2gi9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|ACTIVITY=
|ACTIVITY=
|GENE= spg ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
|GENE= spg ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1pga|1PGA]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gi9 OCA], [http://www.ebi.ac.uk/pdbsum/2gi9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gi9 RCSB]</span>
}}
}}
Line 28: Line 31:
[[Category: gb1]]
[[Category: gb1]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:04:57 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:16:59 2008''

Revision as of 00:17, 31 March 2008


PDB ID 2gi9

Drag the structure with the mouse to rotate
, resolution 1.14Å
Gene: spg (Staphylococcus aureus)
Related: 1PGA


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Backbone Conformational Constraints in a Microcrystalline U-15N-Labeled Protein by 3D Dipolar-Shift Solid-State NMR Spectroscopy


Overview

Structural studies of uniformly labeled proteins by magic-angle spinning NMR spectroscopy have rapidly matured in recent years. Site-specific chemical shifts of several proteins have been assigned and structures determined from 2D or 3D data sets containing internuclear distance information. Here we demonstrate the application of a complementary technique for constraining protein backbone geometry using a site-resolved 3D dipolar-shift pulse sequence. The dipolar line shapes report on the relative orientations of 1H-15N[i] to 1H-15N[i+1] dipole vectors, constraining the torsion angles phi[i] and psi[i]. In addition, from the same 3D data set, several 1H-15N[i] to1H-15N[i+2] line shapes are extracted to constrain the torsion angles phi[i], psi[i], phi[i+1], and psi[i+1]. We report results for the majority of sites in the 56-residue beta1 immunoglobulin binding domain of protein G (GB1), using 3D experiments at 600 MHz 1H frequency. Excellent agreement between the SSNMR results and a new 1.14 A crystal structure illustrate the general potential of this technique for high-resolution structural refinement of solid proteins.

About this Structure

2GI9 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

Backbone conformational constraints in a microcrystalline U-15N-labeled protein by 3D dipolar-shift solid-state NMR spectroscopy., Franks WT, Wylie BJ, Stellfox SA, Rienstra CM, J Am Chem Soc. 2006 Mar 15;128(10):3154-5. PMID:16522090

Page seeded by OCA on Mon Mar 31 03:16:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools