HEADER STRUCTURAL PROTEIN/DNA 15-FEB-13 4J8X
TITLE X-RAY STRUCTURE OF NCP145 WITH BOUND CHLORIDO(ETA-6-P-CYMENE)(N-
TITLE 2 FLUOROPHENYL-2-PYRIDINECARBOTHIOAMIDE)RUTHENIUM(II)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3.2;
COMPND 3 CHAIN: A, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HISTONE H4;
COMPND 7 CHAIN: B, F;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HISTONE H2A;
COMPND 11 CHAIN: C, G;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: HISTONE H2B 1.1;
COMPND 15 CHAIN: D, H;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 5;
COMPND 18 MOLECULE: DNA;
COMPND 19 CHAIN: I;
COMPND 20 ENGINEERED: YES;
COMPND 21 MOL_ID: 6;
COMPND 22 MOLECULE: DNA;
COMPND 23 CHAIN: J;
COMPND 24 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 9 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;
SOURCE 10 ORGANISM_TAXID: 8355;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 15 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;
SOURCE 16 ORGANISM_TAXID: 8355;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 MOL_ID: 4;
SOURCE 20 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 21 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;
SOURCE 22 ORGANISM_TAXID: 8355;
SOURCE 23 GENE: HIST1H2AJ, LOC494591;
SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 26 MOL_ID: 5;
SOURCE 27 SYNTHETIC: YES;
SOURCE 28 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 29 ORGANISM_TAXID: 32630;
SOURCE 30 MOL_ID: 6;
SOURCE 31 SYNTHETIC: YES;
SOURCE 32 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 33 ORGANISM_TAXID: 32630
KEYWDS NUCLEOSOME, HISTONE, STRUCTURAL PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.ADHIREKSAN,C.A.DAVEY
REVDAT 3 28-FEB-24 4J8X 1 REMARK SEQADV LINK
REVDAT 2 15-NOV-17 4J8X 1 REMARK
REVDAT 1 08-MAY-13 4J8X 0
JRNL AUTH S.M.MEIER,M.HANIF,Z.ADHIREKSAN,V.PICHLER,M.NOVAK,
JRNL AUTH 2 E.JIRKOVSKY,M.A.JAKUPEC,V.B.ARION,C.A.DAVEY,B.K.KEPPLER,
JRNL AUTH 3 C.G.HARTINGER
JRNL TITL NOVEL METAL(II) ARENE 2-PYRIDINECARBOTHIOAMIDES: A RATIONALE
JRNL TITL 2 TO ORALLY ACTIVE ORGANOMETALLIC ANTICANCER AGENTS
JRNL REF CHEM SCI V. 4 1837 2013
JRNL REFN ISSN 2041-6520
JRNL DOI 10.1039/C3SC22294B
REMARK 2
REMARK 2 RESOLUTION. 2.87 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 93.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 48147
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 + TEST SET) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.237
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1011
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.87
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3393
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.3940
REMARK 3 BIN FREE R VALUE SET COUNT : 74
REMARK 3 BIN FREE R VALUE : 0.4600
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6086
REMARK 3 NUCLEIC ACID ATOMS : 5939
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.02000
REMARK 3 B22 (A**2) : -3.53000
REMARK 3 B33 (A**2) : 0.51000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.406
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.338
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.483
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.918
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.870
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12873 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18668 ; 1.499 ; 2.546
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 757 ; 4.994 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 271 ;32.486 ;21.255
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1183 ;17.586 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 86 ;20.977 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2119 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7635 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3797 ; 0.672 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6110 ; 1.316 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9076 ; 1.447 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 12510 ; 2.456 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4J8X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1000077744.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.50
REMARK 200 MONOCHROMATOR : BARTELS MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49232
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.870
REMARK 200 RESOLUTION RANGE LOW (A) : 93.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 2.87
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.03
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NONE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40 MM MNCL2, 30 MM KCL, 20 MM K
REMARK 280 -CACODYLATE PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 53.24000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 90.69500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.91000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 90.69500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.24000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.91000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 50640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -133.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, I
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -155.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H, J
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 58520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 73450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -434.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
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 ALA A 1
REMARK 465 ARG A 2
REMARK 465 THR A 3
REMARK 465 LYS A 4
REMARK 465 GLN A 5
REMARK 465 THR A 6
REMARK 465 ALA A 7
REMARK 465 ARG A 8
REMARK 465 LYS A 9
REMARK 465 SER A 10
REMARK 465 THR A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 LYS A 14
REMARK 465 ALA A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 LYS A 18
REMARK 465 GLN A 19
REMARK 465 LEU A 20
REMARK 465 ALA A 21
REMARK 465 THR A 22
REMARK 465 LYS A 23
REMARK 465 ALA A 24
REMARK 465 ALA A 25
REMARK 465 ARG A 26
REMARK 465 LYS A 27
REMARK 465 SER A 28
REMARK 465 ALA A 29
REMARK 465 PRO A 30
REMARK 465 ALA A 31
REMARK 465 THR A 32
REMARK 465 GLY A 33
REMARK 465 GLY A 34
REMARK 465 VAL A 35
REMARK 465 LYS A 36
REMARK 465 LYS A 37
REMARK 465 ALA A 135
REMARK 465 SER B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLY B 4
REMARK 465 LYS B 5
REMARK 465 GLY B 6
REMARK 465 GLY B 7
REMARK 465 LYS B 8
REMARK 465 GLY B 9
REMARK 465 LEU B 10
REMARK 465 GLY B 11
REMARK 465 LYS B 12
REMARK 465 GLY B 13
REMARK 465 GLY B 14
REMARK 465 ALA B 15
REMARK 465 LYS B 16
REMARK 465 ARG B 17
REMARK 465 HIS B 18
REMARK 465 ARG B 19
REMARK 465 LYS B 20
REMARK 465 SER C 1
REMARK 465 GLY C 2
REMARK 465 ARG C 3
REMARK 465 GLY C 4
REMARK 465 LYS C 5
REMARK 465 GLN C 6
REMARK 465 GLY C 7
REMARK 465 GLY C 8
REMARK 465 LYS C 9
REMARK 465 THR C 10
REMARK 465 ARG C 11
REMARK 465 ALA C 12
REMARK 465 LYS C 13
REMARK 465 THR C 120
REMARK 465 GLU C 121
REMARK 465 SER C 122
REMARK 465 SER C 123
REMARK 465 LYS C 124
REMARK 465 SER C 125
REMARK 465 LYS C 126
REMARK 465 SER C 127
REMARK 465 LYS C 128
REMARK 465 PRO D -2
REMARK 465 GLU D -1
REMARK 465 PRO D 0
REMARK 465 ALA D 1
REMARK 465 LYS D 2
REMARK 465 SER D 3
REMARK 465 ALA D 4
REMARK 465 PRO D 5
REMARK 465 ALA D 6
REMARK 465 PRO D 7
REMARK 465 LYS D 8
REMARK 465 LYS D 9
REMARK 465 GLY D 10
REMARK 465 SER D 11
REMARK 465 LYS D 12
REMARK 465 LYS D 13
REMARK 465 ALA D 14
REMARK 465 VAL D 15
REMARK 465 THR D 16
REMARK 465 LYS D 17
REMARK 465 THR D 18
REMARK 465 GLN D 19
REMARK 465 LYS D 20
REMARK 465 LYS D 21
REMARK 465 ASP D 22
REMARK 465 GLY D 23
REMARK 465 LYS D 24
REMARK 465 LYS D 25
REMARK 465 ARG D 26
REMARK 465 ARG D 27
REMARK 465 ALA E 1
REMARK 465 ARG E 2
REMARK 465 THR E 3
REMARK 465 LYS E 4
REMARK 465 GLN E 5
REMARK 465 THR E 6
REMARK 465 ALA E 7
REMARK 465 ARG E 8
REMARK 465 LYS E 9
REMARK 465 SER E 10
REMARK 465 THR E 11
REMARK 465 GLY E 12
REMARK 465 GLY E 13
REMARK 465 LYS E 14
REMARK 465 ALA E 15
REMARK 465 PRO E 16
REMARK 465 ARG E 17
REMARK 465 LYS E 18
REMARK 465 GLN E 19
REMARK 465 LEU E 20
REMARK 465 ALA E 21
REMARK 465 THR E 22
REMARK 465 LYS E 23
REMARK 465 ALA E 24
REMARK 465 ALA E 25
REMARK 465 ARG E 26
REMARK 465 LYS E 27
REMARK 465 SER E 28
REMARK 465 ALA E 29
REMARK 465 PRO E 30
REMARK 465 ALA E 31
REMARK 465 THR E 32
REMARK 465 GLY E 33
REMARK 465 GLY E 34
REMARK 465 VAL E 35
REMARK 465 LYS E 36
REMARK 465 LYS E 37
REMARK 465 ALA E 135
REMARK 465 SER F 1
REMARK 465 GLY F 2
REMARK 465 ARG F 3
REMARK 465 GLY F 4
REMARK 465 LYS F 5
REMARK 465 GLY F 6
REMARK 465 GLY F 7
REMARK 465 LYS F 8
REMARK 465 GLY F 9
REMARK 465 LEU F 10
REMARK 465 GLY F 11
REMARK 465 LYS F 12
REMARK 465 GLY F 13
REMARK 465 GLY F 14
REMARK 465 ALA F 15
REMARK 465 SER G 1
REMARK 465 GLY G 2
REMARK 465 ARG G 3
REMARK 465 GLY G 4
REMARK 465 LYS G 5
REMARK 465 GLN G 6
REMARK 465 GLY G 7
REMARK 465 GLY G 8
REMARK 465 LYS G 9
REMARK 465 THR G 10
REMARK 465 ARG G 11
REMARK 465 ALA G 12
REMARK 465 LYS G 13
REMARK 465 THR G 120
REMARK 465 GLU G 121
REMARK 465 SER G 122
REMARK 465 SER G 123
REMARK 465 LYS G 124
REMARK 465 SER G 125
REMARK 465 LYS G 126
REMARK 465 SER G 127
REMARK 465 LYS G 128
REMARK 465 PRO H -2
REMARK 465 GLU H -1
REMARK 465 PRO H 0
REMARK 465 ALA H 1
REMARK 465 LYS H 2
REMARK 465 SER H 3
REMARK 465 ALA H 4
REMARK 465 PRO H 5
REMARK 465 ALA H 6
REMARK 465 PRO H 7
REMARK 465 LYS H 8
REMARK 465 LYS H 9
REMARK 465 GLY H 10
REMARK 465 SER H 11
REMARK 465 LYS H 12
REMARK 465 LYS H 13
REMARK 465 ALA H 14
REMARK 465 VAL H 15
REMARK 465 THR H 16
REMARK 465 LYS H 17
REMARK 465 THR H 18
REMARK 465 GLN H 19
REMARK 465 LYS H 20
REMARK 465 LYS H 21
REMARK 465 ASP H 22
REMARK 465 GLY H 23
REMARK 465 LYS H 24
REMARK 465 LYS H 25
REMARK 465 ARG H 26
REMARK 465 ARG H 27
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 DA J 28 O3' DA J 28 C3' -0.039
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 DA I -72 O4' - C1' - N9 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DT I -71 C3' - O3' - P ANGL. DEV. = 8.8 DEGREES
REMARK 500 DC I -70 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DT I -67 C3' - C2' - C1' ANGL. DEV. = -6.4 DEGREES
REMARK 500 DT I -67 O4' - C1' - N1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 DA I -62 O4' - C1' - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DC I -61 O4' - C1' - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DC I -61 C3' - O3' - P ANGL. DEV. = 8.1 DEGREES
REMARK 500 DT I -59 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 DG I -55 C1' - O4' - C4' ANGL. DEV. = -7.8 DEGREES
REMARK 500 DG I -55 O4' - C1' - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DA I -54 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT I -53 O4' - C1' - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 DC I -51 C3' - O3' - P ANGL. DEV. = 8.0 DEGREES
REMARK 500 DA I -49 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DC I -48 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 DA I -45 O4' - C1' - N9 ANGL. DEV. = 4.9 DEGREES
REMARK 500 DA I -44 O4' - C1' - N9 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DG I -40 O4' - C1' - N9 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DT I -39 O4' - C1' - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 DA I -38 O4' - C1' - N9 ANGL. DEV. = 5.0 DEGREES
REMARK 500 DT I -37 O4' - C1' - N1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 DG I -33 O4' - C1' - N9 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DC I -29 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DT I -28 C3' - C2' - C1' ANGL. DEV. = -5.3 DEGREES
REMARK 500 DT I -28 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DT I -25 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DT I -25 C4 - C5 - C7 ANGL. DEV. = 4.2 DEGREES
REMARK 500 DC I -24 C3' - C2' - C1' ANGL. DEV. = -5.5 DEGREES
REMARK 500 DC I -24 O4' - C1' - N1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 DC I -20 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DA I -17 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DA I -16 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DG I -14 O4' - C1' - N9 ANGL. DEV. = -5.4 DEGREES
REMARK 500 DG I -10 C3' - O3' - P ANGL. DEV. = 7.4 DEGREES
REMARK 500 DT I -9 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DC I -7 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG I -5 O4' - C1' - N9 ANGL. DEV. = 5.0 DEGREES
REMARK 500 DG I -2 O4' - C1' - N9 ANGL. DEV. = -4.4 DEGREES
REMARK 500 DT I 6 C3' - C2' - C1' ANGL. DEV. = -6.3 DEGREES
REMARK 500 DT I 6 C4 - C5 - C7 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DA I 8 O4' - C1' - C2' ANGL. DEV. = 3.1 DEGREES
REMARK 500 DA I 9 O4' - C1' - N9 ANGL. DEV. = -6.6 DEGREES
REMARK 500 DC I 10 C3' - C2' - C1' ANGL. DEV. = -5.3 DEGREES
REMARK 500 DA I 11 O4' - C1' - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DT I 12 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 DC I 15 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DG I 20 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DA I 21 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DT I 22 O4' - C1' - N1 ANGL. DEV. = 5.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 153 ANGLE DEVIATIONS.
