BMRB: 6261

NMR STRUCTURE OF THE SH3 DOMAIN OF HUMAN LYN TYROSINE KINASE

Authors

Bauer, F., Schweimer, K., Hoffmann, S., Roesch, P., Sticht, H.

Assembly

SH3 domain of Lyn Tyrosine Kinase

Entity

1. SH3 domain of Lyn Tyrosine Kinase (polymer, Thiol state: not present), 68 monomers, 7630.591 Da Detail

GPLGSPEEQG DIVVALYPYD GIHPDDLSFK KGEKMKVLEE HGEWWKAKSL LTKKEGFIPS NYVAKLNT

Formula weight

7630.591 Da

Source organism

Homo sapiens

Exptl. method

NMR

Refine. method

X-PLOR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 91.7 %, Completeness (bb): 96.0 % Detail

Download

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

Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	91.7 % (748 of 816)	96.5 % (413 of 428)	83.7 % (268 of 320)	98.5 % (67 of 68)
Backbone	96.0 % (382 of 398)	96.4 % (133 of 138)	94.9 % (187 of 197)	98.4 % (62 of 63)
Sidechain	88.7 % (425 of 479)	96.6 % (280 of 290)	76.1 % (140 of 184)	100.0 % (5 of 5)
Aromatic	55.3 % (42 of 76)	100.0 % (38 of 38)	5.6 % (2 of 36)	100.0 % (2 of 2)
Methyl	92.4 % (61 of 66)	100.0 % (33 of 33)	84.8 % (28 of 33)

1. SH3 domain of the Lyn kinase

GPLGSPEEQG DIVVALYPYD GIHPDDLSFK KGEKMKVLEE HGEWWKAKSL LTKKEGFIPS NYVAKLNT

Show sample condition

Sample

Temperature 298 (±1) K, pH 6.4 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	SH3 domain of the Lyn kinase	[U-99% 13C; U-98% 15N]		1.5 mM

Hide sample codition

LACS Plot; CA

Referencing offset: -0.57 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
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

Hide chemical shift referencing parameters

LACS Plot; CB

Referencing offset: -0.57 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
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

Hide chemical shift referencing parameters

LACS Plot; HA

Referencing offset: -0.07 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
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

Hide chemical shift referencing parameters

LACS Plot; CO

Referencing offset: 0.61 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
1H	DSS	methyl protons	0.0 ppm	internal	direct	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495

Hide chemical shift referencing parameters

Protein Blocks Logo

Calculated from 20 models in PDB: 1W1F, Strand ID: A Detail

---

Release date

2005-10-16

Citation

Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity
Bauer, F., Schweimer, K., Meiselbach, H., Hoffmann, S., Roesch, P., Sticht, H.
Protein Sci. (2005), 14, 2487-2498, PubMed 16155203 , DOI 10.1110/ps.051563605 , Abstract

Entries sharing articles BMRB: 1, Swiss-Prot: 1 entries Detail

Related entities 1. SH3 domain of Lyn Tyrosine Kinase, : 1 : 5 : 242 entities Detail

Interaction partners 1. SH3 domain of Lyn Tyrosine Kinase, : 94 interactors Detail

Experiments performed 9 experiments Detail