HEADER TRANSFERASE/TRANSFERASE INHIBITOR 10-MAY-16 5JUZ
TITLE CRYSTAL STRUCTURE OF HUMAN FPPS IN COMPLEX WITH AN ALLOSTERIC
TITLE 2 INHIBITOR CL-06-057
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FARNESYL PYROPHOSPHATE SYNTHASE;
COMPND 3 CHAIN: F;
COMPND 4 FRAGMENT: UNP RESIDUES 67-419;
COMPND 5 SYNONYM: FPS,(2E,6E)-FARNESYL DIPHOSPHATE SYNTHASE,
COMPND 6 DIMETHYLALLYLTRANSTRANSFERASE,FARNESYL DIPHOSPHATE SYNTHASE,
COMPND 7 GERANYLTRANSTRANSFERASE;
COMPND 8 EC: 2.5.1.10,2.5.1.1;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FDPS, FPS, KIAA1293;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.PARK,A.MAGDER,C.Y.LEUNG,Y.S.TSANTRIZOS,A.M.BERGHUIS
REVDAT 3 27-SEP-23 5JUZ 1 REMARK
REVDAT 2 22-MAR-17 5JUZ 1 JRNL
REVDAT 1 15-MAR-17 5JUZ 0
JRNL AUTH J.PARK,C.Y.LEUNG,A.N.MATRALIS,C.M.LACBAY,M.TSAKOS,
JRNL AUTH 2 G.FERNANDEZ DE TROCONIZ,A.M.BERGHUIS,Y.S.TSANTRIZOS
JRNL TITL PHARMACOPHORE MAPPING OF THIENOPYRIMIDINE-BASED
JRNL TITL 2 MONOPHOSPHONATE (THP-MP) INHIBITORS OF THE HUMAN FARNESYL
JRNL TITL 3 PYROPHOSPHATE SYNTHASE.
JRNL REF J. MED. CHEM. V. 60 2119 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28208018
JRNL DOI 10.1021/ACS.JMEDCHEM.6B01888
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0123
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 78.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 18322
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 + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 951
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1333
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE SET COUNT : 64
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2610
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 95
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 64.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.84000
REMARK 3 B22 (A**2) : -2.84000
REMARK 3 B33 (A**2) : 5.69000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.269
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.215
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.213
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.608
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2701 ; 0.023 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2500 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3679 ; 2.135 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5709 ; 1.168 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 333 ; 6.472 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 119 ;35.485 ;24.370
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 421 ;15.556 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;22.427 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 413 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3076 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 627 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1341 ; 1.875 ; 3.381
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1340 ; 1.870 ; 3.380
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1671 ; 2.986 ; 5.060
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1672 ; 2.985 ; 5.061
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1359 ; 2.515 ; 3.666
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1360 ; 2.515 ; 3.669
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2008 ; 3.923 ; 5.432
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3256 ; 6.675 ;28.820
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3257 ; 6.674 ;28.834
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 10 F 30
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0175 81.3373 9.9650
REMARK 3 T TENSOR
REMARK 3 T11: 0.2723 T22: 0.5273
REMARK 3 T33: 0.5076 T12: -0.2327
REMARK 3 T13: -0.2076 T23: -0.0427
REMARK 3 L TENSOR
REMARK 3 L11: 9.4200 L22: 5.7900
REMARK 3 L33: 7.3457 L12: 2.2272
REMARK 3 L13: -1.5983 L23: 1.3814
REMARK 3 S TENSOR
REMARK 3 S11: -0.1098 S12: 1.1292 S13: -0.3153
REMARK 3 S21: -0.5802 S22: 0.2617 S23: 0.7854
REMARK 3 S31: 0.7137 S32: -1.5476 S33: -0.1519
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 35 F 179
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8977 85.0928 17.5253
REMARK 3 T TENSOR
REMARK 3 T11: 0.0572 T22: 0.0558
REMARK 3 T33: 0.1911 T12: -0.0407
REMARK 3 T13: -0.0339 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 4.6359 L22: 2.6937
REMARK 3 L33: 2.6980 L12: -0.2592
REMARK 3 L13: -1.9290 L23: -0.0156
REMARK 3 S TENSOR
REMARK 3 S11: -0.0685 S12: 0.2243 S13: -0.2440
REMARK 3 S21: -0.3237 S22: 0.0849 S23: 0.3739
REMARK 3 S31: 0.2076 S32: -0.3733 S33: -0.0164
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 180 F 277
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8044 79.2446 36.3063
REMARK 3 T TENSOR
REMARK 3 T11: 0.1055 T22: 0.2464
REMARK 3 T33: 0.2907 T12: 0.0191
REMARK 3 T13: 0.0614 T23: 0.0526
REMARK 3 L TENSOR
REMARK 3 L11: 5.9363 L22: 5.1916
REMARK 3 L33: 4.4246 L12: -1.4691
REMARK 3 L13: 0.3437 L23: -3.0534
REMARK 3 S TENSOR
REMARK 3 S11: -0.0158 S12: -0.5294 S13: -0.4806
REMARK 3 S21: 0.2431 S22: -0.1773 S23: -0.0985
REMARK 3 S31: 0.2928 S32: 0.5249 S33: 0.1931
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 278 F 350
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1549 72.1584 41.9704
REMARK 3 T TENSOR
REMARK 3 T11: 0.2875 T22: 0.3172
REMARK 3 T33: 0.4847 T12: 0.0365
REMARK 3 T13: 0.0744 T23: 0.1250
REMARK 3 L TENSOR
REMARK 3 L11: 6.2212 L22: 5.4230
REMARK 3 L33: 3.3274 L12: -3.5175
REMARK 3 L13: 1.3028 L23: -2.3253
REMARK 3 S TENSOR
REMARK 3 S11: 0.0860 S12: -0.2627 S13: -0.4417
REMARK 3 S21: 0.2330 S22: -0.3168 S23: -0.3701
REMARK 3 S31: 0.5529 S32: 0.5933 S33: 0.2308
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5JUZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221263.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19304
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 78.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 9.300
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1000
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) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 9.40
REMARK 200 R MERGE FOR SHELL (I) : 0.93100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC 5.8.0123
REMARK 200 STARTING MODEL: 4QXS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.6 M SODIUM PHOSPHATE, 0.6 M
REMARK 280 POTASSIUM PHOSPHATE, 25% GLYCEROL, 0.075 M HEPES, PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 38.50000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 55.45000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 55.45000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 19.25000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 55.45000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 55.45000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 57.75000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 55.45000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.45000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 19.25000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 55.45000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.45000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 57.75000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 38.50000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 4280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 0.000000 -1.000000 0.000000 110.90000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 110.90000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 38.50000
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 MET F -21
REMARK 465 GLY F -20
REMARK 465 SER F -19
REMARK 465 SER F -18
REMARK 465 HIS F -17
REMARK 465 HIS F -16
REMARK 465 HIS F -15
REMARK 465 HIS F -14
REMARK 465 HIS F -13
REMARK 465 HIS F -12
REMARK 465 SER F -11
REMARK 465 SER F -10
