| Entry ID |
Link Type |
Entity ID |
Title |
|
136
|
Sequence mapping |
1 |
NMR Signal Assignments of Amide Protons in the alpha-Helical Domains of
Staphylococcal Nuclease |
|
188
|
Sequence mapping |
1 |
NMR Signal Assignments of Amide Protons in the alpha-Helical Domains of
Staphylococcal Nuclease |
|
189
|
Sequence mapping |
1 |
NMR Signal Assignments of Amide Protons in the alpha-Helical Domains of
Staphylococcal Nuclease |
|
494
|
Sequence mapping |
1 |
Two-Dimensional NMR Studies of Staphylococcal Nuclease. 1. Sequence-Specific
Assignments of Hydrogen-1 Signals and Solution Structure of the Nuclease
H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex |
|
495
|
Sequence mapping |
1 |
Two-Dimensional NMR Studies of Staphylococcal Nuclease. 1. Sequence-Specific
Assignments of Hydrogen-1 Signals and Solution Structure of the Nuclease
H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex |
|
496
|
Sequence mapping |
1 |
Two-Dimensional NMR Studies of Staphylococcal Nuclease. 2. Sequence-Specific
Assignments of Carbon-13 and Nitrogen-15 Signals from the Nuclease
H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex |
|
497
|
Sequence mapping |
1 |
Two-Dimensional NMR Studies of Staphylococcal Nuclease. 2. Sequence-Specific
Assignments of Carbon-13 and Nitrogen-15 Signals from the Nuclease
H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex |
|
530
|
Sequence mapping |
1 |
Two-Dimensional NMR Studies of Staphylococcal Nuclease: Evidence for
Conformational Heterogeneity from Hydrogen-1, Carbon-13, and Nitrogen-15 Spin
System Assignments of the Aromatic Amino Acids in the Nuclease H124L-Thymidine
3',5'-Bisphosp |
|
644
|
Sequence mapping |
1 |
Proline Assignments and Identification of the Cis K116/P117 Peptide Bond in
Liganded Staphylococcal Nuclease Using Isotope Edited 2D NMR Spectroscopy |
|
1581
|
Sequence mapping |
1 |
Deletion of the omega-loop in the Active Site of Staphylococcal Nuclease 2.
Effects on Protein Structure and Dynamics |
|
1582
|
Sequence mapping |
1 |
Deletion of the omega-loop in the Active Site of Staphylococcal Nuclease 2.
Effects on Protein Structure and Dynamics |
|
1704
|
Sequence mapping |
1 |
Two-Dimensional NMR Studies of Staphylococcal Nuclease: Evidence for
Conformational Heterogeneity from Hydrogen-1, Carbon-13, and Nitrogen-15 Spin
System Assignments of the Aromatic Amino Acids in the Nuclease H124L-Thymidine
3',5'-Bisphosp |
|
1874
|
Sequence mapping |
1 |
Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical
Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift
Changes That Accompany Formation of the Nuclease-Thymidine
3',5'-Bisphosphate-Calcium |
|
1875
|
Sequence mapping |
1 |
Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical
Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift
Changes That Accompany Formation of the Nuclease-Thymidine
3',5'-Bisphosphate-Calcium |
|
1876
|
Sequence mapping |
1 |
Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical
Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift
Changes That Accompany Formation of the Nuclease-Thymidine
3',5'-Bisphosphate-Calcium |
|
1877
|
Sequence mapping |
1 |
Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical
Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift
Changes That Accompany Formation of the Nuclease-Thymidine
3',5'-Bisphosphate-Calcium |
|
1878
|
Sequence mapping |
1 |
Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical
Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift
Changes That Accompany Formation of the Nuclease-Thymidine
3',5'-Bisphosphate-Calcium |
|
2784
|
Sequence mapping |
1 |
Dynamics of Methyl Groups in Proteins As Studied by Proton-Detected 13C NMR
Spectroscopy. Application to the Leucine Residues of Staphylococcal Nuclease |
|
2785
|
Sequence mapping |
1 |
Dynamics of Methyl Groups in Proteins As Studied by Proton-Detected 13C NMR
Spectroscopy. Application to the Leucine Residues of Staphylococcal Nuclease |
|
4010
|
Sequence mapping |
1 |
Resonance Assignments for the OB-fold Sub-Domain of Staphylococcal Nuclease
(SNOB) -> Nuclease 1-103 (V66L, G88V) |
|
4052
|
Sequence mapping |
1 |
Solution structures of Staphylococcal Nuclease from multidimensional,
multinuclear NMR: nuclease-H124L and its ternary complex with Ca2+ and
Thymidine-3'-5'-bisphosphate |
|
4905
|
Sequence mapping |
1 |
1H, 13C and 15N Chemical Shift Assignments for Urea-denatured G88W-110 Fragment
of Staphylococcal Nuclease |
|
5536
|
Sequence mapping |
1 |
1H, 13C, and 15N Chemical Shift Assignments for G88W110 fragment of
Staphylococcal Nuclease |
|
6250
|
Sequence mapping |
1 |
Backbone Chemical Shift Assignments for G88W121 fragment of Staphylococcal
Nuclease |
|
6251
|
Sequence mapping |
1 |
Backbone Chemical Shift Assignments for V66W121 fragment of Staphylococcal
Nuclease |
|
6907
|
Sequence mapping |
1 |
Chemical Shift Assignments for V66W110 fragment of Staphylococcal Nuclease |
|
6908
|
Sequence mapping |
1 |
1H, 13C, and 15N Chemical Shift Assignments for SNase110 fragment of
Staphylococcal Nuclease in 2M TMAO |
|
7012
|
Sequence mapping |
1 |
Solution structure of 55-72 segment of staphylococcal nuclease |
|
16585
|
Sequence mapping |
1 |
Solution structure of SNase140 |
|
18013
|
Sequence mapping |
1 |
Staphylococcal Nuclease PHS variant |
|
18788
|
Sequence mapping |
1 |
Solution structure of staphylococcal nuclease E43S mutant in the presence of ssDNA and Cd2+ |
