HEADER REPLICATION 20-APR-01 1II8
TITLE CRYSTAL STRUCTURE OF THE P. FURIOSUS RAD50 ATPASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAD50 ABC-ATPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL FRAGMENT;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: RAD50 ABC-ATPASE;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: C-TERMINAL FRAGMENT;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 8 ORGANISM_TAXID: 2261;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS RAD50, MRE11, DNA DOUBLE-STRAND BREAK REPAIR, ATP, REPLICATION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.-P.HOPFNER,A.KARCHER,L.CRAIG,T.T.WOO,J.P.CARNEY,J.A.TAINER
REVDAT 4 16-AUG-23 1II8 1 REMARK
REVDAT 3 24-FEB-09 1II8 1 VERSN
REVDAT 2 01-APR-03 1II8 1 JRNL
REVDAT 1 30-MAY-01 1II8 0
JRNL AUTH K.P.HOPFNER,A.KARCHER,L.CRAIG,T.T.WOO,J.P.CARNEY,J.A.TAINER
JRNL TITL STRUCTURAL BIOCHEMISTRY AND INTERACTION ARCHITECTURE OF THE
JRNL TITL 2 DNA DOUBLE-STRAND BREAK REPAIR MRE11 NUCLEASE AND
JRNL TITL 3 RAD50-ATPASE.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 105 473 2001
JRNL REFN ISSN 0092-8674
JRNL PMID 11371344
JRNL DOI 10.1016/S0092-8674(01)00335-X
REMARK 2
REMARK 2 RESOLUTION. 3.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH&HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1889335.260
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.6
REMARK 3 NUMBER OF REFLECTIONS : 11823
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.255
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 604
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.012
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.02
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 990
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3002
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 63
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 90.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 33.31000
REMARK 3 B22 (A**2) : 33.31000
REMARK 3 B33 (A**2) : -66.61000
REMARK 3 B12 (A**2) : 23.67000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.56
REMARK 3 ESD FROM SIGMAA (A) : 1.07
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.50
REMARK 3 ESD FROM C-V SIGMAA (A) : 1.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.930
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.350 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.410 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.660 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.830 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.22
REMARK 3 BSOL : 63.72
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1II8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013292.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-AUG-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119376
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.0
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 47.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.34800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1F2T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NA-ACETATE, 8% PEG 6K, 10 MM CA
REMARK 280 -ACETATE, PH 6.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.80233
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 77.60467
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 77.60467
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 38.80233
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -135.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 172.39275
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 77.60467
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 LYS B 721
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 LYS A 2 NZ
REMARK 480 LEU A 3 CD1 CD2
REMARK 480 VAL A 6 CG1 CG2
REMARK 480 ILE A 25 CD1
REMARK 480 ILE A 29 CD1
REMARK 480 GLN A 31 OE1 NE2
REMARK 480 LEU A 39 CD1 CD2
REMARK 480 LEU A 40 CD1 CD2
REMARK 480 LEU A 51 CD1 CD2
REMARK 480 ARG A 52 CZ NH1 NH2
REMARK 480 ILE A 53 CD1
REMARK 480 LYS A 57 CB CG CD CE NZ
REMARK 480 LYS A 58 CD CE NZ
REMARK 480 ASP A 59 CG OD1 OD2
REMARK 480 LYS A 63 CG CD CE NZ
REMARK 480 ALA A 66 CB
REMARK 480 ILE A 71 CD1
REMARK 480 LEU A 73 CD1 CD2
REMARK 480 ILE A 74 CD1
REMARK 480 GLU A 76 OE1 OE2
REMARK 480 LYS A 81 CD CE NZ
REMARK 480 ILE A 84 CD1
REMARK 480 GLU A 96 OE1 OE2
REMARK 480 LYS A 101 CE NZ
REMARK 480 VAL A 104 CG1 CG2
REMARK 480 GLU A 107 CB CG CD OE1 OE2
REMARK 480 LYS A 109 CG CD CE NZ
REMARK 480 GLU A 113 OE1 OE2
REMARK 480 LYS A 117 CD CE NZ
REMARK 480 LYS A 125 CG CD CE NZ
REMARK 480 LEU A 126 CD1 CD2
REMARK 480 ILE A 127 CD1
REMARK 480 LEU A 133 CD1 CD2
REMARK 480 ILE A 136 CD1
REMARK 480 ARG A 139 CG CD NE CZ NH1 NH2
REMARK 480 ILE A 143 CD1
REMARK 480 LEU A 147 CG CD1 CD2
REMARK 480 GLU A 148 CD OE1 OE2
REMARK 480 SER A 149 CB OG
REMARK 480 GLU A 154 OE1 OE2
REMARK 480 LYS A 155 CG CD CE NZ
REMARK 480 VAL A 157 CG1 CG2
REMARK 480 LEU A 161 CD1 CD2
REMARK 480 LEU A 163 CD1 CD2
REMARK 480 ASP A 164 OD1 OD2
REMARK 480 LYS A 165 NZ
REMARK 480 ALA A 169 CB
REMARK 480 LYS A 171 CD CE NZ
REMARK 480 LEU A 173 CD1 CD2
REMARK 480 GLU A 175 CG CD OE1 OE2
REMARK 480 LEU A 176 CD1 CD2
REMARK 480 LYS A 177 NZ
REMARK 480 ILE A 184 CD1
REMARK 480 LYS A 185 NZ
REMARK 480 ILE A 190 CG1 CG2 CD1
REMARK 480 THR A 194 CB OG1 CG2
REMARK 480 GLU B 710 CB CG CD OE1 OE2
REMARK 480 VAL B 712 CG1 CG2
REMARK 480 LYS B 713 NZ
REMARK 480 LYS B 714 CG CD CE NZ
REMARK 480 ILE B 716 CD1
REMARK 480 LYS B 717 CG CD CE NZ
REMARK 480 LYS B 723 CD CE NZ
REMARK 480 LEU B 729 CD1 CD2
REMARK 480 ILE B 730 CD1
REMARK 480 GLU B 731 CG CD OE1 OE2
REMARK 480 LYS B 732 CE NZ
REMARK 480 LYS B 735 CD CE NZ
REMARK 480 LYS B 737 CG CD CE NZ
REMARK 480 ALA B 740 CB
REMARK 480 LEU B 745 CD1 CD2
REMARK 480 LYS B 747 CE NZ
REMARK 480 ILE B 748 CD1
REMARK 480 ILE B 755 CD1
REMARK 480 LYS B 763 CG CD CE NZ
REMARK 480 VAL B 767 CG1 CG2
REMARK 480 VAL B 769 CG1 CG2
REMARK 480 ALA B 771 CB
REMARK 480 GLU B 773 CG CD OE1 OE2
REMARK 480 LYS B 775 CG CD CE NZ
REMARK 480 VAL B 776 CG1 CG2
REMARK 480 ARG B 777 CG CD NE CZ NH1 NH2
REMARK 480 VAL B 780 CG1 CG2
REMARK 480 LYS B 785 CG CD CE NZ
REMARK 480 LEU B 789 CG CD1 CD2
REMARK 480 ILE B 798 CD1
REMARK 480 ALA B 799 CB
REMARK 480 LEU B 800 CD1 CD2