REMARK 465 GLY F -9
REMARK 465 ARG F -8
REMARK 465 GLU F -7
REMARK 465 ASN F -6
REMARK 465 LEU F -5
REMARK 465 TYR F -4
REMARK 465 PHE F -3
REMARK 465 GLN F -2
REMARK 465 GLY F -1
REMARK 465 HIS F 0
REMARK 465 MET F 1
REMARK 465 ASN F 2
REMARK 465 GLY F 3
REMARK 465 ASP F 4
REMARK 465 GLN F 5
REMARK 465 ASN F 6
REMARK 465 SER F 7
REMARK 465 ASP F 8
REMARK 465 VAL F 9
REMARK 465 ASP F 31
REMARK 465 GLU F 32
REMARK 465 MET F 33
REMARK 465 GLY F 34
REMARK 465 GLY F 181
REMARK 465 ARG F 351
REMARK 465 ARG F 352
REMARK 465 LYS F 353
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 F 12 CG CD OE1 NE2
REMARK 470 GLU F 13 CG CD OE1 OE2
REMARK 470 LYS F 14 CE NZ
REMARK 470 GLN F 15 CG CD OE1 NE2
REMARK 470 ASP F 16 CG OD1 OD2
REMARK 470 GLN F 19 CD OE1 NE2
REMARK 470 HIS F 35 CG ND1 CD2 CE1 NE2
REMARK 470 GLU F 37 CG CD OE1 OE2
REMARK 470 LYS F 57 CE NZ
REMARK 470 GLU F 73 CG CD OE1 OE2
REMARK 470 ARG F 75 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 76 CE NZ
REMARK 470 ASN F 182 CG OD1 ND2
REMARK 470 VAL F 183 CG1 CG2
REMARK 470 VAL F 186 CG1 CG2
REMARK 470 ARG F 187 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 191 CD CE NZ
REMARK 470 LYS F 257 CG CD CE NZ
REMARK 470 ILE F 258 CG1 CG2 CD1
REMARK 470 LYS F 266 NZ
REMARK 470 GLU F 281 CG CD OE1 OE2
REMARK 470 GLN F 284 CG CD OE1 NE2
REMARK 470 LYS F 287 CG CD CE NZ
REMARK 470 GLU F 288 CG CD OE1 OE2
REMARK 470 GLN F 292 CD OE1 NE2
REMARK 470 LYS F 293 CG CD CE NZ
REMARK 470 GLU F 294 CG CD OE1 OE2
REMARK 470 GLU F 296 CG CD OE1 OE2
REMARK 470 LYS F 297 CG CD CE NZ
REMARK 470 ARG F 300 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 307 CG CD OE1 OE2
REMARK 470 LYS F 350 CG CD CE NZ
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 GLU F 47 CD GLU F 47 OE2 0.072
REMARK 500 ASP F 107 CB ASP F 107 CG -0.134
REMARK 500 PHE F 203 CG PHE F 203 CD2 0.105
REMARK 500 SER F 323 CB SER F 323 OG -0.083
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 ARG F 69 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG F 84 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG F 84 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ASP F 107 CB - CA - C ANGL. DEV. = -13.3 DEGREES
REMARK 500 ASP F 107 CB - CG - OD1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG F 141 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG F 141 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN F 77 64.50 -103.03
REMARK 500 VAL F 124 -71.09 -104.49
REMARK 500 ALA F 178 77.30 -119.88
REMARK 500 ASN F 289 -24.21 -142.70
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 CL F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue YL4 F 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JV2 RELATED DB: PDB
REMARK 900 RELATED ID: 5JV1 RELATED DB: PDB
REMARK 900 RELATED ID: 5JV0 RELATED DB: PDB
DBREF 5JUZ F 1 353 UNP P14324 FPPS_HUMAN 67 419
SEQADV 5JUZ MET F -21 UNP P14324 INITIATING METHIONINE
SEQADV 5JUZ GLY F -20 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ SER F -19 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ SER F -18 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ HIS F -17 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ HIS F -16 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ HIS F -15 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ HIS F -14 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ HIS F -13 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ HIS F -12 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ SER F -11 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ SER F -10 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ GLY F -9 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ ARG F -8 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ GLU F -7 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ ASN F -6 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ LEU F -5 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ TYR F -4 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ PHE F -3 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ GLN F -2 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ GLY F -1 UNP P14324 EXPRESSION TAG
