NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
17394 | 2com | 10011 | cing | 1-original | MR format | comment |
*HEADER OXIDOREDUCTASE 18-MAY-05 2COM *TITLE THE SOLUTION STRUCTURE OF THE SWIRM DOMAIN OF HUMAN LSD1 *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: LYSINE-SPECIFIC HISTONE DEMETHYLASE 1; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: SWIRM DOMAIN; *COMPND 5 SYNONYM: AMINE OXIDASE FLAVIN CONTAINING DOMAIN PROTEIN 2, *COMPND 6 AOF2 PROTEIN, BRAF35-HDAC COMPLEX PROTEIN BHC110; *COMPND 7 EC: 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: LSD1; *SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040401-21; *SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS *KEYWDS SWIRM DOMAIN, LSD1, AOF2, KIAA0601, HISTONE MODULATION, *KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN *KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL *KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, OXIDOREDUCTASE *EXPDTA SOLUTION NMR *NUMMDL 20 *AUTHOR N.TOCHIO, T.UMEHARA, S.KOSHIBA, M.INOUE, A.TANAKA, T.KIGAWA, *AUTHOR 2 S.YOKOYAMA, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE *AUTHOR 3 (RSGI) *REVDAT 1 12-MAY-09 2COM 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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