HEADER HYDROLASE, LYASE/DNA 13-DEC-12 4IEM
TITLE HUMAN APURINIC/APYRIMIDINIC ENDONUCLEASE (APE1) WITH PRODUCT DNA AND
TITLE 2 MG2+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-(APURINIC OR APYRIMIDINIC SITE) LYASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: APEX NUCLEASE, APEN, APURINIC-APYRIMIDINIC ENDONUCLEASE 1,
COMPND 5 AP ENDONUCLEASE 1, APE-1, REF-1, REDOX FACTOR-1, DNA-(APURINIC OR
COMPND 6 APYRIMIDINIC SITE) LYASE, MITOCHONDRIAL;
COMPND 7 EC: 3.1.-.-, 4.2.99.18;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: DNA (5'-D(*GP*CP*TP*AP*C)-3');
COMPND 11 CHAIN: E, H, K, N;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: DNA (5'-D(P*(3DR)P*GP*AP*TP*CP*G)-3');
COMPND 15 CHAIN: F, I, L, O;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: DNA (5'-D(*CP*GP*AP*TP*CP*GP*GP*TP*AP*GP*C)-3');
COMPND 19 CHAIN: G, J, M, P;
COMPND 20 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: APE, APE1, APEX, APEX1, APX, HAP1, REF1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC DNA;
SOURCE 11 ORGANISM_TAXID: 32630;
SOURCE 12 OTHER_DETAILS: DNA OLIGONUCLEOTIDE SYNTHESIS;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 ORGANISM_SCIENTIFIC: SYNTHETIC DNA;
SOURCE 16 ORGANISM_TAXID: 32630;
SOURCE 17 OTHER_DETAILS: DNA OLIGONUCLEOTIDE SYNTHESIS;
SOURCE 18 MOL_ID: 4;
SOURCE 19 SYNTHETIC: YES;
SOURCE 20 ORGANISM_SCIENTIFIC: SYNTHETIC DNA;
SOURCE 21 ORGANISM_TAXID: 32630;
SOURCE 22 OTHER_DETAILS: DNA OLIGONUCLEOTIDE SYNTHESIS
KEYWDS METALLOPROTEIN, DNA DAMAGE, DNA REPAIR, BASE EXCISION REPAIR,
KEYWDS 2 PROTEIN-DNA, REF1, NUCLEASE, HYDROLASE, LYASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.E.TSUTAKAWA,C.D.MOL,A.S.ARVAI,J.A.TAINER
REVDAT 5 28-FEB-24 4IEM 1 REMARK LINK
REVDAT 4 15-NOV-17 4IEM 1 REMARK
REVDAT 3 10-APR-13 4IEM 1 JRNL
REVDAT 2 13-FEB-13 4IEM 1 HETATM JRNL REMARK SITE
REVDAT 1 23-JAN-13 4IEM 0
JRNL AUTH S.E.TSUTAKAWA,D.S.SHIN,C.D.MOL,T.IZUMI,A.S.ARVAI,A.K.MANTHA,
JRNL AUTH 2 B.SZCZESNY,I.N.IVANOV,D.J.HOSFIELD,B.MAITI,M.E.PIQUE,
JRNL AUTH 3 K.A.FRANKEL,K.HITOMI,R.P.CUNNINGHAM,S.MITRA,J.A.TAINER
JRNL TITL CONSERVED STRUCTURAL CHEMISTRY FOR INCISION ACTIVITY IN
JRNL TITL 2 STRUCTURALLY NON-HOMOLOGOUS APURINIC/APYRIMIDINIC
JRNL TITL 3 ENDONUCLEASE APE1 AND ENDONUCLEASE IV DNA REPAIR ENZYMES.
JRNL REF J.BIOL.CHEM. V. 288 8445 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23355472
JRNL DOI 10.1074/JBC.M112.422774
REMARK 2
REMARK 2 RESOLUTION. 2.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
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) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 3 NUMBER OF REFLECTIONS : 56705
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2868
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 29.6451 - 6.4756 0.98 3064 157 0.1678 0.1741
REMARK 3 2 6.4756 - 5.1487 0.99 3001 166 0.1835 0.2161
REMARK 3 3 5.1487 - 4.5004 0.98 2974 154 0.1759 0.2031
REMARK 3 4 4.5004 - 4.0901 0.95 2852 147 0.1756 0.1971
REMARK 3 5 4.0901 - 3.7976 0.92 2770 143 0.1886 0.2291
REMARK 3 6 3.7976 - 3.5741 0.90 2676 151 0.1976 0.2365
REMARK 3 7 3.5741 - 3.3953 0.88 2620 142 0.2070 0.2463
REMARK 3 8 3.3953 - 3.2477 0.87 2617 134 0.2206 0.2781
REMARK 3 9 3.2477 - 3.1228 0.87 2585 121 0.2339 0.2514
REMARK 3 10 3.1228 - 3.0152 0.87 2626 147 0.2463 0.2939
REMARK 3 11 3.0152 - 2.9210 0.87 2576 138 0.2527 0.3418
REMARK 3 12 2.9210 - 2.8376 0.87 2575 138 0.2556 0.3164
REMARK 3 13 2.8376 - 2.7629 0.87 2616 125 0.2540 0.2781
REMARK 3 14 2.7629 - 2.6955 0.87 2577 150 0.2617 0.3414
REMARK 3 15 2.6955 - 2.6343 0.88 2620 134 0.2532 0.2942
REMARK 3 16 2.6343 - 2.5783 0.88 2607 165 0.2590 0.3228
REMARK 3 17 2.5783 - 2.5267 0.89 2638 140 0.2698 0.3405
REMARK 3 18 2.5267 - 2.4791 0.89 2658 129 0.2772 0.3347
REMARK 3 19 2.4791 - 2.4348 0.89 2630 155 0.2724 0.3432
REMARK 3 20 2.4348 - 2.3936 0.86 2555 132 0.2854 0.3756
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.760
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.86
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 : 0.017 11009
REMARK 3 ANGLE : 0.918 15283
REMARK 3 CHIRALITY : 0.047 1622
REMARK 3 PLANARITY : 0.003 1681
REMARK 3 DIHEDRAL : 19.512 4209
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 45.2061 29.1620 22.3220
REMARK 3 T TENSOR
REMARK 3 T11: 0.3301 T22: 0.3413
REMARK 3 T33: 0.2634 T12: 0.0128
REMARK 3 T13: 0.0212 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 0.9093 L22: 0.9301
REMARK 3 L33: 0.1084 L12: 0.8234
REMARK 3 L13: 0.0257 L23: 0.1705
REMARK 3 S TENSOR
REMARK 3 S11: 0.2309 S12: -0.3189 S13: 0.0861
REMARK 3 S21: 0.2853 S22: -0.2003 S23: 0.0880
REMARK 3 S31: 0.0803 S32: 0.0545 S33: -0.0321
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 44:110 OR RESSEQ
REMARK 3 113:318 ) AND (NOT ELEMENT H)
REMARK 3 SELECTION : CHAIN 'B' AND (RESSEQ 44:110 OR RESSEQ
REMARK 3 113:318 ) AND (NOT ELEMENT H)
REMARK 3 ATOM PAIRS NUMBER : 2154
REMARK 3 RMSD : 0.978
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 44:110 OR RESSEQ
REMARK 3 113:318 ) AND (NOT ELEMENT H)
REMARK 3 SELECTION : CHAIN 'C' AND (RESSEQ 44:110 OR RESSEQ
REMARK 3 113:318 ) AND (NOT ELEMENT H)
REMARK 3 ATOM PAIRS NUMBER : 2170
REMARK 3 RMSD : 0.768
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND (RESSEQ 44:110 OR RESSEQ
REMARK 3 113:318 ) AND (NOT ELEMENT H)
REMARK 3 SELECTION : CHAIN 'D' AND (RESSEQ 44:110 OR RESSEQ
REMARK 3 113:318 ) AND (NOT ELEMENT H)
REMARK 3 ATOM PAIRS NUMBER : 2170
REMARK 3 RMSD : 0.846
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'G' AND (RESSEQ 513:522 ) AND (NOT
REMARK 3 ELEMENT H)
REMARK 3 SELECTION : CHAIN 'J' AND (RESSEQ 513:522 ) AND (NOT
REMARK 3 ELEMENT H)
REMARK 3 ATOM PAIRS NUMBER : 208
REMARK 3 RMSD : 0.242
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN 'G' AND (RESSEQ 513:522 ) AND (NOT
REMARK 3 ELEMENT H)
REMARK 3 SELECTION : CHAIN 'M' AND (RESSEQ 513:522 ) AND (NOT
REMARK 3 ELEMENT H)
REMARK 3 ATOM PAIRS NUMBER : 208
REMARK 3 RMSD : 0.186
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN 'G' AND (RESSEQ 513:522 ) AND (NOT
REMARK 3 ELEMENT H)
REMARK 3 SELECTION : CHAIN 'P' AND (RESSEQ 513:522 ) AND (NOT
REMARK 3 ELEMENT H)
REMARK 3 ATOM PAIRS NUMBER : 208
REMARK 3 RMSD : 0.301
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4IEM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-DEC-12.
REMARK 100 THE DEPOSITION ID IS D_1000076655.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUL-01
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 : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97956
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 : 56727
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.393
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM MES PH 6.0, 200 MM LISO4, AND
REMARK 280 25% MPEG 2K, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 37.04500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 4790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, F, 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 350
REMARK 350 BIOMOLECULE: 2
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: 4450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H, I, J
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 350
REMARK 350 BIOMOLECULE: 3
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: 4430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, K, L, M
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 350
REMARK 350 BIOMOLECULE: 4
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: 4370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, N, O, P
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 PRO A 2
REMARK 465 LYS A 3
REMARK 465 ARG A 4
REMARK 465 GLY A 5
REMARK 465 LYS A 6
REMARK 465 LYS A 7
REMARK 465 GLY A 8
REMARK 465 ALA A 9
REMARK 465 VAL A 10
REMARK 465 ALA A 11
REMARK 465 GLU A 12
REMARK 465 ASP A 13
REMARK 465 GLY A 14
REMARK 465 ASP A 15
REMARK 465 GLU A 16
REMARK 465 LEU A 17
REMARK 465 ARG A 18
REMARK 465 THR A 19
REMARK 465 GLU A 20
REMARK 465 PRO A 21
REMARK 465 GLU A 22
REMARK 465 ALA A 23
REMARK 465 LYS A 24
REMARK 465 LYS A 25
REMARK 465 SER A 26
REMARK 465 LYS A 27
REMARK 465 THR A 28
REMARK 465 ALA A 29
REMARK 465 ALA A 30
REMARK 465 LYS A 31
REMARK 465 LYS A 32
REMARK 465 ASN A 33
REMARK 465 ASP A 34
REMARK 465 LYS A 35
REMARK 465 GLU A 36
REMARK 465 ALA A 37
REMARK 465 ALA A 38
REMARK 465 GLY A 39
REMARK 465 GLU A 40
REMARK 465 PRO B 2
REMARK 465 LYS B 3
REMARK 465 ARG B 4
REMARK 465 GLY B 5
REMARK 465 LYS B 6
REMARK 465 LYS B 7
REMARK 465 GLY B 8
REMARK 465 ALA B 9
REMARK 465 VAL B 10
REMARK 465 ALA B 11
REMARK 465 GLU B 12
REMARK 465 ASP B 13
REMARK 465 GLY B 14
REMARK 465 ASP B 15
REMARK 465 GLU B 16
REMARK 465 LEU B 17
REMARK 465 ARG B 18
REMARK 465 THR B 19
REMARK 465 GLU B 20
REMARK 465 PRO B 21
REMARK 465 GLU B 22
REMARK 465 ALA B 23
REMARK 465 LYS B 24
REMARK 465 LYS B 25
REMARK 465 SER B 26
REMARK 465 LYS B 27
REMARK 465 THR B 28
REMARK 465 ALA B 29
REMARK 465 ALA B 30
REMARK 465 LYS B 31
REMARK 465 LYS B 32
REMARK 465 ASN B 33
REMARK 465 ASP B 34
REMARK 465 LYS B 35
REMARK 465 GLU B 36
REMARK 465 ALA B 37
REMARK 465 ALA B 38
REMARK 465 GLY B 39
REMARK 465 GLU B 40
REMARK 465 GLY B 41
REMARK 465 PRO B 42
REMARK 465 ALA B 43
REMARK 465 DG I 511
REMARK 465 PRO C 2
REMARK 465 LYS C 3
REMARK 465 ARG C 4
REMARK 465 GLY C 5
REMARK 465 LYS C 6
REMARK 465 LYS C 7
REMARK 465 GLY C 8
REMARK 465 ALA C 9
REMARK 465 VAL C 10
REMARK 465 ALA C 11
REMARK 465 GLU C 12
REMARK 465 ASP C 13
REMARK 465 GLY C 14
REMARK 465 ASP C 15
REMARK 465 GLU C 16
REMARK 465 LEU C 17
REMARK 465 ARG C 18
REMARK 465 THR C 19
REMARK 465 GLU C 20
REMARK 465 PRO C 21
REMARK 465 GLU C 22
REMARK 465 ALA C 23
REMARK 465 LYS C 24
REMARK 465 LYS C 25
REMARK 465 SER C 26
REMARK 465 LYS C 27
REMARK 465 THR C 28
REMARK 465 ALA C 29
REMARK 465 ALA C 30
REMARK 465 LYS C 31
REMARK 465 LYS C 32
REMARK 465 ASN C 33
REMARK 465 ASP C 34
REMARK 465 LYS C 35
REMARK 465 GLU C 36
REMARK 465 ALA C 37
REMARK 465 ALA C 38
REMARK 465 GLY C 39
REMARK 465 GLU C 40
REMARK 465 PRO D 2
REMARK 465 LYS D 3
REMARK 465 ARG D 4
REMARK 465 GLY D 5
REMARK 465 LYS D 6
REMARK 465 LYS D 7
REMARK 465 GLY D 8
REMARK 465 ALA D 9
REMARK 465 VAL D 10
REMARK 465 ALA D 11
REMARK 465 GLU D 12
REMARK 465 ASP D 13
REMARK 465 GLY D 14
REMARK 465 ASP D 15
REMARK 465 GLU D 16
REMARK 465 LEU D 17
REMARK 465 ARG D 18
REMARK 465 THR D 19
REMARK 465 GLU D 20
REMARK 465 PRO D 21
REMARK 465 GLU D 22
REMARK 465 ALA D 23
REMARK 465 LYS D 24
REMARK 465 LYS D 25
REMARK 465 SER D 26
REMARK 465 LYS D 27
REMARK 465 THR D 28
REMARK 465 ALA D 29
REMARK 465 ALA D 30
REMARK 465 LYS D 31
REMARK 465 LYS D 32
REMARK 465 ASN D 33
REMARK 465 ASP D 34
REMARK 465 LYS D 35
REMARK 465 GLU D 36
REMARK 465 ALA D 37
REMARK 465 ALA D 38
REMARK 465 GLY D 39
REMARK 465 GLU D 40
REMARK 465 GLY D 41
REMARK 465 PRO D 42
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 DC I 510 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DC I 510 N1 C2 O2 N3 C4 N4 C5
REMARK 470 DC I 510 C6
REMARK 470 DG O 511 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DG O 511 N9 C8 N7 C5 C6 O6 N1
REMARK 470 DG O 511 C2 N2 N3 C4
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 O2 DC E 505 H22 DG G 518 1.54
REMARK 500 OD2 ASP B 50 HH TYR B 315 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 E 501 O4' - C1' - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 DC E 505 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG H 501 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DC H 505 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DC J 512 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DG K 501 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DC K 505 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG M 517 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DC P 512 C1' - O4' - C4' ANGL. DEV. = -8.2 DEGREES
REMARK 500 DC P 512 C3' - C2' - C1' ANGL. DEV. = -9.6 DEGREES
REMARK 500 DC P 512 O4' - C1' - C2' ANGL. DEV. = -6.9 DEGREES
REMARK 500 DC P 512 O4' - C1' - N1 ANGL. DEV. = 9.3 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 LYS A 52 44.95 -102.16
REMARK 500 LYS A 79 35.34 79.32
REMARK 500 SER A 129 -142.87 56.28
REMARK 500 PHE A 232 25.98 -145.85
REMARK 500 SER B 56 2.91 -69.87
REMARK 500 LEU B 62 117.59 -162.41
REMARK 500 LEU B 111 72.72 -107.68
REMARK 500 LEU B 114 51.21 -140.89
REMARK 500 SER B 129 -136.71 58.04
REMARK 500 PHE B 162 -157.41 -119.23
REMARK 500 ASN B 222 70.55 -115.15
REMARK 500 PRO B 234 -39.21 -31.96
REMARK 500 ASN B 259 11.78 -141.48
REMARK 500 THR B 268 153.70 -47.28
REMARK 500 ASN B 272 29.44 47.76
REMARK 500 ASN B 277 48.28 32.57
REMARK 500 HIS B 289 -28.31 -38.92
REMARK 500 LYS C 79 31.25 74.17
REMARK 500 ASP C 124 35.72 -151.89
REMARK 500 SER C 129 -129.63 57.76
REMARK 500 PHE C 232 22.51 -147.04
