BMRB Entry 36630

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36630
MolProbity Validation Chart

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

Title:
Ckappa domain of human 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 light chain, polymer, 111 residues, 12298.498 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):

Entity Sequences (FASTA):
Immunoglobulin kappa light chain: VAAPSVFIFPPSDEQLKSGT ASVVCLLNNFYPREAKVQWK VDNALQSGNSQESVTEQDSK DSTYSLSSTLTLSKADYEKH KVYACEVTHQGLSSPVTKSF NRGESENLYFQ

Data sets:
Data typeCount
13C chemical shifts437
15N chemical shifts122
1H chemical shifts794

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 - 12298.498 Da.

1   VALALAALAPROSERVALPHEILEPHEPRO
2   PROSERASPGLUGLNLEULYSSERGLYTHR
3   ALASERVALVALCYSLEULEUASNASNPHE
4   TYRPROARGGLUALALYSVALGLNTRPLYS
5   VALASPASNALALEUGLNSERGLYASNSER
6   GLNGLUSERVALTHRGLUGLNASPSERLYS
7   ASPSERTHRTYRSERLEUSERSERTHRLEU
8   THRLEUSERLYSALAASPTYRGLULYSHIS
9   LYSVALTYRALACYSGLUVALTHRHISGLN
10   GLYLEUSERSERPROVALTHRLYSSERPHE
11   ASNARGGLYGLUSERGLUASNLEUTYRPHE
12   GLN

Samples:

sample_1: protein, [U-13C; U-15N], 1.0 mM; sodium chloride 50 mM; Napi 5 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: Not defined Not defined; pH: 5.0; pressure: 1 Pa; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

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

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

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

NMR spectrometers:

  • Bruker AVANACE 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