NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
503543 | 1wen | 11354 | cing | 1-original | MR format | comment |
*HEADER DNA BINDING PROTEIN 25-MAY-04 1WEN *TITLE SOLUTION STRUCTURE OF PHD DOMAIN IN ING1-LIKE PROTEIN *TITLE 2 BAC25079 *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: INHIBITOR OF GROWTH FAMILY, MEMBER 4; ING1-LIKE *COMPND 3 PROTEIN; *COMPND 4 CHAIN: A; *COMPND 5 FRAGMENT: PHD DOMAIN; *COMPND 6 SYNONYM: ING1-LIKE PROTEIN BAC25079; *COMPND 7 ENGINEERED: YES *SOURCE MOL_ID: 1; *SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; *SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; *SOURCE 4 ORGANISM_TAXID: 10090; *SOURCE 5 GENE: RIKEN CDNA 1110062A16; *SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030408-71; *SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS *KEYWDS NMR, STRUCTURAL GENOMICS, PHD DOMAIN, ING1-LIKE PROTEIN, *KEYWDS 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, DNA *KEYWDS 3 BINDING PROTEIN *EXPDTA SOLUTION NMR *NUMMDL 20 *AUTHOR F.HE, Y.MUTO, M.INOUE, T.KIGAWA, M.SHIROUZU, T.TERADA, *AUTHOR 2 S.YOKOYAMA, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE *AUTHOR 3 (RSGI) *REVDAT 1 12-MAY-09 1WEN 0 ************************************************************** During the CYANA calculations automatic implicit swapping of restraints involving diastereotopic substitutents was applied for prochrial groups without stereospecific assignment. Diastereotopic substitents were swapped individually in each conformer to calculate the minimal target function and restraint violations. The optimal swapping for a given prochiral group may differ among the 20 conformers that represent the solution structure. The swapping is therefore performed implicitly in the program and is not reflected in the distance restraint file deposited in the PDB. **************************************************************
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