BMRB Entry 25299

Name: Backbone fold of Human Small Ubiquitin like Modifier protein-1 (SUMO-1) based on Prot3D-NMR approach.
Published: 2014-12-01

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PDB ID: 2mw5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25299
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:

Backbone fold of Human Small Ubiquitin like Modifier protein-1 (SUMO-1) based on Prot3D-NMR approach.

Deposition date:

2014-10-28

Original release date:

2014-12-01

Authors:

Kumar, Dinesh; jaiswal, Nancy; raikwal, Nisha; Shukla, Vaibhav; Arora, Ashish

Citation:

Citation: Kumar, Dinesh; jaiswal, Nancy; raikwal, Nisha; Shukla, Vaibhav; Arora, Ashish. "Prot3DNMR: A simple and swift NMR strategy for Three-Dimentional structutral determination of proteins." .

Assembly members:

Assembly members:
entity, polymer, 97 residues, 11149.640 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: pQE80L

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MSDQEAKPSTEDLGDKKEGE YIKLKVIGQDSSEIHFKVKM TTHLKKLKESYCQRQGVPMN SLRFLFEGQRIADNHTPKEL GMEEEDVIEVYQEQTGG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	440
13C chemical shifts	383
15N chemical shifts	94

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 97 residues - 11149.640 Da.

1

MET

SER

ASP

GLN

GLU

ALA

LYS

PRO

SER

THR

2

GLU

ASP

LEU

GLY

ASP

LYS

GLU

GLY

GLU

3

TYR

ILE

LYS

LEU

LYS

VAL

ILE

GLY

GLN

ASP

4

SER

GLU

ILE

HIS

PHE

LYS

VAL

LYS

MET

5

THR

HIS

LEU

LYS

LEU

LYS

GLU

SER

6

TYR

CYS

GLN

ARG

GLN

GLY

VAL

PRO

MET

ASN

7

SER

LEU

ARG

PHE

LEU

PHE

GLU

GLY

GLN

ARG

8

ILE

ALA

ASP

ASN

HIS

THR

PRO

LYS

GLU

LEU

9

GLY

MET

GLU

ASP

VAL

ILE

GLU

VAL

10

TYR

GLN

GLU

GLN

THR

GLY

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.9 ± 0.1 mM; sodium phosphate 200 mM

sample_conditions_1: temperature: 298 K; pH: 6.5; pressure: 1 atm; ionic strength: 200 mM

Experiments:

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

Software:

CARA v9.8, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

BMRB	16611 17536
PDB	1A5R 1TGZ 1WYW 1Y8R 1Z5S 2ASQ 2BF8 2G4D 2IO2 2IY0 2IY1 2KQS 2LAS 2MW5 2PE6 2UYZ 2VRR 3KYC 3KYD 3RZW 3UIP 4WJN 4WJO 4WJP 4WJQ
DBJ	BAB22172 BAB27379 BAB93477 BAC40739 BAE35024
EMBL	CAA67898 CAG31129 CAG46944 CAG46953 CAH92616
GB	AAB39999 AAB40388 AAB40390 AAC39959 AAC50733
REF	NP_001005781 NP_001005782 NP_001009672 NP_001030535 NP_001106146
SP	A7WLH8 P63165 P63166 Q2EF74 Q5E9D1
TPG	DAA32560
AlphaFold	A7WLH8 P63165 P63166 Q2EF74 Q5E9D1