HEADER HYDROLASE 13-JUL-94 2SIL 2SIL 2 COMPND SIALIDASE (E.C.3.2.1.18) (NEURAMINIDASE) 2SIL 3 SOURCE (SALMONELLA TYPHIMURIUM, LT2) EXPRESSION_SYSTEM: 2SIL 4 SOURCE 2 (ESCHERICHIA COLI) GENE: PSX62 2SIL 5 AUTHOR G.L.TAYLOR,S.J.CRENNELL,E.F.GARMAN,E.R.VIMR,W.G.LAVER 2SIL 6 REVDAT 1 31-AUG-94 2SIL 0 2SIL 7 SPRSDE 31-AUG-94 2SIL 1SIL 2SIL 8 JRNL AUTH S.J.CRENNELL,E.F.GARMAN,W.G.LAVER,E.R.VIMR, 2SIL 9 JRNL AUTH 2 G.L.TAYLOR 2SIL 10 JRNL TITL THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2 2SIL 11 JRNL TITL 2 NEURAMINIDASE AND ITS COMPLEX WITH A TRANSITION 2SIL 12 JRNL TITL 3 STATE ANALOGUE AT 1.6 ANGSTROMS RESOLUTION 2SIL 13 JRNL REF TO BE PUBLISHED 2SIL 14 JRNL REFN 0353 2SIL 15 REMARK 1 2SIL 16 REMARK 1 REFERENCE 1 2SIL 17 REMARK 1 AUTH S.J.CRENNELL,E.F.GARMAN,W.G.LAVER,E.R.VIMR, 2SIL 18 REMARK 1 AUTH 2 G.L.TAYLOR 2SIL 19 REMARK 1 TITL CRYSTAL STRUCTURE OF A BACTERIAL SIALIDASE (FROM 2SIL 20 REMARK 1 TITL 2 SALMONELLA TYPHIMURIUM LT2) SHOWS THE SAME FOLD AS 2SIL 21 REMARK 1 TITL 3 AN INFLUENZA VIRUS NEURAMINIDASE 2SIL 22 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 90 9852 1993 2SIL 23 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 0040 2SIL 24 REMARK 1 REFERENCE 2 2SIL 25 REMARK 1 AUTH G.L.TAYLOR,E.R.VIMR,E.F.GARMAN,W.G.LAVER 2SIL 26 REMARK 1 TITL PURIFICATION, CRYSTALLISATION AND PRELIMINARY 2SIL 27 REMARK 1 TITL 2 CRYSTALLOGRAPHIC STUDY OF NEURAMINIDASE FROM VIBRIO 2SIL 28 REMARK 1 TITL 3 CHOLERAE AND SALMONELLA TYPHIMURIUM 2SIL 29 REMARK 1 REF J.MOL.BIOL. V. 226 1287 1992 2SIL 30 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 2SIL 31 REMARK 2 2SIL 32 REMARK 2 RESOLUTION. 1.6 ANGSTROMS. 2SIL 33 REMARK 3 2SIL 34 REMARK 3 REFINEMENT. 2SIL 35 REMARK 3 PROGRAM 1 X-PLOR 2SIL 36 REMARK 3 AUTHORS 1 BRUNGER 2SIL 37 REMARK 3 PROGRAM 2 TNT 2SIL 38 REMARK 3 AUTHORS 2 TRONRUD,TEN EYCK,MATTHEWS 2SIL 39 REMARK 3 R VALUE 0.166 2SIL 40 REMARK 3 MEAN B VALUE 16.4 ANGSTROMS**2 2SIL 41 REMARK 3 ESD FROM LUZZATI PLOT 0.16 ANGSTROMS 2SIL 42 REMARK 3 FINAL RMS COORD. SHIFT 0.011 ANGSTROMS 2SIL 43 REMARK 3 RMSD BOND DISTANCES 0.014 ANGSTROMS 2SIL 44 REMARK 3 RMSD BOND ANGLES 3.17 DEGREES 2SIL 45 REMARK 3 RMSD PLANAR 1-4 DISTANCE 0.017 ANGSTROMS 2SIL 46 REMARK 3 NUMBER OF REFLECTIONS 35140 2SIL 47 REMARK 3 RESOLUTION RANGE 6.0 - 1.6 ANGSTROMS 2SIL 48 REMARK 3 DATA CUTOFF 0. SIGMA(F) 2SIL 49 REMARK 3 2SIL 50 REMARK 3 DATA COLLECTION. 