HEADER HYDROLASE 12-OCT-93 1GHS 1GHS 2 COMPND 1,3-BETA-GLUCANASE (E.C.3.2.1.39) 1GHS 3 COMPND 2 (1,3-BETA-D-GLUCAN ENDOHYDROLASE, ISOZYME II) 1GHS 4 SOURCE GERMINATED BARLEY GRAIN (HORDEUM VULGARE) 1GHS 5 AUTHOR T.P.J.GARRETT,J.N.VARGHESE 1GHS 6 REVDAT 1 01-NOV-94 1GHS 0 1GHS 7 JRNL AUTH J.N.VARGHESE,T.P.J.GARRETT,P.M.COLMAN,L.CHEN, 1GHS 8 JRNL AUTH 2 P.J.HOJ,G.B.FINCHER 1GHS 9 JRNL TITL THE THREE-DIMENSIONAL STRUCTURES OF TWO PLANT 1GHS 10 JRNL TITL 2 BETA-GLUCAN ENDOHYDROLASES WITH DISTINCT SUBSTRATE 1GHS 11 JRNL TITL 3 SPECIFICITIES 1GHS 12 JRNL REF PROC.NAT.ACAD.SCI.USA V. 91 2785 1994 1GHS 13 JRNL REFN ASTM PNASA6 US ISSN 0027-8424 0040 1GHS 14 REMARK 1 1GHS 15 REMARK 1 REFERENCE 1 1GHS 16 REMARK 1 AUTH L.CHEN,T.P.J.GARRETT,J.N.VARGHESE,G.B.FINCHER, 1GHS 17 REMARK 1 AUTH 2 P.B.HOJ 1GHS 18 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF 1GHS 19 REMARK 1 TITL 2 (1,3)- AND (1,3;1,4)-BETA--D-GLUCANASES FROM 1GHS 20 REMARK 1 TITL 3 GERMINATING BARLEY 1GHS 21 REMARK 1 REF J.MOL.BIOL. V. 234 888 1993 1GHS 22 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1GHS 23 REMARK 1 REFERENCE 2 1GHS 24 REMARK 1 AUTH L.CHEN,G.B.FINCHER,P.J.HOJ 1GHS 25 REMARK 1 TITL EVOLUTION OF POLYSACCHARIDE HYDROLASE SUBSTRATE 1GHS 26 REMARK 1 TITL 2 SPECIFICITY 1GHS 27 REMARK 1 REF J.BIOL.CHEM. V. 268 13318 1993 1GHS 28 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1GHS 29 REMARK 2 1GHS 30 REMARK 2 RESOLUTION. 2.3 ANGSTROMS. 1GHS 31 REMARK 3 1GHS 32 REMARK 3 REFINEMENT. 1GHS 33 REMARK 3 PROGRAM X-PLOR 1GHS 34 REMARK 3 AUTHORS BRUNGER 1GHS 35 REMARK 3 R VALUE 0.179 1GHS 36 REMARK 3 RMSD BOND DISTANCES 0.013 ANGSTROMS 1GHS 37 REMARK 3 RMSD BOND ANGLE 1.68 DEGREES 1GHS 38 REMARK 3 1GHS 39 REMARK 3 NUMBER OF REFLECTIONS 22811 1GHS 40 REMARK 3 RESOLUTION RANGE 6.0 - 2.3 ANGSTROMS 1GHS 41 REMARK 3 DATA CUTOFF 4.0 SIGMA(F) 1GHS 42 REMARK 3 PERCENT COMPLETION 78.4 1GHS 43 REMARK 3 1GHS 44 REMARK 3 NUMBER OF PROTEIN ATOMS 4564 1GHS 45 REMARK 3 NUMBER OF SOLVENT ATOMS 59 1GHS 46 REMARK 4 1GHS 47 REMARK 4 THERE ARE TWO MOLECULES IN THE ASYMMETRIC UNIT. 1GHS 48 REMARK 4 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL 1GHS 49 REMARK 4 YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED TO 1GHS 50 REMARK 4 CHAIN *B*. THE RMS DEVIATION IN CA POSITIONS IS 0.30 1GHS 51 REMARK 4 ANGSTROMS. 1GHS 52 REMARK 5 1GHS 53 REMARK 5 CIS PEPTIDES WERE OBSERVED IN THE ELECTRON DENSITY BETWEEN 1GHS 54 REMARK 5 RESIDUES PHE 274 AND ALA 275 FOR EACH MOLECULE. 