HEADER HYDROLASE/DNA 02-APR-14 4Q0Z
TITLE THE CATALYTIC CORE OF RAD2 IN COMPLEX WITH DNA SUBSTRATE (COMPLEX III)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAD2P;
COMPND 3 CHAIN: A, B, E, F;
COMPND 4 FRAGMENT: RAD2 CATALYTIC CORE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (5'-
COMPND 8 D(*TP*GP*CP*TP*CP*CP*CP*TP*TP*GP*TP*CP*TP*CP*AP*GP*T)-3');
COMPND 9 CHAIN: C, G;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: DNA (5'-
COMPND 13 D(*TP*CP*TP*GP*AP*GP*AP*CP*AP*AP*GP*GP*GP*AP*GP*CP*T)-3');
COMPND 14 CHAIN: D, H;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 GENE: RAD2, YGR258C;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) ROSSETA;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES
KEYWDS BA ROSSMANN-LIKE, DNA REPAIR, TFIIH, HYDROLASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MIETUS,E.NOWAK,M.JACIUK,P.KUSTOSZ,M.NOWOTNY
REVDAT 6 20-SEP-23 4Q0Z 1 REMARK LINK
REVDAT 5 22-NOV-17 4Q0Z 1 REMARK
REVDAT 4 09-AUG-17 4Q0Z 1 SOURCE REMARK
REVDAT 3 01-OCT-14 4Q0Z 1 JRNL
REVDAT 2 17-SEP-14 4Q0Z 1 TITLE
REVDAT 1 27-AUG-14 4Q0Z 0
JRNL AUTH M.MIETUS,E.NOWAK,M.JACIUK,P.KUSTOSZ,J.STUDNICKA,M.NOWOTNY
JRNL TITL CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF RAD2: INSIGHTS
JRNL TITL 2 INTO THE MECHANISM OF SUBSTRATE BINDING.
JRNL REF NUCLEIC ACIDS RES. V. 42 10762 2014
JRNL REFN ISSN 0305-1048
JRNL PMID 25120270
JRNL DOI 10.1093/NAR/GKU729
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 92066
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4607
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 34.3328 - 7.4258 0.98 2982 171 0.1703 0.1696
REMARK 3 2 7.4258 - 5.9038 1.00 2969 163 0.1790 0.2164
REMARK 3 3 5.9038 - 5.1604 1.00 2945 163 0.1635 0.2128
REMARK 3 4 5.1604 - 4.6899 1.00 2944 161 0.1456 0.2111
REMARK 3 5 4.6899 - 4.3544 1.00 2949 142 0.1377 0.2135
REMARK 3 6 4.3544 - 4.0981 1.00 2906 157 0.1445 0.2152
REMARK 3 7 4.0981 - 3.8932 1.00 2954 149 0.1481 0.1843
REMARK 3 8 3.8932 - 3.7239 1.00 2942 148 0.1545 0.2025
REMARK 3 9 3.7239 - 3.5807 1.00 2891 158 0.1758 0.2072
REMARK 3 10 3.5807 - 3.4573 1.00 2935 152 0.1804 0.2452
REMARK 3 11 3.4573 - 3.3493 1.00 2953 121 0.1862 0.2543
REMARK 3 12 3.3493 - 3.2536 1.00 2905 160 0.1877 0.2419
REMARK 3 13 3.2536 - 3.1680 1.00 2911 152 0.1872 0.2906
REMARK 3 14 3.1680 - 3.0908 1.00 2908 173 0.1921 0.2693
REMARK 3 15 3.0908 - 3.0206 1.00 2939 150 0.1993 0.2679
REMARK 3 16 3.0206 - 2.9563 1.00 2875 149 0.1987 0.2462
REMARK 3 17 2.9563 - 2.8972 1.00 2934 154 0.1968 0.2661
REMARK 3 18 2.8972 - 2.8426 1.00 2907 153 0.1951 0.2738
REMARK 3 19 2.8426 - 2.7918 1.00 2903 143 0.1933 0.2661
REMARK 3 20 2.7918 - 2.7445 1.00 2882 157 0.1967 0.2654
REMARK 3 21 2.7445 - 2.7003 1.00 2903 180 0.1952 0.2929
REMARK 3 22 2.7003 - 2.6587 1.00 2951 134 0.2009 0.2572
REMARK 3 23 2.6587 - 2.6196 1.00 2907 152 0.2130 0.2561
REMARK 3 24 2.6196 - 2.5828 1.00 2882 152 0.2126 0.3105
REMARK 3 25 2.5828 - 2.5479 1.00 2927 162 0.2109 0.2846
REMARK 3 26 2.5479 - 2.5148 1.00 2911 152 0.2088 0.2943
REMARK 3 27 2.5148 - 2.4834 1.00 2917 154 0.2247 0.2840
REMARK 3 28 2.4834 - 2.4534 1.00 2839 147 0.2330 0.3233
REMARK 3 29 2.4534 - 2.4249 1.00 2957 148 0.2428 0.3362
REMARK 3 30 2.4249 - 2.3977 0.95 2731 150 0.2394 0.3000
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.240
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 13230
REMARK 3 ANGLE : 1.123 18342
REMARK 3 CHIRALITY : 0.068 2031
REMARK 3 PLANARITY : 0.005 1907
REMARK 3 DIHEDRAL : 20.629 5032
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 4Q0Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085467.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.89440
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92066
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.75100
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: PHASER
REMARK 200 STARTING MODEL: 4Q0R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% (W/V) PEG 8000, 20% (V/V) ETHYLENE
REMARK 280 GLYCOL, 0.2 M D-GLUCOSE, 0.2 M D-MANNOSE, 0.2 M D-GALACTOSE, 0.2
REMARK 280 M L-FRUCTOSE, 0.2 M D-XYLOSE, 0.2 M N-ACETYL-D-GLUCOSAMINE, AND
REMARK 280 0.1 M MES/IMIDAZOLE, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 43.01950
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 5510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 THR A 725
REMARK 465 ALA A 726
REMARK 465 ARG A 727
REMARK 465 LYS A 728
REMARK 465 LEU A 729
REMARK 465 LEU A 730
REMARK 465 ALA A 731
REMARK 465 ASN A 732
REMARK 465 THR A 733
REMARK 465 THR A 734
REMARK 465 LEU A 735
REMARK 465 SER A 736
REMARK 465 THR A 737
REMARK 465 SER A 738
REMARK 465 ALA A 739
REMARK 465 GLU A 740
REMARK 465 ARG A 741
REMARK 465 ASN A 742
REMARK 465 VAL A 743
REMARK 465 ALA A 744
REMARK 465 GLU A 745
REMARK 465 ASN A 746
REMARK 465 ALA A 747
REMARK 465 PHE A 748
REMARK 465 VAL A 749
REMARK 465 GLU A 750
REMARK 465 ASP A 751
REMARK 465 GLU A 752
REMARK 465 LEU A 753
REMARK 465 PHE A 754
REMARK 465 GLU A 755
REMARK 465 GLN A 756
REMARK 465 GLN A 757
REMARK 465 MET A 758
REMARK 465 LYS A 759
REMARK 465 ASP A 760
REMARK 465 LYS A 761
REMARK 465 ARG A 762
REMARK 465 ASP A 763
REMARK 465 SER A 764
REMARK 465 ARG A 984
REMARK 465 ASP A 985
REMARK 465 VAL A 986
REMARK 465 GLU B 46
REMARK 465 GLY B 47
REMARK 465 ARG B 711
REMARK 465 LYS B 712
REMARK 465 GLU B 713
REMARK 465 ARG B 714
REMARK 465 ARG B 715
REMARK 465 GLN B 716
REMARK 465 GLY B 717
REMARK 465 LYS B 718
REMARK 465 ARG B 719
REMARK 465 GLU B 720
REMARK 465 SER B 721
REMARK 465 ALA B 722
REMARK 465 LYS B 723
REMARK 465 SER B 724
REMARK 465 THR B 725
REMARK 465 ALA B 726
REMARK 465 ARG B 727
REMARK 465 LYS B 728
REMARK 465 LEU B 729
REMARK 465 LEU B 730
REMARK 465 ALA B 731
REMARK 465 ASN B 732
REMARK 465 THR B 733
REMARK 465 THR B 734
REMARK 465 LEU B 735
REMARK 465 SER B 736
REMARK 465 THR B 737
REMARK 465 SER B 738
REMARK 465 ALA B 739
REMARK 465 GLU B 740
REMARK 465 ARG B 741
REMARK 465 ASN B 742
REMARK 465 VAL B 743
REMARK 465 ALA B 744
REMARK 465 GLU B 745
REMARK 465 ASN B 746
REMARK 465 ALA B 747
REMARK 465 PHE B 748
REMARK 465 VAL B 749
REMARK 465 GLU B 750
REMARK 465 ASP B 751
REMARK 465 GLU B 752
REMARK 465 LEU B 753
REMARK 465 PHE B 754
REMARK 465 GLU B 755
REMARK 465 GLN B 756
REMARK 465 GLN B 757
REMARK 465 MET B 758
REMARK 465 LYS B 759
REMARK 465 ASP B 760
REMARK 465 LYS B 761
REMARK 465 ARG B 762
REMARK 465 ASP B 763
REMARK 465 ARG B 984
REMARK 465 ASP B 985
REMARK 465 VAL B 986
REMARK 465 GLY E 47
REMARK 465 ASN E 48
REMARK 465 GLU E 713
REMARK 465 ARG E 714
REMARK 465 ARG E 715
REMARK 465 GLN E 716
REMARK 465 GLY E 717
REMARK 465 LYS E 718
REMARK 465 ARG E 719
REMARK 465 GLU E 720
REMARK 465 SER E 721
REMARK 465 ALA E 722
REMARK 465 LYS E 723
REMARK 465 SER E 724
REMARK 465 THR E 725
REMARK 465 ALA E 726
REMARK 465 ARG E 727
REMARK 465 LYS E 728
REMARK 465 LEU E 729
REMARK 465 LEU E 730
REMARK 465 ALA E 731
REMARK 465 ASN E 732
REMARK 465 THR E 733
REMARK 465 THR E 734
REMARK 465 LEU E 735
REMARK 465 SER E 736
REMARK 465 THR E 737
REMARK 465 SER E 738
REMARK 465 ALA E 739
REMARK 465 GLU E 740
REMARK 465 ARG E 741
REMARK 465 ASN E 742
REMARK 465 VAL E 743
REMARK 465 ALA E 744
REMARK 465 GLU E 745
REMARK 465 ASN E 746
REMARK 465 ALA E 747
REMARK 465 PHE E 748
REMARK 465 VAL E 749
REMARK 465 GLU E 750
REMARK 465 ASP E 751
REMARK 465 GLU E 752
REMARK 465 LEU E 753
REMARK 465 PHE E 754
REMARK 465 GLU E 755
REMARK 465 GLN E 756
REMARK 465 GLN E 757
REMARK 465 MET E 758
REMARK 465 LYS E 759
REMARK 465 ASP E 760
REMARK 465 LYS E 761
REMARK 465 ARG E 762
REMARK 465 ASP E 763
REMARK 465 SER E 764
REMARK 465 LYS E 901
REMARK 465 ARG E 902
REMARK 465 ASP E 926
REMARK 465 ASP E 927
REMARK 465 ARG E 984
REMARK 465 ASP E 985
REMARK 465 VAL E 986
REMARK 465 ASP F 44
REMARK 465 GLN F 45
REMARK 465 GLU F 46
REMARK 465 GLY F 47
REMARK 465 ASN F 48
REMARK 465 ARG F 715
REMARK 465 GLN F 716
REMARK 465 GLY F 717
REMARK 465 LYS F 718
REMARK 465 ARG F 719
REMARK 465 GLU F 720
REMARK 465 SER F 721
REMARK 465 ALA F 722
REMARK 465 LYS F 723
REMARK 465 SER F 724
REMARK 465 THR F 725
REMARK 465 ALA F 726
REMARK 465 ARG F 727
REMARK 465 LYS F 728
REMARK 465 LEU F 729
REMARK 465 LEU F 730
REMARK 465 ALA F 731
REMARK 465 ASN F 732
REMARK 465 THR F 733
REMARK 465 THR F 734
REMARK 465 LEU F 735
REMARK 465 SER F 736
REMARK 465 THR F 737
REMARK 465 SER F 738
REMARK 465 ALA F 739
REMARK 465 GLU F 740
REMARK 465 ARG F 741
REMARK 465 ASN F 742
REMARK 465 VAL F 743
REMARK 465 ALA F 744
REMARK 465 GLU F 745
REMARK 465 ASN F 746
REMARK 465 ALA F 747
REMARK 465 PHE F 748
REMARK 465 VAL F 749
REMARK 465 GLU F 750
REMARK 465 ASP F 751
REMARK 465 GLU F 752
REMARK 465 LEU F 753
REMARK 465 PHE F 754
REMARK 465 GLU F 755
REMARK 465 GLN F 756
REMARK 465 GLN F 757
REMARK 465 MET F 758
REMARK 465 LYS F 759
REMARK 465 ASP F 760
REMARK 465 LYS F 761
REMARK 465 ARG F 762
REMARK 465 ASP F 763
REMARK 465 SER F 764
REMARK 465 ARG F 984
REMARK 465 ASP F 985
REMARK 465 VAL F 986
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 GLN A 45 CG CD OE1 NE2
REMARK 470 ARG A 85 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 91 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 92 CG CD CE NZ
REMARK 470 ARG A 94 CG CD NE CZ NH1 NH2
REMARK 470 SER A 104 OG
REMARK 470 LYS A 852 CG CD CE NZ
REMARK 470 LYS A 870 CG CD CE NZ
REMARK 470 LYS A 901 CG CD CE NZ
REMARK 470 ARG A 902 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 905 CG CD OE1 OE2
REMARK 470 LYS A 912 CE NZ
REMARK 470 ARG B 18 CZ NH1 NH2
REMARK 470 LYS B 25 CE NZ
REMARK 470 GLN B 45 CG CD OE1 NE2
REMARK 470 ASN B 48 CG OD1 ND2
REMARK 470 LYS B 51 CG CD CE NZ
REMARK 470 ARG B 85 CZ NH1 NH2
REMARK 470 ARG B 89 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 766 CG CD OE1 OE2
REMARK 470 GLN B 802 CG CD OE1 NE2
REMARK 470 ASN B 833 CG OD1 ND2
REMARK 470 LYS B 845 CG CD CE NZ
REMARK 470 LYS B 912 CE NZ
REMARK 470 VAL E 17 CG1 CG2
REMARK 470 GLU E 20 CG CD OE1 OE2
REMARK 470 GLU E 46 CG CD OE1 OE2
REMARK 470 LYS E 51 CG CD CE NZ
REMARK 470 ARG E 85 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 86 CG CD OE1 OE2
REMARK 470 ARG E 89 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 92 CG CD CE NZ
REMARK 470 LYS E 773 CD CE NZ
REMARK 470 GLU E 792 CG CD OE1 OE2
REMARK 470 GLU E 831 CG CD OE1 OE2
REMARK 470 LYS E 832 CG CD CE NZ
REMARK 470 ASN E 833 CG OD1 ND2
REMARK 470 LYS E 852 CE NZ
REMARK 470 LYS E 870 CG CD CE NZ
REMARK 470 ASP E 900 CG OD1 OD2
REMARK 470 LYS E 903 CG CD CE NZ
REMARK 470 GLU E 905 CG CD OE1 OE2
REMARK 470 LYS E 909 CG CD CE NZ
REMARK 470 LYS E 912 CE NZ
REMARK 470 LYS E 916 CG CD CE NZ
REMARK 470 GLU E 977 CG CD OE1 OE2
REMARK 470 LYS F 25 CE NZ
REMARK 470 LYS F 51 CG CD CE NZ
REMARK 470 LYS F 92 CG CD CE NZ
REMARK 470 ARG F 94 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 832 CE NZ
REMARK 470 LYS F 912 CG CD CE NZ
REMARK 470 DT G 16 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DT G 16 N1 C2 O2 N3 C4 O4 C5
REMARK 470 DT G 16 C7 C6
REMARK 470 DT H 16 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DT H 16 N1 C2 O2 N3 C4 O4 C5
REMARK 470 DT H 16 C7 C6
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 D 14 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DC H 15 O4' - C1' - N1 ANGL. DEV. = 1.8 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 24 -4.64 71.65
REMARK 500 MET A 791 -107.15 -126.60
REMARK 500 ARG A 940 59.88 -117.65
REMARK 500 SER B 5 -6.50 74.69
REMARK 500 ASP B 24 -5.63 65.07
REMARK 500 ASP B 44 -160.56 -115.21
REMARK 500 MET B 791 -106.00 -126.95
REMARK 500 ASP B 926 -160.81 -109.34
REMARK 500 SER E 5 -2.07 68.84
REMARK 500 MET E 791 -106.17 -124.71
REMARK 500 ASN E 804 18.23 57.82
REMARK 500 PHE E 829 44.44 -108.37
REMARK 500 GLU E 831 -48.93 68.19
REMARK 500 SER E 863 -168.52 -169.36
REMARK 500 PHE E 899 53.16 -115.54
REMARK 500 MET F 791 -110.70 -128.99
REMARK 500 ASP F 926 -146.04 -108.59
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 A1001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 794 OE2
REMARK 620 2 ASP A 813 OD2 110.5
REMARK 620 3 ASP A 815 OD2 101.7 94.3
REMARK 620 4 HOH A1117 O 70.7 177.2 87.9
REMARK 620 5 HOH A1178 O 168.9 59.7 84.9 118.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1002 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 869 O
REMARK 620 2 MET A 872 O 71.6
REMARK 620 3 HOH A1126 O 150.4 80.6
REMARK 620 4 HOH A1285 O 107.9 144.9 89.1
REMARK 620 5 DA D 9 OP1 76.6 78.5 107.9 136.4
REMARK 620 6 HOH D 116 O 89.3 136.8 118.5 77.3 59.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 794 OE2
REMARK 620 2 ASP B 813 OD2 89.4
REMARK 620 3 ASP B 815 OD2 91.8 92.3
REMARK 620 4 HOH B1183 O 108.0 53.8 139.1
REMARK 620 5 HOH B1224 O 161.9 75.0 79.9 70.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1002 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU B 860 O
REMARK 620 2 LEU B 869 O 72.5
REMARK 620 3 MET B 872 O 73.9 88.8
REMARK 620 4 HOH B1135 O 112.9 173.4 89.2
REMARK 620 5 HOH B1230 O 88.4 106.0 152.5 78.4
REMARK 620 6 DG C 9 OP1 149.8 85.3 85.7 88.3 117.9
REMARK 620 7 HOH C 102 O 142.9 99.5 143.1 78.4 58.3 59.6
REMARK 620 8 DA D 9 OP1 149.1 84.4 85.7 89.1 118.1 0.8 59.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E1001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 794 OE2
REMARK 620 2 ASP E 813 OD2 87.5
REMARK 620 3 ASP E 815 OD2 93.5 97.8
REMARK 620 4 HOH E1149 O 162.2 78.1 78.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E1002 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU E 869 O
REMARK 620 2 MET E 872 O 79.0
REMARK 620 3 HOH E1109 O 89.4 129.9
REMARK 620 4 HOH E1111 O 110.4 163.3 65.4
REMARK 620 5 HOH E1132 O 157.4 90.7 81.8 84.9
REMARK 620 6 DG G 9 OP1 81.8 90.1 136.6 78.1 118.6
REMARK 620 7 DA H 9 OP1 84.2 90.6 136.9 77.1 116.3 2.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F1001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 794 OE1
REMARK 620 2 ASP F 813 OD2 67.4
REMARK 620 3 ASP F 864 OD2 170.3 102.9
REMARK 620 4 HOH F1101 O 51.5 56.4 124.1
REMARK 620 5 HOH F1258 O 74.6 125.3 112.5 121.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K F1002 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU F 869 O
REMARK 620 2 MET F 872 O 75.7
REMARK 620 3 HOH F1114 O 146.9 89.2
REMARK 620 4 HOH F1248 O 89.2 120.8 73.4
REMARK 620 5 DG G 9 OP1 90.4 91.1 119.6 146.8
REMARK 620 6 DA H 9 OP1 89.1 92.8 121.4 144.7 2.4
REMARK 620 7 HOH H 108 O 90.7 162.9 107.8 68.4 78.4 76.3
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K F 1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4Q0R RELATED DB: PDB
REMARK 900 RELATED ID: 4Q0W RELATED DB: PDB
REMARK 900 RELATED ID: 4Q10 RELATED DB: PDB
DBREF 4Q0Z A 2 731 UNP P07276 RAD2_YEAST 2 111
DBREF 4Q0Z A 732 986 UNP P07276 RAD2_YEAST 732 986
DBREF 4Q0Z B 2 731 UNP P07276 RAD2_YEAST 2 111
DBREF 4Q0Z B 732 986 UNP P07276 RAD2_YEAST 732 986
DBREF 4Q0Z E 2 731 UNP P07276 RAD2_YEAST 2 111
DBREF 4Q0Z E 732 986 UNP P07276 RAD2_YEAST 732 986
DBREF 4Q0Z F 2 731 UNP P07276 RAD2_YEAST 2 111
DBREF 4Q0Z F 732 986 UNP P07276 RAD2_YEAST 732 986
DBREF 4Q0Z C 0 16 PDB 4Q0Z 4Q0Z 0 16
DBREF 4Q0Z G 0 16 PDB 4Q0Z 4Q0Z 0 16
DBREF 4Q0Z D 0 16 PDB 4Q0Z 4Q0Z 0 16
DBREF 4Q0Z H 0 16 PDB 4Q0Z 4Q0Z 0 16
SEQRES 1 A 365 GLY VAL HIS SER PHE TRP ASP ILE ALA GLY PRO THR ALA
SEQRES 2 A 365 ARG PRO VAL ARG LEU GLU SER LEU GLU ASP LYS ARG MET
