NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | cing | stage | program | type |
504311 | 2ebt | cing | 1-original | MR format | comment |
*HEADER TRANSCRIPTION 09-FEB-07 2EBT *TITLE SOLUTION STRUCTURE OF THREE TANDEM REPEATS OF ZF-C2H2 *TITLE 2 DOMAINS FROM HUMAN KRUPPEL-LIKE FACTOR 5 *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: KRUEPPEL-LIKE FACTOR 5; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: ZF-C2H2; *COMPND 5 SYNONYM: INTESTINAL-ENRICHED KRUEPPEL-LIKE FACTOR, COLON *COMPND 6 KRUEPPEL-LIKE FACTOR, TRANSCRIPTION FACTOR BTEB2, BASIC *COMPND 7 TRANSCRIPTION ELEMENT-BINDING PROTEIN 2, BTE-BINDING *COMPND 8 PROTEIN 2, GC BOX-BINDING PROTEIN 2; *COMPND 9 ENGINEERED: YES *SOURCE MOL_ID: 1; *SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; *SOURCE 3 ORGANISM_COMMON: HUMAN; *SOURCE 4 ORGANISM_TAXID: 9606; *SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P060116-02; *SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS *KEYWDS C2H2-TYPE ZINC-FINGER, METAL BIND, TRANSCRIPTION FACTOR, *KEYWDS 2 KRUPPEL-LIKE FACTOR, GC-BOX PROMOTER ELEMENTS, STRUCTURAL *KEYWDS 3 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL *KEYWDS 4 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL *KEYWDS 5 GENOMICS/PROTEOMICS INITIATIVE, RSGI *EXPDTA SOLUTION NMR *NUMMDL 20 *AUTHOR T.NAGASHIMA, F.HAYASHI, S.YOKOYAMA, RIKEN STRUCTURAL *AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) *REVDAT 1 12-MAY-09 2EBT 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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