HEADER DNA BINDING PROTEIN/DNA 12-AUG-14 4R2R
TITLE WILMS TUMOR PROTEIN (WT1) ZINC FINGERS IN COMPLEX WITH CARBOXYLATED
TITLE 2 DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WILMS TUMOR PROTEIN, ISOFORM 4/CRA_A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZINC FINGER 2-4;
COMPND 5 SYNONYM: WT33;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-D(*AP*GP*CP*GP*TP*GP*GP*GP*(1CC)P*GP*T)-3');
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: DNA (5'-D(*TP*AP*(5CM)P*GP*CP*CP*CP*AP*CP*GP*C)-3');
COMPND 13 CHAIN: C;
COMPND 14 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: WT1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1, PXC1295;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630;
SOURCE 15 OTHER_DETAILS: CHEMICAL SYNTHESIS;
SOURCE 16 MOL_ID: 3;
SOURCE 17 SYNTHETIC: YES;
SOURCE 18 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 19 ORGANISM_TAXID: 32630;
SOURCE 20 OTHER_DETAILS: CHEMICAL SYNTHESIS
KEYWDS ZINC FINGER, TRANSCRIPTION, DNA BINDING PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HASHIMOTO,Y.O.OLANREWAJU,Y.ZHENG,G.G.WILSON,X.ZHANG,X.CHENG
REVDAT 3 20-SEP-23 4R2R 1 REMARK SEQADV LINK
REVDAT 2 19-NOV-14 4R2R 1 JRNL
REVDAT 1 08-OCT-14 4R2R 0
JRNL AUTH H.HASHIMOTO,Y.O.OLANREWAJU,Y.ZHENG,G.G.WILSON,X.ZHANG,
JRNL AUTH 2 X.CHENG
JRNL TITL WILMS TUMOR PROTEIN RECOGNIZES 5-CARBOXYLCYTOSINE WITHIN A
JRNL TITL 2 SPECIFIC DNA SEQUENCE.
JRNL REF GENES DEV. V. 28 2304 2014
JRNL REFN ISSN 0890-9369
JRNL PMID 25258363
JRNL DOI 10.1101/GAD.250746.114
REMARK 2
REMARK 2 RESOLUTION. 2.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 11418
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 571
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 29.1241 - 3.3147 1.00 2846 151 0.1626 0.1827
REMARK 3 2 3.3147 - 2.6315 1.00 2715 142 0.2178 0.2418
REMARK 3 3 2.6315 - 2.2990 1.00 2688 142 0.2242 0.2801
REMARK 3 4 2.2990 - 2.0889 0.98 2598 136 0.2338 0.2803
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.540
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 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 : 0.004 1335
REMARK 3 ANGLE : 0.680 1885
REMARK 3 CHIRALITY : 0.030 196
REMARK 3 PLANARITY : 0.002 161
REMARK 3 DIHEDRAL : 25.046 561
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4R2R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000086825.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11476
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.089
REMARK 200 RESOLUTION RANGE LOW (A) : 29.121
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.42700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 4R2E
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% (W/V) PEGMME 2000, 0.1 M BISTRIS
REMARK 280 PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 33.47850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.75900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.47850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.75900
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 345
REMARK 465 PRO A 346
REMARK 465 LEU A 347
REMARK 465 GLY A 348
REMARK 465 ARG A 437
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 SER A 349 OG
REMARK 470 GLN A 354 CG CD OE1 NE2
REMARK 470 GLN A 419 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DG C 4 O4' - C1' - N9 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 HIS A 435 2.80 -65.05
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 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 355 SG
REMARK 620 2 CYS A 360 SG 114.4
REMARK 620 3 HIS A 373 NE2 110.0 104.6
REMARK 620 4 HIS A 377 NE2 113.6 111.2 101.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 385 SG
