HEADER TRANSFERASE(PHOSPHOTRANSFERASE) 18-JAN-93 1APM 1APM 2 COMPND $C-/AMP$-DEPENDENT PROTEIN KINASE (E.C.2.7.1.37) ($C/APK$) 1APM 3 COMPND 2 (CATALYTIC SUBUNIT) "ALPHA" ISOENZYME MUTANT WITH SER 139 1APM 4 COMPND 3 REPLACED BY ALA (/S139A$) COMPLEX WITH THE PEPTIDE 1APM 5 COMPND 4 INHIBITOR PKI(5-24) AND THE DETERGENT MEGA-8 1APM 6 SOURCE RECOMBINANT MOUSE (MUS $MUSCULUS) "ALPHA" ISOENZYME 1APM 7 SOURCE 2 S139A MUTANT EXPRESSED IN (ESCHERICHIA $COLI) 1APM 8 AUTHOR D.R.KNIGHTON,S.M.BELL,J.ZHENG,L.F.TEN *EYCK,N.-H.XUONG, 1APM 9 AUTHOR 2 S.S.TAYLOR,J.M.SOWADSKI 1APM 10 REVDAT 1 15-APR-93 1APM 0 1APM 11 JRNL AUTH D.R.KNIGHTON,S.M.BELL,J.ZHENG,L.F.TEN *EYCK, 1APM 12 JRNL AUTH 2 N.-H.XUONG,S.S.TAYLOR,J.M.SOWADSKI 1APM 13 JRNL TITL 2.0 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE 1APM 14 JRNL TITL 2 CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN 1APM 15 JRNL TITL 3 KINASE COMPLEXED WITH A PEPTIDE INHIBITOR AND 1APM 16 JRNL TITL 4 DETERGENT 1APM 17 JRNL REF TO BE PUBLISHED 1APM 18 JRNL REFN ASTM 353 1APM 19 REMARK 1 1APM 20 REMARK 1 REFERENCE 1 1APM 21 REMARK 1 AUTH J.ZHENG,D.R.KNIGHTON,L.F.TEN *EYCK,R.KARLSSON, 1APM 22 REMARK 1 AUTH 2 N.-H.XUONG,S.S.TAYLOR,J.M.SOWADSKI 1APM 23 REMARK 1 TITL CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF 1APM 24 REMARK 1 TITL 2 $C-/AMP$-*DEPENDENT PROTEIN KINASE COMPLEXED WITH 1APM 25 REMARK 1 TITL 3 MG/ATP$ AND PEPTIDE INHIBITOR 1APM 26 REMARK 1 REF BIOCHEMISTRY V. 32 2154 1993 1APM 27 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 1APM 28 REMARK 1 REFERENCE 2 1APM 29 REMARK 1 AUTH D.R.KNIGHTON,J.ZHENG,L.F.TEN *EYCK,V.A.ASHFORD 1APM 30 REMARK 1 AUTH 2 N.-H.XUONG,S.S.TAYLOR,J.M.SOWADSKI 1APM 31 REMARK 1 TITL CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF 1APM 32 REMARK 1 TITL 2 CYCLIC ADENOSINE MONOPHOSPHATE-*DEPENDENT PROTEIN 1APM 33 REMARK 1 TITL 3 KINASE 1APM 34 REMARK 1 REF SCIENCE V. 253 407 1991 1APM 35 REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 038 1APM 36 REMARK 1 REFERENCE 3 1APM 37 REMARK 1 AUTH D.R.KNIGHTON,J.ZHENG,L.F.TEN *EYCK,N.-H.XUONG, 1APM 38 REMARK 1 AUTH 2 S.S.TAYLOR,J.M.SOWADSKI 1APM 39 REMARK 1 TITL STRUCTURE OF A PEPTIDE INHIBITOR BOUND TO THE 1APM 40 REMARK 1 TITL 2 CATALYTIC SUBUNIT OF CYCLIC ADENOSINE 1APM 41 REMARK 1 TITL 3 MONOPHOSPHATE-*DEPENDENT PROTEIN KINASE 1APM 42 REMARK 1 REF SCIENCE V. 253 414 1991 1APM 43 REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 038 1APM 44 REMARK 1 REFERENCE 4 1APM 45 REMARK 1 AUTH L.W.SLICE,S.S.TAYLOR 1APM 46 REMARK 1 TITL EXPRESSION OF THE CATALYTIC SUBUNIT OF 1APM 47 REMARK 1 TITL 2 $C/AMP$-DEPENDENT PROTEIN KINASE IN ESCHERICHIA 1APM 48 REMARK 1 TITL 3 $COLI 1APM 49 REMARK 1 REF J.BIOL.CHEM. V. 264 20940 1989 1APM 50 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1APM 51 REMARK 2 1APM 52 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 1APM 53 REMARK 3 1APM 54 REMARK 3 REFINEMENT. 