HEADER ISOMERASE/DNA 08-DEC-03 1RR8
TITLE STRUCTURAL MECHANISMS OF CAMPTOTHECIN RESISTANCE BY
TITLE 2 MUTATIONS IN HUMAN TOPOISOMERASE I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-
COMPND 3 D(*AP*AP*AP*AP*AP*GP*AP*CP*TP*T*GP*GP*AP*AP*AP*AP*AP*TP*TP*
COMPND 4 TP*TP*T)-3';
COMPND 5 CHAIN: A;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 5'-
COMPND 9 D(*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*CP*AP*AP*GP*TP*CP*TP*TP
COMPND 10 *TP*TP*T)-3';
COMPND 11 CHAIN: B;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: DNA TOPOISOMERASE I;
COMPND 15 CHAIN: C;
COMPND 16 EC: 5.99.1.2;
COMPND 17 ENGINEERED: YES;
COMPND 18 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 GENE: TOP1;
SOURCE 10 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 11 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 13 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR: PFACTBAC1
KEYWDS PROTEIN-DNA COMPLEX, TOPOTECAN, CAMPTOTHECIN, NUCLEIC ACID,
KEYWDS 2 HUMAN TOPOISOMERASE I, ISOMERASE/DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.E.CHRENCIK,B.L.STAKER,A.B.BURGIN,L.STEWART,M.R.REDINBO
REVDAT 2 24-FEB-09 1RR8 1 VERSN
REVDAT 1 06-JUL-04 1RR8 0
JRNL AUTH J.E.CHRENCIK,B.L.STAKER,A.B.BURGIN,P.POURQUIER,
JRNL AUTH 2 Y.POMMIER,L.STEWART,M.R.REDINBO
JRNL TITL MECHANISMS OF CAMPTOTHECIN RESISTANCE BY HUMAN
JRNL TITL 2 TOPOISOMERASE I MUTATIONS
JRNL REF J.MOL.BIOL. V. 339 773 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15165849
JRNL DOI 10.1016/J.JMB.2004.03.077
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 10.0
REMARK 3 NUMBER OF REFLECTIONS : 27855
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) : 0.242
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2744
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 2744
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.006
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4124
REMARK 3 NUCLEIC ACID ATOMS : 895
REMARK 3 HETEROGEN ATOMS : 63
REMARK 3 SOLVENT ATOMS : 304
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.53000
REMARK 3 B22 (A**2) : -7.52000
REMARK 3 B33 (A**2) : 5.99000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 5.78000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM SIGMAA (A) : 0.42
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.48
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.53
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.054
REMARK 3 BOND ANGLES (DEGREES) : 2.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.55
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1RR8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-03.
