NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
14826 | 1x5c | 11114 | cing | 1-original | MR format | comment |
*HEADER ISOMERASE 15-MAY-05 1X5C *TITLE THE SOLUTION STRUCTURE OF THE SECOND THIOREDOXIN-LIKE *TITLE 2 DOMAIN OF HUMAN PROTEIN DISULFIDE-ISOMERASE *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: PROTEIN DISULFIDE-ISOMERASE; *COMPND 3 CHAIN: A; *COMPND 4 FRAGMENT: THIOREDOXIN LIKE DOMAIN; *COMPND 5 SYNONYM: PDI, PROLYL 4- HYDROXYLASE BETA SUBUNIT, CELLULAR *COMPND 6 THYROID HORMONE BINDING PROTEIN, P55; *COMPND 7 EC: 5.3.4.1; *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: P4HB; *SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; *SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040628-09; *SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS *KEYWDS DSI, ERBA2L, GIT, PDI, PDIA1, PO4DB, PO4HB, PROHB, *KEYWDS 2 THIOREDOXIN LIKE DOMAIN, REDOX, STRUCTURAL GENOMICS, NPPSFA, *KEYWDS 3 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL *KEYWDS 4 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, *KEYWDS 5 RSGI, ISOMERASE *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 1X5C 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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