HEADER PLANT SEED PROTEIN 10-SEP-93 1NAR 1NAR 2 COMPND NARBONIN 1NAR 3 SOURCE (VICIA NARBONENSIS L.) 1NAR 4 AUTHOR M.HENNIG,B.SCHLESIER,K.S.WILSON 1NAR 5 REVDAT 1 31-JAN-94 1NAR 0 1NAR 6 JRNL AUTH M.HENNIG,B.SCHLESIER,Z.DAUTER,S.PFEFFER-HENNIG, 1NAR 7 JRNL AUTH 2 V.H.NONG,K.S.WILSON 1NAR 8 JRNL TITL CRYSTAL STRUCTURE OF NARBONIN REFINED AT 1.8 1NAR 9 JRNL TITL 2 ANGSTROMS RESOLUTION 1NAR 10 JRNL REF TO BE PUBLISHED 1NAR 11 JRNL REFN 353 1NAR 12 REMARK 1 1NAR 13 REMARK 1 REFERENCE 1 1NAR 14 REMARK 1 AUTH M.HENNIG,B.SCHLESIER,Z.DAUTER,S.PFEFFER,C.BETZEL, 1NAR 15 REMARK 1 AUTH 2 W.E.HOEHNE,K.S.WILSON 1NAR 16 REMARK 1 TITL A TIM BARREL PROTEIN WITHOUT ENZYMATIC ACTIVITY? 1NAR 17 REMARK 1 TITL 2 CRYSTAL STRUCTURE OF NARBONIN AT 1.8 ANGSTROMS 1NAR 18 REMARK 1 TITL 3 RESOLUTION 1NAR 19 REMARK 1 REF /FEBS$ LETT. V. 306 80 1992 1NAR 20 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 165 1NAR 21 REMARK 1 REFERENCE 2 1NAR 22 REMARK 1 AUTH M.HENNIG,B.SCHLESIER,S.PFEFFER,W.E.HOEHNE 1NAR 23 REMARK 1 TITL NARBONIN, A 2S GLOBULIN FROM VICIA NARBONENSIS L. 1NAR 24 REMARK 1 TITL 2 CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC 1NAR 25 REMARK 1 TITL 3 DATA 1NAR 26 REMARK 1 REF J.MOL.BIOL. V. 215 339 1990 1NAR 27 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1NAR 28 REMARK 2 1NAR 29 REMARK 2 RESOLUTION. 1.8 ANGSTROMS. 1NAR 30 REMARK 3 1NAR 31 REMARK 3 REFINEMENT. 1NAR 32 REMARK 3 PROGRAM PROLSQ 1NAR 33 REMARK 3 AUTHORS KONNERT,HENDRICKSON 1NAR 34 REMARK 3 R VALUE 0.159 1NAR 35 REMARK 3 RMSD BOND DISTANCES 0.015 ANGSTROMS 1NAR 36 REMARK 3 RMSD BOND ANGLES 3.1 DEGREES 1NAR 37 REMARK 3 1NAR 38 REMARK 3 NUMBER OF REFLECTIONS 27227 1NAR 39 REMARK 3 RESOLUTION RANGE 10.0 - 1.8 ANGSTROMS 1NAR 40 REMARK 3 DATA CUTOFF 0.0 SIGMA(F) 1NAR 41 REMARK 3 PER CENT COMPLETION 95.5 1NAR 42 REMARK 3 1NAR 43 REMARK 3 NUMBER OF PROTEIN ATOMS 2333 1NAR 44 REMARK 3 NUMBER OF SOLVENT ATOMS 513 1NAR 45 REMARK 3 1NAR 46 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 1NAR 47 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 1NAR 48 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 1NAR 49 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 1NAR 50 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 1NAR 51 REMARK 3 BOND DISTANCE 0.015(0.020) 1NAR 52 REMARK 3 ANGLE DISTANCE 0.046(0.040) 1NAR 53 REMARK 3 PLANAR 1-4 DISTANCE 0.088(0.050) 1NAR 54 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.014 0.020) 1NAR 55 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.175(0.150) 1NAR 56 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 1NAR 57 REMARK 3 SINGLE TORSION CONTACT 0.173(0.300) 1NAR 58 REMARK 3 MULTIPLE TORSION CONTACT 0.268(0.300) 1NAR 59 REMARK 3 POSSIBLE HYDROGEN BOND 0.230(0.300) 1NAR 60 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 1NAR 61 REMARK 3 PLANAR 17.54(3.000) 1NAR 62 REMARK 3 STAGGERED 16.98(15.00) 1NAR 63 REMARK 3 ORTHONORMAL 22.01(20.00) 1NAR 64 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 1NAR 65 REMARK 3 MAIN-CHAIN BOND 0.835(1.000) 1NAR 66 REMARK 3 MAIN-CHAIN ANGLE 1.433(1.400) 1NAR 67 REMARK 3 SIDE-CHAIN BOND 2.214(2.100) 1NAR 68 REMARK 3 SIDE-CHAIN ANGLE 3.384(2.100) 1NAR 69 REMARK 4 1NAR 70 REMARK 4 THE DATA USED IN THE REFINEMENT WERE COLLECTED FROM A 1NAR 71 REMARK 4 SINGLE CRYSTAL USING SYNCHROTRON RADIATION AND THE IMAGING 1NAR 72 REMARK 4 PLATE DETECTOR AT THE EMBL OUTSTATION IN HAMBURG (GERMANY). 1NAR 73 REMARK 4 PHASES WERE OBTAINED BY MULTIPLE ISOMORPHOUS REPLACEMENT. 1NAR 74 REMARK 5 1NAR 75 REMARK 5 THE AMINO ACID SEQUENCE WAS DETERMINED BY INTERPRETATION 1NAR 76 REMARK 5 OF THE ELECTRON DENSITY (REF. 1). FOR FINAL REFINEMENT THE 1NAR 77 REMARK 5 SEQUENCE WAS CORRECTED AT SEVERAL POSITIONS USING CDNA AND 1NAR 78 REMARK 5 GENOMIC SEQUENCE: SEQUENCE ENTRIES XEMBL: VNNAF6NB, 1NAR 79 REMARK 5 VNNAG2NB, VNNAN21NB. 1NAR 80 REMARK 6 1NAR 81 REMARK 6 THE LAST TWO RESIDUES ARE DISORDERED. RESIDUE 289 IS MODELL 1NAR 82 REMARK 6 AS ALA INSTEAD OF LYS AND 290 ARG IS NOT INCLUDED IN THE MO 1NAR 83 REMARK 7 1NAR 84 REMARK 7 THE SHEET PRESENTED AS *A* ON SHEET RECORDS BELOW IS 1NAR 85 REMARK 7 ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS 1NAR 86 REMARK 7 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST 1NAR 87 REMARK 7 AND LAST STRANDS ARE IDENTICAL. 1NAR 88 SEQRES 1 290 PRO LYS PRO ILE PHE ARG GLU TYR ILE GLY VAL LYS PRO 1NAR 89 SEQRES 2 290 ASN SER THR THR LEU HIS ASP PHE PRO THR GLU ILE ILE 1NAR 90 SEQRES 3 290 ASN THR GLU THR LEU GLU PHE HIS TYR ILE LEU GLY PHE 1NAR 91 SEQRES 4 290 ALA ILE GLU SER TYR TYR GLU SER GLY LYS GLY THR GLY 1NAR 92 SEQRES 5 290 THR PHE GLU GLU SER TRP ASP VAL GLU LEU PHE GLY PRO 1NAR 93 SEQRES 6 290 GLU LYS VAL LYS ASN LEU LYS ARG ARG HIS PRO GLU VAL 1NAR 94 SEQRES 7 290 LYS VAL VAL ILE SER ILE GLY GLY ARG GLY VAL ASN THR 1NAR 95 SEQRES 8 290 PRO PHE ASP PRO ALA GLU GLU ASN VAL TRP VAL SER ASN 1NAR 96 SEQRES 9 290 ALA LYS GLU SER LEU LYS LEU ILE ILE GLN LYS TYR SER 1NAR 97 SEQRES 10 290 ASP ASP SER GLY ASN LEU ILE ASP GLY ILE ASP ILE HIS 1NAR 98 SEQRES 11 290 TYR GLU HIS ILE ARG SER ASP GLU PRO PHE ALA THR LEU 1NAR 99 SEQRES 12 290 MET GLY GLN LEU ILE THR GLU LEU LYS LYS ASP ASP ASP 1NAR 100 SEQRES 13 290 LEU ASN ILE ASN VAL VAL SER ILE ALA PRO SER GLU ASN 1NAR 101 SEQRES 14 290 ASN SER SER HIS TYR GLN LYS LEU TYR ASN ALA LYS LYS 1NAR 102 SEQRES 15 290 ASP TYR ILE ASN TRP VAL ASP TYR GLN PHE SER ASN GLN 1NAR 103 SEQRES 16 290 GLN LYS PRO VAL SER THR ASP