BMRB Entry 16853

Name: NMR structure of the transmembrane and cytoplasmic domains of human CD4
Published: 2012-08-02

Click here to enlarge.

PDB ID: 2klu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16853
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

NMR structure of the transmembrane and cytoplasmic domains of human CD4

Deposition date:

2010-04-09

Original release date:

2012-08-02

Authors:

Wittlich, Marc; Willbold, Dieter

Citation:

Citation: Wittlich, Marc; Koenig, Bernd; Hoffmann, Silke; Willbold, Dieter. "Structural characterization of the transmembrane and cytoplasmic domains of human CD4." Biochim. Biophys. Acta 1768, 2949-2960 (2007).
PubMed: 18035040

Assembly members:

Assembly members:
CD4, polymer, 70 residues, 7850.4 Da.
DPC, non-polymer, 389.445 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: pTKK19xb/ub

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CD4: GPLVPRGSMALIVLGGVAGL LLFIGLGIFFSVRSRHRRRQ AERMSQIKRLLSEKKTSQSP HRFQKTHSPI

Data sets:

assigned_chemical_shifts
- CD4mut_BMRB

Data type	Count
13C chemical shifts	329
15N chemical shifts	68
1H chemical shifts	529

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CD4mut	1
2	micelle	2

Entities:

Entity 1, CD4mut 70 residues - 7850.4 Da.

Residues 1-8 proteolytic left-over, human CD4(372-433) C394S/C397S/C420S/C422S/C430H

1	GLY	PRO	LEU	VAL	PRO	ARG	GLY	SER	MET	ALA
2	LEU	ILE	VAL	LEU	GLY	GLY	VAL	ALA	GLY	LEU
3	LEU	LEU	PHE	ILE	GLY	LEU	GLY	ILE	PHE	PHE
4	SER	VAL	ARG	SER	ARG	HIS	ARG	ARG	ARG	GLN
5	ALA	GLU	ARG	MET	SER	GLN	ILE	LYS	ARG	LEU
6	LEU	SER	GLU	LYS	LYS	THR	SER	GLN	SER	PRO
7	HIS	ARG	PHE	GLN	LYS	THR	HIS	SER	PRO	ILE

Entity 2, micelle - C20 H27 N3 O5 - 389.445 Da.

1

DPC

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

BMRB Entry 16853

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

1	GLY	PRO	LEU	VAL	PRO	ARG	GLY	SER	MET	ALA
2	LEU	ILE	VAL	LEU	GLY	GLY	VAL	ALA	GLY	LEU
3	LEU	LEU	PHE	ILE	GLY	LEU	GLY	ILE	PHE	PHE
4	SER	VAL	ARG	SER	ARG	HIS	ARG	ARG	ARG	GLN
5	ALA	GLU	ARG	MET	SER	GLN	ILE	LYS	ARG	LEU
6	LEU	SER	GLU	LYS	LYS	THR	SER	GLN	SER	PRO
7	HIS	ARG	PHE	GLN	LYS	THR	HIS	SER	PRO	ILE

1	GLY	PRO	LEU	VAL	PRO	ARG	GLY	SER	MET	ALA
2	LEU	ILE	VAL	LEU	GLY	GLY	VAL	ALA	GLY	LEU
3	LEU	LEU	PHE	ILE	GLY	LEU	GLY	ILE	PHE	PHE
4	SER	VAL	ARG	SER	ARG	HIS	ARG	ARG	ARG	GLN
5	ALA	GLU	ARG	MET	SER	GLN	ILE	LYS	ARG	LEU
6	LEU	SER	GLU	LYS	LYS	THR	SER	GLN	SER	PRO
7	HIS	ARG	PHE	GLN	LYS	THR	HIS	SER	PRO	ILE

1	GLY	PRO	LEU	VAL	PRO	ARG	GLY	SER	MET	ALA
2	LEU	ILE	VAL	LEU	GLY	GLY	VAL	ALA	GLY	LEU
3	LEU	LEU	PHE	ILE	GLY	LEU	GLY	ILE	PHE	PHE
4	SER	VAL	ARG	SER	ARG	HIS	ARG	ARG	ARG	GLN
5	ALA	GLU	ARG	MET	SER	GLN	ILE	LYS	ARG	LEU
6	LEU	SER	GLU	LYS	LYS	THR	SER	GLN	SER	PRO
7	HIS	ARG	PHE	GLN	LYS	THR	HIS	SER	PRO	ILE