HEADER ISOMERASE/DNA 01-MAR-00 1EJ9
TITLE CRYSTAL STRUCTURE OF HUMAN TOPOISOMERASE I DNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-
COMPND 3 D(*C*AP*AP*AP*AP*AP*GP*AP*CP*TP*CP*AP*GP*AP*AP*AP*AP*AP*TP*
COMPND 4 TP*TP*TP*T)-3');
COMPND 5 CHAIN: C;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-
COMPND 9 D(*C*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*TP*GP*AP*GP*TP*CP*TP*
COMPND 10 TP*TP*TP*T)-3');
COMPND 11 CHAIN: D;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: DNA TOPOISOMERASE I;
COMPND 15 CHAIN: A;
COMPND 16 FRAGMENT: C-TERMINAL DOMAIN, RESIDUES 203-765;
COMPND 17 EC: 5.99.1.2;
COMPND 18 ENGINEERED: YES;
COMPND 19 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 10 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 12 EXPRESSION_SYSTEM_CELL: SF9 INSECT CELLS
KEYWDS PROTEIN-DNA COMPLEX, TYPE I TOPOISOMERASE, HUMAN,
KEYWDS 2 ISOMERASE/DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.R.REDINBO,J.J.CHAMPOUX,W.G.HOL
REVDAT 2 24-FEB-09 1EJ9 1 VERSN
REVDAT 1 03-AUG-00 1EJ9 0
JRNL AUTH M.R.REDINBO,J.J.CHAMPOUX,W.G.HOL
JRNL TITL NOVEL INSIGHTS INTO CATALYTIC MECHANISM FROM A
JRNL TITL 2 CRYSTAL STRUCTURE OF HUMAN TOPOISOMERASE I IN
JRNL TITL 3 COMPLEX WITH DNA.
JRNL REF BIOCHEMISTRY V. 39 6832 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10841763
JRNL DOI 10.1021/BI992690T
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 29616
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2139
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3966
REMARK 3 NUCLEIC ACID ATOMS : 896
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 353
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 1.74
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EJ9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-00.
REMARK 100 THE RCSB ID CODE IS RCSB010631.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OTHER
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29834
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 1.0
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 0.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.28800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEG 400, 145 MM MGCL2, 20 MM
REMARK 280 MES PH 6.8, 5 MM TRIS PH 8.0, 30 MM DTT, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 295K
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 62.46000
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, A
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 DC C 0
REMARK 465 DC D 100
REMARK 465 ILE A 634
REMARK 465 ALA A 635
REMARK 465 PRO A 636
REMARK 465 PRO A 637
REMARK 465 LYS A 638
REMARK 465 THR A 639
REMARK 465 PHE A 640
REMARK 465 GLU A 641
REMARK 465 LYS A 642
REMARK 465 SER A 643
REMARK 465 MET A 644
REMARK 465 MET A 645
REMARK 465 ASN A 646
REMARK 465 LEU A 647
