HEADER TRANSFERASE (ACYLTRANSFERASE) 09-JUL-90 3CLA 3CLA 2 COMPND TYPE /III$ CHLORAMPHENICOL ACETYLTRANSFERASE (/CAT=III=$) 3CLA 3 COMPND 2 (E.C.2.3.1.28) COMPLEX WITH CHLORAMPHENICOL 3CLA 4 SOURCE (ESCHERICHIA $COLI), STRAIN RZ1032 /CAT$ GENE ENGINEERED 3CLA 5 SOURCE 2 FROM PLASMID R387 EXPRESSED IN (ESCHERICHIA $COLI), STRAIN 3CLA 6 SOURCE 3 /JM101$ HARBORING $P/UC18$ 3CLA 7 AUTHOR A.G.W.LESLIE 3CLA 8 REVDAT 2 15-JUL-92 3CLAA 1 FORMUL 3CLAA 1 REVDAT 1 15-OCT-90 3CLA 0 3CLA 9 REMARK 1 3CLA 10 REMARK 1 REFERENCE 1 3CLA 11 REMARK 1 AUTH A.G.W.LESLIE 3CLA 12 REMARK 1 TITL REFINED CRYSTAL STRUCTURE OF TYPE /III$ 3CLA 13 REMARK 1 TITL 2 CHLORAMPHENICOL ACETYLTRANSFERASE AT 1.75 ANGSTROMS 3CLA 14 REMARK 1 TITL 3 RESOLUTION 3CLA 15 REMARK 1 REF J.MOL.BIOL. V. 213 167 1990 3CLA 16 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 3CLA 17 REMARK 1 REFERENCE 2 3CLA 18 REMARK 1 AUTH M.R.GIBBS,P.C.E.MOODY,A.G.W.LESLIE 3CLA 19 REMARK 1 TITL CRYSTAL STRUCTURE OF THE /ASP$-199-/ASN$ MUTANT OF 3CLA 20 REMARK 1 TITL 2 CHLORAMPHENICOL ACETYLTRANSFERASE TO 2.35 3CLA 21 REMARK 1 TITL 3 ANGSTROMS RESOLUTION. STRUCTURAL CONSEQUENCES OF 3CLA 22 REMARK 1 TITL 4 DISRUPTION OF A BURIED SALT-$BRIDGE. 3CLA 23 REMARK 1 REF TO BE PUBLISHED 3CLA 24 REMARK 1 REFN ASTM 353 3CLA 25 REMARK 1 REFERENCE 3 3CLA 26 REMARK 1 AUTH A.LEWENDON,I.A.MURRAY,W.V.SHAW,M.R.GIBBS, 3CLA 27 REMARK 1 AUTH 2 A.G.W.LESLIE 3CLA 28 REMARK 1 TITL EVIDENCE FOR TRANSITION-$STATE STABILIZATION BY 3CLA 29 REMARK 1 TITL 2 SERINE-148 IN THE CATALYTIC MECHANISM OF 3CLA 30 REMARK 1 TITL 3 CHLORAMPHENICOL ACETYLTRANSFERASE 3CLA 31 REMARK 1 REF BIOCHEMISTRY V. 29 2075 1990 3CLA 32 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 3CLA 33 REMARK 1 REFERENCE 4 3CLA 34 REMARK 1 AUTH A.LEWENDON,I.A.MURRAY,C.KLEANTHOUS,P.M.CULLIS, 3CLA 35 REMARK 1 AUTH 2 W.V.SHAW 3CLA 36 REMARK 1 TITL SUBSTITUTIONS IN THE ACTIVE SITE OF CHLORAMPHENICOL 3CLA 37 REMARK 1 TITL 2 ACETYLTRANSFERASE. ROLE OF A CONSERVED ASPARTATE 3CLA 38 REMARK 1 REF BIOCHEMISTRY V. 27 7385 1988 3CLA 39 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 3CLA 40 REMARK 1 REFERENCE 5 3CLA 41 REMARK 1 AUTH A.G.W.LESLIE,P.C.E.MOODY,W.V.SHAW 3CLA 42 REMARK 1 TITL STRUCTURE OF CHLORAMPHENICOL ACETYLTRANSFERASE 3CLA 43 REMARK 1 TITL 2 AT 1.75-*ANGSTROMS RESOLUTION 3CLA 44 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 85 4133 1988 