2SIL 51 REMARK 3 NUMBER OF UNIQUE REFLECTIONS 59728 2SIL 52 REMARK 3 COMPLETENESS OF DATA 55.9 % 2SIL 53 REMARK 3 REJECTION CRITERIA 3. SIGMA(I) 2SIL 54 REMARK 3 2SIL 55 REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 2SIL 56 REMARK 3 NUMBER OF PROTEIN ATOMS 2954 2SIL 57 REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 2SIL 58 REMARK 3 NUMBER OF HETEROGEN ATOMS 0 2SIL 59 REMARK 3 NUMBER OF SOLVENT ATOMS 195 2SIL 60 REMARK 3 2SIL 61 REMARK 3 THE WEIGHTS USED IN THE TNT REFINEMENT WERE: 2SIL 62 REMARK 3 BOND 1 ANGLE 1 TORSION 1 TRIGONAL 1 2SIL 63 REMARK 3 PLANE 10 CONTACT 10 2SIL 64 REMARK 4 2SIL 65 REMARK 4 THE RESIDUES PRESENTED ON THE *ACT* SITE RECORDS BELOW 2SIL 66 REMARK 4 COMPRISE THE ACTIVE (CATALYTIC/BINDING) SITE OF THE 2SIL 67 REMARK 4 MOLECULE. 2SIL 68 REMARK 5 2SIL 69 REMARK 5 CROSS REFERENCE TO SEQUENCE DATABASE 2SIL 70 REMARK 5 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 2SIL 71 REMARK 5 NANH_SALTY 2SIL 72 REMARK 5 2SIL 73 REMARK 5 SEQUENCE ADVISORY NOTICE 2SIL 74 REMARK 5 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 2SIL 75 REMARK 5 2SIL 76 REMARK 5 SWISS-PROT ENTRY NAME: NANH_SALTY 2SIL 77 REMARK 5 2SIL 78 REMARK 5 SWISS-PROT RESIDUE PDB SEQRES 2SIL 79 REMARK 5 2SIL 80 REMARK 5 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 2SIL 81 REMARK 5 ALA 328 ASP 329 2SIL 82 REMARK 6 2SIL 83 REMARK 6 THE FOLLOWING SOLVENT MOLECULES LIE OUTSIDE THE NORMAL 2SIL 84 REMARK 6 HYDROGEN BONDING SPHERE AND MAY BE ASSOCIATED WITH A 2SIL 85 REMARK 6 SYMMETRY-RELATED PROTEIN/NUCLEIC ACID MOLECULE (M=MODEL 2SIL 86 REMARK 6 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SEQ=SEQUENCE 2SIL 87 REMARK 6 NUMBER; I=INSERTION CODE): 2SIL 88 REMARK 6 2SIL 89 REMARK 6 M RES C SEQI 2SIL 90 REMARK 6 HOH 523 DISTANCE = 7.115 2SIL 91 REMARK 6 HOH 520 DISTANCE = 4.270 2SIL 92 REMARK 6 HOH 519 DISTANCE = 3.747 2SIL 93 REMARK 6 HOH 613 DISTANCE = 3.609 2SIL 94 REMARK 6 HOH 580 DISTANCE = 3.535 2SIL 95 REMARK 6 HOH 554 DISTANCE = 3.522 2SIL 96 SEQRES 1 381 THR VAL GLU LYS SER VAL VAL PHE LYS ALA GLU GLY GLU 2SIL 97 SEQRES 2 381 HIS PHE THR ASP GLN LYS GLY ASN THR ILE VAL GLY SER 2SIL 98 SEQRES 3 381 GLY SER GLY GLY THR THR LYS TYR PHE ARG ILE PRO ALA 2SIL 99 SEQRES 4 381 MET CYS THR THR SER LYS GLY THR ILE VAL VAL PHE ALA 2SIL 100 SEQRES 5 381 ASP ALA ARG HIS ASN THR ALA SER ASP GLN SER PHE ILE 2SIL 101 SEQRES 6 381 ASP THR ALA ALA ALA ARG SER THR ASP GLY GLY LYS THR 2SIL 102 SEQRES 7 381 TRP ASN LYS