1APM 55 REMARK 3 PROGRAM XPLOR/TNT 1APM 56 REMARK 3 AUTHORS BRUNGER/TRONRUD 1APM 57 REMARK 3 R VALUE 0.186 1APM 58 REMARK 3 RMSD BOND DISTANCES 0.013 ANGSTROMS 1APM 59 REMARK 3 RMSD BOND ANGLES 2.3 DEGREES 1APM 60 REMARK 3 1APM 61 REMARK 3 RESOLUTION RANGE 30 - 1.95 ANGSTROMS 1APM 62 REMARK 3 DATA CUTOFF 0.0 SIGMA(F) 1APM 63 REMARK 4 1APM 64 REMARK 4 SECONDARY STRUCTURE ASSIGNMENTS IN THIS ENTRY WERE DONE BY 1APM 65 REMARK 4 THE USE OF PROGRAM *DSSP* OF W.KABSCH AND C.SANDER. THESE 1APM 66 REMARK 4 ASSIGNMENTS DIFFER IN SOME CASES FROM THOSE REPORTED IN THE 1APM 67 REMARK 4 PAPERS CITED AS REFERENCES 2 AND 3 ABOVE, WHICH WERE 1APM 68 REMARK 4 DERIVED FROM VISUAL INSPECTION. 1APM 69 REMARK 5 1APM 70 REMARK 5 INHIBITOR RESIDUE NUMBERING CORRESPONDS TO NUMBERS FROM 1APM 71 REMARK 5 THE SEQUENCE OF THE LARGER NATURALLY OCCURRING PKI PROTEIN 1APM 72 REMARK 5 OF WHICH THE INHIBITOR IS A SYNTHETIC FRAGMENT. 1APM 73 REMARK 6 1APM 74 REMARK 6 RESIDUES SER E 10, THR E 197, AND SER E 338 ARE 1APM 75 REMARK 6 PHOSPHORYLATED. THE PHOSPHATE GROUPS ARE PRESENTED ON 1APM 76 REMARK 6 *HETATM* RECORDS AT THE END OF THE CHAIN. 1APM 77 REMARK 7 1APM 78 REMARK 7 THE MODEL HAS AN N-OCTANE RESIDUE (OCT) THAT IS USED TO 1APM 79 REMARK 7 MODEL THE THE ORDERED PART OF A MEGA-8 (OCTANOYL-N- 1APM 80 REMARK 7 METHYLGLUCAMIDE) DETERGENT MOLECULE OBSERVED NEAR THE 1APM 81 REMARK 7 N-TERMINAL HELIX. 1APM 82 REMARK 8 1APM 83 REMARK 8 THERE IS NO ELECTRON DENSITY FOR THE 9 N-TERMINAL RESIDUES 1APM 84 REMARK 8 OF THE CATALYTIC SUBUNIT, WHICH ARE PRESUMED DISORDERED. 1APM 85 REMARK 9 1APM 86 REMARK 9 RESIDUES E 51-E 55, E 319-E 322, AND I 23-I 24 HAVE WEAK 1APM 87 REMARK 9 BACKBONE ELECTRON DENSITY. 1APM 88 REMARK 10 1APM 89 REMARK 10 SOME SIDE CHAINS HAVE BEEN TRUNCATED DUE TO LACK OF 1APM 90 REMARK 10 SUPPORTING ELECTRON DENSITY (THUS NO COORDINATES SUPPLIED). 1APM 91 REMARK 11 1APM 92 REMARK 11 ELECTRON DENSITY DOES NOT STRONGLY SUPPORT A SINGLE 1APM 93 REMARK 11 CONFORMATION FOR SIDE CHAINS OF THE FOLLOWING, ALTHOUGH 1APM 94 REMARK 11 ATTEMPTED BEST POSITIONS ARE INCLUDED IN THESE COORDINATES: 1APM 95 REMARK 11 SER E 10, GLU E 11, ASP E 276, ARG E 336, HIS I 23, AND 1APM 96 REMARK 11 ASP I 24. 1APM 97 SEQRES 1 E 350 GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU 1APM 98 SEQRES 2 E 350 SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE 1APM 99 SEQRES 3 E 350 LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN 1APM 100 SEQRES 4 E 350 LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY 1APM 101 SEQRES 5 E 350 SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER 1APM 102 SEQRES 6 E 350 GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS 1APM 103 SEQRES 7 E 350 VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU 1APM 104 SEQRES 8 E 350 LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL 1APM 105 SEQRES 9 E 350 LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR 1APM 106 SEQRES 10 E 350 MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER 1APM 107 SEQRES 11 E 350 HIS LEU ARG ARG ILE GLY ARG PHE ALA GLU PRO HIS ALA 1APM 108 SEQRES 12 E 350 ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR 1APM 109 SEQRES 13 E 350 LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO 1APM 110 SEQRES 14 E 350 GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL 1APM 111 SEQRES 15 E 350 THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR 1APM 112 SEQRES 16 E 350 TRP THR LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU 1APM 113 SEQRES 17 E 350 ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP 1APM 114 SEQRES 18 E 350 TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY 1APM 115 SEQRES 19 E 350 TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR 1APM 116 SEQRES 20 E 350 GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS 1APM 117 SEQRES 21 E 350 PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU 1APM 118 SEQRES 22 E 350 GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN 1APM 119 SEQRES 23 E 350 GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR 1APM 120 SEQRES 24 E 350 THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA 1APM 121 SEQRES 25 E 350 PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER 1APM 122 SEQRES 26 E 350 ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SER 1APM 123 SEQRES 27 E 350 ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE 1APM 124 SEQRES 1 I 20 THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY 1APM 125 SEQRES 2 I 20 ARG ARG ASN ALA ILE HIS ASP 1APM 126 FTNOTE 1 1APM 127 FTNOTE 1 RESIDUES SER E 10, THR E 197, AND SER E 338 ARE 1APM 128 FTNOTE 1 PHOSPHORYLATED. 1APM 129 FTNOTE 2 1APM 130 FTNOTE 2 ARG E 56 AND ARG I 18 HAVE TWO MODELED SIDE-CHAIN 1APM 131 FTNOTE 2 CONFORMATIONS. 1APM 132 HET PHO E 10 4 PHOSPHATE GROUP BONDED TO SER E 10 1APM 133 HET PHO E 197 4 PHOSPHATE GROUP BONDED TO THR E 197 1APM 134 HET PHO E 338 4 PHOSPHATE GROUP BONDED TO SER E 338 1APM 135 HET OCT D 1 8 N-OCTANE MODEL OF MEGA-8 DETERGENT 1APM 136 FORMUL 3 PHO 3(O3 P1 --) 1APM 137 FORMUL 4 OCT C8 H18 1APM 138 FORMUL 5 HOH *207(H2 O1) 1APM 139 HELIX 1 A GLU E 11 GLU E 31 1 1APM 140 HELIX 2 AB LEU E 40 GLN E 42 5 NOT NOTED IN REF 2 1APM 141 HELIX 3 B LYS E 76 LYS E 81 1 1APM 142 HELIX 4 C ILE E 85 ALA E 97 1 1APM 143 HELIX 5 D MET E 128 ILE E 135 1 1APM 144 HELIX 6 E GLU E 140 SER E 159 1 1APM 145 HELIX 7 EF0 PRO E 169 ASN E 171 5 NOT NOTED IN REF 2 1APM 146 HELIX 8 EF1 PRO E 202 TYR E 204 5 NOT NOTED IN REF 2 1APM 147 HELIX 9 EF2 PRO E 207 ILE E 210 1 NOT NOTED IN REF 2 1APM 148 HELIX 10 F ALA E 218 ALA E 233 1 1APM 149 HELIX 11 G PRO E 243 SER E 252 1 1APM 150 HELIX 12 H SER E 263 LEU E 272 1 1APM 151 HELIX 13 I ASN E 289 LYS E 292 1 1APM 152 HELIX 14 IJ LYS E 295 PHE E 297 5 NOT NOTED IN REF 2 1APM 153 HELIX 15 J TRP E 302 GLN E 307 1 1APM 154 HELIX 16 IA THR I 6 ALA I 12 1 INHIBITOR N-TERMINAL HELIX 1APM 155 SHEET 1 A 5 PHE E 43 THR E 51 0 1APM 156 SHEET 2 A 5 GLY E 55 HIS E 62 -1 1APM 157 SHEET 3 A 5 HIS E 68 ASP E 75 -1 1APM 158 SHEET 4 A 5 ASN E 115 GLU E 121 -1 1APM 159 SHEET 5 A 5 LEU E 106 LYS E 111 -1 1APM 160 SHEET 1 B 2 LEU E 162 ILE E 163 0 1APM 161 SHEET 2 B 2 LEU E 172 ILE E 174 -1 1APM 162 SHEET 1 C 2 ILE E 180 VAL E 182 0 1APM 163 SHEET 2 C 2 LYS E 189 ARG E 190 -1 1APM 164 CRYST1 73.840 75.760 81.010 90.00 90.00 90.00 P 21 21 21 4 1APM 165 ORIGX1 1.000000 0.000000 0.000000 0.00000 1APM 166 ORIGX2 0.000000 1.000000 0.000000 0.00000 1APM 167 ORIGX3 0.000000 0.000000 1.000000 0.00000 1APM 168 SCALE1 0.013543 0.000000 0.000000 0.00000 1APM 169 SCALE2 0.000000 0.013200 0.000000 0.00000 1APM 170 SCALE3 0.000000 0.000000 0.012344 0.00000 1APM 171