HEADER TRANSFERASE/DNA 09-JAN-17 5UGN
TITLE DNA POLYMERASE BETA IMIDODIPHOSPHATE REACTANT COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*CP*CP*GP*AP*CP*GP*GP*CP*GP*CP*AP*TP*CP*AP*GP*C)-
COMPND 3 3');
COMPND 4 CHAIN: T;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-D(*GP*CP*TP*GP*AP*TP*GP*CP*GP*CP*C)-3');
COMPND 8 CHAIN: P;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: DNA (5'-D(P*GP*TP*CP*GP*G)-3');
COMPND 12 CHAIN: D;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: DNA POLYMERASE BETA;
COMPND 16 CHAIN: A;
COMPND 17 EC: 2.7.7.7,4.2.99.-;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 4 ORGANISM_TAXID: 32630;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 8 ORGANISM_TAXID: 32630;
SOURCE 9 MOL_ID: 3;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 12 ORGANISM_TAXID: 32630;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 GENE: POLB;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE, LYASE, DNA DOMAIN, TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.D.FREUDENTHAL,S.H.WILSON,W.A.BEARD
REVDAT 6 04-OCT-23 5UGN 1 LINK
REVDAT 5 18-DEC-19 5UGN 1 REMARK
REVDAT 4 04-OCT-17 5UGN 1 JRNL
REVDAT 3 16-AUG-17 5UGN 1 JRNL
REVDAT 2 02-AUG-17 5UGN 1 REVDAT
REVDAT 1 26-JUL-17 5UGN 0
JRNL AUTH D.D.SHOCK,B.D.FREUDENTHAL,W.A.BEARD,S.H.WILSON
JRNL TITL MODULATING THE DNA POLYMERASE BETA REACTION EQUILIBRIUM TO
JRNL TITL 2 DISSECT THE REVERSE REACTION.
JRNL REF NAT. CHEM. BIOL. V. 13 1074 2017
JRNL REFN ESSN 1552-4469
JRNL PMID 28759020
JRNL DOI 10.1038/NCHEMBIO.2450
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10_2155
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.15
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 28348
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1421
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 23.1553 - 4.2934 1.00 2762 146 0.1434 0.1959
REMARK 3 2 4.2934 - 3.4113 1.00 2739 143 0.1513 0.2062
REMARK 3 3 3.4113 - 2.9811 1.00 2709 144 0.1960 0.2661
REMARK 3 4 2.9811 - 2.7090 0.99 2691 143 0.2415 0.2950
REMARK 3 5 2.7090 - 2.5151 1.00 2708 143 0.2286 0.3059
REMARK 3 6 2.5151 - 2.3669 1.00 2721 143 0.2159 0.3011
REMARK 3 7 2.3669 - 2.2485 1.00 2710 143 0.1950 0.2664
REMARK 3 8 2.2485 - 2.1507 1.00 2707 142 0.1913 0.2475
REMARK 3 9 2.1507 - 2.0679 0.99 2675 142 0.2009 0.2657
REMARK 3 10 2.0679 - 1.9966 0.93 2505 132 0.2151 0.2598
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.540
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 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 : 0.007 3491
REMARK 3 ANGLE : 0.871 4853