REMARK 465 GLN A 648
REMARK 465 THR A 649
REMARK 465 LYS A 650
REMARK 465 ILE A 651
REMARK 465 ASP A 652
REMARK 465 ALA A 653
REMARK 465 LYS A 654
REMARK 465 LYS A 655
REMARK 465 GLU A 656
REMARK 465 GLN A 657
REMARK 465 LEU A 658
REMARK 465 ALA A 659
REMARK 465 ASP A 660
REMARK 465 ALA A 661
REMARK 465 ARG A 662
REMARK 465 ARG A 663
REMARK 465 ASP A 664
REMARK 465 LEU A 665
REMARK 465 LYS A 666
REMARK 465 SER A 667
REMARK 465 ALA A 668
REMARK 465 LYS A 669
REMARK 465 ALA A 670
REMARK 465 ASP A 671
REMARK 465 ALA A 672
REMARK 465 LYS A 673
REMARK 465 VAL A 674
REMARK 465 MET A 675
REMARK 465 LYS A 676
REMARK 465 ASP A 677
REMARK 465 ALA A 678
REMARK 465 LYS A 679
REMARK 465 THR A 680
REMARK 465 LYS A 681
REMARK 465 LYS A 682
REMARK 465 VAL A 683
REMARK 465 VAL A 684
REMARK 465 GLU A 685
REMARK 465 SER A 686
REMARK 465 LYS A 687
REMARK 465 LYS A 688
REMARK 465 LYS A 689
REMARK 465 ALA A 690
REMARK 465 VAL A 691
REMARK 465 GLN A 692
REMARK 465 ARG A 693
REMARK 465 LEU A 694
REMARK 465 GLU A 695
REMARK 465 GLU A 696
REMARK 465 GLN A 697
REMARK 465 LEU A 698
REMARK 465 MET A 699
REMARK 465 LYS A 700
REMARK 465 LEU A 701
REMARK 465 GLU A 702
REMARK 465 VAL A 703
REMARK 465 GLN A 704
REMARK 465 ALA A 705
REMARK 465 THR A 706
REMARK 465 ASP A 707
REMARK 465 ARG A 708
REMARK 465 GLU A 709
REMARK 465 GLU A 710
REMARK 465 ASN A 711
REMARK 465 LYS A 712
REMARK 465 GLN A 713
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 DA C 1 P OP1 OP2
REMARK 470 DA D 101 P OP1 OP2
REMARK 470 GLU A 209 CG CD OE1 OE2
REMARK 470 ARG A 210 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 213 CG CD OE1 OE2
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 LYS A 321 CG CD CE NZ
REMARK 470 GLU A 322 CG CD OE1 OE2
REMARK 470 LYS A 326 CG CD CE NZ
REMARK 470 LYS A 333 CG CD CE NZ
REMARK 470 GLU A 463 CG CD OE1 OE2
REMARK 470 LYS A 468 CG CD CE NZ
REMARK 470 GLU A 495 CG CD OE1 OE2
REMARK 470 ARG A 546 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 582 CG CD OE1 OE2
REMARK 470 ASP A 609 CG OD1 OD2
REMARK 470 GLU A 610 CG CD OE1 OE2
REMARK 470 ASN A 611 CG OD1 ND2
REMARK 470 ASP A 760 CG OD1 OD2
REMARK 470 ASP A 762 CG OD1 OD2
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 DA C 1 O5' - C5' - C4' ANGL. DEV. = -6.3 DEGREES
REMARK 500 DC C 10 C3' - C2' - C1' ANGL. DEV. = -5.6 DEGREES
REMARK 500 DA D 103 C3' - C2' - C1' ANGL. DEV. = -5.2 DEGREES
REMARK 500 DT D 112 C3' - C2' - C1' ANGL. DEV. = -6.6 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 LYS A 204 72.78 -67.70
REMARK 500 PRO A 212 -179.39 -61.79
REMARK 500 LEU A 264 -36.42 -33.26
REMARK 500 THR A 269 0.25 -62.96
REMARK 500 MET A 319 153.34 -38.25
REMARK 500 ASP A 344 -117.65 57.49
REMARK 500 CYS A 453 16.97 -141.56
REMARK 500 SER A 467 156.01 -41.38
REMARK 500 ALA A 486 38.27 75.69
REMARK 500 LEU A 518 135.72 -172.75
REMARK 500 ASP A 528 94.61 -161.87
REMARK 500 PHE A 565 55.13 -96.15
REMARK 500 ASP A 566 177.82 -57.43
REMARK 500 ASP A 609 36.32 -80.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 DC C 8 0.07 SIDE_CHAIN
REMARK 500 DA C 17 0.05 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A36 RELATED DB: PDB
REMARK 900 RELATED ID: 1A35 RELATED DB: PDB
REMARK 900 RELATED ID: 1A31 RELATED DB: PDB
DBREF 1EJ9 A 203 765 UNP P11387 TOP1_HUMAN 203 765
DBREF 1EJ9 C 0 22 PDB 1EJ9 1EJ9 0 22
DBREF 1EJ9 D 100 122 PDB 1EJ9 1EJ9 100 122
SEQADV 1EJ9 ILE A 634 UNP P11387 ARG 634 ENGINEERED
SEQADV 1EJ9 PHE A 723 UNP P11387 TYR 723 ENGINEERED
SEQRES 1 C 23 DC DA DA DA DA DA DG DA DC DT DC DA DG
SEQRES 2 C 23 DA DA DA DA DA DT DT DT DT DT
SEQRES 1 D 23 DC DA DA DA DA DA DT DT DT DT DT DC DT
SEQRES 2 D 23 DG DA DG DT DC DT DT DT DT DT
SEQRES 1 A 563 TRP LYS TRP TRP GLU GLU GLU ARG TYR PRO GLU GLY ILE
SEQRES 2 A 563 LYS TRP LYS PHE LEU GLU HIS LYS GLY PRO VAL PHE ALA
SEQRES 3 A 563 PRO PRO TYR GLU PRO LEU PRO GLU ASN VAL LYS PHE TYR
SEQRES 4 A 563 TYR ASP GLY LYS VAL MET LYS LEU SER PRO LYS ALA GLU
SEQRES 5 A 563 GLU VAL ALA THR PHE PHE ALA LYS MET LEU ASP HIS GLU
SEQRES 6 A 563 TYR THR THR LYS GLU ILE PHE ARG LYS ASN PHE PHE LYS
SEQRES 7 A 563 ASP TRP ARG LYS GLU MET THR ASN GLU GLU LYS ASN ILE
SEQRES 8 A 563 ILE THR ASN LEU SER LYS CYS ASP PHE THR GLN MET SER
SEQRES 9 A 563 GLN TYR PHE LYS ALA GLN THR GLU ALA ARG LYS GLN MET
SEQRES 10 A 563 SER LYS GLU GLU LYS LEU LYS ILE LYS GLU GLU ASN GLU
SEQRES 11 A 563 LYS LEU LEU LYS GLU TYR GLY PHE CYS ILE MET ASP ASN
SEQRES 12 A 563 HIS LYS GLU ARG ILE ALA ASN PHE LYS ILE GLU PRO PRO
SEQRES 13 A 563 GLY LEU PHE ARG GLY ARG GLY ASN HIS PRO LYS MET GLY
SEQRES 14 A 563 MET LEU LYS ARG ARG ILE MET PRO GLU ASP ILE ILE ILE
SEQRES 15 A 563 ASN CYS SER LYS ASP ALA LYS VAL PRO SER PRO PRO PRO
SEQRES 16 A 563 GLY HIS LYS TRP LYS GLU VAL ARG HIS ASP ASN LYS VAL
SEQRES 17 A 563 THR TRP LEU VAL SER TRP THR GLU ASN ILE GLN GLY SER
SEQRES 18 A 563 ILE LYS TYR ILE MET LEU ASN PRO SER SER ARG ILE LYS
SEQRES 19 A 563 GLY GLU LYS ASP TRP GLN LYS TYR GLU THR ALA ARG ARG
SEQRES 20 A 563 LEU LYS LYS CYS VAL ASP LYS ILE ARG ASN GLN TYR ARG
SEQRES 21 A 563 GLU ASP TRP LYS SER LYS GLU MET LYS VAL ARG GLN ARG
SEQRES 22 A 563 ALA VAL ALA LEU TYR PHE ILE ASP LYS LEU ALA LEU ARG
SEQRES 23 A 563 ALA GLY ASN GLU LYS GLU GLU GLY GLU THR ALA ASP THR
SEQRES 24 A 563 VAL GLY CYS CYS SER LEU ARG VAL GLU HIS ILE ASN LEU
SEQRES 25 A 563 HIS PRO GLU LEU ASP GLY GLN GLU TYR VAL VAL GLU PHE
SEQRES 26 A 563 ASP PHE LEU GLY LYS ASP SER ILE ARG TYR TYR ASN LYS
SEQRES 27 A 563 VAL PRO VAL GLU LYS ARG VAL PHE LYS ASN LEU GLN LEU
SEQRES 28 A 563 PHE MET GLU ASN LYS GLN PRO GLU ASP ASP LEU PHE ASP
SEQRES 29 A 563 ARG LEU ASN THR GLY ILE LEU ASN LYS HIS LEU GLN ASP
SEQRES 30 A 563 LEU MET GLU GLY LEU THR ALA LYS VAL PHE ARG THR TYR
SEQRES 31 A 563 ASN ALA SER ILE THR LEU GLN GLN GLN LEU LYS GLU LEU
SEQRES 32 A 563 THR ALA PRO ASP GLU ASN ILE PRO ALA LYS ILE LEU SER
SEQRES 33 A 563 TYR ASN ARG ALA ASN ARG ALA VAL ALA ILE LEU CYS ASN
SEQRES 34 A 563 HIS GLN ILE ALA PRO PRO LYS THR PHE GLU LYS SER MET
SEQRES 35 A 563 MET ASN LEU GLN THR LYS ILE ASP ALA LYS LYS GLU GLN
SEQRES 36 A 563 LEU ALA ASP ALA ARG ARG ASP LEU LYS SER ALA LYS ALA
SEQRES 37 A 563 ASP ALA LYS VAL MET LYS ASP ALA LYS THR LYS LYS VAL
SEQRES 38 A 563 VAL GLU SER LYS LYS LYS ALA VAL GLN ARG LEU GLU GLU
SEQRES 39 A 563 GLN LEU MET LYS LEU GLU VAL GLN ALA THR ASP ARG GLU
SEQRES 40 A 563 GLU ASN LYS GLN ILE ALA LEU GLY THR SER LYS LEU ASN
SEQRES 41 A 563 PHE LEU ASP PRO ARG ILE THR VAL ALA TRP CYS LYS LYS
SEQRES 42 A 563 TRP GLY VAL PRO ILE GLU LYS ILE TYR ASN LYS THR GLN
SEQRES 43 A 563 ARG GLU LYS PHE ALA TRP ALA ILE ASP MET ALA ASP GLU
SEQRES 44 A 563 ASP TYR GLU PHE
FORMUL 4 HOH *353(H2 O)
HELIX 1 1 LYS A 204 GLU A 208 5 5
HELIX 2 2 SER A 250 LYS A 262 1 13
HELIX 3 3 GLU A 267 THR A 270 5 4
HELIX 4 4 LYS A 271 GLU A 285 1 15
HELIX 5 5 THR A 287 ILE A 294 1 8
HELIX 6 6 PHE A 302 MET A 319 1 18
HELIX 7 7 SER A 320 GLY A 339 1 20
HELIX 8 8 MET A 378 ASP A 381 5 4
HELIX 9 9 SER A 433 TRP A 465 1 33
HELIX 10 10 GLU A 469 ALA A 486 1 18
HELIX 11 11 LYS A 532 SER A 534 5 3
HELIX 12 12 GLU A 544 MET A 555 1 12
HELIX 13 13 ASN A 569 MET A 581 1 13
HELIX 14 14 THR A 585 THR A 606 1 22
HELIX 15 15 ASN A 611 ASN A 631 1 21
HELIX 16 16 LEU A 716 PHE A 723 1 8
HELIX 17 17 ASP A 725 TRP A 736 1 12
HELIX 18 18 PRO A 739 ILE A 743 5 5
HELIX 19 19 ASN A 745 ALA A 753 1 9
HELIX 20 20 PHE A 752 MET A 758 1 7
SHEET 1 A 3 LEU A 220 GLU A 221 0
SHEET 2 A 3 PHE A 340 MET A 343 -1 N ILE A 342 O GLU A 221
SHEET 3 A 3 HIS A 346 ARG A 349 -1 N HIS A 346 O MET A 343
SHEET 1 B 3 LYS A 245 VAL A 246 0
SHEET 2 B 3 TYR A 241 TYR A 242 -1 N TYR A 242 O LYS A 245
SHEET 3 B 3 CYS A 300 ASP A 301 -1 N ASP A 301 O TYR A 241
SHEET 1 C 2 GLY A 359 LEU A 360 0
SHEET 2 C 2 LEU A 373 LYS A 374 -1 N LYS A 374 O GLY A 359
SHEET 1 D 4 GLU A 403 ARG A 405 0
SHEET 2 D 4 ILE A 383 ASN A 385 1 O ILE A 384 N ARG A 405
SHEET 3 D 4 VAL A 414 GLU A 418 -1 O SER A 415 N ILE A 383
SHEET 4 D 4 SER A 423 ILE A 427 -1 O SER A 423 N GLU A 418
SHEET 1 E 3 ILE A 512 LEU A 518 0
SHEET 2 E 3 GLN A 521 LEU A 530 -1 O GLN A 521 N LEU A 518
SHEET 3 E 3 ARG A 536 PRO A 542 -1 N TYR A 537 O PHE A 529
CRYST1 56.980 124.920 72.290 90.00 93.84 90.00 P 1 21 1 2
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 0.017550 0.000000 0.001178 0.00000
SCALE2 0.000000 0.008005 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013864 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
