HEADER ISOMERASE/DNA 29-JAN-98 1A36
TITLE TOPOISOMERASE I/DNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-
COMPND 3 D(*AP*AP*AP*AP*AP*GP*AP*CP*TP*TP*AP*GP*AP*AP*AP*AP*A
COMPND 4 P*TP*TP*TP*TP*T)- 3');
COMPND 5 CHAIN: B;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-
COMPND 9 D(*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*TP*AP*AP*GP*TP*C
COMPND 10 P*TP*TP*TP*TP*T)- 3');
COMPND 11 CHAIN: C;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: TOPOISOMERASE I;
COMPND 15 CHAIN: A;
COMPND 16 FRAGMENT: CORE DOMAIN AND C-TERMINAL DOMAIN;
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 CELLULAR_LOCATION: NUCLEUS;
SOURCE 10 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 11 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS
KEYWDS COMPLEX (ISOMERASE/DNA), DNA, TOPOISOMERASE I
EXPDTA X-RAY DIFFRACTION
AUTHOR L.STEWART,M.R.REDINBO,X.QIU,J.J.CHAMPOUX,W.G.J.HOL
REVDAT 2 24-FEB-09 1A36 1 VERSN
REVDAT 1 12-AUG-98 1A36 0
JRNL AUTH L.STEWART,M.R.REDINBO,X.QIU,W.G.HOL,J.J.CHAMPOUX
JRNL TITL A MODEL FOR THE MECHANISM OF HUMAN TOPOISOMERASE I.
JRNL REF SCIENCE V. 279 1534 1998
JRNL REFN ISSN 0036-8075
JRNL PMID 9488652
JRNL DOI 10.1126/SCIENCE.279.5356.1534
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 21217
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) : 0.224
REMARK 3 FREE R VALUE : 0.312
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1445
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 : 25
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.84
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 710
REMARK 3 BIN R VALUE (WORKING SET) : 0.3220
REMARK 3 BIN FREE R VALUE : 0.4450
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 41
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 : 4332
REMARK 3 NUCLEIC ACID ATOMS : 896
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 57
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.84000
REMARK 3 B22 (A**2) : 1.35400
REMARK 3 B33 (A**2) : 6.48600
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.05000
REMARK 3 B23 (A**2) : 0.00000
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) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.58
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.51
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM_NDBX.DNA
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOP_NDBX.DNA
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A36 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAY-95
REMARK 200 TEMPERATURE (KELVIN) : 100.00
REMARK 200 PH : 7.70
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL1-5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : UNKNOWN
REMARK 200 OPTICS : UNKNOWN
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21217
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
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) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.30500
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: RIGID BODY REFINEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: RECONSTITUTED HUMAN TOPOISOMERASE I COVALENT
REMARK 200 COMPLEX WITH 22 BASE PAIR DUPLEX DNA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.70
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 59.20000
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: B, C, 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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 NOTE THAT RESIDUES 174 - 214 AND 634 - 640 OF CHAIN A ARE
REMARK 400 DISORDERED AND ARE NOT PRESENT IN THE MODEL. 1-22 OF
REMARK 400 CHAIN C COMPRISE THE SCISSILE STRAND OF THE DNA, 101-122 OF
REMARK 400 CHAIN D THE INTACT DNA STRAND.
REMARK 400
REMARK 400 TER
REMARK 400 PHE 765 A IS THE C-TERMINAL RESIDUE OF THE 70 KDA FRAGMENT
REMARK 400 OF HUMAN TOPO I.
REMARK 400 THY 22 C IS THE 3' TERMINAL NUCLEOTIDE ON THE SCISSILE
REMARK 400 STRAND OF THE DNA DUPLEX.
REMARK 400 THY 122 D IS THE 3' TERMINAL NUCLEOTIDE ON THE INTACT
REMARK 400 STRAND OF THE DNA DUPLEX.
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 LYS A 175
REMARK 465 PRO A 176
REMARK 465 LYS A 177
REMARK 465 ASN A 178
REMARK 465 LYS A 179
REMARK 465 ASP A 180
REMARK 465 LYS A 181
REMARK 465 ASP A 182
REMARK 465 LYS A 183
REMARK 465 LYS A 184
REMARK 465 VAL A 185
REMARK 465 PRO A 186
REMARK 465 GLU A 187
REMARK 465 PRO A 188
REMARK 465 ASP A 189
REMARK 465 ASN A 190
REMARK 465 LYS A 191
REMARK 465 LYS A 192
REMARK 465 LYS A 193
REMARK 465 LYS A 194
REMARK 465 PRO A 195
REMARK 465 LYS A 196
REMARK 465 LYS A 197
REMARK 465 GLU A 198
REMARK 465 GLU A 199
REMARK 465 GLU A 200
REMARK 465 GLN A 201
REMARK 465 LYS A 202
REMARK 465 TRP A 203
REMARK 465 LYS A 204
REMARK 465 TRP A 205
REMARK 465 TRP A 206
REMARK 465 GLU A 207
REMARK 465 GLU A 208
REMARK 465 GLU A 209
REMARK 465 ARG A 210
REMARK 465 TYR A 211
REMARK 465 PRO A 212
REMARK 465 GLU A 213
REMARK 465 GLY A 214
REMARK 465 ARG 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 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 LYS A 248 CG CD CE NZ
REMARK 470 LYS A 276 CG CD CE NZ
REMARK 470 GLU A 289 CG CD OE1 OE2
REMARK 470 GLU A 314 CG CD OE1 OE2
REMARK 470 ARG A 316 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 GLN A 318 CG CD OE1 NE2
REMARK 470 MET A 319 CG SD CE
REMARK 470 LYS A 321 CG CD CE NZ
REMARK 470 GLU A 322 CG CD OE1 OE2
REMARK 470 GLU A 323 CG CD OE1 OE2
REMARK 470 LYS A 326 CG CD CE NZ
REMARK 470 GLU A 332 CG CD OE1 OE2
REMARK 470 LYS A 333 CG CD CE NZ
REMARK 470 ARG A 462 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 463 CG CD OE1 OE2
REMARK 470 LYS A 466 CG CD CE NZ
REMARK 470 LYS A 468 CG CD CE NZ
REMARK 470 LYS A 471 CG CD CE NZ
REMARK 470 LYS A 484 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 GLN A 633 CG CD OE1 NE2
REMARK 470 GLU A 641 CG CD OE1 OE2
REMARK 470 LYS A 642 CG CD CE NZ
REMARK 470 SER A 643 OG
REMARK 470 MET A 644 CG SD CE
REMARK 470 MET A 645 CG SD CE
REMARK 470 ASN A 646 CG OD1 ND2
REMARK 470 ASP A 660 CG OD1 OD2
REMARK 470 VAL A 674 CG1 CG2
REMARK 470 ARG A 693 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 696 CG CD OE1 OE2
REMARK 470 LYS A 712 CG CD CE NZ
REMARK 470 LYS A 735 CG CD CE NZ
REMARK 470 GLU A 741 CG CD OE1 OE2
REMARK 470 LYS A 742 CG CD CE NZ
REMARK 470 ASP A 760 CG OD1 OD2
REMARK 470 ASP A 762 CG OD1 OD2
REMARK 470 GLU A 764 CG CD OE1 OE2
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 103 C3' - C2' - C1' ANGL. DEV. = -5.8 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 ASP A 265 31.23 -90.93
REMARK 500 GLU A 272 -71.97 -62.50
REMARK 500 ILE A 293 -61.55 -95.36
REMARK 500 MET A 319 157.73 -45.10
REMARK 500 ASP A 344 -127.85 55.54
REMARK 500 ALA A 351 -72.84 -77.19
REMARK 500 GLU A 403 141.44 -179.92
REMARK 500 ASN A 459 1.43 -68.10
REMARK 500 ASP A 519 38.19 39.27
REMARK 500 PHE A 565 69.56 -108.02
REMARK 500 CYS A 630 0.75 -68.85
REMARK 500 LYS A 642 32.64 -74.63
REMARK 500 LEU A 647 -74.26 -56.20
REMARK 500 ASP A 677 -97.43 -47.90
REMARK 500 ALA A 678 -50.80 -175.74
REMARK 500 GLU A 696 -74.77 -56.37
REMARK 500 ASP A 707 -71.01 -69.36
REMARK 500 ASN A 711 45.69 -106.33
REMARK 500 ASP A 762 31.85 -94.91
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 DT C 108 0.08 SIDE_CHAIN
REMARK 500 DG C 115 0.07 SIDE_CHAIN
REMARK 500 DT C 121 0.08 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 A1025 DISTANCE = 7.26 ANGSTROMS
DBREF 1A36 A 175 765 UNP P11387 TOP1_HUMAN 174 765
DBREF 1A36 B 1 22 PDB 1A36 1A36 1 22
DBREF 1A36 C 101 122 PDB 1A36 1A36 101 122
SEQADV 1A36 PHE A 723 UNP P11387 TYR 723 ENGINEERED
SEQRES 1 B 22 DA DA DA DA DA DG DA DC DT DT DA DG DA
SEQRES 2 B 22 DA DA DA DA DT DT DT DT DT
SEQRES 1 C 22 DA DA DA DA DA DT DT DT DT DT DC DT DA
SEQRES 2 C 22 DA DG DT DC DT DT DT DT DT
SEQRES 1 A 591 LYS PRO LYS ASN LYS ASP LYS ASP LYS LYS VAL PRO GLU
SEQRES 2 A 591 PRO ASP ASN LYS LYS LYS LYS PRO LYS LYS GLU GLU GLU
SEQRES 3 A 591 GLN LYS TRP LYS TRP TRP GLU GLU GLU ARG TYR PRO GLU
SEQRES 4 A 591 GLY ILE LYS TRP LYS PHE LEU GLU HIS LYS GLY PRO VAL
SEQRES 5 A 591 PHE ALA PRO PRO TYR GLU PRO LEU PRO GLU ASN VAL LYS
SEQRES 6 A 591 PHE TYR TYR ASP GLY LYS VAL MET LYS LEU SER PRO LYS
SEQRES 7 A 591 ALA GLU GLU VAL ALA THR PHE PHE ALA LYS MET LEU ASP
SEQRES 8 A 591 HIS GLU TYR THR THR LYS GLU ILE PHE ARG LYS ASN PHE
SEQRES 9 A 591 PHE LYS ASP TRP ARG LYS GLU MET THR ASN GLU GLU LYS
SEQRES 10 A 591 ASN ILE ILE THR ASN LEU SER LYS CYS ASP PHE THR GLN
SEQRES 11 A 591 MET SER GLN TYR PHE LYS ALA GLN THR GLU ALA ARG LYS
SEQRES 12 A 591 GLN MET SER LYS GLU GLU LYS LEU LYS ILE LYS GLU GLU
SEQRES 13 A 591 ASN GLU LYS LEU LEU LYS GLU TYR GLY PHE CYS ILE MET
SEQRES 14 A 591 ASP ASN HIS LYS GLU ARG ILE ALA ASN PHE LYS ILE GLU
SEQRES 15 A 591 PRO PRO GLY LEU PHE ARG GLY ARG GLY ASN HIS PRO LYS
SEQRES 16 A 591 MET GLY MET LEU LYS ARG ARG ILE MET PRO GLU ASP ILE
SEQRES 17 A 591 ILE ILE ASN CYS SER LYS ASP ALA LYS VAL PRO SER PRO
SEQRES 18 A 591 PRO PRO GLY HIS LYS TRP LYS GLU VAL ARG HIS ASP ASN
SEQRES 19 A 591 LYS VAL THR TRP LEU VAL SER TRP THR GLU ASN ILE GLN
SEQRES 20 A 591 GLY SER ILE LYS TYR ILE MET LEU ASN PRO SER SER ARG
SEQRES 21 A 591 ILE LYS GLY GLU LYS ASP TRP GLN LYS TYR GLU THR ALA
SEQRES 22 A 591 ARG ARG LEU LYS LYS CYS VAL ASP LYS ILE ARG ASN GLN
SEQRES 23 A 591 TYR ARG GLU ASP TRP LYS SER LYS GLU MET LYS VAL ARG
SEQRES 24 A 591 GLN ARG ALA VAL ALA LEU TYR PHE ILE ASP LYS LEU ALA
SEQRES 25 A 591 LEU ARG ALA GLY ASN GLU LYS GLU GLU GLY GLU THR ALA
SEQRES 26 A 591 ASP THR VAL GLY CYS CYS SER LEU ARG VAL GLU HIS ILE
SEQRES 27 A 591 ASN LEU HIS PRO GLU LEU ASP GLY GLN GLU TYR VAL VAL
SEQRES 28 A 591 GLU PHE ASP PHE LEU GLY LYS ASP SER ILE ARG TYR TYR
SEQRES 29 A 591 ASN LYS VAL PRO VAL GLU LYS ARG VAL PHE LYS ASN LEU
SEQRES 30 A 591 GLN LEU PHE MET GLU ASN LYS GLN PRO GLU ASP ASP LEU
SEQRES 31 A 591 PHE ASP ARG LEU ASN THR GLY ILE LEU ASN LYS HIS LEU
SEQRES 32 A 591 GLN ASP LEU MET GLU GLY LEU THR ALA LYS VAL PHE ARG
SEQRES 33 A 591 THR TYR ASN ALA SER ILE THR LEU GLN GLN GLN LEU LYS
SEQRES 34 A 591 GLU LEU THR ALA PRO ASP GLU ASN ILE PRO ALA LYS ILE
SEQRES 35 A 591 LEU SER TYR ASN ARG ALA ASN ARG ALA VAL ALA ILE LEU
SEQRES 36 A 591 CYS ASN HIS GLN ARG ALA PRO PRO LYS THR PHE GLU LYS
SEQRES 37 A 591 SER MET MET ASN LEU GLN THR LYS ILE ASP ALA LYS LYS
SEQRES 38 A 591 GLU GLN LEU ALA ASP ALA ARG ARG ASP LEU LYS SER ALA
SEQRES 39 A 591 LYS ALA ASP ALA LYS VAL MET LYS ASP ALA LYS THR LYS
SEQRES 40 A 591 LYS VAL VAL GLU SER LYS LYS LYS ALA VAL GLN ARG LEU
SEQRES 41 A 591 GLU GLU GLN LEU MET LYS LEU GLU VAL GLN ALA THR ASP
SEQRES 42 A 591 ARG GLU GLU ASN LYS GLN ILE ALA LEU GLY THR SER LYS
SEQRES 43 A 591 LEU ASN PHE LEU ASP PRO ARG ILE THR VAL ALA TRP CYS
SEQRES 44 A 591 LYS LYS TRP GLY VAL PRO ILE GLU LYS ILE TYR ASN LYS
SEQRES 45 A 591 THR GLN ARG GLU LYS PHE ALA TRP ALA ILE ASP MET ALA
SEQRES 46 A 591 ASP GLU ASP TYR GLU PHE
FORMUL 4 HOH *57(H2 O)
HELIX 1 1 PRO A 251 MET A 263 1 13
HELIX 2 2 GLU A 267 THR A 270 5 4
HELIX 3 3 GLU A 272 GLU A 285 1 14
HELIX 4 4 ASN A 288 ILE A 293 1 6
HELIX 5 5 THR A 303 GLN A 318 1 16
HELIX 6 6 LYS A 321 TYR A 338 1 18
HELIX 7 7 PRO A 379 ASP A 381 5 3
HELIX 8 8 ARG A 434 ASP A 464 1 31
HELIX 9 9 VAL A 472 LYS A 484 1 13
HELIX 10 10 CYS A 504 SER A 506 5 3
HELIX 11 11 VAL A 509 HIS A 511 5 3
HELIX 12 12 LYS A 532 SER A 534 5 3
HELIX 13 13 LYS A 545 MET A 555 1 11
HELIX 14 14 THR A 570 LEU A 580 1 11
HELIX 15 15 ALA A 586 LEU A 605 1 20
HELIX 16 16 ILE A 612 LEU A 629 1 18
HELIX 17 17 SER A 643 VAL A 674 1 32
HELIX 18 18 LYS A 679 GLU A 710 1 32
HELIX 19 19 SER A 719 ASN A 722 1 4
HELIX 20 20 PRO A 726 TRP A 736 5 11
HELIX 21 21 ILE A 740 LYS A 742 5 3
HELIX 22 22 LYS A 746 LYS A 751 1 6
HELIX 23 23 ALA A 753 ASP A 757 1 5
SHEET 1 A 2 PHE A 240 TYR A 242 0
SHEET 2 A 2 LYS A 245 MET A 247 -1 N MET A 247 O PHE A 240
SHEET 1 B 2 PHE A 340 MET A 343 0
SHEET 2 B 2 HIS A 346 ARG A 349 -1 N GLU A 348 O CYS A 341
SHEET 1 C 2 ILE A 383 ASN A 385 0
SHEET 2 C 2 GLU A 403 ARG A 405 1 N GLU A 403 O ILE A 384
SHEET 1 D 2 VAL A 414 THR A 417 0
SHEET 2 D 2 ILE A 424 ILE A 427 -1 N ILE A 427 O VAL A 414
SHEET 1 E 3 ILE A 512 HIS A 515 0
SHEET 2 E 3 VAL A 524 LEU A 530 -1 N GLU A 526 O ASN A 513
SHEET 3 E 3 ARG A 536 PRO A 542 -1 N VAL A 541 O VAL A 525
CRYST1 56.500 118.400 71.500 90.00 101.20 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 0.017699 0.000000 0.003505 0.00000
SCALE2 0.000000 0.008446 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014258 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
