NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
19059 | 2ecz | 11154 | cing | 1-original | MR format | comment |
*HEADER SIGNALING PROTEIN 14-FEB-07 2ECZ *TITLE SOLUTION STRUCTURE OF THE SH3 DOMAIN OF SORBIN AND SH3 *TITLE 2 DOMAIN-CONTAINING PROTEIN 1 *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: SORBIN AND SH3 DOMAIN-CONTAINING PROTEIN 1; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: SH3 DOMAIN; *COMPND 5 SYNONYM: PONSIN, C-CBL-ASSOCIATED PROTEIN, CAP, SH3 DOMAIN *COMPND 6 PROTEIN 5, SH3P12; *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: SORBS1; *SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050613-24; *SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS *KEYWDS GLYCOPROTEIN, MEMBRANE, NUCLEAR PROTEIN, PHOSPHORYLATION, *KEYWDS 2 POLYMORPHISM, SH3 DOMAIN, TRANSPORT, STRUCTURAL GENOMICS, *KEYWDS 3 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND *KEYWDS 4 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS *KEYWDS 5 INITIATIVE, RSGI, SIGNALING PROTEIN *EXPDTA SOLUTION NMR *NUMMDL 20 *AUTHOR H.ABE, K.MIYAMOTO, N.TOCHIO, K.SAITO, T.KIGAWA, S.YOKOYAMA, *AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) *REVDAT 1 12-MAY-09 2ECZ 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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