BMRB Entry 15189

Name: Solution structure of the N-terminal extracellular domain of the lymphocyte receptor CD5 (CD5 domain 1)
Published: 2008-06-27

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PDB ID: 2jop
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15189
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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 structure of the N-terminal extracellular domain of the lymphocyte receptor CD5 (CD5 domain 1)

Deposition date:

2007-03-19

Original release date:

2008-06-27

Authors:

Garza-Garcia, Acely; Harris, Richard; Esposito, Diego; Driscoll, Paul

Citation:

Citation: Garza-Garcia, Acely; Esposito, Diego; Rieping, Wolfgang; Harris, Richard; Briggs, Cherry; Brown, Marion; Driscoll, Paul. "Three-dimensional solution structure and conformational plasticity of the N-terminal scavenger receptor cysteine-rich domain of human CD5" J. Mol. Biol. 378, 129-144 (2008).
PubMed: 18339402

Assembly members:

Assembly members:
CD5d1, polymer, 131 residues, 12491.134 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: pet15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CD5d1: MGSSHHHHHHSSGLVPRGSH MRLSWYDPDFQARLTRSNSK CQGQLEVYLKDGWHMVCSQS WGRSSKQWEDPSQASKVCQR LNCGDPLSLGPFLKTYTPQS SIICYGQLGSFSNCSHSRND MCHSLGLTCLE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	453
15N chemical shifts	105
1H chemical shifts	692

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CD5d1	1

Entities:

Entity 1, CD5d1 131 residues - 12491.134 Da.

Construct included an N-terminal hexa-histidine tag: MGSSHHHHHHSSGLVPRGSHM

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

ARG

LEU

SER

TRP

TYR

ASP

PRO

ASP

PHE

4

GLN

ALA

ARG

LEU

THR

ARG

SER

ASN

SER

LYS

5

CYS

GLN

GLY

GLN

LEU

GLU

VAL

TYR

LEU

LYS

6

ASP

GLY

TRP

HIS

MET

VAL

CYS

SER

GLN

SER

7

TRP

GLY

ARG

SER

LYS

GLN

TRP

GLU

ASP

8

PRO

SER

GLN

ALA

SER

LYS

VAL

CYS

GLN

ARG

9

LEU

ASN

CYS

GLY

ASP

PRO

LEU

SER

LEU

GLY

10

PRO

PHE

LEU

LYS

THR

TYR

THR

PRO

GLN

SER

11

SER

ILE

CYS

TYR

GLY

GLN

LEU

GLY

SER

12

PHE

SER

ASN

CYS

SER

HIS

SER

ARG

ASN

ASP

13

MET

CYS

HIS

SER

LEU

GLY

LEU

THR

CYS

LEU

14

GLU

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HA(CACO)NH	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1

BMRB Entry 15189

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: