BMRB Entry 16463

Name: Backbone and side-chain 1H, 13C and 15N resonance assignments of LEN, a human immunoglobulin kIV light-chain variable domain
Published: 2009-11-19

Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16463

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone and side-chain 1H, 13C and 15N resonance assignments of LEN, a human immunoglobulin kIV light-chain variable domain

Deposition date:

2009-08-20

Original release date:

2009-11-19

Authors:

Mukherjee, Sujoy; Pondaven, Simon; Hofer, Nicole; Jaroniec, Christopher

Citation:

Citation: Mukherjee, Sujoy; Pondaven, Simon; Hofer, Nicole; Jaroniec, Christopher. "Backbone and side-chain (1)H, (13)C and (15)N resonance assignments of LEN, a human immunoglobulin kappaIV light-chain variable domain." Biomol NMR Assign 3, 255-259 (2009).
PubMed: 19768664

Assembly members:

Assembly members:
LEN, polymer, 114 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: pASK40

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LEN: DIVMTQSPDSLAVSLGERAT INCKSSQSVLYSSNSKNYLA WYQQKPGQPPKLLIYWASTR ESGVPDRFSGSGSGTDFTLT ISSLQAEDVAVYYCQQYYST PYSFGQGTKLEIKR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	429
15N chemical shifts	110
1H chemical shifts	675

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	light chain variable domain	1

Entities:

Entity 1, light chain variable domain 114 residues - Formula weight is not available

1

ASP

ILE

VAL

MET

THR

GLN

SER

PRO

ASP

SER

2

LEU

ALA

VAL

SER

LEU

GLY

GLU

ARG

ALA

THR

3

ILE

ASN

CYS

LYS

SER

GLN

SER

VAL

LEU

4

TYR

SER

ASN

SER

LYS

ASN

TYR

LEU

ALA

5

TRP

TYR

GLN

LYS

PRO

GLY

GLN

PRO

6

LYS

LEU

ILE

TYR

TRP

ALA

SER

THR

ARG

7

GLU

SER

GLY

VAL

PRO

ASP

ARG

PHE

SER

GLY

8

SER

GLY

SER

GLY

THR

ASP

PHE

THR

LEU

THR

9

ILE

SER

LEU

GLN

ALA

GLU

ASP

VAL

ALA

10

VAL

TYR

CYS

GLN

TYR

SER

THR

11

PRO

TYR

SER

PHE

GLY

GLN

GLY

THR

LYS

LEU

12

GLU

ILE

LYS

ARG

Samples:

13C_15N-sample: LEN, [U-13C; U-15N], 1.5 mM; H2O 93%; D2O 7%; NaCl 100 mM; Sodium Phosphate 20 mM

15N-sample: LEN, [U-15N], 1.7 mM; H2O 93%; D2O 7%; NaCl 100 mM; Sodium Phosphate 20 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N-sample	isotropic	sample_conditions_1
3D HNCA	13C_15N-sample	isotropic	sample_conditions_1
3D HNCACB	13C_15N-sample	isotropic	sample_conditions_1
3D HNCO	13C_15N-sample	isotropic	sample_conditions_1
3D HN(CO)CA	13C_15N-sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	13C_15N-sample	isotropic	sample_conditions_1
3D 1H-15N TOCSY	15N-sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	15N-sample	isotropic	sample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker DRX 800 MHz
Bruker DMX 600 MHz

PDB	1EEQ 1EFQ 1LVE 1QAC 2LVE 3LVE 4LVE 5LVE
DBJ	BAC01688 BAC01708
EMBL	CAA26317 CAA81384 CAA83046 CAA86592 CAC10807
GB	AAA72130 AAB22366 AAB26921 AAB31509 AAD01817
PIR	A49138 S37529
PRF	2001180A 751423A
SP	P01625 P06312
AlphaFold	P01625 P06312