HEADER CELL CYCLE 02-SEP-10 3OQ4
TITLE CRYSTAL STRUCTURE OF MOTIF N OF SACCHAROMYCES CEREVISIAE DBF4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DBF4;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 FRAGMENT: RESIDUES 120-250;
COMPND 5 SYNONYM: PROTEIN DNA52;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: D4205, DBF4, DNA52, YD9609.07C, YDR052C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STARPRAREPLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS DDK, BRCT, RAD53, REPLICATION CHECKPOINT, FHA DOMAIN, REGULATORY
KEYWDS 2 SUBUNIT OF DDK, CDC7, PHOSPHORYLATION, NUCLEAR, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.A.MATTHEWS,D.R.JONES,A.A.PRASAD,B.P.DUNCKER,A.GUARNE
REVDAT 1 07-SEP-11 3OQ4 0
JRNL AUTH L.A.MATTHEWS,D.R.JONES,A.A.PRASAD,B.P.DUNCKER,A.GUARNE
JRNL TITL CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIAE DBF4-MOTIF N
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.A.MATTHEWS,A.DUONG,A.A.PRASAD,B.P.DUNCKER,A.GUARNE
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION ANALYSIS
REMARK 1 TITL 2 OF MOTIF N FROM SACCHAROMYCES CEREVISIAE DBF4
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. F65 890 2009
REMARK 1 REFN ESSN 1744-3091
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : 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) : 46.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 42245
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2146
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 46.4170 - 5.1665 0.99 4192 263 0.2032 0.2157
REMARK 3 2 5.1665 - 4.1016 1.00 4091 205 0.1687 0.1931
REMARK 3 3 4.1016 - 3.5834 1.00 4031 203 0.1839 0.1914
REMARK 3 4 3.5834 - 3.2558 1.00 3997 213 0.2023 0.2298
REMARK 3 5 3.2558 - 3.0225 1.00 4006 205 0.2087 0.2525
REMARK 3 6 3.0225 - 2.8443 1.00 3958 216 0.2247 0.2320
REMARK 3 7 2.8443 - 2.7019 1.00 3947 232 0.2312 0.2740
REMARK 3 8 2.7019 - 2.5843 1.00 4015 191 0.2525 0.3165
REMARK 3 9 2.5843 - 2.4848 1.00 3908 220 0.2478 0.2778
REMARK 3 10 2.4848 - 2.3991 0.99 3954 198 0.2462 0.3272
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 40.38
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.850
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) : 17.89630
REMARK 3 B22 (A**2) : -1.54530
REMARK 3 B33 (A**2) : -16.35100
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 4429
REMARK 3 ANGLE : 0.946 5953
REMARK 3 CHIRALITY : 0.065 683
REMARK 3 PLANARITY : 0.003 739
REMARK 3 DIHEDRAL : 13.973 1714
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 3OQ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB061432.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0809
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42318
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.19200
