BMRB Entry 30000

Name: Solution NMR structure of De novo designed PLOOP2X3_50 fold protein, Northeast Structural Genomics Consortium (NESG) target OR258
Published: 2016-06-17

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PDB ID: 5gaj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30000
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:

Solution NMR structure of De novo designed PLOOP2X3_50 fold protein, Northeast Structural Genomics Consortium (NESG) target OR258

Deposition date:

2015-12-01

Original release date:

2016-06-17

Authors:

Liu, G.; Castelllanos, J.; Koga, R.; Koga, N.; Xiao, R.; Pederson, K.; Janjua, H.; Kohan, E.; Acton, T.; Kornhaber, G.; Everett, J.; Baker, D.; Montelione, G.

Citation:

Citation: Koga, N.; Koga, R.; Liu, G.; Castellanos, J.; Montelione, G.; Baker, D.. "Role of backbone strain in de novo design of complex alpha/beta protein structures" Nat. Commun. 12, 3921-3921 (2021).
PubMed: 34168113

Assembly members:

Assembly members:
entity_1, polymer, 134 residues, 15769.068 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli K-12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGTVVIVVSRDERILEELLE VVLKSDPNVKTVRTDDKEKV KEEIEKARKQGRPIVIFIRG ATEEVVRDIVEYAQKEGLRV LVIMVDQDQEELERIYEQLK KDGVDVRVTDNEDEAKKRLK ELLEKVLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	594
15N chemical shifts	130
1H chemical shifts	994

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_1 134 residues - 15769.068 Da.

1

MET

GLY

THR

VAL

ILE

VAL

SER

ARG

2

ASP

GLU

ARG

ILE

LEU

GLU

LEU

GLU

3

VAL

LEU

LYS

SER

ASP

PRO

ASN

VAL

LYS

4

THR

VAL

ARG

THR

ASP

LYS

GLU

LYS

VAL

5

LYS

GLU

ILE

GLU

LYS

ALA

ARG

LYS

GLN

6

GLY

ARG

PRO

ILE

VAL

ILE

PHE

ILE

ARG

GLY

7

ALA

THR

GLU

VAL

ARG

ASP

ILE

VAL

8

GLU

TYR

ALA

GLN

LYS

GLU

GLY

LEU

ARG

VAL

9

LEU

VAL

ILE

MET

VAL

ASP

GLN

ASP

GLN

GLU

10

GLU

LEU

GLU

ARG

ILE

TYR

GLU

GLN

LEU

LYS

11

LYS

ASP

GLY

VAL

ASP

VAL

ARG

VAL

THR

ASP

12

ASN

GLU

ASP

GLU

ALA

LYS

ARG

LEU

LYS

13

GLU

LEU

GLU

LYS

VAL

LEU

GLU

HIS

14

HIS

Name	Sample	Sample state	Sample conditions
3D simutalneous 13C-aromatic, 13C-aliphatic, 15N edited 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC methyl	sample_2	isotropic	sample_conditions_1

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

BMRB Entry 30000

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: