HEADER DNA BINDING PROTEIN/DNA 06-MAY-16 5JRG
TITLE CRYSTAL STRUCTURE OF THE NUCLEOSOME CONTAINING THE DNA WITH
TITLE 2 TETRAHYDROFURAN (THF)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3.1;
COMPND 3 CHAIN: A, E;
COMPND 4 SYNONYM: HISTONE H3/A,HISTONE H3/B,HISTONE H3/C,HISTONE H3/D,HISTONE
COMPND 5 H3/F,HISTONE H3/H,HISTONE H3/I,HISTONE H3/J,HISTONE H3/K,HISTONE
COMPND 6 H3/L;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HISTONE H4;
COMPND 10 CHAIN: B, F;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: HISTONE H2A TYPE 1-B/E;
COMPND 14 CHAIN: C, G;
COMPND 15 SYNONYM: HISTONE H2A.2,HISTONE H2A/A,HISTONE H2A/M;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: HISTONE H2B TYPE 1-J;
COMPND 19 CHAIN: D, H;
COMPND 20 SYNONYM: HISTONE H2B.1,HISTONE H2B.R,H2B/R;
COMPND 21 ENGINEERED: YES;
COMPND 22 MOL_ID: 5;
COMPND 23 MOLECULE: DNA (145-MER);
COMPND 24 CHAIN: I;
COMPND 25 ENGINEERED: YES;
COMPND 26 MOL_ID: 6;
COMPND 27 MOLECULE: DNA (145-MER);
COMPND 28 CHAIN: J;
COMPND 29 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HIST1H3A, H3FA, HIST1H3B, H3FL, HIST1H3C, H3FC, HIST1H3D,
SOURCE 6 H3FB, HIST1H3E, H3FD, HIST1H3F, H3FI, HIST1H3G, H3FH, HIST1H3H,
SOURCE 7 H3FK, HIST1H3I, H3FF, HIST1H3J, H3FJ;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 GENE: HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G,
SOURCE 18 H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C,
SOURCE 19 H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E,
SOURCE 20 H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N,
SOURCE 21 H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 24 EXPRESSION_SYSTEM_STRAIN: JM109(DE3);
SOURCE 25 MOL_ID: 3;
SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 27 ORGANISM_COMMON: HUMAN;
SOURCE 28 ORGANISM_TAXID: 9606;
SOURCE 29 GENE: HIST1H2AB, H2AFM, HIST1H2AE, H2AFA;
SOURCE 30 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 31 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 32 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 33 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 34 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 35 MOL_ID: 4;
SOURCE 36 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 37 ORGANISM_COMMON: HUMAN;
SOURCE 38 ORGANISM_TAXID: 9606;
SOURCE 39 GENE: HIST1H2BJ, H2BFR;
SOURCE 40 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 41 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 42 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 43 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 44 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 45 MOL_ID: 5;
SOURCE 46 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 47 ORGANISM_TAXID: 9606;
SOURCE 48 EXPRESSION_SYSTEM: ESCHERICHIA COLI DH5ALPHA;
SOURCE 49 EXPRESSION_SYSTEM_TAXID: 668369;
SOURCE 50 EXPRESSION_SYSTEM_STRAIN: DH5A;
SOURCE 51 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 52 EXPRESSION_SYSTEM_PLASMID: PGEM-T EASY;
SOURCE 53 MOL_ID: 6;
SOURCE 54 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 55 ORGANISM_TAXID: 9606;
SOURCE 56 EXPRESSION_SYSTEM: ESCHERICHIA COLI DH5ALPHA;
SOURCE 57 EXPRESSION_SYSTEM_TAXID: 668369;
SOURCE 58 EXPRESSION_SYSTEM_STRAIN: DH5A;
SOURCE 59 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 60 EXPRESSION_SYSTEM_PLASMID: PGEM-T EASY
KEYWDS HISTONE FOLD, DNA BINDING, NUCLEUS, CHROMATIN FORMATION, NUCLEOSOME,
KEYWDS 2 AP-SITE, DNA BINDING PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.OSAKABE,Y.ARIMURA,N.HORIKOSHI,H.KURUMIZAKA
REVDAT 3 08-NOV-23 5JRG 1 LINK
REVDAT 2 04-OCT-17 5JRG 1 REMARK
REVDAT 1 08-MAR-17 5JRG 0
JRNL AUTH A.OSAKABE,Y.ARIMURA,S.MATSUMOTO,N.HORIKOSHI,K.SUGASAWA,
JRNL AUTH 2 H.KURUMIZAKA
JRNL TITL POLYMORPHISM OF APYRIMIDINIC DNA STRUCTURES IN THE
JRNL TITL 2 NUCLEOSOME
JRNL REF SCI REP V. 7 41783 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28139742
JRNL DOI 10.1038/SREP41783
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.15
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.440
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 64243
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 3290
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.1555 - 7.1029 1.00 2837 168 0.1516 0.1951
REMARK 3 2 7.1029 - 5.6404 1.00 2727 153 0.1875 0.2186
REMARK 3 3 5.6404 - 4.9281 1.00 2700 139 0.1727 0.1956
REMARK 3 4 4.9281 - 4.4779 1.00 2699 135 0.1663 0.2177
REMARK 3 5 4.4779 - 4.1571 1.00 2689 127 0.1657 0.2181
REMARK 3 6 4.1571 - 3.9121 1.00 2658 148 0.1710 0.2142
REMARK 3 7 3.9121 - 3.7163 1.00 2659 146 0.1925 0.2595
REMARK 3 8 3.7163 - 3.5546 1.00 2645 147 0.1991 0.2547
REMARK 3 9 3.5546 - 3.4178 1.00 2637 142 0.1928 0.2721
REMARK 3 10 3.4178 - 3.2998 1.00 2632 148 0.1958 0.2359
REMARK 3 11 3.2998 - 3.1967 1.00 2623 147 0.1995 0.2613
REMARK 3 12 3.1967 - 3.1053 1.00 2643 136 0.2097 0.2611
REMARK 3 13 3.1053 - 3.0236 1.00 2631 138 0.2257 0.2838
REMARK 3 14 3.0236 - 2.9498 1.00 2631 147 0.2316 0.2818
REMARK 3 15 2.9498 - 2.8828 1.00 2610 146 0.2289 0.2731
REMARK 3 16 2.8828 - 2.8214 1.00 2654 135 0.2261 0.3206
REMARK 3 17 2.8214 - 2.7650 1.00 2594 152 0.2405 0.3191
REMARK 3 18 2.7650 - 2.7128 1.00 2647 132 0.2429 0.3141
REMARK 3 19 2.7128 - 2.6644 1.00 2590 150 0.2512 0.2933
REMARK 3 20 2.6644 - 2.6192 1.00 2608 126 0.2442 0.3092
REMARK 3 21 2.6192 - 2.5770 1.00 2624 147 0.2480 0.3351
REMARK 3 22 2.5770 - 2.5373 1.00 2611 152 0.2370 0.3055
REMARK 3 23 2.5373 - 2.5000 1.00 2604 129 0.2196 0.2708
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.79
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.012 12817
REMARK 3 ANGLE : 1.279 18531
REMARK 3 CHIRALITY : 0.059 2101
REMARK 3 PLANARITY : 0.007 1348
REMARK 3 DIHEDRAL : 29.120 5304
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 5
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN E
REMARK 3 ATOM PAIRS NUMBER : 936
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B
REMARK 3 SELECTION : CHAIN F
REMARK 3 ATOM PAIRS NUMBER : 736
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN C
REMARK 3 SELECTION : CHAIN G
REMARK 3 ATOM PAIRS NUMBER : 966
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN D
REMARK 3 SELECTION : CHAIN H
REMARK 3 ATOM PAIRS NUMBER : 872
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 5
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN I
REMARK 3 SELECTION : CHAIN J
REMARK 3 ATOM PAIRS NUMBER : 2758
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5JRG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221113.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98000
REMARK 200 MONOCHROMATOR : NUMERICAL LINK TYPE SI(111)
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR,
REMARK 200 LIQUID NITROGEN COOLED.
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64545
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 9.200
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.41800
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: PHASER
REMARK 200 STARTING MODEL: 3LZ0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM CACODYLATE, POTASSIUM
REMARK 280 CHLORIDE, MANGANESE CHLORIDE, PH 6.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
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 49.74550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.78550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.38650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.78550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.74550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.38650
REMARK 290 SMTRY3 4 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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 60960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 71400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -504.0 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 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
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 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
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 VAL B 21
REMARK 465 LEU B 22
REMARK 465 ARG B 23
REMARK 465 ASP B 24
REMARK 465 GLY C -3
REMARK 465 SER C -2
REMARK 465 HIS C -1
REMARK 465 MET C 0
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 ALA C 10
REMARK 465 ARG C 11
REMARK 465 LYS C 119
REMARK 465 THR C 120
REMARK 465 GLU C 121
REMARK 465 SER C 122
REMARK 465 HIS C 123
REMARK 465 HIS C 124
REMARK 465 LYS C 125
REMARK 465 ALA C 126
REMARK 465 LYS C 127
REMARK 465 GLY C 128
REMARK 465 LYS C 129
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 HIS D -1
REMARK 465 MET D 0
REMARK 465 PRO D 1
REMARK 465 GLU D 2
REMARK 465 PRO D 3
REMARK 465 ALA D 4
REMARK 465 LYS D 5
REMARK 465 SER D 6
REMARK 465 ALA D 7
REMARK 465 PRO D 8
REMARK 465 ALA D 9
REMARK 465 PRO D 10
REMARK 465 LYS D 11
REMARK 465 LYS D 12
REMARK 465 GLY D 13
REMARK 465 SER D 14
REMARK 465 LYS D 15
REMARK 465 LYS D 16
REMARK 465 ALA D 17
REMARK 465 VAL D 18
REMARK 465 THR D 19
REMARK 465 LYS D 20
REMARK 465 ALA D 21
REMARK 465 GLN D 22
REMARK 465 LYS D 23
REMARK 465 LYS D 24
REMARK 465 ASP D 25
REMARK 465 GLY D 26
REMARK 465 ALA D 124
REMARK 465 LYS D 125
REMARK 465 GLY E -3
REMARK 465 SER E -2
REMARK 465 HIS E -1
REMARK 465 MET E 0
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 GLY F -3
REMARK 465 SER F -2
REMARK 465 HIS F -1
REMARK 465 MET F 0
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 LYS F 16
REMARK 465 GLY G -3
REMARK 465 SER G -2
REMARK 465 HIS G -1
REMARK 465 MET G 0
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 LYS G 119
REMARK 465 THR G 120
REMARK 465 GLU G 121
REMARK 465 SER G 122
REMARK 465 HIS G 123
REMARK 465 HIS G 124
REMARK 465 LYS G 125
REMARK 465 ALA G 126
REMARK 465 LYS G 127
REMARK 465 GLY G 128
REMARK 465 LYS G 129
REMARK 465 GLY H -3
REMARK 465 SER H -2
REMARK 465 HIS H -1
REMARK 465 MET H 0
REMARK 465 PRO H 1
REMARK 465 GLU H 2
REMARK 465 PRO H 3
REMARK 465 ALA H 4
REMARK 465 LYS H 5
REMARK 465 SER H 6
REMARK 465 ALA H 7
REMARK 465 PRO H 8
REMARK 465 ALA H 9
REMARK 465 PRO H 10
REMARK 465 LYS H 11
REMARK 465 LYS H 12
REMARK 465 GLY H 13
REMARK 465 SER H 14
REMARK 465 LYS H 15
REMARK 465 LYS H 16
REMARK 465 ALA H 17
REMARK 465 VAL H 18
REMARK 465 THR H 19
REMARK 465 LYS H 20
REMARK 465 ALA H 21
REMARK 465 GLN H 22
REMARK 465 LYS H 23
REMARK 465 LYS H 24
REMARK 465 ASP H 25
REMARK 465 GLY H 26
REMARK 465 LYS H 27
REMARK 465 LYS H 28
REMARK 465 LYS H 125
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 I 27 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DA I 27 N9 C8 N7 C5 C6 N6 N1
REMARK 470 DA I 27 C2 N3 C4
REMARK 470 DA I 28 P OP1 OP2 O5'
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 OH TYR C 39 OE1 GLU D 71 2.15
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 DC I 47 O3' DC I 47 C3' -0.074
REMARK 500 DG I 71 O3' DG I 71 C3' -0.037
REMARK 500 DA I 76 O3' DA I 76 C3' -0.037
REMARK 500 DG I 80 O3' DG I 80 C3' -0.059
REMARK 500 DG I 97 O3' DG I 97 C3' -0.046
REMARK 500 DC I 100 O3' DC I 100 C3' -0.047
REMARK 500 DA I 101 O3' DA I 101 C3' -0.038
REMARK 500 DC I 106 O3' DC I 106 C3' -0.046
REMARK 500 DG I 121 O3' DG I 121 C3' -0.041
REMARK 500 DT I 122 O3' DT I 122 C3' -0.049
REMARK 500 DG I 124 O3' DG I 124 C3' -0.049
REMARK 500 DC J 3 O3' DC J 3 C3' -0.038
REMARK 500 DA J 27 O3' DA J 27 C3' -0.038
REMARK 500 DA J 28 O3' DA J 28 C3' -0.047
REMARK 500 DA J 29 O3' DA J 29 C3' -0.040
REMARK 500 DG J 31 O3' DG J 31 C3' -0.050
REMARK 500 DT J 37 O3' DT J 37 C3' -0.047
REMARK 500 DC J 44 O3' DC J 44 C3' -0.044
REMARK 500 DT J 45 O3' DT J 45 C3' -0.038
REMARK 500 DG J 46 O3' DG J 46 C3' -0.055
REMARK 500 DC J 47 O3' DC J 47 C3' -0.039
REMARK 500 DG J 59 O3' DG J 59 C3' -0.037
REMARK 500 DC J 66 O3' DC J 66 C3' -0.040
REMARK 500 DG J 71 O3' DG J 71 C3' -0.042
REMARK 500 DC J 88 O3' DC J 88 C3' -0.037
REMARK 500 DG J 99 O3' DG J 99 C3' -0.038
REMARK 500 DC J 100 O3' DC J 100 C3' -0.055
REMARK 500 DA J 101 O3' DA J 101 C3' -0.048
REMARK 500 DC J 107 O3' DC J 107 C3' -0.038
REMARK 500 DT J 118 O3' DT J 118 C3' -0.042
REMARK 500 DA J 123 O3' DA J 123 C3' -0.052
REMARK 500 DG J 130 O3' DG J 130 C3' -0.063
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG D 31 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG D 31 NE - CZ - NH2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 DC I 44 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DT I 45 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC I 49 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DA I 56 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DG I 58 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DA I 84 O4' - C1' - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DG I 86 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DT I 105 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DC I 115 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DG I 124 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DG I 130 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DA I 132 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DA I 138 O5' - P - OP1 ANGL. DEV. = -9.2 DEGREES
REMARK 500 DC J 25 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DT J 34 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DG J 40 O5' - P - OP1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 DC J 49 C3' - C2' - C1' ANGL. DEV. = -4.8 DEGREES
REMARK 500 DC J 49 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DG J 68 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DT J 79 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG J 93 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DC J 107 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DA J 109 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT J 127 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DC J 128 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DT J 135 O4' - C1' - N1 ANGL. DEV. = 2.5 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 ASN C 110 114.87 -161.68
REMARK 500 ASN G 110 114.59 -161.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN E3001 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 315 O
REMARK 620 2 VAL D 48 O 101.8
REMARK 620 3 HOH D 204 O 170.4 81.1
REMARK 620 4 HOH D 210 O 84.3 103.4 86.1
REMARK 620 5 ASP E 77 OD1 101.4 69.8 88.3 171.8
REMARK 620 6 HOH E3110 O 88.5 26.7 90.5 79.2 94.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN I 206 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG I 39 N7
REMARK 620 2 DG I 40 O6 85.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN I 205 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG I 96 N7
REMARK 620 2 DG I 97 O6 81.2
REMARK 620 3 HOH I 339 O 99.1 83.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN I 204 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG I 99 N7
REMARK 620 2 HOH I 310 O 85.6
REMARK 620 3 HOH I 342 O 105.0 90.3
REMARK 620 4 HOH I 348 O 92.3 160.1 109.3
REMARK 620 5 HOH J 315 O 85.6 69.9 157.0 90.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN J 202 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG J 39 N7
REMARK 620 2 HOH J 336 O 93.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN J 201 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG J 120 N7
REMARK 620 2 HOH J 326 O 78.7
REMARK 620 3 HOH J 344 O 92.9 69.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN E 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN I 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN I 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN I 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN I 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN I 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN I 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN I 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN J 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN J 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN J 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN J 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN J 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN J 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide DT I 116 and 3DR
REMARK 800 I 117
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide 3DR I 117 and DT
REMARK 800 I 118
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide DT J 116 and 3DR
REMARK 800 J 117
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide 3DR J 117 and DT
REMARK 800 J 118
DBREF 5JRG A 0 135 UNP P68431 H31_HUMAN 1 136
DBREF 5JRG B 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 5JRG C 0 129 UNP P04908 H2A1B_HUMAN 1 130
DBREF 5JRG D 0 125 UNP P06899 H2B1J_HUMAN 1 126
DBREF 5JRG E 0 135 UNP P68431 H31_HUMAN 1 136
DBREF 5JRG F 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 5JRG G 0 129 UNP P04908 H2A1B_HUMAN 1 130
DBREF 5JRG H 0 125 UNP P06899 H2B1J_HUMAN 1 126
DBREF 5JRG I 1 145 PDB 5JRG 5JRG 1 145
DBREF 5JRG J 1 145 PDB 5JRG 5JRG 1 145
SEQADV 5JRG GLY A -3 UNP P68431 EXPRESSION TAG
SEQADV 5JRG SER A -2 UNP P68431 EXPRESSION TAG
SEQADV 5JRG HIS A -1 UNP P68431 EXPRESSION TAG
SEQADV 5JRG GLY B -3 UNP P62805 EXPRESSION TAG
SEQADV 5JRG SER B -2 UNP P62805 EXPRESSION TAG
SEQADV 5JRG HIS B -1 UNP P62805 EXPRESSION TAG
SEQADV 5JRG GLY C -3 UNP P04908 EXPRESSION TAG
SEQADV 5JRG SER C -2 UNP P04908 EXPRESSION TAG
SEQADV 5JRG HIS C -1 UNP P04908 EXPRESSION TAG
SEQADV 5JRG GLY D -3 UNP P06899 EXPRESSION TAG
SEQADV 5JRG SER D -2 UNP P06899 EXPRESSION TAG
SEQADV 5JRG HIS D -1 UNP P06899 EXPRESSION TAG
SEQADV 5JRG GLY E -3 UNP P68431 EXPRESSION TAG
SEQADV 5JRG SER E -2 UNP P68431 EXPRESSION TAG
SEQADV 5JRG HIS E -1 UNP P68431 EXPRESSION TAG
SEQADV 5JRG GLY F -3 UNP P62805 EXPRESSION TAG
SEQADV 5JRG SER F -2 UNP P62805 EXPRESSION TAG
SEQADV 5JRG HIS F -1 UNP P62805 EXPRESSION TAG
SEQADV 5JRG GLY G -3 UNP P04908 EXPRESSION TAG
SEQADV 5JRG SER G -2 UNP P04908 EXPRESSION TAG
SEQADV 5JRG HIS G -1 UNP P04908 EXPRESSION TAG
SEQADV 5JRG GLY H -3 UNP P06899 EXPRESSION TAG
SEQADV 5JRG SER H -2 UNP P06899 EXPRESSION TAG
SEQADV 5JRG HIS H -1 UNP P06899 EXPRESSION TAG
SEQRES 1 A 139 GLY SER HIS MET ALA ARG THR LYS GLN THR ALA ARG LYS
SEQRES 2 A 139 SER THR GLY GLY LYS ALA PRO ARG LYS GLN LEU ALA THR