REMARK 500 ASN C 277 42.94 39.60
REMARK 500 ALA D 88 67.67 39.46
REMARK 500 ASP D 124 20.69 -144.33
REMARK 500 SER D 129 -142.61 51.11
REMARK 500 PHE D 162 -167.80 -121.48
REMARK 500 ASN D 222 71.86 -119.81
REMARK 500 MET D 271 37.02 35.15
REMARK 500 ALA D 317 78.36 -116.10
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 505 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 44 O
REMARK 620 2 HOH A 666 O 106.0
REMARK 620 N 1
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 GLU A 96 OE1
REMARK 620 2 HOH A 601 O 68.0
REMARK 620 3 HOH A 602 O 73.4 57.5
REMARK 620 4 HOH A 603 O 139.7 88.2 66.3
REMARK 620 5 DC E 505 O3' 69.3 123.3 75.8 101.7
REMARK 620 6 3DR F 506 OP1 103.8 111.6 169.1 115.3 113.4
REMARK 620 N 1 2 3 4 5
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 HOH A 641 O
REMARK 620 2 DC E 505 O2 116.6
REMARK 620 3 DT G 519 O2 122.4 97.6
REMARK 620 4 HOH G 606 O 94.8 148.6 62.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DT L 509 O2
REMARK 620 2 DT M 515 O2 112.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA E 601 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DA E 504 OP2
REMARK 620 2 DA E 504 O5' 52.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 96 OE1
REMARK 620 2 HOH B 502 O 96.6
REMARK 620 3 HOH B 503 O 87.3 78.3
REMARK 620 4 DC H 505 O3' 70.8 84.4 150.4
REMARK 620 5 3DR I 506 OP1 104.7 152.2 119.8 85.9
REMARK 620 6 HOH I 601 O 166.2 89.4 106.1 97.5 66.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 189 OD1
REMARK 620 2 ASP B 189 OD2 44.9
REMARK 620 3 GLU B 236 O 109.3 153.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 257 OH
REMARK 620 2 SER B 298 O 110.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 96 OE1
REMARK 620 2 HOH C 601 O 62.6
REMARK 620 3 HOH C 602 O 157.0 96.6
REMARK 620 4 DC K 505 O3' 68.8 126.0 124.0
REMARK 620 5 HOH K 701 O 90.1 74.7 73.9 83.5
REMARK 620 6 3DR L 506 OP1 97.4 105.7 97.9 102.4 171.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 614 O
REMARK 620 2 HOH C 668 O 84.5
REMARK 620 3 DC K 505 O2 156.7 113.8
REMARK 620 4 HOH K 701 O 94.0 68.0 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 96 OE1
REMARK 620 2 HOH D 501 O 74.9
REMARK 620 3 HOH D 502 O 165.2 90.9
REMARK 620 4 DC N 505 O3' 72.6 145.4 122.1
REMARK 620 5 HOH N 701 O 90.6 82.2 91.8 86.3
REMARK 620 6 3DR O 506 OP1 95.2 99.6 82.7 95.1 174.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA N 601 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DA N 504 OP2
REMARK 620 2 DA N 504 O5' 52.7
REMARK 620 N 1
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 MG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA F 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA N 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IEK RELATED DB: PDB
DBREF 4IEM A 2 318 UNP P27695 APEX1_HUMAN 2 318
DBREF 4IEM B 2 318 UNP P27695 APEX1_HUMAN 2 318
DBREF 4IEM C 2 318 UNP P27695 APEX1_HUMAN 2 318
DBREF 4IEM D 2 318 UNP P27695 APEX1_HUMAN 2 318
DBREF 4IEM E 501 505 PDB 4IEM 4IEM 501 505
DBREF 4IEM H 501 505 PDB 4IEM 4IEM 501 505
DBREF 4IEM K 501 505 PDB 4IEM 4IEM 501 505
DBREF 4IEM N 501 505 PDB 4IEM 4IEM 501 505
DBREF 4IEM F 506 511 PDB 4IEM 4IEM 506 511
DBREF 4IEM I 506 511 PDB 4IEM 4IEM 506 511
DBREF 4IEM L 506 511 PDB 4IEM 4IEM 506 511
DBREF 4IEM O 506 511 PDB 4IEM 4IEM 506 511
DBREF 4IEM G 512 522 PDB 4IEM 4IEM 512 522
DBREF 4IEM J 512 522 PDB 4IEM 4IEM 512 522
DBREF 4IEM M 512 522 PDB 4IEM 4IEM 512 522
DBREF 4IEM P 512 522 PDB 4IEM 4IEM 512 522
SEQRES 1 A 317 PRO LYS ARG GLY LYS LYS GLY ALA VAL ALA GLU ASP GLY
SEQRES 2 A 317 ASP GLU LEU ARG THR GLU PRO GLU ALA LYS LYS SER LYS
SEQRES 3 A 317 THR ALA ALA LYS LYS ASN ASP LYS GLU ALA ALA GLY GLU
SEQRES 4 A 317 GLY PRO ALA LEU TYR GLU ASP PRO PRO ASP GLN LYS THR
SEQRES 5 A 317 SER PRO SER GLY LYS PRO ALA THR LEU LYS ILE CYS SER
SEQRES 6 A 317 TRP ASN VAL ASP GLY LEU ARG ALA TRP ILE LYS LYS LYS
SEQRES 7 A 317 GLY LEU ASP TRP VAL LYS GLU GLU ALA PRO ASP ILE LEU
SEQRES 8 A 317 CYS LEU GLN GLU THR LYS CYS SER GLU ASN LYS LEU PRO
SEQRES 9 A 317 ALA GLU LEU GLN GLU LEU PRO GLY LEU SER HIS GLN TYR
SEQRES 10 A 317 TRP SER ALA PRO SER ASP LYS GLU GLY TYR SER GLY VAL
SEQRES 11 A 317 GLY LEU LEU SER ARG GLN CYS PRO LEU LYS VAL SER TYR
SEQRES 12 A 317 GLY ILE GLY ASP GLU GLU HIS ASP GLN GLU GLY ARG VAL
SEQRES 13 A 317 ILE VAL ALA GLU PHE ASP SER PHE VAL LEU VAL THR ALA
SEQRES 14 A 317 TYR VAL PRO ASN ALA GLY ARG GLY LEU VAL ARG LEU GLU
SEQRES 15 A 317 TYR ARG GLN ARG TRP ASP GLU ALA PHE ARG LYS PHE LEU
SEQRES 16 A 317 LYS GLY LEU ALA SER ARG LYS PRO LEU VAL LEU CYS GLY
SEQRES 17 A 317 ASP LEU ASN VAL ALA HIS GLU GLU ILE ASP LEU ARG ASN
SEQRES 18 A 317 PRO LYS GLY ASN LYS LYS ASN ALA GLY PHE THR PRO GLN
SEQRES 19 A 317 GLU ARG GLN GLY PHE GLY GLU LEU LEU GLN ALA VAL PRO
SEQRES 20 A 317 LEU ALA ASP SER PHE ARG HIS LEU TYR PRO ASN THR PRO
SEQRES 21 A 317 TYR ALA TYR THR PHE TRP THR TYR MET MET ASN ALA ARG
SEQRES 22 A 317 SER LYS ASN VAL GLY TRP ARG LEU ASP TYR PHE LEU LEU
SEQRES 23 A 317 SER HIS SER LEU LEU PRO ALA LEU CYS ASP SER LYS ILE
SEQRES 24 A 317 ARG SER LYS ALA LEU GLY SER ASP HIS CYS PRO ILE THR
SEQRES 25 A 317 LEU TYR LEU ALA LEU
SEQRES 1 E 5 DG DC DT DA DC
SEQRES 1 F 6 3DR DG DA DT DC DG
SEQRES 1 G 11 DC DG DA DT DC DG DG DT DA DG DC
SEQRES 1 B 317 PRO LYS ARG GLY LYS LYS GLY ALA VAL ALA GLU ASP GLY
SEQRES 2 B 317 ASP GLU LEU ARG THR GLU PRO GLU ALA LYS LYS SER LYS
SEQRES 3 B 317 THR ALA ALA LYS LYS ASN ASP LYS GLU ALA ALA GLY GLU
SEQRES 4 B 317 GLY PRO ALA LEU TYR GLU ASP PRO PRO ASP GLN LYS THR
SEQRES 5 B 317 SER PRO SER GLY LYS PRO ALA THR LEU LYS ILE CYS SER
SEQRES 6 B 317 TRP ASN VAL ASP GLY LEU ARG ALA TRP ILE LYS LYS LYS
SEQRES 7 B 317 GLY LEU ASP TRP VAL LYS GLU GLU ALA PRO ASP ILE LEU
SEQRES 8 B 317 CYS LEU GLN GLU THR LYS CYS SER GLU ASN LYS LEU PRO
SEQRES 9 B 317 ALA GLU LEU GLN GLU LEU PRO GLY LEU SER HIS GLN TYR
SEQRES 10 B 317 TRP SER ALA PRO SER ASP LYS GLU GLY TYR SER GLY VAL
SEQRES 11 B 317 GLY LEU LEU SER ARG GLN CYS PRO LEU LYS VAL SER TYR
SEQRES 12 B 317 GLY ILE GLY ASP GLU GLU HIS ASP GLN GLU GLY ARG VAL
SEQRES 13 B 317 ILE VAL ALA GLU PHE ASP SER PHE VAL LEU VAL THR ALA
SEQRES 14 B 317 TYR VAL PRO ASN ALA GLY ARG GLY LEU VAL ARG LEU GLU
SEQRES 15 B 317 TYR ARG GLN ARG TRP ASP GLU ALA PHE ARG LYS PHE LEU
SEQRES 16 B 317 LYS GLY LEU ALA SER ARG LYS PRO LEU VAL LEU CYS GLY
SEQRES 17 B 317 ASP LEU ASN VAL ALA HIS GLU GLU ILE ASP LEU ARG ASN
SEQRES 18 B 317 PRO LYS GLY ASN LYS LYS ASN ALA GLY PHE THR PRO GLN
SEQRES 19 B 317 GLU ARG GLN GLY PHE GLY GLU LEU LEU GLN ALA VAL PRO
SEQRES 20 B 317 LEU ALA ASP SER PHE ARG HIS LEU TYR PRO ASN THR PRO
SEQRES 21 B 317 TYR ALA TYR THR PHE TRP THR TYR MET MET ASN ALA ARG
SEQRES 22 B 317 SER LYS ASN VAL GLY TRP ARG LEU ASP TYR PHE LEU LEU
SEQRES 23 B 317 SER HIS SER LEU LEU PRO ALA LEU CYS ASP SER LYS ILE
SEQRES 24 B 317 ARG SER LYS ALA LEU GLY SER ASP HIS CYS PRO ILE THR
SEQRES 25 B 317 LEU TYR LEU ALA LEU
SEQRES 1 H 5 DG DC DT DA DC
SEQRES 1 I 6 3DR DG DA DT DC DG
SEQRES 1 J 11 DC DG DA DT DC DG DG DT DA DG DC
SEQRES 1 C 317 PRO LYS ARG GLY LYS LYS GLY ALA VAL ALA GLU ASP GLY
SEQRES 2 C 317 ASP GLU LEU ARG THR GLU PRO GLU ALA LYS LYS SER LYS
SEQRES 3 C 317 THR ALA ALA LYS LYS ASN ASP LYS GLU ALA ALA GLY GLU
SEQRES 4 C 317 GLY PRO ALA LEU TYR GLU ASP PRO PRO ASP GLN LYS THR
SEQRES 5 C 317 SER PRO SER GLY LYS PRO ALA THR LEU LYS ILE CYS SER
SEQRES 6 C 317 TRP ASN VAL ASP GLY LEU ARG ALA TRP ILE LYS LYS LYS
SEQRES 7 C 317 GLY LEU ASP TRP VAL LYS GLU GLU ALA PRO ASP ILE LEU
SEQRES 8 C 317 CYS LEU GLN GLU THR LYS CYS SER GLU ASN LYS LEU PRO
SEQRES 9 C 317 ALA GLU LEU GLN GLU LEU PRO GLY LEU SER HIS GLN TYR
SEQRES 10 C 317 TRP SER ALA PRO SER ASP LYS GLU GLY TYR SER GLY VAL
SEQRES 11 C 317 GLY LEU LEU SER ARG GLN CYS PRO LEU LYS VAL SER TYR
SEQRES 12 C 317 GLY ILE GLY ASP GLU GLU HIS ASP GLN GLU GLY ARG VAL
SEQRES 13 C 317 ILE VAL ALA GLU PHE ASP SER PHE VAL LEU VAL THR ALA
SEQRES 14 C 317 TYR VAL PRO ASN ALA GLY ARG GLY LEU VAL ARG LEU GLU
SEQRES 15 C 317 TYR ARG GLN ARG TRP ASP GLU ALA PHE ARG LYS PHE LEU
SEQRES 16 C 317 LYS GLY LEU ALA SER ARG LYS PRO LEU VAL LEU CYS GLY
SEQRES 17 C 317 ASP LEU ASN VAL ALA HIS GLU GLU ILE ASP LEU ARG ASN
SEQRES 18 C 317 PRO LYS GLY ASN LYS LYS ASN ALA GLY PHE THR PRO GLN
SEQRES 19 C 317 GLU ARG GLN GLY PHE GLY GLU LEU LEU GLN ALA VAL PRO
SEQRES 20 C 317 LEU ALA ASP SER PHE ARG HIS LEU TYR PRO ASN THR PRO
SEQRES 21 C 317 TYR ALA TYR THR PHE TRP THR TYR MET MET ASN ALA ARG
SEQRES 22 C 317 SER LYS ASN VAL GLY TRP ARG LEU ASP TYR PHE LEU LEU