ASP ALA PHE VAL GLU ILE 1NAR 104 SEQRES 17 290 PHE LYS SER LEU GLU LYS ASP TYR HIS PRO HIS LYS VAL 1NAR 105 SEQRES 18 290 LEU PRO GLY PHE SER THR ASP PRO LEU ASP THR LYS HIS 1NAR 106 SEQRES 19 290 ASN LYS ILE THR ARG ASP ILE PHE ILE GLY GLY CYS THR 1NAR 107 SEQRES 20 290 ARG LEU VAL GLN THR PHE SER LEU PRO GLY VAL PHE PHE 1NAR 108 SEQRES 21 290 TRP ASN ALA ASN ASP SER VAL ILE PRO LYS ARG ASP GLY 1NAR 109 SEQRES 22 290 ASP LYS PRO PHE ILE VAL GLU LEU THR LEU GLN GLN LEU 1NAR 110 SEQRES 23 290 LEU ALA ALA ARG 1NAR 111 FTNOTE 1 1NAR 112 FTNOTE 1 GLY 38 - PHE 39 OMEGA = 9.34 1NAR 113 FTNOTE 1 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1NAR 114 FTNOTE 2 1NAR 115 FTNOTE 2 CIS PROLINE - PRO 139 1NAR 116 FTNOTE 3 1NAR 117 FTNOTE 3 TRP 261 - ASN 262 OMEGA = 12.67 1NAR 118 FTNOTE 3 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1NAR 119 FORMUL 2 HOH *513(H2 O1) 1NAR 120 HELIX 1 1 PRO 65 ARG 74 1 1NAR 121 HELIX 2 2 TRP 101 LYS 115 1 1NAR 122 HELIX 3 3 PHE 140 LYS 153 1 1NAR 123 HELIX 4 4 SER 171 ALA 180 1 1NAR 124 HELIX 5 5 ASP 202 ASP 215 1 1NAR 125 HELIX 6 6 PRO 229 HIS 234 5 1NAR 126 HELIX 7 7 ARG 239 GLN 251 1 1NAR 127 HELIX 8 8 ALA 263 SER 266 5 1NAR 128 HELIX 9 9 ILE 278 ALA 288 1 1NAR 129 SHEET 1 A 9 ILE 4 ILE 9 0 1NAR 130 SHEET 2 A 9 GLU 32 LEU 37 1 1NAR 131 SHEET 3 A 9 LYS 79 GLY 86 1 1NAR 132 SHEET 4 A 9 GLY 126 TYR 131 1 1NAR 133 SHEET 5 A 9 VAL 161 ILE 164 1 1NAR 134 SHEET 6 A 9 TRP 187 GLN 191 1 1NAR 135 SHEET 7 A 9 VAL 221 SER 226 1 1NAR 136 SHEET 8 A 9 GLY 257 TRP 261 1 1NAR 137 SHEET 9 A 9 ILE 4 ILE 9 1 1NAR 138 SHEET 1 B 2 GLY 38 TYR 44 0 1NAR 139 SHEET 2 B 2 GLY 50 GLU 56 -1 1NAR 140 SHEET 1 C 2 SER 117 ASP 118 0 1NAR 141 SHEET 2 C 2 GLY 121 ASN 122 -1 1NAR 142 TURN 1 T1 LYS 12 SER 15 TYPE I 1NAR 143 TURN 2 T2 THR 23 ILE 26 TYPE I 1NAR 144 TURN 3 T3 TYR 45 GLY 48 TYPE I 1NAR 145 TURN 4 T4 VAL 60 PHE 63 TYPE III 1NAR 146 TURN 5 T5 HIS 75 VAL 78 TYPE I 1NAR 147 TURN 6 T6 GLY 88 THR 91 TYPE I 1NAR 148 TURN 7 T7 GLU 97 VAL 100 TYPE I 1NAR 149 TURN 8 T8 ASP 118 GLY 121 TYPE I 1NAR 150 TURN 9 T9 SER 167 ASN 170 TYPE III 1NAR 151 TURN 10 T10 LYS 181 TYR 184 TYPE III 1NAR 152 TURN 11 T11 GLN 191 ASN 194 TYPE III 1NAR 153 TURN 12 T12 PHE 192 GLN 195 TYPE I 1NAR 154 TURN 13 T13 HIS 217 LYS 220 TYPE II 1NAR 155 TURN 14 T14 ARG 271 ASP 274 TYPE II 1NAR 156 TURN 15 T15 LYS 275 ILE 278 TYPE II 1NAR 157 CRYST1 46.900 75.500 50.900 90.00 120.50 90.00 P 21 2 1NAR 158 ORIGX1 1.000000 0.000000 0.000000 0.00000 1NAR 159 ORIGX2 0.000000 1.000000 0.000000 0.00000 1NAR 160 ORIGX3 0.000000 0.000000 1.000000 0.00000 1NAR 161 SCALE1 0.021322 0.000000 0.012560 0.00000 1NAR 162 SCALE2 0.000000 0.013245 0.000000 0.00000 1NAR 163 SCALE3 0.000000 0.000000 0.022801 0.00000 1NAR 164