NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
13317 | 1ujo | 10068 | cing | 1-original | MR format | comment |
*HEADER STRUCTURAL PROTEIN 08-AUG-03 1UJO *TITLE SOLUTION STRUCTURE OF THE CH DOMAIN FROM MOUSE TRANGELIN *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: TRANSGELIN; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: CALPONIN HOMOLOGY (CH) DOMAIN; *COMPND 5 SYNONYM: SMOOTH MUSCLE PROTEIN 22-ALPHA, SM22-ALPHA, ACTIN- *COMPND 6 ASSOCIATED PROTEIN P27; *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 0610041C11; *SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P020520-56; *SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS *KEYWDS TRANSGELIN, CH DOMAIN, ACTIN BINDING, STRUCTURAL GENOMICS, *KEYWDS 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, *KEYWDS 3 STRUCTURAL PROTEIN *EXPDTA SOLUTION NMR *NUMMDL 20 *AUTHOR T.TOMIZAWA, S.KOSHIBA, T.KIGAWA, S.YOKOYAMA, RIKEN *AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) *REVDAT 1 12-MAY-09 1UJO 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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