SEQRES 23 C 317 SER HIS SER LEU LEU PRO ALA LEU CYS ASP SER LYS ILE
SEQRES 24 C 317 ARG SER LYS ALA LEU GLY SER ASP HIS CYS PRO ILE THR
SEQRES 25 C 317 LEU TYR LEU ALA LEU
SEQRES 1 K 5 DG DC DT DA DC
SEQRES 1 L 6 3DR DG DA DT DC DG
SEQRES 1 M 11 DC DG DA DT DC DG DG DT DA DG DC
SEQRES 1 D 317 PRO LYS ARG GLY LYS LYS GLY ALA VAL ALA GLU ASP GLY
SEQRES 2 D 317 ASP GLU LEU ARG THR GLU PRO GLU ALA LYS LYS SER LYS
SEQRES 3 D 317 THR ALA ALA LYS LYS ASN ASP LYS GLU ALA ALA GLY GLU
SEQRES 4 D 317 GLY PRO ALA LEU TYR GLU ASP PRO PRO ASP GLN LYS THR
SEQRES 5 D 317 SER PRO SER GLY LYS PRO ALA THR LEU LYS ILE CYS SER
SEQRES 6 D 317 TRP ASN VAL ASP GLY LEU ARG ALA TRP ILE LYS LYS LYS
SEQRES 7 D 317 GLY LEU ASP TRP VAL LYS GLU GLU ALA PRO ASP ILE LEU
SEQRES 8 D 317 CYS LEU GLN GLU THR LYS CYS SER GLU ASN LYS LEU PRO
SEQRES 9 D 317 ALA GLU LEU GLN GLU LEU PRO GLY LEU SER HIS GLN TYR
SEQRES 10 D 317 TRP SER ALA PRO SER ASP LYS GLU GLY TYR SER GLY VAL
SEQRES 11 D 317 GLY LEU LEU SER ARG GLN CYS PRO LEU LYS VAL SER TYR
SEQRES 12 D 317 GLY ILE GLY ASP GLU GLU HIS ASP GLN GLU GLY ARG VAL
SEQRES 13 D 317 ILE VAL ALA GLU PHE ASP SER PHE VAL LEU VAL THR ALA
SEQRES 14 D 317 TYR VAL PRO ASN ALA GLY ARG GLY LEU VAL ARG LEU GLU
SEQRES 15 D 317 TYR ARG GLN ARG TRP ASP GLU ALA PHE ARG LYS PHE LEU
SEQRES 16 D 317 LYS GLY LEU ALA SER ARG LYS PRO LEU VAL LEU CYS GLY
SEQRES 17 D 317 ASP LEU ASN VAL ALA HIS GLU GLU ILE ASP LEU ARG ASN
SEQRES 18 D 317 PRO LYS GLY ASN LYS LYS ASN ALA GLY PHE THR PRO GLN
SEQRES 19 D 317 GLU ARG GLN GLY PHE GLY GLU LEU LEU GLN ALA VAL PRO
SEQRES 20 D 317 LEU ALA ASP SER PHE ARG HIS LEU TYR PRO ASN THR PRO
SEQRES 21 D 317 TYR ALA TYR THR PHE TRP THR TYR MET MET ASN ALA ARG
SEQRES 22 D 317 SER LYS ASN VAL GLY TRP ARG LEU ASP TYR PHE LEU LEU
SEQRES 23 D 317 SER HIS SER LEU LEU PRO ALA LEU CYS ASP SER LYS ILE
SEQRES 24 D 317 ARG SER LYS ALA LEU GLY SER ASP HIS CYS PRO ILE THR
SEQRES 25 D 317 LEU TYR LEU ALA LEU
SEQRES 1 N 5 DG DC DT DA DC
SEQRES 1 O 6 3DR DG DA DT DC DG
SEQRES 1 P 11 DC DG DA DT DC DG DG DT DA DG DC
HET 3DR F 506 20
HET 3DR I 506 20
HET 3DR L 506 20
HET 3DR O 506 20
HET MG A 501 1
HET MG A 502 1
HET NA A 504 1
HET NA A 505 1
HET MG A 503 1
HET NA E 601 1
HET NA F 601 1
HET MG B 401 1
HET NA B 402 1
HET NA B 403 1
HET NA B 404 1
HET MG C 401 1
HET MG C 402 1
HET MG D 401 1
HET NA D 402 1
HET NA N 601 1
HETNAM 3DR 1',2'-DIDEOXYRIBOFURANOSE-5'-PHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM NA SODIUM ION
HETSYN 3DR ABASIC DIDEOXYRIBOSE
FORMUL 3 3DR 4(C5 H11 O6 P)
FORMUL 17 MG 7(MG 2+)
FORMUL 19 NA 9(NA 1+)
FORMUL 33 HOH *272(H2 O)
HELIX 1 1 GLY A 71 LYS A 78 1 8
HELIX 2 2 LYS A 79 ALA A 88 1 10
HELIX 3 3 SER A 100 LEU A 104 5 5
HELIX 4 4 PRO A 105 LEU A 111 5 7
HELIX 5 5 ASP A 148 ASP A 152 5 5
HELIX 6 6 GLY A 176 VAL A 180 5 5
HELIX 7 7 ARG A 181 SER A 201 1 21
HELIX 8 8 GLU A 216 LEU A 220 5 5
HELIX 9 9 PRO A 223 LYS A 227 5 5
HELIX 10 10 THR A 233 VAL A 247 1 15
HELIX 11 11 SER A 252 TYR A 257 1 6
HELIX 12 12 TYR A 269 ALA A 273 5 5
HELIX 13 13 HIS A 289 PRO A 293 5 5
HELIX 14 14 GLY B 71 LYS B 78 1 8
HELIX 15 15 LYS B 79 ALA B 88 1 10
HELIX 16 16 PRO B 105 SER B 115 5 11
HELIX 17 17 GLY B 176 VAL B 180 5 5
HELIX 18 18 ARG B 181 ALA B 200 1 20
HELIX 19 19 GLU B 216 LEU B 220 5 5
HELIX 20 20 PRO B 223 LYS B 227 5 5
HELIX 21 21 THR B 233 GLN B 245 1 13
HELIX 22 22 SER B 252 TYR B 257 1 6
HELIX 23 23 ALA B 273 ASN B 277 5 5
HELIX 24 24 HIS B 289 LEU B 292 5 4
HELIX 25 25 GLY C 71 LYS C 78 1 8
HELIX 26 26 LYS C 79 ALA C 88 1 10
HELIX 27 27 SER C 100 LEU C 104 5 5
HELIX 28 28 PRO C 105 LEU C 111 5 7
HELIX 29 29 ASP C 148 ASP C 152 5 5
HELIX 30 30 GLY C 176 VAL C 180 5 5
HELIX 31 31 ARG C 181 SER C 201 1 21
HELIX 32 32 GLU C 216 LEU C 220 5 5
HELIX 33 33 PRO C 223 LYS C 227 5 5
HELIX 34 34 THR C 233 VAL C 247 1 15
HELIX 35 35 SER C 252 TYR C 257 1 6
HELIX 36 36 TYR C 269 ASN C 277 5 9
HELIX 37 37 HIS C 289 PRO C 293 5 5
HELIX 38 38 GLY D 71 LYS D 78 1 8
HELIX 39 39 LYS D 79 ALA D 88 1 10
HELIX 40 40 PRO D 105 SER D 115 5 11
HELIX 41 41 ARG D 181 LYS D 203 1 23
HELIX 42 42 GLU D 216 LEU D 220 5 5
HELIX 43 43 PRO D 223 LYS D 227 5 5
HELIX 44 44 THR D 233 VAL D 247 1 15
HELIX 45 45 SER D 252 TYR D 257 1 6
HELIX 46 46 TYR D 269 ALA D 273 5 5
HELIX 47 47 SER D 290 PRO D 293 5 4
