HEADER CALCIUM-BINDING PROTEIN 07-JUN-93 1DEG 1DEG 2 COMPND CALMODULIN MUTANT WITH GLU 84 DELETED (DEL E84) 1DEG 3 SOURCE BOVINE (BOS TAURUS) BRAIN RECOMBINANT FORM EXPRESSED IN 1DEG 4 SOURCE 2 (ESCHERICHIA COLI) 1DEG 5 AUTHOR S.RAGHUNATHAN,R.CHANDROSS,B.P.CHENG,A.PERSECHINI, 1DEG 6 AUTHOR 2 S.E.SOBOTTK,R.H.KRETSINGER 1DEG 7 REVDAT 1 31-MAY-94 1DEG 0 1DEG 8 JRNL AUTH R.H.KRETSINGER,S.RAGHUNATHAN,R.J.CHANDROSS, 1DEG 9 JRNL AUTH 2 A.PERSECHINI 1DEG 10 JRNL TITL THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS 1DEG 11 JRNL TITL 2 SEEN IN THE CRYSTAL STRUCTURE 1DEG 12 JRNL REF BIOPHYS.J. V. 61 403 1992 1DEG 13 JRNL REFN ASTM BIOJAU US ISSN 0006-3495 0030 1DEG 14 REMARK 1 1DEG 15 REMARK 1 REFERENCE 1 1DEG 16 REMARK 1 AUTH M.KATAOKA,J.F.HEAD,A.PERSECHINI,R.H.KRETSINGER, 1DEG 17 REMARK 1 AUTH 2 D.M.ENGELMAN 1DEG 18 REMARK 1 TITL SMALL-ANGLE X-RAY SCATTERING STUDIES OF 1DEG 19 REMARK 1 TITL 2 CALMODULIN MUTANTS WITH DELETIONS IN THE LINKER 1DEG 20 REMARK 1 TITL 3 REGION OF THE CENTRAL HELIX INDICATE THAT THE 1DEG 21 REMARK 1 TITL 4 LINKER REGION RETAINS A PREDOMINANTLY A-HELICAL 1DEG 22 REMARK 1 TITL 5 CONFORMATION 1DEG 23 REMARK 1 REF BIOCHEMISTRY V. 30 1188 1991 1DEG 24 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1DEG 25 REMARK 1 REFERENCE 2 1DEG 26 REMARK 1 AUTH A.PERSECHINI,R.H.KRETSINGER,T.N.DAVIS 1DEG 27 REMARK 1 TITL CALMODULINS WITH DELETIONS IN THE CENTRAL HELIX 1DEG 28 REMARK 1 TITL 2 FUNCTIONALLY REPLACE THE NATIVE PROTEIN IN YEAST 1DEG 29 REMARK 1 TITL 3 CELLS 1DEG 30 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 88 449 1991 1DEG 31 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 0040 1DEG 32 REMARK 1 REFERENCE 3 1DEG 33 REMARK 1 AUTH A.PERSECHINI,D.K.BLUMENTHAL,H.W.JARRETT,C.B.KLEE, 1DEG 34 REMARK 1 AUTH 2 D.O.HARDY,R.H.KRETSINGER 1DEG 35 REMARK 1 TITL THE EFFECTS OF DELETIONS IN THE CENTRAL HELIX OF 1DEG 36 REMARK 1 TITL 2 CALMODULIN ON ENZYME ACTIVATION AND PEPTIDE 1DEG 37 REMARK 1 TITL 3 BINDING 1DEG 38 REMARK 1 REF J.BIOL.CHEM. V. 264 8052 1989 1DEG 39 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1DEG 40 REMARK 1 REFERENCE 4 1DEG 41 REMARK 1 AUTH A.PERSECHINI,R.H.KRETSINGER 1DEG 42 REMARK 1 TITL THE CENTRAL HELIX OF CALMODULIN FUNCTIONS AS A 1DEG 43 REMARK 1 TITL 2 FLEXIBLE TETHER 1DEG 44 REMARK 1 REF J.BIOL.CHEM. V. 263 12175 1988 1DEG 45 