REMARK 200 R SYM (I) : 0.20600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9200
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.73700
REMARK 200 R SYM FOR SHELL (I) : 0.50200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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: PDB ENTRY 3OQ0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% MPD (V/V) AND 100 MM NA/K
REMARK 280 PHOSPHATE BUFFER PH 7.1, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 41.85700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.85350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.85700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.85350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 117
REMARK 465 SER A 118
REMARK 465 LEU A 243
REMARK 465 TYR A 244
REMARK 465 GLY A 245
REMARK 465 PRO A 246
REMARK 465 THR A 247
REMARK 465 ASP A 248
REMARK 465 ARG A 249
REMARK 465 ASP A 250
REMARK 465 GLY B 117
REMARK 465 SER B 118
REMARK 465 HIS B 119
REMARK 465 MET B 120
REMARK 465 LYS B 121
REMARK 465 THR B 224
REMARK 465 LYS B 225
REMARK 465 SER B 226
REMARK 465 ALA B 227
REMARK 465 SER B 228
REMARK 465 LEU B 229
REMARK 465 ALA B 230
REMARK 465 ALA B 231
REMARK 465 PRO B 232
REMARK 465 THR B 233
REMARK 465 LEU B 234
REMARK 465 SER B 235
REMARK 465 ASN B 236
REMARK 465 LEU B 237
REMARK 465 LEU B 238
REMARK 465 HIS B 239
REMARK 465 ASN B 240
REMARK 465 GLU B 241
REMARK 465 LYS B 242
REMARK 465 LEU B 243
REMARK 465 TYR B 244
REMARK 465 GLY B 245
REMARK 465 PRO B 246
REMARK 465 THR B 247
REMARK 465 ASP B 248
REMARK 465 ARG B 249
REMARK 465 ASP B 250
REMARK 465 GLY C 117
REMARK 465 SER C 118
REMARK 465 HIS C 119
REMARK 465 MET C 120
REMARK 465 LYS C 121
REMARK 465 ARG C 122
REMARK 465 SER C 222
REMARK 465 LYS C 223
REMARK 465 THR C 224
REMARK 465 LYS C 225
REMARK 465 SER C 226
REMARK 465 ALA C 227
REMARK 465 SER C 228
REMARK 465 LEU C 229
REMARK 465 ALA C 230
REMARK 465 ALA C 231
REMARK 465 PRO C 232
REMARK 465 THR C 233
REMARK 465 LEU C 234
REMARK 465 SER C 235
REMARK 465 ASN C 236
REMARK 465 LEU C 237
REMARK 465 LEU C 238
REMARK 465 HIS C 239
REMARK 465 ASN C 240
REMARK 465 GLU C 241
REMARK 465 LYS C 242
REMARK 465 LEU C 243
REMARK 465 TYR C 244
REMARK 465 GLY C 245
REMARK 465 PRO C 246
REMARK 465 THR C 247
REMARK 465 ASP C 248
REMARK 465 ARG C 249
REMARK 465 ASP C 250
REMARK 465 GLY D 117
REMARK 465 SER D 118
REMARK 465 LEU D 218
REMARK 465 ASP D 219
REMARK 465 HIS D 220
REMARK 465 LEU D 221
REMARK 465 SER D 222
REMARK 465 LYS D 223
REMARK 465 THR D 224
REMARK 465 LYS D 225
REMARK 465 SER D 226
REMARK 465 ALA D 227
REMARK 465 SER D 228
REMARK 465 LEU D 229
REMARK 465 ALA D 230
REMARK 465 ALA D 231
REMARK 465 PRO D 232
REMARK 465 THR D 233
REMARK 465 LEU D 234
REMARK 465 SER D 235
REMARK 465 ASN D 236
REMARK 465 LEU D 237
REMARK 465 LEU D 238
REMARK 465 HIS D 239
REMARK 465 ASN D 240
REMARK 465 GLU D 241
REMARK 465 LYS D 242
REMARK 465 LEU D 243
REMARK 465 TYR D 244
REMARK 465 GLY D 245
REMARK 465 PRO D 246
REMARK 465 THR D 247
REMARK 465 ASP D 248
REMARK 465 ARG D 249
REMARK 465 ASP D 250
REMARK 465 GLY E 117
REMARK 465 SER E 118
REMARK 465 HIS E 119
REMARK 465 MET E 120
REMARK 465 ASP E 217
REMARK 465 LEU E 218
REMARK 465 ASP E 219
REMARK 465 HIS E 220
REMARK 465 LEU E 221
REMARK 465 SER E 222
REMARK 465 LYS E 223
REMARK 465 THR E 224
REMARK 465 LYS E 225
REMARK 465 SER E 226
REMARK 465 ALA E 227
REMARK 465 SER E 228
REMARK 465 LEU E 229
REMARK 465 ALA E 230
REMARK 465 ALA E 231
REMARK 465 PRO E 232
REMARK 465 THR E 233
REMARK 465 LEU E 234
REMARK 465 SER E 235
REMARK 465 ASN E 236
REMARK 465 LEU E 237
REMARK 465 LEU E 238
REMARK 465 HIS E 239
REMARK 465 ASN E 240
REMARK 465 GLU E 241
REMARK 465 LYS E 242
REMARK 465 LEU E 243
REMARK 465 TYR E 244
REMARK 465 GLY E 245
REMARK 465 PRO E 246
REMARK 465 THR E 247
REMARK 465 ASP E 248
REMARK 465 ARG E 249
REMARK 465 ASP E 250
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 HIS D 119 CG ND1 CD2 CE1 NE2
REMARK 470 ARG D 122 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 209 CG CD NE CZ NH1 NH2
REMARK 470 ALA E 207 O
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 ASN D 197 9.88 -69.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OQ0 RELATED DB: PDB
REMARK 900 (6XHIS)DBF4-N
DBREF 3OQ4 A 120 250 UNP P32325 DBF4_YEAST 120 250
DBREF 3OQ4 B 120 250 UNP P32325 DBF4_YEAST 120 250
DBREF 3OQ4 C 120 250 UNP P32325 DBF4_YEAST 120 250
DBREF 3OQ4 D 120 250 UNP P32325 DBF4_YEAST 120 250
DBREF 3OQ4 E 120 250 UNP P32325 DBF4_YEAST 120 250
SEQADV 3OQ4 GLY A 117 UNP P32325 EXPRESSION TAG
SEQADV 3OQ4 SER A 118 UNP P32325 EXPRESSION TAG
SEQADV 3OQ4 HIS A 119 UNP P32325 EXPRESSION TAG
SEQADV 3OQ4 GLY B 117 UNP P32325 EXPRESSION TAG
SEQADV 3OQ4 SER B 118 UNP P32325 EXPRESSION TAG
SEQADV 3OQ4 HIS B 119 UNP P32325 EXPRESSION TAG
SEQADV 3OQ4 GLY C 117 UNP P32325 EXPRESSION TAG
SEQADV 3OQ4 SER C 118 UNP P32325 EXPRESSION TAG
SEQADV 3OQ4 HIS C 119 UNP P32325 EXPRESSION TAG
SEQADV 3OQ4 GLY D 117 UNP P32325 EXPRESSION TAG
SEQADV 3OQ4 SER D 118 UNP P32325 EXPRESSION TAG
SEQADV 3OQ4 HIS D 119 UNP P32325 EXPRESSION TAG
SEQADV 3OQ4 GLY E 117 UNP P32325 EXPRESSION TAG
SEQADV 3OQ4 SER E 118 UNP P32325 EXPRESSION TAG
SEQADV 3OQ4 HIS E 119 UNP P32325 EXPRESSION TAG
SEQRES 1 A 134 GLY SER HIS MET LYS ARG ASP SER ARG ILE TYR PHE ASP
SEQRES 2 A 134 ILE THR ASP ASP VAL GLU MET ASN THR TYR ASN LYS SER
SEQRES 3 A 134 LYS MET ASP LYS ARG ARG ASP LEU LEU LYS ARG GLY PHE
SEQRES 4 A 134 LEU THR LEU GLY ALA GLN ILE THR GLN PHE PHE ASP THR
SEQRES 5 A 134 THR VAL THR ILE VAL ILE THR ARG ARG SER VAL GLU ASN
SEQRES 6 A 134 ILE TYR LEU LEU LYS ASP THR ASP ILE LEU SER ARG ALA
SEQRES 7 A 134 LYS LYS ASN TYR MET LYS VAL TRP SER TYR GLU LYS ALA
SEQRES 8 A 134 ALA ARG PHE LEU LYS ASN LEU ASP VAL ASP LEU ASP HIS
SEQRES 9 A 134 LEU SER LYS THR LYS SER ALA SER LEU ALA ALA PRO THR
SEQRES 10 A 134 LEU SER ASN LEU LEU HIS ASN GLU LYS LEU TYR GLY PRO
SEQRES 11 A 134 THR ASP ARG ASP
SEQRES 1 B 134 GLY SER HIS MET LYS ARG ASP SER ARG ILE TYR PHE ASP
SEQRES 2 B 134 ILE THR ASP ASP VAL GLU MET ASN THR TYR ASN LYS SER
SEQRES 3 B 134 LYS MET ASP LYS ARG ARG ASP LEU LEU LYS ARG GLY PHE
SEQRES 4 B 134 LEU THR LEU GLY ALA GLN ILE THR GLN PHE PHE ASP THR
SEQRES 5 B 134 THR VAL THR ILE VAL ILE THR ARG ARG SER VAL GLU ASN
SEQRES 6 B 134 ILE TYR LEU LEU LYS ASP THR ASP ILE LEU SER ARG ALA
SEQRES 7 B 134 LYS LYS ASN TYR MET LYS VAL TRP SER TYR GLU LYS ALA
SEQRES 8 B 134 ALA ARG PHE LEU LYS ASN LEU ASP VAL ASP LEU ASP HIS
SEQRES 9 B 134 LEU SER LYS THR LYS SER ALA SER LEU ALA ALA PRO THR
SEQRES 10 B 134 LEU SER ASN LEU LEU HIS ASN GLU LYS LEU TYR GLY PRO
SEQRES 11 B 134 THR ASP ARG ASP
SEQRES 1 C 134 GLY SER HIS MET LYS ARG ASP SER ARG ILE TYR PHE ASP
SEQRES 2 C 134 ILE THR ASP ASP VAL GLU MET ASN THR TYR ASN LYS SER
SEQRES 3 C 134 LYS MET ASP LYS ARG ARG ASP LEU LEU LYS ARG GLY PHE
SEQRES 4 C 134 LEU THR LEU GLY ALA GLN ILE THR GLN PHE PHE ASP THR
SEQRES 5 C 134 THR VAL THR ILE VAL ILE THR ARG ARG SER VAL GLU ASN
SEQRES 6 C 134 ILE TYR LEU LEU LYS ASP THR ASP ILE LEU SER ARG ALA
SEQRES 7 C 134 LYS LYS ASN TYR MET LYS VAL TRP SER TYR GLU LYS ALA
SEQRES 8 C 134 ALA ARG PHE LEU LYS ASN LEU ASP VAL ASP LEU ASP HIS
SEQRES 9 C 134 LEU SER LYS THR LYS SER ALA SER LEU ALA ALA PRO THR
SEQRES 10 C 134 LEU SER ASN LEU LEU HIS ASN GLU LYS LEU TYR GLY PRO
SEQRES 11 C 134 THR ASP ARG ASP
SEQRES 1 D 134 GLY SER HIS MET LYS ARG ASP SER ARG ILE TYR PHE ASP
SEQRES 2 D 134 ILE THR ASP ASP VAL GLU MET ASN THR TYR ASN LYS SER
SEQRES 3 D 134 LYS MET ASP LYS ARG ARG ASP LEU LEU LYS ARG GLY PHE
SEQRES 4 D 134 LEU THR LEU GLY ALA GLN ILE THR GLN PHE PHE ASP THR
SEQRES 5 D 134 THR VAL THR ILE VAL ILE THR ARG ARG SER VAL GLU ASN
SEQRES 6 D 134 ILE TYR LEU LEU LYS ASP THR ASP ILE LEU SER ARG ALA
SEQRES 7 D 134 LYS LYS ASN TYR MET LYS VAL TRP SER TYR GLU LYS ALA
SEQRES 8 D 134 ALA ARG PHE LEU LYS ASN LEU ASP VAL ASP LEU ASP HIS
SEQRES 9 D 134 LEU SER LYS THR LYS SER ALA SER LEU ALA ALA PRO THR
SEQRES 10 D 134 LEU SER ASN LEU LEU HIS ASN GLU LYS LEU TYR GLY PRO
SEQRES 11 D 134 THR ASP ARG ASP
SEQRES 1 E 134 GLY SER HIS MET LYS ARG ASP SER ARG ILE TYR PHE ASP
SEQRES 2 E 134 ILE THR ASP ASP VAL GLU MET ASN THR TYR ASN LYS SER
SEQRES 3 E 134 LYS MET ASP LYS ARG ARG ASP LEU LEU LYS ARG GLY PHE
SEQRES 4 E 134 LEU THR LEU GLY ALA GLN ILE THR GLN PHE PHE ASP THR
SEQRES 5 E 134 THR VAL THR ILE VAL ILE THR ARG ARG SER VAL GLU ASN
SEQRES 6 E 134 ILE TYR LEU LEU LYS ASP THR ASP ILE LEU SER ARG ALA
SEQRES 7 E 134 LYS LYS ASN TYR MET LYS VAL TRP SER TYR GLU LYS ALA
SEQRES 8 E 134 ALA ARG PHE LEU LYS ASN LEU ASP VAL ASP LEU ASP HIS
SEQRES 9 E 134 LEU SER LYS THR LYS SER ALA SER LEU ALA ALA PRO THR
SEQRES 10 E 134 LEU SER ASN LEU LEU HIS ASN GLU LYS LEU TYR GLY PRO
SEQRES 11 E 134 THR ASP ARG ASP
FORMUL 6 HOH *230(H2 O)
HELIX 1 1 ASN A 137 LEU A 158 1 22
HELIX 2 2 SER A 178 LEU A 185 5 8
HELIX 3 3 ASP A 189 ASN A 197 1 9
HELIX 4 4 TYR A 204 LEU A 214 1 11
HELIX 5 5 ASP A 217 SER A 222 1 6
HELIX 6 6 PRO A 232 LYS A 242 1 11
HELIX 7 7 ASN B 137 THR B 157 1 21
HELIX 8 8 SER B 178 LEU B 185 5 8
HELIX 9 9 ASP B 189 ASN B 197 1 9
HELIX 10 10 TYR B 204 LEU B 214 1 11
HELIX 11 11 ASP B 217 LYS B 223 1 7
HELIX 12 12 ASN C 137 GLY C 159 1 23
HELIX 13 13 SER C 178 LEU C 185 5 8
HELIX 14 14 ASP C 189 ASN C 197 1 9
HELIX 15 15 TYR C 204 LEU C 214 1 11
HELIX 16 16 ASN D 137 LEU D 158 1 22
HELIX 17 17 SER D 178 LEU D 185 5 8
HELIX 18 18 ASP D 189 ASN D 197 1 9
HELIX 19 19 TYR D 204 LEU D 214 1 11
HELIX 20 20 ASN E 137 LEU E 158 1 22
HELIX 21 21 ASN E 181 LEU E 185 5 5
HELIX 22 22 ASP E 189 ASN E 197 1 9
HELIX 23 23 GLU E 205 ASP E 215 1 11
SHEET 1 A 5 LYS A 200 SER A 203 0
SHEET 2 A 5 ILE A 172 THR A 175 1 N THR A 175 O TRP A 202
SHEET 3 A 5 ARG A 125 PHE A 128 1 N TYR A 127 O ILE A 172
SHEET 4 A 5 GLN A 161 THR A 163 1 O GLN A 161 N ILE A 126
SHEET 5 A 5 VAL B 134 GLU B 135 -1 O GLU B 135 N ILE A 162
SHEET 1 B 5 LYS B 200 SER B 203 0
SHEET 2 B 5 ILE B 172 THR B 175 1 N VAL B 173 O LYS B 200
SHEET 3 B 5 ARG B 125 PHE B 128 1 N TYR B 127 O ILE B 174
SHEET 4 B 5 GLN B 161 THR B 163 1 O GLN B 161 N ILE B 126
SHEET 5 B 5 VAL C 134 GLU C 135 -1 O GLU C 135 N ILE B 162
SHEET 1 C 5 LYS C 200 SER C 203 0
SHEET 2 C 5 ILE C 172 THR C 175 1 N VAL C 173 O LYS C 200
SHEET 3 C 5 ARG C 125 PHE C 128 1 N TYR C 127 O ILE C 172
SHEET 4 C 5 GLN C 161 THR C 163 1 O GLN C 161 N ILE C 126
SHEET 5 C 5 VAL D 134 GLU D 135 -1 O GLU D 135 N ILE C 162
SHEET 1 D 5 LYS D 200 SER D 203 0
SHEET 2 D 5 ILE D 172 THR D 175 1 N THR D 175 O TRP D 202
SHEET 3 D 5 ARG D 125 PHE D 128 1 N TYR D 127 O ILE D 174
SHEET 4 D 5 GLN D 161 THR D 163 1 O GLN D 161 N ILE D 126
SHEET 5 D 5 VAL E 134 GLU E 135 -1 O GLU E 135 N ILE D 162
SHEET 1 E 4 GLN E 161 ILE E 162 0
SHEET 2 E 4 ARG E 125 PHE E 128 1 N ILE E 126 O GLN E 161
SHEET 3 E 4 ILE E 172 THR E 175 1 O ILE E 174 N TYR E 127
SHEET 4 E 4 LYS E 200 SER E 203 1 O LYS E 200 N VAL E 173
CRYST1 83.714 99.707 127.045 90.00 90.00 90.00 P 21 21 2 20
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 0.011945 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010029 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007871 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