REMARK 3 CHIRALITY : 0.051 523
REMARK 3 PLANARITY : 0.005 512
REMARK 3 DIHEDRAL : 19.016 2029
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 5UGN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1000225833.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28404
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.997
REMARK 200 RESOLUTION RANGE LOW (A) : 23.154
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.50400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: 2FMS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM IMIDAZOLE, 350 MM SODIUM
REMARK 280 CHLORIDE, 17% PEG3350, PH 8, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 39.96100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, P, D, A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 MET A 1
REMARK 465 SER A 2
REMARK 465 LYS A 3
REMARK 465 ARG A 4
REMARK 465 LYS A 5
REMARK 465 ALA A 6
REMARK 465 PRO A 7
REMARK 465 GLN A 8
REMARK 465 GLU A 9
REMARK 465 VAL A 303
REMARK 465 THR A 304
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 248 CG CD CE NZ
REMARK 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 O HOH A 686 O HOH A 709 2.14
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 DC T 5 O4' - C1' - N1 ANGL. DEV. = 2.2 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 CYS A 178 -138.07 -113.54
REMARK 500 ASP A 246 -9.26 74.88
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 MG A 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DC P 10 O3'
REMARK 620 2 DC P 10 O3' 17.7
REMARK 620 3 DC P 11 OP1 79.3 65.8
REMARK 620 4 ASP A 190 OD2 143.9 128.8 90.3
REMARK 620 5 ASP A 192 OD1 91.2 101.7 88.8 123.4
REMARK 620 6 ASP A 256 OD2 78.0 89.5 154.5 101.2 103.2
REMARK 620 7 8CP A 404 O2A 82.1 68.3 2.9 87.6 89.5 156.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DC P 11 OP1
REMARK 620 2 ASP A 190 OD1 87.5
REMARK 620 3 ASP A 192 OD2 88.7 100.1
REMARK 620 4 2PN A 401 O2 103.2 84.9 167.4
REMARK 620 5 2PN A 401 O6 105.7 164.8 88.0 84.7
REMARK 620 6 8CP A 404 O2A 12.7 95.6 97.0 94.0 96.2
REMARK 620 7 8CP A 404 O1B 96.7 167.4 91.9 82.6 9.9 86.7
REMARK 620 8 8CP A 404 O3G 94.5 82.4 176.1 8.9 88.9 85.8 85.4
REMARK 620 9 HOH A 544 O 170.4 88.2 83.6 85.0 79.8 176.0 89.3 93.5
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2PN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8CP A 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UGO RELATED DB: PDB
REMARK 900 RELATED ID: 5UGP RELATED DB: PDB
DBREF 5UGN T 1 16 PDB 5UGN 5UGN 1 16
DBREF 5UGN P 1 11 PDB 5UGN 5UGN 1 11
DBREF 5UGN D 1 5 PDB 5UGN 5UGN 1 5
DBREF 5UGN A 1 335 UNP P06746 DPOLB_HUMAN 1 335
