NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | cing | stage | program | type |
18348 | 2dlh | cing | 1-original | MR format | comment |
*HEADER HYDROLASE 18-APR-06 2DLH *TITLE SOLUTION STRUCTURE OF THE SECOND FN3 DOMAIN OF HUMAN *TITLE 2 RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE DELTA *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE DELTA; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: FN3, FIBRONECTIN TYPE-III; *COMPND 5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE DELTA, R-PTP-DELTA; *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: PTPRD; *SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS; *SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050302-29; *SOURCE 9 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS *KEYWDS PROTEIN-TYROSINE PHOSPHATASE DELTA, R-PTP-DELTA, STRUCTURAL *KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL *KEYWDS 3 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL *KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, HYDROLASE *EXPDTA SOLUTION NMR *NUMMDL 20 *AUTHOR K.SEIMIYA, F.HAYASHI, M.YOSHIDA, S.YOKOYAMA, RIKEN *AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) *REVDAT 1 12-MAY-09 2DLH 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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