HEADER TRANSFERASE, LYASE/DNA 07-MAY-13 4KLM
TITLE DNA POLYMERASE BETA MATCHED PRODUCT COMPLEX WITH MG2+, 11 H
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*CP*CP*GP*AP*CP*GP*GP*CP*GP*CP*AP*TP*CP*AP*GP*C)-3';
COMPND 3 CHAIN: T;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: 5'-D(*GP*CP*TP*GP*AP*TP*GP*CP*GP*CP*C)-3';
COMPND 7 CHAIN: P;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: 5'-D(P*GP*TP*CP*GP*G)-3';
COMPND 11 CHAIN: D;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: DNA POLYMERASE BETA;
COMPND 15 CHAIN: A;
COMPND 16 EC: 2.7.7.7, 4.2.99.-;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 MOL_ID: 4;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: POLB;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: TAP56;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PWL11
KEYWDS DNA POLYMERASE, TRANSFERASE, LYASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.D.FREUDENTHAL,W.A.BEARD,D.D.SHOCK,S.H.WILSON
REVDAT 3 20-SEP-23 4KLM 1 REMARK LINK
REVDAT 2 15-NOV-17 4KLM 1 REMARK
REVDAT 1 17-JUL-13 4KLM 0
JRNL AUTH B.D.FREUDENTHAL,W.A.BEARD,D.D.SHOCK,S.H.WILSON
JRNL TITL OBSERVING A DNA POLYMERASE CHOOSE RIGHT FROM WRONG.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 154 157 2013
JRNL REFN ISSN 0092-8674
JRNL PMID 23827680
JRNL DOI 10.1016/J.CELL.2013.05.048
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7_650
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) : 23.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.5
REMARK 3 NUMBER OF REFLECTIONS : 37565
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.930
REMARK 3 FREE R VALUE TEST SET COUNT : 3729
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 23.8350 - 5.2228 1.00 1454 162 0.1831 0.2157
REMARK 3 2 5.2228 - 4.1526 1.00 1432 160 0.1416 0.1804
REMARK 3 3 4.1526 - 3.6298 0.99 1420 144 0.1508 0.2032
REMARK 3 4 3.6298 - 3.2988 0.99 1431 139 0.1790 0.2311
REMARK 3 5 3.2988 - 3.0629 0.99 1408 164 0.1928 0.2230
REMARK 3 6 3.0629 - 2.8826 0.98 1401 147 0.1967 0.2382
REMARK 3 7 2.8826 - 2.7385 0.97 1355 164 0.2023 0.2579
REMARK 3 8 2.7385 - 2.6194 0.97 1377 148 0.2029 0.2603
REMARK 3 9 2.6194 - 2.5187 0.96 1363 144 0.2086 0.2298
REMARK 3 10 2.5187 - 2.4319 0.96 1360 144 0.1989 0.2551
REMARK 3 11 2.4319 - 2.3559 0.96 1362 165 0.1966 0.2839
REMARK 3 12 2.3559 - 2.2886 0.93 1301 158 0.2189 0.2579
REMARK 3 13 2.2886 - 2.2284 0.96 1362 147 0.2031 0.2562
REMARK 3 14 2.2284 - 2.1741 0.92 1295 150 0.2042 0.3098
REMARK 3 15 2.1741 - 2.1247 0.95 1328 153 0.2108 0.2576
REMARK 3 16 2.1247 - 2.0795 0.95 1338 164 0.2070 0.2469
REMARK 3 17 2.0795 - 2.0379 0.95 1314 144 0.2111 0.3187
REMARK 3 18 2.0379 - 1.9995 0.92 1334 137 0.2020 0.2814
REMARK 3 19 1.9995 - 1.9638 0.90 1284 131 0.2039 0.2463
REMARK 3 20 1.9638 - 1.9305 0.86 1205 132 0.2309 0.3050
REMARK 3 21 1.9305 - 1.8994 0.97 1338 148 0.2181 0.2621
REMARK 3 22 1.8994 - 1.8702 0.78 1118 127 0.2373 0.3292
REMARK 3 23 1.8702 - 1.8427 0.77 1061 119 0.2199 0.3181
REMARK 3 24 1.8427 - 1.8168 0.70 1004 101 0.2487 0.3483
REMARK 3 25 1.8168 - 1.7922 0.60 840 93 0.2589 0.2884
REMARK 3 26 1.7922 - 1.7689 0.53 755 90 0.2648 0.3989
REMARK 3 27 1.7689 - 1.7470 0.43 596 54 0.3016 0.3066
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 39.87
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.43370
REMARK 3 B22 (A**2) : -0.53550
REMARK 3 B33 (A**2) : -2.89820
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.05760
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 : 0.009 3477
REMARK 3 ANGLE : 1.099 4838
REMARK 3 CHIRALITY : 0.063 523
REMARK 3 PLANARITY : 0.004 516
REMARK 3 DIHEDRAL : 18.804 1380
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 4KLM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079492.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40346
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.747
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : 0.05300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.5000
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) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.30
REMARK 200 R MERGE FOR SHELL (I) : 0.27700
REMARK 200 R SYM FOR SHELL (I) : 0.27700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.325
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2FMS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM IMIDAZOLE, 350 MM SODIUM
REMARK 280 CHLORIDE, 17% PEG3350, PH 8.0, VAPOR DIFFUSION, 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 39.88000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.0 KCAL/MOL
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 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 DC T 2 O3' DC T 2 C3' -0.040
REMARK 500 DG P 1 O3' DG P 1 C3' -0.036
REMARK 500 DC P 11 N1 DC P 11 C6 -0.039
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 2 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DC T 5 O4' - C1' - N1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 DG T 6 O4' - C1' - N9 ANGL. DEV. = -5.2 DEGREES
REMARK 500 DA T 11 O4' - C1' - N9 ANGL. DEV. = -4.3 DEGREES
REMARK 500 DG P 1 O4' - C1' - C2' ANGL. DEV. = 3.9 DEGREES
REMARK 500 DC P 11 O4' - C1' - N1 ANGL. DEV. = 2.3 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 -151.26 -117.30
REMARK 500 ASP A 246 -9.66 72.65
REMARK 500 ASN A 294 -166.90 -128.28
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 NA A 404 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG P 9 OP1
REMARK 620 2 HOH P 102 O 86.2
REMARK 620 3 THR A 101 O 167.4 82.9
REMARK 620 4 VAL A 103 O 94.2 177.8 96.4
REMARK 620 5 ILE A 106 O 93.2 94.1 93.9 88.1
REMARK 620 6 HOH A 548 O 89.8 88.5 83.6 89.3 176.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DC P 10 O3'
REMARK 620 2 DC P 11 OP1 61.9
REMARK 620 3 ASP A 190 OD2 121.0 85.9
REMARK 620 4 ASP A 190 OD1 126.5 65.5 44.7
REMARK 620 5 ASP A 192 OD1 105.7 85.4 120.3 78.6
REMARK 620 6 ASP A 256 OD2 94.2 155.4 104.0 136.4 107.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 405 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DC P 11 OP1
REMARK 620 2 ASP A 190 OD1 95.2
REMARK 620 3 ASP A 192 OD2 94.3 97.4
REMARK 620 4 PPV A 401 O32 97.1 163.4 92.6
REMARK 620 5 HOH A 501 O 177.6 83.4 87.9 83.8
REMARK 620 6 HOH A 512 O 90.0 82.3 175.7 86.7 87.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DC D 3 OP1
REMARK 620 2 HOH D 103 O 76.3
REMARK 620 3 LYS A 60 O 165.1 90.3
REMARK 620 4 LEU A 62 O 93.6 169.6 100.0
REMARK 620 5 VAL A 65 O 81.7 86.8 91.2 94.3
REMARK 620 6 HOH A 667 O 83.3 96.5 105.0 79.6 163.4
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 PPV A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 407
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KLD RELATED DB: PDB
REMARK 900 RELATED ID: 4KLE RELATED DB: PDB
REMARK 900 RELATED ID: 4KLF RELATED DB: PDB
REMARK 900 RELATED ID: 4KLG RELATED DB: PDB
REMARK 900 RELATED ID: 4KLH RELATED DB: PDB
REMARK 900 RELATED ID: 4KLI RELATED DB: PDB
REMARK 900 RELATED ID: 4KLJ RELATED DB: PDB
REMARK 900 RELATED ID: 4KLL RELATED DB: PDB
REMARK 900 RELATED ID: 4KLO RELATED DB: PDB
REMARK 900 RELATED ID: 4KLP RELATED DB: PDB
REMARK 900 RELATED ID: 4KLQ RELATED DB: PDB
REMARK 900 RELATED ID: 4KLS RELATED DB: PDB
REMARK 900 RELATED ID: 4KLT RELATED DB: PDB
REMARK 900 RELATED ID: 4KLU RELATED DB: PDB
DBREF 4KLM A 1 335 UNP P06746 DPOLB_HUMAN 1 335
DBREF 4KLM T 1 16 PDB 4KLM 4KLM 1 16
DBREF 4KLM P 1 11 PDB 4KLM 4KLM 1 11
DBREF 4KLM D 1 5 PDB 4KLM 4KLM 1 5
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 PPV A 401 9
HET NA A 402 1
HET NA A 403 1
HET NA A 404 1
HET MG A 405 1
HET CL A 406 1
HET CL A 407 1
HETNAM PPV PYROPHOSPHATE
HETNAM NA SODIUM ION
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 5 PPV H4 O7 P2
FORMUL 6 NA 3(NA 1+)
FORMUL 9 MG MG 2+
FORMUL 10 CL 2(CL 1-)
FORMUL 12 HOH *344(H2 O)
HELIX 1 1 ASN A 12 VAL A 29 1 18
HELIX 2 2 ALA A 32 TYR A 49 1 18
HELIX 3 3 SER A 55 LYS A 61 1 7
HELIX 4 4 GLY A 66 GLY A 80 1 15
HELIX 5 5 LEU A 82 ASP A 91 1 10
HELIX 6 6 ASP A 91 THR A 101 1 11
HELIX 7 7 GLY A 107 GLU A 117 1 11
HELIX 8 8 THR A 121 ASN A 128 1 8
HELIX 9 9 GLU A 129 LEU A 132 5 4
HELIX 10 10 ASN A 133 TYR A 142 1 10
HELIX 11 11 TYR A 142 GLU A 147 1 6
HELIX 12 12 ARG A 152 ASP A 170 1 19
HELIX 13 13 GLY A 179 ARG A 182 5 4
HELIX 14 14 LYS A 209 VAL A 221 1 13
HELIX 15 15 PRO A 261 ASP A 263 5 3
HELIX 16 16 GLN A 264 GLY A 274 1 11
HELIX 17 17 SER A 275 LYS A 289 1 15
HELIX 18 18 SER A 315 ILE A 323 1 9
HELIX 19 19 GLU A 329 ARG A 333 5 5
SHEET 1 A 2 ILE A 150 PRO A 151 0
SHEET 2 A 2 SER A 187 SER A 188 -1 O SER A 188 N ILE A 150
SHEET 1 B 5 ILE A 174 CYS A 178 0
SHEET 2 B 5 MET A 191 THR A 196 -1 O LEU A 194 N THR A 176
SHEET 3 B 5 ARG A 253 LEU A 259 1 O ARG A 258 N LEU A 195
SHEET 4 B 5 LYS A 234 CYS A 239 -1 N GLY A 237 O ILE A 255
SHEET 5 B 5 ILE A 224 LYS A 230 -1 N LEU A 228 O MET A 236
SHEET 1 C 2 PHE A 291 ILE A 293 0
SHEET 2 C 2 ILE A 298 PRO A 300 -1 O ARG A 299 N THR A 292
LINK OP1 DG P 9 NA NA A 404 1555 1555 2.49
LINK O3' DC P 10 NA NA A 402 1555 1555 2.35
LINK OP1 DC P 11 NA NA A 402 1555 1555 2.45
LINK OP1 DC P 11 MG MG A 405 1555 1555 2.09
LINK O HOH P 102 NA NA A 404 1555 1555 2.49
LINK OP1 DC D 3 NA NA A 403 1555 1555 2.79
LINK O HOH D 103 NA NA A 403 1555 1555 2.71
LINK O LYS A 60 NA NA A 403 1555 1555 2.27
LINK O LEU A 62 NA NA A 403 1555 1555 2.28
LINK O VAL A 65 NA NA A 403 1555 1555 2.55
LINK O THR A 101 NA NA A 404 1555 1555 2.22
LINK O VAL A 103 NA NA A 404 1555 1555 2.48
LINK O ILE A 106 NA NA A 404 1555 1555 2.47
LINK OD2 ASP A 190 NA NA A 402 1555 1555 2.21
LINK OD1 ASP A 190 NA NA A 402 1555 1555 3.10
LINK OD1 ASP A 190 MG MG A 405 1555 1555 2.04
LINK OD1 ASP A 192 NA NA A 402 1555 1555 2.13
LINK OD2 ASP A 192 MG MG A 405 1555 1555 2.04
LINK OD2 ASP A 256 NA NA A 402 1555 1555 2.21
LINK O32 PPV A 401 MG MG A 405 1555 1555 2.05
LINK NA NA A 403 O HOH A 667 1555 1555 2.52
LINK NA NA A 404 O HOH A 548 1555 1555 2.47
LINK MG MG A 405 O HOH A 501 1555 1555 2.12
LINK MG MG A 405 O HOH A 512 1555 1555 2.08
CISPEP 1 GLY A 274 SER A 275 0 3.54
SITE 1 AC1 14 ARG A 149 GLY A 179 SER A 180 ARG A 183
SITE 2 AC1 14 SER A 188 GLY A 189 ASP A 192 MG A 405
SITE 3 AC1 14 HOH A 501 HOH A 506 HOH A 512 HOH A 554
SITE 4 AC1 14 HOH A 731 DC P 11
SITE 1 AC2 6 ASP A 190 ASP A 192 ASP A 256 MG A 405
SITE 2 AC2 6 DC P 10 DC P 11
SITE 1 AC3 6 LYS A 60 LEU A 62 VAL A 65 HOH A 667
SITE 2 AC3 6 DC D 3 HOH D 103
SITE 1 AC4 6 THR A 101 VAL A 103 ILE A 106 HOH A 548
SITE 2 AC4 6 DG P 9 HOH P 102
SITE 1 AC5 7 ASP A 190 ASP A 192 PPV A 401 NA A 402
SITE 2 AC5 7 HOH A 501 HOH A 512 DC P 11
SITE 1 AC6 3 ALA A 32 HIS A 34 LYS A 35
SITE 1 AC7 4 ASN A 294 THR A 297 ARG A 299 HOH A 672
CRYST1 50.588 79.760 55.338 90.00 107.70 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 0.019768 0.000000 0.006309 0.00000
SCALE2 0.000000 0.012538 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018969 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
