HEADER GLYCOSIDASE 01-JUN-94 1XNB 1XNB 2 COMPND XYLANASE (ENDO-1,4-BETA-XYLANASE) (E.C.3.2.1.8) 1XNB 3 SOURCE (BACILLUS CIRCULANS) 1XNB 4 AUTHOR R.L.CAMPBELL 1XNB 5 REVDAT 1 20-DEC-94 1XNB 0 1XNB 6 JRNL AUTH R.L.CAMPBELL,D.R.ROSE,W.W.WAKARCHUK,R.J.TO,W.SUNG, 1XNB 7 JRNL AUTH 2 M.YAGUCHI 1XNB 8 JRNL TITL HIGH-RESOLUTION STRUCTURES OF XYLANASES FROM B. 1XNB 9 JRNL TITL 2 CIRCULANS AND T. HARZIANUM IDENTIFY A NEW FOLDING 1XNB 10 JRNL TITL 3 PATTERN AND IMPLICATIONS FOR THE ATOMIC BASIS OF 1XNB 11 JRNL TITL 4 THE CATALYSIS 1XNB 12 JRNL REF TO BE PUBLISHED 1XNB 13 JRNL REFN 0353 1XNB 14 REMARK 1 1XNB 15 REMARK 2 1XNB 16 REMARK 2 RESOLUTION. 1.49 ANGSTROMS. 1XNB 17 REMARK 3 1XNB 18 REMARK 3 REFINEMENT. 1XNB 19 REMARK 3 PROGRAM X-PLOR 1XNB 20 REMARK 3 AUTHORS BRUNGER 1XNB 21 REMARK 3 R VALUE 0.165 1XNB 22 REMARK 3 RMSD BOND DISTANCES 0.010 ANGSTROMS 1XNB 23 REMARK 3 RMSD BOND ANGLES 1.61 DEGREES 1XNB 24 REMARK 3 RMSD DIHEDRAL ANGLES 26.896 DEGREES 1XNB 25 REMARK 3 RMSD IMPROPER ANGLES 1.190 DEGREES 1XNB 26 REMARK 3 1XNB 27 REMARK 3 NUMBER OF REFLECTIONS 27189 1XNB 28 REMARK 3 RESOLUTION RANGE 8. - 1.49 ANGSTROMS 1XNB 29 REMARK 3 DATA CUTOFF 2. SIGMA(F) 1XNB 30 REMARK 3 PERCENT COMPLETION 90. 1XNB 31 REMARK 3 1XNB 32 REMARK 3 NUMBER OF PROTEIN ATOMS 1448 1XNB 33 REMARK 3 NUMBER OF SOLVENT ATOMS 154 1XNB 34 REMARK 4 1XNB 35 REMARK 4 SITE AS1 (GLU 78, GLU 172) REFERS TO THE CATALYTIC ACIDIC 1XNB 36 REMARK 4 RESIDUES. 1XNB 37 REMARK 5 1XNB 38 REMARK 5 SITE AS2 (TYR 5, TYR 69, TYR 80, TYR 166) REFERS TO THE 1XNB 39 REMARK 5 GROUP OF TYROSINE RESIDUES IN THE ACTIVE SITE THAT APPEAR 1XNB 40 REMARK 5 TO BE IMPORTANT FOR SUBSTRATE BINDING. 1XNB 41 REMARK 6 1XNB 42 REMARK 6 ALL NON-GLYCINE RESIDUES LIE WITHIN THE ALLOWED REGIONS OF 1XNB 43 REMARK 6 A RAMACHANDRAN PLOT EXCEPT ASP 121 AND ALA 165. THE 1XNB 44 REMARK 6 ELECTRON DENSITY FOR BOTH ASP 121 AND ALA 165 IS VERY 1XNB 45 REMARK 6 CLEAR. 1XNB 46 REMARK 7 1XNB 47 REMARK 7 CROSS REFERENCE TO SEQUENCE DATABASE 1XNB 48 REMARK 7 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1XNB 49 REMARK 7 XYNA_BACCI 1XNB 50 SEQRES 1 185 ALA SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY 1XNB 51 SEQRES 2 185 GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR 1XNB 52 SEQRES 3 185 SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY 1XNB 53 SEQRES 4 185 LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN 1XNB 54 SEQRES 