HEADER TOXIN 22-JUN-94 1DLC 1DLC 2 COMPND DELTA-ENDOTOXIN CRYIIIA (BT13) 1DLC 3 SOURCE (BACILLUS THURINGIENSIS, SUBSPECIES TENEBRIONIS) 1DLC 4 AUTHOR J.LI 1DLC 5 REVDAT 1 30-SEP-94 1DLC 0 1DLC 6 REMARK 1 1DLC 7 REMARK 1 REFERENCE 1 1DLC 8 REMARK 1 AUTH J.LI,J.CARROLL,D.J.ELLAR 1DLC 9 REMARK 1 TITL CRYSTAL STRUCTURE OF INSECTICIDAL DELTA-ENDOTOXIN 1DLC 10 REMARK 1 TITL 2 FROM BACILLUS THURINGIENSIS AT 2.5 ANGSTROMS 1DLC 11 REMARK 1 TITL 3 RESOLUTION 1DLC 12 REMARK 1 REF NATURE V. 353 815 1991 1DLC 13 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006 1DLC 14 REMARK 1 REFERENCE 2 1DLC 15 REMARK 1 AUTH J.LI,R.HENDERSON,J.CARROLL,D.ELLAR 1DLC 16 REMARK 1 TITL X-RAY ANALYSIS OF THE CRYSTALLINE PARASPORAL 1DLC 17 REMARK 1 TITL 2 INCLUSION IN BACILLUS THURINGIENSIS VAR. 1DLC 18 REMARK 1 TITL 3 TENEBRIONIS 1DLC 19 REMARK 1 REF J.MOL.BIOL. V. 199 543 1988 1DLC 20 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1DLC 21 REMARK 2 1DLC 22 REMARK 2 RESOLUTION. 2.5 ANGSTROMS. 1DLC 23 REMARK 3 1DLC 24 REMARK 3 REFINEMENT. 1DLC 25 REMARK 3 PROGRAM X-PLOR 1DLC 26 REMARK 3 AUTHORS BRUNGER 1DLC 27 REMARK 3 R VALUE 0.183 1DLC 28 REMARK 3 RMSD BOND DISTANCES 0.011 ANGSTROMS 1DLC 29 REMARK 3 RMSD BOND ANGLES 1.58 DEGREES 1DLC 30 REMARK 3 RMSD DIHEDRAL ANGLES 25.06 DEGREES 1DLC 31 REMARK 3 RMSD IMPROPER ROTATION 1.471 DEGREES 1DLC 32 REMARK 3 1DLC 33 REMARK 3 NUMBER OF REFLECTIONS 27726 1DLC 34 REMARK 3 RESOLUTION RANGE 16.0 - 2.5 ANGSTROMS 1DLC 35 REMARK 3 DATA CUTOFF 0.0 SIGMA(F) 1DLC 36 REMARK 3 PERCENT COMPLETION 100. 1DLC 37 REMARK 3 1DLC 38 REMARK 3 NUMBER OF PROTEIN ATOMS 4697 1DLC 39 REMARK 3 NUMBER OF SOLVENT ATOMS 106 1DLC 40 REMARK 3 1DLC 41 REMARK 3 THE ATOMIC MODEL INCLUDES RESIDUES 61 - 644 OF THE PROTEIN 1DLC 42 REMARK 3 AND 106 BOUND WATER MOLECULES. BULK SOLVENT CONTRIBUTION 1DLC 43 REMARK 3 TO THE STRUCTURE FACTOR WAS CALCULATED USING THE CCP4 1DLC 44 REMARK 3 PROGRAM SFALL AND INCLUDED IN THIS REFINEMENT. 1DLC 45 REMARK 3 1DLC 46 REMARK 4 1DLC 47 REMARK 4 CRYIIIA BELONGS TO THE "CRY" FAMILY OF DELTA-ENDOTOXINS, 1DLC 48 REMARK 4 WHICH ARE PORE-FORMING INSECTICIDAL PROTEIN TOXINS 1DLC 49 REMARK 4 CONTAINED IN THE CRYSTALLINE PARASPORAL INCLUSIONS OF 1DLC 50 REMARK 4 BACILLUS THURINGIENSIS. THE SUBCLASS III IS TOXIC 1DLC 51 REMARK 4 SPECIFICALLY TO COLEOPTERAN INSECTS, I.E., BEETLES. THEY 1DLC 52 REMARK 4 FUNCTION BY BINDING TO MIDGUT EPITHELIAL CELLS AND INDUCE 1DLC 53 REMARK 4 COLLOIDOSMOTIC LYSIS. 1DLC 54 REMARK 5 1DLC 55 REMARK 5 THE SEQUENCE OF CRYIIIA IN THE ATOMIC MODEL IS TAKEN FROM: 1DLC 56 REMARK 5 HOEFTE, H., SEURINCK, J., VAN HOUTVEN, A. AND VAECK, M. 1DLC 57 REMARK 5 (1987) NUCLEIC ACIDS RES. 15:7183. EMBL ACCESSION NUMBER 1DLC 58 REMARK 5 P07130, ENTRY NAME CR70_BACTT. RESIDUES 1 - 57 ARE 1DLC 59 REMARK 5 REMOVED IN THE MATURE TOXIN. RESIDUES 58 - 60 ARE 1DLC 60 REMARK 5 INVISIBLE IN THE CRYSTAL STRUCTURE. 1DLC 61 REMARK 6 1DLC 62 REMARK 6 THE STRUCTURE WAS REPORTED IN PAPER [1] ABOVE AFTER 1DLC 63 REMARK 6 PRELIMINARY REFINEMENT. THE COORDINATES BEING DEPOSITED 1DLC 64 REMARK 6 HERE RESULTED FROM FURTHER REFINEMENT. 1DLC 65 REMARK 7 1DLC 66 REMARK 7 CROSS REFERENCE TO SEQUENCE DATABASE 1DLC 67 REMARK 7 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1DLC 68 REMARK 7 CR70_BACTT 1DLC 69 SEQRES 1 584 THR THR LYS ASP VAL ILE GLN LYS GLY ILE SER VAL VAL 1DLC 70 SEQRES 2 584 GLY ASP LEU LEU GLY VAL VAL GLY PHE PRO PHE GLY GLY 1DLC 71 SEQRES 3 584 ALA LEU VAL SER PHE TYR THR ASN PHE LEU ASN THR ILE 1DLC 72 SEQRES 4 584 TRP PRO SER GLU ASP PRO TRP LYS ALA PHE MET GLU GLN 1DLC 73 SEQRES 5 584 VAL GLU ALA LEU MET ASP GLN LYS ILE ALA ASP TYR ALA 1DLC 74 SEQRES 6 584 LYS ASN LYS ALA LEU ALA GLU LEU GLN GLY LEU GLN ASN 1DLC 75 SEQRES 7 584 ASN VAL GLU ASP TYR VAL SER ALA LEU SER SER TRP GLN 1DLC 76 SEQRES 8 584 LYS ASN PRO VAL SER SER ARG ASN PRO HIS SER GLN GLY 1DLC 77 SEQRES 9 584 ARG ILE ARG GLU LEU PHE SER GLN ALA GLU SER HIS PHE 1DLC 78 SEQRES 10 584 ARG ASN SER MET PRO SER PHE ALA ILE SER GLY TYR GLU 1DLC 79 SEQRES 11 584 VAL LEU PHE LEU THR THR TYR ALA GLN ALA ALA ASN THR 1DLC 80 SEQRES 12 584 HIS LEU PHE LEU LEU LYS ASP ALA GLN ILE TYR GLY GLU 1DLC 81 SEQRES 13 584 GLU TRP GLY TYR GLU LYS GLU ASP ILE ALA GLU PHE TYR 1DLC 82 SEQRES 14 584 LYS ARG GLN LEU LYS LEU THR GLN GLU TYR THR ASP HIS 1DLC 83 SEQRES 15 584 CYS VAL LYS TRP TYR ASN VAL GLY LEU ASP LYS LEU ARG 1DLC 84 SEQRES 16 584 GLY SER SER TYR GLU SER TRP VAL ASN PHE ASN ARG TYR 1DLC 85 SEQRES 17 584 ARG ARG GLU MET THR LEU THR VAL LEU ASP LEU ILE ALA 1DLC 86 SEQRES 18 584 LEU PHE PRO LEU TYR ASP VAL ARG LEU TYR PRO LYS GLU 1DLC 87 SEQRES 19 584 VAL LYS THR GLU LEU THR ARG ASP VAL LEU THR ASP PRO 1DLC 88 SEQRES 20 584 ILE VAL GLY VAL ASN ASN LEU ARG GLY TYR GLY THR THR 1DLC 89 SEQRES 21 584 PHE SER ASN ILE GLU ASN TYR ILE ARG LYS PRO HIS LEU 1DLC 90 SEQRES 22 584 PHE ASP TYR LEU HIS ARG ILE GLN PHE HIS THR ARG PHE 1DLC 91 SEQRES 23 584 GLN PRO GLY TYR TYR GLY ASN ASP SER PHE ASN TYR TRP 1DLC 92 SEQRES 24 584 SER GLY ASN TYR VAL SER THR ARG PRO SER ILE GLY SER 1DLC 93 SEQRES 25 584 ASN ASP ILE ILE THR SER PRO PHE TYR GLY ASN LYS SER 1DLC 94 SEQRES 26 584 SER GLU PRO VAL GLN ASN LEU GLU PHE ASN GLY GLU LYS 1DLC 95 SEQRES 27 584 VAL TYR ARG ALA VAL ALA ASN THR ASN LEU ALA VAL TRP 1DLC 96 SEQRES 28 584 PRO SER ALA VAL TYR SER GLY VAL THR LYS VAL GLU PHE 1DLC 97 SEQRES 29 584 SER GLN TYR ASN ASP GLN THR ASP GLU ALA SER THR GLN 1DLC 98 SEQRES 30 584 THR TYR ASP SER LYS ARG ASN VAL GLY ALA VAL SER TRP 1DLC 99 SEQRES 31 584 ASP SER ILE ASP GLN LEU PRO PRO GLU THR THR ASP GLU 1DLC 100 SEQRES 32 584 PRO LEU GLU LYS GLY TYR SER HIS GLN LEU ASN TYR VAL 1DLC 101 SEQRES 33 584 MET CYS PHE LEU MET GLN GLY SER ARG GLY THR ILE PRO 1DLC 102 SEQRES 34 584 VAL LEU THR TRP THR HIS LYS SER VAL ASP PHE PHE ASN 1DLC 103 SEQRES 35 584 MET ILE ASP SER LYS LYS ILE THR GLN LEU PRO LEU VAL 1DLC 104 SEQRES 36 584 LYS ALA TYR LYS LEU GLN SER GLY ALA SER VAL VAL ALA 1DLC 105 SEQRES 37 584 GLY PRO ARG PHE THR GLY GLY ASP ILE ILE GLN CYS THR 1DLC 106 SEQRES 38 584 GLU ASN GLY SER ALA ALA THR ILE TYR VAL THR PRO ASP 1DLC 107 SEQRES 39 584 VAL SER TYR SER GLN LYS TYR ARG ALA ARG ILE HIS TYR 1DLC 108 SEQRES 40 584 ALA SER THR SER GLN ILE THR PHE THR LEU SER LEU ASP 1DLC 109 SEQRES 41 584 GLY ALA PRO PHE ASN GLN TYR TYR PHE ASP LYS THR ILE 1DLC 110 SEQRES 42 584 ASN LYS GLY ASP THR LEU THR TYR ASN SER PHE ASN LEU 1DLC 111 SEQRES 43 584 ALA SER PHE SER THR PRO PHE GLU LEU SER GLY ASN ASN 1DLC 112 SEQRES 44 584 LEU GLN ILE GLY VAL THR GLY LEU SER ALA GLY ASP LYS 1DLC 113 SEQRES 45 584 VAL TYR ILE ASP LYS ILE GLU PHE ILE PRO VAL ASN 1DLC 114 FTNOTE 1 1DLC 115 FTNOTE 1 RESIDUE ARG 443 IS MODELED IN TWO CONFORMATIONS. 1DLC 116 FORMUL 2 HOH *106(H2 O1) 1DLC 117 CRYST1 117.090 134.260 104.500 90.00 90.00 90.00 C 2 2 21 8 1DLC 118 ORIGX1 1.000000 0.000000 0.000000 0.00000 1DLC 119 ORIGX2 0.000000 1.000000 0.000000 0.00000 1DLC 120 ORIGX3 0.000000 0.000000 1.000000 0.00000 1DLC 121 SCALE1 0.008540 0.000000 0.000000 0.00000 1DLC 122 SCALE2 0.000000 0.007448 0.000000 0.00000 1DLC 123 SCALE3 0.000000 0.000000 0.009569 0.00000 1DLC 124