NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
18475 | 2dn7 | 10263 | cing | 1-original | MR format | comment |
*HEADER SIGNALING PROTEIN, HYDROLASE 25-APR-06 2DN7 *TITLE SOLUTION STRUCTURES OF THE 6TH FN3 DOMAIN OF HUMAN RECEPTOR- *TITLE 2 TYPE TYROSINE-PROTEIN PHOSPHATASE F *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE F; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: FIBRONECTIN TYPE III DOMAIN; *COMPND 5 SYNONYM: LAR PROTEIN, LEUKOCYTE ANTIGEN RELATED; *COMPND 6 EC: 3.1.3.48; *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: PTPRF, LAR; *SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS; *SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050719-01; *SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS *KEYWDS LAR PROTEIN, LEUKOCYTE ANTIGEN RELATED, STRUCTURAL GENOMICS, *KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND *KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS *KEYWDS 4 INITIATIVE, RSGI, SIGNALING PROTEIN, HYDROLASE *EXPDTA SOLUTION NMR *NUMMDL 20 *AUTHOR M.SATO, N.TOCHIO, S.KOSHIBA, M.INOUE, T.KIGAWA, S.YOKOYAMA, *AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) *REVDAT 1 12-MAY-09 2DN7 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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