NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | bmrb_id | cing | stage | program | type |
18082 | 2def | 4089 | cing | 1-original | MR format | comment |
*HEADER HYDROLASE 15-DEC-97 2DEF *TITLE PEPTIDE DEFORMYLASE CATALYTIC CORE (RESIDUES 1 - 147), NMR, *TITLE 2 20 STRUCTURES *COMPND MOL_ID: 1; *COMPND 2 MOLECULE: PEPTIDE DEFORMYLASE; *COMPND 3 CHAIN: NULL; *COMPND 4 FRAGMENT: ACTIVE CATALYTIC CORE, RESIDUES 1 - 147; *COMPND 5 EC: 3.5.1.31; *COMPND 6 ENGINEERED: YES; *COMPND 7 MUTATION: S1A; *COMPND 8 BIOLOGICAL_UNIT: MONOMER; *COMPND 9 OTHER_DETAILS: ACTIVE FORM CONTAINING ONE NICKEL ION IN THE *COMPND 10 METAL BINDING SITE *SOURCE MOL_ID: 1; *SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; *SOURCE 3 STRAIN: PAL421TR; *SOURCE 4 PLASMID: PTDEF-DELTA; *SOURCE 5 GENE: FMS (CODONS 1-147); *SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; *SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PUC18 *SOURCE 8 (IPTG-INDUCIBLE LAC PROMOTOR), PDEF-EC1-147; *SOURCE 9 EXPRESSION_SYSTEM_GENE: FMS (CODONS 1-147) *KEYWDS HYDROLASE, HYDROLASE, METALLOPROTEASE *EXPDTA NMR, 20 STRUCTURES *AUTHOR T.MEINNEL,F.DARDEL *REVDAT 1 18-MAR-98 2DEF 0 !Derniere modif le 18/11/97 !set message=off echo=off end !Fichier NOEs deformylase
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