BMRB Entry 31137

Name: Solution NMR Structure of de novo design protein 312 parent
Published: 2024-08-02

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PDB ID: 8vl4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31137
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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 design protein 312 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 design protein 312 parent" .

Assembly members:

Assembly members:
entity_1, polymer, 115 residues, 12981.034 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: GLLTREEIEAALKEAGFTEE EIRKVLAWLERVGGERKVLK VAGKILIIVEKRAGSRLLLL YAGRVIEKEGMSREEVEAIK QLISAGATVEEIEAIIKRIE ARGSHHWGSHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	276
15N chemical shifts	94
1H chemical shifts	94

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_1 115 residues - 12981.034 Da.

1

GLY

LEU

THR

ARG

GLU

ILE

GLU

ALA

2

ALA

LEU

LYS

GLU

ALA

GLY

PHE

THR

GLU

3

GLU

ILE

ARG

LYS

VAL

LEU

ALA

TRP

LEU

GLU

4

ARG

VAL

GLY

GLU

ARG

LYS

VAL

LEU

LYS

5

VAL

ALA

GLY

LYS

ILE

LEU

ILE

VAL

GLU

6

LYS

ARG

ALA

GLY

SER

ARG

LEU

7

TYR

ALA

GLY

ARG

VAL

ILE

GLU

LYS

GLU

GLY

8

MET

SER

ARG

GLU

VAL

GLU

ALA

ILE

LYS

9

GLN

LEU

ILE

SER

ALA

GLY

ALA

THR

VAL

GLU

10

GLU

ILE

GLU

ALA

ILE

LYS

ARG

ILE

GLU

11

ALA

ARG

GLY

SER

HIS

TRP

GLY

SER

HIS

12

HIS

Samples:

sample_1: 312 Parent, [U-13C; U-15N], 205 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 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