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1DEG 46 REMARK 1 REFERENCE 5 1DEG 47 REMARK 1 AUTH A.PERSECHINI,R.H.KRETSINGER 1DEG 48 REMARK 1 TITL TOWARD A MODEL OF THE CALMODULIN-MYOSIN LIGHT 1DEG 49 REMARK 1 TITL 2 CHAIN KINASE COMPLEX: IMPLICATIONS OF CALMODULIN 1DEG 50 REMARK 1 TITL 3 FUNCTION 1DEG 51 REMARK 1 REF J.CARDIOVASC.PHARMACOL., V. 12 1 1988 1DEG 52 REMARK 1 REF 2 SUPPL.5 1DEG 53 REMARK 1 REFN ASTM JCPCDT US ISSN 0160-2446 0764 1DEG 54 REMARK 2 1DEG 55 REMARK 2 RESOLUTION. 2.9 ANGSTROMS. 1DEG 56 REMARK 3 1DEG 57 REMARK 3 REFINEMENT. 1DEG 58 REMARK 3 PROGRAM X-PLOR 1DEG 59 REMARK 3 AUTHORS BRUNGER 1DEG 60 REMARK 3 R VALUE 0.23 1DEG 61 REMARK 3 RMSD BOND DISTANCES 0.03 ANGSTROMS 1DEG 62 REMARK 3 RMSD BOND ANGLES 5.49 DEGREES 1DEG 63 REMARK 4 1DEG 64 REMARK 4 HELIX RECORDS: AT THE PRESENT LEVEL OF STRUCTURE 1DEG 65 REMARK 4 DETERMINATION THESE STRETCHES OF RESIDUES ARE CLASSIFIED 1DEG 66 REMARK 4 AS POSSIBLE ALPHA HELICES. 1DEG 67 REMARK 5 1DEG 68 REMARK 5 THERE IS AN APPROXIMATE NON-CRYSTALLOGRAPHIC TWO-FOLD AXIS 1DEG 69 REMARK 5 ROUGHLY PARALLEL TO B, RELATING DOMAIN I, (RESIDUES 12 - 1DEG 70 REMARK 5 74) AND DOMAIN II (RESIDUES 85 - 147). THE TRANSFORMATION 1DEG 71 REMARK 5 PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE 1DEG 72 REMARK 5 COORDINATES FOR DOMAIN I WHEN APPLIED TO DOMAIN II. 1DEG 73 REMARK 6 1DEG 74 REMARK 6 THERE IS A BEND OF 40 DEGREES BETWEEN THE F2 HELIX RESIDUES 1DEG 75 REMARK 6 66 - 76, AND THE LINKER 77 - 83. THE ANGLE BETWEEN THE 1DEG 76 REMARK 6 LINKER AND THE E3 HELIX, 85 - 92, IS 85 DEGREES. 1DEG 77 REMARK 7 1DEG 78 REMARK 7 SEQUENCE ADVISORY NOTICE 1DEG 79 REMARK 7 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1DEG 80 REMARK 7 1DEG 81 REMARK 7 SWISS-PROT ENTRY NAME: CALM_HUMAN 1DEG 82 REMARK 7 1DEG 83 REMARK 7 SWISS-PROT RESIDUE PDB SEQRES 1DEG 84 REMARK 7 1DEG 85 REMARK 7 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1DEG 86 REMARK 7 ASP 129 ASN 129 1DEG 87 SEQRES 1 142 THR GLU GLU GLN ILE ALA GLU PHE LYS GLU ALA PHE SER 1DEG 88 SEQRES 2 142 LEU PHE ASP LYS ASP GLY ASP GLY THR ILE THR THR LYS 1DEG 89 SEQRES 3 142 GLU LEU GLY THR VAL MET ARG SER LEU GLY GLN ASN PRO 1DEG 90 SEQRES 4 142 THR GLU ALA GLU LEU GLN ASP MET ILE ASN GLU VAL ASP 1DEG 91 SEQRES 5 142 ALA ASP GLY ASN GLY THR ILE ASP PHE PRO GLU PHE LEU 1DEG 92 SEQRES 6 142 THR