NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
18225 | 2djs | 10258 | cing | 1-original | MR format | comment |
*HEADER SIGNALING PROTEIN 05-APR-06 2DJS *TITLE SOLUTION STRUCTURES OF THE FN3 DOMAIN OF HUMAN EPHRIN TYPE- *TITLE 2 B RECEPTOR 1 *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: EPHRIN TYPE-B RECEPTOR 1; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: FIBRONECTIN TYPE III DOMAIN; *COMPND 5 SYNONYM: TYROSINE-PROTEIN KINASE RECEPTOR EPH-2, NET, HEK6, *COMPND 6 ELK; *COMPND 7 EC: 2.7.1.112; *COMPND 8 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: EPHB1; *SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS; *SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050912-11; *SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS *KEYWDS TYROSINE-PROTEIN KINASE RECEPTOR EPH-2, NET, HEK6, ELK, *KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN *KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL *KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING PROTEIN *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 2DJS 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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