1GHS 55 REMARK 6 1GHS 56 REMARK 6 THIS DEPOSITION CORRESPONDS TO THE INITIAL STRUCTURE 1GHS 57 REMARK 6 REPORT. DIFFRACTION DATA EXTEND TO ABOUT 1.8 A. 1GHS 58 REMARK 7 1GHS 59 REMARK 7 CROSS REFERENCE TO SEQUENCE DATABASE 1GHS 60 REMARK 7 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1GHS 61 REMARK 7 E13B_HORVU A 1GHS 62 REMARK 7 E13B_HORVU B 1GHS 63 SEQRES 1 A 306 ILE GLY VAL CYS TYR GLY VAL ILE GLY ASN ASN LEU PRO 1GHS 64 SEQRES 2 A 306 SER ARG SER ASP VAL VAL GLN LEU TYR ARG SER LYS GLY 1GHS 65 SEQRES 3 A 306 ILE ASN GLY MET ARG ILE TYR PHE ALA ASP GLY GLN ALA 1GHS 66 SEQRES 4 A 306 LEU SER ALA LEU ARG ASN SER GLY ILE GLY LEU ILE LEU 1GHS 67 SEQRES 5 A 306 ASP ILE GLY ASN ASP GLN LEU ALA ASN ILE ALA ALA SER 1GHS 68 SEQRES 6 A 306 THR SER ASN ALA ALA SER TRP VAL GLN ASN ASN VAL ARG 1GHS 69 SEQRES 7 A 306 PRO TYR TYR PRO ALA VAL ASN ILE LYS TYR ILE ALA ALA 1GHS 70 SEQRES 8 A 306 GLY ASN GLU VAL GLN GLY GLY ALA THR GLN SER ILE LEU 1GHS 71 SEQRES 9 A 306 PRO ALA MET ARG ASN LEU ASN ALA ALA LEU SER ALA ALA 1GHS 72 SEQRES 10 A 306 GLY LEU GLY ALA ILE LYS VAL SER THR SER ILE ARG PHE 1GHS 73 SEQRES 11 A 306 ASP GLU VAL ALA ASN SER PHE PRO PRO SER ALA GLY VAL 1GHS 74 SEQRES 12 A 306 PHE LYS ASN ALA TYR MET THR ASP VAL ALA ARG LEU LEU 1GHS 75 SEQRES 13 A 306 ALA SER THR GLY ALA PRO LEU LEU ALA ASN VAL TYR PRO 1GHS 76 SEQRES 14 A 306 TYR PHE ALA TYR ARG ASP ASN PRO GLY SER ILE SER LEU 1GHS 77 SEQRES 15 A 306 ASN TYR ALA THR PHE GLN PRO GLY THR THR VAL ARG ASP 1GHS 78 SEQRES 16 A 306 GLN ASN ASN GLY LEU THR TYR THR SER LEU PHE ASP ALA 1GHS 79 SEQRES 17 A 306 MET VAL ASP ALA VAL TYR ALA ALA LEU GLU LYS ALA GLY 1GHS 80 SEQRES 18 A 306 ALA PRO ALA VAL LYS VAL VAL VAL SER GLU SER GLY TRP 1GHS 81 SEQRES 19 A 306 PRO SER ALA GLY GLY PHE ALA ALA SER ALA GLY ASN ALA 1GHS 82 SEQRES 20 A 306 ARG THR TYR ASN GLN GLY LEU ILE ASN HIS VAL GLY GLY 1GHS 83 SEQRES 21 A 306 GLY THR PRO LYS LYS ARG GLU ALA LEU GLU THR TYR ILE 1GHS 84 SEQRES 22 A 306 PHE ALA MET PHE ASN GLU ASN GLN LYS THR GLY ASP ALA 1GHS 85 SEQRES 23 A 306 THR GLU ARG SER PHE GLY LEU PHE ASN PRO ASP LYS SER 1GHS 86 SEQRES 24 A 306 PRO ALA TYR ASN ILE GLN PHE 1GHS 87 SEQRES 1 B 306 ILE GLY VAL CYS TYR GLY VAL ILE GLY ASN ASN LEU PRO 1GHS 88 SEQRES 2 B 306 SER ARG SER ASP VAL VAL GLN LEU TYR ARG SER LYS GLY 1GHS 89 SEQRES 3 B 306 ILE ASN GLY MET ARG ILE TYR PHE ALA ASP GLY GLN ALA 1GHS 90 SEQRES 4 B 306 LEU SER ALA LEU ARG ASN SER GLY ILE GLY LEU ILE LEU 1GHS 91 SEQRES 5 B 306 ASP ILE GLY ASN ASP GLN LEU ALA ASN ILE ALA ALA SER 1GHS 92 SEQRES 6 B 306 THR