3CLA 45 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 3CLA 46 REMARK 1 REFERENCE 6 3CLA 47 REMARK 1 AUTH A.G.W.LESLIE,J.M.LIDDELL,W.V.SHAW 3CLA 48 REMARK 1 TITL CRYSTALLIZATION OF A TYPE /III$ CHLORAMPHENICOL 3CLA 49 REMARK 1 TITL 2 ACETYL TRANSFERASE 3CLA 50 REMARK 1 REF J.MOL.BIOL. V. 188 283 1986 3CLA 51 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 3CLA 52 REMARK 2 3CLA 53 REMARK 2 RESOLUTION. 1.75 ANGSTROMS. 3CLA 54 REMARK 3 3CLA 55 REMARK 3 REFINEMENT. BY THE RESTRAINED LEAST-SQUARES PROCEDURE OF J. 3CLA 56 REMARK 3 KONNERT AND W. HENDRICKSON (PROGRAM *PROLSQ), USING A 3CLA 57 REMARK 3 MODIFIED VERSION IN WHICH THE STRUCTURE FACTOR AND 3CLA 58 REMARK 3 DERIVATIVE CALCULATIONS ARE PERFORMED USING AN FFT 3CLA 59 REMARK 3 ALGORITHM DUE TO AGARWAL AND ISAACS AS IMPLEMENTED BY E. 3CLA 60 REMARK 3 DODSON USING THE VERSION APPROPRIATE FOR SPACE GROUP R3. 3CLA 61 REMARK 3 THIS WAS FOUND TO CONTAIN AN ERROR AFFECTING PRIMARILY THE 3CLA 62 REMARK 3 ATOMIC TEMPERATURE REFINEMENT AND WAS ABANDONED IN FAVOR 3CLA 63 REMARK 3 OF THE PROGRAM *DERIV* (A. JACK, M. LEVITT, ACTA 3CLA 64 REMARK 3 CRYSTALLOGR., V. A34, P. 931, 1978). THIS REDUCED THE R 3CLA 65 REMARK 3 VALUE FROM 0.183 (USING THE DODSON PROGRAM) TO 0.157. THE 3CLA 66 REMARK 3 R VALUE IS 0.157 FOR ALL DATA IN THE RESOLUTION RANGE 6.0 3CLA 67 REMARK 3 TO 1.75 ANGSTROMS. THE RMS DEVIATION FROM IDEALITY OF THE 3CLA 68 REMARK 3 BOND LENGTHS IS 0.019 ANGSTROMS. THE RMS DEVIATION FROM 3CLA 69 REMARK 3 IDEALITY OF THE BOND ANGLES IS 3.0 DEGREES. 3CLA 70 REMARK 4 3CLA 71 REMARK 4 CAT IS A TRIMER OF IDENTICAL SUBUNITS (SUBUNIT MOLECULAR 3CLA 72 REMARK 4 WEIGHT 25000). THE THREE-FOLD AXIS OF THE TRIMER IS 3CLA 73 REMARK 4 COINCIDENT WITH THE CRYSTALLOGRAPHIC THREE-FOLD AXIS. THE 3CLA 74 REMARK 4 COORDINATES ARE FOR ONE SUBUNIT OF THE TRIMER. THE 3CLA 75 REMARK 4 COORDINATES FOR THE OTHER TWO SUBUNITS CAN BE DERIVED BY 3CLA 76 REMARK 4 APPLYING ROTATIONS OF 120 DEGREES AND 240 DEGREES ABOUT 3CLA 77 REMARK 4 THE Z AXIS. 3CLA 78 REMARK 4 3CLA 79 REMARK 4 TO GENERATE THESE SYMMETRY RELATED SUBUNITS APPLY THE 3CLA 80 REMARK 4 FOLLOWING MATRICES TO THE COORDINATES GIVEN BELOW: 3CLA 81 REMARK 4 3CLA 82 REMARK 4 1. -0.50000 -0.86603 0.00000 3CLA 83 REMARK 4 0.86603 -0.50000 0.00000 3CLA 84 REMARK 4 0.00000 0.00000 1.00000 3CLA 85 REMARK 4 3CLA 86 REMARK 4 2. -0.50000 0.86603 0.00000 3CLA 87 REMARK 4 -0.86603 -0.50000 0.00000 3CLA 88 REMARK 4 0.00000 0.00000 1.00000 3CLA 89 REMARK 4 3CLA 90 REMARK 4 THE COBALT IONS PLAY A CRUCIAL ROLE IN STABILIZING THE 3CLA 91 REMARK 4 CRYSTAL LATTICE. 3CLA 92 REMARK 5 3CLA 93 REMARK 5 THE NUMBERING SCHEME ADOPTED IS BASED ON THE ALIGNMENT OF A 3CLA 94 REMARK 5 NUMBER OF CAT SEQUENCES. FOR THE TYPE III ENZYME WHOSE 3CLA 95 REMARK 5 COORDINATES ARE PRESENTED IN THIS ENTRY, MET 6 IS THE 3CLA 96 REMARK 5 N-TERMINAL RESIDUE AND THERE IS NO RESIDUE NUMBER 79. 3CLA 97 REMARK 6 3CLA 98 REMARK 6 SHEET 1 ACTUALLY HAS SEVEN STRANDS. DATA BANK CONVENTIONS 3CLA 99 REMARK 6 DO NOT ALLOW LISTING RESIDUES WHICH ARE SYMMETRY RELATED. 3CLA 100 REMARK 6 THE FINAL STRAND, SER 157 - VAL 162, IS IN AN ADJACENT 3CLA 101 REMARK 6 (THREE-FOLD RELATED) SUBUNIT OF THE TRIMER. N OF ASN 159 3CLA 102 REMARK 6 IS HYDROGEN BONDED TO O OF SER 34. 3CLA 103 REMARK 7 3CLA 104 REMARK 7 THE FOLLOWING IS A TABLE WHICH LISTS THE CORRESPONDENCE 3CLA 105 REMARK 7 BETWEEN THE ATOM NAMING SCHEME USED BY THE PROTEIN DATA 3CLA 106 REMARK 7 BANK AND THAT USED BY THE DEPOSITORS FOR THE ATOMS IN 3CLA 107 REMARK 7 CHLORAMPHENICOL (CLM), 3CLA 108 REMARK 7 3CLA 109 REMARK 7 SCHEME USED BY- 3CLA 110 REMARK 7 PDB DEPOSITOR 3CLA 111 REMARK 7 3CLA 112 REMARK 7 C1 C3 3CLA 113 REMARK 7 C2 C4 3CLA 114 REMARK 7 C3 C5 3CLA 115 REMARK 7 C4 C6 3CLA 116 REMARK 7 C5 C7 3CLA 117 REMARK 7 C6 C8 3CLA 118 REMARK 7 C7 C9 3CLA 119 REMARK 7 C8 C10 3CLA 120 REMARK 7 C9 C11 3CLA 121 REMARK 7 C10 C12 3CLA 122 REMARK 7 C11 C13 3CLA 123 REMARK 7 O2 O14 3CLA 124 REMARK 7 O4 O15 3CLA 125 REMARK 7 O5 O16 3CLA 126 REMARK 7 O9A O17 3CLA 127 REMARK 7 O9B O18 3CLA 128 REMARK 7 N2 N19 3CLA 129 REMARK 7 N9 N20 3CLA 130 REMARK 7 CL1A CL1 3CLA 131 REMARK 7 CL1B CL2 3CLA 132 REMARK 8 3CLAA 2 REMARK 8 CORRECTION. STANDARDIZE FORMAT OF FORMUL RECORD. 3CLAA 3 REMARK 8 15-JUL-92. 3CLAA 4 SEQRES 1 213 MET ASN TYR THR LYS PHE ASP VAL LYS ASN TRP VAL ARG 3CLA 133 SEQRES 2 213 ARG GLU HIS PHE GLU PHE TYR ARG HIS ARG LEU PRO CYS 3CLA 134 SEQRES 3 213 GLY PHE SER LEU THR SER LYS ILE ASP ILE THR THR LEU 3CLA 135 SEQRES 4 213 LYS LYS SER LEU ASP ASP SER ALA TYR LYS PHE TYR PRO 3CLA 136 SEQRES 5 213 VAL MET ILE TYR LEU ILE ALA GLN ALA VAL ASN GLN PHE 3CLA 137 SEQRES 6 213 ASP GLU LEU ARG MET ALA ILE LYS ASP ASP GLU LEU ILE 3CLA 138 SEQRES 7 213 VAL TRP ASP SER VAL ASP PRO GLN PHE