BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19724

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments of the Cytoplasmic Tail of Ig-beta (CD79b) 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: Salavei, Pavel; Bentrop, Detlef; Reth, Michael; Fakler, Bernd. "A heterodimeric construct mimicking the cytoplasmic region of the B-cell antigen receptor complex-associated protein"  Not known ., .-..

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:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

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

Data sets:
Data typeCount
13C chemical shifts119
15N chemical shifts83
1H chemical shifts283
heteronuclear NOE values79

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ig-alpha Ig-beta construct, subunit 11
2Ig-alpha Ig-beta construct, subunit 22

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   SERGLYGLYVALALAGLNLEUARGGLUARG
2   VALLYSTHRLEUARGALAGLNASNTYRGLU
3   LEUGLUSERGLUVALGLNARGLEUARGGLU
4   GLNVALALAGLNLEUSERGLYGLYARGLYS
5   ARGTRPGLNASNGLULYSLEUGLYLEUASP
6   ALAGLYASPGLUTYRGLUASPGLUASNLEU
7   TYRGLUGLYLEUASNLEUASPASPCYSSER
8   METTYRGLUASPILESERARGGLYLEUGLN
9   GLYTHRTYRGLNASPVALGLYSERLEUASN
10   ILEGLYASPVALGLNLEUGLULYSPRO

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   SERGLYGLYVALASPGLULEUGLNALAGLU
2   VALASPGLNLEUGLNASPGLUASNTYRALA
3   LEULYSTHRLYSVALALAGLNLEUARGLYS
4   LYSVALGLULYSLEUSERGLYGLYASPLYS
5   ASPASPSERLYSALAGLYMETGLUGLUASP
6   HISTHRTYRGLUGLYLEUASPILEASPGLN
7   THRALATHRTYRGLUASPILEVALTHRLEU
8   ARGTHRGLYGLUVALLYSTRPSERVALGLY
9   GLUHISPROGLYGLNGLU

Samples:

sample_1: cytoplasmic Ig-alpha polypeptide 0.5 mM; cytoplasmic Ig-beta polypeptide, [U-98% 13C; U-98% 15N], 0.5 mM; sodium phosphate 50 mM

sample_2: cytoplasmic Ig-alpha polypeptide 0.25 mM; cytoplasmic Ig-beta polypeptide, [U-98% 13C; U-98% 15N], 0.25 mM; sodium phosphate 50 mM

sample_3: cytoplasmic Ig-alpha polypeptide 0.3 mM; cytoplasmic Ig-beta polypeptide, [U-98% 15N], 0.3 mM; sodium phosphate 50 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D CBCANHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D HNHAsample_3isotropicsample_conditions_1
2D 1H-15N heteroNOEsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_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
  • Bruker Avance 700 MHz

Related Database Links:

EMBL S46706.1 CAA58523 M80461.1
BMRB 18867 19644 19645 19648 19649 19723 19725 18884 19650 19651 19723 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

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts