BMRB: 15110

Solution structure of V21C/V59C Lymphotactin/XCL1

Authors

Volkman, B.F., Tuinstra, R.L., Peterson, F.C., Elgin, E.S.

Assembly

Lymphotactin

Entity

1. Lymphotactin (polymer, Thiol state: all disulfide bound), 92 monomers, 10180.56 Da Detail

GSEVSDKRTC VSLTTQRLPC SRIKTYTITE GSLRAVIFIT KRGLKVCADP QATWVRDCVR SMDRKSNTRN NMIQTKPTGT QQSTNTAVTL TG

Formula weight

10180.56 Da

Entity Connection

disulfide 2 Detail

---

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS20:SG	1:CYS58:SG
2	disulfide	sing	1:CYS10:SG	1:CYS47:SG

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

AUTOMATED METHODS WERE USED FOR BACKBONE CHEMICAL SHIFT ASSIGNMENT AND ITERATIVE NOE REFINEMENT.

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.9 %, Completeness: 92.4 %, Completeness (bb): 96.3 % Detail

Download

• NMR-STAR v3.1 (partial)
• BMRB/XML (partial)
• CSV
• TSV

Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	92.4 % (957 of 1036)	91.1 % (491 of 539)	95.0 % (378 of 398)	88.9 % (88 of 99)
Backbone	96.3 % (526 of 546)	95.7 % (178 of 186)	96.3 % (261 of 271)	97.8 % (87 of 89)
Sidechain	89.8 % (518 of 577)	88.7 % (313 of 353)	95.3 % (204 of 214)	10.0 % (1 of 10)
Aromatic	86.7 % (26 of 30)	100.0 % (15 of 15)	71.4 % (10 of 14)	100.0 % (1 of 1)
Methyl	93.5 % (101 of 108)	94.4 % (51 of 54)	92.6 % (50 of 54)

1. Lymphotactin

GSEVSDKRTC VSLTTQRLPC SRIKTYTITE GSLRAVIFIT KRGLKVCADP QATWVRDCVR SMDRKSNTRN NMIQTKPTGT QQSTNTAVTL TG

Show sample condition

Sample

Solvent system 90% H2O, 10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0, Details 1 mM CC3 hLtn, U-15N, 13C; 20 mM phospate buffer, 90% H2O, 10% D2O

#	Name	Isotope labeling	Type	Concentration
1	Lymphotactin	[U-99% 13C; U-99% 15N]		1 mM
2	sodium phosphate	natural abundance		20 mM
3	H2O			90 %
4	D2O			10 %

Hide sample codition

LACS Plot; CA

Referencing offset: -0.2 ppm, Outliers: 2 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Hide chemical shift referencing parameters

LACS Plot; CB

Referencing offset: -0.2 ppm, Outliers: 2 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Hide chemical shift referencing parameters

LACS Plot; HA

Referencing offset: -0.03 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Hide chemical shift referencing parameters

LACS Plot; CO

Referencing offset: 0.07 ppm, Outliers: 3 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

Hide chemical shift referencing parameters

Protein Blocks Logo

Calculated from 20 models in PDB: 2HDM, Strand ID: A Detail

---

Release date

2007-05-03

Citation

An engineered second disulfide bond restricts lymphotactin/XCL1 to a chemokine-like conformation with XCR1 agonist activity
Tuinstra, R.L., Peterson, F.C., Elgin, E.S., Pelzek, A.J., Volkman, B.F.
Biochemistry (2007), 46, 2564-2573, PubMed 17302442 , DOI 10.1021/bi602365d , Abstract

Related entities 1. Lymphotactin, : 1 : 7 : 10 entities Detail

Interaction partners 1. Lymphotactin, : 18 interactors Detail

Experiments performed 3 experiments Detail