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1g6x

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(New page: 200px<br /><applet load="1g6x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g6x, resolution 0.86&Aring;" /> '''ULTRA HIGH RESOLUTIO...)
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[[Image:1g6x.gif|left|200px]]<br /><applet load="1g6x" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1g6x, resolution 0.86&Aring;" />
caption="1g6x, resolution 0.86&Aring;" />
'''ULTRA HIGH RESOLUTION STRUCTURE OF BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI) MUTANT WITH ALTERED BINDING LOOP SEQUENCE'''<br />
'''ULTRA HIGH RESOLUTION STRUCTURE OF BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI) MUTANT WITH ALTERED BINDING LOOP SEQUENCE'''<br />
==Overview==
==Overview==
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The crystal structure of a mutant of bovine pancreatic trypsin inhibitor, has been refined to 0.86 A resolution using low-temperature synchrotron, data. The variant contains three mutations in the binding loop (Thr11Ala, Pro13Ala, Lys15Arg) and an unrelated Met52Leu substitution. Refinement, with anisotropic displacement parameters and with removal of main-chain, stereochemical restraints converged with R = 0.1035. The use of, full-matrix refinement provided an estimate of the variances in the, derived parameters. Some stereochemical parameters, such as the planarity, of the peptide group and the value of the N-C(alpha)-C angle, show a wide, spread, suggesting that the standard values used as restraints in protein, structure refinements may not always be entirely appropriate. Comparison, with the recently determined room-temperature structure of the same mutant, at 1.42 A resolution confirms the previous observations and provides new, details, such as a double conformation of the main chain at Leu29 and at, Gly56-Gly57, a high proportion (over 20%) of residues in double, conformations, correlation of disorder through lattice contacts and the, positions of H atoms, including those in water molecules, and their, involvement in C-H...O and N-H...pi hydrogen bonds.
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The crystal structure of a mutant of bovine pancreatic trypsin inhibitor has been refined to 0.86 A resolution using low-temperature synchrotron data. The variant contains three mutations in the binding loop (Thr11Ala, Pro13Ala, Lys15Arg) and an unrelated Met52Leu substitution. Refinement with anisotropic displacement parameters and with removal of main-chain stereochemical restraints converged with R = 0.1035. The use of full-matrix refinement provided an estimate of the variances in the derived parameters. Some stereochemical parameters, such as the planarity of the peptide group and the value of the N-C(alpha)-C angle, show a wide spread, suggesting that the standard values used as restraints in protein structure refinements may not always be entirely appropriate. Comparison with the recently determined room-temperature structure of the same mutant at 1.42 A resolution confirms the previous observations and provides new details, such as a double conformation of the main chain at Leu29 and at Gly56-Gly57, a high proportion (over 20%) of residues in double conformations, correlation of disorder through lattice contacts and the positions of H atoms, including those in water molecules, and their involvement in C-H...O and N-H...pi hydrogen bonds.
==About this Structure==
==About this Structure==
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1G6X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G6X OCA].
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1G6X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G6X OCA].
==Reference==
==Reference==
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[[Category: serine protease inhibitor]]
[[Category: serine protease inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:46:02 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:47 2008''

Revision as of 10:46, 21 February 2008

Image:1g6x.gif

1g6x, resolution 0.86Å

Drag the structure with the mouse to rotate

ULTRA HIGH RESOLUTION STRUCTURE OF BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI) MUTANT WITH ALTERED BINDING LOOP SEQUENCE

Overview

The crystal structure of a mutant of bovine pancreatic trypsin inhibitor has been refined to 0.86 A resolution using low-temperature synchrotron data. The variant contains three mutations in the binding loop (Thr11Ala, Pro13Ala, Lys15Arg) and an unrelated Met52Leu substitution. Refinement with anisotropic displacement parameters and with removal of main-chain stereochemical restraints converged with R = 0.1035. The use of full-matrix refinement provided an estimate of the variances in the derived parameters. Some stereochemical parameters, such as the planarity of the peptide group and the value of the N-C(alpha)-C angle, show a wide spread, suggesting that the standard values used as restraints in protein structure refinements may not always be entirely appropriate. Comparison with the recently determined room-temperature structure of the same mutant at 1.42 A resolution confirms the previous observations and provides new details, such as a double conformation of the main chain at Leu29 and at Gly56-Gly57, a high proportion (over 20%) of residues in double conformations, correlation of disorder through lattice contacts and the positions of H atoms, including those in water molecules, and their involvement in C-H...O and N-H...pi hydrogen bonds.

About this Structure

1G6X is a Single protein structure of sequence from Bos taurus with and as ligands. Full crystallographic information is available from OCA.

Reference

Ultrahigh-resolution structure of a BPTI mutant., Addlagatta A, Krzywda S, Czapinska H, Otlewski J, Jaskolski M, Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):649-63. Epub 2001, Apr 24. PMID:11320305

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