HEADER TOXIN 01-MAR-94 1DDT 1DDT 2 COMPND DIPHTHERIA TOXIN (DIMERIC) 1DDT 3 SOURCE (CORYNEBACTERIUM DIPHTHERIAE) 1DDT 4 AUTHOR M.J.BENNETT,D.EISENBERG 1DDT 5 REVDAT 1 31-JUL-94 1DDT 0 1DDT 6 JRNL AUTH M.J.BENNETT,S.CHOE,D.EISENBERG 1DDT 7 JRNL TITL THE REFINED STRUCTURE OF DIMERIC DIPHTHERIA TOXIN 1DDT 8 JRNL TITL 2 AT 2.0 ANGSTROMS RESOLUTION 1DDT 9 JRNL REF TO BE PUBLISHED 1DDT 10 JRNL REFN 0353 1DDT 11 REMARK 1 1DDT 12 REMARK 1 REFERENCE 1 1DDT 13 REMARK 1 AUTH M.J.BENNETT,S.CHOE,D.EISENBERG 1DDT 14 REMARK 1 TITL DOMAIN SWAPPING: ENTANGLING ALLIANCES BETWEEN 1DDT 15 REMARK 1 TITL 2 PROTEINS 1DDT 16 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 91 3127 1994 1DDT 17 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 0040 1DDT 18 REMARK 1 REFERENCE 2 1DDT 19 REMARK 1 AUTH S.CHOE,M.J.BENNETT,G.FUJII,P.M.G.CURMI, 1DDT 20 REMARK 1 AUTH 2 K.A.KANTARDJIEFF,R.J.COLLIER,D.EISENBERG 1DDT 21 REMARK 1 TITL THE CRYSTAL STRUCTURE OF DIPHTHERIA TOXIN 1DDT 22 REMARK 1 REF NATURE V. 357 216 1992 1DDT 23 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 0006 1DDT 24 REMARK 2 1DDT 25 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 1DDT 26 REMARK 3 1DDT 27 REMARK 3 REFINEMENT. 1DDT 28 REMARK 3 PROGRAM X-PLOR 1DDT 29 REMARK 3 AUTHORS BRUNGER 1DDT 30 REMARK 3 R VALUE 0.195 1DDT 31 REMARK 3 RMSD BOND DISTANCES 0.018 ANGSTROMS 1DDT 32 REMARK 3 RMSD BOND ANGLES 2.6 DEGREES 1DDT 33 REMARK 3 1DDT 34 REMARK 3 NUMBER OF REFLECTIONS 37727 1DDT 35 REMARK 3 RESOLUTION RANGE 10.0 - 2.0 ANGSTROMS 1DDT 36 REMARK 3 DATA CUTOFF 1.0 SIGMA(F) 1DDT 37 REMARK 3 PERCENT COMPLETION 90.4 1DDT 38 REMARK 3 1DDT 39 REMARK 3 NUMBER OF PROTEIN ATOMS 4021 1DDT 40 REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 43 1DDT 41 REMARK 3 NUMBER OF SOLVENT ATOMS 405 1DDT 42 REMARK 4 1DDT 43 REMARK 4 THIS ENTRY CONTAINS 523 OF 535 RESIDUES IN THE PROTEIN; 1DDT 44 REMARK 4 RESIDUES 188 - 199 ARE DISORDERED AND WERE NOT MODELED. 1DDT 45 REMARK 5 1DDT 46 REMARK 5 SHEET R1 IS NOT A CLOSED BARREL, BUT IS CLOSED ON ONE SIDE 1DDT 47 REMARK 5 AND FLATTENED. 1DDT 48 REMARK 6 1DDT 49 REMARK 6 SITE "CAT", PRESENTED ON SITE RECORDS BELOW, IS THE 1DDT 50 REMARK 6 CATALYTIC SITE. 1DDT 51 REMARK 7 1DDT 52 REMARK 7 WATER 669 LIES ON THE CRYSTALLOGRAPHIC TWO-FOLD AXIS. 1DDT 53 SEQRES 1 535 GLY ALA ASP ASP VAL VAL ASP SER SER LYS SER PHE VAL 1DDT 54 SEQRES 2 535 MET GLU ASN PHE SER SER TYR HIS GLY THR LYS PRO GLY 1DDT 55 SEQRES 3 535 TYR VAL ASP SER ILE GLN LYS GLY ILE GLN LYS PRO LYS 1DDT 56 SEQRES 4 535 SER GLY THR GLN GLY ASN TYR ASP ASP ASP TRP LYS GLY 1DDT 57 SEQRES 5 535 PHE TYR SER THR ASP ASN LYS TYR ASP ALA ALA GLY TYR 1DDT 58 SEQRES 6 535 SER VAL ASP ASN GLU ASN PRO LEU SER GLY LYS ALA GLY 1DDT 59 SEQRES 7 535 GLY VAL VAL LYS VAL THR TYR PRO GLY LEU THR LYS VAL 1DDT 60 SEQRES 8 535 LEU ALA LEU LYS VAL ASP ASN ALA GLU THR ILE LYS LYS 1DDT 61 SEQRES 9 535 GLU LEU GLY LEU SER LEU THR GLU PRO LEU MET GLU GLN 1DDT 62 SEQRES 10 535 VAL GLY THR GLU GLU PHE ILE LYS ARG PHE GLY ASP GLY 1DDT 63 SEQRES 11 535 ALA SER ARG VAL VAL LEU SER LEU PRO PHE ALA GLU GLY 1DDT 64 SEQRES 12 535 SER SER SER VAL GLU TYR ILE ASN ASN TRP GLU GLN ALA 1DDT 65 SEQRES 13 535 LYS ALA LEU SER VAL GLU LEU GLU ILE ASN PHE GLU THR 1DDT 66 SEQRES 14 535 ARG GLY LYS ARG GLY GLN ASP ALA MET TYR GLU TYR MET 1DDT 67 SEQRES 15 535 ALA GLN ALA CYS ALA GLY ASN ARG VAL ARG ARG SER VAL 1DDT 68 SEQRES 16 535 GLY SER SER LEU SER CYS ILE ASN LEU ASP TRP ASP VAL 1DDT 69 SEQRES 17 535 ILE ARG ASP LYS THR LYS THR LYS ILE GLU SER LEU LYS 1DDT 70 SEQRES 18 535 GLU HIS GLY PRO ILE LYS ASN LYS MET SER GLU SER PRO 1DDT 71 SEQRES 19 535 ASN LYS THR VAL SER GLU GLU LYS ALA LYS GLN TYR LEU 1DDT 72 SEQRES 20 535 GLU GLU PHE HIS GLN THR ALA LEU GLU HIS PRO GLU LEU 1DDT 73 SEQRES 21 535 SER GLU LEU LYS THR VAL THR GLY THR ASN PRO VAL PHE 1DDT 74 SEQRES 22 535 ALA GLY ALA ASN TYR ALA ALA TRP ALA VAL ASN VAL ALA 1DDT 75 SEQRES 23 535 GLN VAL ILE ASP SER GLU THR ALA ASP ASN LEU GLU LYS 1DDT 76 SEQRES 24 535 THR THR ALA ALA LEU SER ILE LEU PRO GLY ILE GLY SER 1DDT 77 SEQRES 25 535 VAL MET GLY ILE ALA ASP GLY ALA VAL HIS HIS ASN THR 1DDT 78 SEQRES 26 535 GLU GLU ILE VAL ALA GLN SER ILE ALA LEU SER SER LEU 1DDT 79 SEQRES 27 535 MET VAL ALA GLN ALA ILE PRO LEU VAL GLY GLU LEU VAL 1DDT 80 SEQRES 28 535 ASP ILE GLY PHE ALA ALA TYR ASN PHE VAL GLU SER ILE 1DDT 81 SEQRES 29 535 ILE ASN LEU PHE GLN VAL VAL HIS ASN SER TYR ASN ARG 1DDT 82 SEQRES 30 535 PRO ALA TYR SER PRO GLY HIS LYS THR GLN PRO PHE LEU 1DDT 83 SEQRES 31 535 HIS ASP GLY TYR ALA VAL SER TRP ASN THR VAL GLU ASP 1DDT 84 SEQRES 32 535 SER ILE ILE ARG THR GLY PHE GLN GLY GLU SER GLY HIS 1DDT 85 SEQRES 33 535 ASP ILE LYS ILE THR ALA GLU ASN THR PRO LEU PRO ILE 1DDT 86 SEQRES 34 535 ALA GLY VAL LEU LEU PRO THR ILE PRO GLY LYS LEU ASP 1DDT 87 SEQRES 35 535 VAL ASN LYS SER LYS THR HIS ILE SER VAL ASN GLY ARG 1DDT 88 SEQRES 36 535 LYS ILE ARG MET ARG CYS ARG ALA ILE ASP GLY ASP VAL 1DDT 89 SEQRES 37 535 THR PHE CYS ARG PRO LYS SER PRO VAL TYR VAL GLY ASN 1DDT 90 SEQRES 38 535 GLY VAL HIS ALA ASN LEU HIS VAL ALA PHE HIS ARG SER 1DDT 91 SEQRES 39 535 SER SER GLU LYS ILE HIS SER ASN GLU ILE SER SER ASP 1DDT 92 SEQRES 40 535 SER ILE GLY VAL LEU GLY TYR GLN LYS THR VAL ASP HIS 1DDT 93 SEQRES 41 535 THR LYS VAL ASN SER LYS LEU SER LEU PHE PHE GLU ILE 1DDT 94 SEQRES 42 535 LYS SER 1DDT 95 HET APU 950 50 ADENYLYL 3'-5' URIDINE 3' MONOPHOSPHATE 1DDT 96 FORMUL 2 APU C19 H23 N7 O15 P2 - 1DDT 97 FORMUL 3 HOH *405(H2 O1) 1DDT 98 HELIX 1 CH2 ASP 29 LYS 33 5 1DDT 99 HELIX 2 CH3 LYS 59 SER 66 1 1DDT 100 HELIX 3 CH4 ALA 99 LEU 106 1 1DDT 101 HELIX 4 C4P LEU 114 GLY 119 1 REFERRED TO AS CH4' IN PAPERS 1DDT 102 HELIX 5 CH5 GLU 121 GLY 128 1 1DDT 103 HELIX 6 C5P GLN 155 ALA 158 5 REFERRED TO AS CH5' IN PAPERS 1DDT 104 HELIX 7 CH7 ASP 176 CYS 186 1 1DDT 105 HELIX 8 TH1 TRP 206 GLU 222 1 1DDT 106 HELIX 9 TH2 GLY 224 GLU 232 1 1DDT 107 HELIX 10 TH3 GLU 240 ALA 254 1 1DDT 108 HELIX 11 TH4 LEU 260 GLY 268 1 1DDT 109 HELIX 12 TH5 GLY 275 VAL 288 1 1DDT 110 HELIX 13 T5P SER 291 ASP 295 1 REFERRED TO AS TH5' IN PAPERS 1DDT 111 HELIX 14 TH6 LEU 297 LEU 304 1 1DDT 112 HELIX 15 TH7 ILE 310 MET 314 1 1DDT 113 HELIX 16 TH8 GLU 326 VAL 347 1 1DDT 114 HELIX 17 TH9 TYR 358 ASN 376 1 1DDT 115 SHEET 1 C1 5 PHE 12 GLU 15 0 1DDT 116 SHEET 2 C1 5 LEU 88 LEU 94 -1 O VAL 91 N PHE 12 1DDT 117 SHEET 3 C1 5 ARG 133 PRO 139 1 O VAL 135 N LEU 92 1DDT 118 SHEET 4 C1 5 VAL 147 ASN 151 -1 O ILE 150 N LEU 136 1DDT 119 SHEET 5 C1 5 PHE 53 THR 56 -1 N SER 55 O TYR 149 1DDT 120 SHEET 1 C2 3 PHE 17 THR 23 0 1DDT 121 SHEET 2 C2 3 GLY 79 TYR 85 -1 N TYR 85 O PHE 17 1DDT 122 SHEET 3 C2 3 SER 160 ASN 166 -1 O SER 160 N THR 84 1DDT 123 SHEET 1 R1 11 PHE 389 HIS 391 0 1DDT 124 SHEET 2 R1 11 TYR 394 TRP 398 -1 N VAL 396 O PHE 389 1DDT 125 SHEET 3 R1 11 GLY 412 ALA 422 -1 N THR 421 O ALA 395 1DDT 126 SHEET 4 R1 11 ALA 485 ARG 493 -1 N ALA 485 O ILE 420 1DDT 127 SHEET 5 R1 11 HIS 449 VAL 452 -1 O SER 451 N ASN 486 1DDT 128 SHEET 6 R1 11 ARG 455 ALA 463 -1 N ILE 457 O ILE 450 1DDT 129 SHEET 7 R1 11 VAL 468 PRO 473 -1 O ARG 472 N ARG 460 1DDT 130 SHEET 8 R1 11 GLY 431 PRO 435 -1 N VAL 432 O CYS 471 1DDT 131 SHEET 9 R1 11 SER 508 LYS 516 -1 O GLY 510 N LEU 433 1DDT 132 SHEET 10 R1 11 VAL 523 LYS 534 -1 N LEU 529 O ILE 509 1DDT 133 SHEET 11 R1 11 ILE 405 THR 408 1 O ILE 406 N LYS 534 1DDT 134 TURN 1 T1 GLY 1 ASP 4 1DDT 135 TURN 2 T2 ASP 7 LYS 10 1DDT 136 TURN 3 T3 LYS 24 TYR 27 1DDT 137 TURN 4 T4 THR 42 ASN 45 1DDT 138 TURN 5 T5 ASP 47 TRP 50 1DDT 139 TURN 6 T6 ASP 68 ASN 71 1DDT 140 TURN 7 T7 GLY 128 ALA 131 1DDT 141 TURN 8 T8 ALA 141 SER 144 1DDT 142 TURN 9 T9 ARG 173 ASP 176 1DDT 143 TURN 10 T10 HIS 257 LEU 260 1DDT 144 TURN 11 T11 ASN 270 PHE 273 1DDT 145 TURN 12 T12 ALA 317 ALA 320 1DDT 146 TURN 13 T13 SER 381 HIS 384 1DDT 147 TURN 14 T14 HIS 384 GLN 387 1DDT 148 TURN 15 T15 HIS 391 TYR 394 1DDT 149 TURN 16 T16 VAL 401 SER 404 1DDT 150 TURN 17 T17 VAL 452 ARG 455 1DDT 151 TURN 18 T18 GLY 480 VAL 483 1DDT 152 TURN 19 T19 HIS 500 GLU 503 1DDT 153 SSBOND 1 CYS 186 CYS 201 1DDT 154 SSBOND 2 CYS 461 CYS 471 1DDT 155 SITE 1 CAT 5 HIS 21 TYR 65 GLU 148 SER 446 1DDT 156 SITE 2 CAT 5 ARG 458 1DDT 157 CRYST1 105.640 92.560 65.580 90.00 94.60 90.00 C 2 4 1DDT 158 ORIGX1 1.000000 0.000000 0.000000 0.00000 1DDT 159 ORIGX2 0.000000 1.000000 0.000000 0.00000 1DDT 160 ORIGX3 0.000000 0.000000 1.000000 0.00000 1DDT 161 SCALE1 0.009466 0.000000 0.000762 0.00000 1DDT 162 SCALE2 0.000000 0.010804 0.000000 0.00000 1DDT 163 SCALE3 0.000000 0.000000 0.015298 0.00000 1DDT 164