SEQRES 3 A 365 ALA VAL ASP ALA SER ILE TRP ILE TYR GLN PHE LEU LYS
SEQRES 4 A 365 ALA VAL ARG ASP GLN GLU GLY ASN ALA VAL LYS ASN SER
SEQRES 5 A 365 HIS ILE THR GLY PHE PHE ARG ARG ILE CYS LYS LEU LEU
SEQRES 6 A 365 TYR PHE GLY ILE ARG PRO VAL PHE VAL PHE ASP GLY GLY
SEQRES 7 A 365 VAL PRO VAL LEU LYS ARG GLU THR ILE ARG GLN ARG LYS
SEQRES 8 A 365 GLU ARG ARG GLN GLY LYS ARG GLU SER ALA LYS SER THR
SEQRES 9 A 365 ALA ARG LYS LEU LEU ALA ASN THR THR LEU SER THR SER
SEQRES 10 A 365 ALA GLU ARG ASN VAL ALA GLU ASN ALA PHE VAL GLU ASP
SEQRES 11 A 365 GLU LEU PHE GLU GLN GLN MET LYS ASP LYS ARG ASP SER
SEQRES 12 A 365 ASP GLU VAL THR MET ASP MET ILE LYS GLU VAL GLN GLU
SEQRES 13 A 365 LEU LEU SER ARG PHE GLY ILE PRO TYR ILE THR ALA PRO
SEQRES 14 A 365 MET GLU ALA GLU ALA GLN CYS ALA GLU LEU LEU GLN LEU
SEQRES 15 A 365 ASN LEU VAL ASP GLY ILE ILE THR ASP ASP SER ASP VAL
SEQRES 16 A 365 PHE LEU PHE GLY GLY THR LYS ILE TYR LYS ASN MET PHE
SEQRES 17 A 365 HIS GLU LYS ASN TYR VAL GLU PHE TYR ASP ALA GLU SER
SEQRES 18 A 365 ILE LEU LYS LEU LEU GLY LEU ASP ARG LYS ASN MET ILE
SEQRES 19 A 365 GLU LEU ALA GLN LEU LEU GLY SER ASP TYR THR ASN GLY
SEQRES 20 A 365 LEU LYS GLY MET GLY PRO VAL SER SER ILE GLU VAL ILE
SEQRES 21 A 365 ALA GLU PHE GLY ASN LEU LYS ASN PHE LYS ASP TRP TYR
SEQRES 22 A 365 ASN ASN GLY GLN PHE ASP LYS ARG LYS GLN GLU THR GLU
SEQRES 23 A 365 ASN LYS PHE GLU LYS ASP LEU ARG LYS LYS LEU VAL ASN
SEQRES 24 A 365 ASN GLU ILE ILE LEU ASP ASP ASP PHE PRO SER VAL MET
SEQRES 25 A 365 VAL TYR ASP ALA TYR MET ARG PRO GLU VAL ASP HIS ASP
SEQRES 26 A 365 THR THR PRO PHE VAL TRP GLY VAL PRO ASP LEU ASP MET
SEQRES 27 A 365 LEU ARG SER PHE MET LYS THR GLN LEU GLY TRP PRO HIS
SEQRES 28 A 365 GLU LYS SER ASP GLU ILE LEU ILE PRO LEU ILE ARG ASP
SEQRES 29 A 365 VAL
SEQRES 1 B 365 GLY VAL HIS SER PHE TRP ASP ILE ALA GLY PRO THR ALA
SEQRES 2 B 365 ARG PRO VAL ARG LEU GLU SER LEU GLU ASP LYS ARG MET
SEQRES 3 B 365 ALA VAL ASP ALA SER ILE TRP ILE TYR GLN PHE LEU LYS
SEQRES 4 B 365 ALA VAL ARG ASP GLN GLU GLY ASN ALA VAL LYS ASN SER
SEQRES 5 B 365 HIS ILE THR GLY PHE PHE ARG ARG ILE CYS LYS LEU LEU
SEQRES 6 B 365 TYR PHE GLY ILE ARG PRO VAL PHE VAL PHE ASP GLY GLY
SEQRES 7 B 365 VAL PRO VAL LEU LYS ARG GLU THR ILE ARG GLN ARG LYS
SEQRES 8 B 365 GLU ARG ARG GLN GLY LYS ARG GLU SER ALA LYS SER THR
SEQRES 9 B 365 ALA ARG LYS LEU LEU ALA ASN THR THR LEU SER THR SER
SEQRES 10 B 365 ALA GLU ARG ASN VAL ALA GLU ASN ALA PHE VAL GLU ASP
SEQRES 11 B 365 GLU LEU PHE GLU GLN GLN MET LYS ASP LYS ARG ASP SER
SEQRES 12 B 365 ASP GLU VAL THR MET ASP MET ILE LYS GLU VAL GLN GLU
SEQRES 13 B 365 LEU LEU SER ARG PHE GLY ILE PRO TYR ILE THR ALA PRO
SEQRES 14 B 365 MET GLU ALA GLU ALA GLN CYS ALA GLU LEU LEU GLN LEU
SEQRES 15 B 365 ASN LEU VAL ASP GLY ILE ILE THR ASP ASP SER ASP VAL
SEQRES 16 B 365 PHE LEU PHE GLY GLY THR LYS ILE TYR LYS ASN MET PHE
SEQRES 17 B 365 HIS GLU LYS ASN TYR VAL GLU PHE TYR ASP ALA GLU SER
SEQRES 18 B 365 ILE LEU LYS LEU LEU GLY LEU ASP ARG LYS ASN MET ILE
SEQRES 19 B 365 GLU LEU ALA GLN LEU LEU GLY SER ASP TYR THR ASN GLY
SEQRES 20 B 365 LEU LYS GLY MET GLY PRO VAL SER SER ILE GLU VAL ILE
SEQRES 21 B 365 ALA GLU PHE GLY ASN LEU LYS ASN PHE LYS ASP TRP TYR
SEQRES 22 B 365 ASN ASN GLY GLN PHE ASP LYS ARG LYS GLN GLU THR GLU
SEQRES 23 B 365 ASN LYS PHE GLU LYS ASP LEU ARG LYS LYS LEU VAL ASN
SEQRES 24 B 365 ASN GLU ILE ILE LEU ASP ASP ASP PHE PRO SER VAL MET
SEQRES 25 B 365 VAL TYR ASP ALA TYR MET ARG PRO GLU VAL ASP HIS ASP
SEQRES 26 B 365 THR THR PRO PHE VAL TRP GLY VAL PRO ASP LEU ASP MET
SEQRES 27 B 365 LEU ARG SER PHE MET LYS THR GLN LEU GLY TRP PRO HIS
SEQRES 28 B 365 GLU LYS SER ASP GLU ILE LEU ILE PRO LEU ILE ARG ASP
SEQRES 29 B 365 VAL
SEQRES 1 C 17 DT DG DC DT DC DC DC DT DT DG DT DC DT
SEQRES 2 C 17 DC DA DG DT
SEQRES 1 D 17 DT DC DT DG DA DG DA DC DA DA DG DG DG
SEQRES 2 D 17 DA DG DC DT
SEQRES 1 E 365 GLY VAL HIS SER PHE TRP ASP ILE ALA GLY PRO THR ALA
SEQRES 2 E 365 ARG PRO VAL ARG LEU GLU SER LEU GLU ASP LYS ARG MET
SEQRES 3 E 365 ALA VAL ASP ALA SER ILE TRP ILE TYR GLN PHE LEU LYS
SEQRES 4 E 365 ALA VAL ARG ASP GLN GLU GLY ASN ALA VAL LYS ASN SER
SEQRES 5 E 365 HIS ILE THR GLY PHE PHE ARG ARG ILE CYS LYS LEU LEU
SEQRES 6 E 365 TYR PHE GLY ILE ARG PRO VAL PHE VAL PHE ASP GLY GLY
SEQRES 7 E 365 VAL PRO VAL LEU LYS ARG GLU THR ILE ARG GLN ARG LYS
SEQRES 8 E 365 GLU ARG ARG GLN GLY LYS ARG GLU SER ALA LYS SER THR
SEQRES 9 E 365 ALA ARG LYS LEU LEU ALA ASN THR THR LEU SER THR SER
SEQRES 10 E 365 ALA GLU ARG ASN VAL ALA GLU ASN ALA PHE VAL GLU ASP
SEQRES 11 E 365 GLU LEU PHE GLU GLN GLN MET LYS ASP LYS ARG ASP SER
SEQRES 12 E 365 ASP GLU VAL THR MET ASP MET ILE LYS GLU VAL GLN GLU
SEQRES 13 E 365 LEU LEU SER ARG PHE GLY ILE PRO TYR ILE THR ALA PRO
SEQRES 14 E 365 MET GLU ALA GLU ALA GLN CYS ALA GLU LEU LEU GLN LEU
SEQRES 15 E 365 ASN LEU VAL ASP GLY ILE ILE THR ASP ASP SER ASP VAL
SEQRES 16 E 365 PHE LEU PHE GLY GLY THR LYS ILE TYR LYS ASN MET PHE
SEQRES 17 E 365 HIS GLU LYS ASN TYR VAL GLU PHE TYR ASP ALA GLU SER
SEQRES 18 E 365 ILE LEU LYS LEU LEU GLY LEU ASP ARG LYS ASN MET ILE
SEQRES 19 E 365 GLU LEU ALA GLN LEU LEU GLY SER ASP TYR THR ASN GLY
SEQRES 20 E 365 LEU LYS GLY MET GLY PRO VAL SER SER ILE GLU VAL ILE
SEQRES 21 E 365 ALA GLU PHE GLY ASN LEU LYS ASN PHE LYS ASP TRP TYR
SEQRES 22 E 365 ASN ASN GLY GLN PHE ASP LYS ARG LYS GLN GLU THR GLU
SEQRES 23 E 365 ASN LYS PHE GLU LYS ASP LEU ARG LYS LYS LEU VAL ASN
SEQRES 24 E 365 ASN GLU ILE ILE LEU ASP ASP ASP PHE PRO SER VAL MET
SEQRES 25 E 365 VAL TYR ASP ALA TYR MET ARG PRO GLU VAL ASP HIS ASP
SEQRES 26 E 365 THR THR PRO PHE VAL TRP GLY VAL PRO ASP LEU ASP MET
SEQRES 27 E 365 LEU ARG SER PHE MET LYS THR GLN LEU GLY TRP PRO HIS
SEQRES 28 E 365 GLU LYS SER ASP GLU ILE LEU ILE PRO LEU ILE ARG ASP
SEQRES 29 E 365 VAL
SEQRES 1 F 365 GLY VAL HIS SER PHE TRP ASP ILE ALA GLY PRO THR ALA
SEQRES 2 F 365 ARG PRO VAL ARG LEU GLU SER LEU GLU ASP LYS ARG MET
SEQRES 3 F 365 ALA VAL ASP ALA SER ILE TRP ILE TYR GLN PHE LEU LYS
SEQRES 4 F 365 ALA VAL ARG ASP GLN GLU GLY ASN ALA VAL LYS ASN SER
SEQRES 5 F 365 HIS ILE THR GLY PHE PHE ARG ARG ILE CYS LYS LEU LEU
SEQRES 6 F 365 TYR PHE GLY ILE ARG PRO VAL PHE VAL PHE ASP GLY GLY
SEQRES 7 F 365 VAL PRO VAL LEU LYS ARG GLU THR ILE ARG GLN ARG LYS
SEQRES 8 F 365 GLU ARG ARG GLN GLY LYS ARG GLU SER ALA LYS SER THR
SEQRES 9 F 365 ALA ARG LYS LEU LEU ALA ASN THR THR LEU SER THR SER
SEQRES 10 F 365 ALA GLU ARG ASN VAL ALA GLU ASN ALA PHE VAL GLU ASP
SEQRES 11 F 365 GLU LEU PHE GLU GLN GLN MET LYS ASP LYS ARG ASP SER
SEQRES 12 F 365 ASP GLU VAL THR MET ASP MET ILE LYS GLU VAL GLN GLU
SEQRES 13 F 365 LEU LEU SER ARG PHE GLY ILE PRO TYR ILE THR ALA PRO
SEQRES 14 F 365 MET GLU ALA GLU ALA GLN CYS ALA GLU LEU LEU GLN LEU
SEQRES 15 F 365 ASN LEU VAL ASP GLY ILE ILE THR ASP ASP SER ASP VAL
SEQRES 16 F 365 PHE LEU PHE GLY GLY THR LYS ILE TYR LYS ASN MET PHE
SEQRES 17 F 365 HIS GLU LYS ASN TYR VAL GLU PHE TYR ASP ALA GLU SER
SEQRES 18 F 365 ILE LEU LYS LEU LEU GLY LEU ASP ARG LYS ASN MET ILE
SEQRES 19 F 365 GLU LEU ALA GLN LEU LEU GLY SER ASP TYR THR ASN GLY
SEQRES 20 F 365 LEU LYS GLY MET GLY PRO VAL SER SER ILE GLU VAL ILE
SEQRES 21 F 365 ALA GLU PHE GLY ASN LEU LYS ASN PHE LYS ASP TRP TYR
SEQRES 22 F 365 ASN ASN GLY GLN PHE ASP LYS ARG LYS GLN GLU THR GLU
SEQRES 23 F 365 ASN LYS PHE GLU LYS ASP LEU ARG LYS LYS LEU VAL ASN
SEQRES 24 F 365 ASN GLU ILE ILE LEU ASP ASP ASP PHE PRO SER VAL MET
SEQRES 25 F 365 VAL TYR ASP ALA TYR MET ARG PRO GLU VAL ASP HIS ASP
SEQRES 26 F 365 THR THR PRO PHE VAL TRP GLY VAL PRO ASP LEU ASP MET
SEQRES 27 F 365 LEU ARG SER PHE MET LYS THR GLN LEU GLY TRP PRO HIS
SEQRES 28 F 365 GLU LYS SER ASP GLU ILE LEU ILE PRO LEU ILE ARG ASP
SEQRES 29 F 365 VAL
SEQRES 1 G 17 DT DG DC DT DC DC DC DT DT DG DT DC DT
SEQRES 2 G 17 DC DA DG DT
SEQRES 1 H 17 DT DC DT DG DA DG DA DC DA DA DG DG DG
SEQRES 2 H 17 DA DG DC DT
HET CA A1001 1
HET K A1002 1
HET CA B1001 1
HET K B1002 1
HET CA E1001 1
HET K E1002 1
HET CA F1001 1
HET K F1002 1
HETNAM CA CALCIUM ION
HETNAM K POTASSIUM ION
FORMUL 9 CA 4(CA 2+)
FORMUL 10 K 4(K 1+)
FORMUL 17 HOH *823(H2 O)
HELIX 1 1 SER A 5 GLY A 11 1 7
HELIX 2 2 PRO A 12 ALA A 14 5 3
HELIX 3 3 GLU A 20 GLU A 23 5 4
HELIX 4 4 ILE A 33 VAL A 42 1 10
HELIX 5 5 ASN A 52 PHE A 68 1 17
HELIX 6 6 PRO A 81 GLY A 97 1 17
HELIX 7 7 THR A 768 PHE A 782 1 15
HELIX 8 8 GLU A 792 LEU A 803 1 12
HELIX 9 9 SER A 814 PHE A 819 1 6
HELIX 10 10 ASP A 839 GLY A 848 1 10
HELIX 11 11 ASP A 850 GLY A 862 1 13
HELIX 12 12 GLY A 873 GLY A 885 1 13
HELIX 13 13 ASN A 886 GLY A 897 1 12
HELIX 14 14 ASN A 908 ASN A 921 1 14
HELIX 15 15 SER A 931 ARG A 940 1 10
HELIX 16 16 ASP A 956 GLY A 969 1 14
HELIX 17 17 PRO A 971 ILE A 983 1 13
HELIX 18 18 SER B 5 GLY B 11 1 7
HELIX 19 19 PRO B 12 ALA B 14 5 3
HELIX 20 20 GLU B 20 GLU B 23 5 4
HELIX 21 21 ILE B 33 VAL B 42 1 10
HELIX 22 22 ASN B 52 PHE B 68 1 17
HELIX 23 23 PRO B 81 ARG B 89 1 9
HELIX 24 24 THR B 768 PHE B 782 1 15
HELIX 25 25 GLU B 792 LEU B 803 1 12
HELIX 26 26 SER B 814 PHE B 819 1 6
HELIX 27 27 ASP B 839 GLY B 848 1 10
HELIX 28 28 ASP B 850 GLY B 862 1 13
HELIX 29 29 GLY B 873 GLY B 885 1 13
HELIX 30 30 ASN B 886 ASP B 900 1 15
HELIX 31 31 ASP B 900 THR B 906 1 7
HELIX 32 32 ASN B 908 ASN B 921 1 14
HELIX 33 33 SER B 931 ARG B 940 1 10
HELIX 34 34 ASP B 956 GLY B 969 1 14
HELIX 35 35 PRO B 971 ILE B 980 1 10
HELIX 36 36 PRO B 981 ILE B 983 5 3
HELIX 37 37 SER E 5 GLY E 11 1 7
HELIX 38 38 PRO E 12 ALA E 14 5 3
HELIX 39 39 ARG E 18 GLU E 23 5 6
HELIX 40 40 ILE E 33 VAL E 42 1 10
HELIX 41 41 ASN E 52 PHE E 68 1 17
HELIX 42 42 PRO E 81 LYS E 92 1 12
HELIX 43 43 THR E 768 GLY E 783 1 16
HELIX 44 44 GLU E 792 LEU E 803 1 12
HELIX 45 45 SER E 814 PHE E 819 1 6
HELIX 46 46 ASP E 839 GLY E 848 1 10
HELIX 47 47 ASP E 850 GLY E 862 1 13
HELIX 48 48 GLY E 873 GLY E 885 1 13
HELIX 49 49 ASN E 886 GLN E 898 1 13
HELIX 50 50 ASN E 908 ASN E 921 1 14
HELIX 51 51 SER E 931 ARG E 940 1 10
HELIX 52 52 ASP E 956 GLY E 969 1 14
HELIX 53 53 PRO E 971 ILE E 980 1 10
HELIX 54 54 SER F 5 GLY F 11 1 7
HELIX 55 55 PRO F 12 ALA F 14 5 3
HELIX 56 56 ARG F 18 GLU F 23 5 6
HELIX 57 57 ILE F 33 VAL F 42 1 10
HELIX 58 58 ASN F 52 PHE F 68 1 17
HELIX 59 59 PRO F 81 ARG F 94 1 14
HELIX 60 60 THR F 768 GLY F 783 1 16
HELIX 61 61 GLU F 792 LEU F 803 1 12
HELIX 62 62 SER F 814 PHE F 819 1 6
HELIX 63 63 ASP F 839 GLY F 848 1 10
HELIX 64 64 ASP F 850 GLY F 862 1 13
HELIX 65 65 GLY F 873 GLY F 885 1 13
HELIX 66 66 ASN F 886 ASP F 900 1 15
HELIX 67 67 LYS F 901 GLU F 907 5 7
HELIX 68 68 ASN F 908 ASN F 921 1 14
HELIX 69 69 SER F 931 ARG F 940 1 10
HELIX 70 70 ASP F 956 GLY F 969 1 14
HELIX 71 71 PRO F 971 ILE F 983 1 13
SHEET 1 A 7 ARG A 15 ARG A 18 0
SHEET 2 A 7 TYR A 834 TYR A 838 -1 O PHE A 837 N ARG A 15
SHEET 3 A 7 ILE A 824 LYS A 826 -1 N LYS A 826 O GLU A 836
SHEET 4 A 7 GLY A 808 ILE A 810 1 N ILE A 809 O TYR A 825
SHEET 5 A 7 ARG A 26 ASP A 30 1 N ALA A 28 O ILE A 810
SHEET 6 A 7 ARG A 71 PHE A 76 1 O VAL A 73 N VAL A 29
SHEET 7 A 7 TYR A 786 THR A 788 1 O ILE A 787 N PHE A 74
SHEET 1 B 7 ARG B 15 ARG B 18 0
SHEET 2 B 7 TYR B 834 TYR B 838 -1 O PHE B 837 N ARG B 15
SHEET 3 B 7 ILE B 824 LYS B 826 -1 N ILE B 824 O TYR B 838
SHEET 4 B 7 GLY B 808 ILE B 810 1 N ILE B 809 O TYR B 825
SHEET 5 B 7 ARG B 26 ASP B 30 1 N ALA B 28 O ILE B 810
SHEET 6 B 7 ARG B 71 PHE B 76 1 O VAL B 73 N VAL B 29
SHEET 7 B 7 TYR B 786 THR B 788 1 O ILE B 787 N PHE B 74
SHEET 1 C 7 ARG E 15 PRO E 16 0
SHEET 2 C 7 GLU E 836 TYR E 838 -1 O PHE E 837 N ARG E 15
SHEET 3 C 7 ILE E 824 LYS E 826 -1 N LYS E 826 O GLU E 836
SHEET 4 C 7 GLY E 808 ILE E 810 1 N ILE E 809 O TYR E 825
SHEET 5 C 7 ARG E 26 ASP E 30 1 N ALA E 28 O ILE E 810
SHEET 6 C 7 ARG E 71 PHE E 76 1 O VAL E 73 N VAL E 29
SHEET 7 C 7 TYR E 786 THR E 788 1 O ILE E 787 N PHE E 74
SHEET 1 D 6 TYR F 786 THR F 788 0
SHEET 2 D 6 ARG F 71 PHE F 76 1 N PHE F 74 O ILE F 787
SHEET 3 D 6 ARG F 26 ASP F 30 1 N VAL F 29 O VAL F 73
SHEET 4 D 6 GLY F 808 ILE F 810 1 O ILE F 810 N ALA F 28
SHEET 5 D 6 ILE F 824 LYS F 826 1 O TYR F 825 N ILE F 809
SHEET 6 D 6 GLU F 836 TYR F 838 -1 O TYR F 838 N ILE F 824
LINK OE2BGLU A 794 CA CA A1001 1555 1555 2.39
LINK OD2 ASP A 813 CA CA A1001 1555 1555 3.04
LINK OD2 ASP A 815 CA CA A1001 1555 1555 2.77
LINK O LEU A 869 K K A1002 1555 1555 3.29
LINK O MET A 872 K K A1002 1555 1555 3.38
LINK CA CA A1001 O HOH A1117 1555 1555 2.79
LINK CA CA A1001 O HOH A1178 1555 1555 2.98
LINK K K A1002 O HOH A1126 1555 1555 2.49
LINK K K A1002 O HOH A1285 1555 1555 2.51
LINK K K A1002 OP1B DA D 9 1555 1555 3.43
LINK K K A1002 O HOH D 116 1555 1555 2.60
LINK OE2 GLU B 794 CA CA B1001 1555 1555 2.48
LINK OD2 ASP B 813 CA CA B1001 1555 1555 2.52
LINK OD2 ASP B 815 CA CA B1001 1555 1555 3.01
LINK O LEU B 860 K K B1002 1555 1555 3.34
LINK O LEU B 869 K K B1002 1555 1555 2.76
LINK O MET B 872 K K B1002 1555 1555 2.92
LINK CA CA B1001 O HOH B1183 1555 1555 2.97
LINK CA CA B1001 O HOH B1224 1555 1555 2.36
LINK K K B1002 O HOH B1135 1555 1555 2.62
LINK K K B1002 O HOH B1230 1555 1555 2.62
LINK K K B1002 OP1B DG C 9 1555 1555 3.18
LINK K K B1002 O HOH C 102 1555 1555 2.80
LINK K K B1002 OP1A DA D 9 1555 1555 3.18
LINK OE2 GLU E 794 CA CA E1001 1555 1555 2.59
LINK OD2 ASP E 813 CA CA E1001 1555 1555 2.59
LINK OD2 ASP E 815 CA CA E1001 1555 1555 2.58
LINK O LEU E 869 K K E1002 1555 1555 3.19
LINK O MET E 872 K K E1002 1555 1555 2.98
LINK CA CA E1001 O HOH E1149 1555 1555 2.56
LINK K K E1002 O HOH E1109 1555 1555 2.55
LINK K K E1002 O HOH E1111 1555 1555 2.56
LINK K K E1002 O HOH E1132 1555 1555 2.54
LINK K K E1002 OP1A DG G 9 1555 1555 3.21
LINK K K E1002 OP1B DA H 9 1555 1555 3.12
LINK OE1 GLU F 794 CA CA F1001 1555 1555 2.73
LINK OD2 ASP F 813 CA CA F1001 1555 1555 2.92
LINK OD2 ASP F 864 CA CA F1001 1555 1555 2.76
LINK O LEU F 869 K K F1002 1555 1555 3.18
LINK O MET F 872 K K F1002 1555 1555 3.30
LINK CA CA F1001 O HOH F1101 1555 1555 2.67
LINK CA CA F1001 O HOH F1258 1555 1555 2.40
LINK K K F1002 O HOH F1114 1555 1555 2.56
LINK K K F1002 O HOH F1248 1555 1555 2.68
LINK K K F1002 OP1B DG G 9 1555 1555 3.06
LINK K K F1002 OP1A DA H 9 1555 1555 3.27
LINK K K F1002 O HOH H 108 1555 1555 2.50
CISPEP 1 PHE A 929 PRO A 930 0 -6.82
CISPEP 2 PHE B 929 PRO B 930 0 -6.29
CISPEP 3 PHE E 929 PRO E 930 0 -0.49
CISPEP 4 PHE F 929 PRO F 930 0 -4.85
SITE 1 AC1 5 GLU A 794 ASP A 813 ASP A 815 HOH A1117
SITE 2 AC1 5 HOH A1178
SITE 1 AC2 7 LEU A 869 MET A 872 HOH A1126 HOH A1285
SITE 2 AC2 7 DG C 9 DA D 9 HOH D 116
SITE 1 AC3 7 LYS B 84 GLU B 794 ASP B 813 ASP B 815
SITE 2 AC3 7 ASP B 864 HOH B1183 HOH B1224
SITE 1 AC4 9 LEU B 860 LEU B 861 LEU B 869 MET B 872
SITE 2 AC4 9 HOH B1135 HOH B1230 DG C 9 HOH C 102
SITE 3 AC4 9 DA D 9
SITE 1 AC5 5 GLU E 794 ASP E 813 ASP E 815 ASP E 864
SITE 2 AC5 5 HOH E1149
SITE 1 AC6 7 LEU E 869 MET E 872 HOH E1109 HOH E1111
SITE 2 AC6 7 HOH E1132 DG G 9 DA H 9
SITE 1 AC7 6 GLU F 794 ASP F 813 ASP F 815 ASP F 864
SITE 2 AC7 6 HOH F1101 HOH F1258
SITE 1 AC8 7 LEU F 869 MET F 872 HOH F1114 HOH F1248
SITE 2 AC8 7 DG G 9 DA H 9 HOH H 108
CRYST1 110.278 86.039 134.440 90.00 110.95 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 0.009068 0.000000 0.003472 0.00000
SCALE2 0.000000 0.011623 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007965 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