SEQRES 1 T 16 DC DC DG DA DC DG DG DC DG DC DA DT DC
SEQRES 2 T 16 DA DG DC
SEQRES 1 P 11 DG DC DT DG DA DT DG DC DG DC DC
SEQRES 1 D 5 DG DT DC DG DG
SEQRES 1 A 335 MET SER LYS ARG LYS ALA PRO GLN GLU THR LEU ASN GLY
SEQRES 2 A 335 GLY ILE THR ASP MET LEU THR GLU LEU ALA ASN PHE GLU
SEQRES 3 A 335 LYS ASN VAL SER GLN ALA ILE HIS LYS TYR ASN ALA TYR
SEQRES 4 A 335 ARG LYS ALA ALA SER VAL ILE ALA LYS TYR PRO HIS LYS
SEQRES 5 A 335 ILE LYS SER GLY ALA GLU ALA LYS LYS LEU PRO GLY VAL
SEQRES 6 A 335 GLY THR LYS ILE ALA GLU LYS ILE ASP GLU PHE LEU ALA
SEQRES 7 A 335 THR GLY LYS LEU ARG LYS LEU GLU LYS ILE ARG GLN ASP
SEQRES 8 A 335 ASP THR SER SER SER ILE ASN PHE LEU THR ARG VAL SER
SEQRES 9 A 335 GLY ILE GLY PRO SER ALA ALA ARG LYS PHE VAL ASP GLU
SEQRES 10 A 335 GLY ILE LYS THR LEU GLU ASP LEU ARG LYS ASN GLU ASP
SEQRES 11 A 335 LYS LEU ASN HIS HIS GLN ARG ILE GLY LEU LYS TYR PHE
SEQRES 12 A 335 GLY ASP PHE GLU LYS ARG ILE PRO ARG GLU GLU MET LEU
SEQRES 13 A 335 GLN MET GLN ASP ILE VAL LEU ASN GLU VAL LYS LYS VAL
SEQRES 14 A 335 ASP SER GLU TYR ILE ALA THR VAL CYS GLY SER PHE ARG
SEQRES 15 A 335 ARG GLY ALA GLU SER SER GLY ASP MET ASP VAL LEU LEU
SEQRES 16 A 335 THR HIS PRO SER PHE THR SER GLU SER THR LYS GLN PRO
SEQRES 17 A 335 LYS LEU LEU HIS GLN VAL VAL GLU GLN LEU GLN LYS VAL
SEQRES 18 A 335 HIS PHE ILE THR ASP THR LEU SER LYS GLY GLU THR LYS
SEQRES 19 A 335 PHE MET GLY VAL CYS GLN LEU PRO SER LYS ASN ASP GLU
SEQRES 20 A 335 LYS GLU TYR PRO HIS ARG ARG ILE ASP ILE ARG LEU ILE
SEQRES 21 A 335 PRO LYS ASP GLN TYR TYR CYS GLY VAL LEU TYR PHE THR
SEQRES 22 A 335 GLY SER ASP ILE PHE ASN LYS ASN MET ARG ALA HIS ALA
SEQRES 23 A 335 LEU GLU LYS GLY PHE THR ILE ASN GLU TYR THR ILE ARG
SEQRES 24 A 335 PRO LEU GLY VAL THR GLY VAL ALA GLY GLU PRO LEU PRO
SEQRES 25 A 335 VAL ASP SER GLU LYS ASP ILE PHE ASP TYR ILE GLN TRP
SEQRES 26 A 335 LYS TYR ARG GLU PRO LYS ASP ARG SER GLU
HET 2PN A 401 9
HET MG A 402 1
HET MG A 403 1
HET 8CP A 404 28
HETNAM 2PN IMIDODIPHOSPHORIC ACID
HETNAM MG MAGNESIUM ION
HETNAM 8CP 2'-DEOXY-5'-O-[(R)-HYDROXY{[(R)-
HETNAM 2 8CP HYDROXY(PHOSPHONOAMINO)
HETNAM 3 8CP PHOSPHORYL]OXY}PHOSPHORYL]CYTIDINE
FORMUL 5 2PN H5 N O6 P2
FORMUL 6 MG 2(MG 2+)
FORMUL 8 8CP C9 H17 N4 O12 P3
FORMUL 9 HOH *256(H2 O)
HELIX 1 AA1 ASN A 12 VAL A 29 1 18
HELIX 2 AA2 ALA A 32 TYR A 49 1 18
HELIX 3 AA3 SER A 55 LYS A 61 1 7
HELIX 4 AA4 GLY A 66 GLY A 80 1 15
HELIX 5 AA5 LEU A 82 ASP A 91 1 10
HELIX 6 AA6 ASP A 91 ARG A 102 1 12
HELIX 7 AA7 GLY A 107 GLU A 117 1 11
HELIX 8 AA8 THR A 121 LYS A 127 1 7
HELIX 9 AA9 ASN A 128 LEU A 132 5 5