SER ASN ALA ALA SER TRP VAL GLN ASN ASN VAL ARG 1GHS 93 SEQRES 7 B 306 PRO TYR TYR PRO ALA VAL ASN ILE LYS TYR ILE ALA ALA 1GHS 94 SEQRES 8 B 306 GLY ASN GLU VAL GLN GLY GLY ALA THR GLN SER ILE LEU 1GHS 95 SEQRES 9 B 306 PRO ALA MET ARG ASN LEU ASN ALA ALA LEU SER ALA ALA 1GHS 96 SEQRES 10 B 306 GLY LEU GLY ALA ILE LYS VAL SER THR SER ILE ARG PHE 1GHS 97 SEQRES 11 B 306 ASP GLU VAL ALA ASN SER PHE PRO PRO SER ALA GLY VAL 1GHS 98 SEQRES 12 B 306 PHE LYS ASN ALA TYR MET THR ASP VAL ALA ARG LEU LEU 1GHS 99 SEQRES 13 B 306 ALA SER THR GLY ALA PRO LEU LEU ALA ASN VAL TYR PRO 1GHS 100 SEQRES 14 B 306 TYR PHE ALA TYR ARG ASP ASN PRO GLY SER ILE SER LEU 1GHS 101 SEQRES 15 B 306 ASN TYR ALA THR PHE GLN PRO GLY THR THR VAL ARG ASP 1GHS 102 SEQRES 16 B 306 GLN ASN ASN GLY LEU THR TYR THR SER LEU PHE ASP ALA 1GHS 103 SEQRES 17 B 306 MET VAL ASP ALA VAL TYR ALA ALA LEU GLU LYS ALA GLY 1GHS 104 SEQRES 18 B 306 ALA PRO ALA VAL LYS VAL VAL VAL SER GLU SER GLY TRP 1GHS 105 SEQRES 19 B 306 PRO SER ALA GLY GLY PHE ALA ALA SER ALA GLY ASN ALA 1GHS 106 SEQRES 20 B 306 ARG THR TYR ASN GLN GLY LEU ILE ASN HIS VAL GLY GLY 1GHS 107 SEQRES 21 B 306 GLY THR PRO LYS LYS ARG GLU ALA LEU GLU THR TYR ILE 1GHS 108 SEQRES 22 B 306 PHE ALA MET PHE ASN GLU ASN GLN LYS THR GLY ASP ALA 1GHS 109 SEQRES 23 B 306 THR GLU ARG SER PHE GLY LEU PHE ASN PRO ASP LYS SER 1GHS 110 SEQRES 24 B 306 PRO ALA TYR ASN ILE GLN PHE 1GHS 111 FTNOTE 1 1GHS 112 FTNOTE 1 CIS PROLINE - PRO A 82 1GHS 113 FTNOTE 2 1GHS 114 FTNOTE 2 CIS PROLINE - PRO A 138 1GHS 115 FTNOTE 3 1GHS 116 FTNOTE 3 PHE A 274 - ALA A 275 OMEGA = 0.24 1GHS 117 FTNOTE 3 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1GHS 118 FTNOTE 4 1GHS 119 FTNOTE 4 CIS PROLINE - PRO B 82 1GHS 120 FTNOTE 5 1GHS 121 FTNOTE 5 CIS PROLINE - PRO B 138 1GHS 122 FTNOTE 6 1GHS 123 FTNOTE 6 PHE B 274 - ALA B 275 OMEGA = 0.07 1GHS 124 FTNOTE 6 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1GHS 125 FORMUL 3 HOH *59(H2 O1) 1GHS 126 CRYST1 86.900 86.900 156.000 90.00 90.00 120.00 P 32 2 1 12 1GHS 127 ORIGX1 1.000000 0.000000 0.000000 0.00000 1GHS 128 ORIGX2 0.000000 1.000000 0.000000 0.00000 1GHS 129 ORIGX3 0.000000 0.000000 1.000000 0.00000 1GHS 130 SCALE1 0.011507 0.006644 0.000000 0.00000 1GHS 131 SCALE2 0.000000 0.013288 0.000000 0.00000 1GHS 132 SCALE3 0.000000 0.000000 0.006410 0.00000 1GHS 133 MTRIX1 1 0.492900 0.869200 -0.039400 35.18700 1 1GHS 134 MTRIX2 1 -0.869800 0.490900 -0.050300 44.84000 1 1GHS 135 MTRIX3 1 -0.024300 0.059100 0.998000 40.35400 1 1GHS 136