NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | cing | stage | program | type |
505368 | 2yqp | cing | 1-original | MR format | comment |
*HEADER GENE REGULATION, HYDROLASE 30-MAR-07 2YQP *TITLE SOLUTION STRUCTURE OF THE ZF-HIT DOMAIN IN DEAD (ASP-GLU- *TITLE 2 ALA-ASP) BOX POLYPEPTIDE 59 *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: PROBABLE ATP-DEPENDENT RNA HELICASE DDX59; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: ZF-HIT DOMAIN; *COMPND 5 SYNONYM: DEAD BOX PROTEIN 59, ZINC FINGER HIT DOMAIN- *COMPND 6 CONTAINING PROTEIN 5; *COMPND 7 EC: 3.6.1.-; *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: RP11-92G12.2; *SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P060925-04; *SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS *KEYWDS NMR, STRUCTURE GENOMICS, ZF-HIT DOMAIN, DEAD BOX *KEYWDS 2 POLYPEPTIDE 59 ISOFORM 2, STRUCTURAL GENOMICS, NPPSFA, *KEYWDS 3 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL *KEYWDS 4 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, *KEYWDS 5 RSGI, GENE REGULATION, HYDROLASE *EXPDTA SOLUTION NMR *NUMMDL 20 *AUTHOR F.HE, Y.MUTO, M.INOUE, T.KIGAWA, M.SHIROUZU, T.TARADA, *AUTHOR 2 S.YOKOYAMA, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE *AUTHOR 3 (RSGI) *REVDAT 1 12-MAY-09 2YQP 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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