MET MET ALA ARG LYS MET LYS ASP THR ASP SER GLU 1DEG 93 SEQRES 7 142 GLU ILE ARG GLU ALA PHE ARG VAL PHE ASP LYS ASP GLY 1DEG 94 SEQRES 8 142 ASN GLY TYR ILE SER ALA ALA GLU LEU ARG HIS VAL MET 1DEG 95 SEQRES 9 142 THR ASN LEU GLY GLU LYS LEU THR ASP GLU GLU VAL ASP 1DEG 96 SEQRES 10 142 GLU MET ILE ARG GLU ALA ASN ILE ASP GLY ASP GLY GLN 1DEG 97 SEQRES 11 142 VAL ASN TYR GLU GLU PHE VAL GLN MET MET THR ALA 1DEG 98 HET CA 1 1 CALCIUM +2 COUNTER ION 1DEG 99 HET CA 2 1 CALCIUM +2 COUNTER ION 1DEG 100 HET CA 3 1 CALCIUM +2 COUNTER ION 1DEG 101 HET CA 4 1 CALCIUM +2 COUNTER ION 1DEG 102 FORMUL 2 CA 4(CA1 ++ ) 1DEG 103 HELIX 1 H1 THR 5 PHE 19 1 1DEG 104 HELIX 2 H2 THR 29 SER 38 1 1DEG 105 HELIX 3 H3 GLU 45 VAL 55 1 1DEG 106 HELIX 4 H4 PHE 65 ASP 80 1 1DEG 107 HELIX 5 H5 ARG 86 PHE 92 1 1DEG 108 HELIX 6 H6 ALA 102 ASN 111 1 1DEG 109 HELIX 7 H7 ASP 118 ALA 128 1 1DEG 110 HELIX 8 H8 TYR 138 ALA 147 1 1DEG 111 SHEET 1 BET 2 THR 26 THR 28 0 1DEG 112 SHEET 2 BET 2 THR 62 ASP 64 -1 1DEG 113 SHEET 1 BT2 2 TYR 99 SER 101 0 1DEG 114 SHEET 2 BT2 2 GLN 135 ASN 137 -1 1DEG 115 SITE 1 EF1 12 ASP 20 LYS 21 ASP 22 GLY 23 1DEG 116 SITE 2 EF1 12 ASP 24 GLY 25 THR 26 ILE 27 1DEG 117 SITE 3 EF1 12 THR 28 THR 29 LYS 30 GLU 31 1DEG 118 SITE 1 EF2 12 ASP 56 ALA 57 ASP 58 GLY 59 1DEG 119 SITE 2 EF2 12 ASN 60 GLY 61 THR 62 ILE 63 1DEG 120 SITE 3 EF2 12 ASP 64 PHE 65 PRO 66 GLU 67 1DEG 121 SITE 1 EF3 12 ASP 93 LYS 94 ASP 95 GLY 96 1DEG 122 SITE 2 EF3 12 ASN 97 GLY 98 TYR 99 ILE 100 1DEG 123 SITE 3 EF3 12 SER 101 ALA 102 ALA 103 GLU 104 1DEG 124 SITE 1 EF4 12 ASN 129 ILE 130 ASP 131 GLY 132 1DEG 125 SITE 2 EF4 12 ASP 133 GLY 134 GLN 135 VAL 136 1DEG 126 SITE 3 EF4 12 ASN 137 TYR 138 GLU 139 GLU 140 1DEG 127 CRYST1 45.300 49.900 62.400 90.00 90.00 90.00 P 21 21 21 4 1DEG 128 ORIGX1 1.000000 0.000000 0.000000 0.00000 1DEG 129 ORIGX2 0.000000 1.000000 0.000000 0.00000 1DEG 130 ORIGX3 0.000000 0.000000 1.000000 0.00000 1DEG 131 SCALE1 0.022075 0.000000 0.000000 0.00000 1DEG 132 SCALE2 0.000000 0.020040 0.000000 0.00000 1DEG 133 SCALE3 0.000000 0.000000 0.016026 0.00000 1DEG 134 MTRIX1 1 -0.990874 0.076905 0.110695 109.81735 1 1DEG 135 MTRIX2 1 0.098889 0.972835 0.209316 -8.59274 1 1DEG 136 MTRIX3 1 -0.091590 0.218352 -0.971562 -30.20036 1 1DEG 137 (ATOM LINES ARE NOT SHOWN.) 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