HEADER CALCIUM-BINDING PROTEIN 24-APR-96 1DMO TITLE CALMODULIN, NMR, 30 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALMODULIN; COMPND 3 CHAIN: NULL; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS; SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 4 EXPRESSION_SYSTEM_PLASMID: PAS; SOURCE 5 EXPRESSION_SYSTEM_GENE: XENOPUS LAEVIS KEYWDS CALCIUM-INDUCED CONFORMATIONAL CHANGE, CALCIUM-BINDING KEYWDS 2 PROTEIN EXPDTA NMR, 30 STRUCTURES AUTHOR M.ZHANG,T.TANAKA,M.IKURA REVDAT 1 01-AUG-96 1DMO 0 JRNL AUTH M.ZHANG,T.TANAKA,M.IKURA JRNL TITL CALCIUM-INDUCED CONFORMATIONAL TRANSITION REVEALED JRNL TITL 2 BY THE SOLUTION STRUCTURE OF APO CALMODULIN JRNL REF NAT.STRUCT.BIOL. V. 2 758 1995 JRNL REFN ASTM NSBIEW US ISSN 1072-8368 2024 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.0 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 PAIRWISE RMSD (ROOT-MEAN-SQUARE DEVIATION) OF 0.45 REMARK 3 (BACKBONE) AND 1.06 (HEAVY ATOMS) ANGSTROMS FOR THE REMARK 3 N-TERMINAL DOMAIN OF THE PROTEIN. RMSD VALUES OF THE REMARK 3 C-TERMINAL DOMAIN ARE 0.49 AND 1.22 ANGSTROMS FOR REMARK 3 BACKBONE AND HEAVY ATOMS, RESPECTIVELY. REMARK 4 REMARK 4 1DMO COMPLIES WITH FORMAT V. 2.0, 16-FEB-1996 REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 REMARK: NULL REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE DEPOSITORS STATE THAT THERE IS A DIFFERENCE BETWEEN THE REMARK 999 SEQUENCE OF HUMAN CALMODULIN AND XENOPIS LAEVIS REMARK 999 CALMODULIN. SWISSPROT HAS ONE ENTRY FOR BOTH SPECIES. DBREF 1DMO 1 148 SWS P02593 CALM_HUMAN 1 148 SEQADV 1DMO ASN 129 SWS P02593 ASP 129 CONFLICT SEQRES 1 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS SEQRES 2 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR SEQRES 3 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU SEQRES 4 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE SEQRES 5 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE SEQRES 6 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP SEQRES 7 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL SEQRES 8 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU SEQRES 9 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR SEQRES 10 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASN ILE SEQRES 11 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN SEQRES 12 148 MET MET THR ALA LYS HELIX 1 1 GLU 6 LEU 18 1 13 HELIX 2 2 THR 29 LEU 39 1 11 HELIX 3 3 GLU 45 VAL 55 1 11 HELIX 4 4 PHE 65 MET 76 1 12 HELIX 5 5 GLU 82 ARG 90 1 9 HELIX 6 6 ALA 102 LEU 112 1 11 HELIX 7 7 ASP 118 GLU 127 1 10 HELIX 8 8 TYR 138 GLN 143 1 6 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 MODEL 1 (ATOM LINES ARE NOT SHOWN.) END