SEQRES 3 A 139 LYS ALA ALA ARG LYS SER ALA PRO ALA THR GLY GLY VAL
SEQRES 4 A 139 LYS LYS PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU
SEQRES 5 A 139 ARG GLU ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU
SEQRES 6 A 139 ILE ARG LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE
SEQRES 7 A 139 ALA GLN ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER
SEQRES 8 A 139 ALA VAL MET ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU
SEQRES 9 A 139 VAL GLY LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS
SEQRES 10 A 139 ALA LYS ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU
SEQRES 11 A 139 ALA ARG ARG ILE ARG GLY GLU ARG ALA
SEQRES 1 B 106 GLY SER HIS MET SER GLY ARG GLY LYS GLY GLY LYS GLY
SEQRES 2 B 106 LEU GLY LYS GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU
SEQRES 3 B 106 ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG
SEQRES 4 B 106 ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY
SEQRES 5 B 106 LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE
SEQRES 6 B 106 LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU
SEQRES 7 B 106 HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL
SEQRES 8 B 106 TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE
SEQRES 9 B 106 GLY GLY
SEQRES 1 C 133 GLY SER HIS MET SER GLY ARG GLY LYS GLN GLY GLY LYS
SEQRES 2 C 133 ALA ARG ALA LYS ALA LYS THR ARG SER SER ARG ALA GLY
SEQRES 3 C 133 LEU GLN PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG
SEQRES 4 C 133 LYS GLY ASN TYR SER GLU ARG VAL GLY ALA GLY ALA PRO
SEQRES 5 C 133 VAL TYR LEU ALA ALA VAL LEU GLU TYR LEU THR ALA GLU
SEQRES 6 C 133 ILE LEU GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS
SEQRES 7 C 133 LYS THR ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE
SEQRES 8 C 133 ARG ASN ASP GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL
SEQRES 9 C 133 THR ILE ALA GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA
SEQRES 10 C 133 VAL LEU LEU PRO LYS LYS THR GLU SER HIS HIS LYS ALA
SEQRES 11 C 133 LYS GLY LYS
SEQRES 1 D 129 GLY SER HIS MET PRO GLU PRO ALA LYS SER ALA PRO ALA
SEQRES 2 D 129 PRO LYS LYS GLY SER LYS LYS ALA VAL THR LYS ALA GLN
SEQRES 3 D 129 LYS LYS ASP GLY LYS LYS ARG LYS ARG SER ARG LYS GLU
SEQRES 4 D 129 SER TYR SER ILE TYR VAL TYR LYS VAL LEU LYS GLN VAL
SEQRES 5 D 129 HIS PRO ASP THR GLY ILE SER SER LYS ALA MET GLY ILE
SEQRES 6 D 129 MET ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA
SEQRES 7 D 129 GLY GLU ALA SER ARG LEU ALA HIS TYR ASN LYS ARG SER
SEQRES 8 D 129 THR ILE THR SER ARG GLU ILE GLN THR ALA VAL ARG LEU
SEQRES 9 D 129 LEU LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU
SEQRES 10 D 129 GLY THR LYS ALA VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 E 139 GLY SER HIS MET ALA ARG THR LYS GLN THR ALA ARG LYS
SEQRES 2 E 139 SER THR GLY GLY LYS ALA PRO ARG LYS GLN LEU ALA THR
SEQRES 3 E 139 LYS ALA ALA ARG LYS SER ALA PRO ALA THR GLY GLY VAL
SEQRES 4 E 139 LYS LYS PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU
SEQRES 5 E 139 ARG GLU ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU
SEQRES 6 E 139 ILE ARG LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE
SEQRES 7 E 139 ALA GLN ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER
SEQRES 8 E 139 ALA VAL MET ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU
SEQRES 9 E 139 VAL GLY LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS
SEQRES 10 E 139 ALA LYS ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU
SEQRES 11 E 139 ALA ARG ARG ILE ARG GLY GLU ARG ALA
SEQRES 1 F 106 GLY SER HIS MET SER GLY ARG GLY LYS GLY GLY LYS GLY
SEQRES 2 F 106 LEU GLY LYS GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU
SEQRES 3 F 106 ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG
SEQRES 4 F 106 ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY
SEQRES 5 F 106 LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE
SEQRES 6 F 106 LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU
SEQRES 7 F 106 HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL
SEQRES 8 F 106 TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE
SEQRES 9 F 106 GLY GLY
SEQRES 1 G 133 GLY SER HIS MET SER GLY ARG GLY LYS GLN GLY GLY LYS
SEQRES 2 G 133 ALA ARG ALA LYS ALA LYS THR ARG SER SER ARG ALA GLY
SEQRES 3 G 133 LEU GLN PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG
SEQRES 4 G 133 LYS GLY ASN TYR SER GLU ARG VAL GLY ALA GLY ALA PRO
SEQRES 5 G 133 VAL TYR LEU ALA ALA VAL LEU GLU TYR LEU THR ALA GLU
SEQRES 6 G 133 ILE LEU GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS
SEQRES 7 G 133 LYS THR ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE
SEQRES 8 G 133 ARG ASN ASP GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL
SEQRES 9 G 133 THR ILE ALA GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA
SEQRES 10 G 133 VAL LEU LEU PRO LYS LYS THR GLU SER HIS HIS LYS ALA
SEQRES 11 G 133 LYS GLY LYS
SEQRES 1 H 129 GLY SER HIS MET PRO GLU PRO ALA LYS SER ALA PRO ALA
SEQRES 2 H 129 PRO LYS LYS GLY SER LYS LYS ALA VAL THR LYS ALA GLN
SEQRES 3 H 129 LYS LYS ASP GLY LYS LYS ARG LYS ARG SER ARG LYS GLU
SEQRES 4 H 129 SER TYR SER ILE TYR VAL TYR LYS VAL LEU LYS GLN VAL
SEQRES 5 H 129 HIS PRO ASP THR GLY ILE SER SER LYS ALA MET GLY ILE
SEQRES 6 H 129 MET ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA
SEQRES 7 H 129 GLY GLU ALA SER ARG LEU ALA HIS TYR ASN LYS ARG SER
SEQRES 8 H 129 THR ILE THR SER ARG GLU ILE GLN THR ALA VAL ARG LEU
SEQRES 9 H 129 LEU LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU
SEQRES 10 H 129 GLY THR LYS ALA 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 DT 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 DC 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 3DR
SEQRES 10 I 145 DT DT DG DG DT DA DG DA 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 DT 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 DG 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 3DR
SEQRES 10 J 145 DT DT DG DG DT DA DG DA 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 3DR I 117 11
HET 3DR J 117 11
HET CL A 201 1
HET CL C 201 1
HET MN E3001 1
HET CL E3002 1
HET CL G2001 1
HET MN I 201 1
HET MN I 202 1
HET MN I 203 1
HET MN I 204 1
HET MN I 205 1
HET MN I 206 1
HET MN I 207 1
HET MN I 208 1
HET MN J 201 1
HET MN J 202 1
HET MN J 203 1
HET MN J 204 1
HET MN J 205 1
HET MN J 206 1
HETNAM 3DR 1',2'-DIDEOXYRIBOFURANOSE-5'-PHOSPHATE
HETNAM CL CHLORIDE ION
HETNAM MN MANGANESE (II) ION
HETSYN 3DR ABASIC DIDEOXYRIBOSE
FORMUL 9 3DR 2(C5 H11 O6 P)
FORMUL 11 CL 4(CL 1-)
FORMUL 13 MN 15(MN 2+)
FORMUL 30 HOH *244(H2 O)
HELIX 1 AA1 GLY A 44 SER A 57 1 14
HELIX 2 AA2 ARG A 63 ASP A 77 1 15
HELIX 3 AA3 GLN A 85 ALA A 114 1 30
HELIX 4 AA4 MET A 120 ARG A 131 1 12
HELIX 5 AA5 ASN B 25 ILE B 29 5 5
HELIX 6 AA6 THR B 30 GLY B 41 1 12
HELIX 7 AA7 LEU B 49 ALA B 76 1 28
HELIX 8 AA8 THR B 82 GLN B 93 1 12
HELIX 9 AA9 THR C 16 GLY C 22 1 7
HELIX 10 AB1 PRO C 26 LYS C 36 1 11
HELIX 11 AB2 GLY C 46 ASN C 73 1 28
HELIX 12 AB3 ILE C 79 ASN C 89 1 11
HELIX 13 AB4 ASP C 90 LEU C 97 1 8
HELIX 14 AB5 GLN C 112 LEU C 116 5 5
HELIX 15 AB6 TYR D 37 HIS D 49 1 13
HELIX 16 AB7 SER D 55 ASN D 84 1 30
HELIX 17 AB8 THR D 90 LEU D 102 1 13
HELIX 18 AB9 PRO D 103 SER D 123 1 21
HELIX 19 AC1 GLY E 44 SER E 57 1 14
HELIX 20 AC2 ARG E 63 LYS E 79 1 17
HELIX 21 AC3 GLN E 85 ALA E 114 1 30
HELIX 22 AC4 MET E 120 ARG E 131 1 12
HELIX 23 AC5 ASP F 24 ILE F 29 5 6
HELIX 24 AC6 THR F 30 GLY F 41 1 12
HELIX 25 AC7 LEU F 49 ALA F 76 1 28
HELIX 26 AC8 THR F 82 GLN F 93 1 12
HELIX 27 AC9 THR G 16 GLY G 22 1 7
HELIX 28 AD1 PRO G 26 GLY G 37 1 12
HELIX 29 AD2 GLY G 46 ASN G 73 1 28
HELIX 30 AD3 ILE G 79 ASN G 89 1 11
