1rn1: Difference between revisions

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[[Image:1rn1.~~jpg~~|left|200px]]

[[Image:1rn1.png|left|200px]]

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~~'''~~THREE-DIMENSIONAL STRUCTURE OF GLN 25-RIBONUCLEASE T1 AT 1.84 ANGSTROMS RESOLUTION: STRUCTURAL VARIATIONS AT THE BASE RECOGNITION AND CATALYTIC SITES~~'''~~

===THREE-DIMENSIONAL STRUCTURE OF GLN 25-RIBONUCLEASE T1 AT 1.84 ANGSTROMS RESOLUTION: STRUCTURAL VARIATIONS AT THE BASE RECOGNITION AND CATALYTIC SITES===

~~==Overview==~~

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The ~~structure of~~ the ~~Gln25 variant of ribonuclease T1~~ (~~RNase T1) crystallized~~ at ~~pH 7 and at high ionic strength has been solved by molecular replacement using the coordinates of the Lys25-RNase T1~~/~~2'-guanylic acid (2'GMP) complex at pH 5 [Arni et al. (1988) J. Biol. Chem~~. ~~263, 15358-15368] and refined by energy minimization and stereochemically restrained least-squares minimization to a crystallographic R-factor of 14~~.4% at 1.84-A resolution. The asymmetric unit contains three molecules, and the final model consists of 2302 protein atoms, 3 sulfates (at the catalytic sites), and 179 solvent water molecules. The estimated root mean square (rms) ~~error in the coordinates is 0.15 A~~, ~~and the rms deviation from ideality~~ is ~~0.018 A for bond lengths and 1.8 degrees for bond angles. Significant differences are observed between the three molecules in the asymmetric unit at~~ the ~~base recognition and catalytic sites~~.

The line below this paragraph, {{ABSTRACT_PUBMED_1554699}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 1554699 is the PubMed ID number.

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==About this Structure==

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[[Category: Ravichandran, K G.]]

[[Category: Tulinsky, A.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 07~~:41:25 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:28:06 2008''

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-[[Image:1rn1.jpg|left|200px]]
+{{Seed}}
+[[Image:1rn1.png|left|200px]]
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@@ Line 9: / Line 10: @@
 {{STRUCTURE_1rn1|  PDB=1rn1  |  SCENE=  }}
-'''THREE-DIMENSIONAL STRUCTURE OF GLN 25-RIBONUCLEASE T1 AT 1.84 ANGSTROMS RESOLUTION: STRUCTURAL VARIATIONS AT THE BASE RECOGNITION AND CATALYTIC SITES'''
+===THREE-DIMENSIONAL STRUCTURE OF GLN 25-RIBONUCLEASE T1 AT 1.84 ANGSTROMS RESOLUTION: STRUCTURAL VARIATIONS AT THE BASE RECOGNITION AND CATALYTIC SITES===
-==Overview==
+<!--
-The structure of the Gln25 variant of ribonuclease T1 (RNase T1) crystallized at pH 7 and at high ionic strength has been solved by molecular replacement using the coordinates of the Lys25-RNase T1/2'-guanylic acid (2'GMP) complex at pH 5 [Arni et al. (1988) J. Biol. Chem. 263, 15358-15368] and refined by energy minimization and stereochemically restrained least-squares minimization to a crystallographic R-factor of 14.4% at 1.84-A resolution. The asymmetric unit contains three molecules, and the final model consists of 2302 protein atoms, 3 sulfates (at the catalytic sites), and 179 solvent water molecules. The estimated root mean square (rms) error in the coordinates is 0.15 A, and the rms deviation from ideality is 0.018 A for bond lengths and 1.8 degrees for bond angles. Significant differences are observed between the three molecules in the asymmetric unit at the base recognition and catalytic sites.
+The line below this paragraph, {{ABSTRACT_PUBMED_1554699}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 1554699 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_1554699}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Ravichandran, K G.]]
 [[Category: Tulinsky, A.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:41:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:28:06 2008''