HEADER HYDROLASE/DNA 28-FEB-13 4JGC
TITLE HUMAN TDG N140A MUTANT IN A COMPLEX WITH 5-CARBOXYLCYTOSINE (5CAC)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: G/T MISMATCH-SPECIFIC THYMINE DNA GLYCOSYLASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 111-308;
COMPND 5 SYNONYM: THYMINE-DNA GLYCOSYLASE;
COMPND 6 EC: 3.2.2.29;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: OLIGONUCLEOTIDE;
COMPND 11 CHAIN: C;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: OLIGONUCLEOTIDE CONTAINING 5-CARBOXYLCYTOSINE;
COMPND 15 CHAIN: D;
COMPND 16 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: TDG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PXC1057;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: DNA SYNTHESIS;
SOURCE 12 MOL_ID: 3;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 OTHER_DETAILS: DNA SYNTHESIS
KEYWDS 5-CARBOXYLCYTOSINE; THYMINE DNA GLYCOSYLASE; DNA MODIFICATION; DNA
KEYWDS 2 5MC OXIDATION; EPIGENETIC REGULATION, DNA DEMETHYLATION, 5-
KEYWDS 3 CARBOXYLCYTOSINE, HYDROLASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.HASHIMOTO,X.ZHANG,X.CHENG
REVDAT 3 20-SEP-23 4JGC 1 REMARK SEQADV LINK
REVDAT 2 03-JUL-13 4JGC 1 JRNL
REVDAT 1 29-MAY-13 4JGC 0
JRNL AUTH H.HASHIMOTO,X.ZHANG,X.CHENG
JRNL TITL ACTIVITY AND CRYSTAL STRUCTURE OF HUMAN THYMINE DNA
JRNL TITL 2 GLYCOSYLASE MUTANT N140A WITH 5-CARBOXYLCYTOSINE DNA AT LOW
JRNL TITL 3 PH.
JRNL REF DNA REPAIR V. 12 535 2013
JRNL REFN ISSN 1568-7864
JRNL PMID 23680598
JRNL DOI 10.1016/J.DNAREP.2013.04.003
REMARK 2
REMARK 2 RESOLUTION. 2.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 2.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 11567
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 578
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 45.5691 - 4.0986 1.00 3030 161 0.1939 0.2354
REMARK 3 2 4.0986 - 3.2535 0.99 2974 156 0.2277 0.2911
REMARK 3 3 3.2535 - 2.8423 0.92 2753 139 0.2794 0.3647
REMARK 3 4 2.8423 - 2.5824 0.76 2232 122 0.3834 0.3985
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 : 0.32
REMARK 3 B_SOL : 38.34
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.620
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) : 31.10960
REMARK 3 B22 (A**2) : -10.65790
REMARK 3 B33 (A**2) : -20.45170
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -3.79970
REMARK 3 B23 (A**2) : 0.00000
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 : 0.019 2853
REMARK 3 ANGLE : 1.196 4097
REMARK 3 CHIRALITY : 0.050 451
REMARK 3 PLANARITY : 0.007 331
REMARK 3 DIHEDRAL : 22.916 1131
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 4JGC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000078010.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : ROSENBAUM-ROCK MONOCHROMATO HIGH
REMARK 200 -RESOLUTION DOUBLE-CRYSTAL
REMARK 200 SI(220) SAGITTAL FOCUSING,
REMARK 200 ROSENBAUM-ROCK VERTICAL FOCUSING
REMARK 200 MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11604
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.582
REMARK 200 RESOLUTION RANGE LOW (A) : 45.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.36500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 4FNC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% POLYETHYLENE GLYCOL (PEG) 4000,
REMARK 280 0.2 M AMMONIUM ACETATE, 0.1 M SODIUM ACETATE, PH 4.6, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 45.74300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.77750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.74300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.77750
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: 5000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 5-CARBOXY-2'-DEOXYCYTIDINE MONOPHOSPHATE IN THE DNA GOT CLEAVED
REMARK 400 INTO 5-CARBOXYLCYTOSINE BASE AND 2-DEOXY-5-PHOSPHONO-RIBOSE
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 105
REMARK 465 SER A 106
REMARK 465 HIS A 107
REMARK 465 MET A 108
REMARK 465 ALA A 109
REMARK 465 MET A 306
REMARK 465 ASP A 307
REMARK 465 VAL A 308
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 GLU A 116 CG CD OE1 OE2
REMARK 470 GLU A 118 CG CD OE1 OE2
REMARK 470 LYS A 161 CG CD CE NZ
REMARK 470 LYS A 201 CG CD CE NZ
REMARK 470 LYS A 206 CG CD CE NZ
REMARK 470 ILE A 302 CG1 CG2 CD1
