HEADER TRANSFERASE, LYASE/DNA 07-MAY-13 4KLU
TITLE DNA POLYMERASE BETA MISMATCHED PRODUCT COMPLEX WITH MN2+, 15 H
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE BETA;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.7.7, 4.2.99.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: 5'-D(*CP*CP*GP*AP*CP*GP*GP*CP*GP*CP*AP*TP*CP*AP*GP*C)-3';
COMPND 8 CHAIN: T;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: 5'-D(*GP*CP*TP*GP*AP*TP*GP*CP*GP*CP*A)-3';
COMPND 12 CHAIN: P;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: 5'-D(P*GP*TP*CP*GP*G)-3';
COMPND 16 CHAIN: D;
COMPND 17 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: POLB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TAP56;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PWL11;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 MOL_ID: 4;
SOURCE 16 SYNTHETIC: YES
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 4KLU 1 REMARK LINK
REVDAT 2 15-NOV-17 4KLU 1 REMARK
REVDAT 1 17-JUL-13 4KLU 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. 1.97 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) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 30436
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 1509
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 31.9890 - 5.4263 0.99 2869 135 0.2001 0.2082
REMARK 3 2 5.4263 - 4.3104 1.00 2861 154 0.1831 0.2096
REMARK 3 3 4.3104 - 3.7665 1.00 2876 150 0.1739 0.2056
REMARK 3 4 3.7665 - 3.4225 1.00 2869 157 0.1888 0.2233
REMARK 3 5 3.4225 - 3.1774 1.00 2909 148 0.2060 0.2633
REMARK 3 6 3.1774 - 2.9903 1.00 2891 155 0.2134 0.2401
REMARK 3 7 2.9903 - 2.8406 0.99 2822 146 0.2373 0.2866
REMARK 3 8 2.8406 - 2.7170 0.99 2880 148 0.2412 0.2929
REMARK 3 9 2.7170 - 2.6125 0.98 2822 150 0.2400 0.3111
REMARK 3 10 2.6125 - 2.5224 0.98 2775 136 0.2422 0.2873
REMARK 3 11 2.5224 - 2.4435 0.97 2832 149 0.2278 0.2769
REMARK 3 12 2.4435 - 2.3737 0.97 2751 156 0.2334 0.2876
REMARK 3 13 2.3737 - 2.3112 0.95 2776 127 0.2275 0.3194
REMARK 3 14 2.3112 - 2.2548 0.94 2732 145 0.2371 0.3058
REMARK 3 15 2.2548 - 2.2036 0.93 2657 143 0.2339 0.2967
REMARK 3 16 2.2036 - 2.1567 0.91 2593 143 0.2349 0.2578
REMARK 3 17 2.1567 - 2.1136 0.87 2505 129 0.2423 0.2520
REMARK 3 18 2.1136 - 2.0737 0.81 2326 128 0.2487 0.2863
REMARK 3 19 2.0737 - 2.0367 0.72 2103 110 0.2614 0.3541
REMARK 3 20 2.0367 - 2.0022 0.64 1825 89 0.2469 0.2857
REMARK 3 21 2.0022 - 1.9700 0.53 1535 79 0.2467 0.2808
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 : 0.35
REMARK 3 B_SOL : 32.88
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.770
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.36750
REMARK 3 B22 (A**2) : 1.92210
REMARK 3 B33 (A**2) : 5.44550
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.79730
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 : 0.007 3373
REMARK 3 ANGLE : 1.111 4678
REMARK 3 CHIRALITY : 0.069 516
REMARK 3 PLANARITY : 0.004 491
REMARK 3 DIHEDRAL : 20.596 1321
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 4KLU 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_1000079500.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : 1.00
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK DOUBLE-CRYSTAL
REMARK 200 SI(111)
REMARK 200 OPTICS : VERTICAL FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31557
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.970
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 (%) : 97.2
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.22700
REMARK 200 R SYM FOR SHELL (I) : 0.22700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.429
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 3ISB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
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 40.05250
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: 4740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, T, P, 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 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 THR A 10
REMARK 465 THR A 205
REMARK 465 LYS A 206
REMARK 465 ASN A 245
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 203 CG CD OE1 OE2
REMARK 470 GLN A 207 CG CD OE1 NE2
REMARK 470 LYS A 244 CG CD CE NZ
REMARK 470 ASP A 246 CG OD1 OD2
REMARK 470 GLU A 247 CG CD OE1 OE2
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 P 10 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DT D 2 O4' - C1' - N1 ANGL. DEV. = -4.5 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 -155.27 -108.93
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 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 60 O
REMARK 620 2 LEU A 62 O 96.8
REMARK 620 3 VAL A 65 O 95.5 97.8
REMARK 620 4 HOH A 617 O 92.2 85.7 171.2
REMARK 620 5 DC D 3 OP1 168.7 93.5 87.8 83.8
REMARK 620 6 HOH D 206 O 94.6 166.5 88.3 86.6 74.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 101 O
REMARK 620 2 VAL A 103 O 95.0
REMARK 620 3 ILE A 106 O 95.2 89.0
REMARK 620 4 HOH A 604 O 84.0 92.5 178.4
REMARK 620 5 DG P 9 OP1 165.0 96.8 94.3 86.2
REMARK 620 6 HOH P 101 O 82.1 175.2 87.4 91.0 86.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN T 101 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG T 3 N7
REMARK 620 2 HOH T 221 O 95.9
REMARK 620 3 HOH T 224 O 90.9 173.1
REMARK 620 4 HOH T 229 O 96.4 80.6 99.5
REMARK 620 5 HOH T 239 O 85.4 102.7 77.1 176.1
REMARK 620 6 HOH T 241 O 174.6 80.5 92.7 79.0 99.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN D 101 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG D 4 N7
REMARK 620 2 HOH D 201 O 93.8
REMARK 620 3 HOH D 202 O 88.5 82.8
REMARK 620 4 HOH D 203 O 179.4 85.7 91.2
REMARK 620 5 HOH D 208 O 93.0 105.7 171.3 87.4
REMARK 620 6 HOH D 218 O 84.8 169.1 86.3 95.7 85.2
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 NA 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 MN T 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 101
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: 4KLM 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
DBREF 4KLU A 1 335 UNP P06746 DPOLB_HUMAN 1 335
DBREF 4KLU T 1 16 PDB 4KLU 4KLU 1 16
DBREF 4KLU P 1 11 PDB 4KLU 4KLU 1 11
DBREF 4KLU D 1 5 PDB 4KLU 4KLU 1 5
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
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 DA
SEQRES 1 D 5 DG DT DC DG DG
HET NA A 401 1
HET NA A 402 1
HET MN T 101 1
HET MN D 101 1
HETNAM NA SODIUM ION
HETNAM MN MANGANESE (II) ION
FORMUL 5 NA 2(NA 1+)
FORMUL 7 MN 2(MN 2+)
FORMUL 9 HOH *298(H2 O)
HELIX 1 1 ASN A 12 VAL A 29 1 18
HELIX 2 2 ALA A 32 LYS A 48 1 17
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 GLN A 90 1 9
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 GLY A 184 5 6
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 VAL A 177 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 CYS A 239 O ARG A 253
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 O LYS A 60 NA NA A 402 1555 1555 2.37
LINK O LEU A 62 NA NA A 402 1555 1555 2.30
LINK O VAL A 65 NA NA A 402 1555 1555 2.34
LINK O THR A 101 NA NA A 401 1555 1555 2.31
LINK O VAL A 103 NA NA A 401 1555 1555 2.42
LINK O ILE A 106 NA NA A 401 1555 1555 2.44
LINK NA NA A 401 O HOH A 604 1555 1555 2.56
LINK NA NA A 401 OP1 DG P 9 1555 1555 2.46
LINK NA NA A 401 O HOH P 101 1555 1555 2.66
LINK NA NA A 402 O HOH A 617 1555 1555 2.40
LINK NA NA A 402 OP1 DC D 3 1555 1555 3.02
LINK NA NA A 402 O HOH D 206 1555 1555 2.39
LINK N7 DG T 3 MN MN T 101 1555 1555 2.39
LINK MN MN T 101 O HOH T 221 1555 1555 2.39
LINK MN MN T 101 O HOH T 224 1555 1555 2.54
LINK MN MN T 101 O HOH T 229 1555 1555 2.40
LINK MN MN T 101 O HOH T 239 1555 1555 2.34
LINK MN MN T 101 O HOH T 241 1555 1555 2.33
LINK N7 DG D 4 MN MN D 101 1555 1555 2.36
LINK MN MN D 101 O HOH D 201 1555 1555 2.25
LINK MN MN D 101 O HOH D 202 1555 1555 2.00
LINK MN MN D 101 O HOH D 203 1555 1555 2.11
LINK MN MN D 101 O HOH D 208 1555 1555 2.41
LINK MN MN D 101 O HOH D 218 1555 1555 1.96
CISPEP 1 GLY A 274 SER A 275 0 2.83
SITE 1 AC1 6 THR A 101 VAL A 103 ILE A 106 HOH A 604
SITE 2 AC1 6 DG P 9 HOH P 101
SITE 1 AC2 6 LYS A 60 LEU A 62 VAL A 65 HOH A 617
SITE 2 AC2 6 DC D 3 HOH D 206
SITE 1 AC3 6 DG T 3 HOH T 221 HOH T 224 HOH T 229
SITE 2 AC3 6 HOH T 239 HOH T 241
SITE 1 AC4 6 DG D 4 HOH D 201 HOH D 202 HOH D 203
SITE 2 AC4 6 HOH D 208 HOH D 218
CRYST1 55.222 80.105 55.812 90.00 109.64 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 0.018109 0.000000 0.006462 0.00000
SCALE2 0.000000 0.012484 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019024 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
