NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
13291 | 1uht | 10067 | cing | 1-original | MR format | comment |
*HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 10-JUL-03 1UHT *TITLE SOLUTION STRUCTURE OF THE FHA DOMAIN OF ARABIDOPSIS *TITLE 2 THALIANA HYPOTHETICAL PROTEIN *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: EXPRESSED PROTEIN; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: FORKHEAD ASSOCIATED DOMAIN, FHA DOMAIN; *COMPND 5 SYNONYM: HYPOTHETICAL PROTEIN; *COMPND 6 ENGINEERED: YES *SOURCE MOL_ID: 1; *SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; *SOURCE 3 ORGANISM_COMMON: THALE CRESS; *SOURCE 4 ORGANISM_TAXID: 3702; *SOURCE 5 GENE: RIKEN CDNA RAFL09-79-A12; *SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021218-71; *SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS *KEYWDS FHA DOMAIN, BETA-SANDWICH, ANTIPARALLEL BETA-SHEETS, *KEYWDS 2 PHOSPHOPEPTIDE BINDING MOTIF, STRUCTURAL GENOMICS, RIKEN *KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN *KEYWDS 4 FUNCTION *EXPDTA SOLUTION NMR *NUMMDL 20 *AUTHOR T.TOMIZAWA, M.INOUE, S.KOSHIBA, F.HAYASHI, M.SHIROUZU, *AUTHOR 2 T.TERADA, T.YABUKI, M.AOKI, T.MATSUDA, E.SEKI, H.HIROTA, *AUTHOR 3 M.YOSHIDA, A.TANAKA, T.OSANAI, K.SHINOZAKI, M.SEKI, *AUTHOR 4 T.KIGAWA, S.YOKOYAMA, RIKEN STRUCTURAL GENOMICS/PROTEOMICS *AUTHOR 5 INITIATIVE (RSGI) *REVDAT 1 12-MAY-09 1UHT 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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