BMRB Entry 27305

Name: Chemical Shift Assignments of Retinal Degeneration 3 Protein (RD3)
Published: 2018-01-22

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PDB ID: 6drf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27305
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:

Chemical Shift Assignments of Retinal Degeneration 3 Protein (RD3)

Deposition date:

2017-11-07

Original release date:

2018-01-22

Authors:

Ames, James; Lim, Sunghyuk

Citation:

Citation: Lim, Sunghyuk; Cudia, Diana; Peshenko, Igor; Dizhoor, Alexander; Ames, James. "Chemical shift assignments of retinal degeneration 3 protein (RD3)" Biomol. NMR Assignments 12, 167-170 (2018).
PubMed: 29327102

Assembly members:

Assembly members:
RD3, polymer, 143 residues, Formula weight is not available

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: pET-11d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RD3: ARSPAEMVLETLMMELTGQM REAERQQRERSNAVRKVCTG VDYSWLASTPDSTYDLSPIE RLQLEDVCVKIHPSYCGPAI LRFRQLLAEQEPEVQEVSQL FRSVLQEVLERMKQEEEAHK LTRQWSLRPRGSLATFETEA EID

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	521
15N chemical shifts	142
1H chemical shifts	909

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RD3 monomer	1

Entities:

Entity 1, RD3 monomer 143 residues - Formula weight is not available

1

ALA

ARG

SER

PRO

ALA

GLU

MET

VAL

LEU

GLU

2

THR

LEU

MET

GLU

LEU

THR

GLY

GLN

MET

3

ARG

GLU

ALA

GLU

ARG

GLN

ARG

GLU

ARG

4

SER

ASN

ALA

VAL

ARG

LYS

VAL

CYS

THR

GLY

5

VAL

ASP

TYR

SER

TRP

LEU

ALA

SER

THR

PRO

6

ASP

SER

THR

TYR

ASP

LEU

SER

PRO

ILE

GLU

7

ARG

LEU

GLN

LEU

GLU

ASP

VAL

CYS

VAL

LYS

8

ILE

HIS

PRO

SER

TYR

CYS

GLY

PRO

ALA

ILE

9

LEU

ARG

PHE

ARG

GLN

LEU

ALA

GLU

GLN

10

GLU

PRO

GLU

VAL

GLN

GLU

VAL

SER

GLN

LEU

11

PHE

ARG

SER

VAL

LEU

GLN

GLU

VAL

LEU

GLU

12

ARG

MET

LYS

GLN

GLU

ALA

HIS

LYS

13

LEU

THR

ARG

GLN

TRP

SER

LEU

ARG

PRO

ARG

14

GLY

SER

LEU

ALA

THR

PHE

GLU

THR

GLU

ALA

15

GLU

ILE

ASP

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D H(CC)(CO)NH	sample_2	isotropic	sample_conditions_1
3D (H)CC(CO)NH	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 27305

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: