HEADER DNA BINDING PROTEIN 19-NOV-18 6I8A
TITLE THE CRYSTAL STRUCTURE OF THE POL2 CATALYTIC DOMAIN OF DNA POLYMERASE
TITLE 2 EPSILON CARRYING A P301R SUBSTITUTION.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DNA POLYMERASE II SUBUNIT A;
COMPND 5 EC: 2.7.7.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PRIMER DNA;
COMPND 10 CHAIN: P, C;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: TEMPLATE DNA;
COMPND 14 CHAIN: T, D;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: POL2, DUN2, YNL262W, N0825;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 13 ORGANISM_TAXID: 32630;
SOURCE 14 MOL_ID: 3;
SOURCE 15 SYNTHETIC: YES;
SOURCE 16 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 17 ORGANISM_TAXID: 32630
KEYWDS DNA, POL2, P301R, P286R, CANCER, ENDOMETRIAL, DNA BINDING PROTEIN,
KEYWDS 2 POL EPSILON
EXPDTA X-RAY DIFFRACTION
AUTHOR V.PARKASH,E.JOHANSSON
REVDAT 3 24-JAN-24 6I8A 1 REMARK LINK
REVDAT 2 06-FEB-19 6I8A 1 JRNL
REVDAT 1 30-JAN-19 6I8A 0
JRNL AUTH V.PARKASH,Y.KULKARNI,J.TER BEEK,P.V.SHCHERBAKOVA,
JRNL AUTH 2 S.C.L.KAMERLIN,E.JOHANSSON
JRNL TITL STRUCTURAL CONSEQUENCE OF THE MOST FREQUENTLY RECURRING
JRNL TITL 2 CANCER-ASSOCIATED SUBSTITUTION IN DNA POLYMERASE EPSILON.
JRNL REF NAT COMMUN V. 10 373 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 30670696
JRNL DOI 10.1038/S41467-018-08114-9
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 90534
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 4564
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 19.9577 - 8.0611 0.97 2943 175 0.1605 0.1893
REMARK 3 2 8.0611 - 6.4700 0.99 2920 173 0.1971 0.2465
REMARK 3 3 6.4700 - 5.6736 1.00 2939 169 0.2102 0.2931
REMARK 3 4 5.6736 - 5.1647 1.00 2924 157 0.1929 0.2569
REMARK 3 5 5.1647 - 4.8001 1.00 2915 148 0.1957 0.2331
REMARK 3 6 4.8001 - 4.5205 1.00 2941 143 0.1871 0.2507
REMARK 3 7 4.5205 - 4.2965 1.00 2877 164 0.1903 0.2542
REMARK 3 8 4.2965 - 4.1112 1.00 2909 143 0.2043 0.2541
REMARK 3 9 4.1112 - 3.9542 1.00 2869 155 0.2202 0.2524
REMARK 3 10 3.9542 - 3.8187 0.99 2919 144 0.2295 0.3059
REMARK 3 11 3.8187 - 3.7001 0.99 2862 137 0.2484 0.3114
REMARK 3 12 3.7001 - 3.5949 0.99 2892 163 0.2464 0.3057
REMARK 3 13 3.5949 - 3.5008 1.00 2873 158 0.2411 0.2937
REMARK 3 14 3.5008 - 3.4158 0.99 2881 161 0.2461 0.2987
REMARK 3 15 3.4158 - 3.3385 1.00 2830 140 0.2532 0.2990
REMARK 3 16 3.3385 - 3.2678 1.00 2909 165 0.2794 0.3220
REMARK 3 17 3.2678 - 3.2027 0.99 2880 143 0.2887 0.3896
REMARK 3 18 3.2027 - 3.1425 0.99 2903 132 0.2907 0.3085
REMARK 3 19 3.1425 - 3.0866 1.00 2882 148 0.2927 0.3158
REMARK 3 20 3.0866 - 3.0344 0.99 2849 159 0.3032 0.3729
REMARK 3 21 3.0344 - 2.9857 0.99 2914 145 0.3132 0.3179
REMARK 3 22 2.9857 - 2.9399 1.00 2836 155 0.3092 0.3646
REMARK 3 23 2.9399 - 2.8968 1.00 2874 142 0.3189 0.3479
REMARK 3 24 2.8968 - 2.8561 1.00 2896 163 0.3168 0.3901
REMARK 3 25 2.8561 - 2.8176 1.00 2842 148 0.3440 0.3772
REMARK 3 26 2.8176 - 2.7811 1.00 2895 152 0.3483 0.4140
REMARK 3 27 2.7811 - 2.7464 0.99 2880 154 0.3480 0.3740
REMARK 3 28 2.7464 - 2.7134 0.99 2805 171 0.3617 0.3715
REMARK 3 29 2.7134 - 2.6819 0.97 2821 142 0.3807 0.4617
REMARK 3 30 2.6819 - 2.6519 0.79 2290 115 0.3934 0.4136
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.770
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 72.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 78.01
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 6I8A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1200012981.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5-7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : SI (111) SILICON CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91152
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 19.957
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.422
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.45
REMARK 200 R MERGE FOR SHELL (I) : 1.20300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.890
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4M8O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES PH 6.5, 150MM NAAC, 8%PEG20K,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 6530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P, T
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 6380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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 GLY A -4
REMARK 465 GLY A -3
REMARK 465 ASP A -2
REMARK 465 PRO A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 MET A 2
REMARK 465 PHE A 3
REMARK 465 GLY A 4
REMARK 465 LYS A 5
REMARK 465 LYS A 6
REMARK 465 LYS A 7
REMARK 465 ASN A 8
REMARK 465 ASN A 9
REMARK 465 GLY A 10
REMARK 465 GLY A 11
REMARK 465 SER A 12
REMARK 465 SER A 13
REMARK 465 THR A 14
REMARK 465 ALA A 15
REMARK 465 ARG A 16
REMARK 465 TYR A 17
REMARK 465 SER A 18
REMARK 465 ALA A 19
REMARK 465 GLY A 20
REMARK 465 ASN A 21
REMARK 465 LYS A 22
REMARK 465 TYR A 23
REMARK 465 ASN A 24
REMARK 465 THR A 25
REMARK 465 LEU A 26
REMARK 465 SER A 27
REMARK 465 ASN A 28
REMARK 465 ASN A 29
REMARK 465 TYR A 30
REMARK 465 THR A 91
REMARK 465 LEU A 92
REMARK 465 SER A 93
REMARK 465 SER A 94
REMARK 465 GLY A 95
REMARK 465 SER A 96
REMARK 465 ASN A 97
REMARK 465 GLY A 98
REMARK 465 GLY A 99
REMARK 465 GLY A 100
REMARK 465 ASN A 101
REMARK 465 SER A 102
REMARK 465 ASN A 103
REMARK 465 ASP A 104
REMARK 465 GLY A 105
REMARK 465 GLU A 106
REMARK 465 ARG A 107
REMARK 465 VAL A 108
REMARK 465 THR A 109
REMARK 465 THR A 110
REMARK 465 VAL A 225
REMARK 465 ALA A 226
REMARK 465 ALA A 227
REMARK 465 ASN A 228
REMARK 465 GLY A 229
REMARK 465 SER A 230
REMARK 465 GLU A 231
REMARK 465 LYS A 232
REMARK 465 ARG A 663
REMARK 465 ASP A 664
REMARK 465 CYS A 665
REMARK 465 ALA A 666
REMARK 465 SER A 667
REMARK 465 CYS A 668
REMARK 465 ASP A 669
REMARK 465 PHE A 670
REMARK 465 ASN A 671
REMARK 465 ARG A 672
REMARK 465 PRO A 673
REMARK 465 GLY A 674
REMARK 465 LYS A 675
REMARK 465 LYS A 714
REMARK 465 PHE A 715
REMARK 465 SER A 716
REMARK 465 LYS A 717
REMARK 465 LYS A 718
REMARK 465 LYS A 719
REMARK 465 VAL A 720
REMARK 465 DC T 1
REMARK 465 GLY B -4
REMARK 465 GLY B -3
REMARK 465 ASP B -2
REMARK 465 PRO B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 MET B 2
REMARK 465 PHE B 3
REMARK 465 GLY B 4
REMARK 465 LYS B 5
REMARK 465 LYS B 6
REMARK 465 LYS B 7
REMARK 465 ASN B 8
REMARK 465 ASN B 9
REMARK 465 GLY B 10
REMARK 465 GLY B 11
REMARK 465 SER B 12
REMARK 465 SER B 13
REMARK 465 THR B 14
REMARK 465 ALA B 15
REMARK 465 ARG B 16
REMARK 465 TYR B 17
REMARK 465 SER B 18
REMARK 465 ALA B 19
REMARK 465 GLY B 20
REMARK 465 ASN B 21
REMARK 465 LYS B 22
REMARK 465 TYR B 23
REMARK 465 ASN B 24
REMARK 465 THR B 25
REMARK 465 LEU B 26
REMARK 465 SER B 27
REMARK 465 ASN B 28
REMARK 465 GLU B 90
REMARK 465 THR B 91
REMARK 465 LEU B 92
REMARK 465 SER B 93
REMARK 465 SER B 94
REMARK 465 GLY B 95
REMARK 465 SER B 96
REMARK 465 ASN B 97
REMARK 465 GLY B 98
REMARK 465 GLY B 99
REMARK 465 GLY B 100
REMARK 465 ASN B 101
REMARK 465 SER B 102
REMARK 465 ASN B 103
REMARK 465 ASP B 104
REMARK 465 GLY B 105
REMARK 465 GLU B 106
REMARK 465 ARG B 107
REMARK 465 VAL B 108
REMARK 465 THR B 109
REMARK 465 THR B 110
REMARK 465 ASN B 111
REMARK 465 VAL B 225
REMARK 465 ALA B 226
REMARK 465 ALA B 227
REMARK 465 ASN B 228
REMARK 465 GLY B 229
REMARK 465 SER B 230
REMARK 465 GLU B 231
REMARK 465 LYS B 232
REMARK 465 ALA B 661
REMARK 465 GLU B 662
REMARK 465 ARG B 663
REMARK 465 ASP B 664
REMARK 465 CYS B 665
REMARK 465 ALA B 666
REMARK 465 SER B 667
REMARK 465 CYS B 668
REMARK 465 ASP B 669
REMARK 465 PHE B 670
REMARK 465 ASN B 671
REMARK 465 ARG B 672
REMARK 465 PRO B 673
REMARK 465 GLY B 674
REMARK 465 LYS B 675
REMARK 465 ASN B 713
REMARK 465 LYS B 714
REMARK 465 PHE B 715
REMARK 465 SER B 716
REMARK 465 LYS B 717
REMARK 465 LYS B 718
REMARK 465 LYS B 719
REMARK 465 VAL B 720
REMARK 465 LEU B 721
REMARK 465 SER B 743
REMARK 465 ARG B 744
REMARK 465 LYS B 745
REMARK 465 VAL B 746
REMARK 465 TYR B 747
REMARK 465 HIS B 748
REMARK 465 ARG B 749
REMARK 465 VAL B 750
REMARK 465 LYS B 751
REMARK 465 DC D 1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 32 CG CD1 CD2
REMARK 470 LYS A 42 CG CD CE NZ
REMARK 470 GLU A 53 CD OE1 OE2
REMARK 470 GLN A 59 CG CD OE1 NE2
REMARK 470 ASN A 61 CG OD1 ND2
REMARK 470 ARG A 63 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 64 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 67 CG CD CE NZ
REMARK 470 GLN A 89 CG CD OE1 NE2
REMARK 470 ASN A 111 CG OD1 ND2
REMARK 470 GLN A 112 CD OE1 NE2
REMARK 470 GLU A 125 CB CG CD OE1 OE2
REMARK 470 GLU A 154 CG CD OE1 OE2
REMARK 470 LYS A 157 CG CD CE NZ
REMARK 470 GLU A 161 CG CD OE1 OE2
REMARK 470 SER A 162 OG
REMARK 470 GLN A 198 CD OE1 NE2
REMARK 470 GLU A 201 CG CD OE1 OE2
REMARK 470 LYS A 204 CG CD CE NZ
REMARK 470 ARG A 207 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 211 CG CD OE1 NE2
REMARK 470 ASN A 217 OD1 ND2
REMARK 470 VAL A 218 CG1 CG2
REMARK 470 GLN A 219 CG CD OE1 NE2
REMARK 470 ARG A 220 NE CZ NH1 NH2
REMARK 470 ASP A 234 CG OD1 OD2
REMARK 470 LYS A 236 CG CD CE NZ
REMARK 470 HIS A 237 ND1 CD2 CE1 NE2
REMARK 470 GLU A 240 CD OE1 OE2
REMARK 470 LYS A 257 CD CE NZ
REMARK 470 LYS A 266 CE NZ
REMARK 470 GLN A 269 CG CD OE1 NE2
REMARK 470 LEU A 298 CG CD1 CD2
REMARK 470 LYS A 299 CG CD CE NZ
REMARK 470 GLN A 307 CG CD OE1 NE2
REMARK 470 GLU A 318 CD OE1 OE2
REMARK 470 ARG A 325 CD NE CZ NH1 NH2
REMARK 470 GLU A 333 CG CD OE1 OE2
REMARK 470 LYS A 340 CD CE NZ
REMARK 470 PHE A 346 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 440 CE NZ
REMARK 470 PHE A 464 CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 466 CG CD CE NZ
REMARK 470 GLU A 472 CG CD OE1 OE2
REMARK 470 LYS A 487 CD CE NZ
REMARK 470 ASP A 537 CG OD1 OD2
REMARK 470 ARG A 541 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 549 CG CD OE1 OE2
REMARK 470 LYS A 571 CE NZ
REMARK 470 GLU A 573 CG CD OE1 OE2
REMARK 470 LYS A 575 CG CD CE NZ
REMARK 470 GLN A 586 CG CD OE1 NE2
REMARK 470 GLU A 597 CG CD OE1 OE2
REMARK 470 LYS A 601 CE NZ
REMARK 470 LYS A 606 CG CD CE NZ
REMARK 470 ILE A 613 CD1
REMARK 470 LEU A 622 CD1 CD2
REMARK 470 LYS A 625 CD CE NZ
REMARK 470 GLU A 626 CD OE1 OE2
REMARK 470 GLU A 632 CG CD OE1 OE2
REMARK 470 LYS A 660 CG CD CE NZ
REMARK 470 GLU A 662 CD OE1 OE2
REMARK 470 LYS A 682 CD CE NZ
REMARK 470 GLU A 688 CD OE1 OE2
REMARK 470 LYS A 693 CG CD CE NZ
REMARK 470 ASP A 695 CG OD1 OD2
REMARK 470 ILE A 700 CG1 CG2 CD1
REMARK 470 LYS A 701 CG CD CE NZ
REMARK 470 ARG A 702 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 704 CG CD1 CD2
REMARK 470 GLN A 705 CG CD OE1 NE2
REMARK 470 ASN A 706 CB CG OD1 ND2
REMARK 470 THR A 708 OG1 CG2
REMARK 470 ASN A 711 CG OD1 ND2
REMARK 470 LYS A 712 CG CD CE NZ
REMARK 470 GLU A 725 CG CD OE1 OE2
REMARK 470 ILE A 733 CB CG1 CG2 CD1
REMARK 470 ILE A 735 CG1 CG2 CD1
REMARK 470 LYS A 736 CG CD CE NZ
REMARK 470 LYS A 737 CG CD CE NZ
REMARK 470 ARG A 738 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 739 CG CD1 CD2
REMARK 470 THR A 740 OG1 CG2
REMARK 470 GLU A 741 CG CD OE1 OE2
REMARK 470 TYR A 742 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 745 CG CD CE NZ
REMARK 470 HIS A 748 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 751 CD CE NZ
REMARK 470 LYS A 775 CD CE NZ
REMARK 470 LYS A 792 NZ
REMARK 470 SER A 796 OG
REMARK 470 LYS A 797 CB CG CD CE NZ
REMARK 470 ILE A 798 CB CG1 CG2 CD1
REMARK 470 ASP A 799 CG OD1 OD2
REMARK 470 SER A 801 OG
REMARK 470 ASP A 802 CG OD1 OD2
REMARK 470 LYS A 803 CG CD CE NZ
REMARK 470 LYS A 810 CG CD CE NZ
REMARK 470 LYS A 811 CG CD CE NZ
REMARK 470 LYS A 837 CD CE NZ
REMARK 470 LYS A 885 CD CE NZ
REMARK 470 GLU A 896 CG CD OE1 OE2
REMARK 470 ASN A 897 OD1 ND2
REMARK 470 LYS A 899 CG CD CE NZ
REMARK 470 GLN A 916 CG CD OE1 NE2
REMARK 470 LYS A 917 CD CE NZ
REMARK 470 LYS A 927 CD CE NZ
REMARK 470 LYS A 959 CD CE NZ
REMARK 470 GLU A 960 OE1 OE2
REMARK 470 LYS A 963 CD CE NZ
REMARK 470 GLU A 980 OE1 OE2
REMARK 470 LYS A 996 CG CD CE NZ
REMARK 470 LYS A1004 CE NZ
REMARK 470 GLU A1013 CG CD OE1 OE2
REMARK 470 SER A1017 OG
REMARK 470 SER A1021 OG
REMARK 470 ARG A1025 CD NE CZ NH1 NH2
REMARK 470 GLU A1038 CD OE1 OE2
REMARK 470 GLU A1040 CD OE1 OE2
REMARK 470 GLU A1060 CG CD OE1 OE2
REMARK 470 LYS A1063 CG CD CE NZ
REMARK 470 LYS A1085 CG CD CE NZ
REMARK 470 LYS A1090 CG CD CE NZ
REMARK 470 LYS A1096 CG CD CE NZ
REMARK 470 GLU A1104 OE1 OE2
REMARK 470 ASP A1115 CG OD1 OD2
REMARK 470 ARG A1120 CD NE CZ NH1 NH2
REMARK 470 ARG A1125 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1133 CG CD OE1 OE2
REMARK 470 ASP A1136 CG OD1 OD2
REMARK 470 GLU A1148 CD OE1 OE2
REMARK 470 GLU A1175 CG CD OE1 OE2
REMARK 470 LYS A1181 NZ
REMARK 470 LYS A1183 CG CD CE NZ
REMARK 470 DT P 1 C7
REMARK 470 ASN B 29 CG OD1 ND2
REMARK 470 TYR B 30 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 42 CD CE NZ
REMARK 470 GLU B 53 CG CD OE1 OE2
REMARK 470 GLN B 59 CG CD OE1 NE2
REMARK 470 ARG B 63 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 64 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 67 CG CD CE NZ
REMARK 470 GLN B 71 CG CD OE1 NE2
REMARK 470 GLN B 89 CG CD OE1 NE2
REMARK 470 GLU B 125 CG CD OE1 OE2
REMARK 470 ASN B 150 OD1 ND2
REMARK 470 GLU B 153 CG CD OE1 OE2
REMARK 470 GLU B 154 CG CD OE1 OE2
REMARK 470 LYS B 157 CG CD CE NZ
REMARK 470 LYS B 158 CG CD CE NZ
REMARK 470 GLU B 161 CD OE1 OE2
REMARK 470 ILE B 170 CD1
REMARK 470 GLU B 201 CG CD OE1 OE2
REMARK 470 LYS B 204 CG CD CE NZ
REMARK 470 ARG B 207 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 211 CD OE1 NE2
REMARK 470 ASN B 215 CG OD1 ND2
REMARK 470 VAL B 218 CG1 CG2
REMARK 470 GLN B 219 CG CD OE1 NE2
REMARK 470 ARG B 220 CD NE CZ NH1 NH2
REMARK 470 LYS B 236 CG CD CE NZ
REMARK 470 GLU B 240 CG CD OE1 OE2
REMARK 470 LYS B 266 CG CD CE NZ
REMARK 470 GLN B 269 CG CD OE1 NE2
REMARK 470 LYS B 299 CG CD CE NZ
REMARK 470 GLU B 318 OE1 OE2
REMARK 470 ILE B 322 CG1 CG2 CD1
REMARK 470 ARG B 325 CD NE CZ NH1 NH2
REMARK 470 GLU B 330 CG CD OE1 OE2
REMARK 470 GLU B 333 CG CD OE1 OE2
REMARK 470 LYS B 340 CG CD CE NZ
REMARK 470 PHE B 346 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 364 OE1 OE2
REMARK 470 ASP B 368 CG OD1 OD2
REMARK 470 GLU B 409 CD OE1 OE2
REMARK 470 LYS B 440 CG CD CE NZ
REMARK 470 GLU B 457 OE1 OE2
REMARK 470 PHE B 464 CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 466 CD CE NZ
REMARK 470 GLN B 468 CD OE1 NE2
REMARK 470 HIS B 469 ND1 CD2 CE1 NE2
REMARK 470 GLU B 472 CG CD OE1 OE2
REMARK 470 SER B 474 OG
REMARK 470 VAL B 479 CG1 CG2
REMARK 470 LYS B 487 CG CD CE NZ
REMARK 470 ASP B 537 CG OD1 OD2
REMARK 470 ILE B 539 CD1
REMARK 470 ARG B 541 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 549 CG CD OE1 OE2
REMARK 470 LYS B 571 CG CD CE NZ
REMARK 470 GLU B 573 CG CD OE1 OE2
REMARK 470 LYS B 575 CG CD CE NZ
REMARK 470 ASP B 582 CG OD1 OD2
REMARK 470 LYS B 593 CG CD CE NZ
REMARK 470 GLU B 597 CD OE1 OE2
REMARK 470 GLU B 599 CG CD OE1 OE2
REMARK 470 LYS B 601 CG CD CE NZ
REMARK 470 LYS B 606 CD CE NZ
REMARK 470 GLU B 612 OE1 OE2
REMARK 470 ASN B 615 CB CG OD1 ND2
REMARK 470 GLN B 619 CG CD OE1 NE2
REMARK 470 LEU B 621 CG CD1 CD2
REMARK 470 LEU B 622 CB CG CD1 CD2
REMARK 470 GLU B 623 CG CD OE1 OE2
REMARK 470 LEU B 624 CG CD1 CD2
REMARK 470 LYS B 625 CD CE NZ
REMARK 470 GLU B 626 CG CD OE1 OE2
REMARK 470 ASN B 628 OD1 ND2
REMARK 470 GLU B 632 CG CD OE1 OE2
REMARK 470 LYS B 680 CG CD CE NZ
REMARK 470 LYS B 682 CG CD CE NZ
REMARK 470 GLU B 688 CG CD OE1 OE2
REMARK 470 LYS B 693 CG CD CE NZ
REMARK 470 ASP B 695 CB CG OD1 OD2
REMARK 470 TYR B 697 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN B 698 CG OD1 ND2
REMARK 470 MET B 699 CG SD CE
REMARK 470 ILE B 700 CG1 CG2 CD1
REMARK 470 LYS B 701 CB CG CD CE NZ
REMARK 470 ARG B 702 CB CG CD NE CZ NH1 NH2
REMARK 470 LEU B 704 CG CD1 CD2
REMARK 470 GLN B 705 CG CD OE1 NE2
REMARK 470 ASN B 706 CG OD1 ND2
REMARK 470 GLU B 707 CG CD OE1 OE2
REMARK 470 PHE B 709 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN B 711 CG OD1 ND2
REMARK 470 LYS B 712 CG CD CE NZ
REMARK 470 GLU B 725 CG CD OE1 OE2
REMARK 470 LEU B 726 CG CD1 CD2
REMARK 470 LYS B 736 CG CD CE NZ
REMARK 470 LYS B 737 CG CD CE NZ
REMARK 470 ARG B 738 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 739 CG CD1 CD2
REMARK 470 LYS B 775 CD CE NZ
REMARK 470 GLU B 783 OE1 OE2
REMARK 470 LYS B 789 CD CE NZ
REMARK 470 LYS B 792 CD CE NZ
REMARK 470 LEU B 795 CG CD1 CD2
REMARK 470 SER B 796 OG
REMARK 470 LYS B 797 CG CD CE NZ
REMARK 470 ILE B 798 CG1 CG2 CD1
REMARK 470 ASP B 802 CG OD1 OD2
REMARK 470 LYS B 803 CE NZ
REMARK 470 LYS B 810 CG CD CE NZ
REMARK 470 LYS B 811 CG CD CE NZ
REMARK 470 LYS B 837 CD CE NZ
REMARK 470 LYS B 885 CG CD CE NZ
REMARK 470 SER B 886 OG
REMARK 470 PHE B 892 CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 896 CG CD OE1 OE2
REMARK 470 LYS B 899 CG CD CE NZ
REMARK 470 LYS B 900 CG CD CE NZ
REMARK 470 MET B 909 CG SD CE
REMARK 470 ARG B 913 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 917 CG CD CE NZ
REMARK 470 GLU B 925 CD OE1 OE2
REMARK 470 LYS B 927 CG CD CE NZ
REMARK 470 LYS B 951 CG CD CE NZ
REMARK 470 GLU B 960 CD OE1 OE2
REMARK 470 LYS B1004 CG CD CE NZ
REMARK 470 GLU B1013 CG CD OE1 OE2
REMARK 470 SER B1017 OG
REMARK 470 SER B1021 OG
REMARK 470 ARG B1025 CD NE CZ NH1 NH2
REMARK 470 LYS B1057 CD CE NZ
REMARK 470 GLU B1060 CG CD OE1 OE2
REMARK 470 LYS B1063 CG CD CE NZ
REMARK 470 LYS B1083 CG CD CE NZ
REMARK 470 LYS B1085 CD CE NZ
REMARK 470 LYS B1090 CD CE NZ
REMARK 470 LYS B1096 CG CD CE NZ
REMARK 470 PHE B1098 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN B1099 CG OD1 ND2
REMARK 470 GLU B1104 CG CD OE1 OE2
REMARK 470 ASP B1115 CG OD1 OD2
REMARK 470 ARG B1120 CD NE CZ NH1 NH2
REMARK 470 ARG B1124 CD NE CZ NH1 NH2
REMARK 470 ARG B1125 CG CD NE CZ NH1 NH2
REMARK 470 LEU B1132 CB CG CD1 CD2
REMARK 470 GLU B1133 CG CD OE1 OE2
REMARK 470 ASP B1134 CG OD1 OD2
REMARK 470 LEU B1135 CG CD1 CD2
REMARK 470 ASP B1136 CB CG OD1 OD2
REMARK 470 ILE B1140 CG1 CG2 CD1
REMARK 470 SER B1168 OG
REMARK 470 GLU B1175 CD OE1 OE2
REMARK 470 LYS B1183 CD CE NZ
REMARK 470 DT C 1 C7
REMARK 470 DT D 15 C7
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 DT P 1 P OP1 OP2 O5'
REMARK 480 DT C 1 P OP1 OP2 O5'
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 DT P 10 O3' DOC P 11 P -0.094
REMARK 500 DT C 10 O3' DOC C 11 P -0.077
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 DOC P 11 O3' - P - OP2 ANGL. DEV. = 19.2 DEGREES
REMARK 500 DG T 13 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG C 8 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DOC C 11 O3' - P - O5' ANGL. DEV. = 17.7 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 68 64.63 -118.27
REMARK 500 GLN A 89 66.80 -64.46
REMARK 500 LEU A 160 55.41 -99.23
REMARK 500 CYS A 163 -7.82 -147.27
REMARK 500 GLN A 168 147.15 174.67
REMARK 500 ARG A 220 -86.64 -115.99
REMARK 500 HIS A 237 8.51 -66.22
REMARK 500 ILE A 279 -65.88 -94.91
REMARK 500 LEU A 298 -8.55 68.54
REMARK 500 LYS A 299 -164.66 -103.68
REMARK 500 SER A 329 0.83 -66.96
REMARK 500 ASN A 353 -74.96 -71.34
REMARK 500 ARG A 370 68.90 64.34
REMARK 500 ASN A 378 15.61 57.06
REMARK 500 PHE A 382 -70.13 -96.81
REMARK 500 GLU A 465 -78.57 -72.93
REMARK 500 TYR A 488 -50.79 -125.06
REMARK 500 PRO A 501 46.20 -79.91
REMARK 500 ASP A 544 46.28 37.43
REMARK 500 GLN A 586 26.83 -79.59
REMARK 500 GLU A 587 -59.44 -138.59
REMARK 500 LEU A 588 -19.32 -46.95
REMARK 500 THR A 608 -69.30 -97.51
REMARK 500 ASN A 609 40.45 -77.70
REMARK 500 ASN A 627 64.71 -106.38
REMARK 500 ALA A 661 -159.19 -136.53
REMARK 500 LYS A 712 24.73 -143.31
REMARK 500 TYR A 747 -33.28 -132.46
REMARK 500 HIS A 748 -10.27 68.22
REMARK 500 ASN A 767 109.83 -45.71
REMARK 500 PRO A 768 35.30 -84.11
REMARK 500 ASP A 802 86.32 -65.65
REMARK 500 SER A 843 92.78 -163.79
REMARK 500 VAL A 868 -9.48 -146.38
REMARK 500 THR A 876 -60.23 53.06
REMARK 500 GLU A 889 -85.38 -116.53
REMARK 500 LYS A 899 -164.62 -74.54
REMARK 500 ASN A 940 114.34 -161.13
REMARK 500 ASP A1080 -5.88 -55.48
REMARK 500 VAL A1082 32.84 -99.66
REMARK 500 ASN A1099 16.76 58.99
REMARK 500 ARG A1105 50.66 -97.41
REMARK 500 PHE A1112 8.33 -66.13
REMARK 500 ALA B 66 3.52 -64.96
REMARK 500 ASP B 68 50.05 -119.87
REMARK 500 GLN B 168 149.29 -170.40
REMARK 500 GLN B 219 -75.12 -81.91
REMARK 500 ARG B 220 -127.24 58.46
REMARK 500 THR B 294 158.76 -47.87
REMARK 500 ILE B 327 -38.62 -130.05
REMARK 500
REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS.
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 CA A1303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 290 OD1
REMARK 620 2 ASP A 290 OD2 45.6
REMARK 620 3 GLU A 292 OE2 79.2 78.0
REMARK 620 4 ASP A 477 OD2 127.0 82.3 102.1
REMARK 620 5 HOH A1402 O 109.8 128.8 150.6 94.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 641 O
REMARK 620 2 ASP A 877 OD2 81.7
REMARK 620 3 DTP A1301 O3G 102.5 172.9
REMARK 620 4 DTP A1301 O2B 80.8 94.1 81.1
REMARK 620 5 DTP A1301 O2A 146.2 70.2 103.8 82.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A1304 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 677 SG
REMARK 620 2 CYS A 763 SG 87.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 290 OD1
REMARK 620 2 ASP B 290 OD2 43.7
REMARK 620 3 GLU B 292 OE1 104.1 69.6
REMARK 620 4 ASP B 477 OD2 101.4 85.9 106.3
REMARK 620 5 HOH B1401 O 62.5 101.1 114.3 138.7
REMARK 620 6 HOH B1403 O 98.6 140.9 145.4 94.2 55.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 640 OD1
REMARK 620 2 ASP B 640 OD2 46.8
REMARK 620 3 VAL B 641 O 99.8 84.1
REMARK 620 4 ASP B 877 OD2 64.4 107.5 87.7
REMARK 620 5 DTP B1301 O1G 119.6 80.5 101.8 168.4
REMARK 620 6 DTP B1301 O1B 152.9 159.6 93.0 92.5 80.4
REMARK 620 7 DTP B1301 O1A 79.4 107.8 161.0 74.8 94.9 80.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B1304 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 677 SG
REMARK 620 2 CYS B 763 SG 104.7
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 DTP A 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 1304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DTP B 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE B 1304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-nucleotide DT C 10 and DOC C
REMARK 800 11
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6FWK RELATED DB: PDB
REMARK 900 6FWK CONTAINS SAME PROTEIN WITH WILD TYPE EXONUCLEASE DOMAIN
REMARK 900 RELATED ID: 6G0A RELATED DB: PDB
REMARK 900 6G0A IS SAME MUTANT STRUCTURE AS THIS ONE.
DBREF 6I8A A 1 1185 UNP P21951 DPOE_YEAST 1 1185
DBREF 6I8A P 1 11 PDB 6I8A 6I8A 1 11
DBREF 6I8A T 1 16 PDB 6I8A 6I8A 1 16
DBREF 6I8A B 1 1185 UNP P21951 DPOE_YEAST 1 1185
DBREF 6I8A C 1 11 PDB 6I8A 6I8A 1 11
DBREF 6I8A D 1 16 PDB 6I8A 6I8A 1 16
SEQADV 6I8A GLY A -4 UNP P21951 EXPRESSION TAG
SEQADV 6I8A GLY A -3 UNP P21951 EXPRESSION TAG
SEQADV 6I8A ASP A -2 UNP P21951 EXPRESSION TAG
SEQADV 6I8A PRO A -1 UNP P21951 EXPRESSION TAG
SEQADV 6I8A HIS A 0 UNP P21951 EXPRESSION TAG
SEQADV 6I8A ARG A 301 UNP P21951 PRO 301 ENGINEERED MUTATION
SEQADV 6I8A GLY B -4 UNP P21951 EXPRESSION TAG
SEQADV 6I8A GLY B -3 UNP P21951 EXPRESSION TAG
SEQADV 6I8A ASP B -2 UNP P21951 EXPRESSION TAG
SEQADV 6I8A PRO B -1 UNP P21951 EXPRESSION TAG
SEQADV 6I8A HIS B 0 UNP P21951 EXPRESSION TAG
SEQADV 6I8A ARG B 301 UNP P21951 PRO 301 ENGINEERED MUTATION
SEQRES 1 A 1190 GLY GLY ASP PRO HIS MET MET PHE GLY LYS LYS LYS ASN
SEQRES 2 A 1190 ASN GLY GLY SER SER THR ALA ARG TYR SER ALA GLY ASN
SEQRES 3 A 1190 LYS TYR ASN THR LEU SER ASN ASN TYR ALA LEU SER ALA
SEQRES 4 A 1190 GLN GLN LEU LEU ASN ALA SER LYS ILE ASP ASP ILE ASP
SEQRES 5 A 1190 SER MET MET GLY PHE GLU ARG TYR VAL PRO PRO GLN TYR
SEQRES 6 A 1190 ASN GLY ARG PHE ASP ALA LYS ASP ILE ASP GLN ILE PRO
SEQRES 7 A 1190 GLY ARG VAL GLY TRP LEU THR ASN MET HIS ALA THR LEU
SEQRES 8 A 1190 VAL SER GLN GLU THR LEU SER SER GLY SER ASN GLY GLY
SEQRES 9 A 1190 GLY ASN SER ASN ASP GLY GLU ARG VAL THR THR ASN GLN
SEQRES 10 A 1190 GLY ILE SER GLY VAL ASP PHE TYR PHE LEU ASP GLU GLU
SEQRES 11 A 1190 GLY GLY SER PHE LYS SER THR VAL VAL TYR ASP PRO TYR
SEQRES 12 A 1190 PHE PHE ILE ALA CYS ASN ASP GLU SER ARG VAL ASN ASP
SEQRES 13 A 1190 VAL GLU GLU LEU VAL LYS LYS TYR LEU GLU SER CYS LEU
SEQRES 14 A 1190 LYS SER LEU GLN ILE ILE ARG LYS GLU ASP LEU THR MET
SEQRES 15 A 1190 ASP ASN HIS LEU LEU GLY LEU GLN LYS THR LEU ILE LYS
SEQRES 16 A 1190 LEU SER PHE VAL ASN SER ASN GLN LEU PHE GLU ALA ARG
SEQRES 17 A 1190 LYS LEU LEU ARG PRO ILE LEU GLN ASP ASN ALA ASN ASN
SEQRES 18 A 1190 ASN VAL GLN ARG ASN ILE TYR ASN VAL ALA ALA ASN GLY
SEQRES 19 A 1190 SER GLU LYS VAL ASP ALA LYS HIS LEU ILE GLU ASP ILE
SEQRES 20 A 1190 ARG GLU TYR ASP VAL PRO TYR HIS VAL ARG VAL SER ILE
SEQRES 21 A 1190 ASP LYS ASP ILE ARG VAL GLY LYS TRP TYR LYS VAL THR
SEQRES 22 A 1190 GLN GLN GLY PHE ILE GLU ASP THR ARG LYS ILE ALA PHE
SEQRES 23 A 1190 ALA ASP PRO VAL VAL MET ALA PHE ASP ILE GLU THR THR
SEQRES 24 A 1190 LYS PRO PRO LEU LYS PHE ARG ASP SER ALA VAL ASP GLN
SEQRES 25 A 1190 ILE MET MET ILE SER TYR MET ILE ASP GLY GLU GLY PHE
SEQRES 26 A 1190 LEU ILE THR ASN ARG GLU ILE ILE SER GLU ASP ILE GLU
SEQRES 27 A 1190 ASP PHE GLU TYR THR PRO LYS PRO GLU TYR PRO GLY PHE
SEQRES 28 A 1190 PHE THR ILE PHE ASN GLU ASN ASP GLU VAL ALA LEU LEU
SEQRES 29 A 1190 GLN ARG PHE PHE GLU HIS ILE ARG ASP VAL ARG PRO THR
SEQRES 30 A 1190 VAL ILE SER THR PHE ASN GLY ASP PHE PHE ASP TRP PRO
SEQRES 31 A 1190 PHE ILE HIS ASN ARG SER LYS ILE HIS GLY LEU ASP MET
SEQRES 32 A 1190 PHE ASP GLU ILE GLY PHE ALA PRO ASP ALA GLU GLY GLU
SEQRES 33 A 1190 TYR LYS SER SER TYR CYS SER HIS MET ASP CYS PHE ARG
SEQRES 34 A 1190 TRP VAL LYS ARG ASP SER TYR LEU PRO GLN GLY SER GLN
SEQRES 35 A 1190 GLY LEU LYS ALA VAL THR GLN SER LYS LEU GLY TYR ASN
SEQRES 36 A 1190 PRO ILE GLU LEU ASP PRO GLU LEU MET THR PRO TYR ALA
SEQRES 37 A 1190 PHE GLU LYS PRO GLN HIS LEU SER GLU TYR SER VAL SER
SEQRES 38 A 1190 ASP ALA VAL ALA THR TYR TYR LEU TYR MET LYS TYR VAL
SEQRES 39 A 1190 HIS PRO PHE ILE PHE SER LEU CYS THR ILE ILE PRO LEU
SEQRES 40 A 1190 ASN PRO ASP GLU THR LEU ARG LYS GLY THR GLY THR LEU
SEQRES 41 A 1190 CYS GLU MET LEU LEU MET VAL GLN ALA TYR GLN HIS ASN
SEQRES 42 A 1190 ILE LEU LEU PRO ASN LYS HIS THR ASP PRO ILE GLU ARG
SEQRES 43 A 1190 PHE TYR ASP GLY HIS LEU LEU GLU SER GLU THR TYR VAL
SEQRES 44 A 1190 GLY GLY HIS VAL GLU SER LEU GLU ALA GLY VAL PHE ARG
SEQRES 45 A 1190 SER ASP LEU LYS ASN GLU PHE LYS ILE ASP PRO SER ALA
SEQRES 46 A 1190 ILE ASP GLU LEU LEU GLN GLU LEU PRO GLU ALA LEU LYS
SEQRES 47 A 1190 PHE SER VAL GLU VAL GLU ASN LYS SER SER VAL ASP LYS
SEQRES 48 A 1190 VAL THR ASN PHE GLU GLU ILE LYS ASN GLN ILE THR GLN
SEQRES 49 A 1190 LYS LEU LEU GLU LEU LYS GLU ASN ASN ILE ARG ASN GLU
SEQRES 50 A 1190 LEU PRO LEU ILE TYR HIS VAL ASP VAL ALA SER MET TYR
SEQRES 51 A 1190 PRO ASN ILE MET THR THR ASN ARG LEU GLN PRO ASP SER
SEQRES 52 A 1190 ILE LYS ALA GLU ARG ASP CYS ALA SER CYS ASP PHE ASN
SEQRES 53 A 1190 ARG PRO GLY LYS THR CYS ALA ARG LYS LEU LYS TRP ALA
SEQRES 54 A 1190 TRP ARG GLY GLU PHE PHE PRO SER LYS MET ASP GLU TYR
SEQRES 55 A 1190 ASN MET ILE LYS ARG ALA LEU GLN ASN GLU THR PHE PRO
SEQRES 56 A 1190 ASN LYS ASN LYS PHE SER LYS LYS LYS VAL LEU THR PHE
SEQRES 57 A 1190 ASP GLU LEU SER TYR ALA ASP GLN VAL ILE HIS ILE LYS
SEQRES 58 A 1190 LYS ARG LEU THR GLU TYR SER ARG LYS VAL TYR HIS ARG
SEQRES 59 A 1190 VAL LYS VAL SER GLU ILE VAL GLU ARG GLU ALA ILE VAL
SEQRES 60 A 1190 CYS GLN ARG GLU ASN PRO PHE TYR VAL ASP THR VAL LYS
SEQRES 61 A 1190 SER PHE ARG ASP ARG ARG TYR GLU PHE LYS GLY LEU ALA
SEQRES 62 A 1190 LYS THR TRP LYS GLY ASN LEU SER LYS ILE ASP PRO SER
SEQRES 63 A 1190 ASP LYS HIS ALA ARG ASP GLU ALA LYS LYS MET ILE VAL
SEQRES 64 A 1190 LEU TYR ASP SER LEU GLN LEU ALA HIS LYS VAL ILE LEU
SEQRES 65 A 1190 ASN SER PHE TYR GLY TYR VAL MET ARG LYS GLY SER ARG
SEQRES 66 A 1190 TRP TYR SER MET GLU MET ALA GLY ILE THR CYS LEU THR
SEQRES 67 A 1190 GLY ALA THR ILE ILE GLN MET ALA ARG ALA LEU VAL GLU
SEQRES 68 A 1190 ARG VAL GLY ARG PRO LEU GLU LEU ASP THR ASP GLY ILE
SEQRES 69 A 1190 TRP CYS ILE LEU PRO LYS SER PHE PRO GLU THR TYR PHE
SEQRES 70 A 1190 PHE THR LEU GLU ASN GLY LYS LYS LEU TYR LEU SER TYR
SEQRES 71 A 1190 PRO CYS SER MET LEU ASN TYR ARG VAL HIS GLN LYS PHE
SEQRES 72 A 1190 THR ASN HIS GLN TYR GLN GLU LEU LYS ASP PRO LEU ASN
SEQRES 73 A 1190 TYR ILE TYR GLU THR HIS SER GLU ASN THR ILE PHE PHE
SEQRES 74 A 1190 GLU VAL ASP GLY PRO TYR LYS ALA MET ILE LEU PRO SER
SEQRES 75 A 1190 SER LYS GLU GLU GLY LYS GLY ILE LYS LYS ARG TYR ALA
SEQRES 76 A 1190 VAL PHE ASN GLU ASP GLY SER LEU ALA GLU LEU LYS GLY
SEQRES 77 A 1190 PHE GLU LEU LYS ARG ARG GLY GLU LEU GLN LEU ILE LYS
SEQRES 78 A 1190 ASN PHE GLN SER ASP ILE PHE LYS VAL PHE LEU GLU GLY
SEQRES 79 A 1190 ASP THR LEU GLU GLY CYS TYR SER ALA VAL ALA SER VAL
SEQRES 80 A 1190 CYS ASN ARG TRP LEU ASP VAL LEU ASP SER HIS GLY LEU
SEQRES 81 A 1190 MET LEU GLU ASP GLU ASP LEU VAL SER LEU ILE CYS GLU
SEQRES 82 A 1190 ASN ARG SER MET SER LYS THR LEU LYS GLU TYR GLU GLY
SEQRES 83 A 1190 GLN LYS SER THR SER ILE THR THR ALA ARG ARG LEU GLY
SEQRES 84 A 1190 ASP PHE LEU GLY GLU ASP MET VAL LYS ASP LYS GLY LEU
SEQRES 85 A 1190 GLN CYS LYS TYR ILE ILE SER SER LYS PRO PHE ASN ALA
SEQRES 86 A 1190 PRO VAL THR GLU ARG ALA ILE PRO VAL ALA ILE PHE SER
SEQRES 87 A 1190 ALA ASP ILE PRO ILE LYS ARG SER PHE LEU ARG ARG TRP
SEQRES 88 A 1190 THR LEU ASP PRO SER LEU GLU ASP LEU ASP ILE ARG THR
SEQRES 89 A 1190 ILE ILE ASP TRP GLY TYR TYR ARG GLU ARG LEU GLY SER
SEQRES 90 A 1190 ALA ILE GLN LYS ILE ILE THR ILE PRO ALA ALA LEU GLN
SEQRES 91 A 1190 GLY VAL SER ASN PRO VAL PRO ARG VAL GLU HIS PRO ASP
SEQRES 92 A 1190 TRP LEU LYS ARG LYS ILE ALA
SEQRES 1 P 11 DT DA DA DC DC DG DC DG DT DT DOC
SEQRES 1 T 16 DC DT DC DT DT DG DA DA DC DG DC DG DG
SEQRES 2 T 16 DT DT DA
SEQRES 1 B 1190 GLY GLY ASP PRO HIS MET MET PHE GLY LYS LYS LYS ASN
SEQRES 2 B 1190 ASN GLY GLY SER SER THR ALA ARG TYR SER ALA GLY ASN
SEQRES 3 B 1190 LYS TYR ASN THR LEU SER ASN ASN TYR ALA LEU SER ALA
SEQRES 4 B 1190 GLN GLN LEU LEU ASN ALA SER LYS ILE ASP ASP ILE ASP
SEQRES 5 B 1190 SER MET MET GLY PHE GLU ARG TYR VAL PRO PRO GLN TYR
SEQRES 6 B 1190 ASN GLY ARG PHE ASP ALA LYS ASP ILE ASP GLN ILE PRO
SEQRES 7 B 1190 GLY ARG VAL GLY TRP LEU THR ASN MET HIS ALA THR LEU
SEQRES 8 B 1190 VAL SER GLN GLU THR LEU SER SER GLY SER ASN GLY GLY
SEQRES 9 B 1190 GLY ASN SER ASN ASP GLY GLU ARG VAL THR THR ASN GLN
SEQRES 10 B 1190 GLY ILE SER GLY VAL ASP PHE TYR PHE LEU ASP GLU GLU
SEQRES 11 B 1190 GLY GLY SER PHE LYS SER THR VAL VAL TYR ASP PRO TYR
SEQRES 12 B 1190 PHE PHE ILE ALA CYS ASN ASP GLU SER ARG VAL ASN ASP
SEQRES 13 B 1190 VAL GLU GLU LEU VAL LYS LYS TYR LEU GLU SER CYS LEU
SEQRES 14 B 1190 LYS SER LEU GLN ILE ILE ARG LYS GLU ASP LEU THR MET
SEQRES 15 B 1190 ASP ASN HIS LEU LEU GLY LEU GLN LYS THR LEU ILE LYS
SEQRES 16 B 1190 LEU SER PHE VAL ASN SER ASN GLN LEU PHE GLU ALA ARG
SEQRES 17 B 1190 LYS LEU LEU ARG PRO ILE LEU GLN ASP ASN ALA ASN ASN
SEQRES 18 B 1190 ASN VAL GLN ARG ASN ILE TYR ASN VAL ALA ALA ASN GLY
SEQRES 19 B 1190 SER GLU LYS VAL ASP ALA LYS HIS LEU ILE GLU ASP ILE
SEQRES 20 B 1190 ARG GLU TYR ASP VAL PRO TYR HIS VAL ARG VAL SER ILE
SEQRES 21 B 1190 ASP LYS ASP ILE ARG VAL GLY LYS TRP TYR LYS VAL THR
SEQRES 22 B 1190 GLN GLN GLY PHE ILE GLU ASP THR ARG LYS ILE ALA PHE
SEQRES 23 B 1190 ALA ASP PRO VAL VAL MET ALA PHE ASP ILE GLU THR THR
SEQRES 24 B 1190 LYS PRO PRO LEU LYS PHE ARG ASP SER ALA VAL ASP GLN
SEQRES 25 B 1190 ILE MET MET ILE SER TYR MET ILE ASP GLY GLU GLY PHE
SEQRES 26 B 1190 LEU ILE THR ASN ARG GLU ILE ILE SER GLU ASP ILE GLU
SEQRES 27 B 1190 ASP PHE GLU TYR THR PRO LYS PRO GLU TYR PRO GLY PHE
SEQRES 28 B 1190 PHE THR ILE PHE ASN GLU ASN ASP GLU VAL ALA LEU LEU
SEQRES 29 B 1190 GLN ARG PHE PHE GLU HIS ILE ARG ASP VAL ARG PRO THR
SEQRES 30 B 1190 VAL ILE SER THR PHE ASN GLY ASP PHE PHE ASP TRP PRO
SEQRES 31 B 1190 PHE ILE HIS ASN ARG SER LYS ILE HIS GLY LEU ASP MET
SEQRES 32 B 1190 PHE ASP GLU ILE GLY PHE ALA PRO ASP ALA GLU GLY GLU
SEQRES 33 B 1190 TYR LYS SER SER TYR CYS SER HIS MET ASP CYS PHE ARG
SEQRES 34 B 1190 TRP VAL LYS ARG ASP SER TYR LEU PRO GLN GLY SER GLN
SEQRES 35 B 1190 GLY LEU LYS ALA VAL THR GLN SER LYS LEU GLY TYR ASN
SEQRES 36 B 1190 PRO ILE GLU LEU ASP PRO GLU LEU MET THR PRO TYR ALA
SEQRES 37 B 1190 PHE GLU LYS PRO GLN HIS LEU SER GLU TYR SER VAL SER
SEQRES 38 B 1190 ASP ALA VAL ALA THR TYR TYR LEU TYR MET LYS TYR VAL
SEQRES 39 B 1190 HIS PRO PHE ILE PHE SER LEU CYS THR ILE ILE PRO LEU
SEQRES 40 B 1190 ASN PRO ASP GLU THR LEU ARG LYS GLY THR GLY THR LEU
SEQRES 41 B 1190 CYS GLU MET LEU LEU MET VAL GLN ALA TYR GLN HIS ASN
SEQRES 42 B 1190 ILE LEU LEU PRO ASN LYS HIS THR ASP PRO ILE GLU ARG
SEQRES 43 B 1190 PHE TYR ASP GLY HIS LEU LEU GLU SER GLU THR TYR VAL
SEQRES 44 B 1190 GLY GLY HIS VAL GLU SER LEU GLU ALA GLY VAL PHE ARG
SEQRES 45 B 1190 SER ASP LEU LYS ASN GLU PHE LYS ILE ASP PRO SER ALA
SEQRES 46 B 1190 ILE ASP GLU LEU LEU GLN GLU LEU PRO GLU ALA LEU LYS
SEQRES 47 B 1190 PHE SER VAL GLU VAL GLU ASN LYS SER SER VAL ASP LYS
SEQRES 48 B 1190 VAL THR ASN PHE GLU GLU ILE LYS ASN GLN ILE THR GLN
SEQRES 49 B 1190 LYS LEU LEU GLU LEU LYS GLU ASN ASN ILE ARG ASN GLU
SEQRES 50 B 1190 LEU PRO LEU ILE TYR HIS VAL ASP VAL ALA SER MET TYR
SEQRES 51 B 1190 PRO ASN ILE MET THR THR ASN ARG LEU GLN PRO ASP SER
SEQRES 52 B 1190 ILE LYS ALA GLU ARG ASP CYS ALA SER CYS ASP PHE ASN
SEQRES 53 B 1190 ARG PRO GLY LYS THR CYS ALA ARG LYS LEU LYS TRP ALA
SEQRES 54 B 1190 TRP ARG GLY GLU PHE PHE PRO SER LYS MET ASP GLU TYR
SEQRES 55 B 1190 ASN MET ILE LYS ARG ALA LEU GLN ASN GLU THR PHE PRO
SEQRES 56 B 1190 ASN LYS ASN LYS PHE SER LYS LYS LYS VAL LEU THR PHE
SEQRES 57 B 1190 ASP GLU LEU SER TYR ALA ASP GLN VAL ILE HIS ILE LYS
SEQRES 58 B 1190 LYS ARG LEU THR GLU TYR SER ARG LYS VAL TYR HIS ARG
SEQRES 59 B 1190 VAL LYS VAL SER GLU ILE VAL GLU ARG GLU ALA ILE VAL
SEQRES 60 B 1190 CYS GLN ARG GLU ASN PRO PHE TYR VAL ASP THR VAL LYS
SEQRES 61 B 1190 SER PHE ARG ASP ARG ARG TYR GLU PHE LYS GLY LEU ALA
SEQRES 62 B 1190 LYS THR TRP LYS GLY ASN LEU SER LYS ILE ASP PRO SER
SEQRES 63 B 1190 ASP LYS HIS ALA ARG ASP GLU ALA LYS LYS MET ILE VAL
SEQRES 64 B 1190 LEU TYR ASP SER LEU GLN LEU ALA HIS LYS VAL ILE LEU
SEQRES 65 B 1190 ASN SER PHE TYR GLY TYR VAL MET ARG LYS GLY SER ARG
SEQRES 66 B 1190 TRP TYR SER MET GLU MET ALA GLY ILE THR CYS LEU THR
SEQRES 67 B 1190 GLY ALA THR ILE ILE GLN MET ALA ARG ALA LEU VAL GLU
SEQRES 68 B 1190 ARG VAL GLY ARG PRO LEU GLU LEU ASP THR ASP GLY ILE
SEQRES 69 B 1190 TRP CYS ILE LEU PRO LYS SER PHE PRO GLU THR TYR PHE
SEQRES 70 B 1190 PHE THR LEU GLU ASN GLY LYS LYS LEU TYR LEU SER TYR
SEQRES 71 B 1190 PRO CYS SER MET LEU ASN TYR ARG VAL HIS GLN LYS PHE
SEQRES 72 B 1190 THR ASN HIS GLN TYR GLN GLU LEU LYS ASP PRO LEU ASN
SEQRES 73 B 1190 TYR ILE TYR GLU THR HIS SER GLU ASN THR ILE PHE PHE
SEQRES 74 B 1190 GLU VAL ASP GLY PRO TYR LYS ALA MET ILE LEU PRO SER
SEQRES 75 B 1190 SER LYS GLU GLU GLY LYS GLY ILE LYS LYS ARG TYR ALA
SEQRES 76 B 1190 VAL PHE ASN GLU ASP GLY SER LEU ALA GLU LEU LYS GLY
SEQRES 77 B 1190 PHE GLU LEU LYS ARG ARG GLY GLU LEU GLN LEU ILE LYS
SEQRES 78 B 1190 ASN PHE GLN SER ASP ILE PHE LYS VAL PHE LEU GLU GLY
SEQRES 79 B 1190 ASP THR LEU GLU GLY CYS TYR SER ALA VAL ALA SER VAL
SEQRES 80 B 1190 CYS ASN ARG TRP LEU ASP VAL LEU ASP SER HIS GLY LEU
SEQRES 81 B 1190 MET LEU GLU ASP GLU ASP LEU VAL SER LEU ILE CYS GLU
SEQRES 82 B 1190 ASN ARG SER MET SER LYS THR LEU LYS GLU TYR GLU GLY
SEQRES 83 B 1190 GLN LYS SER THR SER ILE THR THR ALA ARG ARG LEU GLY
SEQRES 84 B 1190 ASP PHE LEU GLY GLU ASP MET VAL LYS ASP LYS GLY LEU
SEQRES 85 B 1190 GLN CYS LYS TYR ILE ILE SER SER LYS PRO PHE ASN ALA
SEQRES 86 B 1190 PRO VAL THR GLU ARG ALA ILE PRO VAL ALA ILE PHE SER
SEQRES 87 B 1190 ALA ASP ILE PRO ILE LYS ARG SER PHE LEU ARG ARG TRP
SEQRES 88 B 1190 THR LEU ASP PRO SER LEU GLU ASP LEU ASP ILE ARG THR
SEQRES 89 B 1190 ILE ILE ASP TRP GLY TYR TYR ARG GLU ARG LEU GLY SER
SEQRES 90 B 1190 ALA ILE GLN LYS ILE ILE THR ILE PRO ALA ALA LEU GLN
SEQRES 91 B 1190 GLY VAL SER ASN PRO VAL PRO ARG VAL GLU HIS PRO ASP
SEQRES 92 B 1190 TRP LEU LYS ARG LYS ILE ALA
SEQRES 1 C 11 DT DA DA DC DC DG DC DG DT DT DOC
SEQRES 1 D 16 DC DT DC DT DT DG DA DA DC DG DC DG DG
SEQRES 2 D 16 DT DT DA
HET DOC P 11 18
HET DOC C 11 18
HET DTP A1301 30
HET CA A1302 1
HET CA A1303 1
HET FE A1304 1
HET DTP B1301 30
HET CA B1302 1
HET CA B1303 1
HET FE B1304 1
HETNAM DOC 2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE
HETNAM DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE
HETNAM CA CALCIUM ION
HETNAM FE FE (III) ION
FORMUL 2 DOC 2(C9 H14 N3 O6 P)
FORMUL 7 DTP 2(C10 H16 N5 O12 P3)
FORMUL 8 CA 4(CA 2+)
FORMUL 10 FE 2(FE 3+)
FORMUL 15 HOH *6(H2 O)
HELIX 1 AA1 LEU A 32 MET A 50 1 19
HELIX 2 AA2 ASP A 65 ILE A 69 5 5
HELIX 3 AA3 ASP A 145 SER A 147 5 3
HELIX 4 AA4 ARG A 148 LEU A 160 1 13
HELIX 5 AA5 ASN A 179 GLY A 183 5 5
HELIX 6 AA6 ASN A 195 ALA A 214 1 20
HELIX 7 AA7 ASP A 234 HIS A 237 5 4
HELIX 8 AA8 PRO A 248 LYS A 257 1 10
HELIX 9 AA9 ASP A 354 ARG A 370 1 17
HELIX 10 AB1 PHE A 382 HIS A 394 1 13
HELIX 11 AB2 ASP A 397 GLY A 403 1 7
HELIX 12 AB3 CYS A 422 ASP A 429 1 8
HELIX 13 AB4 PRO A 433 GLN A 437 5 5
HELIX 14 AB5 GLY A 438 LEU A 447 1 10
HELIX 15 AB6 ASP A 455 THR A 460 1 6
HELIX 16 AB7 PRO A 461 PHE A 464 5 4
HELIX 17 AB8 LYS A 466 TYR A 488 1 23
HELIX 18 AB9 TYR A 488 THR A 498 1 11
HELIX 19 AC1 ASN A 503 LYS A 510 1 8
HELIX 20 AC2 GLY A 511 HIS A 527 1 17
HELIX 21 AC3 ASP A 577 GLN A 586 1 10
HELIX 22 AC4 GLU A 587 VAL A 598 1 12
HELIX 23 AC5 SER A 603 VAL A 607 5 5
HELIX 24 AC6 ASN A 609 ASN A 627 1 19
HELIX 25 AC7 SER A 643 ASN A 652 1 10
HELIX 26 AC8 GLN A 655 ASP A 657 5 3
HELIX 27 AC9 LYS A 693 GLU A 707 1 15
HELIX 28 AD1 THR A 722 LEU A 726 5 5
HELIX 29 AD2 SER A 727 TYR A 747 1 21
HELIX 30 AD3 PRO A 768 LEU A 795 1 28
HELIX 31 AD4 ASP A 802 TYR A 833 1 32
HELIX 32 AD5 VAL A 834 ARG A 836 5 3
HELIX 33 AD6 SER A 843 ARG A 867 1 25
HELIX 34 AD7 TYR A 905 PHE A 918 1 14
HELIX 35 AD8 LEU A 992 PHE A 1003 1 12
HELIX 36 AD9 LYS A 1004 GLU A 1008 5 5
HELIX 37 AE1 THR A 1011 SER A 1032 1 22
HELIX 38 AE2 GLU A 1038 CYS A 1047 1 10
HELIX 39 AE3 THR A 1055 GLU A 1060 5 6
HELIX 40 AE4 SER A 1064 GLY A 1078 1 15
HELIX 41 AE5 GLU A 1079 VAL A 1082 5 4
HELIX 42 AE6 ALA A 1110 ALA A 1114 5 5
HELIX 43 AE7 ASP A 1115 LEU A 1128 1 14
HELIX 44 AE8 ASP A 1136 ILE A 1141 1 6
HELIX 45 AE9 ASP A 1142 ILE A 1158 1 17
HELIX 46 AF1 ILE A 1158 GLN A 1165 1 8
HELIX 47 AF2 PRO A 1177 ILE A 1184 1 8
HELIX 48 AF3 TYR B 30 MET B 50 1 21
HELIX 49 AF4 ASP B 65 ILE B 72 5 8
HELIX 50 AF5 ASP B 145 SER B 147 5 3
HELIX 51 AF6 ARG B 148 LEU B 160 1 13
HELIX 52 AF7 ASN B 179 GLY B 183 5 5
HELIX 53 AF8 ASN B 195 ASN B 215 1 21
HELIX 54 AF9 ASP B 234 HIS B 237 5 4
HELIX 55 AG1 PRO B 248 LYS B 257 1 10
HELIX 56 AG2 ASP B 354 ARG B 370 1 17
HELIX 57 AG3 PHE B 382 HIS B 394 1 13
HELIX 58 AG4 ASP B 397 ILE B 402 1 6
HELIX 59 AG5 CYS B 422 SER B 430 1 9
HELIX 60 AG6 PRO B 433 GLN B 437 5 5
HELIX 61 AG7 GLY B 438 LEU B 447 1 10
HELIX 62 AG8 ASP B 455 GLU B 457 5 3
HELIX 63 AG9 LEU B 458 LYS B 466 1 9
HELIX 64 AH1 LYS B 466 TYR B 488 1 23
HELIX 65 AH2 TYR B 488 THR B 498 1 11
HELIX 66 AH3 ASN B 503 LYS B 510 1 8
HELIX 67 AH4 GLY B 511 HIS B 527 1 17
HELIX 68 AH5 ASP B 577 VAL B 598 1 22
HELIX 69 AH6 SER B 603 VAL B 607 5 5
HELIX 70 AH7 ASN B 609 ASN B 627 1 19
HELIX 71 AH8 SER B 643 ARG B 653 1 11
HELIX 72 AH9 GLN B 655 ILE B 659 5 5
HELIX 73 AI1 LYS B 693 ASN B 706 1 14
HELIX 74 AI2 SER B 727 LYS B 737 1 11
HELIX 75 AI3 PRO B 768 ILE B 798 1 31
HELIX 76 AI4 ASP B 802 TYR B 833 1 32
HELIX 77 AI5 SER B 843 GLU B 866 1 24
HELIX 78 AI6 TYR B 905 PHE B 918 1 14
HELIX 79 AI7 LEU B 992 PHE B 1003 1 12
HELIX 80 AI8 LYS B 1004 GLU B 1008 5 5
HELIX 81 AI9 THR B 1011 SER B 1032 1 22
HELIX 82 AJ1 GLU B 1038 CYS B 1047 1 10
HELIX 83 AJ2 THR B 1055 GLU B 1060 5 6
HELIX 84 AJ3 SER B 1064 GLY B 1078 1 15
HELIX 85 AJ4 GLU B 1079 LYS B 1083 5 5
HELIX 86 AJ5 PRO B 1101 GLU B 1104 5 4
HELIX 87 AJ6 ALA B 1110 ALA B 1114 5 5
HELIX 88 AJ7 ASP B 1115 LEU B 1128 1 14
HELIX 89 AJ8 ASP B 1136 ILE B 1141 1 6
HELIX 90 AJ9 ASP B 1142 ILE B 1158 1 17
HELIX 91 AK1 ILE B 1158 LEU B 1164 1 7
HELIX 92 AK2 PRO B 1177 ALA B 1185 1 9
SHEET 1 AA1 5 SER A 128 VAL A 134 0
SHEET 2 AA1 5 ILE A 114 ASP A 123 -1 N PHE A 119 O SER A 131
SHEET 3 AA1 5 ARG A 75 VAL A 87 -1 N TRP A 78 O LEU A 122
SHEET 4 AA1 5 TRP A 264 VAL A 267 -1 O TYR A 265 N GLY A 77
SHEET 5 AA1 5 PHE A 272 GLU A 274 -1 O ILE A 273 N LYS A 266
SHEET 1 AA2 4 ILE A 169 LYS A 172 0
SHEET 2 AA2 4 LYS A 186 SER A 192 -1 O LYS A 186 N LYS A 172
SHEET 3 AA2 4 TYR A 138 CYS A 143 -1 N ILE A 141 O ILE A 189
SHEET 4 AA2 4 ILE A 239 ARG A 243 -1 O ASP A 241 N ALA A 142
SHEET 1 AA3 7 PHE A 335 GLU A 336 0
SHEET 2 AA3 7 PHE A 346 GLU A 352 -1 O PHE A 347 N PHE A 335
SHEET 3 AA3 7 GLU A 318 ASN A 324 1 N THR A 323 O GLU A 352
SHEET 4 AA3 7 ILE A 308 ILE A 315 -1 N ILE A 315 O GLU A 318
SHEET 5 AA3 7 VAL A 286 THR A 293 -1 N ASP A 290 O SER A 312
SHEET 6 AA3 7 VAL A 373 THR A 376 1 O SER A 375 N MET A 287
SHEET 7 AA3 7 SER A 418 ASP A 421 1 O MET A 420 N ILE A 374
SHEET 1 AA4 2 PHE A 404 PRO A 406 0
SHEET 2 AA4 2 TYR A 412 SER A 414 -1 O LYS A 413 N ALA A 405
SHEET 1 AA5 5 PHE A 542 TYR A 543 0
SHEET 2 AA5 5 HIS A 546 TYR A 553 -1 O HIS A 546 N TYR A 543
SHEET 3 AA5 5 ARG A 679 PHE A 689 -1 O ARG A 686 N THR A 552
SHEET 4 AA5 5 VAL A 752 VAL A 762 -1 O VAL A 756 N TRP A 685
SHEET 5 AA5 5 ILE A 659 LYS A 660 -1 N LYS A 660 O ILE A 761
SHEET 1 AA6 5 VAL A 558 SER A 560 0
SHEET 2 AA6 5 ARG A 870 ASP A 875 -1 O LEU A 874 N GLU A 559
SHEET 3 AA6 5 GLY A 878 PRO A 884 -1 O TRP A 880 N GLU A 873
SHEET 4 AA6 5 PRO A 634 VAL A 641 -1 N TYR A 637 O CYS A 881
SHEET 5 AA6 5 PHE A 944 TYR A 950 -1 O TYR A 950 N ILE A 636
SHEET 1 AA7 4 GLY A 564 ARG A 567 0
SHEET 2 AA7 4 ALA A 952 LEU A 955 -1 O LEU A 955 N GLY A 564
SHEET 3 AA7 4 TYR A 969 PHE A 972 -1 O PHE A 972 N ALA A 952
SHEET 4 AA7 4 LEU A 978 LYS A 982 -1 O ALA A 979 N VAL A 971
SHEET 1 AA8 2 ASN A 572 LYS A 575 0
SHEET 2 AA8 2 ILE A 629 GLU A 632 -1 O GLU A 632 N ASN A 572
SHEET 1 AA9 2 THR A 890 THR A 894 0
SHEET 2 AA9 2 LYS A 900 SER A 904 -1 O LEU A 903 N TYR A 891
SHEET 1 AB1 2 ASN A 920 ASP A 928 0
SHEET 2 AB1 2 ILE A 933 GLU A 939 -1 O ILE A 933 N LYS A 927
SHEET 1 AB2 3 GLU A1048 MET A1052 0
SHEET 2 AB2 3 LEU A1087 ILE A1093 -1 O CYS A1089 N ARG A1050
SHEET 3 AB2 3 ALA A1106 PRO A1108 -1 O ILE A1107 N ILE A1092
SHEET 1 AB3 5 SER B 128 VAL B 134 0
SHEET 2 AB3 5 ILE B 114 ASP B 123 -1 N PHE B 121 O PHE B 129
SHEET 3 AB3 5 ARG B 75 VAL B 87 -1 N TRP B 78 O LEU B 122
SHEET 4 AB3 5 TRP B 264 THR B 268 -1 O TYR B 265 N GLY B 77
SHEET 5 AB3 5 GLY B 271 GLU B 274 -1 O ILE B 273 N LYS B 266
SHEET 1 AB4 4 ILE B 169 LYS B 172 0
SHEET 2 AB4 4 LYS B 186 SER B 192 -1 O LYS B 186 N LYS B 172
SHEET 3 AB4 4 TYR B 138 CYS B 143 -1 N PHE B 139 O LEU B 191
SHEET 4 AB4 4 ILE B 239 ARG B 243 -1 O ASP B 241 N ALA B 142
SHEET 1 AB5 7 PHE B 335 GLU B 336 0
SHEET 2 AB5 7 PHE B 346 GLU B 352 -1 O PHE B 347 N PHE B 335
SHEET 3 AB5 7 GLU B 318 ASN B 324 1 N LEU B 321 O PHE B 350
SHEET 4 AB5 7 ILE B 308 ILE B 315 -1 N TYR B 313 O PHE B 320
SHEET 5 AB5 7 VAL B 286 THR B 293 -1 N ASP B 290 O SER B 312
SHEET 6 AB5 7 VAL B 373 THR B 376 1 O SER B 375 N MET B 287
SHEET 7 AB5 7 SER B 418 ASP B 421 1 O SER B 418 N ILE B 374
SHEET 1 AB6 2 ALA B 405 PRO B 406 0
SHEET 2 AB6 2 TYR B 412 LYS B 413 -1 O LYS B 413 N ALA B 405
SHEET 1 AB7 4 PHE B 542 TYR B 543 0
SHEET 2 AB7 4 HIS B 546 TYR B 553 -1 O HIS B 546 N TYR B 543
SHEET 3 AB7 4 ALA B 678 PHE B 689 -1 O GLU B 688 N GLU B 549
SHEET 4 AB7 4 SER B 753 CYS B 763 -1 O ALA B 760 N LEU B 681
SHEET 1 AB8 5 VAL B 558 SER B 560 0
SHEET 2 AB8 5 ARG B 870 ASP B 875 -1 O LEU B 874 N GLU B 559
SHEET 3 AB8 5 GLY B 878 PRO B 884 -1 O TRP B 880 N GLU B 873
SHEET 4 AB8 5 PRO B 634 VAL B 641 -1 N VAL B 639 O ILE B 879
SHEET 5 AB8 5 PHE B 944 TYR B 950 -1 O GLU B 945 N ASP B 640
SHEET 1 AB9 4 GLY B 564 ARG B 567 0
SHEET 2 AB9 4 ALA B 952 LEU B 955 -1 O LEU B 955 N GLY B 564
SHEET 3 AB9 4 TYR B 969 PHE B 972 -1 O ALA B 970 N ILE B 954
SHEET 4 AB9 4 LEU B 978 LYS B 982 -1 O GLU B 980 N VAL B 971
SHEET 1 AC1 2 ASN B 572 LYS B 575 0
SHEET 2 AC1 2 ILE B 629 GLU B 632 -1 O GLU B 632 N ASN B 572
SHEET 1 AC2 2 THR B 890 TYR B 891 0
SHEET 2 AC2 2 LEU B 903 SER B 904 -1 O LEU B 903 N TYR B 891
SHEET 1 AC3 2 ASN B 920 ASP B 928 0
SHEET 2 AC3 2 ILE B 933 GLU B 939 -1 O GLU B 935 N GLU B 925
SHEET 1 AC4 3 GLU B1048 SER B1051 0
SHEET 2 AC4 3 GLN B1088 ILE B1093 -1 O CYS B1089 N ARG B1050
SHEET 3 AC4 3 ALA B1106 PRO B1108 -1 O ILE B1107 N ILE B1092
LINK O3' DT P 10 P DOC P 11 1555 1555 1.51
LINK O3' DT C 10 P DOC C 11 1555 1555 1.53
LINK OD1 ASP A 290 CA CA A1303 1555 1555 3.03
LINK OD2 ASP A 290 CA CA A1303 1555 1555 2.42
LINK OE2 GLU A 292 CA CA A1303 1555 1555 2.33
LINK OD2 ASP A 477 CA CA A1303 1555 1555 2.40
LINK O VAL A 641 CA CA A1302 1555 1555 2.51
LINK SG CYS A 677 FE FE A1304 1555 1555 2.31
LINK SG CYS A 763 FE FE A1304 1555 1555 2.28
LINK OD2 ASP A 877 CA CA A1302 1555 1555 2.15
LINK O3G DTP A1301 CA CA A1302 1555 1555 2.14
LINK O2B DTP A1301 CA CA A1302 1555 1555 2.21
LINK O2A DTP A1301 CA CA A1302 1555 1555 2.34
LINK CA CA A1303 O HOH A1402 1555 1555 2.38
LINK OD1 ASP B 290 CA CA B1303 1555 1555 3.11
LINK OD2 ASP B 290 CA CA B1303 1555 1555 2.64
LINK OE1 GLU B 292 CA CA B1303 1555 1555 2.63
LINK OD2 ASP B 477 CA CA B1303 1555 1555 2.31
LINK OD1 ASP B 640 CA CA B1302 1555 1555 3.00
LINK OD2 ASP B 640 CA CA B1302 1555 1555 2.23
LINK O VAL B 641 CA CA B1302 1555 1555 2.36
LINK SG CYS B 677 FE FE B1304 1555 1555 2.27
LINK SG CYS B 763 FE FE B1304 1555 1555 2.32
LINK OD2 ASP B 877 CA CA B1302 1555 1555 2.11
LINK O1G DTP B1301 CA CA B1302 1555 1555 2.26
LINK O1B DTP B1301 CA CA B1302 1555 1555 2.29
LINK O1A DTP B1301 CA CA B1302 1555 1555 2.47
LINK CA CA B1303 O HOH B1401 1555 1555 2.76
LINK CA CA B1303 O HOH B1403 1555 1555 2.74
CISPEP 1 GLY A 948 PRO A 949 0 -0.50
CISPEP 2 LYS A 1096 PRO A 1097 0 3.39
CISPEP 3 GLY B 948 PRO B 949 0 0.47
SITE 1 AC1 16 ASP A 640 VAL A 641 ALA A 642 SER A 643
SITE 2 AC1 16 MET A 644 TYR A 645 PRO A 646 ARG A 781
SITE 3 AC1 16 LYS A 785 LYS A 824 ASN A 828 ASP A 877
SITE 4 AC1 16 CA A1302 DOC P 11 DT T 5 DG T 6
SITE 1 AC2 4 ASP A 640 VAL A 641 ASP A 877 DTP A1301
SITE 1 AC3 4 ASP A 290 GLU A 292 ASP A 477 HOH A1402
SITE 1 AC4 2 CYS A 677 CYS A 763
SITE 1 AC5 14 ASP B 640 VAL B 641 SER B 643 MET B 644
SITE 2 AC5 14 TYR B 645 ARG B 781 LYS B 785 LYS B 824
SITE 3 AC5 14 ASN B 828 ASP B 877 CA B1302 DOC C 11
SITE 4 AC5 14 DT D 5 DG D 6
SITE 1 AC6 4 ASP B 640 VAL B 641 ASP B 877 DTP B1301
SITE 1 AC7 5 ASP B 290 GLU B 292 ASP B 477 HOH B1401
SITE 2 AC7 5 HOH B1403
SITE 1 AC8 2 CYS B 677 CYS B 763
SITE 1 AC9 13 ASP B 875 THR B 876 ASP B 877 LYS B 967
SITE 2 AC9 13 TYR B 969 LYS B 982 GLY B 983 LYS B 987
SITE 3 AC9 13 DTP B1301 DT C 9 DG D 6 DA D 7
SITE 4 AC9 13 DA D 8
CRYST1 154.466 70.257 159.335 90.00 112.85 90.00 P 1 2 1 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 0.006474 0.000000 0.002729 0.00000
SCALE2 0.000000 0.014233 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006811 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
