BMRB Entry 36011

Name: Solution structure of SUMO from Plasmodium falciparum
Published: 2017-03-16

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PDB ID: 5gjl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36011
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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 SUMO from Plasmodium falciparum

Deposition date:

2016-06-30

Original release date:

2017-03-16

Authors:

Singh, J.; Shukla, V.; Gujrati, M.; Mishra, R.; Kumar, A.

Citation:

Citation: Singh, Jai Shankar; Shukla, Vaibhav Kumar; Gujrati, Mansi; Mishra, Ram Kumar; Kumar, Ashutosh. "Backbone and side-chain resonance assignments of Plasmodium falciparum SUMO" Biomol NMR Assign 11, 17-20 (2017).
PubMed: 27699617

Assembly members:

Assembly members:
PfSUMO, polymer, 98 residues, 10838.997 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 57267 Superkingdom: Eukaryota Kingdom: not available Genus/species: Plasmodium Plasmodium falciparum

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PfSUMO: MGDDDSAVNNNGSSPVNNQG EHIQVKVRSPDGAEVFFKIK RKTKLEKLMEVYCNRLGQSM EAVRFLYDGDRIHGDNTPEQ LGIEDGDVIDAMVQQTGG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	355
15N chemical shifts	93
1H chemical shifts	556

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 98 residues - 10838.997 Da.

1

MET

GLY

ASP

SER

ALA

VAL

ASN

2

ASN

GLY

SER

PRO

VAL

ASN

GLN

GLY

3

GLU

HIS

ILE

GLN

VAL

LYS

VAL

ARG

SER

PRO

4

ASP

GLY

ALA

GLU

VAL

PHE

LYS

ILE

LYS

5

ARG

LYS

THR

LYS

LEU

GLU

LYS

LEU

MET

GLU

6

VAL

TYR

CYS

ASN

ARG

LEU

GLY

GLN

SER

MET

7

GLU

ALA

VAL

ARG

PHE

LEU

TYR

ASP

GLY

ASP

8

ARG

ILE

HIS

GLY

ASP

ASN

THR

PRO

GLU

GLN

9

LEU

GLY

ILE

GLU

ASP

GLY

ASP

VAL

ILE

ASP

10

ALA

MET

VAL

GLN

THR

GLY

Samples:

sample_1: PfSUMO, [U-100% 15N], 1 mM; TRIS 20 mM; sodium chloride 50 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: PfSUMO, [U-100% 13C; U-100% 15N], 1 mM; TRIS 20 mM; sodium chloride 50 mM; H2O 90%; D2O, [U-2H], 10%

sample_3: PfSUMO, [U-100% 13C; U-100% 15N], 1 mM; TRIS 20 mM; sodium chloride 50 mM; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCcoNH	sample_2	isotropic	sample_conditions_1
3D CCcoNH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

Bruker ASCEND 750 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