REMARK 480 LEU B 806 CD1 CD2
REMARK 480 LEU B 812 CD1 CD2
REMARK 480 ILE B 816 CD1
REMARK 480 ILE B 820 CD1
REMARK 480 LEU B 821 CD1 CD2
REMARK 480 LEU B 828 CD1 CD2
REMARK 480 GLU B 831 CG CD OE1 OE2
REMARK 480 ARG B 834 CG CD NE CZ NH1 NH2
REMARK 480 LYS B 835 CE NZ
REMARK 480 LEU B 836 CD1 CD2
REMARK 480 ILE B 837 CD1
REMARK 480 THR B 838 OG1 CG2
REMARK 480 ILE B 839 CG1 CG2 CD1
REMARK 480 GLU B 841 OE1 OE2
REMARK 480 ILE B 851 CD1
REMARK 480 LEU B 852 CD1 CD2
REMARK 480 SER B 854 OG
REMARK 480 LEU B 859 CD1 CD2
REMARK 480 LYS B 860 CG CD CE NZ
REMARK 480 ALA B 863 CB
REMARK 480 VAL B 866 CG1 CG2
REMARK 480 ILE B 869 CD1
REMARK 480 LEU B 871 CD1 CD2
REMARK 480 GLU B 872 CB CG CD OE1 OE2
REMARK 480 LYS B 877 CG CD CE NZ
REMARK 480 VAL B 878 CG1 CG2
REMARK 480 VAL B 881 CG1 CG2
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 ARG A 5 119.18 -161.66
REMARK 500 ASN A 10 48.30 72.92
REMARK 500 ARG A 12 -148.91 59.41
REMARK 500 ASP A 16 61.71 -156.61
REMARK 500 ILE A 43 -70.90 -46.66
REMARK 500 TRP A 49 142.99 -36.74
REMARK 500 LEU A 51 153.92 -49.12
REMARK 500 LYS A 54 -108.53 51.76
REMARK 500 ASP A 55 34.02 -149.94
REMARK 500 PHE A 61 -68.46 -103.23
REMARK 500 THR A 62 -67.12 -28.70
REMARK 500 SER A 94 92.50 47.82
REMARK 500 ALA A 99 130.28 -173.03
REMARK 500 HIS A 110 174.79 -58.03
REMARK 500 VAL A 111 20.67 -148.32
REMARK 500 THR A 112 150.98 165.84
REMARK 500 GLU A 113 123.53 -37.42
REMARK 500 PRO A 114 38.71 -64.00
REMARK 500 ILE A 127 83.58 -177.35
REMARK 500 PRO A 128 138.92 -39.33
REMARK 500 PHE A 132 -71.32 -70.51
REMARK 500 LEU A 133 -19.19 -48.71
REMARK 500 ALA A 135 -37.32 -165.06
REMARK 500 ILE A 138 99.77 -69.98
REMARK 500 SER A 149 -168.16 67.55
REMARK 500 GLU A 159 -80.36 -70.91
REMARK 500 ASP A 164 -70.52 -56.74
REMARK 500 LYS A 165 -75.38 -25.13
REMARK 500 PHE A 166 -70.55 -29.68
REMARK 500 GLU B 710 -76.08 -51.46
REMARK 500 ALA B 738 -75.31 -50.44
REMARK 500 ASN B 774 48.77 33.17
REMARK 500 LYS B 775 128.63 179.93
REMARK 500 ALA B 799 -74.41 -56.70
REMARK 500 GLU B 823 98.64 50.66
REMARK 500 LEU B 828 66.14 35.23
REMARK 500 TYR B 843 -53.90 -142.17
REMARK 500 GLU B 857 -44.39 -26.38
REMARK 500 ASN B 873 72.31 58.85
REMARK 500 VAL B 881 -33.42 -142.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1003
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1II7 RELATED DB: PDB
REMARK 900 RELATED ID: 1F2T RELATED DB: PDB
REMARK 900 RELATED ID: 1F2U RELATED DB: PDB
DBREF 1II8 A 1 195 UNP P58301 RAD50_PYRFU 1 195
DBREF 1II8 B 709 882 UNP P58301 RAD50_PYRFU 709 882
SEQRES 1 A 195 MET LYS LEU GLU ARG VAL THR VAL LYS ASN PHE ARG SER
SEQRES 2 A 195 HIS SER ASP THR VAL VAL GLU PHE LYS GLU GLY ILE ASN
SEQRES 3 A 195 LEU ILE ILE GLY GLN ASN GLY SER GLY LYS SER SER LEU
SEQRES 4 A 195 LEU ASP ALA ILE LEU VAL GLY LEU TYR TRP PRO LEU ARG
SEQRES 5 A 195 ILE LYS ASP ILE LYS LYS ASP GLU PHE THR LYS VAL GLY
SEQRES 6 A 195 ALA ARG ASP THR TYR ILE ASP LEU ILE PHE GLU LYS ASP
SEQRES 7 A 195 GLY THR LYS TYR ARG ILE THR ARG ARG PHE LEU LYS GLY
SEQRES 8 A 195 TYR SER SER GLY GLU ILE HIS ALA MET LYS ARG LEU VAL
SEQRES 9 A 195 GLY ASN GLU TRP LYS HIS VAL THR GLU PRO SER SER LYS
