NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | cing | stage | program | type |
5945 | 1i8g | cing | 1-original | MR format | comment |
*HEADER HYDROLASE/ISOMERASE 14-MAR-01 1I8G *TITLE SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH CDC25 *TITLE 2 PHOSPHOTHREONINE PEPTIDE *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: M-PHASE INDUCER PHOSPHATASE 3; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: RESIDUES 63-72; *COMPND 5 EC: 3.1.3.48; *COMPND 6 ENGINEERED: YES; *COMPND 7 MOL_ID: 2; *COMPND 8 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA- *COMPND 9 INTERACTING 1; *COMPND 10 CHAIN: B; *COMPND 11 FRAGMENT: WW DOMAIN (RESIDUES 6-44); *COMPND 12 EC: 5.2.1.8; *COMPND 13 ENGINEERED: YES *SOURCE MOL_ID: 1; *SOURCE 2 SYNTHETIC: YES; *SOURCE 3 OTHER_DETAILS: THE LIGAND PHOSPHOPEPTIDE WAS SYNTHESIZED *SOURCE 4 FROM RINK AMIDE RESIN USING THE FMOC STRATEGY AND *SOURCE 5 ACTIVATION BY HBTU AND HOBT IN A 431A PEPTIDE SYNTHESIZER. *SOURCE 6 THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN XENOPUS *SOURCE 7 LAEVIS (AFRICAN CLAWED FROG).; *SOURCE 8 MOL_ID: 2; *SOURCE 9 SYNTHETIC: YES; *SOURCE 10 OTHER_DETAILS: THE PIN1 WW DOMAIN WAS OBTAINED BY PEPTIDE *SOURCE 11 SYNTHESIS USING THE BOC-BENZYL STRATEGY AND THE HBTU IN *SOURCE 12 SITU ACTIVATION PROTOCOL ON AN APPLIED 430A PEPTIDE *SOURCE 13 SYNTHESIZER. THE SEQUENCE OF THE PEPTIDE IS NATURALLY *SOURCE 14 FOUND IN HOMO SAPIENS (HUMAN). *KEYWDS CELL DIVISION, NUCLEAR PROTEIN *EXPDTA NMR, 10 STRUCTURES *AUTHOR R.WINTJENS, J.-M.WIERUSZESKI, H.DROBECQ, G.LIPPENS, *AUTHOR 2 I.LANDRIEU *REVDAT 1 18-JUL-01 1I8G 0 assign (atom "WW" 6 HE1 )(atom "WW" 6 HZ2 ) 2.0 0.2 1.0
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