BMRB Entry 36631

Title:
Ckappa domain of mouse immunoglobulin
Deposition date:
2023-12-23
Original release date:
2026-02-06
Authors:
Yanaka, S.; Kodama, A.; Miyanoiri, Y.; Kato, K.
Citation:

Citation: Yanaka, Saeko; Kodama, Atsuji; Nishiguchi, Shigetaka; Fujita, Rina; Shen, Jiana; Boonsri, Pornthip; Sung, Duckyong; Isono, Yukiko; Yagi, Hirokazu; Miyanoiri, Yohei; Uchihashi, Takayuki; Kato, Koichi. "Identification of potential C1-binding sites in the immunoglobulin CL domains."  Int. Immunol. 36, 405-412 (2024).
PubMed: 38564192

Assembly members:

Assembly members:
Immunoglobulin kappa constant, polymer, 112 residues, 12568.637 Da.

Natural source:

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: not available   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts431
15N chemical shifts123
1H chemical shifts787

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 112 residues - 12568.637 Da.

1   ALAASPALAALAPROTHRVALSERILEPHE
2   PROPROSERSERGLUGLNLEUTHRSERGLY
3   GLYALASERVALVALCYSPHELEUASNASN
4   PHETYRPROLYSASPILEASNVALLYSTRP
5   LYSILEASPGLYSERGLUARGGLNASNGLY
6   VALLEUASNSERTRPTHRASPGLNASPSER
7   LYSASPSERTHRTYRSERMETSERSERTHR
8   LEUTHRLEUTHRLYSASPGLUTYRGLUARG
9   HISASNSERTYRTHRCYSGLUALATHRHIS
10   LYSTHRSERTHRSERPROILEVALLYSSER
11   PHEASNARGASNGLUSERGLUASNLEUTYR
12   PHEGLN

Samples:

sample_1: Ckappa domain of mouse immunoglobulin, [U-13C; U-15N], 1.6 mM; sodium chloride 50 mM; NaPi 5 mM; H2O 95%; D2O, [U-2H], 5%

sample_2: Ckappa domain of mouse immunoglobulin, [U-13C; U-15N], 1.6 mM; H2O 95%; D2O, [U-2H], 5%

sample_3: Ckappa domain of mouse immunoglobulin, [U-13C; U-15N], 1.6 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: Not defined Not defined; pH: 6.0; pressure: 1 Pa; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

ARTINA, Klukowski, P., Riek, R. and Guntert, P. - refinement

ARTINA, Klukowski, P., Riek, R. and Guntert, P. - structure calculation

ARTINA, Klukowski, P., Riek, R. and Guntert, P. - chemical shift assignment

ARTINA, Klukowski, P., Riek, R. and Guntert, P. - peak picking

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks