HEADER ISOMERASE/DNA/ISOMERASE INHIBITOR 01-MAR-11 3QX3
TITLE HUMAN TOPOISOMERASE IIBETA IN COMPLEX WITH DNA AND ETOPOSIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA TOPOISOMERASE 2-BETA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HTOP2BETA CLEAVAGE CORE, UNP RESIDUES 450-1206;
COMPND 5 SYNONYM: DNA TOPOISOMERASE II, BETA ISOZYME;
COMPND 6 EC: 5.99.1.3;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA (5'-D(P*AP*GP*CP*CP*GP*AP*GP*C)-3');
COMPND 10 CHAIN: C, E;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA (5'-D(P*TP*GP*CP*AP*GP*CP*TP*CP*GP*GP*CP*T)-3');
COMPND 14 CHAIN: D, F;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TOP2B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21STAR(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET51B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THE OLIGONUCLEOTIDE SEQUENCE 5'-AGCCGAGCTGCAGCTCGGCT-
SOURCE 14 3' WAS PURCHASED FROM VIOGENE.;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 OTHER_DETAILS: THE OLIGONUCLEOTIDE SEQUENCE 5'-AGCCGAGCTGCAGCTCGGCT-
SOURCE 18 3' WAS PURCHASED FROM VIOGENE.
KEYWDS TOPRIM DOMAIN, WINGED-HELIX DOMAIN, COILED-COIL DOMAIN, DNA BINDING
KEYWDS 2 AND CLEAVAGE, NUCLEUS, ISOMERASE-DNA-ISOMERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.C.WU,T.K.LI,L.FARH,L.Y.LIN,T.S.LIN,Y.J.YU,T.J.YEN,C.W.CHIANG,
AUTHOR 2 N.L.CHAN
REVDAT 3 01-NOV-23 3QX3 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 2 1 LINK
REVDAT 2 25-JAN-12 3QX3 1 JRNL VERSN
REVDAT 1 06-JUL-11 3QX3 0
JRNL AUTH C.C.WU,T.K.LI,L.FARH,L.Y.LIN,T.S.LIN,Y.J.YU,T.J.YEN,
JRNL AUTH 2 C.W.CHIANG,N.L.CHAN
JRNL TITL STRUCTURAL BASIS OF TYPE II TOPOISOMERASE INHIBITION BY THE
JRNL TITL 2 ANTICANCER DRUG ETOPOSIDE
JRNL REF SCIENCE V. 333 459 2011
JRNL REFN ISSN 0036-8075
JRNL PMID 21778401
JRNL DOI 10.1126/SCIENCE.1204117
REMARK 2
REMARK 2 RESOLUTION. 2.16 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 3 NUMBER OF REFLECTIONS : 117720
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 5917
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.5462 - 4.6522 0.90 11184 581 0.1726 0.1982
REMARK 3 2 4.6522 - 3.6949 0.92 11317 625 0.1397 0.1686
REMARK 3 3 3.6949 - 3.2285 0.95 11700 594 0.1513 0.1895
REMARK 3 4 3.2285 - 2.9336 0.95 11605 652 0.1656 0.2181
REMARK 3 5 2.9336 - 2.7235 0.94 11577 630 0.1712 0.2131
REMARK 3 6 2.7235 - 2.5630 0.93 11420 574 0.1781 0.2357
REMARK 3 7 2.5630 - 2.4347 0.91 11223 576 0.1902 0.2316
REMARK 3 8 2.4347 - 2.3288 0.90 11012 576 0.1945 0.2482
REMARK 3 9 2.3288 - 2.2391 0.87 10652 537 0.2097 0.2689
REMARK 3 10 2.2391 - 2.1619 0.82 10113 572 0.2325 0.2882
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 40.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.200
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.09
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.31550
REMARK 3 B22 (A**2) : 1.07170
REMARK 3 B33 (A**2) : 3.91190
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 5.99530
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 12326
REMARK 3 ANGLE : 1.058 16825
REMARK 3 CHIRALITY : 0.069 1857
REMARK 3 PLANARITY : 0.004 2017
REMARK 3 DIHEDRAL : 15.442 4791
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3QX3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064212.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL12B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90000
REMARK 200 MONOCHROMATOR : FIXED-EXIT DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR (CRYSTAL TYPE SI(1
REMARK 200 1 1))
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 129411
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.160
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.16
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.47200
REMARK 200 R SYM FOR SHELL (I) : 0.47200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.6.4_486
REMARK 200 STARTING MODEL: PDB ENTRY 3L4K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MAGNESIUM ACETATE, 50MM 2-(N
REMARK 280 -MORPHOLINO)ETHANESULFONIC ACID PH 5.8, 22% 2-METHYL-2, 4-
REMARK 280 PENTANEDIOL (MPT), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 88.40050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 64430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 419
REMARK 465 ALA A 420
REMARK 465 SER A 421
REMARK 465 TRP A 422
REMARK 465 SER A 423
REMARK 465 HIS A 424
REMARK 465 PRO A 425
REMARK 465 GLN A 426
REMARK 465 PHE A 427
REMARK 465 GLU A 428
REMARK 465 LYS A 429
REMARK 465 GLY A 430
REMARK 465 ALA A 431
REMARK 465 ASP A 432
REMARK 465 ASP A 433
REMARK 465 ASP A 434
REMARK 465 ASP A 435
REMARK 465 LYS A 436
REMARK 465 VAL A 437
REMARK 465 PRO A 438
REMARK 465 ASP A 439
REMARK 465 PRO A 440
REMARK 465 THR A 441
REMARK 465 SER A 442
REMARK 465 VAL A 443
REMARK 465 ASP A 444
REMARK 465 SER A 445
REMARK 465 VAL A 446
REMARK 465 LYS A 447
REMARK 465 TYR A 448
REMARK 465 SER A 449
REMARK 465 LYS A 450
REMARK 465 ILE A 451
REMARK 465 PRO A 592
REMARK 465 ILE A 593
REMARK 465 VAL A 594
REMARK 465 LYS A 595
REMARK 465 ALA A 596
REMARK 465 SER A 597
REMARK 465 LYS A 598
REMARK 465 ASN A 599
REMARK 465 LYS A 600
REMARK 465 GLN A 601
REMARK 465 GLU A 602
REMARK 465 LEU A 603
REMARK 465 SER A 604
REMARK 465 PHE A 605
REMARK 465 TYR A 606
REMARK 465 SER A 607
REMARK 465 ILE A 608
REMARK 465 PRO A 609
REMARK 465 GLU A 610
REMARK 465 PHE A 611
REMARK 465 ASP A 612
REMARK 465 GLU A 613
REMARK 465 TRP A 614
REMARK 465 LYS A 615
REMARK 465 LYS A 616
REMARK 465 HIS A 617
REMARK 465 ILE A 618
REMARK 465 GLU A 619
REMARK 465 ASN A 620
REMARK 465 GLN A 621
REMARK 465 LYS A 622
REMARK 465 ALA A 623
REMARK 465 TRP A 624
REMARK 465 LYS A 625
REMARK 465 ILE A 626
REMARK 465 LYS A 627
REMARK 465 TYR A 628
REMARK 465 TYR A 629
REMARK 465 LYS A 630
REMARK 465 GLY A 631
REMARK 465 LEU A 632
REMARK 465 GLY A 633
REMARK 465 THR A 634
REMARK 465 SER A 635
REMARK 465 THR A 636
REMARK 465 ALA A 637
REMARK 465 PRO A 697
REMARK 465 GLU A 698
REMARK 465 GLN A 699
REMARK 465 PHE A 700
REMARK 465 LEU A 701
REMARK 465 TYR A 702
REMARK 465 GLY A 703
REMARK 465 THR A 704
REMARK 465 ALA A 705
REMARK 465 THR A 706
REMARK 465 LYS A 1112
REMARK 465 ALA A 1113
REMARK 465 ALA A 1114
REMARK 465 GLU A 1115
REMARK 465 GLU A 1116
REMARK 465 ASP A 1117
REMARK 465 GLU A 1118
REMARK 465 THR A 1119
REMARK 465 GLN A 1120
REMARK 465 ASN A 1121
REMARK 465 GLN A 1122
REMARK 465 HIS A 1123
REMARK 465 ASP A 1124
REMARK 465 ASP A 1125
REMARK 465 SER A 1126
REMARK 465 SER A 1127
REMARK 465 SER A 1128
REMARK 465 ASP A 1129
REMARK 465 SER A 1130
REMARK 465 GLY A 1131
REMARK 465 THR A 1132
REMARK 465 PRO A 1133
REMARK 465 SER A 1134
REMARK 465 GLY A 1202
REMARK 465 ALA A 1203
REMARK 465 PRO A 1204
REMARK 465 GLY A 1205
REMARK 465 PHE A 1206
REMARK 465 SER A 1207
REMARK 465 SER A 1208
REMARK 465 ILE A 1209
REMARK 465 SER A 1210
REMARK 465 ALA A 1211
REMARK 465 HIS A 1212
REMARK 465 HIS A 1213
REMARK 465 HIS A 1214
REMARK 465 HIS A 1215
REMARK 465 HIS A 1216
REMARK 465 HIS A 1217
REMARK 465 HIS A 1218
REMARK 465 HIS A 1219
REMARK 465 HIS A 1220
REMARK 465 HIS A 1221
REMARK 465 MET B 419
REMARK 465 ALA B 420
REMARK 465 SER B 421
REMARK 465 TRP B 422
REMARK 465 SER B 423
REMARK 465 HIS B 424
REMARK 465 PRO B 425
REMARK 465 GLN B 426
REMARK 465 PHE B 427
REMARK 465 GLU B 428
REMARK 465 LYS B 429
REMARK 465 GLY B 430
REMARK 465 ALA B 431
REMARK 465 ASP B 432
REMARK 465 ASP B 433
REMARK 465 ASP B 434
REMARK 465 ASP B 435
REMARK 465 LYS B 436
REMARK 465 VAL B 437
REMARK 465 PRO B 438
REMARK 465 ASP B 439
REMARK 465 PRO B 440
REMARK 465 THR B 441
REMARK 465 SER B 442
REMARK 465 VAL B 443
REMARK 465 ASP B 444
REMARK 465 SER B 445
REMARK 465 VAL B 446
REMARK 465 LYS B 447
REMARK 465 TYR B 448
REMARK 465 ILE B 593
REMARK 465 VAL B 594
REMARK 465 LYS B 595
REMARK 465 ALA B 596
REMARK 465 SER B 597
REMARK 465 LYS B 598
REMARK 465 ASN B 599
REMARK 465 LYS B 600
REMARK 465 GLN B 601
REMARK 465 GLU B 602
REMARK 465 LEU B 603
REMARK 465 SER B 604
REMARK 465 PHE B 605
REMARK 465 TYR B 606
REMARK 465 SER B 607
REMARK 465 ILE B 608
REMARK 465 PRO B 609
REMARK 465 GLU B 610
REMARK 465 PHE B 611
REMARK 465 ASP B 612
REMARK 465 GLU B 613
REMARK 465 TRP B 614
REMARK 465 LYS B 615
REMARK 465 LYS B 616
REMARK 465 HIS B 617
REMARK 465 ILE B 618
REMARK 465 GLU B 619
REMARK 465 ASN B 620
REMARK 465 GLN B 621
REMARK 465 LYS B 622
REMARK 465 ALA B 623
REMARK 465 TRP B 624
REMARK 465 LYS B 625
REMARK 465 ILE B 626
REMARK 465 LYS B 627
REMARK 465 TYR B 628
REMARK 465 TYR B 629
REMARK 465 LYS B 630
REMARK 465 GLY B 631
REMARK 465 LEU B 632
REMARK 465 GLY B 633
REMARK 465 THR B 634
REMARK 465 SER B 635
REMARK 465 THR B 636
REMARK 465 LEU B 696
REMARK 465 PRO B 697
REMARK 465 GLU B 698
REMARK 465 GLN B 699
REMARK 465 PHE B 700
REMARK 465 LEU B 701
REMARK 465 TYR B 702
REMARK 465 GLY B 703
REMARK 465 THR B 704
REMARK 465 ALA B 705
REMARK 465 THR B 963
REMARK 465 ASP B 964
REMARK 465 LYS B 965
REMARK 465 THR B 966
REMARK 465 GLU B 1111
REMARK 465 LYS B 1112
REMARK 465 ALA B 1113
REMARK 465 ALA B 1114
REMARK 465 GLU B 1115
REMARK 465 GLU B 1116
REMARK 465 ASP B 1117
REMARK 465 GLU B 1118
REMARK 465 THR B 1119
REMARK 465 GLN B 1120
REMARK 465 ASN B 1121
REMARK 465 GLN B 1122
REMARK 465 HIS B 1123
REMARK 465 ASP B 1124
REMARK 465 ASP B 1125
REMARK 465 SER B 1126
REMARK 465 SER B 1127
REMARK 465 SER B 1128
REMARK 465 ASP B 1129
REMARK 465 SER B 1130
REMARK 465 GLY B 1131
REMARK 465 THR B 1132
REMARK 465 PRO B 1133
REMARK 465 SER B 1134
REMARK 465 GLY B 1202
REMARK 465 ALA B 1203
REMARK 465 PRO B 1204
REMARK 465 GLY B 1205
REMARK 465 PHE B 1206
REMARK 465 SER B 1207
REMARK 465 SER B 1208
REMARK 465 ILE B 1209
REMARK 465 SER B 1210
REMARK 465 ALA B 1211
REMARK 465 HIS B 1212
REMARK 465 HIS B 1213
REMARK 465 HIS B 1214
REMARK 465 HIS B 1215
REMARK 465 HIS B 1216
REMARK 465 HIS B 1217
REMARK 465 HIS B 1218
REMARK 465 HIS B 1219
REMARK 465 HIS B 1220
REMARK 465 HIS B 1221
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS B 1193 CA CB CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 MG MG F 1 O HOH F 871 1.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 743 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 DA C 1 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG C 2 O4' - C1' - N9 ANGL. DEV. = 4.1 DEGREES
REMARK 500 DC C 8 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DG D 13 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DC D 19 C1' - O4' - C4' ANGL. DEV. = -7.5 DEGREES
REMARK 500 DG E 2 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG E 5 C3' - C2' - C1' ANGL. DEV. = -4.9 DEGREES
REMARK 500 DA E 6 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DG E 7 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DC E 8 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DT F 9 O4' - C1' - N1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 DA F 12 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG F 13 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC F 16 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DG F 17 O4' - C1' - N9 ANGL. DEV. = -5.2 DEGREES
REMARK 500 DC F 19 P - O5' - C5' ANGL. DEV. = -9.8 DEGREES
REMARK 500 DC F 19 C1' - O4' - C4' ANGL. DEV. = -7.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 503 38.51 -92.55
REMARK 500 ARG A 503 40.28 -93.94
REMARK 500 LYS A 535 -22.45 74.63
REMARK 500 TYR A 538 65.77 -119.86
REMARK 500 GLN A 558 45.03 -78.12
REMARK 500 HIS A 694 -104.56 -97.34
REMARK 500 SER A 794 -111.01 -99.71
REMARK 500 PHE A 834 75.46 -119.86
REMARK 500 ASN A 849 -9.73 73.54
REMARK 500 VAL A 852 -142.86 -121.42
REMARK 500 VAL A 955 -55.45 -124.28
REMARK 500 ASP A1101 106.70 -35.11
REMARK 500 ARG B 503 44.00 -96.03
REMARK 500 ARG B 503 41.15 -93.88
REMARK 500 LYS B 535 -5.21 74.59
REMARK 500 TYR B 538 57.06 -103.69
REMARK 500 HIS B 694 -124.37 -133.18
REMARK 500 ASN B 790 18.28 -141.96
REMARK 500 SER B 794 -112.17 -100.08
REMARK 500 ASN B 849 -19.20 79.12
REMARK 500 VAL B 852 -143.82 -120.18
REMARK 500 PRO B 862 90.67 -68.93
REMARK 500 VAL B 932 -66.41 -92.06
REMARK 500 ASN B 935 -12.45 91.59
REMARK 500 ASN B 961 -118.39 -100.71
REMARK 500 ASP B1101 104.23 -24.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1222 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 557 OD2
REMARK 620 2 ASP A 559 OD2 99.8
REMARK 620 3 HOH A1333 O 100.0 89.4
REMARK 620 4 HOH A1348 O 80.4 90.3 179.5
REMARK 620 5 HOH C 633 O 168.3 77.9 91.5 88.1
REMARK 620 6 HOH C 795 O 90.8 169.3 90.8 89.5 91.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1223 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1466 O
REMARK 620 2 HOH A1467 O 60.6
REMARK 620 3 HOH C1143 O 58.5 117.4
REMARK 620 4 HOH C1145 O 71.9 71.5 77.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 1 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 46 O
REMARK 620 2 ASP B 557 OD2 87.3
REMARK 620 3 ASP B 559 OD2 87.0 102.1
REMARK 620 4 HOH B1250 O 92.1 84.0 173.8
REMARK 620 5 HOH B1291 O 174.5 87.3 95.0 86.5
REMARK 620 6 HOH E 64 O 90.9 172.5 85.1 88.8 94.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1222 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B1470 O
REMARK 620 2 HOH E1148 O 73.1
REMARK 620 3 HOH E1150 O 99.8 85.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 21 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 553 O
REMARK 620 2 HOH D 765 O 86.5
REMARK 620 3 HOH D 766 O 85.6 162.8
REMARK 620 4 HOH D 767 O 94.6 101.1 94.7
REMARK 620 5 HOH D 768 O 93.2 77.7 87.5 172.0
REMARK 620 6 HOH E1224 O 149.7 63.3 122.8 93.4 79.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 1 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH F 763 O
REMARK 620 2 HOH F 764 O 78.6
REMARK 620 3 HOH F 866 O 86.2 164.6
REMARK 620 4 HOH F1123 O 75.8 91.0 87.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EVP A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1222
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1223
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1222
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EVP D 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QXK RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF DNA USED IN THE EXPERIMENT WAS 5'-
REMARK 999 AGCCGAGCTGCAGCTCGGCT-3'. AND THE DNAS WERE CLEAVED INTO TWO PIECES
REMARK 999 (TOTALLY 4 STRANDS, DESIGNATED AS CHAIN C, D, E AND F) DURING
REMARK 999 EXPERIMENT.
DBREF 3QX3 A 445 1201 UNP Q02880 TOP2B_HUMAN 450 1206
DBREF 3QX3 B 445 1201 UNP Q02880 TOP2B_HUMAN 450 1206
DBREF 3QX3 C 1 8 PDB 3QX3 3QX3 1 8
DBREF 3QX3 E 1 8 PDB 3QX3 3QX3 1 8
DBREF 3QX3 D 9 20 PDB 3QX3 3QX3 9 20
DBREF 3QX3 F 9 20 PDB 3QX3 3QX3 9 20
SEQADV 3QX3 MET A 419 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ALA A 420 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 SER A 421 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 TRP A 422 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 SER A 423 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS A 424 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 PRO A 425 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 GLN A 426 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 PHE A 427 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 GLU A 428 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 LYS A 429 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 GLY A 430 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ALA A 431 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ASP A 432 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ASP A 433 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ASP A 434 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ASP A 435 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 LYS A 436 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 VAL A 437 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 PRO A 438 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ASP A 439 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 PRO A 440 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 THR A 441 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 SER A 442 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 VAL A 443 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ASP A 444 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 GLY A 1202 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ALA A 1203 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 PRO A 1204 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 GLY A 1205 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 PHE A 1206 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 SER A 1207 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 SER A 1208 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ILE A 1209 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 SER A 1210 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ALA A 1211 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS A 1212 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS A 1213 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS A 1214 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS A 1215 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS A 1216 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS A 1217 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS A 1218 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS A 1219 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS A 1220 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS A 1221 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 MET B 419 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ALA B 420 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 SER B 421 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 TRP B 422 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 SER B 423 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS B 424 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 PRO B 425 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 GLN B 426 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 PHE B 427 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 GLU B 428 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 LYS B 429 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 GLY B 430 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ALA B 431 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ASP B 432 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ASP B 433 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ASP B 434 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ASP B 435 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 LYS B 436 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 VAL B 437 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 PRO B 438 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ASP B 439 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 PRO B 440 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 THR B 441 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 SER B 442 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 VAL B 443 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ASP B 444 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 GLY B 1202 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ALA B 1203 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 PRO B 1204 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 GLY B 1205 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 PHE B 1206 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 SER B 1207 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 SER B 1208 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ILE B 1209 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 SER B 1210 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 ALA B 1211 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS B 1212 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS B 1213 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS B 1214 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS B 1215 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS B 1216 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS B 1217 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS B 1218 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS B 1219 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS B 1220 UNP Q02880 EXPRESSION TAG
SEQADV 3QX3 HIS B 1221 UNP Q02880 EXPRESSION TAG
SEQRES 1 A 803 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 A 803 ASP ASP ASP ASP LYS VAL PRO ASP PRO THR SER VAL ASP
SEQRES 3 A 803 SER VAL LYS TYR SER LYS ILE LYS GLY ILE PRO LYS LEU
SEQRES 4 A 803 ASP ASP ALA ASN ASP ALA GLY GLY LYS HIS SER LEU GLU
SEQRES 5 A 803 CYS THR LEU ILE LEU THR GLU GLY ASP SER ALA LYS SER
SEQRES 6 A 803 LEU ALA VAL SER GLY LEU GLY VAL ILE GLY ARG ASP ARG
SEQRES 7 A 803 TYR GLY VAL PHE PRO LEU ARG GLY LYS ILE LEU ASN VAL
SEQRES 8 A 803 ARG GLU ALA SER HIS LYS GLN ILE MET GLU ASN ALA GLU
SEQRES 9 A 803 ILE ASN ASN ILE ILE LYS ILE VAL GLY LEU GLN TYR LYS
SEQRES 10 A 803 LYS SER TYR ASP ASP ALA GLU SER LEU LYS THR LEU ARG
SEQRES 11 A 803 TYR GLY LYS ILE MET ILE MET THR ASP GLN ASP GLN ASP
SEQRES 12 A 803 GLY SER HIS ILE LYS GLY LEU LEU ILE ASN PHE ILE HIS
SEQRES 13 A 803 HIS ASN TRP PRO SER LEU LEU LYS HIS GLY PHE LEU GLU
SEQRES 14 A 803 GLU PHE ILE THR PRO ILE VAL LYS ALA SER LYS ASN LYS
SEQRES 15 A 803 GLN GLU LEU SER PHE TYR SER ILE PRO GLU PHE ASP GLU
SEQRES 16 A 803 TRP LYS LYS HIS ILE GLU ASN GLN LYS ALA TRP LYS ILE
SEQRES 17 A 803 LYS TYR TYR LYS GLY LEU GLY THR SER THR ALA LYS GLU
SEQRES 18 A 803 ALA LYS GLU TYR PHE ALA ASP MET GLU ARG HIS ARG ILE
SEQRES 19 A 803 LEU PHE ARG TYR ALA GLY PRO GLU ASP ASP ALA ALA ILE
SEQRES 20 A 803 THR LEU ALA PHE SER LYS LYS LYS ILE ASP ASP ARG LYS
SEQRES 21 A 803 GLU TRP LEU THR ASN PHE MET GLU ASP ARG ARG GLN ARG
SEQRES 22 A 803 ARG LEU HIS GLY LEU PRO GLU GLN PHE LEU TYR GLY THR
SEQRES 23 A 803 ALA THR LYS HIS LEU THR TYR ASN ASP PHE ILE ASN LYS
SEQRES 24 A 803 GLU LEU ILE LEU PHE SER ASN SER ASP ASN GLU ARG SER
SEQRES 25 A 803 ILE PRO SER LEU VAL ASP GLY PHE LYS PRO GLY GLN ARG
SEQRES 26 A 803 LYS VAL LEU PHE THR CYS PHE LYS ARG ASN ASP LYS ARG
SEQRES 27 A 803 GLU VAL LYS VAL ALA GLN LEU ALA GLY SER VAL ALA GLU
SEQRES 28 A 803 MET SER ALA TYR HIS HIS GLY GLU GLN ALA LEU MET MET
SEQRES 29 A 803 THR ILE VAL ASN LEU ALA GLN ASN PHE VAL GLY SER ASN
SEQRES 30 A 803 ASN ILE ASN LEU LEU GLN PRO ILE GLY GLN PHE GLY THR
SEQRES 31 A 803 ARG LEU HIS GLY GLY LYS ASP ALA ALA SER PRO ARG TYR
SEQRES 32 A 803 ILE PHE THR MET LEU SER THR LEU ALA ARG LEU LEU PHE
SEQRES 33 A 803 PRO ALA VAL ASP ASP ASN LEU LEU LYS PHE LEU TYR ASP
SEQRES 34 A 803 ASP ASN GLN ARG VAL GLU PRO GLU TRP TYR ILE PRO ILE
SEQRES 35 A 803 ILE PRO MET VAL LEU ILE ASN GLY ALA GLU GLY ILE GLY
SEQRES 36 A 803 THR GLY TRP ALA CYS LYS LEU PRO ASN TYR ASP ALA ARG
SEQRES 37 A 803 GLU ILE VAL ASN ASN VAL ARG ARG MET LEU ASP GLY LEU
SEQRES 38 A 803 ASP PRO HIS PRO MET LEU PRO ASN TYR LYS ASN PHE LYS
SEQRES 39 A 803 GLY THR ILE GLN GLU LEU GLY GLN ASN GLN TYR ALA VAL
SEQRES 40 A 803 SER GLY GLU ILE PHE VAL VAL ASP ARG ASN THR VAL GLU
SEQRES 41 A 803 ILE THR GLU LEU PRO VAL ARG THR TRP THR GLN VAL TYR
SEQRES 42 A 803 LYS GLU GLN VAL LEU GLU PRO MET LEU ASN GLY THR ASP
SEQRES 43 A 803 LYS THR PRO ALA LEU ILE SER ASP TYR LYS GLU TYR HIS
SEQRES 44 A 803 THR ASP THR THR VAL LYS PHE VAL VAL LYS MET THR GLU
SEQRES 45 A 803 GLU LYS LEU ALA GLN ALA GLU ALA ALA GLY LEU HIS LYS
SEQRES 46 A 803 VAL PHE LYS LEU GLN THR THR LEU THR CYS ASN SER MET
SEQRES 47 A 803 VAL LEU PHE ASP HIS MET GLY CYS LEU LYS LYS TYR GLU
SEQRES 48 A 803 THR VAL GLN ASP ILE LEU LYS GLU PHE PHE ASP LEU ARG
SEQRES 49 A 803 LEU SER TYR TYR GLY LEU ARG LYS GLU TRP LEU VAL GLY
SEQRES 50 A 803 MET LEU GLY ALA GLU SER THR LYS LEU ASN ASN GLN ALA
SEQRES 51 A 803 ARG PHE ILE LEU GLU LYS ILE GLN GLY LYS ILE THR ILE
SEQRES 52 A 803 GLU ASN ARG SER LYS LYS ASP LEU ILE GLN MET LEU VAL
SEQRES 53 A 803 GLN ARG GLY TYR GLU SER ASP PRO VAL LYS ALA TRP LYS
SEQRES 54 A 803 GLU ALA GLN GLU LYS ALA ALA GLU GLU ASP GLU THR GLN
SEQRES 55 A 803 ASN GLN HIS ASP ASP SER SER SER ASP SER GLY THR PRO
SEQRES 56 A 803 SER GLY PRO ASP PHE ASN TYR ILE LEU ASN MET SER LEU
SEQRES 57 A 803 TRP SER LEU THR LYS GLU LYS VAL GLU GLU LEU ILE LYS
SEQRES 58 A 803 GLN ARG ASP ALA LYS GLY ARG GLU VAL ASN ASP LEU LYS
SEQRES 59 A 803 ARG LYS SER PRO SER ASP LEU TRP LYS GLU ASP LEU ALA
SEQRES 60 A 803 ALA PHE VAL GLU GLU LEU ASP LYS VAL GLU SER GLN GLU
SEQRES 61 A 803 ARG GLU ASP GLY ALA PRO GLY PHE SER SER ILE SER ALA
SEQRES 62 A 803 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 803 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 B 803 ASP ASP ASP ASP LYS VAL PRO ASP PRO THR SER VAL ASP
SEQRES 3 B 803 SER VAL LYS TYR SER LYS ILE LYS GLY ILE PRO LYS LEU
SEQRES 4 B 803 ASP ASP ALA ASN ASP ALA GLY GLY LYS HIS SER LEU GLU
SEQRES 5 B 803 CYS THR LEU ILE LEU THR GLU GLY ASP SER ALA LYS SER
SEQRES 6 B 803 LEU ALA VAL SER GLY LEU GLY VAL ILE GLY ARG ASP ARG
SEQRES 7 B 803 TYR GLY VAL PHE PRO LEU ARG GLY LYS ILE LEU ASN VAL
SEQRES 8 B 803 ARG GLU ALA SER HIS LYS GLN ILE MET GLU ASN ALA GLU
SEQRES 9 B 803 ILE ASN ASN ILE ILE LYS ILE VAL GLY LEU GLN TYR LYS
SEQRES 10 B 803 LYS SER TYR ASP ASP ALA GLU SER LEU LYS THR LEU ARG
SEQRES 11 B 803 TYR GLY LYS ILE MET ILE MET THR ASP GLN ASP GLN ASP
SEQRES 12 B 803 GLY SER HIS ILE LYS GLY LEU LEU ILE ASN PHE ILE HIS
SEQRES 13 B 803 HIS ASN TRP PRO SER LEU LEU LYS HIS GLY PHE LEU GLU
SEQRES 14 B 803 GLU PHE ILE THR PRO ILE VAL LYS ALA SER LYS ASN LYS
SEQRES 15 B 803 GLN GLU LEU SER PHE TYR SER ILE PRO GLU PHE ASP GLU
SEQRES 16 B 803 TRP LYS LYS HIS ILE GLU ASN GLN LYS ALA TRP LYS ILE
SEQRES 17 B 803 LYS TYR TYR LYS GLY LEU GLY THR SER THR ALA LYS GLU
SEQRES 18 B 803 ALA LYS GLU TYR PHE ALA ASP MET GLU ARG HIS ARG ILE
SEQRES 19 B 803 LEU PHE ARG TYR ALA GLY PRO GLU ASP ASP ALA ALA ILE
SEQRES 20 B 803 THR LEU ALA PHE SER LYS LYS LYS ILE ASP ASP ARG LYS
SEQRES 21 B 803 GLU TRP LEU THR ASN PHE MET GLU ASP ARG ARG GLN ARG
SEQRES 22 B 803 ARG LEU HIS GLY LEU PRO GLU GLN PHE LEU TYR GLY THR
SEQRES 23 B 803 ALA THR LYS HIS LEU THR TYR ASN ASP PHE ILE ASN LYS
SEQRES 24 B 803 GLU LEU ILE LEU PHE SER ASN SER ASP ASN GLU ARG SER
SEQRES 25 B 803 ILE PRO SER LEU VAL ASP GLY PHE LYS PRO GLY GLN ARG
SEQRES 26 B 803 LYS VAL LEU PHE THR CYS PHE LYS ARG ASN ASP LYS ARG
SEQRES 27 B 803 GLU VAL LYS VAL ALA GLN LEU ALA GLY SER VAL ALA GLU
SEQRES 28 B 803 MET SER ALA TYR HIS HIS GLY GLU GLN ALA LEU MET MET
SEQRES 29 B 803 THR ILE VAL ASN LEU ALA GLN ASN PHE VAL GLY SER ASN
SEQRES 30 B 803 ASN ILE ASN LEU LEU GLN PRO ILE GLY GLN PHE GLY THR
SEQRES 31 B 803 ARG LEU HIS GLY GLY LYS ASP ALA ALA SER PRO ARG TYR
SEQRES 32 B 803 ILE PHE THR MET LEU SER THR LEU ALA ARG LEU LEU PHE
SEQRES 33 B 803 PRO ALA VAL ASP ASP ASN LEU LEU LYS PHE LEU TYR ASP
SEQRES 34 B 803 ASP ASN GLN ARG VAL GLU PRO GLU TRP TYR ILE PRO ILE
SEQRES 35 B 803 ILE PRO MET VAL LEU ILE ASN GLY ALA GLU GLY ILE GLY
SEQRES 36 B 803 THR GLY TRP ALA CYS LYS LEU PRO ASN TYR ASP ALA ARG
SEQRES 37 B 803 GLU ILE VAL ASN ASN VAL ARG ARG MET LEU ASP GLY LEU
SEQRES 38 B 803 ASP PRO HIS PRO MET LEU PRO ASN TYR LYS ASN PHE LYS
SEQRES 39 B 803 GLY THR ILE GLN GLU LEU GLY GLN ASN GLN TYR ALA VAL
SEQRES 40 B 803 SER GLY GLU ILE PHE VAL VAL ASP ARG ASN THR VAL GLU
SEQRES 41 B 803 ILE THR GLU LEU PRO VAL ARG THR TRP THR GLN VAL TYR
SEQRES 42 B 803 LYS GLU GLN VAL LEU GLU PRO MET LEU ASN GLY THR ASP
SEQRES 43 B 803 LYS THR PRO ALA LEU ILE SER ASP TYR LYS GLU TYR HIS
SEQRES 44 B 803 THR ASP THR THR VAL LYS PHE VAL VAL LYS MET THR GLU
SEQRES 45 B 803 GLU LYS LEU ALA GLN ALA GLU ALA ALA GLY LEU HIS LYS
SEQRES 46 B 803 VAL PHE LYS LEU GLN THR THR LEU THR CYS ASN SER MET
SEQRES 47 B 803 VAL LEU PHE ASP HIS MET GLY CYS LEU LYS LYS TYR GLU
SEQRES 48 B 803 THR VAL GLN ASP ILE LEU LYS GLU PHE PHE ASP LEU ARG
SEQRES 49 B 803 LEU SER TYR TYR GLY LEU ARG LYS GLU TRP LEU VAL GLY
SEQRES 50 B 803 MET LEU GLY ALA GLU SER THR LYS LEU ASN ASN GLN ALA
SEQRES 51 B 803 ARG PHE ILE LEU GLU LYS ILE GLN GLY LYS ILE THR ILE
SEQRES 52 B 803 GLU ASN ARG SER LYS LYS ASP LEU ILE GLN MET LEU VAL
SEQRES 53 B 803 GLN ARG GLY TYR GLU SER ASP PRO VAL LYS ALA TRP LYS
SEQRES 54 B 803 GLU ALA GLN GLU LYS ALA ALA GLU GLU ASP GLU THR GLN
SEQRES 55 B 803 ASN GLN HIS ASP ASP SER SER SER ASP SER GLY THR PRO
SEQRES 56 B 803 SER GLY PRO ASP PHE ASN TYR ILE LEU ASN MET SER LEU
SEQRES 57 B 803 TRP SER LEU THR LYS GLU LYS VAL GLU GLU LEU ILE LYS
SEQRES 58 B 803 GLN ARG ASP ALA LYS GLY ARG GLU VAL ASN ASP LEU LYS
SEQRES 59 B 803 ARG LYS SER PRO SER ASP LEU TRP LYS GLU ASP LEU ALA
SEQRES 60 B 803 ALA PHE VAL GLU GLU LEU ASP LYS VAL GLU SER GLN GLU
SEQRES 61 B 803 ARG GLU ASP GLY ALA PRO GLY PHE SER SER ILE SER ALA
SEQRES 62 B 803 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 C 8 DA DG DC DC DG DA DG DC
SEQRES 1 D 12 DT DG DC DA DG DC DT DC DG DG DC DT
SEQRES 1 E 8 DA DG DC DC DG DA DG DC
SEQRES 1 F 12 DT DG DC DA DG DC DT DC DG DG DC DT
HET EVP A 1 42
HET MG A1222 1
HET MG A1223 1
HET MG B 1 1
HET MG B1222 1
HET EVP D 1 42
HET MG D 21 1
HET MG F 1 1
HETNAM EVP (5S,5AR,8AR,9R)-9-(4-HYDROXY-3,5-DIMETHOXYPHENYL)-8-
HETNAM 2 EVP OXO-5,5A,6,8,8A,9-HEXAHYDROFURO[3',4':6,7]NAPHTHO[2,3-
HETNAM 3 EVP D][1,3]DIOXOL -5-YL 4,6-O-[(1R)-ETHYLIDENE]-BETA-D-
HETNAM 4 EVP GLUCOPYRANOSIDE
HETNAM MG MAGNESIUM ION
HETSYN EVP ETOPOSIDE; VP-16
FORMUL 7 EVP 2(C29 H32 O13)
FORMUL 8 MG 6(MG 2+)
FORMUL 15 HOH *1047(H2 O)
HELIX 1 1 HIS A 467 GLU A 470 5 4
HELIX 2 2 GLY A 478 SER A 487 1 10
HELIX 3 3 VAL A 491 ASP A 495 5 5
HELIX 4 4 SER A 513 ASN A 520 1 8
HELIX 5 5 ASN A 520 GLY A 531 1 12
HELIX 6 6 GLU A 542 LEU A 547 5 6
HELIX 7 7 ASP A 559 TRP A 577 1 19
HELIX 8 8 PRO A 578 HIS A 583 5 6
HELIX 9 9 LYS A 638 ASP A 646 1 9
HELIX 10 10 ASP A 646 HIS A 650 1 5
HELIX 11 11 GLY A 658 SER A 670 1 13
HELIX 12 12 LYS A 673 HIS A 694 1 22
HELIX 13 13 TYR A 711 GLU A 718 1 8
HELIX 14 14 GLU A 718 ILE A 731 1 14
HELIX 15 15 LYS A 739 ASN A 753 1 15
HELIX 16 16 VAL A 760 ALA A 772 1 13
HELIX 17 17 GLY A 776 GLN A 789 1 14
HELIX 18 18 LEU A 829 PHE A 834 1 6
HELIX 19 19 PRO A 835 ASN A 840 1 6
HELIX 20 20 PRO A 862 ASN A 867 1 6
HELIX 21 21 ASP A 884 ASP A 897 1 14
HELIX 22 22 TRP A 947 VAL A 955 1 9
HELIX 23 23 VAL A 955 GLY A 962 1 8
HELIX 24 24 THR A 989 GLY A 1000 1 12
HELIX 25 25 GLY A 1000 PHE A 1005 1 6
HELIX 26 26 THR A 1030 GLN A 1076 1 47
HELIX 27 27 SER A 1085 ARG A 1096 1 12
HELIX 28 28 ASP A 1101 GLN A 1110 1 10
HELIX 29 29 PHE A 1138 ASN A 1143 1 6
HELIX 30 30 SER A 1145 LEU A 1149 5 5
HELIX 31 31 THR A 1150 ARG A 1173 1 24
HELIX 32 32 SER A 1175 ASP A 1201 1 27
HELIX 33 33 HIS B 467 GLU B 470 5 4
HELIX 34 34 GLY B 478 ARG B 494 1 17
HELIX 35 35 SER B 513 GLU B 519 1 7
HELIX 36 36 ASN B 520 GLY B 531 1 12
HELIX 37 37 GLU B 542 LEU B 547 5 6
HELIX 38 38 ASP B 559 TRP B 577 1 19
HELIX 39 39 TRP B 577 HIS B 583 1 7
HELIX 40 40 ALA B 637 ASP B 646 1 10
HELIX 41 41 ASP B 646 HIS B 650 1 5
HELIX 42 42 GLY B 658 SER B 670 1 13
HELIX 43 43 LYS B 673 HIS B 694 1 22
HELIX 44 44 TYR B 711 GLU B 718 1 8
HELIX 45 45 GLU B 718 ILE B 731 1 14
HELIX 46 46 LYS B 739 ASN B 753 1 15
HELIX 47 47 VAL B 760 ALA B 772 1 13
HELIX 48 48 GLY B 776 GLN B 789 1 14
HELIX 49 49 LEU B 829 PHE B 834 1 6
HELIX 50 50 PRO B 835 LEU B 842 5 8
HELIX 51 51 PRO B 862 ASN B 867 1 6
HELIX 52 52 ASP B 884 ASP B 897 1 14
HELIX 53 53 TRP B 947 VAL B 955 1 9
HELIX 54 54 VAL B 955 ASN B 961 1 7
HELIX 55 55 THR B 989 ALA B 999 1 11
HELIX 56 56 GLY B 1000 PHE B 1005 1 6
HELIX 57 57 THR B 1030 GLN B 1076 1 47
HELIX 58 58 SER B 1085 ARG B 1096 1 12
HELIX 59 59 ASP B 1101 GLN B 1110 1 10
HELIX 60 60 PHE B 1138 ASN B 1143 1 6
HELIX 61 61 SER B 1145 LEU B 1149 5 5
HELIX 62 62 THR B 1150 LYS B 1174 1 25
HELIX 63 63 SER B 1175 ASP B 1201 1 27
SHEET 1 A 6 TYR A 497 LEU A 502 0
SHEET 2 A 6 THR A 472 GLU A 477 1 N THR A 476 O LEU A 502
SHEET 3 A 6 LYS A 551 MET A 555 1 O MET A 553 N LEU A 473
SHEET 4 A 6 LEU A 586 PHE A 589 1 O GLU A 587 N ILE A 554
SHEET 5 A 6 ARG A 651 ARG A 655 -1 O ILE A 652 N GLU A 588
SHEET 6 A 6 HIS A 708 THR A 710 1 O LEU A 709 N ARG A 655
SHEET 1 B 2 VAL A 758 LYS A 759 0
SHEET 2 B 2 PHE A 823 THR A 824 -1 O THR A 824 N VAL A 758
SHEET 1 C 2 PHE A 844 ASP A 847 0
SHEET 2 C 2 GLN A 850 PRO A 854 -1 O VAL A 852 N LEU A 845
SHEET 1 D 2 GLU A 870 ILE A 872 0
SHEET 2 D 2 ALA A 877 LYS A 879 -1 O CYS A 878 N GLY A 871
SHEET 1 E 3 THR A 914 GLY A 919 0
SHEET 2 E 3 GLN A 922 SER A 926 -1 O GLN A 922 N LEU A 918
SHEET 3 E 3 GLN A1008 THR A1012 -1 O LEU A1011 N TYR A 923
SHEET 1 F 4 GLU A 928 ASP A 933 0
SHEET 2 F 4 THR A 936 GLU A 941 -1 O GLU A 938 N PHE A 930
SHEET 3 F 4 PHE A 984 LYS A 987 -1 O VAL A 986 N VAL A 937
SHEET 4 F 4 ASP A 972 GLU A 975 -1 N ASP A 972 O LYS A 987
SHEET 1 G 2 MET A1016 PHE A1019 0
SHEET 2 G 2 LEU A1025 TYR A1028 -1 O TYR A1028 N MET A1016
SHEET 1 H 6 TYR B 497 LEU B 502 0
SHEET 2 H 6 THR B 472 GLU B 477 1 N THR B 476 O LEU B 502
SHEET 3 H 6 LYS B 551 MET B 555 1 O MET B 555 N LEU B 475
SHEET 4 H 6 LEU B 586 PHE B 589 1 O GLU B 587 N ILE B 554
SHEET 5 H 6 ARG B 651 ARG B 655 -1 O ILE B 652 N GLU B 588
SHEET 6 H 6 HIS B 708 THR B 710 1 O LEU B 709 N LEU B 653
SHEET 1 I 2 VAL B 758 LYS B 759 0
SHEET 2 I 2 PHE B 823 THR B 824 -1 O THR B 824 N VAL B 758
SHEET 1 J 2 PHE B 844 ASP B 847 0
SHEET 2 J 2 GLN B 850 PRO B 854 -1 O VAL B 852 N LEU B 845
SHEET 1 K 2 GLU B 870 ILE B 872 0
SHEET 2 K 2 ALA B 877 LYS B 879 -1 O CYS B 878 N GLY B 871
SHEET 1 L 3 THR B 914 GLY B 919 0
SHEET 2 L 3 GLN B 922 SER B 926 -1 O SER B 926 N THR B 914
SHEET 3 L 3 GLN B1008 THR B1012 -1 O THR B1009 N VAL B 925
SHEET 1 M 4 GLU B 928 ASP B 933 0
SHEET 2 M 4 THR B 936 GLU B 941 -1 O GLU B 938 N PHE B 930
SHEET 3 M 4 PHE B 984 LYS B 987 -1 O VAL B 986 N VAL B 937
SHEET 4 M 4 ASP B 972 GLU B 975 -1 N ASP B 972 O LYS B 987
SHEET 1 N 2 MET B1016 PHE B1019 0
SHEET 2 N 2 LEU B1025 TYR B1028 -1 O TYR B1028 N MET B1016
LINK OH TYR A 821 P DT F 9 1555 1555 1.62
LINK OH TYR B 821 P DT D 9 1555 1555 1.62
LINK OD2 ASP A 557 MG MG A1222 1555 1555 2.30
LINK OD2 ASP A 559 MG MG A1222 1555 1555 2.24
LINK MG MG A1222 O HOH A1333 1555 1555 2.22
LINK MG MG A1222 O HOH A1348 1555 1555 2.34
LINK MG MG A1222 O HOH C 633 1555 1555 2.37
LINK MG MG A1222 O HOH C 795 1555 1555 2.32
LINK MG MG A1223 O HOH A1466 1555 1555 2.51
LINK MG MG A1223 O HOH A1467 1555 1555 2.20
LINK MG MG A1223 O HOH C1143 1555 1555 2.07
LINK MG MG A1223 O HOH C1145 1555 1555 2.21
LINK MG MG B 1 O HOH B 46 1555 1555 2.24
LINK MG MG B 1 OD2 ASP B 557 1555 1555 2.31
LINK MG MG B 1 OD2 ASP B 559 1555 1555 2.12
LINK MG MG B 1 O HOH B1250 1555 1555 2.29
LINK MG MG B 1 O HOH B1291 1555 1555 2.34
LINK MG MG B 1 O HOH E 64 1555 1555 2.38
LINK MG MG B1222 O HOH B1470 1555 1555 1.91
LINK MG MG B1222 O HOH E1148 1555 1555 2.21
LINK MG MG B1222 O HOH E1150 1555 1555 2.02
LINK MG MG D 21 O HOH D 553 1555 1555 2.11
LINK MG MG D 21 O HOH D 765 1555 1555 2.36
LINK MG MG D 21 O HOH D 766 1555 1555 2.37
LINK MG MG D 21 O HOH D 767 1555 1555 2.39
LINK MG MG D 21 O HOH D 768 1555 1555 2.20
LINK MG MG D 21 O HOH E1224 1555 1555 2.45
LINK MG MG F 1 O HOH F 763 1555 1555 2.20
LINK MG MG F 1 O HOH F 764 1555 1555 2.31
LINK MG MG F 1 O HOH F 866 1555 1555 2.37
LINK MG MG F 1 O HOH F1123 1555 1555 2.00
SITE 1 AC1 10 GLY A 478 ASP A 479 ARG A 503 GLN A 778
SITE 2 AC1 10 MET A 782 DC C 8 DT D 9 DG D 10
SITE 3 AC1 10 DA F 12 DG F 13
SITE 1 AC2 2 ASP A 557 ASP A 559
SITE 1 AC3 3 ASN A 867 GLY A 868 GLU A 870
SITE 1 AC4 2 ASP B 557 ASP B 559
SITE 1 AC5 1 ASN B 867
SITE 1 AC6 9 GLY B 478 ASP B 479 ARG B 503 MET B 782
SITE 2 AC6 9 DA D 12 DG D 13 DC E 8 DT F 9
SITE 3 AC6 9 DG F 10
CRYST1 80.149 176.801 94.067 90.00 111.58 90.00 P 1 21 1 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 0.012477 0.000000 0.004935 0.00000
SCALE2 0.000000 0.005656 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011432 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
