HEADER LYASE(CARBON-OXYGEN) 15-MAY-91 8ACN COMPND ACONITASE (E.C.4.2.1.3) COMPLEX WITH NITROISOCITRATE SOURCE BOVINE (BOS TAURUS) HEART AUTHOR H.LAUBLE,M.C.KENNEDY,H.BEINERT,C.D.STOUT REVDAT 1 31-OCT-93 8ACN 0 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH H.LAUBLE,M.C.KENNEDY,H.BEINERT,C.D.STOUT REMARK 1 TITL CRYSTAL STRUCTURES OF ACONITASE WITH ISOCITRATE REMARK 1 TITL 2 AND NITROISOCITRATE BOUND REMARK 1 REF BIOCHEMISTRY V. 31 2735 1992 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 REMARK 1 REFERENCE 2 REMARK 1 AUTH A.H.ROBBINS,C.D.STOUT REMARK 1 TITL STRUCTURE OF ACTIVATED ACONITASE. FORMATION OF THE REMARK 1 TITL 2 (4*FE-4*S) CLUSTER IN THE CRYSTAL REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 86 3639 1989 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 REMARK 1 REFERENCE 3 REMARK 1 AUTH A.H.ROBBINS,C.D.STOUT REMARK 1 TITL THE STRUCTURE OF ACONITASE REMARK 1 REF PROTEINS.STRUCT.,FUNCT., V. 5 289 1989 REMARK 1 REF 2 GENET. REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 867 REMARK 1 REFERENCE 4 REMARK 1 AUTH A.H.ROBBINS,C.D.STOUT REMARK 1 TITL IRON-*SULFUR CLUSTER IN ACONITASE. CRYSTALLOGRAPHIC REMARK 1 TITL 2 EVIDENCE FOR A THREE-IRON CENTER REMARK 1 REF J.BIOL.CHEM. V. 260 2328 1985 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 REMARK 2 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM X-PLOR REMARK 3 AUTHORS BRUNGER REMARK 3 R VALUE 0.161 REMARK 3 RMSD BOND DISTANCES 0.015 ANGSTROMS REMARK 3 RMSD BOND ANGLES 3.03 DEGREES REMARK 4 REMARK 4 THE DENSITY FOR THE FOLLOWING REGIONS IS WEAK AND THE REMARK 4 FINAL REBUILDING STEPS USED STEREOCHEMICAL CONSIDERATIONS - REMARK 4 N-TERMINAL PCA REMARK 4 ILE 433 THROUGH GLU 437 REMARK 4 THR 488 THROUGH LYS 494 REMARK 4 LYS 522 THROUGH GLN 527 REMARK 4 C-TERMINAL GLN 752 THROUGH LYS 754 REMARK 5 REMARK 5 RESIDUE 647 IS ARG FROM THE DNA SEQUENCE, (H. ZALKIN, REMARK 5 PRIVATE COMMUNICATION) BUT CANNOT BE ACCOMMODATED AS SUCH REMARK 5 IN THE STRUCTURE. IT HAS BEEN MODELED AS SER, BASED ON REMARK 5 THE EXTENT OF THE SIDE CHAIN DENSITY. SEQRES 1 754 PCA ARG ALA LYS VAL ALA MET SER HIS PHE GLU PRO HIS SEQRES 2 754 GLU TYR ILE ARG TYR ASP LEU LEU GLU LYS ASN ILE ASP SEQRES 3 754 ILE VAL ARG LYS ARG LEU ASN ARG PRO LEU THR LEU SER SEQRES 4 754 GLU LYS ILE VAL TYR GLY HIS LEU ASP ASP PRO ALA ASN SEQRES 5 754 GLN GLU ILE GLU ARG GLY LYS THR TYR LEU ARG LEU ARG SEQRES 6 754 PRO ASP ARG VAL ALA MET GLN ASP ALA THR ALA GLN MET SEQRES 7 754 ALA MET LEU GLN PHE ILE SER SER GLY LEU PRO LYS VAL SEQRES 8 754 ALA VAL PRO SER THR ILE HIS CYS ASP HIS LEU ILE GLU SEQRES 9 754 ALA GLN LEU GLY GLY GLU LYS ASP LEU ARG ARG ALA LYS SEQRES 10 754 ASP ILE ASN GLN GLU VAL TYR ASN PHE LEU ALA THR ALA SEQRES 11 754 GLY ALA LYS TYR GLY VAL GLY PHE TRP ARG PRO GLY SER SEQRES 12 754 GLY ILE ILE HIS GLN ILE ILE LEU GLU ASN TYR ALA TYR SEQRES 13 754 PRO GLY VAL LEU LEU ILE GLY THR ASP SER HIS THR PRO SEQRES 14 754 ASN GLY GLY GLY LEU GLY GLY ILE CYS ILE GLY VAL GLY SEQRES 15 754 GLY ALA ASP ALA VAL ASP VAL MET ALA GLY ILE PRO TRP SEQRES 16 754 GLU LEU LYS CYS PRO LYS VAL ILE GLY VAL LYS LEU THR SEQRES 17 754 GLY SER LEU SER GLY TRP THR SER PRO LYS ASP VAL ILE SEQRES 18 754 LEU LYS VAL ALA GLY ILE LEU THR VAL LYS GLY GLY THR SEQRES 19 754 GLY ALA ILE VAL GLU TYR HIS GLY PRO GLY VAL ASP SER SEQRES 20 754 ILE SER CYS THR GLY MET ALA THR ILE CYS ASN MET GLY SEQRES 21 754 ALA GLU ILE GLY ALA THR THR SER VAL PHE PRO TYR ASN SEQRES 22 754 HIS ARG MET LYS LYS TYR LEU SER LYS THR GLY ARG ALA SEQRES 23 754 ASP ILE ALA ASN LEU ALA ASP GLU PHE LYS ASP HIS LEU SEQRES 24 754 VAL PRO ASP SER GLY CYS HIS TYR ASP GLN LEU ILE GLU SEQRES 25 754 ILE ASN LEU SER GLU LEU LYS PRO HIS ILE ASN GLY PRO SEQRES 26 754 PHE THR PRO ASP LEU ALA HIS PRO VAL ALA GLU VAL GLY SEQRES 27 754 SER VAL ALA GLU LYS GLU GLY TRP PRO LEU ASP ILE ARG SEQRES 28 754 VAL GLY LEU ILE GLY SER CYS THR ASN SER SER TYR GLU SEQRES 29 754 ASP MET GLY ARG SER ALA ALA VAL ALA LYS GLN ALA LEU SEQRES 30 754 ALA HIS GLY LEU LYS CYS LYS SER GLN PHE THR ILE THR SEQRES 31 754 PRO GLY SER GLU GLN ILE ARG ALA THR ILE GLU ARG ASP SEQRES 32 754 GLY TYR ALA GLN VAL LEU ARG ASP VAL GLY GLY ILE VAL SEQRES 33 754 LEU ALA ASN ALA CYS GLY PRO CYS ILE GLY GLN TRP ASP SEQRES 34 754 ARG LYS ASP ILE LYS LYS GLY GLU LYS ASN THR ILE VAL SEQRES 35 754 THR SER TYR ASN ARG ASN PHE THR GLY ARG ASN ASP ALA SEQRES 36 754 ASN PRO GLU THR HIS ALA PHE VAL THR SER PRO GLU ILE SEQRES 37 754 VAL THR ALA LEU ALA ILE ALA GLY THR LEU LYS PHE ASN SEQRES 38 754 PRO GLU THR ASP PHE LEU THR GLY LYS ASP GLY LYS LYS SEQRES 39 754 PHE LYS LEU GLU ALA PRO ASP ALA ASP GLU LEU PRO ARG SEQRES 40 754 ALA GLU PHE ASP PRO GLY GLN ASP THR TYR GLN HIS PRO SEQRES 41 754 PRO LYS ASP SER SER GLY GLN ARG VAL ASP VAL SER PRO SEQRES 42 754 THR SER GLN ARG LEU GLN LEU LEU GLU PRO PHE ASP LYS SEQRES 43 754 TRP ASP GLY LYS ASP LEU GLU ASP LEU GLN ILE LEU ILE SEQRES 44 754 LYS VAL LYS GLY LYS CYS THR THR ASP HIS ILE SER ALA SEQRES 45 754 ALA GLY PRO TRP LEU LYS PHE ARG GLY HIS LEU ASP ASN SEQRES 46 754 ILE SER ASN ASN LEU LEU ILE GLY ALA ILE ASN SER GLU SEQRES 47 754 ASN ARG LYS ALA ASN SER VAL ARG ASN ALA VAL THR GLN SEQRES 48 754 GLU PHE GLY PRO VAL PRO ASP THR ALA ARG TYR TYR LYS SEQRES 49 754 GLN HIS GLY ILE ARG TRP VAL VAL ILE GLY ASP GLU ASN SEQRES 50 754 TYR GLY GLU GLY SER SER ARG GLU HIS SER ALA LEU GLU SEQRES 51 754 PRO ARG PHE LEU GLY GLY ARG ALA ILE ILE THR LYS SER SEQRES 52 754 PHE ALA ARG ILE HIS GLU THR ASN LEU LYS LYS GLN GLY SEQRES 53 754 LEU LEU PRO LEU THR PHE ALA ASP PRO ALA ASP TYR ASN SEQRES 54 754 LYS ILE HIS PRO VAL ASP LYS LEU THR ILE GLN GLY LEU SEQRES 55 754 LYS ASP PHE ALA PRO GLY LYS PRO LEU THR CYS ILE ILE SEQRES 56 754 LYS HIS PRO ASN GLY THR GLN GLU THR ILE LEU LEU ASN SEQRES 57 754 HIS THR PHE ASN GLU THR GLN ILE GLU TRP PHE ARG ALA SEQRES 58 754 GLY SER ALA LEU ASN ARG MET LYS GLU LEU GLN GLN LYS FTNOTE 1 FTNOTE 1 RESIDUE 325 IS A CIS PROLINE. FTNOTE 2 FTNOTE 2 SEE REMARK 5. HET FS4 999 8 FE4-S4 CLUSTER HET NIC 755 13 NITROISOCITRATE FORMUL 2 FS4 FE4 S4 FORMUL 3 NIC C5 H7 O7 FORMUL 4 HOH *321(H2 O1) HELIX 1 H1 TYR 18 ASN 33 1 3(10) AT C-TERMINUS HELIX 2 H2 LEU 38 GLY 45 1 HELIX 3 H3 PRO 50 GLN 53 1 HELIX 4 H4 ALA 76 SER 86 1 HELIX 5 H5 GLU 110 ILE 119 1 HELIX 6 H6 GLN 121 TYR 134 1 HELIX 7 H7 HIS 147 GLU 152 1 HELIX 8 H8 SER 166 LEU 174 5 3 TURN 3(10) AT ACTIVE SITE HELIX 9 H9 GLY 183 ALA 191 1 HELIX 10 H10 PRO 217 LEU 228 1 HELIX 11 H11 VAL 230 THR 234 5 DISTORTED HELIX 12 H12 PRO 243 SER 247 5 HELIX 13 H13 CYS 250 ILE 263 1 3(10) TURN AT C-TERMINUS HELIX 14 H14 HIS 274 LYS 282 1 HELIX 15 H15 ALA 286 HIS 298 1 3(10) TURN AT C-TERMINUS HELIX 16 H16 GLU 336 GLU 344 1 HELIX 17 H17 TYR 363 ALA 378 1 BENT, 3(10) H-BOND AT 372N HELIX 18 H18 GLU 394 ASP 403 1 HELIX 19 H19 TYR 405 VAL 412 1 HELIX 20 H20 PRO 423 ILE 425 5 CONTAINS 424 CYS LIGAND HELIX 21 H21 PRO 466 ALA 475 1 HELIX 22 H22 THR 567 ILE 570 1 HELIX 23 H23 PRO 575 PHE 579 5 HELIX 24 H24 LEU 583 ASN 589 1 3(10) TURN AT C-TERMINUS HELIX 25 H25 VAL 616 GLN 625 1 HELIX 26 H26 GLU 645 LEU 654 1 HELIX 27 H27 ARG 666 GLN 675 1 HELIX 28 H28 ALA 686 ILE 691 1 3(10) H-BONDS AT N-TERMINUS HELIX 29 H29 GLU 733 ALA 741 1 HELIX 30 H30 ALA 744 LEU 751 1 SHEET 1 S1 2 THR 60 LEU 64 0 SHEET 2 S1 2 PRO 194 CYS 199 -1 O TRP 195 N LEU 64 SHEET 1 S2 6 GLY 176 VAL 181 0 SHEET 2 S2 6 VAL 159 GLY 163 1 N LEU 161 O ILE 177 SHEET 3 S2 6 ASP 67 ASP 73 1 O ARG 68 N ILE 162 SHEET 4 S2 6 PRO 94 HIS 98 1 O THR 96 N MET 71 SHEET 5 S2 6 VAL 136 TRP 139 1 N TRP 139 O ILE 97 SHEET 6 S2 6 THR 516 GLN 518 -1 O GLN 518 N PHE 138 SHEET 1 S3 4 THR 266 PHE 270 0 SHEET 2 S3 4 GLY 235 PRO 243 1 N TYR 240 O VAL 269 SHEET 3 S3 4 LYS 201 GLY 209 1 N ILE 203 O ILE 237 SHEET 4 S3 4 GLN 309 LEU 315 1 N ILE 313 O LYS 206 SHEET 1 S4 7 LEU 330 PRO 333 0 SHEET 2 S4 7 PRO 320 ASN 323 -1 N ILE 322 O HIS 332 SHEET 3 S4 7 THR 459 THR 464 1 N PHE 462 O ASN 323 SHEET 4 S4 7 ASN 439 SER 444 1 N THR 443 O PHE 462 SHEET 5 S4 7 ARG 351 SER 357 1 N LEU 354 O SER 444 SHEET 6 S4 7 GLN 386 THR 390 1 N THR 388 O ILE 355 SHEET 7 S4 7 ILE 415 LEU 417 1 O ILE 415 N ILE 389 SHEET 1 S5 4 LEU 552 LEU 555 0 SHEET 2 S5 4 ASP 695 GLN 700 -1 N ILE 699 O LEU 552 SHEET 3 S5 4 PRO 710 HIS 717 -1 N HIS 717 O LYS 696 SHEET 4 S5 4 THR 721 ASN 728 -1 O GLU 723 N ILE 715 SHEET 1 S6 5 GLN 556 VAL 561 0 SHEET 2 S6 5 TRP 630 ASP 635 1 O ILE 633 N VAL 561 SHEET 3 S6 5 ARG 657 LYS 662 1 O ALA 658 N VAL 632 SHEET 4 S6 5 LEU 677 PHE 682 1 O LEU 680 N THR 661 SHEET 5 S6 5 LEU 727 ASN 728 1 N ASN 728 O THR 681 TURN 1 T1 SER 8 GLU 11 TURN 2 T2 GLU 56 LYS 59 TURN 3 T3 ARG 140 SER 143 TURN 4 T4 TYR 156 VAL 159 TURN 5 G1 GLY 163 ASP 165 GAMMA TURN TURN 6 T5 SER 212 THR 215 TURN 7 T6 GLY 233 ALA 236 TURN 8 T7 ASP 302 CYS 305 TURN 9 T8 ASN 314 GLU 317 TURN 10 T9 PRO 333 GLU 336 TURN 11 T10 SER 357 ASN 360 TURN 12 G2 ALA 418 ALA 420 GAMMA TURN TURN 13 T11 LYS 434 GLU 437 TURN 14 T12 PHE 449 ARG 452 TURN 15 T13 ASN 456 THR 459 TURN 16 T14 THR 477 PHE 480 TURN 17 T15 ASN 481 THR 484 TURN 18 T16 GLY 489 GLY 492 492 GLY IN G1 BULGE TURN 19 T17 PRO 521 SER 524 TURN 20 G3 SER 524 GLY 526 GAMMA TURN TURN 21 T18 SER 532 SER 535 TURN 22 T19 PHE 579 HIS 582 TURN 23 T20 ASN 589 ILE 592 TURN 24 T21 ASN 596 ARG 600 I TO I+4 H-BOND TURN 25 T22 ASN 607 GLN 611 I TO I+4 H-BOND TURN 26 T23 ASN 637 GLU 640 TURN 27 T24 HIS 692 ASP 695 TURN 28 T25 LEU 702 PHE 705 TURN 29 T26 HIS 717 GLY 720 SITE 1 ACT 18 GLN 72 ASP 100 HIS 101 HIS 147 SITE 2 ACT 18 ASP 165 SER 166 HIS 167 ASN 170 SITE 3 ACT 18 ASN 258 GLU 262 ASN 446 ARG 447 SITE 4 ACT 18 ARG 452 ARG 580 SER 642 SER 643 SITE 5 ACT 18 ARG 644 FS4 999 CRYST1 185.500 72.000 73.000 90.00 90.00 77.70 B 2 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.005391 -0.001175 0.000000 0.00000 SCALE2 0.000000 0.014215 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013699 0.00000