BMRB Entry 15110

Name: Solution structure of V21C/V59C Lymphotactin/XCL1
Published: 2007-05-04

Click here to enlarge.

PDB ID: 2hdm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15110
MolProbity Validation Chart

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

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of V21C/V59C Lymphotactin/XCL1

Deposition date:

2007-01-23

Original release date:

2007-05-04

Authors:

Volkman, B.; Tuinstra, R.; Peterson, F.; Elgin, E.

Citation:

Citation: Tuinstra, R.; Peterson, F.; Elgin, E.; Pelzek, A.; Volkman, B.. "An engineered second disulfide bond restricts lymphotactin/XCL1 to a chemokine-like conformation with XCR1 agonist activity" Biochemistry 46, 2564-2573 (2007).
PubMed: 17302442

Assembly members:

Assembly members:
Lymphotactin, polymer, 92 residues, 10198.776 Da.

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: pQE308HT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Lymphotactin: GSEVSDKRTCVSLTTQRLPC SRIKTYTITEGSLRAVIFIT KRGLKVCADPQATWVRDCVR SMDRKSNTRNNMIQTKPTGT QQSTNTAVTLTG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	377
15N chemical shifts	88
1H chemical shifts	593

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Lymphotactin	1

Entities:

Entity 1, Lymphotactin 92 residues - 10198.776 Da.

1

GLY

SER

GLU

VAL

SER

ASP

LYS

ARG

THR

CYS

2

VAL

SER

LEU

THR

GLN

ARG

LEU

PRO

CYS

3

SER

ARG

ILE

LYS

THR

TYR

THR

ILE

THR

GLU

4

GLY

SER

LEU

ARG

ALA

VAL

ILE

PHE

ILE

THR

5

LYS

ARG

GLY

LEU

LYS

VAL

CYS

ALA

ASP

PRO

6

GLN

ALA

THR

TRP

VAL

ARG

ASP

CYS

VAL

ARG

7

SER

MET

ASP

ARG

LYS

SER

ASN

THR

ARG

ASN

8

ASN

MET

ILE

GLN

THR

LYS

PRO

THR

GLY

THR

9

GLN

SER

THR

ASN

THR

ALA

VAL

THR

LEU

10

THR

GLY

Samples:

sample: Lymphotactin, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 10 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D_15N-separated_NOESY	sample	isotropic	sample_conditions_1
3D_13C-separated_NOESY	sample	isotropic	sample_conditions_1
3D_13C-separated_NOESY (AROMATIC)	sample	isotropic	sample_conditions_1

Software:

xwinnmr v3.5, Bruker Biospin - collection

NMRPipe v2004, Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A. - processing

XEASY v1.3, Bartels, C, Xia, T.-H., Billeter, M., Guntert, P., Wuthrich, K. - data analysis

GARANT v2.1, Bartels, C., Billeter, M., Guntert, P., Wuthrich, K. - data analysis

CYANA v2.1, Herrmann, T., Guntert, P., Wuthrich, K. - structure solution

X-PLOR NIH v2.9.3, Schwieters, C.D., Kuszewski, J.J, Tjandra, N., Clore, G.M. - refinement

NMR spectrometers:

Bruker DRX 600 MHz

BMRB	15215
PDB	1J8I 1J9O 2HDM 2JP1 2NYZ
DBJ	BAA07825 BAA09859
EMBL	CAA60198
GB	AAC50164 AAH69817 AAH70309 AIC49701 AJA36131
REF	NP_002986 XP_003824662 XP_004027907 XP_009436138 XP_011508167
SP	P47992
AlphaFold	P47992