HEADER TRANSFERASE/DNA 01-AUG-19 6Q02
TITLE POLYMERASE ETA-CATALYZED INSERTION OF THE MISMATCHED A OPPOSITE
TITLE 2 TEMPLATE CYTARABINE (ARAC) RESIDUE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE ETA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RAD30 HOMOLOG A,XERODERMA PIGMENTOSUM VARIANT TYPE PROTEIN;
COMPND 5 EC: 2.7.7.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA PRIMER STRAND;
COMPND 10 CHAIN: P;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA TEMPLATE CONTAINING A CYTARABIN (ARAC) RESIDUE;
COMPND 14 CHAIN: T;
COMPND 15 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: POLH, RAD30, RAD30A, XPV;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET28B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 13 ORGANISM_TAXID: 32630;
SOURCE 14 MOL_ID: 3;
SOURCE 15 SYNTHETIC: YES;
SOURCE 16 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 17 ORGANISM_TAXID: 32630
KEYWDS LESION BYPASS, DNA DAMAGE, DNA REPLICATION, CHEMOTHERAPY,
KEYWDS 2 TRANSFERASE, TRANSFERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR O.RECHKOBLIT,A.K.AGGARWAL
REVDAT 3 11-OCT-23 6Q02 1 LINK
REVDAT 2 04-DEC-19 6Q02 1 REMARK
REVDAT 1 20-NOV-19 6Q02 0
JRNL AUTH O.RECHKOBLIT,R.E.JOHNSON,A.BUKU,L.PRAKASH,S.PRAKASH,
JRNL AUTH 2 A.K.AGGARWAL
JRNL TITL STRUCTURAL INSIGHTS INTO MUTAGENICITY OF ANTICANCER
JRNL TITL 2 NUCLEOSIDE ANALOG CYTARABINE DURING REPLICATION BY DNA
JRNL TITL 3 POLYMERASE ETA.
JRNL REF SCI REP V. 9 16400 2019
JRNL REFN ESSN 2045-2322
JRNL PMID 31704958
JRNL DOI 10.1038/S41598-019-52703-7
REMARK 2
REMARK 2 RESOLUTION. 2.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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) : 2.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 85.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 27041
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850
REMARK 3 FREE R VALUE TEST SET COUNT : 1312
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 85.7200 - 4.3477 1.00 2959 102 0.1715 0.2060
REMARK 3 2 4.3477 - 3.4509 1.00 2879 137 0.1578 0.2276
REMARK 3 3 3.4509 - 3.0146 1.00 2838 155 0.1874 0.2274
REMARK 3 4 3.0146 - 2.7390 1.00 2868 140 0.2111 0.2635
REMARK 3 5 2.7390 - 2.5426 1.00 2814 184 0.2254 0.2471
REMARK 3 6 2.5426 - 2.3927 1.00 2852 140 0.2259 0.2499
REMARK 3 7 2.3927 - 2.2729 1.00 2852 147 0.2318 0.2889
REMARK 3 8 2.2729 - 2.1739 1.00 2846 122 0.2592 0.2599
REMARK 3 9 2.1739 - 2.0902 1.00 2821 185 0.2958 0.3303
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.530
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.26
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 : 0.010 3924
REMARK 3 ANGLE : 0.636 5388
REMARK 3 CHIRALITY : 0.040 603
REMARK 3 PLANARITY : 0.003 630
REMARK 3 DIHEDRAL : 21.374 2304
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 6Q02 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-19.
REMARK 100 THE DEPOSITION ID IS D_1000243331.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-17
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 : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97919
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27083
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090
REMARK 200 RESOLUTION RANGE LOW (A) : 85.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.13300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
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) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 1.77500
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: 6D0Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES BUFFER, PEG1500, PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 27.26367
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 54.52733
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.89550
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 68.15917
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 13.63183
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: 5230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P, T
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 -2
REMARK 465 THR A 156
REMARK 465 ALA A 157
REMARK 465 GLU A 158
REMARK 465 GLU A 159
REMARK 465 DC T 1
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 MET A 1 CB CG SD CE
REMARK 470 VAL A 108 CG1 CG2
REMARK 470 GLN A 126 CD OE1 NE2
REMARK 470 GLU A 127 CG CD OE1 OE2
REMARK 470 GLN A 130 CG CD OE1 NE2
REMARK 470 LYS A 131 CB CG CD CE NZ
REMARK 470 LEU A 132 CG CD1 CD2
REMARK 470 GLN A 133 CG CD OE1 NE2
REMARK 470 GLN A 135 CG CD OE1 NE2
REMARK 470 THR A 155 OG1 CG2
REMARK 470 THR A 160 OG1 CG2
REMARK 470 GLN A 162 CG CD OE1 NE2
REMARK 470 ASP A 181 CG OD1 OD2
REMARK 470 LYS A 293 CG CD CE NZ
REMARK 470 LYS A 328 CB CG CD CE NZ
REMARK 470 ARG A 334 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 376 CG CD CE NZ
REMARK 470 MET A 406 CE
REMARK 470 GLN A 412 CG CD OE1 NE2
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 HH12 ARG A 84 OE1 GLU A 350 1.52
REMARK 500 NH1 ARG A 84 OE1 GLU A 350 2.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O LEU A 75 HG SER A 288 6545 1.55
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 DG P 7 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DA T 7 O4' - C1' - N9 ANGL. DEV. = 1.9 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 16 71.38 22.65
REMARK 500 TYR A 39 178.40 64.88
REMARK 500 LYS A 40 -11.03 -148.28
REMARK 500 SER A 62 -4.45 82.19
REMARK 500 ARG A 111 107.82 -59.14
REMARK 500 SER A 217 -156.93 -158.48
REMARK 500 ASN A 230 51.82 -142.35
REMARK 500 SER A 257 -8.44 89.61
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 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 13 OD1
REMARK 620 2 MET A 14 O 72.0
REMARK 620 3 ASP A 115 OD2 93.9 84.6
REMARK 620 4 DZ4 A 503 O1A 114.9 173.0 95.1
REMARK 620 5 DZ4 A 503 O1B 157.3 88.2 95.2 84.9
REMARK 620 6 DZ4 A 503 O1G 92.2 89.7 170.0 89.5 76.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 13 OD2
REMARK 620 2 ASP A 115 OD1 125.9
REMARK 620 3 GLU A 116 OE2 102.4 97.5
REMARK 620 4 DZ4 A 503 O1A 92.1 97.0 147.5
REMARK 620 5 HOH A 601 O 62.4 157.7 100.5 60.9
REMARK 620 6 DT P 8 O3' 157.6 76.4 68.6 87.0 98.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DZ4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6PZ3 RELATED DB: PDB
REMARK 900 STRUCTURE POL ETA INSERTING CORRECT C OPPOSITE THE TEMPLATE ARAC
REMARK 900 RESIDUE
DBREF 6Q02 A 1 432 UNP Q9Y253 POLH_HUMAN 1 432
DBREF 6Q02 P 1 8 PDB 6Q02 6Q02 1 8
DBREF 6Q02 T 1 12 PDB 6Q02 6Q02 1 12
SEQADV 6Q02 GLY A -2 UNP Q9Y253 EXPRESSION TAG
SEQADV 6Q02 PRO A -1 UNP Q9Y253 EXPRESSION TAG
SEQADV 6Q02 HIS A 0 UNP Q9Y253 EXPRESSION TAG
SEQADV 6Q02 MET A 406 UNP Q9Y253 CYS 406 ENGINEERED MUTATION
SEQRES 1 A 435 GLY PRO HIS MET ALA THR GLY GLN ASP ARG VAL VAL ALA
SEQRES 2 A 435 LEU VAL ASP MET ASP CYS PHE PHE VAL GLN VAL GLU GLN
SEQRES 3 A 435 ARG GLN ASN PRO HIS LEU ARG ASN LYS PRO CYS ALA VAL
SEQRES 4 A 435 VAL GLN TYR LYS SER TRP LYS GLY GLY GLY ILE ILE ALA
SEQRES 5 A 435 VAL SER TYR GLU ALA ARG ALA PHE GLY VAL THR ARG SER
SEQRES 6 A 435 MET TRP ALA ASP ASP ALA LYS LYS LEU CYS PRO ASP LEU
SEQRES 7 A 435 LEU LEU ALA GLN VAL ARG GLU SER ARG GLY LYS ALA ASN
SEQRES 8 A 435 LEU THR LYS TYR ARG GLU ALA SER VAL GLU VAL MET GLU
SEQRES 9 A 435 ILE MET SER ARG PHE ALA VAL ILE GLU ARG ALA SER ILE
SEQRES 10 A 435 ASP GLU ALA TYR VAL ASP LEU THR SER ALA VAL GLN GLU
SEQRES 11 A 435 ARG LEU GLN LYS LEU GLN GLY GLN PRO ILE SER ALA ASP
SEQRES 12 A 435 LEU LEU PRO SER THR TYR ILE GLU GLY LEU PRO GLN GLY
SEQRES 13 A 435 PRO THR THR ALA GLU GLU THR VAL GLN LYS GLU GLY MET
SEQRES 14 A 435 ARG LYS GLN GLY LEU PHE GLN TRP LEU ASP SER LEU GLN
SEQRES 15 A 435 ILE ASP ASN LEU THR SER PRO ASP LEU GLN LEU THR VAL
SEQRES 16 A 435 GLY ALA VAL ILE VAL GLU GLU MET ARG ALA ALA ILE GLU
SEQRES 17 A 435 ARG GLU THR GLY PHE GLN CYS SER ALA GLY ILE SER HIS
SEQRES 18 A 435 ASN LYS VAL LEU ALA LYS LEU ALA CYS GLY LEU ASN LYS
SEQRES 19 A 435 PRO ASN ARG GLN THR LEU VAL SER HIS GLY SER VAL PRO
SEQRES 20 A 435 GLN LEU PHE SER GLN MET PRO ILE ARG LYS ILE ARG SER
SEQRES 21 A 435 LEU GLY GLY LYS LEU GLY ALA SER VAL ILE GLU ILE LEU
SEQRES 22 A 435 GLY ILE GLU TYR MET GLY GLU LEU THR GLN PHE THR GLU
SEQRES 23 A 435 SER GLN LEU GLN SER HIS PHE GLY GLU LYS ASN GLY SER
SEQRES 24 A 435 TRP LEU TYR ALA MET CYS ARG GLY ILE GLU HIS ASP PRO
SEQRES 25 A 435 VAL LYS PRO ARG GLN LEU PRO LYS THR ILE GLY CYS SER
SEQRES 26 A 435 LYS ASN PHE PRO GLY LYS THR ALA LEU ALA THR ARG GLU
SEQRES 27 A 435 GLN VAL GLN TRP TRP LEU LEU GLN LEU ALA GLN GLU LEU
SEQRES 28 A 435 GLU GLU ARG LEU THR LYS ASP ARG ASN ASP ASN ASP ARG
SEQRES 29 A 435 VAL ALA THR GLN LEU VAL VAL SER ILE ARG VAL GLN GLY
SEQRES 30 A 435 ASP LYS ARG LEU SER SER LEU ARG ARG CYS CYS ALA LEU
SEQRES 31 A 435 THR ARG TYR ASP ALA HIS LYS MET SER HIS ASP ALA PHE
SEQRES 32 A 435 THR VAL ILE LYS ASN MET ASN THR SER GLY ILE GLN THR
SEQRES 33 A 435 GLU TRP SER PRO PRO LEU THR MET LEU PHE LEU CYS ALA
SEQRES 34 A 435 THR LYS PHE SER ALA SER
SEQRES 1 P 8 DT DG DC DA DC DT DG DT
SEQRES 1 T 12 DC DA DT CAR DA DC DA DG DT DG DC DG
HET CAR T 4 31
HET MG A 501 1
HET MG A 502 1
HET DZ4 A 503 44
HET GOL A 504 14
HET GOL A 505 14
HETNAM CAR CYTOSINE ARABINOSE-5'-PHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM DZ4 2'-DEOXY-5'-O-[(R)-HYDROXY{[(R)-HYDROXY(PHOSPHONOOXY)
HETNAM 2 DZ4 PHOSPHORYL]AMINO}PHOSPHORYL]ADENOSINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 CAR C9 H14 N3 O8 P
FORMUL 4 MG 2(MG 2+)
FORMUL 6 DZ4 C10 H17 N6 O11 P3
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 9 HOH *208(H2 O)
HELIX 1 AA1 CYS A 16 ASN A 26 1 11
HELIX 2 AA2 PRO A 27 ARG A 30 5 4
HELIX 3 AA3 SER A 51 ALA A 56 1 6
HELIX 4 AA4 TRP A 64 CYS A 72 1 9
HELIX 5 AA5 LEU A 89 SER A 104 1 16
HELIX 6 AA6 LEU A 121 LEU A 132 1 12
HELIX 7 AA7 SER A 138 LEU A 142 5 5
HELIX 8 AA8 GLN A 162 SER A 177 1 16
HELIX 9 AA9 SER A 185 GLY A 209 1 25
HELIX 10 AB1 ASN A 219 GLY A 228 1 10
HELIX 11 AB2 LEU A 229 LYS A 231 5 3
HELIX 12 AB3 SER A 239 GLY A 241 5 3
HELIX 13 AB4 SER A 242 GLN A 249 1 8
HELIX 14 AB5 MET A 250 ILE A 255 5 6
HELIX 15 AB6 GLY A 260 GLY A 271 1 12
HELIX 16 AB7 TYR A 274 PHE A 281 5 8
HELIX 17 AB8 THR A 282 GLY A 291 1 10
HELIX 18 AB9 GLY A 291 CYS A 302 1 12
HELIX 19 AC1 PRO A 326 ALA A 330 5 5
HELIX 20 AC2 ARG A 334 ASP A 360 1 27
HELIX 21 AC3 ASP A 391 ASN A 405 1 15
SHEET 1 AA1 6 ILE A 109 SER A 113 0
SHEET 2 AA1 6 GLU A 116 ASP A 120 -1 O TYR A 118 N GLU A 110
SHEET 3 AA1 6 VAL A 9 MET A 14 -1 N ALA A 10 O VAL A 119
SHEET 4 AA1 6 CYS A 212 SER A 217 -1 O SER A 217 N VAL A 9
SHEET 5 AA1 6 GLN A 235 LEU A 237 1 O THR A 236 N ILE A 216
SHEET 6 AA1 6 THR A 145 ILE A 147 1 N TYR A 146 O LEU A 237
SHEET 1 AA2 3 GLY A 46 VAL A 50 0
SHEET 2 AA2 3 CYS A 34 GLN A 38 -1 N GLN A 38 O GLY A 46
SHEET 3 AA2 3 LEU A 76 GLN A 79 1 O ALA A 78 N VAL A 37
SHEET 1 AA3 2 GLU A 82 SER A 83 0
SHEET 2 AA3 2 LYS A 86 ALA A 87 -1 O LYS A 86 N SER A 83
SHEET 1 AA4 3 ILE A 319 ASN A 324 0
SHEET 2 AA4 3 GLU A 414 ALA A 431 -1 O LEU A 424 N CYS A 321
SHEET 3 AA4 3 LEU A 331 THR A 333 -1 N LEU A 331 O LEU A 419
SHEET 1 AA5 4 ILE A 319 ASN A 324 0
SHEET 2 AA5 4 GLU A 414 ALA A 431 -1 O LEU A 424 N CYS A 321
SHEET 3 AA5 4 ARG A 361 VAL A 372 -1 N VAL A 367 O CYS A 425
SHEET 4 AA5 4 LEU A 381 ALA A 386 -1 O ARG A 383 N VAL A 368
LINK O3' DT T 3 P CAR T 4 1555 1555 1.61
LINK O3' CAR T 4 P DA T 5 1555 1555 1.60
LINK OD1 ASP A 13 MG MG A 501 1555 1555 2.01
LINK OD2 ASP A 13 MG MG A 502 1555 1555 2.19
LINK O MET A 14 MG MG A 501 1555 1555 2.32
LINK OD2 ASP A 115 MG MG A 501 1555 1555 2.07
LINK OD1 ASP A 115 MG MG A 502 1555 1555 2.12
LINK OE2 GLU A 116 MG MG A 502 1555 1555 2.12
LINK MG MG A 501 O1A DZ4 A 503 1555 1555 2.17
LINK MG MG A 501 O1B DZ4 A 503 1555 1555 2.02
LINK MG MG A 501 O1G DZ4 A 503 1555 1555 2.05
LINK MG MG A 502 O1A DZ4 A 503 1555 1555 2.44
LINK MG MG A 502 O HOH A 601 1555 1555 2.13
LINK MG MG A 502 O3' DT P 8 1555 1555 2.44
CISPEP 1 LEU A 150 PRO A 151 0 0.73
CISPEP 2 LYS A 231 PRO A 232 0 -0.60
CISPEP 3 SER A 416 PRO A 417 0 -3.59
SITE 1 AC1 5 ASP A 13 MET A 14 ASP A 115 MG A 502
SITE 2 AC1 5 DZ4 A 503
SITE 1 AC2 7 ASP A 13 ASP A 115 GLU A 116 MG A 501
SITE 2 AC2 7 DZ4 A 503 HOH A 601 DT P 8
SITE 1 AC3 22 ASP A 13 MET A 14 ASP A 15 CYS A 16
SITE 2 AC3 22 PHE A 17 PHE A 18 ILE A 48 ALA A 49
SITE 3 AC3 22 TYR A 52 ARG A 55 ARG A 61 ASP A 115
SITE 4 AC3 22 LYS A 231 MG A 501 MG A 502 HOH A 601
SITE 5 AC3 22 HOH A 613 HOH A 679 HOH A 737 DT P 8
SITE 6 AC3 22 CAR T 4 DA T 5
SITE 1 AC4 9 ARG A 24 PRO A 244 PHE A 247 SER A 248
SITE 2 AC4 9 GLY A 276 GLU A 277 HOH A 629 HOH A 635
SITE 3 AC4 9 HOH A 665
SITE 1 AC5 7 ASN A 26 PRO A 27 GLY A 271 ILE A 272
SITE 2 AC5 7 GLU A 273 TYR A 274 GLU A 277
CRYST1 98.974 98.974 81.791 90.00 90.00 120.00 P 61 6
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 0.010104 0.005833 0.000000 0.00000
SCALE2 0.000000 0.011667 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012226 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