HELIX 31 AD4 ASP G 90 LEU G 97 1 8
HELIX 32 AD5 GLN G 112 LEU G 116 5 5
HELIX 33 AD6 TYR H 37 HIS H 49 1 13
HELIX 34 AD7 SER H 55 ASN H 84 1 30
HELIX 35 AD8 THR H 90 LEU H 102 1 13
HELIX 36 AD9 PRO H 103 ALA H 124 1 22
SHEET 1 AA1 2 ARG A 83 PHE A 84 0
SHEET 2 AA1 2 THR B 80 VAL B 81 1 O VAL B 81 N ARG A 83
SHEET 1 AA2 2 THR A 118 ILE A 119 0
SHEET 2 AA2 2 ARG B 45 ILE B 46 1 O ARG B 45 N ILE A 119
SHEET 1 AA3 2 THR B 96 TYR B 98 0
SHEET 2 AA3 2 VAL G 100 ILE G 102 1 O THR G 101 N TYR B 98
SHEET 1 AA4 2 ARG C 42 VAL C 43 0
SHEET 2 AA4 2 THR D 88 ILE D 89 1 O ILE D 89 N ARG C 42
SHEET 1 AA5 2 ARG C 77 ILE C 78 0
SHEET 2 AA5 2 GLY D 53 ILE D 54 1 O GLY D 53 N ILE C 78
SHEET 1 AA6 2 VAL C 100 ILE C 102 0
SHEET 2 AA6 2 THR F 96 TYR F 98 1 O TYR F 98 N THR C 101
SHEET 1 AA7 2 ARG E 83 PHE E 84 0
SHEET 2 AA7 2 THR F 80 VAL F 81 1 O VAL F 81 N ARG E 83
SHEET 1 AA8 2 THR E 118 ILE E 119 0
SHEET 2 AA8 2 ARG F 45 ILE F 46 1 O ARG F 45 N ILE E 119
SHEET 1 AA9 2 ARG G 42 VAL G 43 0
SHEET 2 AA9 2 THR H 88 ILE H 89 1 O ILE H 89 N ARG G 42
SHEET 1 AB1 2 ARG G 77 ILE G 78 0
SHEET 2 AB1 2 GLY H 53 ILE H 54 1 O GLY H 53 N ILE G 78
LINK O3' DT I 116 P 3DR I 117 1555 1555 1.61
LINK O3' 3DR I 117 P DT I 118 1555 1555 1.60
LINK O3' DT J 116 P 3DR J 117 1555 1555 1.61
LINK O3' 3DR J 117 P DT J 118 1555 1555 1.61
LINK O HOH C 315 MN MN E3001 3959 1555 1.91
LINK O VAL D 48 MN MN E3001 1555 3949 2.26
LINK O HOH D 204 MN MN E3001 3959 1555 2.31
LINK O HOH D 210 MN MN E3001 3959 1555 1.82
LINK OD1 ASP E 77 MN MN E3001 1555 1555 2.17
LINK MN MN E3001 O HOH E3110 1555 1555 2.20
LINK N7 DG I 39 MN MN I 206 1555 1555 2.62
LINK O6 DG I 40 MN MN I 206 1555 1555 2.33
LINK N7 DG I 96 MN MN I 205 1555 1555 2.63
LINK O6 DG I 97 MN MN I 205 1555 1555 2.54
LINK N7 DG I 99 MN MN I 204 1555 1555 2.44
LINK N7 DG I 120 MN MN I 203 1555 1555 2.39
LINK OP1 DT I 135 MN MN I 201 1555 1555 2.32
LINK MN MN I 202 O HOH I 314 1555 4499 2.35
LINK MN MN I 204 O HOH I 310 1555 1555 2.36
LINK MN MN I 204 O HOH I 342 1555 1555 2.42
LINK MN MN I 204 O HOH I 348 1555 1555 2.52
LINK MN MN I 204 O HOH J 315 1555 1555 2.42
LINK MN MN I 205 O HOH I 339 1555 1555 2.79
LINK MN MN I 207 O HOH I 325 1555 1555 2.68
LINK OP1 DT J 37 MN MN J 206 1555 1555 2.06
LINK N7 DG J 39 MN MN J 202 1555 1555 2.24
LINK N7 DG J 68 MN MN J 205 1555 1555 2.74
LINK N7 DG J 99 MN MN J 204 1555 1555 2.47
LINK N7 DG J 120 MN MN J 201 1555 1555 2.54
LINK N7 DG J 133 MN MN J 203 1555 1555 2.59
LINK MN MN J 201 O HOH J 326 1555 1555 2.16
LINK MN MN J 201 O HOH J 344 1555 1555 2.58
LINK MN MN J 202 O HOH J 336 1555 1555 2.19
CISPEP 1 LYS E 37 PRO E 38 0 -11.59
SITE 1 AC1 2 PRO A 121 LYS A 122
SITE 1 AC2 4 GLY C 46 ALA C 47 THR D 90 SER D 91
SITE 1 AC3 2 ASP E 77 HOH E3110
SITE 1 AC4 2 PRO E 121 LYS E 122
SITE 1 AC5 7 GLY G 44 ALA G 45 GLY G 46 ALA G 47
SITE 2 AC5 7 THR H 90 SER H 91 HOH I 337
SITE 1 AC6 1 DT I 135
SITE 1 AC7 1 DG I 120
SITE 1 AC8 5 DG I 99 HOH I 310 HOH I 342 HOH I 348
SITE 2 AC8 5 HOH J 315
SITE 1 AC9 3 DG I 96 DG I 97 HOH I 339
SITE 1 AD1 4 DG I 39 DG I 40 HOH I 306 DC J 106
SITE 1 AD2 3 DA I 132 DG I 133 HOH I 325
SITE 1 AD3 2 DG I 68 HOH I 347
SITE 1 AD4 3 DG J 120 HOH J 326 HOH J 344
SITE 1 AD5 3 DG J 39 DG J 40 HOH J 336
SITE 1 AD6 1 DG J 133
SITE 1 AD7 1 DG J 99
SITE 1 AD8 1 DG J 68
SITE 1 AD9 1 DT J 37
SITE 1 AE1 6 ARG G 11 DC I 115 DT I 118 DA J 29
SITE 2 AE1 6 DA J 30 DG J 31
SITE 1 AE2 4 DT I 116 DT I 119 DA J 27 DA J 28
SITE 1 AE3 5 DA I 29 DA I 30 DG I 31 DC J 115
SITE 2 AE3 5 DT J 118
SITE 1 AE4 5 DA I 28 DA I 29 DA I 30 DT J 116
SITE 2 AE4 5 DT J 119
CRYST1 99.491 108.773 169.571 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 0.010051 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009193 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005897 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
