NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
28423 | 2yup | 10195 | cing | 1-original | MR format | comment |
*HEADER CELL ADHESION 06-APR-07 2YUP *TITLE SOLUTION STRUCTURE OF THE SECOND SH3 DOMAIN OF HUMAN VINEXIN *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: VINEXIN; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: SH3 DOMAIN; *COMPND 5 SYNONYM: SORBIN AND SH3 DOMAIN-CONTAINING PROTEIN 3, SH3- *COMPND 6 CONTAINING ADAPTER MOLECULE 1, SCAM-1; *COMPND 7 ENGINEERED: YES *SOURCE MOL_ID: 1; *SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; *SOURCE 3 ORGANISM_COMMON: HUMAN; *SOURCE 4 ORGANISM_TAXID: 9606; *SOURCE 5 GENE: SORBS3; *SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050627-09; *SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS *KEYWDS SORBIN AND SH3 DOMAIN-CONTAINING PROTEIN 3, SH3-CONTAINING *KEYWDS 2 ADAPTER MOLECULE 1, SCAM-1, STRUCTURAL GENOMICS, NPPSFA, *KEYWDS 3 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL *KEYWDS 4 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, *KEYWDS 5 RSGI, CELL ADHESION *EXPDTA SOLUTION NMR *NUMMDL 20 *AUTHOR H.ABE, N.TOCHIO, K.MIYAMOTO, K.SAITO, A.SASAGAWA, S.KOSHIBA, *AUTHOR 2 M.INOUE, T.KIGAWA, S.YOKOYAMA, RIKEN STRUCTURAL *AUTHOR 3 GENOMICS/PROTEOMICS INITIATIVE (RSGI) *REVDAT 1 12-MAY-09 2YUP 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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