REMARK 470 GLU A 303 CG CD OE1 OE2
REMARK 470 ARG A 304 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 305 CG OD1 ND2
REMARK 470 DC C 1 O5'
REMARK 470 DA D 1 O5'
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 GLY A 156 C GLY A 156 O -0.178
REMARK 500 ASN A 157 N ASN A 157 CA -0.193
REMARK 500 ASN A 157 CG ASN A 157 OD1 -0.158
REMARK 500 ASN A 157 CG ASN A 157 ND2 -0.155
REMARK 500 ARG A 275 CB ARG A 275 CG -0.430
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 A 275 CD - NE - CZ ANGL. DEV. = 10.8 DEGREES
REMARK 500 ARG A 275 NE - CZ - NH1 ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG A 275 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 DG C 3 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DC D 21 O4' - C1' - N1 ANGL. DEV. = 2.0 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 ALA A 140 137.54 -176.26
REMARK 500 GLU A 170 -8.37 65.59
REMARK 500 GLN A 223 72.02 52.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 153 GLY A 154 -137.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1RT D 417
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FNC RELATED DB: PDB
REMARK 900 HUMAN TDG IN A POST-REACTIVE COMPLEX WITH 5-HYDROXYMETHYLURACIL
REMARK 900 (5HMU)
DBREF 4JGC A 111 308 UNP Q13569 TDG_HUMAN 111 308
DBREF 4JGC C 1 28 PDB 4JGC 4JGC 1 28
DBREF 4JGC D 1 28 PDB 4JGC 4JGC 1 28
SEQADV 4JGC GLY A 105 UNP Q13569 EXPRESSION TAG
SEQADV 4JGC SER A 106 UNP Q13569 EXPRESSION TAG
SEQADV 4JGC HIS A 107 UNP Q13569 EXPRESSION TAG
SEQADV 4JGC MET A 108 UNP Q13569 EXPRESSION TAG
SEQADV 4JGC ALA A 109 UNP Q13569 EXPRESSION TAG
SEQADV 4JGC SER A 110 UNP Q13569 EXPRESSION TAG
SEQADV 4JGC ALA A 140 UNP Q13569 ASN 140 ENGINEERED MUTATION
SEQRES 1 A 204 GLY SER HIS MET ALA SER PHE ASN GLY VAL SER GLU ALA
SEQRES 2 A 204 GLU LEU LEU THR LYS THR LEU PRO ASP ILE LEU THR PHE
SEQRES 3 A 204 ASN LEU ASP ILE VAL ILE ILE GLY ILE ALA PRO GLY LEU
SEQRES 4 A 204 MET ALA ALA TYR LYS GLY HIS HIS TYR PRO GLY PRO GLY
SEQRES 5 A 204 ASN HIS PHE TRP LYS CYS LEU PHE MET SER GLY LEU SER
SEQRES 6 A 204 GLU VAL GLN LEU ASN HIS MET ASP ASP HIS THR LEU PRO
SEQRES 7 A 204 GLY LYS TYR GLY ILE GLY PHE THR ASN MET VAL GLU ARG
SEQRES 8 A 204 THR THR PRO GLY SER LYS ASP LEU SER SER LYS GLU PHE
SEQRES 9 A 204 ARG GLU GLY GLY ARG ILE LEU VAL GLN LYS LEU GLN LYS
SEQRES 10 A 204 TYR GLN PRO ARG ILE ALA VAL PHE ASN GLY LYS CYS ILE
SEQRES 11 A 204 TYR GLU ILE PHE SER LYS GLU VAL PHE GLY VAL LYS VAL
SEQRES 12 A 204 LYS ASN LEU GLU PHE GLY LEU GLN PRO HIS LYS ILE PRO
SEQRES 13 A 204 ASP THR GLU THR LEU CYS TYR VAL MET PRO SER SER SER
SEQRES 14 A 204 ALA ARG CYS ALA GLN PHE PRO ARG ALA GLN ASP LYS VAL
SEQRES 15 A 204 HIS TYR TYR ILE LYS LEU LYS ASP LEU ARG ASP GLN LEU
SEQRES 16 A 204 LYS GLY ILE GLU ARG ASN MET ASP VAL
SEQRES 1 C 28 DC DA DG DC DT DC DT DG DT DA DC DG DT
SEQRES 2 C 28 DG DA DG DC DA DG DT DG DG DA DC DA DG
SEQRES 3 C 28 DC DT
SEQRES 1 D 28 DA DG DC DT DG DT DC DC DA DC DT DG DC
SEQRES 2 D 28 DT DC DA ORP DG DT DA DC DA DG DA DG DC
SEQRES 3 D 28 DT DG
HET ORP D 17 12
HET 1RT D 417 11
HETNAM ORP 2-DEOXY-5-PHOSPHONO-RIBOSE
HETNAM 1RT 4-AMINO-2-OXO-1,2-DIHYDROPYRIMIDINE-5-CARBOXYLIC ACID
FORMUL 3 ORP C5 H11 O7 P
FORMUL 4 1RT C5 H5 N3 O3
FORMUL 5 HOH *22(H2 O)
HELIX 1 1 SER A 115 LYS A 122 1 8
HELIX 2 2 GLY A 142 GLY A 149 1 8
HELIX 3 3 HIS A 158 SER A 166 1 9
HELIX 4 4 ASN A 174 HIS A 179 5 6
HELIX 5 5 THR A 180 TYR A 185 1 6
HELIX 6 6 SER A 204 GLN A 223 1 20
HELIX 7 7 LYS A 232 PHE A 243 1 12
HELIX 8 8 ARG A 281 ASN A 305 1 25
SHEET 1 A 5 ILE A 187 ASN A 191 0
SHEET 2 A 5 ILE A 134 GLY A 138 1 N ILE A 134 O GLY A 188
SHEET 3 A 5 ILE A 226 ASN A 230 1 O VAL A 228 N ILE A 137
SHEET 4 A 5 LEU A 265 MET A 269 1 O LEU A 265 N ALA A 227
SHEET 5 A 5 GLY A 253 LEU A 254 -1 N GLY A 253 O VAL A 268
LINK O3' DA D 16 P ORP D 17 1555 1555 1.61
LINK O3 ORP D 17 P DG D 18 1555 1555 1.61
SITE 1 AC1 10 GLY A 138 ILE A 139 ALA A 140 PRO A 141
SITE 2 AC1 10 GLY A 142 TYR A 152 ASN A 191 ASN A 230
SITE 3 AC1 10 SER A 271 ORP D 17
CRYST1 91.486 53.555 81.902 90.00 95.10 90.00 C 1 2 1 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 0.010931 0.000000 0.000976 0.00000
SCALE2 0.000000 0.018672 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012258 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
