NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
18449 | 2dml | 11100 | cing | 1-original | MR format | comment |
*HEADER ISOMERASE 22-APR-06 2DML *TITLE THE SOLUTION STRUCTURE OF THE FIRST THIOREDOXIN DOMAIN OF *TITLE 2 MOUSE PROTEIN DISULFIDE-ISOMERASE A6 *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: PROTEIN DISULFIDE-ISOMERASE A6; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: 1ST THIOREDOXIN DOMAIN; *COMPND 5 SYNONYM: THIOREDOXIN DOMAIN-CONTAINING PROTEIN 7; *COMPND 6 EC: 5.3.4.1; *COMPND 7 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: PDIA6; *SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS; *SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050509-11; *SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS *KEYWDS THIOREDOXIN DOMAIN-CONTAINING PROTEIN 7, ENDOPLASMIC *KEYWDS 2 RETICULUM, ISOMERASE, REDOX-ACTIVE CENTER, 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 N.TOCHIO, S.KOSHIBA, M.INOUE, T.KIGAWA, S.YOKOYAMA, RIKEN *AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) *REVDAT 1 12-MAY-09 2DML 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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