NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
19156 | 2edz | 10267 | cing | 1-original | MR format | comment |
*HEADER SIGNALING PROTEIN 15-FEB-07 2EDZ *TITLE SOLUTION STRUCTURES OF THE PDZ DOMAIN OF MUS MUSCULUS PDZ *TITLE 2 DOMAIN-CONTAINING PROTEIN 1 *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: PDZ DOMAIN-CONTAINING PROTEIN 1; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: PDZ DOMAIN; *COMPND 5 SYNONYM: CFTR-ASSOCIATED PROTEIN OF 70 KDA, NA/PI *COMPND 6 COTRANSPORTER C-TERMINAL-ASSOCIATED PROTEIN, NAPI-CAP1, *COMPND 7 NA+, /H+, EXCHANGER REGULATORY FACTOR 3, SODIUM-HYDROGEN *COMPND 8 EXCHANGER REGULATORY FACTOR 3; *COMPND 9 ENGINEERED: YES *SOURCE MOL_ID: 1; *SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; *SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; *SOURCE 4 ORGANISM_TAXID: 10090; *SOURCE 5 GENE: PDZK1; *SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P060313-12; *SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS *KEYWDS CFTR-ASSOCIATED PROTEIN OF 70 KDA, NA/PI COTRANSPORTER C- *KEYWDS 2 TERMINAL-ASSOCIATED PROTEIN, NAPI-CAP1, NA(+)/H(+) *KEYWDS 3 EXCHANGER REGULATORY FACTOR 3, SODIUM-HYDROGEN EXCHANGER *KEYWDS 4 REGULATORY FACTOR 3, STRUCTURAL GENOMICS, NPPSFA, NATIONAL *KEYWDS 5 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, *KEYWDS 6 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, *KEYWDS 7 SIGNALING PROTEIN *EXPDTA SOLUTION NMR *NUMMDL 20 *AUTHOR M.SATO, S.KOSHIBA, S.WATANABE, T.HARADA, T.KIGAWA, *AUTHOR 2 S.YOKOYAMA, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE *AUTHOR 3 (RSGI) *REVDAT 1 12-MAY-09 2EDZ 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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