REMARK 620 2 CYS A 388 SG 116.7
REMARK 620 3 HIS A 401 NE2 111.0 104.3
REMARK 620 4 HIS A 405 NE2 110.4 109.7 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 413 SG
REMARK 620 2 CYS A 418 SG 111.3
REMARK 620 3 HIS A 431 NE2 106.9 114.0
REMARK 620 4 HIS A 435 NE2 111.7 117.8 93.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4R2A RELATED DB: PDB
REMARK 900 RELATED ID: 4R2C RELATED DB: PDB
REMARK 900 RELATED ID: 4R2D RELATED DB: PDB
REMARK 900 RELATED ID: 4R2E RELATED DB: PDB
REMARK 900 RELATED ID: 4R2P RELATED DB: PDB
REMARK 900 RELATED ID: 4R2Q RELATED DB: PDB
REMARK 900 RELATED ID: 4R2S RELATED DB: PDB
DBREF 4R2R A 350 437 UNP P19544 WT1_HUMAN 350 437
DBREF 4R2R B 1 11 PDB 4R2R 4R2R 1 11
DBREF 4R2R C 1 11 PDB 4R2R 4R2R 1 11
SEQADV 4R2R GLY A 345 UNP P19544 EXPRESSION TAG
SEQADV 4R2R PRO A 346 UNP P19544 EXPRESSION TAG
SEQADV 4R2R LEU A 347 UNP P19544 EXPRESSION TAG
SEQADV 4R2R GLY A 348 UNP P19544 EXPRESSION TAG
SEQADV 4R2R SER A 349 UNP P19544 EXPRESSION TAG
SEQRES 1 A 93 GLY PRO LEU GLY SER GLU LYS PRO TYR GLN CYS ASP PHE
SEQRES 2 A 93 LYS ASP CYS GLU ARG ARG PHE SER ARG SER ASP GLN LEU
SEQRES 3 A 93 LYS ARG HIS GLN ARG ARG HIS THR GLY VAL LYS PRO PHE
SEQRES 4 A 93 GLN CYS LYS THR CYS GLN ARG LYS PHE SER ARG SER ASP
SEQRES 5 A 93 HIS LEU LYS THR HIS THR ARG THR HIS THR GLY GLU LYS
SEQRES 6 A 93 PRO PHE SER CYS ARG TRP PRO SER CYS GLN LYS LYS PHE
SEQRES 7 A 93 ALA ARG SER ASP GLU LEU VAL ARG HIS HIS ASN MET HIS
SEQRES 8 A 93 GLN ARG
SEQRES 1 B 11 DA DG DC DG DT DG DG DG 1CC DG DT
SEQRES 1 C 11 DT DA 5CM DG DC DC DC DA DC DG DC
MODRES 4R2R 1CC B 9 DC
MODRES 4R2R 5CM C 3 DC
HET 1CC B 9 22
HET 5CM C 3 31
HET ZN A 501 1
HET ZN A 502 1
HET ZN A 503 1
HET EDO A 504 4
HETNAM 1CC 5-CARBOXY-2'-DEOXYCYTIDINE MONOPHOSPHATE
HETNAM 5CM 5-METHYL-2'-DEOXY-CYTIDINE-5'-MONOPHOSPHATE
HETNAM ZN ZINC ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 1CC C10 H14 N3 O9 P
FORMUL 3 5CM C10 H16 N3 O7 P
FORMUL 4 ZN 3(ZN 2+)
FORMUL 7 EDO C2 H6 O2
FORMUL 8 HOH *111(H2 O)
HELIX 1 1 ARG A 366 GLY A 379 1 14
HELIX 2 2 ARG A 394 GLY A 407 1 14
HELIX 3 3 ARG A 424 HIS A 435 1 12
SHEET 1 A 2 TYR A 353 GLN A 354 0
SHEET 2 A 2 ARG A 363 PHE A 364 -1 O PHE A 364 N TYR A 353
SHEET 1 B 2 PHE A 383 GLN A 384 0
SHEET 2 B 2 LYS A 391 PHE A 392 -1 O PHE A 392 N PHE A 383
SHEET 1 C 2 PHE A 411 SER A 412 0
SHEET 2 C 2 LYS A 421 PHE A 422 -1 O PHE A 422 N PHE A 411
LINK O3' DG B 8 P 1CC B 9 1555 1555 1.61
LINK O3'A DA C 2 P A5CM C 3 1555 1555 1.61
LINK O3'B DA C 2 P B5CM C 3 1555 1555 1.61
LINK O3'A5CM C 3 P A DG C 4 1555 1555 1.61
LINK O3'B5CM C 3 P B DG C 4 1555 1555 1.61
LINK SG CYS A 355 ZN ZN A 501 1555 1555 2.27
LINK SG CYS A 360 ZN ZN A 501 1555 1555 2.26
LINK NE2 HIS A 373 ZN ZN A 501 1555 1555 2.03
LINK NE2 HIS A 377 ZN ZN A 501 1555 1555 2.05
LINK SG CYS A 385 ZN ZN A 502 1555 1555 2.27
LINK SG CYS A 388 ZN ZN A 502 1555 1555 2.29
LINK NE2 HIS A 401 ZN ZN A 502 1555 1555 2.05
LINK NE2 HIS A 405 ZN ZN A 502 1555 1555 2.04
LINK SG CYS A 413 ZN ZN A 503 1555 1555 2.26
LINK SG CYS A 418 ZN ZN A 503 1555 1555 2.27
LINK NE2 HIS A 431 ZN ZN A 503 1555 1555 2.02
LINK NE2 HIS A 435 ZN ZN A 503 1555 1555 2.04
SITE 1 AC1 4 CYS A 355 CYS A 360 HIS A 373 HIS A 377
SITE 1 AC2 4 CYS A 385 CYS A 388 HIS A 401 HIS A 405
SITE 1 AC3 4 CYS A 413 CYS A 418 HIS A 431 HIS A 435
SITE 1 AC4 5 ARG A 372 SER A 393 ARG A 394 DG B 6
SITE 2 AC4 5 HOH B 111
CRYST1 66.957 77.518 35.585 90.00 90.00 90.00 P 21 21 2 4
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 0.014935 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012900 0.000000 0.00000
SCALE3 0.000000 0.000000 0.028102 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