THR VAL PHE HIS 3CLA 139 SEQRES 8 213 GLN GLU THR GLU THR PHE SER ALA LEU SER CYS PRO TYR 3CLA 140 SEQRES 9 213 SER SER ASP ILE ASP GLN PHE MET VAL ASN TYR LEU SER 3CLA 141 SEQRES 10 213 VAL MET GLU ARG TYR LYS SER ASP THR LYS LEU PHE PRO 3CLA 142 SEQRES 11 213 GLN GLY VAL THR PRO GLU ASN HIS LEU ASN ILE SER ALA 3CLA 143 SEQRES 12 213 LEU PRO TRP VAL ASN PHE ASP SER PHE ASN LEU ASN VAL 3CLA 144 SEQRES 13 213 ALA ASN PHE THR ASP TYR PHE ALA PRO ILE ILE THR MET 3CLA 145 SEQRES 14 213 ALA LYS TYR GLN GLN GLU GLY ASP ARG LEU LEU LEU PRO 3CLA 146 SEQRES 15 213 LEU SER VAL GLN VAL HIS HIS ALA VAL CYS ASP GLY PHE 3CLA 147 SEQRES 16 213 HIS VAL ALA ARG PHE ILE ASN ARG LEU GLN GLU LEU CYS 3CLA 148 SEQRES 17 213 ASN SER LYS LEU LYS 3CLA 149 FTNOTE 1 3CLA 150 FTNOTE 1 THERE IS A WIDE BETA-BULGE INVOLVING RESIDUES LYS 177, 3CLA 151 FTNOTE 1 TYR 178, AND LEU 187. 3CLA 152 FTNOTE 2 3CLA 153 FTNOTE 2 RESIDUES 157 - 162 FORM AN EXTENSION TO THE SIX STRANDED 3CLA 154 FTNOTE 2 BETA-SHEET OF AN ADJACENT SHEET WHICH SPANS THE SUBUNIT 3CLA 155 FTNOTE 2 INTERFACE. 3CLA 156 HET CLM 221 20 CHLORAMPHENICOL 3CLA 157 HET CO 222 1 COBALT ION 3CLA 158 HET CO 223 1 COBALT ION 3CLA 159 FORMUL 2 CLM C11 H22 N2 O5 CL2 3CLAA 5 FORMUL 3 CO 2(CO1 ++) 3CLA 161 FORMUL 4 HOH *204(H2 O1) 3CLA 162 HELIX 1 H1 ARG 19 ARG 28 1 24-28 RIGHT-HANDED PI 3CLA 163 HELIX 2 H2 THR 42 ASP 49 1 3CLA 164 HELIX 3 H3 PHE 55 LEU 73 1 67-73 RIGHT-HANDED 3/10 3CLA 165 HELIX 4 H4 ILE 114 ARG 127 1 3CLA 166 HELIX 5 H5 GLY 200 CYS 214 1 3CLA 167 SHEET 1 SH1 6 PHE 103 SER 107 0 3CLA 168 SHEET 2 SH1 6 ASP 90 PHE 96 -1 N PHE 93 O LEU 106 3CLA 169 SHEET 3 SH1 6 HIS 144 ALA 149 1 N ILE 147 O GLN 92 3CLA 170 SHEET 4 SH1 6 ILE 172 GLU 181 1 N ILE 173 O ASN 146 3CLA 171 SHEET 5 SH1 6 ARG 184 HIS 194 -1 N GLN 192 O ILE 172 3CLA 172 SHEET 6 SH1 6 CYS 31 ASP 40 -1 N LEU 35 O VAL 191 3CLA 173 SHEET 1 SH2 3 TYR 8 LYS 10 0 3CLA 174 SHEET 2 SH2 3 GLU 82 TRP 86 -1 N VAL 85 O THR 9 3CLA 175 SHEET 3 SH2 3 MET 75 LYS 78 -1 N ALA 76 O ILE 84 3CLA 176 CRYST1 107.600 107.600 123.600 90.00 90.00 120.00 R 3 2 18 3CLA 177 ORIGX1 1.000000 0.000000 0.000000 0.00000 3CLA 178 ORIGX2 0.000000 1.000000 0.000000 0.00000 3CLA 179 ORIGX3 0.000000 0.000000 1.000000 0.00000 3CLA 180 SCALE1 0.009294 0.005366 0.000000 0.00000 3CLA 181 SCALE2 0.000000 0.010731 0.000000 0.00000 3CLA 182 SCALE3 0.000000 0.000000 0.008091 0.00000 3CLA 183