NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
17816 | 2d7l | 11134 | cing | 1-original | MR format | comment |
*HEADER GENE REGULATION, DNA BINDING PROTEIN 24-NOV-05 2D7L *TITLE SOLUTION STRUCTURE OF THE HMG BOX DOMAIN FROM HUMAN WD *TITLE 2 REPEAT AND HMG-BOX DNA BINDING PROTEIN 1 *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: WD REPEAT AND HMG-BOX DNA BINDING PROTEIN 1; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: HMG BOX DOMAIN; *COMPND 5 SYNONYM: ACIDIC NUCLEOPLASMIC DNA- BINDING PROTEIN 1, AND- *COMPND 6 1; *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: WDHD1; *SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050111-08; *SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS *KEYWDS HIGH MOBILITY GROUP BOX DOMAIN, HELIX-TURN-HELIX, DNA *KEYWDS 2 BINDING, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON *KEYWDS 3 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN *KEYWDS 4 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, GENE *KEYWDS 5 REGULATION, DNA BINDING PROTEIN *EXPDTA SOLUTION NMR *NUMMDL 20 *AUTHOR T.TOMIZAWA, T.KIGAWA, K.SAITO, S.KOSHIBA, M.INOUE, *AUTHOR 2 Y.O.KAMATARI, S.YOKOYAMA, RIKEN STRUCTURAL *AUTHOR 3 GENOMICS/PROTEOMICS INITIATIVE (RSGI) *REVDAT 1 12-MAY-09 2D7L 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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