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 ASN C 110 110.85 -160.38
REMARK 500 LYS C 118 -116.71 54.63
REMARK 500 ALA D 121 51.75 -119.75
REMARK 500 HIS F 18 142.46 72.77
REMARK 500 THR F 96 133.55 -36.51
REMARK 500 HIS H 46 86.17 -157.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 CHLORIDO(ETA-6-P-CYMENE)(N-FLUOROPHENYL-2-PYRIDINECARBOTHIOAMIDE)
REMARK 600 RUTHENIUM(II) WAS USED IN CRYSTALLIZATION. HOWEVER, UPON REACTING
REMARK 600 WITH PROTEIN (HIS 79 CHAINS H,D), THE CL DEPARTED AND THE
REMARK 600 CARBOTHIAMIDE GROUP WAS CLEAVED OFF. THE REMAINING LIGAND IS
REMARK 600 DESCRIBED BY CHEMICAL COMPONENT RU7
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 RU7 D1102 RU1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 79 NE2
REMARK 620 2 RU7 D1102 C4 82.9
REMARK 620 3 RU7 D1102 C5 97.1 37.8
REMARK 620 4 RU7 D1102 C6 131.1 67.9 37.3
REMARK 620 5 RU7 D1102 C3 100.0 36.4 66.6 79.4
REMARK 620 6 RU7 D1102 C2 135.9 67.5 79.4 67.1 38.1
REMARK 620 7 RU7 D1102 C1 163.9 81.2 68.3 38.0 68.5 37.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 RU7 H 203 RU1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 79 NE2
REMARK 620 2 RU7 H 203 C4 87.5
REMARK 620 3 RU7 H 203 C5 105.9 37.7
REMARK 620 4 RU7 H 203 C6 140.8 67.5 37.0
REMARK 620 5 RU7 H 203 C3 98.0 36.2 66.7 79.6
REMARK 620 6 RU7 H 203 C2 131.3 67.0 79.0 67.0 38.3
REMARK 620 7 RU7 H 203 C1 166.6 80.5 67.6 37.6 68.7 37.5
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RU7 D 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RU7 H 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4J8U RELATED DB: PDB
REMARK 900 RELATED ID: 4J8W RELATED DB: PDB
REMARK 900 RELATED ID: 4J8X RELATED DB: PDB
DBREF 4J8X A 1 135 UNP P84233 H32_XENLA 2 136
DBREF 4J8X B 1 102 UNP P62799 H4_XENLA 2 103
DBREF 4J8X C 1 128 UNP Q6AZJ8 Q6AZJ8_XENLA 2 130
DBREF 4J8X D -2 122 UNP P02281 H2B11_XENLA 2 126
DBREF 4J8X E 1 135 UNP P84233 H32_XENLA 2 136
DBREF 4J8X F 1 102 UNP P62799 H4_XENLA 2 103
DBREF 4J8X G 1 128 UNP Q6AZJ8 Q6AZJ8_XENLA 2 130
DBREF 4J8X H -2 122 UNP P02281 H2B11_XENLA 2 126
DBREF 4J8X I -72 72 PDB 4J8X 4J8X -72 72
DBREF 4J8X J -72 72 PDB 4J8X 4J8X -72 72
SEQADV 4J8X ALA A 102 UNP P84233 GLY 103 CONFLICT
SEQADV 4J8X C UNP Q6AZJ8 ALA 127 DELETION
SEQADV 4J8X THR D 29 UNP P02281 SER 33 CONFLICT
SEQADV 4J8X ALA E 102 UNP P84233 GLY 103 CONFLICT
SEQADV 4J8X G UNP Q6AZJ8 ALA 127 DELETION
SEQADV 4J8X THR H 29 UNP P02281 SER 33 CONFLICT
SEQRES 1 A 135 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 A 135 LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG
SEQRES 3 A 135 LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS
SEQRES 4 A 135 ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG
SEQRES 5 A 135 ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU
SEQRES 6 A 135 PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE
SEQRES 7 A 135 LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA
SEQRES 8 A 135 LEU GLN GLU ALA SER GLU ALA TYR LEU VAL ALA LEU PHE
SEQRES 9 A 135 GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL
SEQRES 10 A 135 THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE
SEQRES 11 A 135 ARG GLY GLU ARG ALA
SEQRES 1 B 102 SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY
SEQRES 2 B 102 GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE
SEQRES 3 B 102 GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG
SEQRES 4 B 102 ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU
SEQRES 5 B 102 GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL
SEQRES 6 B 102 ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG
SEQRES 7 B 102 LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS
SEQRES 8 B 102 ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 C 128 SER GLY ARG GLY LYS GLN GLY GLY LYS THR ARG ALA LYS
SEQRES 2 C 128 ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE PRO
SEQRES 3 C 128 VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN TYR
SEQRES 4 C 128 ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA
SEQRES 5 C 128 ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU LEU
SEQRES 6 C 128 ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE
SEQRES 7 C 128 ILE PRO ARG HIS LEU GLN LEU ALA VAL ARG ASN ASP GLU
SEQRES 8 C 128 GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA GLN
SEQRES 9 C 128 GLY GLY VAL LEU PRO ASN ILE GLN SER VAL LEU LEU PRO
SEQRES 10 C 128 LYS LYS THR GLU SER SER LYS SER LYS SER LYS
SEQRES 1 D 125 PRO GLU PRO ALA LYS SER ALA PRO ALA PRO LYS LYS GLY
SEQRES 2 D 125 SER LYS LYS ALA VAL THR LYS THR GLN LYS LYS ASP GLY
SEQRES 3 D 125 LYS LYS ARG ARG LYS THR ARG LYS GLU SER TYR ALA ILE
SEQRES 4 D 125 TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR
SEQRES 5 D 125 GLY ILE SER SER LYS ALA MET SER ILE MET ASN SER PHE
SEQRES 6 D 125 VAL ASN ASP VAL PHE GLU ARG ILE ALA GLY GLU ALA SER
SEQRES 7 D 125 ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR SER
SEQRES 8 D 125 ARG GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY
SEQRES 9 D 125 GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA
SEQRES 10 D 125 VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 E 135 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 E 135 LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG
SEQRES 3 E 135 LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS
SEQRES 4 E 135 ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG
SEQRES 5 E 135 ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU
SEQRES 6 E 135 PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE
SEQRES 7 E 135 LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA
SEQRES 8 E 135 LEU GLN GLU ALA SER GLU ALA TYR LEU VAL ALA LEU PHE
SEQRES 9 E 135 GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL
SEQRES 10 E 135 THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE
SEQRES 11 E 135 ARG GLY GLU ARG ALA
SEQRES 1 F 102 SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY
SEQRES 2 F 102 GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE
SEQRES 3 F 102 GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG
SEQRES 4 F 102 ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU
SEQRES 5 F 102 GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL
SEQRES 6 F 102 ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG
SEQRES 7 F 102 LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS
SEQRES 8 F 102 ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 G 128 SER GLY ARG GLY LYS GLN GLY GLY LYS THR ARG ALA LYS
SEQRES 2 G 128 ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE PRO
SEQRES 3 G 128 VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN TYR
SEQRES 4 G 128 ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA
SEQRES 5 G 128 ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU LEU
SEQRES 6 G 128 ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE
SEQRES 7 G 128 ILE PRO ARG HIS LEU GLN LEU ALA VAL ARG ASN ASP GLU
SEQRES 8 G 128 GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA GLN
SEQRES 9 G 128 GLY GLY VAL LEU PRO ASN ILE GLN SER VAL LEU LEU PRO
SEQRES 10 G 128 LYS LYS THR GLU SER SER LYS SER LYS SER LYS
SEQRES 1 H 125 PRO GLU PRO ALA LYS SER ALA PRO ALA PRO LYS LYS GLY
SEQRES 2 H 125 SER LYS LYS ALA VAL THR LYS THR GLN LYS LYS ASP GLY
SEQRES 3 H 125 LYS LYS ARG ARG LYS THR ARG LYS GLU SER TYR ALA ILE
SEQRES 4 H 125 TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR
SEQRES 5 H 125 GLY ILE SER SER LYS ALA MET SER ILE MET ASN SER PHE
SEQRES 6 H 125 VAL ASN ASP VAL PHE GLU ARG ILE ALA GLY GLU ALA SER
SEQRES 7 H 125 ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR SER
SEQRES 8 H 125 ARG GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY
SEQRES 9 H 125 GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA
SEQRES 10 H 125 VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 I 145 DA DT DC DA DA DT DA DT DC DC DA DC DC
SEQRES 2 I 145 DT DG DC DA DG DA DT DA DC DT DA DC DC
SEQRES 3 I 145 DA DA DA DA DG DT DG DT DA DT DT DT DG
SEQRES 4 I 145 DG DA DA DA DC DT DG DC DT DC DC DA DT
SEQRES 5 I 145 DC DA DA DA DA DG DG DC DA DT DG DT DT
SEQRES 6 I 145 DC DA DG DC DT DG DA DA DT DC DA DG DC
SEQRES 7 I 145 DT DG DA DA DC DA DT DG DC DC DT DT DT
SEQRES 8 I 145 DT DG DA DT DG DG DA DG DC DA DG DT DT
SEQRES 9 I 145 DT DC DC DA DA DA DT DA DC DA DC DT DT
SEQRES 10 I 145 DT DT DG DG DT DA DG DT DA DT DC DT DG
SEQRES 11 I 145 DC DA DG DG DT DG DG DA DT DA DT DT DG
SEQRES 12 I 145 DA DT
SEQRES 1 J 145 DA DT DC DA DA DT DA DT DC DC DA DC DC
SEQRES 2 J 145 DT DG DC DA DG DA DT DA DC DT DA DC DC
SEQRES 3 J 145 DA DA DA DA DG DT DG DT DA DT DT DT DG
SEQRES 4 J 145 DG DA DA DA DC DT DG DC DT DC DC DA DT
SEQRES 5 J 145 DC DA DA DA DA DG DG DC DA DT DG DT DT
SEQRES 6 J 145 DC DA DG DC DT DG DA DT DT DC DA DG DC
SEQRES 7 J 145 DT DG DA DA DC DA DT DG DC DC DT DT DT
SEQRES 8 J 145 DT DG DA DT DG DG DA DG DC DA DG DT DT
SEQRES 9 J 145 DT DC DC DA DA DA DT DA DC DA DC DT DT
SEQRES 10 J 145 DT DT DG DG DT DA DG DT DA DT DC DT DG
SEQRES 11 J 145 DC DA DG DG DT DG DG DA DT DA DT DT DG
SEQRES 12 J 145 DA DT
HET SO4 D1101 5
HET RU7 D1102 11
HET MG E1001 1
HET SO4 H 201 5
HET SO4 H 202 5
HET RU7 H 203 11
HETNAM SO4 SULFATE ION
HETNAM RU7 PARA-CYMENE RUTHENIUM CHLORIDE
HETNAM MG MAGNESIUM ION
FORMUL 11 SO4 3(O4 S 2-)
FORMUL 12 RU7 2(C10 H14 CL2 RU)
FORMUL 13 MG MG 2+
HELIX 1 1 GLY A 44 SER A 57 1 14
HELIX 2 2 ARG A 63 ASP A 77 1 15
HELIX 3 3 GLN A 85 ALA A 114 1 30
HELIX 4 4 MET A 120 ARG A 131 1 12
HELIX 5 5 ASP B 24 ILE B 29 5 6
HELIX 6 6 THR B 30 GLY B 41 1 12
HELIX 7 7 LEU B 49 ALA B 76 1 28
HELIX 8 8 THR B 82 GLN B 93 1 12
HELIX 9 9 THR C 16 ALA C 21 1 6
HELIX 10 10 PRO C 26 GLY C 37 1 12
HELIX 11 11 ALA C 45 ASN C 73 1 29
HELIX 12 12 ILE C 79 ASP C 90 1 12
HELIX 13 13 ASP C 90 LEU C 97 1 8
HELIX 14 14 GLN C 112 LEU C 116 5 5
HELIX 15 15 TYR D 34 HIS D 46 1 13
HELIX 16 16 SER D 52 ASN D 81 1 30
HELIX 17 17 THR D 87 LEU D 99 1 13
HELIX 18 18 PRO D 100 SER D 120 1 21
HELIX 19 19 GLY E 44 SER E 57 1 14
HELIX 20 20 ARG E 63 LYS E 79 1 17
HELIX 21 21 GLN E 85 ALA E 114 1 30
HELIX 22 22 MET E 120 ARG E 131 1 12
HELIX 23 23 ASP F 24 ILE F 29 5 6
HELIX 24 24 THR F 30 GLY F 41 1 12
HELIX 25 25 LEU F 49 LYS F 77 1 29
HELIX 26 26 THR F 82 GLN F 93 1 12
HELIX 27 27 THR G 16 ALA G 21 1 6
HELIX 28 28 PRO G 26 LYS G 36 1 11
HELIX 29 29 GLY G 46 ASN G 73 1 28
HELIX 30 30 ILE G 79 ASN G 89 1 11
HELIX 31 31 ASP G 90 LEU G 97 1 8
HELIX 32 32 GLN G 112 LEU G 116 5 5
HELIX 33 33 TYR H 34 HIS H 46 1 13
HELIX 34 34 SER H 52 ASN H 81 1 30
HELIX 35 35 THR H 87 LEU H 99 1 13
HELIX 36 36 PRO H 100 SER H 120 1 21
SHEET 1 A 2 ARG A 83 PHE A 84 0
SHEET 2 A 2 THR B 80 VAL B 81 1 O VAL B 81 N ARG A 83
SHEET 1 B 2 THR A 118 ILE A 119 0
SHEET 2 B 2 ARG B 45 ILE B 46 1 O ARG B 45 N ILE A 119
SHEET 1 C 2 THR B 96 TYR B 98 0
SHEET 2 C 2 VAL G 100 ILE G 102 1 O THR G 101 N THR B 96
SHEET 1 D 2 ARG C 42 VAL C 43 0
SHEET 2 D 2 THR D 85 ILE D 86 1 O ILE D 86 N ARG C 42
SHEET 1 E 2 ARG C 77 ILE C 78 0
SHEET 2 E 2 GLY D 50 ILE D 51 1 O GLY D 50 N ILE C 78
SHEET 1 F 2 VAL C 100 ILE C 102 0
SHEET 2 F 2 THR F 96 TYR F 98 1 O TYR F 98 N THR C 101
SHEET 1 G 2 ARG E 83 PHE E 84 0
SHEET 2 G 2 THR F 80 VAL F 81 1 O VAL F 81 N ARG E 83
SHEET 1 H 2 THR E 118 ILE E 119 0
SHEET 2 H 2 ARG F 45 ILE F 46 1 O ARG F 45 N ILE E 119
SHEET 1 I 2 ARG G 42 VAL G 43 0
SHEET 2 I 2 THR H 85 ILE H 86 1 O ILE H 86 N ARG G 42
SHEET 1 J 2 ARG G 77 ILE G 78 0
SHEET 2 J 2 GLY H 50 ILE H 51 1 O GLY H 50 N ILE G 78
LINK NE2 HIS D 79 RU1 RU7 D1102 1555 1555 2.48
LINK OD1 ASP E 77 MG MG E1001 1555 1555 2.12
LINK NE2 HIS H 79 RU1 RU7 H 203 1555 1555 2.18
SITE 1 AC1 7 GLY C 44 ALA C 45 GLY C 46 ALA C 47
SITE 2 AC1 7 THR D 87 SER D 88 ARG D 89
SITE 1 AC2 4 HIS D 79 TYR G 39 PHE H 67 GLU H 68
SITE 1 AC3 2 VAL D 45 ASP E 77
SITE 1 AC4 6 GLY G 44 ALA G 45 GLY G 46 ALA G 47
SITE 2 AC4 6 THR H 87 SER H 88
SITE 1 AC5 4 HIS H 46 PRO H 47 ASP H 48 THR H 49
SITE 1 AC6 4 LYS C 36 TYR C 39 GLU D 68 HIS H 79
CRYST1 106.480 109.820 181.390 90.00 90.00 90.00 P 21 21 21 8
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 0.009391 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009106 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005513 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
