HEADER TRIOSEPHOSPHATE ISOMERASE 22-DEC-93 1TPH 1TPH 2 COMPND TRIOSEPHOSPHATE ISOMERASE (E.C.5.3.1.1) COMPLEXED WITH 1TPH 3 COMPND 2 PHOSPHOGLYCOLOHYDROXAMATE 1TPH 4 SOURCE CHICKEN (GALLUS GALLUS) MUSCLE 1TPH 5 AUTHOR Z.ZHANG,S.SUGIO,E.A.KOMIVES,K.D.LIU,J.R.KNOWLES,G.A.PETSKO, 1TPH 6 AUTHOR 2 D.RINGE 1TPH 7 REVDAT 1 30-APR-94 1TPH 0 1TPH 8 JRNL AUTH Z.ZHANG,S.SUGIO,E.A.KOMIVES,K.D.LIU,J.R.KNOWLES, 1TPH 9 JRNL AUTH 2 G.A.PETSKO,D.RINGE 1TPH 10 JRNL TITL 1.8 ANGSTROMS CRYSTAL STRUCTURE OF WILD TYPE 1TPH 11 JRNL TITL 2 CHICKEN TRIOSEPHOSPHATE 1TPH 12 JRNL TITL 3 ISOMERASE-PHOSPHOGLYCOLOHYDROXAMATE COMPLEX 1TPH 13 JRNL REF TO BE PUBLISHED 1TPH 14 JRNL REFN 353 1TPH 15 REMARK 1 1TPH 16 REMARK 2 1TPH 17 REMARK 2 RESOLUTION. 1.8 ANGSTROMS. 1TPH 18 REMARK 3 1TPH 19 REMARK 3 REFINEMENT. 1TPH 20 REMARK 3 PROGRAM PROLSQ 1TPH 21 REMARK 3 AUTHORS KONNERT,HENDRICKSON 1TPH 22 REMARK 3 R VALUE 0.185 1TPH 23 REMARK 3 RMSD BOND DISTANCES 0.017 ANGSTROMS 1TPH 24 REMARK 3 RMSD BOND ANGLES 2.2 DEGREES 1TPH 25 REMARK 3 1TPH 26 REMARK 3 NUMBER OF REFLECTIONS 47198 1TPH 27 REMARK 3 RESOLUTION RANGE 6.0 - 1.8 ANGSTROMS 1TPH 28 REMARK 3 DATA CUTOFF 1.0 SIGMA(F) 1TPH 29 REMARK 3 1TPH 30 REMARK 3 NUMBER OF PROTEIN ATOMS 3712 1TPH 31 REMARK 3 NUMBER OF SOLVENT ATOMS 249 1TPH 32 REMARK 3 1TPH 33 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 1TPH 34 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 1TPH 35 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 1TPH 36 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 1TPH 37 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 1TPH 38 REMARK 3 BOND DISTANCE 0.017(0.020) 1TPH 39 REMARK 3 ANGLE DISTANCE 0.034(0.035) 1TPH 40 REMARK 3 PLANAR 1-4 DISTANCE 0.048(0.050) 1TPH 41 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.013(0.020) 1TPH 42 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.125(0.130) 1TPH 43 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 1TPH 44 REMARK 3 SINGLE TORSION CONTACT 0.183(0.400) 1TPH 45 REMARK 3 MULTIPLE TORSION CONTACT 0.185(0.400) 1TPH 46 REMARK 3 POSSIBLE HYDROGEN BOND 0.170(0.400) 1TPH 47 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 1TPH 48 REMARK 3 PLANAR 2.300(3.000) 1TPH 49 REMARK 3 STAGGERED 15.80(15.00) 1TPH 50 REMARK 3 ORTHONORMAL 34.50(20.00) 1TPH 51 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 1TPH 52 REMARK 3 MAIN-CHAIN BOND 0.766(1.000) 1TPH 53 REMARK 3 MAIN-CHAIN ANGLE 1.227(1.500) 1TPH 54 REMARK 3 SIDE-CHAIN BOND 1.532(1.500) 1TPH 55 REMARK 3 SIDE-CHAIN ANGLE 2.327(2.000) 1TPH 56 REMARK 4 1TPH 57 REMARK 4 MOLECULAR REPLACEMENT METHOD (PROGRAM PACKAGE MERLOT, 1TPH 58 REMARK 4 VERSION 2.3, FITZGERALD, 1988) WAS USED IN CRYSTAL 1TPH 59 REMARK 4 STRUCTURE SOLUTION. 1TPH 60 REMARK 5 1TPH 61 REMARK 5 SEQUENCE ADVISORY NOTICE: 1TPH 62 REMARK 5 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1TPH 63 REMARK 5 1TPH 64 REMARK 5 SWISS-PROT ENTRY NAME: TPIS_CHICK 1TPH 65 REMARK 5 1TPH 66 REMARK 5 SWISS-PROT RESIDUE PDB SEQRES 1TPH 67 REMARK 5 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1TPH 68 REMARK 5 SER 194 THR 194 1TPH 69 SEQRES 1 1 247 ALA PRO ARG LYS PHE PHE VAL GLY GLY ASN TRP LYS MET 1TPH 70 SEQRES 2 1 247 ASN GLY ASP LYS LYS SER LEU GLY GLU LEU ILE HIS THR 1TPH 71 SEQRES 3 1 247 LEU ASN GLY ALA LYS LEU SER ALA ASP THR GLU VAL VAL 1TPH 72 SEQRES 4 1 247 CYS GLY ALA PRO SER ILE TYR LEU ASP PHE ALA ARG GLN 1TPH 73 SEQRES 5 1 247 LYS LEU ASP ALA LYS ILE GLY VAL ALA ALA GLN ASN CYS 1TPH 74 SEQRES 6 1 247 TYR LYS VAL PRO LYS GLY ALA PHE THR GLY GLU ILE SER 1TPH 75 SEQRES 7 1 247 PRO ALA MET ILE LYS ASP ILE GLY ALA ALA TRP VAL ILE 1TPH 76 SEQRES 8 1 247 LEU GLY HIS SER GLU ARG ARG HIS VAL PHE GLY GLU SER 1TPH 77 SEQRES 9 1 247 ASP GLU LEU ILE GLY GLN LYS VAL ALA HIS ALA LEU ALA 1TPH 78 SEQRES 10 1 247 GLU GLY LEU GLY VAL ILE ALA CYS ILE GLY GLU LYS LEU 1TPH 79 SEQRES 11 1 247 ASP GLU ARG GLU ALA GLY ILE THR GLU LYS VAL VAL PHE 1TPH 80 SEQRES 12 1 247 GLU GLN THR LYS ALA ILE ALA ASP ASN VAL LYS ASP TRP 1TPH 81 SEQRES 13 1 247 SER LYS VAL VAL LEU ALA TYR GLU PRO VAL TRP ALA ILE 1TPH 82 SEQRES 14 1 247 GLY THR GLY LYS THR ALA THR PRO GLN GLN ALA GLN GLU 1TPH 83 SEQRES 15 1 247 VAL HIS GLU LYS LEU ARG GLY TRP LEU LYS THR HIS VAL 1TPH 84 SEQRES 16 1 247 SER ASP ALA VAL ALA GLN SER THR ARG ILE ILE TYR GLY 1TPH 85 SEQRES 17 1 247 GLY SER VAL THR GLY GLY ASN CYS LYS GLU LEU ALA SER 1TPH 86 SEQRES 18 1 247 GLN HIS ASP VAL ASP GLY PHE LEU VAL GLY GLY ALA SER 1TPH 87 SEQRES 19 1 247 LEU LYS PRO GLU PHE VAL ASP ILE ILE ASN ALA LYS HIS 1TPH 88 SEQRES 1 2 247 ALA PRO ARG LYS PHE PHE VAL GLY GLY ASN TRP LYS MET 1TPH 89 SEQRES 2 2 247 ASN GLY ASP LYS LYS SER LEU GLY GLU LEU ILE HIS THR 1TPH 90 SEQRES 3 2 247 LEU ASN GLY ALA LYS LEU SER ALA ASP THR GLU VAL VAL 1TPH 91 SEQRES 4 2 247 CYS GLY ALA PRO SER ILE TYR LEU ASP PHE ALA ARG GLN 1TPH 92 SEQRES 5 2 247 LYS LEU ASP ALA LYS ILE GLY VAL ALA ALA GLN ASN CYS 1TPH 93 SEQRES 6 2 247 TYR LYS VAL PRO LYS GLY ALA PHE THR GLY GLU ILE SER 1TPH 94 SEQRES 7 2 247 PRO ALA MET ILE LYS ASP ILE GLY ALA ALA TRP VAL ILE 1TPH 95 SEQRES 8 2 247 LEU GLY HIS SER GLU ARG ARG HIS VAL PHE GLY GLU SER 1TPH 96 SEQRES 9 2 247 ASP GLU LEU ILE GLY GLN LYS VAL ALA HIS ALA LEU ALA 1TPH 97 SEQRES 10 2 247 GLU GLY LEU GLY VAL ILE ALA CYS ILE GLY GLU LYS LEU 1TPH 98 SEQRES 11 2 247 ASP GLU ARG GLU ALA GLY ILE THR GLU LYS VAL VAL PHE 1TPH 99 SEQRES 12 2 247 GLU GLN THR LYS ALA ILE ALA ASP ASN VAL LYS ASP TRP 1TPH 100 SEQRES 13 2 247 SER LYS VAL VAL LEU ALA TYR GLU PRO VAL TRP ALA ILE 1TPH 101 SEQRES 14 2 247 GLY THR GLY LYS THR ALA THR PRO GLN GLN ALA GLN GLU 1TPH 102 SEQRES 15 2 247 VAL HIS GLU LYS LEU ARG GLY TRP LEU LYS THR HIS VAL 1TPH 103 SEQRES 16 2 247 SER ASP ALA VAL ALA GLN SER THR ARG ILE ILE TYR GLY 1TPH 104 SEQRES 17 2 247 GLY SER VAL THR GLY GLY ASN CYS LYS GLU LEU ALA SER 1TPH 105 SEQRES 18 2 247 GLN HIS ASP VAL ASP GLY PHE LEU VAL GLY GLY ALA SER 1TPH 106 SEQRES 19 2 247 LEU LYS PRO GLU PHE VAL ASP ILE ILE ASN ALA LYS HIS 1TPH 107 HET PGH 1 250 10 PHOSPHOGLYCOLOHYDROXAMATE 1TPH 108 HET PGH 2 250 10 PHOSPHOGLYCOLOHYDROXAMATE 1TPH 109 FORMUL 3 PGH 2(C2 H6 N1 O6 P1) 1TPH 110 FORMUL 4 HOH *249(H2 O1) 1TPH 111 HELIX 1 H1 LYS 1 18 GLY 1 30 1 1TPH 112 HELIX 2 H2 LEU 1 48 LYS 1 54 1 1TPH 113 HELIX 3 H3 PRO 1 80 ILE 1 86 1 1TPH 114 HELIX 4 H4 SER 1 96 HIS 1 100 1 1TPH 115 HELIX 5 H5 ASP 1 106 ALA 1 118 1 1TPH 116 HELIX 6 H6 LEU 1 131 GLU 1 135 1 1TPH 117 HELIX 7 H7 THR 1 139 ALA 1 151 1 1TPH 118 HELIX 8 H8 THR 1 175 LEU 1 192 1 1TPH 119 HELIX 9 H9 ASP 1 198 SER 1 203 1 1TPH 120 HELIX 10 H10 CYS 1 217 ALA 1 221 1 1TPH 121 HELIX 11 H11 PHE 1 240 ILE 1 244 1 1TPH 122 HELIX 12 H12 LYS 2 18 GLY 2 30 1 1TPH 123 HELIX 13 H13 LEU 2 48 LYS 2 54 1 1TPH 124 HELIX 14 H14 PRO 2 80 ILE 2 86 1 1TPH 125 HELIX 15 H15 SER 2 96 HIS 2 100 1 1TPH 126 HELIX 16 H16 ASP 2 106 ALA 2 118 1 1TPH 127 HELIX 17 H17 LEU 2 131 GLU 2 135 1 1TPH 128 HELIX 18 H18 THR 2 139 ALA 2 151 1 1TPH 129 HELIX 19 H19 THR 2 175 LEU 2 192 1 1TPH 130 HELIX 20 H20 ASP 2 198 SER 2 203 1 1TPH 131 HELIX 21 H21 CYS 2 217 ALA 2 221 1 1TPH 132 HELIX 22 H22 PHE 2 240 ILE 2 244 1 1TPH 133 SHEET 1 S1 8 PHE 1 6 ASN 1 11 0 1TPH 134 SHEET 2 S1 8 THR 1 37 GLY 1 42 1 1TPH 135 SHEET 3 S1 8 GLY 1 60 ALA 1 63 1 1TPH 136 SHEET 4 S1 8 TRP 1 90 LEU 1 93 1 1TPH 137 SHEET 5 S1 8 GLY 1 122 ILE 1 127 1 1TPH 138 SHEET 6 S1 8 VAL 1 160 TYR 1 164 1 1TPH 139 SHEET 7 S1 8 THR 1 204 ILE 1 206 1 1TPH 140 SHEET 8 S1 8 VAL 1 226 VAL 1 231 1 1TPH 141 SHEET 1 S2 8 PHE 2 6 ASN 2 11 0 1TPH 142 SHEET 2 S2 8 THR 2 37 GLY 2 42 1 1TPH 143 SHEET 3 S2 8 GLY 2 60 ALA 2 63 1 1TPH 144 SHEET 4 S2 8 TRP 2 90 LEU 2 93 1 1TPH 145 SHEET 5 S2 8 GLY 2 122 ILE 2 127 1 1TPH 146 SHEET 6 S2 8 VAL 2 160 TYR 2 164 1 1TPH 147 SHEET 7 S2 8 THR 2 204 ILE 2 206 1 1TPH 148 SHEET 8 S2 8 VAL 2 226 VAL 2 231 1 1TPH 149 SITE 1 ACT 4 GLU 1 165 HIS 1 95 SER 1 96 LYS 1 13 1TPH 150 SITE 1 BCT 4 GLU 2 165 HIS 2 95 SER 2 96 LYS 2 13 1TPH 151 CRYST1 136.400 74.000 57.200 90.00 90.00 90.00 P 21 21 21 8 1TPH 152 ORIGX1 1.000000 0.000000 0.000000 0.00000 1TPH 153 ORIGX2 0.000000 1.000000 0.000000 0.00000 1TPH 154 ORIGX3 0.000000 0.000000 1.000000 0.00000 1TPH 155 SCALE1 0.007331 0.000000 0.000000 0.00000 1TPH 156 SCALE2 0.000000 0.013514 0.000000 0.00000 1TPH 157 SCALE3 0.000000 0.000000 0.017483 0.00000 1TPH 158