SHEET 1 A 6 HIS A 116 SER A 120 0
SHEET 2 A 6 VAL A 131 SER A 135 -1 O LEU A 133 N TYR A 118
SHEET 3 A 6 ILE A 91 GLN A 95 -1 N LEU A 92 O LEU A 134
SHEET 4 A 6 LEU A 62 ASN A 68 1 N CYS A 65 O CYS A 93
SHEET 5 A 6 ILE A 312 LEU A 316 -1 O LEU A 314 N ILE A 64
SHEET 6 A 6 LEU A 295 ILE A 300 -1 N LYS A 299 O THR A 313
SHEET 1 B 6 LYS A 141 TYR A 144 0
SHEET 2 B 6 VAL A 157 GLU A 161 -1 O GLU A 161 N LYS A 141
SHEET 3 B 6 VAL A 166 TYR A 171 -1 O LEU A 167 N ALA A 160
SHEET 4 B 6 LEU A 205 ASP A 210 1 O VAL A 206 N VAL A 168
SHEET 5 B 6 ASP A 283 LEU A 287 -1 O LEU A 286 N LEU A 207
SHEET 6 B 6 ALA A 250 ASP A 251 -1 N ALA A 250 O LEU A 287
SHEET 1 C 6 HIS B 116 SER B 120 0
SHEET 2 C 6 VAL B 131 SER B 135 -1 O VAL B 131 N SER B 120
SHEET 3 C 6 ILE B 91 GLN B 95 -1 N LEU B 92 O LEU B 134
SHEET 4 C 6 LEU B 62 ASN B 68 1 N CYS B 65 O ILE B 91
SHEET 5 C 6 ILE B 312 LEU B 316 -1 O LEU B 314 N ILE B 64
SHEET 6 C 6 LEU B 295 SER B 298 -1 N ASP B 297 O TYR B 315
SHEET 1 D 6 LYS B 141 TYR B 144 0
SHEET 2 D 6 VAL B 157 GLU B 161 -1 O GLU B 161 N LYS B 141
SHEET 3 D 6 VAL B 166 ALA B 170 -1 O LEU B 167 N ALA B 160
SHEET 4 D 6 LEU B 205 ASP B 210 1 O VAL B 206 N VAL B 166
SHEET 5 D 6 ASP B 283 LEU B 287 -1 O LEU B 286 N LEU B 207
SHEET 6 D 6 ALA B 250 ASP B 251 -1 N ALA B 250 O LEU B 287
SHEET 1 E 6 HIS C 116 SER C 120 0
SHEET 2 E 6 VAL C 131 SER C 135 -1 O LEU C 133 N TYR C 118
SHEET 3 E 6 ILE C 91 GLN C 95 -1 N LEU C 92 O LEU C 134
SHEET 4 E 6 LEU C 62 ASN C 68 1 N CYS C 65 O CYS C 93
SHEET 5 E 6 ILE C 312 LEU C 316 -1 O LEU C 314 N ILE C 64
SHEET 6 E 6 LEU C 295 ILE C 300 -1 N LYS C 299 O THR C 313
SHEET 1 F 6 LYS C 141 TYR C 144 0
SHEET 2 F 6 VAL C 157 GLU C 161 -1 O GLU C 161 N LYS C 141
SHEET 3 F 6 VAL C 166 TYR C 171 -1 O LEU C 167 N ALA C 160
SHEET 4 F 6 LEU C 205 ASP C 210 1 O CYS C 208 N VAL C 168
SHEET 5 F 6 ASP C 283 LEU C 287 -1 O LEU C 286 N LEU C 207
SHEET 6 F 6 ALA C 250 ASP C 251 -1 N ALA C 250 O LEU C 287
SHEET 1 G 6 HIS D 116 SER D 120 0
SHEET 2 G 6 VAL D 131 SER D 135 -1 O LEU D 133 N TYR D 118
SHEET 3 G 6 ILE D 91 GLN D 95 -1 N LEU D 94 O GLY D 132
SHEET 4 G 6 LEU D 62 ASN D 68 1 N CYS D 65 O ILE D 91
SHEET 5 G 6 ILE D 312 LEU D 316 -1 O LEU D 314 N ILE D 64
SHEET 6 G 6 LEU D 295 ILE D 300 -1 N LYS D 299 O THR D 313
SHEET 1 H 6 LYS D 141 TYR D 144 0
SHEET 2 H 6 VAL D 157 GLU D 161 -1 O VAL D 159 N SER D 143
SHEET 3 H 6 VAL D 166 TYR D 171 -1 O LEU D 167 N ALA D 160
SHEET 4 H 6 LEU D 205 ASP D 210 1 O VAL D 206 N VAL D 166
SHEET 5 H 6 ASP D 283 SER D 288 -1 O LEU D 286 N LEU D 207
SHEET 6 H 6 LEU D 249 ASP D 251 -1 N ALA D 250 O LEU D 287
LINK O3' 3DR F 506 P DG F 507 1555 1555 1.61
LINK O3' 3DR I 506 P DG I 507 1555 1555 1.60
LINK O3' 3DR L 506 P DG L 507 1555 1555 1.61
LINK O3' 3DR O 506 P DG O 507 1555 1555 1.61
LINK O LEU A 44 NA NA A 505 1555 1555 2.35
LINK OE1 GLU A 96 MG MG A 502 1555 1555 2.45
LINK O TYR A 269 NA NA A 504 1555 1555 2.18
LINK MG MG A 501 O HOH A 641 1555 1555 2.07
LINK MG MG A 501 O2 DC E 505 1555 1555 2.03
LINK MG MG A 501 O2 DT G 519 1555 1555 2.74
LINK MG MG A 501 O HOH G 606 1555 1555 2.03
LINK MG MG A 502 O HOH A 601 1555 1555 2.18
LINK MG MG A 502 O HOH A 602 1555 1555 2.93
LINK MG MG A 502 O HOH A 603 1555 1555 1.92
LINK MG MG A 502 O3' DC E 505 1555 1555 2.23
LINK MG MG A 502 OP1 3DR F 506 1555 1555 2.05
LINK MG MG A 503 O2 DT L 509 1555 1555 2.15
LINK MG MG A 503 O2 DT M 515 1555 1555 2.27
LINK NA NA A 505 O HOH A 666 1555 1555 3.19
LINK OP2 DA E 504 NA NA E 601 1555 1555 2.21
LINK O5' DA E 504 NA NA E 601 1555 1555 3.06
LINK OP2 DC F 510 NA NA F 601 1555 1555 2.34
LINK OE1 GLU B 96 MG MG B 401 1555 1555 2.11
LINK OD1 ASP B 189 NA NA B 403 1555 1555 2.19
LINK OD2 ASP B 189 NA NA B 403 1555 1555 3.11
LINK O ASP B 189 NA NA B 404 1555 1555 2.20
LINK O GLU B 236 NA NA B 403 1555 1555 2.85
LINK OH TYR B 257 NA NA B 402 1555 1555 2.54
LINK O SER B 298 NA NA B 402 1555 1555 2.47
LINK MG MG B 401 O HOH B 502 1555 1555 2.91
LINK MG MG B 401 O HOH B 503 1555 1555 2.11
LINK MG MG B 401 O3' DC H 505 1555 1555 2.12
LINK MG MG B 401 OP1 3DR I 506 1555 1555 2.40
LINK MG MG B 401 O HOH I 601 1555 1555 2.06
LINK OE1 GLU C 96 MG MG C 401 1555 1555 2.49
LINK MG MG C 401 O HOH C 601 1555 1555 2.40
LINK MG MG C 401 O HOH C 602 1555 1555 1.94
