BMRB Entry 36634

Title:
Clamda1 domain of human immunoglobulin
Deposition date:
2023-12-25
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 lambda constant 2, polymer, 111 residues, 12026.254 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: not available   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts439
15N chemical shifts116
1H chemical shifts786

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 111 residues - 12026.254 Da.

1   GLNPROLYSALAALAPROSERVALTHRLEU
2   PHEPROPROSERSERGLUGLULEUGLNALA
3   ASNLYSALATHRLEUVALCYSLEUILESER
4   ASPPHETYRPROGLYALAVALTHRVALALA
5   TRPLYSALAASPSERSERPROVALLYSALA
6   GLYVALGLUTHRTHRTHRPROSERLYSGLN
7   SERASNASNLYSTYRALAALASERSERTYR
8   LEUSERLEUTHRPROGLUGLNTRPLYSSER
9   HISARGSERTYRSERCYSGLNVALTHRHIS
10   GLUGLYSERTHRVALGLULYSTHRVALALA
11   PROTHRGLUSERSERGLUASNLEUTYRPHE
12   GLN

Samples:

sample_1: Clamda1 domain of human immunoglobulin, [U-100% 13C; U-100% 15N], 1.6 mM; sodium chloride 50 mM; NaPi 5 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CCH-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