HELIX 10 AB1 ASN A 133 TYR A 142 1 10
HELIX 11 AB2 TYR A 142 LYS A 148 1 7
HELIX 12 AB3 ARG A 152 ASP A 170 1 19
HELIX 13 AB4 CYS A 178 ARG A 183 1 6
HELIX 14 AB5 LYS A 209 VAL A 221 1 13
HELIX 15 AB6 PRO A 261 ASP A 263 5 3
HELIX 16 AB7 GLN A 264 GLY A 274 1 11
HELIX 17 AB8 SER A 275 LYS A 289 1 15
HELIX 18 AB9 SER A 315 ILE A 323 1 9
HELIX 19 AC1 GLU A 329 ARG A 333 5 5
SHEET 1 AA1 2 ILE A 150 PRO A 151 0
SHEET 2 AA1 2 SER A 187 SER A 188 -1 O SER A 188 N ILE A 150
SHEET 1 AA2 5 ILE A 174 VAL A 177 0
SHEET 2 AA2 5 MET A 191 THR A 196 -1 O LEU A 194 N THR A 176
SHEET 3 AA2 5 ARG A 253 LEU A 259 1 O ASP A 256 N VAL A 193
SHEET 4 AA2 5 LYS A 234 CYS A 239 -1 N CYS A 239 O ARG A 253
SHEET 5 AA2 5 ILE A 224 LYS A 230 -1 N LEU A 228 O MET A 236
SHEET 1 AA3 2 PHE A 291 ILE A 293 0
SHEET 2 AA3 2 ILE A 298 PRO A 300 -1 O ARG A 299 N THR A 292
LINK O3'A DC P 10 MG MG A 403 1555 1555 2.41
LINK O3'B DC P 10 MG MG A 403 1555 1555 2.41
LINK OP1B DC P 11 MG MG A 402 1555 1555 2.19
LINK OP1B DC P 11 MG MG A 403 1555 1555 2.21
LINK OD1 ASP A 190 MG MG A 402 1555 1555 2.03
LINK OD2 ASP A 190 MG MG A 403 1555 1555 1.98
LINK OD2 ASP A 192 MG MG A 402 1555 1555 2.09
LINK OD1 ASP A 192 MG MG A 403 1555 1555 2.07
LINK OD2 ASP A 256 MG MG A 403 1555 1555 2.16
LINK O2 B2PN A 401 MG MG A 402 1555 1555 2.29
LINK O6 B2PN A 401 MG MG A 402 1555 1555 2.18
LINK MG MG A 402 O2AA8CP A 404 1555 1555 2.02
LINK MG MG A 402 O1BA8CP A 404 1555 1555 1.94
LINK MG MG A 402 O3GA8CP A 404 1555 1555 2.13
LINK MG MG A 402 O HOH A 544 1555 1555 2.35
LINK MG MG A 403 O2AA8CP A 404 1555 1555 2.69
CISPEP 1 GLY A 274 SER A 275 0 2.76
SITE 1 AC1 15 ARG A 149 GLY A 179 SER A 180 ARG A 183
SITE 2 AC1 15 SER A 188 GLY A 189 ASP A 190 ASP A 192
SITE 3 AC1 15 MG A 402 8CP A 404 HOH A 544 HOH A 603
SITE 4 AC1 15 HOH A 638 HOH A 662 DC P 11
SITE 1 AC2 7 ASP A 190 ASP A 192 2PN A 401 MG A 403
SITE 2 AC2 7 8CP A 404 HOH A 544 DC P 11
SITE 1 AC3 7 ASP A 190 ASP A 192 ASP A 256 MG A 402
SITE 2 AC3 7 8CP A 404 DC P 10 DC P 11
SITE 1 AC4 24 GLY A 179 SER A 180 ARG A 183 SER A 188
SITE 2 AC4 24 GLY A 189 ASP A 190 ASP A 192 TYR A 271
SITE 3 AC4 24 PHE A 272 THR A 273 GLY A 274 ASP A 276
SITE 4 AC4 24 ASN A 279 2PN A 401 MG A 402 MG A 403
SITE 5 AC4 24 HOH A 544 HOH A 603 HOH A 638 HOH A 662
SITE 6 AC4 24 DC P 10 DC P 11 HOH P 104 DG T 6
CRYST1 50.778 79.922 55.321 90.00 107.67 90.00 P 1 21 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019694 0.000000 0.006274 0.00000
SCALE2 0.000000 0.012512 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018971 0.00000
(ATOM LINES ARE NOT SHOWN.)
END