LYS ILE ALA ILE TYR ASN ASP ARG VAL ASN 2SIL 103 SEQRES 8 381 SER LYS LEU SER ARG VAL MET ASP PRO THR CYS ILE VAL 2SIL 104 SEQRES 9 381 ALA ASN ILE GLN GLY ARG GLU THR ILE LEU VAL MET VAL 2SIL 105 SEQRES 10 381 GLY LYS TRP ASN ASN ASN ASP LYS THR TRP GLY ALA TYR 2SIL 106 SEQRES 11 381 ARG ASP LYS ALA PRO ASP THR ASP TRP ASP LEU VAL LEU 2SIL 107 SEQRES 12 381 TYR LYS SER THR ASP ASP GLY VAL THR PHE SER LYS VAL 2SIL 108 SEQRES 13 381 GLU THR ASN ILE HIS ASP ILE VAL THR LYS ASN GLY THR 2SIL 109 SEQRES 14 381 ILE SER ALA MET LEU GLY GLY VAL GLY SER GLY LEU GLN 2SIL 110 SEQRES 15 381 LEU ASN ASP GLY LYS LEU VAL PHE PRO VAL GLN MET VAL 2SIL 111 SEQRES 16 381 ARG THR LYS ASN ILE THR THR VAL LEU ASN THR SER PHE 2SIL 112 SEQRES 17 381 ILE TYR SER THR ASP GLY ILE THR TRP SER LEU PRO SER 2SIL 113 SEQRES 18 381 GLY TYR CYS GLU GLY PHE GLY SER GLU ASN ASN ILE ILE 2SIL 114 SEQRES 19 381 GLU PHE ASN ALA SER LEU VAL ASN ASN ILE ARG ASN SER 2SIL 115 SEQRES 20 381 GLY LEU ARG ARG SER PHE GLU THR LYS ASP PHE GLY LYS 2SIL 116 SEQRES 21 381 THR TRP THR GLU PHE PRO PRO MET ASP LYS LYS VAL ASP 2SIL 117 SEQRES 22 381 ASN ARG ASN HIS GLY VAL GLN GLY SER THR ILE THR ILE 2SIL 118 SEQRES 23 381 PRO SER GLY ASN LYS LEU VAL ALA ALA HIS SER SER ALA 2SIL 119 SEQRES 24 381 GLN ASN LYS ASN ASN ASP TYR THR ARG SER ASP ILE SER 2SIL 120 SEQRES 25 381 LEU TYR ALA HIS ASN LEU TYR SER GLY GLU VAL LYS LEU 2SIL 121 SEQRES 26 381 ILE ASP ASP PHE TYR PRO LYS VAL GLY ASN ALA SER GLY 2SIL 122 SEQRES 27 381 ALA GLY TYR SER CYS LEU SER TYR ARG LYS ASN VAL ASP 2SIL 123 SEQRES 28 381 LYS GLU THR LEU TYR VAL VAL TYR GLU ALA ASN GLY SER 2SIL 124 SEQRES 29 381 ILE GLU PHE GLN ASP LEU SER ARG HIS LEU PRO VAL ILE 2SIL 125 SEQRES 30 381 LYS SER TYR ASN 2SIL 126 FTNOTE 1 2SIL 127 FTNOTE 1 CIS PROLINE - PRO 136 2SIL 128 FORMUL 2 HOH *195(H2 O1) 2SIL 129 SSBOND 1 CYS 42 CYS 103 2SIL 130 SITE 1 ACT 13 ARG 37 ARG 56 ASP 62 MET 99 2SIL 131 SITE 2 ACT 13 ASP 100 TRP 121 TRP 128 LEU 175 2SIL 132 SITE 3 ACT 13 GLU 231 ARG 246 ARG 309 TYR 342 2SIL 133 SITE 4 ACT 13 GLU 361 2SIL 134 CRYST1 47.500 82.500 91.900 90.00 90.00 90.00 P 21 21 21 4 2SIL 135 ORIGX1 1.000000 0.000000 0.000000 0.00000 2SIL 136 ORIGX2 0.000000 1.000000 0.000000 0.00000 2SIL 137 ORIGX3 0.000000 0.000000 1.000000 0.00000 2SIL 138 SCALE1 0.021053 0.000000 0.000000 0.00000 2SIL 139 SCALE2 0.000000 0.012121 0.000000 0.00000 2SIL 140 SCALE3 0.000000 0.000000 0.010881 0.00000 2SIL 141