADDAAQAGDNAE YIKIKVVGQDSNEVHFRVKY GTSMAKLKKSYADRTGVAVN SLRFLFDGRRINDDDTPKTL EMEDDDVIEVYQEQLGG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	364
15N chemical shifts	88
1H chemical shifts	547

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 97 residues - 11048.223 Da.

1

MET

HIS

MET

ALA

ASP

2

ASP

ALA

GLN

ALA

GLY

ASP

ASN

ALA

GLU

3

TYR

ILE

LYS

ILE

LYS

VAL

GLY

GLN

ASP

4

SER

ASN

GLU

VAL

HIS

PHE

ARG

VAL

LYS

TYR

5

GLY

THR

SER

MET

ALA

LYS

LEU

LYS

SER

6

TYR

ALA

ASP

ARG

THR

GLY

VAL

ALA

VAL

ASN

7

SER

LEU

ARG

PHE

LEU

PHE

ASP

GLY

ARG

8

ILE

ASN

ASP

THR

PRO

LYS

THR

LEU

9

GLU

MET

GLU

ASP

VAL

ILE

GLU

VAL

10

TYR

GLN

GLU

GLN

LEU

GLY

Samples:

sample_1: SMO1, Small Ubiquitin like modifier in C. elegans, [U-13C; U-15N], 620 uM; NaCl 150 mM; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	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 HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

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

SPARKY, Goddard - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker AvanceIII 800 MHz

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