HEADER OXIDOREDUCTASE 13-JUL-94 3MDD 3MDD 2 COMPND MEDIUM CHAIN ACYL-COA DEHYDROGENASE (MCAD) (E.C.1.3.99.3) 3MDD 3 SOURCE PIG (SUS SCROFA) LIVER 3MDD 4 AUTHOR J.-J.P.KIM,M.WANG,R.PASCHKE 3MDD 5 REVDAT 1 30-SEP-94 3MDD 0 3MDD 6 JRNL AUTH J.-J.P.KIM,M.WANG,R.PASCHKE 3MDD 7 JRNL TITL CRYSTAL STRUCTURES OF MEDIUM CHAIN ACYL-COA 3MDD 8 JRNL TITL 2 DEHYDROGENASE FROM PIG LIVER MITOCHONDRIA WITH 3MDD 9 JRNL TITL 3 AND WITHOUT SUBSTRATE 3MDD 10 JRNL REF PROC.NAT.ACAD.SCI.USA V. 90 7523 1993 3MDD 11 JRNL REFN ASTM PNASA6 US ISSN 0027-8424 0040 3MDD 12 REMARK 1 3MDD 13 REMARK 1 REFERENCE 1 3MDD 14 REMARK 1 AUTH J.-J.P.KIM,J.WU 3MDD 15 REMARK 1 TITL STRUCTURE OF THE MEDIUM-CHAIN ACYL-COA 3MDD 16 REMARK 1 TITL 2 DEHYDROGENASE FROM PIG LIVER MITOCHONDRIA AT 3MDD 17 REMARK 1 TITL 3 3-ANGSTROMS RESOLUTION 3MDD 18 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 85 6677 1988 3MDD 19 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 0040 3MDD 20 REMARK 2 3MDD 21 REMARK 2 RESOLUTION. 2.4 ANGSTROMS. 3MDD 22 REMARK 3 3MDD 23 REMARK 3 REFINEMENT. 3MDD 24 REMARK 3 PROGRAM GPRLSA 3MDD 25 REMARK 3 AUTHORS HENDRICKSON 3MDD 26 REMARK 3 R VALUE 0.173 3MDD 27 REMARK 3 RMSD BOND DISTANCES 0.008 ANGSTROMS 3MDD 28 REMARK 3 RMSD BOND ANGLE DISTANCES 0.021 ANGSTROMS 3MDD 29 REMARK 3 3MDD 30 REMARK 3 NUMBER OF REFLECTIONS 30930 3MDD 31 REMARK 3 RESOLUTION RANGE 6.0 - 2.4 ANGSTROMS 3MDD 32 REMARK 3 DATA CUTOFF 3.0 SIGMA(F) 3MDD 33 REMARK 3 PERCENT COMPLETION 84.0 3MDD 34 REMARK 3 3MDD 35 REMARK 3 NUMBER OF PROTEIN ATOMS 5964 3MDD 36 REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 3MDD 37 REMARK 3 NUMBER OF NON-PROTEIN COFACTOR ATOMS 106 3MDD 38 REMARK 3 NUMBER OF SOLVENT ATOMS 166 3MDD 39 REMARK 4 3MDD 40 REMARK 4 THE SEQUENCE HAS NOT BEEN REPORTED YET. A.W.STRAUSS, 3MDD 41 REMARK 4 D.KELLY, AND J.-J.P.KIM, MANUSCRIPT IN PREPARATION. 3MDD 42 REMARK 5 3MDD 43 REMARK 5 STRAND 4 OF SHEET 2 DOES NOT INCLUDE RESIDUE 229. 3MDD 44 REMARK 6 3MDD 45 REMARK 6 PDB ADVISORY NOTICE: 3MDD 46 REMARK 6 WATER MOLECULE 923 MAKES A CLOSE CONTACT OF 1.22 ANGSTROMS 3MDD 47 REMARK 6 WITH LEU B 238. 3MDD 48 SEQRES 1 A 385 GLY PHE SER PHE GLU LEU THR GLU GLN GLN LYS GLU PHE 3MDD 49 SEQRES 2 A 385 GLN ALA THR ALA ARG LYS PHE ALA ARG GLU GLU ILE ILE 3MDD 50 SEQRES 3 A 385 PRO VAL ALA ALA GLU TYR ASP ARG THR GLY GLU TYR PRO 3MDD 51 SEQRES 4 A 385 VAL PRO LEU LEU LYS ARG ALA TRP GLU LEU GLY LEU MET 3MDD 52 SEQRES 5 A 385 ASN THR HIS ILE PRO GLU SER PHE GLY GLY LEU GLY LEU 3MDD 53 SEQRES 6 A 385 GLY ILE ILE ASP SER CYS LEU ILE THR GLU GLU LEU ALA 3MDD 54 SEQRES 7 A 385 TYR GLY CYS THR GLY VAL GLN THR ALA ILE GLU ALA ASN 3MDD 55 SEQRES 8 A 385 THR LEU GLY GLN VAL PRO LEU ILE ILE GLY GLY ASN TYR 3MDD 56 SEQRES 9 A 385 GLN GLN GLN LYS LYS TYR LEU GLY ARG MET THR GLU GLU 3MDD 57 SEQRES 10 A 385 PRO LEU MET CYS ALA TYR CYS VAL THR GLU PRO GLY ALA 3MDD 58 SEQRES 11 A 385 GLY SER ASP VAL ALA GLY ILE LYS THR LYS ALA GLU LYS 3MDD 59 SEQRES 12 A 385 LYS GLY ASP GLU TYR ILE ILE ASN GLY GLN LYS MET TRP 3MDD 60 SEQRES 13 A 385 ILE THR ASN GLY GLY LYS ALA ASN TRP TYR PHE LEU LEU 3MDD 61 SEQRES 14 A 385 ALA ARG SER ASP PRO ASP PRO LYS ALA PRO ALA SER LYS 3MDD 62 SEQRES 15 A 385 ALA PHE THR GLY PHE ILE VAL GLU ALA ASP THR PRO GLY 3MDD 63 SEQRES 16 A 385 VAL GLN ILE GLY ARG LYS GLU ILE ASN MET GLY GLN ARG 3MDD 64 SEQRES 17 A 385 CYS SER ASP THR ARG GLY ILE VAL PHE GLU ASP VAL ARG 3MDD 65 SEQRES 18 A 385 VAL PRO LYS GLU ASN VAL LEU THR GLY GLU GLY ALA GLY 3MDD 66 SEQRES 19 A 385 PHE LYS ILE ALA MET GLY THR PHE ASP LYS THR ARG PRO 3MDD 67 SEQRES 20 A 385 PRO VAL ALA ALA GLY ALA VAL GLY LEU ALA GLN ARG ALA 3MDD 68 SEQRES 21 A 385 LEU ASP GLU ALA THR LYS TYR ALA LEU GLU ARG LYS THR 3MDD 69 SEQRES 22 A 385 PHE GLY LYS LEU LEU ALA GLU HIS GLN GLY ILE SER PHE 3MDD 70 SEQRES 23 A 385 LEU LEU ALA ASP MET ALA MET LYS VAL GLU LEU ALA ARG 3MDD 71 SEQRES 24 A 385 LEU SER TYR GLN ARG ALA ALA TRP GLU ILE ASP SER GLY 3MDD 72 SEQRES 25 A 385 ARG ARG ASN THR TYR TYR ALA SER ILE ALA LYS ALA TYR 3MDD 73 SEQRES 26 A 385 ALA ALA ASP ILE ALA ASN GLN LEU ALA THR ASP ALA VAL 3MDD 74 SEQRES 27 A 385 GLN VAL PHE GLY GLY ASN GLY PHE ASN THR GLU TYR PRO 3MDD 75 SEQRES 28 A 385 VAL GLU LYS LEU MET ARG ASP ALA LYS ILE TYR GLN ILE 3MDD 76 SEQRES 29 A 385 TYR GLU GLY THR ALA GLN ILE GLN ARG ILE ILE ILE ALA 3MDD 77 SEQRES 30 A 385 ARG GLU HIS ILE GLY ARG TYR LYS 3MDD 78 SEQRES 1 B 385 GLY PHE SER PHE GLU LEU THR GLU GLN GLN LYS GLU PHE 3MDD 79 SEQRES 2 B 385 GLN ALA THR ALA ARG LYS PHE ALA ARG GLU GLU ILE ILE 3MDD 80 SEQRES 3 B 385 PRO VAL ALA ALA GLU TYR ASP ARG THR GLY GLU TYR PRO 3MDD 81 SEQRES 4 B 385 VAL PRO LEU LEU LYS ARG ALA TRP GLU LEU GLY LEU MET 3MDD 82 SEQRES 5 B 385 ASN THR HIS ILE PRO GLU SER PHE GLY GLY LEU GLY LEU 3MDD 83 SEQRES 6 B 385 GLY ILE ILE ASP SER CYS LEU ILE THR GLU GLU LEU ALA 3MDD 84 SEQRES 7 B 385 TYR GLY CYS THR GLY VAL GLN THR ALA ILE GLU ALA ASN 3MDD 85 SEQRES 8 B 385 THR LEU GLY GLN VAL PRO LEU ILE ILE GLY GLY ASN TYR 3MDD 86 SEQRES 9 B 385 GLN GLN GLN LYS LYS TYR LEU GLY ARG MET THR GLU GLU 3MDD 87 SEQRES 10 B 385 PRO LEU MET CYS ALA TYR CYS VAL THR GLU PRO GLY ALA 3MDD 88 SEQRES 11 B 385 GLY SER ASP VAL ALA GLY ILE LYS THR LYS ALA GLU LYS 3MDD 89 SEQRES 12 B 385 LYS GLY ASP GLU TYR ILE ILE ASN GLY GLN LYS MET TRP 3MDD 90 SEQRES 13 B 385 ILE THR ASN GLY GLY LYS ALA ASN TRP TYR PHE LEU LEU 3MDD 91 SEQRES 14 B 385 ALA ARG SER ASP PRO ASP PRO LYS ALA PRO ALA SER LYS 3MDD 92 SEQRES 15 B 385 ALA PHE THR GLY PHE ILE VAL GLU ALA ASP THR PRO GLY 3MDD 93 SEQRES 16 B 385 VAL GLN ILE GLY ARG LYS GLU ILE ASN MET GLY GLN ARG 3MDD 94 SEQRES 17 B 385 CYS SER ASP THR ARG GLY ILE VAL PHE GLU ASP VAL ARG 3MDD 95 SEQRES 18 B 385 VAL PRO LYS GLU ASN VAL LEU THR GLY GLU GLY ALA GLY 3MDD 96 SEQRES 19 B 385 PHE LYS ILE ALA MET GLY THR PHE ASP LYS THR ARG PRO 3MDD 97 SEQRES 20 B 385 PRO VAL ALA ALA GLY ALA VAL GLY LEU ALA GLN ARG ALA 3MDD 98 SEQRES 21 B 385 LEU ASP GLU ALA THR LYS TYR ALA LEU GLU ARG LYS THR 3MDD 99 SEQRES 22 B 385 PHE GLY LYS LEU LEU ALA GLU HIS GLN GLY ILE SER PHE 3MDD 100 SEQRES 23 B 385 LEU LEU ALA ASP MET ALA MET LYS VAL GLU LEU ALA ARG 3MDD 101 SEQRES 24 B 385 LEU SER TYR GLN ARG ALA ALA TRP GLU ILE ASP SER GLY 3MDD 102 SEQRES 25 B 385 ARG ARG ASN THR TYR TYR ALA SER ILE ALA LYS ALA TYR 3MDD 103 SEQRES 26 B 385 ALA ALA ASP ILE ALA ASN GLN LEU ALA THR ASP ALA VAL 3MDD 104 SEQRES 27 B 385 GLN VAL PHE GLY GLY ASN GLY PHE ASN THR GLU TYR PRO 3MDD 105 SEQRES 28 B 385 VAL GLU LYS LEU MET ARG ASP ALA LYS ILE TYR GLN ILE 3MDD 106 SEQRES 29 B 385 TYR GLU GLY THR ALA GLN ILE GLN ARG ILE ILE ILE ALA 3MDD 107 SEQRES 30 B 385 ARG GLU HIS ILE GLY ARG TYR LYS 3MDD 108 HET FAD A 399 53 FLAVIN-ADENINE DINUCLEOTIDE 3MDD 109 HET FAD B 399 53 FLAVIN-ADENINE DINUCLEOTIDE 3MDD 110 FORMUL 3 FAD 2(C27 H33 N9 O15 P2) 3MDD 111 FORMUL 4 HOH *166(H2 O1) 3MDD 112 HELIX 1 A GLU A 18 PRO A 37 1 3MDD 113 HELIX 2 B ALA A 40 THR A 45 1 3MDD 114 HELIX 3 C VAL A 50 GLY A 60 1 3MDD 115 HELIX 4 D ILE A 77 TYR A 89 1 3MDD 116 HELIX 5 E THR A 92 LEU A 108 1 3MDD 117 HELIX 6 F TYR A 114 GLU A 126 1 LAST 2 TURNS ARE 3/10 HELIX 3MDD 118 HELIX 7 G ALA A 243 LEU A 279 1 SHARP BEND AT PRO257 & PRO258 3MDD 119 HELIX 8 H GLN A 292 SER A 321 1 3MDD 120 HELIX 9 I ASN A 325 PHE A 351 1 3MDD 121 HELIX 10 J VAL A 362 GLN A 373 1 3MDD 122 HELIX 11 K ALA A 379 GLY A 392 1 3MDD 123 HELIX 12 A GLU B 18 PRO B 37 1 3MDD 124 HELIX 13 B ALA B 40 THR B 45 1 3MDD 125 HELIX 14 C VAL B 50 GLY B 60 1 3MDD 126 HELIX 15 D ILE B 77 TYR B 89 1 3MDD 127 HELIX 16 E THR B 92 LEU B 108 1 3MDD 128 HELIX 17 F TYR B 114 GLU B 126 1 LAST 2 TURNS ARE 3/10 HELIX 3MDD 129 HELIX 18 G ALA B 243 LEU B 279 1 SHARP BEND AT PRO257 & PRO258 3MDD 130 HELIX 19 H GLN B 292 SER B 321 1 3MDD 131 HELIX 20 I ASN B 325 PHE B 351 1 3MDD 132 HELIX 21 J VAL B 362 GLN B 373 1 3MDD 133 HELIX 22 K ALA B 379 GLY B 392 1 3MDD 134 SHEET 1 1 3 LEU A 129 VAL A 135 0 3MDD 135 SHEET 2 1 3 TRP A 175 ARG A 181 1 3MDD 136 SHEET 3 1 3 PHE A 194 GLU A 200 -1 3MDD 137 SHEET 1 2 4 THR A 149 LYS A 154 0 3MDD 138 SHEET 2 2 4 GLU A 157 MET A 165 -1 3MDD 139 SHEET 3 2 4 GLY A 205 GLU A 212 1 3MDD 140 SHEET 4 2 4 THR A 222 PRO A 233 -1 3MDD 141 SHEET 1 1 3 LEU B 129 VAL B 135 0 3MDD 142 SHEET 2 1 3 TRP B 175 ARG B 181 1 3MDD 143 SHEET 3 1 3 PHE B 194 GLU B 200 -1 3MDD 144 SHEET 1 2 4 THR B 149 LYS B 154 0 3MDD 145 SHEET 2 2 4 GLU B 157 MET B 165 -1 3MDD 146 SHEET 3 2 4 GLY B 205 GLU B 212 1 3MDD 147 SHEET 4 2 4 THR B 222 PRO B 233 -1 3MDD 148 TURN 1 T1 PRO A 67 PHE A 70 3MDD 149 TURN 2 T2 ASP A 143 GLY A 146 3MDD 150 TURN 3 T3 ILE A 167 GLY A 170 3MDD 151 TURN 4 T4 LYS A 234 VAL A 237 3MDD 152 TURN 5 T5 THR A 283 LYS A 286 3MDD 153 TURN 6 T6 LEU A 287 GLU A 290 3MDD 154 TURN 7 T7 ILE A 319 GLY A 322 3MDD 155 TURN 8 T8 ASN A 357 TYR A 360 3MDD 156 TURN 9 T1 PRO B 67 PHE B 70 3MDD 157 TURN 10 T2 ASP B 143 GLY B 146 3MDD 158 TURN 11 T3 ILE B 167 GLY B 170 3MDD 159 TURN 12 T4 LYS B 234 VAL B 237 3MDD 160 TURN 13 T5 THR B 283 LYS B 286 3MDD 161 TURN 14 T6 LEU B 287 GLU B 290 3MDD 162 TURN 15 T7 ILE B 319 GLY B 322 3MDD 163 TURN 16 T8 ASN B 357 TYR B 360 3MDD 164 CRYST1 128.820 136.130 106.140 90.00 90.00 90.00 C 2 2 21 16 3MDD 165 ORIGX1 1.000000 0.000000 0.000000 0.00000 3MDD 166 ORIGX2 0.000000 1.000000 0.000000 0.00000 3MDD 167 ORIGX3 0.000000 0.000000 1.000000 0.00000 3MDD 168 SCALE1 0.007763 0.000000 0.000000 0.00000 3MDD 169 SCALE2 0.000000 0.007346 0.000000 0.00000 3MDD 170 SCALE3 0.000000 0.000000 0.009422 0.00000 3MDD 171