NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
459879 | 1x5l | 11208 | cing | 1-original | MR format | comment |
*HEADER SIGNALING PROTEIN 16-MAY-05 1X5L *TITLE SOLUTION STRUCTURE OF THE SECOND FN3 DOMAIN OF EPH RECEPTOR *TITLE 2 A8 PROTEIN *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: EPHRIN TYPE-A RECEPTOR 8; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: FN3 DOMAIN; *COMPND 5 SYNONYM: TYROSINE-PROTEIN KINASE RECEPTOR EEK, EPH-AND ELK- *COMPND 6 RELATED KINASE, HEK3; *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: KAZUSA CDNA FH16961; *SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040705-14; *SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS *KEYWDS FN3 DOMAIN, EPHRIN TYPE-A RECEPTOR 8 PRECURSOR/TYROSINE- *KEYWDS 2 PROTEIN KINASE RECEPTOR EEK, STRUCTURAL GENOMICS, NPPSFA, *KEYWDS 3 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL *KEYWDS 4 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, *KEYWDS 5 RSGI, SIGNALING PROTEIN *EXPDTA SOLUTION NMR *NUMMDL 20 *AUTHOR X.R.QIN, T.NAGASHIMA, F.HAYASHI, S.YOKOYAMA, RIKEN *AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) *REVDAT 1 12-MAY-09 1X5L 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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