5 185 TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR 1XNB 55 SEQRES 6 185 LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU 1XNB 56 SEQRES 7 185 TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR 1XNB 57 SEQRES 8 185 GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR 1XNB 58 SEQRES 9 185 TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER 1XNB 59 SEQRES 10 185 ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER 1XNB 60 SEQRES 11 185 VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR 1XNB 61 SEQRES 12 185 ILE THR PHE THR ASN HIS VAL ASN ALA TRP LYS SER HIS 1XNB 62 SEQRES 13 185 GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET 1XNB 63 SEQRES 14 185 ALA THR GLU GLY TYR GLN SER SER GLY SER SER ASN VAL 1XNB 64 SEQRES 15 185 THR VAL TRP 1XNB 65 FTNOTE 1 1XNB 66 FTNOTE 1 CIS PROLINE - PRO 75 1XNB 67 HET SO4 191 5 SULFATE 1XNB 68 FORMUL 2 SO4 O4 S1 -- 1XNB 69 FORMUL 3 HOH *154(H2 O1) 1XNB 70 HELIX 1 A THR 147 LYS 154 1 1XNB 71 SHEET 1 A 5 ILE 15 GLY 21 0 1XNB 72 SHEET 2 A 5 ASN 25 SER 31 -1 O ASN 25 N GLY 21 1XNB 73 SHEET 3 A 5 GLY 178 VAL 184 -1 N GLY 178 O TRP 30 1XNB 74 SHEET 4 A 5 ARG 49 PRO 60 -1 N ASN 54 O THR 183 1XNB 75 SHEET 5 A 5 ASN 141 PHE 146 -1 N ALA 142 O TYR 53 1XNB 76 SHEET 1 B 5 SER 2 THR 10 0 1XNB 77 SHEET 2 B 5 ASN 35 VAL 38 -1 N VAL 37 O TRP 9 1XNB 78 SHEET 3 B 5 ALA 170 TYR 174 -1 N THR 171 O VAL 38 1XNB 79 SHEET 4 B 5 ASN 63 LEU 66 -1 O ASN 63 N TYR 174 1XNB 80 SHEET 5 B 5 SER 84 GLY 86 -1 N SER 84 O LEU 66 1XNB 81 SHEET 1 C 6 GLY 96 SER 100 0 1XNB 82 SHEET 2 C 6 GLY 103 TYR 113 -1 N GLY 103 O SER 100 1XNB 83 SHEET 3 C 6 PHE 125 VAL 131 -1 N PHE 125 O ARG 112 1XNB 84 SHEET 4 C 6 ILE 77 VAL 81 1 N GLU 78 O THR 126 1XNB 85 SHEET 5 C 6 LEU 68 ARG 73 -1 N LEU 68 O VAL 81 1XNB 86 SHEET 6 C 6 ASN 163 VAL 168 -1 N ASN 163 O ARG 73 1XNB 87 TURN 1 A SER 22 ASN 25 1XNB 88 TURN 2 B SER 100 GLY 103 1XNB 89 TURN 3 C SER 117 GLY 120 1XNB 90 TURN 4 D LYS 154 GLY 157 1XNB 91 SITE 1 AS1 2 GLU 78 GLU 172 1XNB 92 SITE 1 AS2 4 TYR 5 TYR 69 TYR 80 TYR 166 1XNB 93 CRYST1 44.000 52.780 78.390 90.00 90.00 90.00 P 21 21 21 4 1XNB 94 ORIGX1 1.000000 0.000000 0.000000 0.00000 1XNB 95 ORIGX2 0.000000 1.000000 0.000000 0.00000 1XNB 96 ORIGX3 0.000000 0.000000 1.000000 0.00000 1XNB 97 SCALE1 0.022727 0.000000 0.000000 0.00000 1XNB 98 SCALE2 0.000000 0.018947 0.000000 0.00000 1XNB 99 SCALE3 0.000000 0.000000 0.012757 0.00000 1XNB 100