BMRB Entry 19723

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments of the Cytoplasmic Tail of Ig-alpha (CD79a) in a Heterodimeric Construct
Published: 2014-02-06

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19723

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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments of the Cytoplasmic Tail of Ig-alpha (CD79a) in a Heterodimeric Construct

Deposition date:

2014-01-08

Original release date:

2014-02-06

Authors:

Bentrop, Detlef; Salavei, Pavel; Reth, Michael; Fakler, Bernd

Citation:

Citation: Salavei, Pavel; Bentrop, Detlef; Reth, Michael; Fakler, Bernd. "A heterodimeric construct mimicking the cytoplasmic region of the B-cell antigen receptor complex-associated protein" .

Assembly members:

Assembly members:
cytoplasmic_Ig-alpha_polypeptide, polymer, 99 residues, Formula weight is not available
cytoplasmic_Ig-beta_polypeptide, polymer, 86 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: pET23a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cytoplasmic_Ig-alpha_polypeptide: SGGVAQLRERVKTLRAQNYE LESEVQRLREQVAQLSGGRK RWQNEKLGLDAGDEYEDENL YEGLNLDDCSMYEDISRGLQ GTYQDVGSLNIGDVQLEKP
cytoplasmic_Ig-beta_polypeptide: SGGVDELQAEVDQLQDENYA LKTKVAQLRKKVEKLSGGDK DDSKAGMEEDHTYEGLDIDQ TATYEDIVTLRTGEVKWSVG EHPGQE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1

Data type	Count
13C chemical shifts	236
15N chemical shifts	95
1H chemical shifts	187
heteronuclear NOE values	92

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Ig-alpha Ig-beta construct, subunit 1	1
2	Ig-alpha Ig-beta construct, subunit 2	2

Entities:

Entity 1, Ig-alpha Ig-beta construct, subunit 1 99 residues - Formula weight is not available

Residues 1-3 represent a linker to an affinity tag that was removed by proteolysis. Residues 4-35 are a coiled-coil heterodimerization domain (A2, see citation 3 and 1, respectively). Residues 36-38 represent a linker. Residues 39-99 are the cytoplasmic region of human Ig-alpha and contain an immunoreceptor tyrosine-based activation motif (ITAM).

1

SER

GLY

VAL

ALA

GLN

LEU

ARG

GLU

ARG

2

VAL

LYS

THR

LEU

ARG

ALA

GLN

ASN

TYR

GLU

3

LEU

GLU

SER

GLU

VAL

GLN

ARG

LEU

ARG

GLU

4

GLN

VAL

ALA

GLN

LEU

SER

GLY

ARG

LYS

5

ARG

TRP

GLN

ASN

GLU

LYS

LEU

GLY

LEU

ASP

6

ALA

GLY

ASP

GLU

TYR

GLU

ASP

GLU

ASN

LEU

7

TYR

GLU

GLY

LEU

ASN

LEU

ASP

CYS

SER

8

MET

TYR

GLU

ASP

ILE

SER

ARG

GLY

LEU

GLN

9

GLY

THR

TYR

GLN

ASP

VAL

GLY

SER

LEU

ASN

10

ILE

GLY

ASP

VAL

GLN

LEU

GLU

LYS

PRO

Entity 2, Ig-alpha Ig-beta construct, subunit 2 86 residues - Formula weight is not available

Residues 1-3 represent a linker to an affinity tag that was removed by proteolysis. Residues 4-35 are a coiled-coil heterodimerization domain (B1, see citation 3 and 1, respectively). Residues 36-38 represent a linker. Residues 39-86 are the cytoplasmic region of human Ig-beta and contain an immunoreceptor tyrosine-based activation motif (ITAM)."

1

SER

GLY

VAL

ASP

GLU

LEU

GLN

ALA

GLU

2

VAL

ASP

GLN

LEU

GLN

ASP

GLU

ASN

TYR

ALA

3

LEU

LYS

THR

LYS

VAL

ALA

GLN

LEU

ARG

LYS

4

LYS

VAL

GLU

LYS

LEU

SER

GLY

ASP

LYS

5

ASP

SER

LYS

ALA

GLY

MET

GLU

ASP

6

HIS

THR

TYR

GLU

GLY

LEU

ASP

ILE

ASP

GLN

7

THR

ALA

THR

TYR

GLU

ASP

ILE

VAL

THR

LEU

8

ARG

THR

GLY

GLU

VAL

LYS

TRP

SER

VAL

GLY

9

GLU

HIS

PRO

GLY

GLN

GLU

Samples:

sample_1: cytoplasmic Ig-alpha polypeptide, [U-98% 13C; U-98% 15N], 0.25 mM; cytoplasmic Ig-beta polypeptide 0.25 mM; sodium phosphate 50 mM

sample_2: cytoplasmic Ig-alpha polypeptide, [U-98% 15N], 0.3 mM; cytoplasmic Ig-beta polypeptide 0.3 mM; sodium phosphate 50 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 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 HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D HNHA	sample_2	isotropic	sample_conditions_1
2D 1H-15N heteroNOE	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - NMR data acquisition

CARA vv1.8.4.2, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

EMBL	S46706.1 CAA58523 M80461.1
BMRB	18867 19644 19645 19648 19649 19724 19725 18884 19650 19651 19724 19725
DBJ	BAD97091 BAG37737
GB	AAA20495 AAA57274 AAA59556 AAA59557 AAA60270 EDM06394 EGV99168 ELW67499
REF	NP_001774 NP_067612 XP_001152742 XP_002829327 XP_003779238 XP_003501912 XP_003913329 XP_006041680 XP_006041681 XP_006146855
SP	P11912
AlphaFold	P11912