HEADER TRANSFERASE/DNA/RNA 03-JUL-13 4BWM
TITLE KLENTAQ MUTANT IN COMPLEX WITH A RNA/DNA HYBRID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE I, THERMOSTABLE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KLENOW FRAGMENT, RESIDUES 293-832;
COMPND 5 SYNONYM: TAQ POLYMERASE 1;
COMPND 6 EC: 2.7.7.7;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: 5'-D(*GP*AP*CP*CP*AP*CP*GP*GP*CP*GP*CP*DOCP)-3';
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: PRIMER;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: 5'-R(*AP*AP*AP*GP*GP*GP*CP*GP*CP*CP*GP*UP*GP*GP*UP*C)-3';
COMPND 16 CHAIN: G;
COMPND 17 SYNONYM: TEMPLATE;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS AQUATICUS;
SOURCE 3 ORGANISM_TAXID: 271;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGDR11;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 12 ORGANISM_TAXID: 32630;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 16 ORGANISM_TAXID: 32630
KEYWDS TRANSFERASE-DNA-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.BLATTER,K.BERGEN,W.WELTE,K.DIEDERICHS,A.MARX
REVDAT 5 20-DEC-23 4BWM 1 REMARK LINK
REVDAT 4 08-MAY-19 4BWM 1 REMARK LINK
REVDAT 3 23-SEP-15 4BWM 1 SOURCE JRNL REMARK
REVDAT 2 25-DEC-13 4BWM 1 JRNL
REVDAT 1 18-SEP-13 4BWM 0
JRNL AUTH N.BLATTER,K.BERGEN,O.NOLTE,W.WELTE,K.DIEDERICHS,J.MAYER,
JRNL AUTH 2 M.WIELAND,A.MARX
JRNL TITL STRUCTURE AND FUNCTION OF AN RNA-READING THERMOSTABLE DNA
JRNL TITL 2 POLYMERASE.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 52 11935 2013
JRNL REFN ISSN 1433-7851
JRNL PMID 24106012
JRNL DOI 10.1002/ANIE.201306655
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.BLATTER,K.BERGEN,O.NOLTE,W.WELTE,K.DIEDERICHS,J.MAYER,
REMARK 1 AUTH 2 M.WIELAND,A.MARX
REMARK 1 TITL STRUKTUR UND FUNKTION EINER RNA-LESENDEN THERMOSTABILEN
REMARK 1 TITL 2 DNA-POLYMERASE
REMARK 1 REF ANGEW.CHEM. V. 125 12154 2013
REMARK 1 REFN ISSN 1433-7851
REMARK 1 DOI 10.1002/ANGE.201306655
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1411)
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 79632
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3989
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 48.0030 - 5.3081 1.00 2931 152 0.1625 0.2148
REMARK 3 2 5.3081 - 4.2140 1.00 2791 146 0.1368 0.1616
REMARK 3 3 4.2140 - 3.6815 1.00 2758 153 0.1336 0.1700
REMARK 3 4 3.6815 - 3.3450 1.00 2710 167 0.1495 0.1922
REMARK 3 5 3.3450 - 3.1053 1.00 2764 136 0.1722 0.2255
REMARK 3 6 3.1053 - 2.9223 1.00 2724 140 0.1793 0.2338
REMARK 3 7 2.9223 - 2.7759 1.00 2724 116 0.1794 0.2458
REMARK 3 8 2.7759 - 2.6551 1.00 2704 162 0.1827 0.2191
REMARK 3 9 2.6551 - 2.5529 1.00 2675 152 0.1806 0.2253
REMARK 3 10 2.5529 - 2.4648 1.00 2717 132 0.1743 0.2214
REMARK 3 11 2.4648 - 2.3877 1.00 2683 149 0.1697 0.2382
REMARK 3 12 2.3877 - 2.3195 1.00 2691 147 0.1716 0.1990
REMARK 3 13 2.3195 - 2.2584 1.00 2697 131 0.1717 0.2331
REMARK 3 14 2.2584 - 2.2033 1.00 2702 139 0.1617 0.1902
REMARK 3 15 2.2033 - 2.1532 1.00 2687 145 0.1629 0.1953
REMARK 3 16 2.1532 - 2.1074 1.00 2676 137 0.1671 0.2065
REMARK 3 17 2.1074 - 2.0653 1.00 2687 135 0.1777 0.1928
REMARK 3 18 2.0653 - 2.0263 1.00 2684 144 0.1799 0.2120
REMARK 3 19 2.0263 - 1.9901 1.00 2658 162 0.1944 0.2317
REMARK 3 20 1.9901 - 1.9564 1.00 2673 134 0.1944 0.2190
REMARK 3 21 1.9564 - 1.9248 1.00 2674 142 0.1963 0.2465
REMARK 3 22 1.9248 - 1.8952 1.00 2693 144 0.2093 0.2472
REMARK 3 23 1.8952 - 1.8673 1.00 2659 141 0.2153 0.2217
REMARK 3 24 1.8673 - 1.8410 1.00 2645 147 0.2255 0.2323
REMARK 3 25 1.8410 - 1.8161 1.00 2682 137 0.2316 0.2517
REMARK 3 26 1.8161 - 1.7925 1.00 2673 149 0.2429 0.2715
REMARK 3 27 1.7925 - 1.7701 1.00 2701 124 0.2481 0.2563
REMARK 3 28 1.7701 - 1.7488 0.97 2580 126 0.2574 0.2844
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.980
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.55
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 : 0.007 5043
REMARK 3 ANGLE : 1.089 6942
REMARK 3 CHIRALITY : 0.070 767
REMARK 3 PLANARITY : 0.005 819
REMARK 3 DIHEDRAL : 14.698 1992
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 295 THROUGH 433 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1569 19.1825 2.6349
REMARK 3 T TENSOR
REMARK 3 T11: 0.0950 T22: 0.0929
REMARK 3 T33: 0.1910 T12: -0.0075
REMARK 3 T13: -0.0233 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 0.6949 L22: 0.1703
REMARK 3 L33: 0.2182 L12: -0.1149
REMARK 3 L13: 0.2941 L23: 0.0834
REMARK 3 S TENSOR
REMARK 3 S11: -0.1084 S12: -0.0391 S13: 0.2061
REMARK 3 S21: 0.0246 S22: 0.0293 S23: -0.0949
REMARK 3 S31: -0.0345 S32: 0.0033 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 434 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.4906 -10.5362 -11.5175
REMARK 3 T TENSOR
REMARK 3 T11: 0.1672 T22: 0.1011
REMARK 3 T33: 0.0803 T12: -0.0037
REMARK 3 T13: -0.0154 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.0607 L22: 0.0559
REMARK 3 L33: 0.3227 L12: -0.0310
REMARK 3 L13: 0.1173 L23: 0.0857
REMARK 3 S TENSOR
REMARK 3 S11: 0.0375 S12: -0.0265 S13: 0.0176
REMARK 3 S21: -0.0829 S22: -0.0246 S23: -0.0472
REMARK 3 S31: 0.0744 S32: -0.0133 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 604 THROUGH 775 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.2541 7.9901 -11.8373
REMARK 3 T TENSOR
REMARK 3 T11: 0.1234 T22: 0.1315
REMARK 3 T33: 0.1068 T12: 0.0099
REMARK 3 T13: -0.0446 T23: 0.0503
REMARK 3 L TENSOR
REMARK 3 L11: 0.1809 L22: 0.4115
REMARK 3 L33: 0.7827 L12: -0.0230
REMARK 3 L13: 0.2235 L23: -0.4834
REMARK 3 S TENSOR
REMARK 3 S11: 0.0355 S12: -0.0491 S13: 0.0509
REMARK 3 S21: -0.0987 S22: 0.1162 S23: 0.1101
REMARK 3 S31: 0.0867 S32: -0.0837 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 776 THROUGH 832 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.0566 -0.1513 8.8692
REMARK 3 T TENSOR
REMARK 3 T11: 0.0889 T22: 0.1381
REMARK 3 T33: 0.1055 T12: 0.0139
REMARK 3 T13: 0.0069 T23: 0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 0.1520 L22: 0.0803
REMARK 3 L33: 0.1337 L12: -0.0355
REMARK 3 L13: 0.0486 L23: 0.0411
REMARK 3 S TENSOR
REMARK 3 S11: 0.0146 S12: -0.0535 S13: -0.0461
REMARK 3 S21: 0.0474 S22: 0.0283 S23: 0.0881
REMARK 3 S31: 0.0226 S32: -0.0845 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND (RESID 103 THROUGH 111 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.7143 0.9984 -22.9811
REMARK 3 T TENSOR
REMARK 3 T11: 0.2580 T22: 0.1896
REMARK 3 T33: 0.1345 T12: -0.0434
REMARK 3 T13: -0.0018 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: -0.0060 L22: 0.0165
REMARK 3 L33: 0.0698 L12: 0.0170
REMARK 3 L13: 0.0266 L23: 0.0063
REMARK 3 S TENSOR
REMARK 3 S11: 0.0520 S12: 0.0399 S13: 0.4698
REMARK 3 S21: 0.0659 S22: 0.1924 S23: 0.0056
REMARK 3 S31: 0.4443 S32: -0.0375 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN G AND (RESID 1 THROUGH 14 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.6765 2.4380 -23.8398
REMARK 3 T TENSOR
REMARK 3 T11: 0.1179 T22: 0.3239
REMARK 3 T33: 0.1450 T12: -0.0159
REMARK 3 T13: 0.0032 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: -0.0659 L22: -0.0816
REMARK 3 L33: 0.0791 L12: -0.0533
REMARK 3 L13: 0.0036 L23: 0.0407
REMARK 3 S TENSOR
REMARK 3 S11: -0.2869 S12: 0.2763 S13: 0.2177
REMARK 3 S21: 0.1365 S22: 0.1423 S23: -0.0839
REMARK 3 S31: -0.0042 S32: 0.1191 S33: 0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 15 AND 16 OF THE TEMPLATE AND
REMARK 3 1 AND 2 OF THE PRIMER ARE DISORDERED
REMARK 4
REMARK 4 4BWM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1290057573.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000040
REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT SI(111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : DYNAMICALLY BENDABLE MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79729
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 47.340
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.590
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.62
REMARK 200 R MERGE FOR SHELL (I) : 1.12000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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 3RTV
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP. 100MM TRIS PH8.5, 200MM
REMARK 280 MG-FORMATE, 20% PEG 8K MICROSEEDED, VAPOR DIFFUSION, HANGING DROP
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 71.59600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.14100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 71.59600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.14100
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: 6740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G
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 ALA A 293
REMARK 465 LEU A 294
REMARK 465 DG B 101
REMARK 465 DA B 102
REMARK 465 U G 15
REMARK 465 C G 16
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 OD1 ASP A 551 O HOH A 2223 2.13
REMARK 500 OD1 ASP A 578 O HOH A 2394 2.14
REMARK 500 O HOH A 2164 O HOH A 2180 2.15
REMARK 500 O HOH A 2413 O HOH A 2419 2.15
REMARK 500 O HOH A 2181 O HOH A 2182 2.18
REMARK 500 O HOH G 2010 O HOH G 2018 2.18
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 B 110 C3' - C2' - C1' ANGL. DEV. = -5.0 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 ASP A 381 116.13 -166.73
REMARK 500 VAL A 433 -66.72 -122.59
REMARK 500 ASP A 496 -62.75 -92.70
REMARK 500 TYR A 545 -56.20 -123.04
REMARK 500 HIS A 784 -123.44 53.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2120 DISTANCE = 5.86 ANGSTROMS
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 A1836 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DCT A1833 O2A
REMARK 620 2 DCT A1833 O1B 89.0
REMARK 620 3 DCT A1833 O1G 95.3 94.2
REMARK 620 4 HOH A2423 O 93.0 177.3 87.5
REMARK 620 5 HOH A2425 O 178.8 90.9 83.5 87.2
REMARK 620 6 HOH A2426 O 96.4 82.8 167.9 95.0 84.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1112 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DC B 111 OP2
REMARK 620 2 HOH B2025 O 98.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1113 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B2001 O
REMARK 620 2 HOH B2002 O 87.5
REMARK 620 3 HOH B2006 O 97.4 92.0
REMARK 620 4 HOH B2027 O 103.2 168.0 81.3
REMARK 620 5 HOH B2028 O 176.6 89.1 82.3 80.1
REMARK 620 6 HOH B2029 O 95.2 92.8 166.7 91.6 85.4
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 DCT A 1833
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1834
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1835
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1836
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1837
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1838
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1839
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1112
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1113
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT G 1015
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BWJ RELATED DB: PDB
REMARK 900 KLENTAQ MUTANT IN COMPLEX WITH DNA AND DDCTP
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-TERMINALLY TRUNCATED, KLENOW FRAGMENT
DBREF 4BWM A 293 832 UNP P19821 DPO1_THEAQ 293 832
DBREF 4BWM B 101 112 PDB 4BWM 4BWM 101 112
DBREF 4BWM G 1 16 PDB 4BWM 4BWM 1 16
SEQADV 4BWM MET A 459 UNP P19821 LEU 459 ENGINEERED MUTATION
SEQADV 4BWM ARG A 515 UNP P19821 SER 515 ENGINEERED MUTATION
SEQADV 4BWM PHE A 638 UNP P19821 ILE 638 ENGINEERED MUTATION
SEQADV 4BWM LYS A 747 UNP P19821 MET 747 ENGINEERED MUTATION
SEQRES 1 A 540 ALA LEU GLU GLU ALA PRO TRP PRO PRO PRO GLU GLY ALA
SEQRES 2 A 540 PHE VAL GLY PHE VAL LEU SER ARG LYS GLU PRO MET TRP
SEQRES 3 A 540 ALA ASP LEU LEU ALA LEU ALA ALA ALA ARG GLY GLY ARG
SEQRES 4 A 540 VAL HIS ARG ALA PRO GLU PRO TYR LYS ALA LEU ARG ASP
SEQRES 5 A 540 LEU LYS GLU ALA ARG GLY LEU LEU ALA LYS ASP LEU SER
SEQRES 6 A 540 VAL LEU ALA LEU ARG GLU GLY LEU GLY LEU PRO PRO GLY
SEQRES 7 A 540 ASP ASP PRO MET LEU LEU ALA TYR LEU LEU ASP PRO SER
SEQRES 8 A 540 ASN THR THR PRO GLU GLY VAL ALA ARG ARG TYR GLY GLY
SEQRES 9 A 540 GLU TRP THR GLU GLU ALA GLY GLU ARG ALA ALA LEU SER
SEQRES 10 A 540 GLU ARG LEU PHE ALA ASN LEU TRP GLY ARG LEU GLU GLY
SEQRES 11 A 540 GLU GLU ARG LEU LEU TRP LEU TYR ARG GLU VAL GLU ARG
SEQRES 12 A 540 PRO LEU SER ALA VAL LEU ALA HIS MET GLU ALA THR GLY
SEQRES 13 A 540 VAL ARG LEU ASP VAL ALA TYR LEU ARG ALA MET SER LEU
SEQRES 14 A 540 GLU VAL ALA GLU GLU ILE ALA ARG LEU GLU ALA GLU VAL
SEQRES 15 A 540 PHE ARG LEU ALA GLY HIS PRO PHE ASN LEU ASN SER ARG
SEQRES 16 A 540 ASP GLN LEU GLU ARG VAL LEU PHE ASP GLU LEU GLY LEU
SEQRES 17 A 540 PRO ALA ILE GLY LYS THR GLU LYS THR GLY LYS ARG SER
SEQRES 18 A 540 THR ARG ALA ALA VAL LEU GLU ALA LEU ARG GLU ALA HIS
SEQRES 19 A 540 PRO ILE VAL GLU LYS ILE LEU GLN TYR ARG GLU LEU THR
SEQRES 20 A 540 LYS LEU LYS SER THR TYR ILE ASP PRO LEU PRO ASP LEU
SEQRES 21 A 540 ILE HIS PRO ARG THR GLY ARG LEU HIS THR ARG PHE ASN
SEQRES 22 A 540 GLN THR ALA THR ALA THR GLY ARG LEU SER SER SER ASP
SEQRES 23 A 540 PRO ASN LEU GLN ASN ILE PRO VAL ARG THR PRO LEU GLY
SEQRES 24 A 540 GLN ARG ILE ARG ARG ALA PHE ILE ALA GLU GLU GLY TRP
SEQRES 25 A 540 LEU LEU VAL ALA LEU ASP TYR SER GLN ILE GLU LEU ARG
SEQRES 26 A 540 VAL LEU ALA HIS LEU SER GLY ASP GLU ASN LEU ILE ARG
SEQRES 27 A 540 VAL PHE GLN GLU GLY ARG ASP PHE HIS THR GLU THR ALA
SEQRES 28 A 540 SER TRP MET PHE GLY VAL PRO ARG GLU ALA VAL ASP PRO
SEQRES 29 A 540 LEU MET ARG ARG ALA ALA LYS THR ILE ASN PHE GLY VAL
SEQRES 30 A 540 LEU TYR GLY MET SER ALA HIS ARG LEU SER GLN GLU LEU
SEQRES 31 A 540 ALA ILE PRO TYR GLU GLU ALA GLN ALA PHE ILE GLU ARG
SEQRES 32 A 540 TYR PHE GLN SER PHE PRO LYS VAL ARG ALA TRP ILE GLU
SEQRES 33 A 540 LYS THR LEU GLU GLU GLY ARG ARG ARG GLY TYR VAL GLU
SEQRES 34 A 540 THR LEU PHE GLY ARG ARG ARG TYR VAL PRO ASP LEU GLU
SEQRES 35 A 540 ALA ARG VAL LYS SER VAL ARG GLU ALA ALA GLU ARG LYS
SEQRES 36 A 540 ALA PHE ASN MET PRO VAL GLN GLY THR ALA ALA ASP LEU
SEQRES 37 A 540 MET LYS LEU ALA MET VAL LYS LEU PHE PRO ARG LEU GLU
SEQRES 38 A 540 GLU MET GLY ALA ARG MET LEU LEU GLN VAL HIS ASP GLU
SEQRES 39 A 540 LEU VAL LEU GLU ALA PRO LYS GLU ARG ALA GLU ALA VAL
SEQRES 40 A 540 ALA ARG LEU ALA LYS GLU VAL MET GLU GLY VAL TYR PRO
SEQRES 41 A 540 LEU ALA VAL PRO LEU GLU VAL GLU VAL GLY ILE GLY GLU
SEQRES 42 A 540 ASP TRP LEU SER ALA LYS GLU
SEQRES 1 B 12 DG DA DC DC DA DC DG DG DC DG DC DOC
SEQRES 1 G 16 A A A G G G C G C C G U G
SEQRES 2 G 16 G U C
MODRES 4BWM DOC B 112 DC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
HET DOC B 112 18
HET DCT A1833 27
HET CL A1834 1
HET CL A1835 1
HET MG A1836 1
HET FMT A1837 3
HET FMT A1838 3
HET FMT A1839 3
HET MG B1112 1
HET MG B1113 1
HET FMT G1015 3
HETNAM DOC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
HETNAM DCT 2',3'-DIDEOXYCYTIDINE 5'-TRIPHOSPHATE
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETNAM FMT FORMIC ACID
FORMUL 2 DOC C9 H14 N3 O6 P
FORMUL 4 DCT C9 H16 N3 O12 P3
FORMUL 5 CL 2(CL 1-)
FORMUL 7 MG 3(MG 2+)
FORMUL 8 FMT 4(C H2 O2)
FORMUL 14 HOH *631(H2 O)
HELIX 1 1 GLU A 315 ALA A 319 5 5
HELIX 2 2 GLU A 337 ARG A 343 1 7
HELIX 3 3 LEU A 352 GLU A 363 1 12
HELIX 4 4 ASP A 372 ASP A 381 1 10
HELIX 5 5 THR A 386 GLY A 395 1 10
HELIX 6 6 GLU A 401 LEU A 420 1 20
HELIX 7 7 GLU A 423 VAL A 433 1 11
HELIX 8 8 VAL A 433 GLY A 448 1 16
HELIX 9 9 ASP A 452 GLY A 479 1 28
HELIX 10 10 SER A 486 ASP A 496 1 11
HELIX 11 11 ARG A 515 LEU A 522 1 8
HELIX 12 12 PRO A 527 TYR A 545 1 19
HELIX 13 13 ASP A 547 LEU A 552 1 6
HELIX 14 14 ASN A 580 ILE A 584 5 5
HELIX 15 15 THR A 588 ALA A 597 1 10
HELIX 16 16 GLN A 613 GLY A 624 1 12
HELIX 17 17 ASP A 625 GLU A 634 1 10
HELIX 18 18 ASP A 637 GLY A 648 1 12
HELIX 19 19 PRO A 650 VAL A 654 5 5
HELIX 20 20 ASP A 655 TYR A 671 1 17
HELIX 21 21 SER A 674 LEU A 682 1 9
HELIX 22 22 PRO A 685 PHE A 700 1 16
HELIX 23 23 PHE A 700 GLY A 718 1 19
HELIX 24 24 PRO A 731 ALA A 735 5 5
HELIX 25 25 VAL A 737 MET A 775 1 39
HELIX 26 26 ARG A 795 GLY A 809 1 15
HELIX 27 27 ASP A 826 GLU A 832 1 7
SHEET 1 AA 4 GLU A 296 ALA A 297 0
SHEET 2 AA 4 ARG A 331 ARG A 334 1 O VAL A 332 N ALA A 297
SHEET 3 AA 4 LEU A 321 ARG A 328 -1 O ALA A 326 N HIS A 333
SHEET 4 AA 4 PHE A 306 LEU A 311 -1 O PHE A 306 N ALA A 327
SHEET 1 AB 2 ARG A 450 LEU A 451 0
SHEET 2 AB 2 PHE A 598 ILE A 599 -1 O ILE A 599 N ARG A 450
SHEET 1 AC 2 ILE A 553 HIS A 554 0
SHEET 2 AC 2 ARG A 559 LEU A 560 -1 O ARG A 559 N HIS A 554
SHEET 1 AD 2 ARG A 563 ASN A 565 0
SHEET 2 AD 2 SER A 575 SER A 577 -1 O SER A 575 N ASN A 565
SHEET 1 AE 4 ARG A 778 VAL A 783 0
SHEET 2 AE 4 GLU A 786 PRO A 792 -1 O GLU A 786 N VAL A 783
SHEET 3 AE 4 TRP A 604 TYR A 611 -1 O LEU A 605 N ALA A 791
SHEET 4 AE 4 VAL A 819 GLY A 824 -1 O GLU A 820 N ASP A 610
SHEET 1 AF 2 TYR A 719 GLU A 721 0
SHEET 2 AF 2 ARG A 727 TYR A 729 -1 O ARG A 728 N VAL A 720
LINK O3' DC B 111 P DOC B 112 1555 1555 1.58
LINK O2A DCT A1833 MG MG A1836 1555 1555 1.98
LINK O1B DCT A1833 MG MG A1836 1555 1555 2.09
LINK O1G DCT A1833 MG MG A1836 1555 1555 1.93
LINK MG MG A1836 O HOH A2423 1555 1555 2.11
LINK MG MG A1836 O HOH A2425 1555 1555 2.07
LINK MG MG A1836 O HOH A2426 1555 1555 1.94
LINK OP2 DC B 111 MG MG B1112 1555 1555 2.22
LINK MG MG B1112 O HOH B2025 1555 1555 2.93
LINK MG MG B1113 O HOH B2001 1555 1555 2.10
LINK MG MG B1113 O HOH B2002 1555 1555 2.26
LINK MG MG B1113 O HOH B2006 1555 1555 2.17
LINK MG MG B1113 O HOH B2027 1555 1555 2.16
LINK MG MG B1113 O HOH B2028 1555 1555 2.40
LINK MG MG B1113 O HOH B2029 1555 1555 2.16
CISPEP 1 TRP A 299 PRO A 300 0 1.10
CISPEP 2 ASP A 578 PRO A 579 0 5.10
SITE 1 AC1 20 GLN A 613 HIS A 639 ARG A 659 LYS A 663
SITE 2 AC1 20 PHE A 667 ASP A 785 MG A1836 HOH A2381
SITE 3 AC1 20 HOH A2423 HOH A2425 HOH A2426 HOH A2429
SITE 4 AC1 20 HOH A2430 HOH A2433 HOH A2546 HOH A2581
SITE 5 AC1 20 HOH A2582 DOC B 112 G G 4 G G 5
SITE 1 AC2 1 ARG A 559
SITE 1 AC3 3 VAL A 730 PRO A 731 ASP A 732
SITE 1 AC4 4 DCT A1833 HOH A2423 HOH A2425 HOH A2426
SITE 1 AC5 5 GLU A 424 LEU A 427 ARG A 431 HOH A2452
SITE 2 AC5 5 HOH A2453
SITE 1 AC6 3 ASP A 371 ARG A 435 HOH A2161
SITE 1 AC7 4 TYR A 545 ASN A 583 HOH A2396 HOH A2398
SITE 1 AC8 3 DG B 110 DC B 111 HOH B2025
SITE 1 AC9 6 HOH B2001 HOH B2002 HOH B2006 HOH B2027
SITE 2 AC9 6 HOH B2028 HOH B2029
SITE 1 BC1 5 GLN A 582 HOH A2380 HOH A2386 G G 6
SITE 2 BC1 5 C G 7
CRYST1 143.192 86.282 63.094 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 0.006984 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011590 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015849 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