SEQRES 10 A 195 ALA ILE SER ALA PHE MET GLU LYS LEU ILE PRO TYR ASN
SEQRES 11 A 195 ILE PHE LEU ASN ALA ILE TYR ILE ARG GLN GLY GLN ILE
SEQRES 12 A 195 ASP ALA ILE LEU GLU SER ASP GLU ALA ARG GLU LYS VAL
SEQRES 13 A 195 VAL ARG GLU VAL LEU ASN LEU ASP LYS PHE GLU THR ALA
SEQRES 14 A 195 TYR LYS LYS LEU SER GLU LEU LYS LYS THR ILE ASN ASN
SEQRES 15 A 195 ARG ILE LYS GLU TYR ARG ASP ILE LEU ALA ARG THR GLU
SEQRES 1 B 174 ARG GLU ARG VAL LYS LYS GLU ILE LYS ASP LEU GLU LYS
SEQRES 2 B 174 ALA LYS ASP PHE THR GLU GLU LEU ILE GLU LYS VAL LYS
SEQRES 3 B 174 LYS TYR LYS ALA LEU ALA ARG GLU ALA ALA LEU SER LYS
SEQRES 4 B 174 ILE GLY GLU LEU ALA SER GLU ILE PHE ALA GLU PHE THR
SEQRES 5 B 174 GLU GLY LYS TYR SER GLU VAL VAL VAL ARG ALA GLU GLU
SEQRES 6 B 174 ASN LYS VAL ARG LEU PHE VAL VAL TRP GLU GLY LYS GLU
SEQRES 7 B 174 ARG PRO LEU THR PHE LEU SER GLY GLY GLU ARG ILE ALA
SEQRES 8 B 174 LEU GLY LEU ALA PHE ARG LEU ALA MET SER LEU TYR LEU
SEQRES 9 B 174 ALA GLY GLU ILE SER LEU LEU ILE LEU ASP GLU PRO THR
SEQRES 10 B 174 PRO TYR LEU ASP GLU GLU ARG ARG ARG LYS LEU ILE THR
SEQRES 11 B 174 ILE MET GLU ARG TYR LEU LYS LYS ILE PRO GLN VAL ILE
SEQRES 12 B 174 LEU VAL SER HIS ASP GLU GLU LEU LYS ASP ALA ALA ASP
SEQRES 13 B 174 HIS VAL ILE ARG ILE SER LEU GLU ASN GLY SER SER LYS
SEQRES 14 B 174 VAL GLU VAL VAL SER
HET PO4 A1001 5
HET PO4 A1003 5
HETNAM PO4 PHOSPHATE ION
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 5 HOH *63(H2 O)
HELIX 1 1 GLY A 35 TRP A 49 1 15
HELIX 2 2 LYS A 58 LYS A 63 1 6
HELIX 3 3 SER A 115 ILE A 127 1 13
HELIX 4 4 PRO A 128 LEU A 133 1 6
HELIX 5 5 ILE A 143 LEU A 147 5 5
HELIX 6 6 ASP A 150 LEU A 161 1 12
HELIX 7 7 LEU A 163 GLU A 195 1 33
HELIX 8 8 ARG B 709 GLU B 761 1 53
HELIX 9 9 PRO B 788 LEU B 792 5 5
HELIX 10 10 SER B 793 GLY B 814 1 22
HELIX 11 11 GLU B 830 TYR B 843 1 14
HELIX 12 12 LEU B 844 ILE B 847 5 4
HELIX 13 13 ASP B 856 ALA B 862 5 7
SHEET 1 A 6 THR A 17 GLU A 20 0
SHEET 2 A 6 LYS A 2 LYS A 9 -1 O VAL A 6 N VAL A 19
SHEET 3 A 6 THR A 69 LYS A 77 -1 N TYR A 70 O LYS A 9
SHEET 4 A 6 THR A 80 LEU A 89 -1 O THR A 80 N LYS A 77
SHEET 5 A 6 GLY A 95 VAL A 104 -1 O GLY A 95 N LEU A 89
SHEET 6 A 6 GLU A 107 LYS A 109 -1 N GLU A 107 O VAL A 104
SHEET 1 B 6 TYR A 137 ILE A 138 0
SHEET 2 B 6 LEU B 818 ASP B 822 1 O ILE B 820 N ILE A 138
SHEET 3 B 6 GLN B 849 SER B 854 1 O GLN B 849 N LEU B 819
SHEET 4 B 6 GLY A 24 ILE A 29 1 O GLY A 24 N VAL B 850
SHEET 5 B 6 HIS B 865 LEU B 871 1 N HIS B 865 O ILE A 25
SHEET 6 B 6 SER B 876 VAL B 880 -1 N LYS B 877 O SER B 870
SHEET 1 C 2 GLU B 766 GLU B 772 0
SHEET 2 C 2 LYS B 775 VAL B 781 -1 O LYS B 775 N GLU B 772
CISPEP 1 TRP A 49 PRO A 50 0 0.99
SITE 1 AC1 9 GLN A 31 ASN A 32 GLY A 33 SER A 34
SITE 2 AC1 9 GLY A 35 LYS A 36 SER A 37 HOH A1004
SITE 3 AC1 9 HOH A1013
SITE 1 AC2 7 TRP A 49 PRO A 50 LEU A 51 ARG A 52
SITE 2 AC2 7 ILE A 53 ILE A 56 PHE A 61
CRYST1 99.531 99.531 116.407 90.00 90.00 120.00 P 31 2 1 6
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 0.010047 0.005801 0.000000 0.00000
SCALE2 0.000000 0.011601 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008591 0.00000
(ATOM LINES ARE NOT SHOWN.)
END