HEADER OXIDOREDUCTASE (OXYGEN(A)) 14-JUN-89 1GOX 1GOX 3 COMPND GLYCOLATE OXIDASE (E.C.1.1.3.1) 1GOX 4 SOURCE SPINACH (SPINACIA $OLERACEA) 1GOX 5 AUTHOR Y.LINDQVIST 1GOX 6 REVDAT 1 15-OCT-89 1GOX 0 1GOX 7 JRNL AUTH Y.LINDQVIST 1GOX 8 JRNL TITL REFINED STRUCTURE OF SPINACH GLYCOLATE OXIDASE AT 1GOX 9 JRNL TITL 2 2 ANGSTROMS RESOLUTION 1GOX 10 JRNL REF J.MOL.BIOL. V. 209 151 1989 1GOX 11 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 1GOX 12 REMARK 1 1GOX 13 REMARK 1 REFERENCE 1 1GOX 14 REMARK 1 AUTH Y.LINDQVIST,C.-*I.BRANDEN 1GOX 15 REMARK 1 TITL THE ACTIVE SITE OF SPINACH GLYCOLATE OXIDASE 1GOX 16 REMARK 1 REF J.BIOL.CHEM. V. 264 3624 1989 1GOX 17 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1GOX 18 REMARK 1 REFERENCE 2 1GOX 19 REMARK 1 AUTH E.CEDERLUND,Y.LINDQVIST,G.SODERLUND,C.-*I.BRANDEN, 1GOX 20 REMARK 1 AUTH 2 H.JORNVALL 1GOX 21 REMARK 1 TITL PRIMARY STRUCTURE OF GLYCOLATE OXIDASE FROM SPINACH 1GOX 22 REMARK 1 REF EUR.J.BIOCHEM. V. 173 523 1988 1GOX 23 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 1GOX 24 REMARK 1 REFERENCE 3 1GOX 25 REMARK 1 AUTH Y.LINDQVIST,C.-*I.BRANDEN 1GOX 26 REMARK 1 TITL STRUCTURE OF GLYCOLATE OXIDASE FROM SPINACH 1GOX 27 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 82 6855 1985 1GOX 28 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 1GOX 29 REMARK 1 REFERENCE 4 1GOX 30 REMARK 1 AUTH Y.LINDQVIST,C.-*I.BRANDEN 1GOX 31 REMARK 1 TITL STRUCTURE OF GLYCOLATE OXIDASE FROM SPINACH AT A 1GOX 32 REMARK 1 TITL 2 RESOLUTION OF 5.5 ANGSTROMS 1GOX 33 REMARK 1 REF J.MOL.BIOL. V. 143 201 1980 1GOX 34 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1GOX 35 REMARK 1 REFERENCE 5 1GOX 36 REMARK 1 AUTH Y.LINDQVIST,C.-*I.BRANDEN 1GOX 37 REMARK 1 TITL PRELIMINARY CRYSTALLOGRAPHIC DATA FOR GLYCOLATE 1GOX 38 REMARK 1 TITL 2 OXIDASE FROM SPINACH 1GOX 39 REMARK 1 REF J.BIOL.CHEM. V. 254 7403 1979 1GOX 40 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1GOX 41 REMARK 2 1GOX 42 REMARK 2 RESOLUTION. 2.0 ANGSTROMS NOMINAL. 1GOX 43 REMARK 3 1GOX 44 REMARK 3 REFINEMENT. BY THE RESTRAINED LEAST SQUARES PROCEDURE OF J. 1GOX 45 REMARK 3 KONNERT AND W. HENDRICKSON (PROGRAM *PROLSQ*). THE R 1GOX 46 REMARK 3 VALUE IS 0.189. 1GOX 47 REMARK 3 1GOX 48 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 1GOX 49 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 1GOX 50 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 1GOX 51 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 1GOX 52 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 1GOX 53 REMARK 3 BOND DISTANCE 0.015(0.030) 1GOX 54 REMARK 3 ANGLE DISTANCE 0.043(0.040) 1GOX 55 REMARK 3 PLANAR 1-4 DISTANCE 0.046(0.050) 1GOX 56 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.011(0.020) 1GOX 57 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.173(0.150) 1GOX 58 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 1GOX 59 REMARK 3 SINGLE TORSION CONTACT 0.194(0.500) 1GOX 60 REMARK 3 MULTIPLE TORSION CONTACT 0.200(0.500) 1GOX 61 REMARK 3 POSSIBLE HYDROGEN BOND 0.223(0.500) 1GOX 62 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 1GOX 63 REMARK 3 PLANAR (OMEGA) 2.0(3.0) 1GOX 64 REMARK 3 STAGGERED 19.5(15.0) 1GOX 65 REMARK 3 ORTHONORMAL 27.4(20.0) 1GOX 66 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 1GOX 67 REMARK 3 MAIN-CHAIN BOND 1.312(1.000) 1GOX 68 REMARK 3 MAIN-CHAIN ANGLE 1.452(1.500) 1GOX 69 REMARK 3 SIDE-CHAIN BOND 0.813(1.000) 1GOX 70 REMARK 3 SIDE-CHAIN ANGLE 1.521(1.500) 1GOX 71 REMARK 4 1GOX 72 REMARK 4 COORDINATES FOR RESIDUES 189 - 197 AND 360 - 369 ARE NOT 1GOX 73 REMARK 4 INCLUDED IN THIS ENTRY. THESE REGIONS ARE FLEXIBLE IN THE 1GOX 74 REMARK 4 CRYSTAL AND IT WAS NOT POSSIBLE TO TRACE THE CHAIN. 1GOX 75 REMARK 5 1GOX 76 REMARK 5 THE SHEET PRESENTED AS *BAR* ON SHEET RECORDS BELOW IS 1GOX 77 REMARK 5 ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS 1GOX 78 REMARK 5 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND 1GOX 79 REMARK 5 LAST STRANDS ARE IDENTICAL. 1GOX 80 SEQRES 1 369 MET GLU ILE THR ASN VAL ASN GLU TYR GLU ALA ILE ALA 1GOX 81 SEQRES 2 369 LYS GLN LYS LEU PRO LYS MET VAL TYR ASP TYR TYR ALA 1GOX 82 SEQRES 3 369 SER GLY ALA GLU ASP GLN TRP THR LEU ALA GLU ASN ARG 1GOX 83 SEQRES 4 369 ASN ALA PHE SER ARG ILE LEU PHE ARG PRO ARG ILE LEU 1GOX 84 SEQRES 5 369 ILE ASP VAL THR ASN ILE ASP MET THR THR THR ILE LEU 1GOX 85 SEQRES 6 369 GLY PHE LYS ILE SER MET PRO ILE MET ILE ALA PRO THR 1GOX 86 SEQRES 7 369 ALA MET GLN LYS MET ALA HIS PRO GLU GLY GLU TYR ALA 1GOX 87 SEQRES 8 369 THR ALA ARG ALA ALA SER ALA ALA GLY THR ILE MET THR 1GOX 88 SEQRES 9 369 LEU SER SER TRP ALA THR SER SER VAL GLU GLU VAL ALA 1GOX 89 SEQRES 10 369 SER THR GLY PRO GLY ILE ARG PHE PHE GLN LEU TYR VAL 1GOX 90 SEQRES 11 369 TYR LYS ASP ARG ASN VAL VAL ALA GLN LEU VAL ARG ARG 1GOX 91 SEQRES 12 369 ALA GLU ARG ALA GLY PHE LYS ALA ILE ALA LEU THR VAL 1GOX 92 SEQRES 13 369 ASP THR PRO ARG LEU GLY ARG ARG GLU ALA ASP ILE LYS 1GOX 93 SEQRES 14 369 ASN ARG PHE VAL LEU PRO PRO PHE LEU THR LEU LYS ASN 1GOX 94 SEQRES 15 369 PHE GLU GLY ILE ASP LEU GLY LYS MET ASP LYS ALA ASN 1GOX 95 SEQRES 16 369 ASP SER GLY LEU SER SER TYR VAL ALA GLY GLN ILE ASP 1GOX 96 SEQRES 17 369 ARG SER LEU SER TRP LYS ASP VAL ALA TRP LEU GLN THR 1GOX 97 SEQRES 18 369 ILE THR SER LEU PRO ILE LEU VAL LYS GLY VAL ILE THR 1GOX 98 SEQRES 19 369 ALA GLU ASP ALA ARG LEU ALA VAL GLN HIS GLY ALA ALA 1GOX 99 SEQRES 20 369 GLY ILE ILE VAL SER ASN HIS GLY ALA ARG GLN LEU ASP 1GOX 100 SEQRES 21 369 TYR VAL PRO ALA THR ILE MET ALA LEU GLU GLU VAL VAL 1GOX 101 SEQRES 22 369 LYS ALA ALA GLN GLY ARG ILE PRO VAL PHE LEU ASP GLY 1GOX 102 SEQRES 23 369 GLY VAL ARG ARG GLY THR ASP VAL PHE LYS ALA LEU ALA 1GOX 103 SEQRES 24 369 LEU GLY ALA ALA GLY VAL PHE ILE GLY ARG PRO VAL VAL 1GOX 104 SEQRES 25 369 PHE SER LEU ALA ALA GLU GLY GLU ALA GLY VAL LYS LYS 1GOX 105 SEQRES 26 369 VAL LEU GLN MET MET ARG ASP GLU PHE GLU LEU THR MET 1GOX 106 SEQRES 27 369 ALA LEU SER GLY CYS ARG SER LEU LYS GLU ILE SER ARG 1GOX 107 SEQRES 28 369 SER HIS ILE ALA ALA ASP TRP ASP GLY PRO SER SER ARG 1GOX 108 SEQRES 29 369 ALA VAL ALA ARG LEU 1GOX 109 HET FMN 1 31 FLAVIN MONONUCLEOTIDE PROSTHETIC GROUP 1GOX 110 FORMUL 2 FMN C17 H19 N4 O9 P1 -- 1GOX 111 FORMUL 3 HOH *298(H2 O1) 1GOX 112 HELIX 1 A GLU 8 LYS 16 1 1GOX 113 HELIX 2 B LYS 19 ALA 26 1 1GOX 114 HELIX 3 C GLN 32 ASN 40 1 1GOX 115 HELIX 4 1 GLY 88 ALA 99 1 1GOX 116 HELIX 5 2 VAL 113 ALA 117 1 1GOX 117 HELIX 6 3 ARG 134 ARG 146 1 1GOX 118 HELIX 7 D GLU 165 LYS 169 1 1GOX 119 HELIX 8 E LEU 199 GLN 206 1 1GOX 120 HELIX 9 4 TRP 213 ILE 222 1 1GOX 121 HELIX 10 5 ALA 235 GLN 243 1 1GOX 122 HELIX 11 6 THR 265 ALA 276 1 1GOX 123 HELIX 12 7 GLY 291 LEU 300 1 1GOX 124 HELIX 13 F ARG 309 GLY 319 1 1GOX 125 HELIX 14 8 GLY 319 SER 341 1 1GOX 126 SHEET 1 BAR 9 ILE 73 ILE 75 0 1GOX 127 SHEET 2 BAR 9 MET 103 LEU 105 1 1GOX 128 SHEET 3 BAR 9 ARG 124 LEU 128 1 1GOX 129 SHEET 4 BAR 9 ALA 151 THR 155 1 1GOX 130 SHEET 5 BAR 9 ILE 227 LYS 230 1 1GOX 131 SHEET 6 BAR 9 GLY 248 VAL 251 1 1GOX 132 SHEET 7 BAR 9 VAL 282 ASP 285 1 1GOX 133 SHEET 8 BAR 9 GLY 304 ILE 307 1 1GOX 134 SHEET 9 BAR 9 ILE 73 ILE 75 1 1GOX 135 CRYST1 148.100 148.100 135.100 90.00 90.00 90.00 I 4 2 2 16 1GOX 136 ORIGX1 1.000000 0.000000 0.000000 0.00000 1GOX 137 ORIGX2 0.000000 1.000000 0.000000 0.00000 1GOX 138 ORIGX3 0.000000 0.000000 1.000000 0.00000 1GOX 139 SCALE1 0.006752 0.000000 0.000000 0.00000 1GOX 140 SCALE2 0.000000 0.006752 0.000000 0.00000 1GOX 141 SCALE3 0.000000 0.000000 0.007402 0.00000 1GOX 142