SEQADV 5JUZ HIS F 0 UNP P14324 EXPRESSION TAG
SEQRES 1 F 375 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 375 ARG GLU ASN LEU TYR PHE GLN GLY HIS MET ASN GLY ASP
SEQRES 3 F 375 GLN ASN SER ASP VAL TYR ALA GLN GLU LYS GLN ASP PHE
SEQRES 4 F 375 VAL GLN HIS PHE SER GLN ILE VAL ARG VAL LEU THR GLU
SEQRES 5 F 375 ASP GLU MET GLY HIS PRO GLU ILE GLY ASP ALA ILE ALA
SEQRES 6 F 375 ARG LEU LYS GLU VAL LEU GLU TYR ASN ALA ILE GLY GLY
SEQRES 7 F 375 LYS TYR ASN ARG GLY LEU THR VAL VAL VAL ALA PHE ARG
SEQRES 8 F 375 GLU LEU VAL GLU PRO ARG LYS GLN ASP ALA ASP SER LEU
SEQRES 9 F 375 GLN ARG ALA TRP THR VAL GLY TRP CYS VAL GLU LEU LEU
SEQRES 10 F 375 GLN ALA PHE PHE LEU VAL ALA ASP ASP ILE MET ASP SER
SEQRES 11 F 375 SER LEU THR ARG ARG GLY GLN ILE CYS TRP TYR GLN LYS
SEQRES 12 F 375 PRO GLY VAL GLY LEU ASP ALA ILE ASN ASP ALA ASN LEU
SEQRES 13 F 375 LEU GLU ALA CYS ILE TYR ARG LEU LEU LYS LEU TYR CYS
SEQRES 14 F 375 ARG GLU GLN PRO TYR TYR LEU ASN LEU ILE GLU LEU PHE
SEQRES 15 F 375 LEU GLN SER SER TYR GLN THR GLU ILE GLY GLN THR LEU
SEQRES 16 F 375 ASP LEU LEU THR ALA PRO GLN GLY ASN VAL ASP LEU VAL
SEQRES 17 F 375 ARG PHE THR GLU LYS ARG TYR LYS SER ILE VAL LYS TYR
SEQRES 18 F 375 LYS THR ALA PHE TYR SER PHE TYR LEU PRO ILE ALA ALA
SEQRES 19 F 375 ALA MET TYR MET ALA GLY ILE ASP GLY GLU LYS GLU HIS
SEQRES 20 F 375 ALA ASN ALA LYS LYS ILE LEU LEU GLU MET GLY GLU PHE
SEQRES 21 F 375 PHE GLN ILE GLN ASP ASP TYR LEU ASP LEU PHE GLY ASP
SEQRES 22 F 375 PRO SER VAL THR GLY LYS ILE GLY THR ASP ILE GLN ASP
SEQRES 23 F 375 ASN LYS CYS SER TRP LEU VAL VAL GLN CYS LEU GLN ARG
SEQRES 24 F 375 ALA THR PRO GLU GLN TYR GLN ILE LEU LYS GLU ASN TYR
SEQRES 25 F 375 GLY GLN LYS GLU ALA GLU LYS VAL ALA ARG VAL LYS ALA
SEQRES 26 F 375 LEU TYR GLU GLU LEU ASP LEU PRO ALA VAL PHE LEU GLN
SEQRES 27 F 375 TYR GLU GLU ASP SER TYR SER HIS ILE MET ALA LEU ILE
SEQRES 28 F 375 GLU GLN TYR ALA ALA PRO LEU PRO PRO ALA VAL PHE LEU
SEQRES 29 F 375 GLY LEU ALA ARG LYS ILE TYR LYS ARG ARG LYS
HET CL F 401 1
HET CL F 402 1
HET YL4 F 403 31
HETNAM CL CHLORIDE ION
HETNAM YL4 [(R)-(2,3-DIHYDRO-1-BENZOFURAN-5-YL){[6-(4-
HETNAM 2 YL4 METHYLPHENYL)THIENO[2,3-D]PYRIMIDIN-4-
HETNAM 3 YL4 YL]AMINO}METHYL]PHOSPHONIC ACID
FORMUL 2 CL 2(CL 1-)
FORMUL 4 YL4 C22 H20 N3 O4 P S
FORMUL 5 HOH *95(H2 O)
HELIX 1 AA1 GLU F 13 THR F 29 1 17
HELIX 2 AA2 GLU F 30 GLU F 30 5 1
HELIX 3 AA3 HIS F 35 GLU F 37 5 3
HELIX 4 AA4 ILE F 38 ILE F 54 1 17
HELIX 5 AA5 TYR F 58 VAL F 72 1 15
HELIX 6 AA6 GLU F 73 GLN F 77 5 5
HELIX 7 AA7 ASP F 78 ASP F 107 1 30
HELIX 8 AA8 TRP F 118 LYS F 121 5 4
HELIX 9 AA9 VAL F 124 LEU F 126 5 3
HELIX 10 AB1 ASP F 127 ARG F 148 1 22
HELIX 11 AB2 TYR F 152 ALA F 178 1 27
HELIX 12 AB3 THR F 189 THR F 201 1 13
HELIX 13 AB4 THR F 201 ALA F 217 1 17
HELIX 14 AB5 GLY F 221 GLY F 250 1 30
HELIX 15 AB6 ASP F 251 GLY F 256 1 6
HELIX 16 AB7 SER F 268 ARG F 277 1 10
HELIX 17 AB8 THR F 279 LYS F 287 1 9
HELIX 18 AB9 GLU F 294 LEU F 308 1 15
HELIX 19 AC1 ASP F 309 ALA F 333 1 25
HELIX 20 AC2 PRO F 337 LYS F 350 1 14
SHEET 1 AA1 2 THR F 111 ARG F 112 0
SHEET 2 AA1 2 GLN F 115 ILE F 116 -1 O GLN F 115 N ARG F 112
CISPEP 1 ALA F 334 PRO F 335 0 5.54
SITE 1 AC1 2 ASP F 80 ARG F 84
SITE 1 AC2 2 LYS F 57 ASN F 59
SITE 1 AC3 9 LYS F 57 ASN F 59 ARG F 113 SER F 205
SITE 2 AC3 9 PHE F 206 PHE F 239 ASP F 243 LEU F 344
SITE 3 AC3 9 HOH F 559
CRYST1 110.900 110.900 77.000 90.00 90.00 90.00 P 41 21 2 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 0.009017 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009017 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012987 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
