BMRB Entry 31136

Name: Solution NMR structure of de novo designed protein F3 parent
Published: 2024-08-02

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PDB ID: 8vl3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31136
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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 protein F3 parent

Deposition date:

2024-01-11

Original release date:

2024-08-02

Authors:

McShan, A.; Simma, M.

Citation:

Citation: McShan, A.; Simma, M.. "Solution NMR structure of de novo designed protein F3 parent" .

Assembly members:

Assembly members:
entity_1, polymer, 114 residues, 13330.564 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: synthetic construct

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DERKKELVAQLKEEGFSERD IAEILGKISQGYSLIELERL NNAIIIILRKETEIIILVAK GEKKRILSLRGMSKKEIKKK LREAGLDEKEIEKVLRLLEK EGSHHWGSHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	278
15N chemical shifts	95
1H chemical shifts	95

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 114 residues - 13330.564 Da.

1

ASP

GLU

ARG

LYS

GLU

LEU

VAL

ALA

GLN

2

LEU

LYS

GLU

GLY

PHE

SER

GLU

ARG

ASP

3

ILE

ALA

GLU

ILE

LEU

GLY

LYS

ILE

SER

GLN

4

GLY

TYR

SER

LEU

ILE

GLU

LEU

GLU

ARG

LEU

5

ASN

ALA

ILE

LEU

ARG

LYS

6

GLU

THR

GLU

ILE

LEU

VAL

ALA

LYS

7

GLY

GLU

LYS

ARG

ILE

LEU

SER

LEU

ARG

8

GLY

MET

SER

LYS

GLU

ILE

LYS

9

LEU

ARG

GLU

ALA

GLY

LEU

ASP

GLU

LYS

GLU

10

ILE

GLU

LYS

VAL

LEU

ARG

LEU

GLU

LYS

11

GLU

GLY

SER

HIS

TRP

GLY

SER

HIS

12

HIS

Samples:

sample_1: 312 parent, [U-13C; U-15N], 1056.00 uM; NaCl 100 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 310.15 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

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

Sparky, Goddard - chemical shift assignment

CS-ROSETTA, Shen, Vernon, Baker and Bax - refinement, structure calculation

TALOS-N, Bax - structure calculation

NMR spectrometers:

Bruker AVANCE III HD 800 MHz

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