4wbc: Difference between revisions

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[[Image:4wbc.jpg|left|200px]]<br /><applet load="4wbc" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:4wbc.jpg|left|200px]]<br /><applet load="4wbc" size="350" color="white" frame="true" align="right" spinBox="true"

caption="4wbc, resolution 2.138Å" />

'''2.13 A STRUCTURE OF A KUNITZ-TYPE WINGED BEAN CHYMOTRYPSIN INHIBITOR PROTEIN'''<br />

==Overview==

The crystal structure of a Kunitz-type double-headed alpha--chymotrypsin, inhibitor from winged bean seeds has been refined at 2.13 A resolution, using data collected from cryo-cooled (90 K) crystals which belong to the, hexagonal space group P6(1)22 with unit-cell parameters a = b = 60.84, c =, 207.91 A. The volume of the unit cell is reduced by 5.3% on cooling. The, refinement converged to an R value of 20.0% (R(free) = 25.8%) for 11100, unique reflections and the model shows good stereochemistry, with r.m.s., deviations from ideal values for bond lengths and bond angles of 0.011 A, and 1.4 degrees, respectively. The structural architecture of the protein, consists of 12 antiparallel beta-strands joined in the form of a, characteristic beta-trefoil fold, with the two reactive-site regions, Asn38-Leu43 and Gln63-Phe68, situated on two external loops. Although the, overall protein fold is the same as that of the room-temperature model, some conformational changes are observed in the loop regions and in the, side chains of a few surface residues. A total of 176 ordered water, molecules and five sulfate ions are included in the model.

The crystal structure of a Kunitz-type double-headed alpha--chymotrypsin inhibitor from winged bean seeds has been refined at 2.13 A resolution using data collected from cryo-cooled (90 K) crystals which belong to the hexagonal space group P6(1)22 with unit-cell parameters a = b = 60.84, c = 207.91 A. The volume of the unit cell is reduced by 5.3% on cooling. The refinement converged to an R value of 20.0% (R(free) = 25.8%) for 11100 unique reflections and the model shows good stereochemistry, with r.m.s. deviations from ideal values for bond lengths and bond angles of 0.011 A and 1.4 degrees, respectively. The structural architecture of the protein consists of 12 antiparallel beta-strands joined in the form of a characteristic beta-trefoil fold, with the two reactive-site regions, Asn38-Leu43 and Gln63-Phe68, situated on two external loops. Although the overall protein fold is the same as that of the room-temperature model, some conformational changes are observed in the loop regions and in the side chains of a few surface residues. A total of 176 ordered water molecules and five sulfate ions are included in the model.

==About this Structure==

4WBC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Psophocarpus_tetragonolobus Psophocarpus tetragonolobus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. This structure ~~superseeds~~ the now removed PDB entry 3WBC. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=4WBC OCA].

4WBC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Psophocarpus_tetragonolobus Psophocarpus tetragonolobus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 3WBC. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WBC OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Chakrabarti, C.]]

[[Category: Dattagupta, J.K.]]

[[Category: Dattagupta, J K.]]

[[Category: Ravichandran, S.]]

[[Category: Sen, U.]]

Line 20:

[[Category: serine protease inhibitor]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 19:51:~~41 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:14:38 2008''

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@@ Line 1: / Line 1: @@
-[[Image:4wbc.jpg|left|200px]]<br /><applet load="4wbc" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:4wbc.jpg|left|200px]]<br /><applet load="4wbc" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="4wbc, resolution 2.138&Aring;" />
 '''2.13 A STRUCTURE OF A KUNITZ-TYPE WINGED BEAN CHYMOTRYPSIN INHIBITOR PROTEIN'''<br />
 ==Overview==
-The crystal structure of a Kunitz-type double-headed alpha--chymotrypsin, inhibitor from winged bean seeds has been refined at 2.13 A resolution, using data collected from cryo-cooled (90 K) crystals which belong to the, hexagonal space group P6(1)22 with unit-cell parameters a = b = 60.84, c =, 207.91 A. The volume of the unit cell is reduced by 5.3% on cooling. The, refinement converged to an R value of 20.0% (R(free) = 25.8%) for 11100, unique reflections and the model shows good stereochemistry, with r.m.s., deviations from ideal values for bond lengths and bond angles of 0.011 A, and 1.4 degrees, respectively. The structural architecture of the protein, consists of 12 antiparallel beta-strands joined in the form of a, characteristic beta-trefoil fold, with the two reactive-site regions, Asn38-Leu43 and Gln63-Phe68, situated on two external loops. Although the, overall protein fold is the same as that of the room-temperature model, some conformational changes are observed in the loop regions and in the, side chains of a few surface residues. A total of 176 ordered water, molecules and five sulfate ions are included in the model.
+The crystal structure of a Kunitz-type double-headed alpha--chymotrypsin inhibitor from winged bean seeds has been refined at 2.13 A resolution using data collected from cryo-cooled (90 K) crystals which belong to the hexagonal space group P6(1)22 with unit-cell parameters a = b = 60.84, c = 207.91 A. The volume of the unit cell is reduced by 5.3% on cooling. The refinement converged to an R value of 20.0% (R(free) = 25.8%) for 11100 unique reflections and the model shows good stereochemistry, with r.m.s. deviations from ideal values for bond lengths and bond angles of 0.011 A and 1.4 degrees, respectively. The structural architecture of the protein consists of 12 antiparallel beta-strands joined in the form of a characteristic beta-trefoil fold, with the two reactive-site regions, Asn38-Leu43 and Gln63-Phe68, situated on two external loops. Although the overall protein fold is the same as that of the room-temperature model, some conformational changes are observed in the loop regions and in the side chains of a few surface residues. A total of 176 ordered water molecules and five sulfate ions are included in the model.
 ==About this Structure==
-WBC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Psophocarpus_tetragonolobus Psophocarpus tetragonolobus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 3WBC. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4WBC OCA].
+WBC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Psophocarpus_tetragonolobus Psophocarpus tetragonolobus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 3WBC. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WBC OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Chakrabarti, C.]]
-[[Category: Dattagupta, J.K.]]
+[[Category: Dattagupta, J K.]]
 [[Category: Ravichandran, S.]]
 [[Category: Sen, U.]]
@@ Line 20: / Line 20: @@
 [[Category: serine protease inhibitor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:51:41 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:14:38 2008''