LINK MG MG C 401 O3' DC K 505 1555 1555 1.89
LINK MG MG C 401 O HOH K 701 1555 1555 2.40
LINK MG MG C 401 OP1 3DR L 506 1555 1555 2.14
LINK MG MG C 402 O HOH C 614 1555 1555 2.15
LINK MG MG C 402 O HOH C 668 1555 1555 2.18
LINK MG MG C 402 O2 DC K 505 1555 1555 2.24
LINK MG MG C 402 O HOH K 701 1555 1555 2.32
LINK OE1 GLU D 96 MG MG D 401 1555 1555 2.42
LINK MG MG D 401 O HOH D 501 1555 1555 2.36
LINK MG MG D 401 O HOH D 502 1555 1555 1.86
LINK MG MG D 401 O3' DC N 505 1555 1555 1.83
LINK MG MG D 401 O HOH N 701 1555 1555 2.25
LINK MG MG D 401 OP1 3DR O 506 1555 1555 2.42
LINK NA NA D 402 OP2 DT O 509 1555 1555 2.25
LINK OP2 DA N 504 NA NA N 601 1555 1555 2.38
LINK O5' DA N 504 NA NA N 601 1555 1555 3.03
CISPEP 1 VAL A 247 PRO A 248 0 -0.06
CISPEP 2 VAL B 247 PRO B 248 0 -4.99
CISPEP 3 VAL C 247 PRO C 248 0 -4.57
CISPEP 4 VAL D 247 PRO D 248 0 -0.98
SITE 1 AC1 5 HOH A 641 DC E 505 DG G 518 DT G 519
SITE 2 AC1 5 HOH G 606
SITE 1 AC2 6 GLU A 96 HOH A 601 HOH A 602 HOH A 603
SITE 2 AC2 6 DC E 505 3DR F 506
SITE 1 AC3 2 DT L 509 DT M 515
SITE 1 AC4 5 TYR A 269 MET A 270 MET A 271 ASN A 272
SITE 2 AC4 5 DG G 518
SITE 1 AC5 2 LEU A 44 TYR A 45
SITE 1 AC6 6 GLU B 96 HOH B 502 HOH B 503 DC H 505
SITE 2 AC6 6 3DR I 506 HOH I 601
SITE 1 AC7 4 ASP B 47 TYR B 257 SER B 298 LYS B 299
SITE 1 AC8 4 ARG B 185 ASP B 189 VAL B 213 GLU B 236
SITE 1 AC9 3 ASP B 189 ARG B 193 LEU B 243
SITE 1 BC1 6 GLU C 96 HOH C 601 HOH C 602 DC K 505
SITE 2 BC1 6 HOH K 701 3DR L 506
SITE 1 BC2 7 ASP C 70 HOH C 614 HOH C 668 DC K 505
SITE 2 BC2 7 HOH K 701 DG M 518 DT M 519
SITE 1 BC3 6 GLU D 96 HOH D 501 HOH D 502 DC N 505
SITE 2 BC3 6 HOH N 701 3DR O 506
SITE 1 BC4 2 ASN D 222 DT O 509
SITE 1 BC5 2 DT E 503 DA E 504
SITE 1 BC6 1 DC F 510
SITE 1 BC7 2 DT N 503 DA N 504
CRYST1 104.639 74.090 112.138 90.00 111.98 90.00 P 1 21 1 8
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 0.009557 0.000000 0.003857 0.00000
SCALE2 0.000000 0.013497 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009617 0.00000
MTRIX1 1 -0.581627 -0.731172 -0.356507 53.39940 1
MTRIX2 1 -0.667779 0.178901 0.722541 -6.19556 1
MTRIX3 1 -0.464522 0.658317 -0.592315 33.68120 1
MTRIX1 2 0.894140 0.444622 0.053154 -57.40500 1
MTRIX2 2 -0.444112 0.865349 0.232241 -24.68810 1
MTRIX3 2 0.057262 -0.231262 0.971205 0.04294 1
MTRIX1 3 -0.798439 -0.580856 -0.158435 117.22000 1
MTRIX2 3 -0.532119 0.557681 0.637057 -5.88341 1
MTRIX3 3 -0.281682 0.592957 -0.754359 24.74960 1
MTRIX1 4 -0.581135 -0.727055 -0.365613 53.54450 1
MTRIX2 4 -0.680993 0.188478 0.707619 -5.39382 1
MTRIX3 4 -0.445568 0.660202 -0.604650 33.37850 1
MTRIX1 5 0.889803 0.453482 0.051039 -57.59540 1
MTRIX2 5 -0.452596 0.862652 0.225806 -23.88750 1
MTRIX3 5 0.058370 -0.224023 0.972834 -0.29516 1
MTRIX1 6 -0.798711 -0.580556 -0.158163 117.25900 1
MTRIX2 6 -0.533259 0.561187 0.633012 -5.82706 1
MTRIX3 6 -0.278740 0.589935 -0.757813 24.80110 1
MTRIX1 7 -0.549254 -0.759527 -0.348481 52.46090 1
MTRIX2 7 -0.689030 0.175673 0.703120 -4.46962 1
MTRIX3 7 -0.472819 0.626305 -0.619826 35.90550 1
MTRIX1 8 0.910785 0.411567 0.032910 -56.40980 1
MTRIX2 8 -0.407280 0.882488 0.235241 -26.81700 1
MTRIX3 8 0.067775 -0.227658 0.971380 -0.35956 1
MTRIX1 9 -0.789146 -0.597013 -0.144306 116.92100 1
MTRIX2 9 -0.548883 0.580038 0.601900 -4.34031 1
MTRIX3 9 -0.275639 0.554194 -0.785425 27.87340 1
MTRIX1 10 -0.593273 -0.733033 -0.332699 53.01830 1
MTRIX2 10 -0.655148 0.199514 0.728680 -7.43813 1
MTRIX3 10 -0.467769 0.650274 -0.598612 34.38800 1
MTRIX1 11 0.875337 0.481549 0.043544 -58.13220 1
MTRIX2 11 -0.476317 0.843325 0.248850 -22.28730 1
MTRIX3 11 0.083112 -0.238568 0.967563 -0.46497 1
MTRIX1 12 -0.803601 -0.581267 -0.127887 116.57400 1
MTRIX2 12 -0.519189 0.579585 0.628112 -8.06579 1
MTRIX3 12 -0.290979 0.571149 -0.767542 27.69070 1
MTRIX1 13 -0.572453 -0.734266 -0.364897 53.26990 1
MTRIX2 13 -0.666090 0.156934 0.729175 -5.83705 1
MTRIX3 13 -0.478144 0.660473 -0.578925 33.82870 1
MTRIX1 14 0.876780 0.478297 0.049890 -57.88220 1
MTRIX2 14 -0.477268 0.852767 0.212139 -22.35610 1
MTRIX3 14 0.058921 -0.209810 0.975965 -0.89294 1
MTRIX1 15 -0.783895 -0.595282 -0.176489 117.12000 1
MTRIX2 15 -0.544635 0.522764 0.655813 -2.90258 1
MTRIX3 15 -0.298132 0.610211 -0.734003 24.95920 1
(ATOM LINES ARE NOT SHOWN.)
END