REMARK 100 THE RCSB ID CODE IS RCSB020981.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27855
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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) : 2.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1K4T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, 200MM LITHIUM SULFATE,
REMARK 280 100MM MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 289K
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 57.79250
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: A, B, C
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 PRO C 637
REMARK 465 LYS C 638
REMARK 465 THR C 639
REMARK 465 PHE C 640
REMARK 465 GLU C 641
REMARK 465 LYS C 642
REMARK 465 SER C 643
REMARK 465 MET C 644
REMARK 465 MET C 645
REMARK 465 ASN C 646
REMARK 465 LEU C 647
REMARK 465 GLN C 648
REMARK 465 THR C 649
REMARK 465 LYS C 650
REMARK 465 ILE C 651
REMARK 465 ASP C 652
REMARK 465 ALA C 653
REMARK 465 LYS C 654
REMARK 465 LYS C 655
REMARK 465 GLU C 656
REMARK 465 GLN C 657
REMARK 465 LEU C 658
REMARK 465 ALA C 659
REMARK 465 ASP C 660
REMARK 465 ALA C 661
REMARK 465 ARG C 662
REMARK 465 ARG C 663
REMARK 465 ASP C 664
REMARK 465 LEU C 665
REMARK 465 LYS C 666
REMARK 465 SER C 667
REMARK 465 ALA C 668
REMARK 465 LYS C 669
REMARK 465 ALA C 670
REMARK 465 ASP C 671
REMARK 465 ALA C 672
REMARK 465 LYS C 673
REMARK 465 VAL C 674
REMARK 465 MET C 675
REMARK 465 LYS C 676
REMARK 465 ASP C 677
REMARK 465 ALA C 678
REMARK 465 LYS C 679
REMARK 465 THR C 680
REMARK 465 LYS C 681
REMARK 465 LYS C 682
REMARK 465 VAL C 683
REMARK 465 VAL C 684
REMARK 465 GLU C 685
REMARK 465 SER C 686
REMARK 465 LYS C 687
REMARK 465 LYS C 688
REMARK 465 LYS C 689
REMARK 465 ALA C 690
REMARK 465 VAL C 691
REMARK 465 GLN C 692
REMARK 465 ARG C 693
REMARK 465 LEU C 694
REMARK 465 GLU C 695
REMARK 465 GLU C 696
REMARK 465 GLN C 697
REMARK 465 LEU C 698
REMARK 465 MET C 699
REMARK 465 LYS C 700
REMARK 465 LEU C 701
REMARK 465 GLU C 702
REMARK 465 VAL C 703
REMARK 465 GLN C 704
REMARK 465 ALA C 705
REMARK 465 THR C 706
REMARK 465 ASP C 707
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 DT A 10 O3'
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 OP1 DG A 11 O HOH A 886 1.67
REMARK 500 P DG A 11 O HOH A 886 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 DG A 11 P DG A 11 O5' 1.590
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 DG A 11 O5' - P - OP2 ANGL. DEV. = -13.1 DEGREES
REMARK 500 DG A 11 P - O5' - C5' ANGL. DEV. = -86.9 DEGREES
REMARK 500 LEU C 335 CA - CB - CG ANGL. DEV. = 13.9 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 THR C 303 -38.73 -39.83
REMARK 500 ASP C 344 89.33 47.48
REMARK 500 ASN C 345 -2.31 59.44
REMARK 500 ALA C 351 -83.43 -66.51
REMARK 500 ASN C 352 78.58 -117.93
REMARK 500 CYS C 453 -15.38 -145.46
REMARK 500 ASN C 711 30.91 -83.71
REMARK 500 ALA C 759 136.69 170.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PTR C 723 LEU C 724 -131.63
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 DA A 1 0.05 SIDE_CHAIN
REMARK 500 DT A 9 0.06 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 856 DISTANCE = 10.18 ANGSTROMS
REMARK 525 HOH C 783 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH A 916 DISTANCE = 16.84 ANGSTROMS
REMARK 525 HOH C 934 DISTANCE = 5.37 ANGSTROMS
REMARK 525 HOH C1024 DISTANCE = 7.04 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTG A 1991
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTC A 100
DBREF 1RR8 C 203 765 UNP P11387 TOP1_HUMAN 203 765
DBREF 1RR8 A 1 22 PDB 1RR8 1RR8 1 22
DBREF 1RR8 B 101 122 PDB 1RR8 1RR8 101 122
SEQADV 1RR8 ALA C 201 UNP P11387 CLONING ARTIFACT
SEQADV 1RR8 ALA C 202 UNP P11387 CLONING ARTIFACT
SEQADV 1RR8 SER C 361 UNP P11387 PHE 361 ENGINEERED
SEQADV 1RR8 GLN C 634 UNP P11387 ARG 634 ENGINEERED
SEQADV 1RR8 PTR C 723 UNP P11387 TYR 723 MODIFIED RESIDUE
SEQRES 1 A 22 DA DA DA DA DA DG DA DC DT DT DG DG DA
SEQRES 2 A 22 DA DA DA DA DT DT DT DT DT
SEQRES 1 B 22 DA DA DA DA DA DT DT DT DT DT DC DC DA
SEQRES 2 B 22 DA DG DT DC DT DT DT DT DT
SEQRES 1 C 565 ALA ALA TRP LYS TRP TRP GLU GLU GLU ARG TYR PRO GLU
SEQRES 2 C 565 GLY ILE LYS TRP LYS PHE LEU GLU HIS LYS GLY PRO VAL
SEQRES 3 C 565 PHE ALA PRO PRO TYR GLU PRO LEU PRO GLU ASN VAL LYS
SEQRES 4 C 565 PHE TYR TYR ASP GLY LYS VAL MET LYS LEU SER PRO LYS
SEQRES 5 C 565 ALA GLU GLU VAL ALA THR PHE PHE ALA LYS MET LEU ASP
SEQRES 6 C 565 HIS GLU TYR THR THR LYS GLU ILE PHE ARG LYS ASN PHE
SEQRES 7 C 565 PHE LYS ASP TRP ARG LYS GLU MET THR ASN GLU GLU LYS
SEQRES 8 C 565 ASN ILE ILE THR ASN LEU SER LYS CYS ASP PHE THR GLN
SEQRES 9 C 565 MET SER GLN TYR PHE LYS ALA GLN THR GLU ALA ARG LYS
SEQRES 10 C 565 GLN MET SER LYS GLU GLU LYS LEU LYS ILE LYS GLU GLU
SEQRES 11 C 565 ASN GLU LYS LEU LEU LYS GLU TYR GLY PHE CYS ILE MET
SEQRES 12 C 565 ASP ASN HIS LYS GLU ARG ILE ALA ASN PHE LYS ILE GLU
SEQRES 13 C 565 PRO PRO GLY LEU SER ARG GLY ARG GLY ASN HIS PRO LYS
SEQRES 14 C 565 MET GLY MET LEU LYS ARG ARG ILE MET PRO GLU ASP ILE
SEQRES 15 C 565 ILE ILE ASN CYS SER LYS ASP ALA LYS VAL PRO SER PRO
SEQRES 16 C 565 PRO PRO GLY HIS LYS TRP LYS GLU VAL ARG HIS ASP ASN
SEQRES 17 C 565 LYS VAL THR TRP LEU VAL SER TRP THR GLU ASN ILE GLN
SEQRES 18 C 565 GLY SER ILE LYS TYR ILE MET LEU ASN PRO SER SER ARG
SEQRES 19 C 565 ILE LYS GLY GLU LYS ASP TRP GLN LYS TYR GLU THR ALA
SEQRES 20 C 565 ARG ARG LEU LYS LYS CYS VAL ASP LYS ILE ARG ASN GLN
SEQRES 21 C 565 TYR ARG GLU ASP TRP LYS SER LYS GLU MET LYS VAL ARG
SEQRES 22 C 565 GLN ARG ALA VAL ALA LEU TYR PHE ILE ASP LYS LEU ALA
SEQRES 23 C 565 LEU ARG ALA GLY ASN GLU LYS GLU GLU GLY GLU THR ALA
SEQRES 24 C 565 ASP THR VAL GLY CYS CYS SER LEU ARG VAL GLU HIS ILE
SEQRES 25 C 565 ASN LEU HIS PRO GLU LEU ASP GLY GLN GLU TYR VAL VAL
SEQRES 26 C 565 GLU PHE ASP PHE LEU GLY LYS ASP SER ILE ARG TYR TYR
SEQRES 27 C 565 ASN LYS VAL PRO VAL GLU LYS ARG VAL PHE LYS ASN LEU
SEQRES 28 C 565 GLN LEU PHE MET GLU ASN LYS GLN PRO GLU ASP ASP LEU
SEQRES 29 C 565 PHE ASP ARG LEU ASN THR GLY ILE LEU ASN LYS HIS LEU
SEQRES 30 C 565 GLN ASP LEU MET GLU GLY LEU THR ALA LYS VAL PHE ARG
SEQRES 31 C 565 THR TYR ASN ALA SER ILE THR LEU GLN GLN GLN LEU LYS
SEQRES 32 C 565 GLU LEU THR ALA PRO ASP GLU ASN ILE PRO ALA LYS ILE
SEQRES 33 C 565 LEU SER TYR ASN ARG ALA ASN ARG ALA VAL ALA ILE LEU
SEQRES 34 C 565 CYS ASN HIS GLN GLN ALA PRO PRO LYS THR PHE GLU LYS
SEQRES 35 C 565 SER MET MET ASN LEU GLN THR LYS ILE ASP ALA LYS LYS
SEQRES 36 C 565 GLU GLN LEU ALA ASP ALA ARG ARG ASP LEU LYS SER ALA
SEQRES 37 C 565 LYS ALA ASP ALA LYS VAL MET LYS ASP ALA LYS THR LYS
SEQRES 38 C 565 LYS VAL VAL GLU SER LYS LYS LYS ALA VAL GLN ARG LEU
SEQRES 39 C 565 GLU GLU GLN LEU MET LYS LEU GLU VAL GLN ALA THR ASP
SEQRES 40 C 565 ARG GLU GLU ASN LYS GLN ILE ALA LEU GLY THR SER LYS
SEQRES 41 C 565 LEU ASN PTR LEU ASP PRO ARG ILE THR VAL ALA TRP CYS
SEQRES 42 C 565 LYS LYS TRP GLY VAL PRO ILE GLU LYS ILE TYR ASN LYS
SEQRES 43 C 565 THR GLN ARG GLU LYS PHE ALA TRP ALA ILE ASP MET ALA
SEQRES 44 C 565 ASP GLU ASP TYR GLU PHE
MODRES 1RR8 PTR C 723 TYR O-PHOSPHOTYROSINE
HET PTR C 723 16
HET TTG A1991 32
HET TTC A 100 31
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM TTG 2-(1-DIMETHYLAMINOMETHYL-2-HYDROXY-8-HYDROXYMETHYL-9-
HETNAM 2 TTG OXO-9,11-DIHYDRO-INDOLIZINO[1,2-B]QUINOLIN-7-YL)-2-
HETNAM 3 TTG HYDROXY-BUTYRIC ACID
HETNAM TTC (S)-10-[(DIMETHYLAMINO)METHYL]-4-ETHYL-4,9-DIHYDROXY-
HETNAM 2 TTC 1H-PYRANO[3',4':6,7]INOLIZINO[1,2-B]-QUINOLINE-3,
HETNAM 3 TTC 14(4H,12H)-DIONE
HETSYN PTR PHOSPHONOTYROSINE
HETSYN TTG HYDROLYZED PRODUCT OF TOPOTECAN
HETSYN TTC TOPOTECAN, HYCAMTIN
FORMUL 3 PTR C9 H12 N O6 P
FORMUL 4 TTG C23 H25 N3 O6
FORMUL 4 TTC C23 H23 N3 O5
FORMUL 5 HOH *304(H2 O)
HELIX 1 1 SER C 250 LEU C 264 1 15
HELIX 2 2 HIS C 266 THR C 270 5 5
HELIX 3 3 LYS C 271 GLU C 285 1 15
HELIX 4 4 THR C 287 ASN C 292 1 6
HELIX 5 5 PHE C 302 LYS C 317 1 16
HELIX 6 6 SER C 320 TYR C 338 1 19
HELIX 7 7 MET C 378 ASP C 381 5 4
HELIX 8 8 SER C 433 LYS C 452 1 20
HELIX 9 9 CYS C 453 ASP C 464 1 12
HELIX 10 10 GLU C 469 LEU C 485 1 17
HELIX 11 11 ARG C 508 GLU C 510 5 3
HELIX 12 12 LYS C 532 SER C 534 5 3
HELIX 13 13 GLU C 544 GLU C 556 1 13
HELIX 14 14 ASN C 569 MET C 581 1 13
HELIX 15 15 LYS C 587 THR C 606 1 20
HELIX 16 16 ASN C 611 CYS C 630 1 20
HELIX 17 17 LEU C 716 PTR C 723 1 8
HELIX 18 18 ASP C 725 GLY C 737 1 13
HELIX 19 19 PRO C 739 ILE C 743 5 5
HELIX 20 20 ASN C 745 PHE C 752 1 8
HELIX 21 21 PHE C 752 MET C 758 1 7
SHEET 1 A 3 LEU C 220 GLU C 221 0
SHEET 2 A 3 PHE C 340 MET C 343 -1 O ILE C 342 N GLU C 221
SHEET 3 A 3 HIS C 346 ARG C 349 -1 O GLU C 348 N CYS C 341
SHEET 1 B 3 LYS C 245 VAL C 246 0
SHEET 2 B 3 TYR C 241 TYR C 242 -1 N TYR C 242 O LYS C 245
SHEET 3 B 3 CYS C 300 ASP C 301 -1 O ASP C 301 N TYR C 241
SHEET 1 C 2 GLY C 359 LEU C 360 0
SHEET 2 C 2 LEU C 373 LYS C 374 -1 O LYS C 374 N GLY C 359
SHEET 1 D 4 GLU C 403 ARG C 405 0
SHEET 2 D 4 ILE C 383 ASN C 385 1 N ILE C 384 O ARG C 405
SHEET 3 D 4 VAL C 414 THR C 417 -1 O SER C 415 N ILE C 383
SHEET 4 D 4 ILE C 424 ILE C 427 -1 O LYS C 425 N TRP C 416
SHEET 1 E 3 ILE C 512 LEU C 518 0
SHEET 2 E 3 GLN C 521 LEU C 530 -1 O VAL C 524 N HIS C 515
SHEET 3 E 3 ARG C 536 PRO C 542 -1 O TYR C 537 N PHE C 529
LINK C ASN C 722 N PTR C 723 1555 1555 1.33
LINK C PTR C 723 N LEU C 724 1555 1555 1.34
LINK C21 TTC A 100 C25 TTG A1991 1555 1555 1.86
LINK O26 TTC A 100 C2 TTG A1991 1555 1555 1.42
LINK C30 TTC A 100 N28 TTG A1991 1555 1555 1.61
LINK C29 TTC A 100 N28 TTG A1991 1555 1555 1.39
LINK C31 TTC A 100 C25 TTG A1991 1555 1555 1.49
LINK C25 TTC A 100 C31 TTG A1991 1555 1555 1.67
LINK O24 TTC A 100 C21 TTG A1991 1555 1555 1.65
LINK C16 TTC A 100 C21 TTG A1991 1555 1555 1.51
LINK C25 TTC A 100 C21 TTG A1991 1555 1555 1.32
LINK C20 TTC A 100 C21 TTG A1991 1555 1555 1.76
LINK C21 TTC A 100 O24 TTG A1991 1555 1555 1.26
LINK C21 TTC A 100 C16 TTG A1991 1555 1555 1.71
LINK C15 TTC A 100 C16 TTG A1991 1555 1555 1.24
LINK C17 TTC A 100 C16 TTG A1991 1555 1555 1.48
LINK C21 TTC A 100 C20 TTG A1991 1555 1555 1.47
LINK O23 TTC A 100 C20 TTG A1991 1555 1555 1.23
LINK O22 TTC A 100 C20 TTG A1991 1555 1555 1.53
LINK C16 TTC A 100 C15 TTG A1991 1555 1555 1.61
LINK C14 TTC A 100 C15 TTG A1991 1555 1555 1.41
LINK C19 TTC A 100 C15 TTG A1991 1555 1555 1.58
LINK C16 TTC A 100 C17 TTG A1991 1555 1555 1.43
LINK C13 TTC A 100 C17 TTG A1991 1555 1555 1.31
LINK O22 TTC A 100 O23 TTG A1991 1555 1555 1.84
LINK C20 TTC A 100 O22 TTG A1991 1555 1555 1.41
LINK O23 TTC A 100 O22 TTG A1991 1555 1555 1.63
LINK O22 TTC A 100 O22 TTG A1991 1555 1555 1.76
LINK C15 TTC A 100 C14 TTG A1991 1555 1555 1.80
LINK N12 TTC A 100 C14 TTG A1991 1555 1555 1.36
LINK O18 TTC A 100 C14 TTG A1991 1555 1555 1.16
LINK C15 TTC A 100 C19 TTG A1991 1555 1555 1.66
LINK C17 TTC A 100 C13 TTG A1991 1555 1555 1.55
LINK N12 TTC A 100 C13 TTG A1991 1555 1555 1.26
LINK C9 TTC A 100 C13 TTG A1991 1555 1555 1.40
LINK C14 TTC A 100 O18 TTG A1991 1555 1555 1.46
LINK C14 TTC A 100 N12 TTG A1991 1555 1555 1.47
LINK C13 TTC A 100 N12 TTG A1991 1555 1555 1.48
LINK C11 TTC A 100 N12 TTG A1991 1555 1555 1.37
LINK C13 TTC A 100 C9 TTG A1991 1555 1555 1.43
LINK C8 TTC A 100 C9 TTG A1991 1555 1555 1.41
LINK N10 TTC A 100 C9 TTG A1991 1555 1555 1.40
LINK N12 TTC A 100 C11 TTG A1991 1555 1555 1.69
LINK C8 TTC A 100 C11 TTG A1991 1555 1555 1.50
LINK C7 TTC A 100 C8 TTG A1991 1555 1555 1.31
LINK C9 TTC A 100 C8 TTG A1991 1555 1555 1.56
LINK C11 TTC A 100 C8 TTG A1991 1555 1555 1.56
LINK C5 TTC A 100 N10 TTG A1991 1555 1555 1.44
LINK C9 TTC A 100 N10 TTG A1991 1555 1555 1.30
LINK C6 TTC A 100 C7 TTG A1991 1555 1555 1.45
LINK C8 TTC A 100 C7 TTG A1991 1555 1555 1.43
LINK C6 TTC A 100 C5 TTG A1991 1555 1555 1.44
LINK C4 TTC A 100 C5 TTG A1991 1555 1555 1.42
LINK N10 TTC A 100 C5 TTG A1991 1555 1555 1.39
LINK C7 TTC A 100 C6 TTG A1991 1555 1555 1.47
LINK C5 TTC A 100 C6 TTG A1991 1555 1555 1.44
LINK C1 TTC A 100 C6 TTG A1991 1555 1555 1.45
LINK C5 TTC A 100 C4 TTG A1991 1555 1555 1.33
LINK C3 TTC A 100 C4 TTG A1991 1555 1555 1.48
LINK C6 TTC A 100 C1 TTG A1991 1555 1555 1.45
LINK C2 TTC A 100 C1 TTG A1991 1555 1555 1.41
LINK C27 TTC A 100 C1 TTG A1991 1555 1555 1.58
LINK C4 TTC A 100 C3 TTG A1991 1555 1555 1.35
LINK C2 TTC A 100 C3 TTG A1991 1555 1555 1.44
LINK C1 TTC A 100 C2 TTG A1991 1555 1555 1.44
LINK C3 TTC A 100 C2 TTG A1991 1555 1555 1.36
LINK C1 TTC A 100 C27 TTG A1991 1555 1555 1.52
LINK N28 TTC A 100 C27 TTG A1991 1555 1555 1.60
LINK C27 TTC A 100 N28 TTG A1991 1555 1555 1.36
LINK N28 TTC A 100 C29 TTG A1991 1555 1555 1.67
LINK N28 TTC A 100 C30 TTG A1991 1555 1555 1.47
LINK C2 TTC A 100 O26 TTG A1991 1555 1555 1.35
LINK C19 TTC A 100 O19 TTG A1991 1555 1555 1.47
LINK O PTR C 723 N LEU C 724 1555 1555 1.80
SITE 1 AC1 13 DT A 10 DG A 11 DG A 12 TTC A 100
SITE 2 AC1 13 HOH A 886 DC B 112 DA B 113 GLU C 356
SITE 3 AC1 13 ARG C 364 LYS C 532 ASP C 533 THR C 718
SITE 4 AC1 13 ASN C 722
SITE 1 AC2 14 DT A 10 DG A 11 DG A 12 HOH A 886
SITE 2 AC2 14 TTG A1991 DC B 112 DA B 113 HOH B 878
SITE 3 AC2 14 GLU C 356 ARG C 364 LYS C 532 ASP C 533
SITE 4 AC2 14 THR C 718 PTR C 723
CRYST1 57.590 115.585 75.010 90.00 96.29 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 0.017364 0.000000 0.001914 0.00000
SCALE2 0.000000 0.008652 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013412 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
