HEADER TRANSFERASE 21-OCT-13 4N9U
TITLE THE ROLE OF LYSINE 200 IN THE HUMAN FARNESYL PYROPHOSPHATE SYNTHASE
TITLE 2 CATALYTIC MECHANISM AND THE MODE OF INHIBITION BY THE NITROGEN-
TITLE 3 CONTAINING BISPHOSPHONATES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FARNESYL PYROPHOSPHATE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 67-419;
COMPND 5 SYNONYM: FPP SYNTHASE, 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;
COMPND 10 MUTATION: 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: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET 11
KEYWDS ALPHA-HELICAL PRENYLTRANSFERASE FOLD, ISOPRENE BIOSYNTHESIS, LIPID
KEYWDS 2 SYNTHESIS, STEROID BIOSYNTHESIS, DIMETHYLALLYL PYROPHOSPHATE,
KEYWDS 3 ISOPENTENYL PYROPHOSPHATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.K.TSOUMPRA,J.R.C.MUNIZ,B.L.BARNETT,E.PILKA,A.A.KWAASI,K.L.KAVANAGH,
AUTHOR 2 A.EVDOKIMOV,R.L.WALTER,F.H.EBETINO,U.OPPERMANN,R.G.G.RUSSELL,
AUTHOR 3 J.E.DUNFORD
REVDAT 2 20-SEP-23 4N9U 1 REMARK SEQADV HETSYN LINK
REVDAT 1 22-OCT-14 4N9U 0
JRNL AUTH M.K.TSOUMPRA,J.R.C.MUNIZ,B.L.BARNETT,E.PILKA,A.A.KWAASI,
JRNL AUTH 2 K.L.KAVANAGH,A.EVDOKIMOV,R.L.WALTER,F.H.EBETINO,U.OPPERMANN,
JRNL AUTH 3 R.G.G.RUSSELL,J.E.DUNFORD
JRNL TITL THE ROLE OF LYSINE 200 IN THE HUMAN FARNESYL PYROPHOSPHATE
JRNL TITL 2 SYNTHASE CATALYTIC MECHANISM AND THE MODE OF INHIBITION BY
JRNL TITL 3 THE NITROGEN-CONTAINING BISPHOSPHONATES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.11 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.11
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 25568
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1303
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 13
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.11
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.20
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2835
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2305
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2702
REMARK 3 BIN R VALUE (WORKING SET) : 0.2287
REMARK 3 BIN FREE R VALUE : 0.2711
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.69
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 133
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 : 2662
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 121
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.51
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.53170
REMARK 3 B22 (A**2) : 4.53170
REMARK 3 B33 (A**2) : -9.06350
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.340
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.180
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2773 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3769 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1288 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 71 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 401 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2773 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 3 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 355 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3439 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.93
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.70
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.97
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|8 - 28}
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9053 0.8765 24.9107
REMARK 3 T TENSOR
REMARK 3 T11: 0.0493 T22: -0.3040
REMARK 3 T33: 0.2752 T12: -0.1520
REMARK 3 T13: -0.0870 T23: -0.1477
REMARK 3 L TENSOR
REMARK 3 L11: 3.5668 L22: 1.5194
REMARK 3 L33: 0.0500 L12: 1.0550
REMARK 3 L13: -0.5825 L23: -1.5654
REMARK 3 S TENSOR
REMARK 3 S11: -0.0295 S12: 0.0879 S13: 0.0602
REMARK 3 S21: 0.1745 S22: 0.0722 S23: -0.0456
REMARK 3 S31: -0.2061 S32: 0.1763 S33: -0.0427
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|29 - 52}
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0072 -15.8764 33.2467
REMARK 3 T TENSOR
REMARK 3 T11: -0.2154 T22: -0.2818
REMARK 3 T33: 0.3040 T12: -0.0648
REMARK 3 T13: -0.0661 T23: -0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 0.6157 L22: 0.1219
REMARK 3 L33: 5.1287 L12: -2.8740
REMARK 3 L13: -2.5536 L23: 1.3249
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: -0.2812 S13: 0.1460
REMARK 3 S21: 0.4056 S22: 0.0332 S23: -0.1333
REMARK 3 S31: -0.1563 S32: -0.1183 S33: -0.0342
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|53 - 78}
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9259 5.5779 17.3363
REMARK 3 T TENSOR
REMARK 3 T11: -0.0238 T22: -0.3040
REMARK 3 T33: 0.3040 T12: -0.0823
REMARK 3 T13: -0.0030 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 3.2567 L22: 8.1160
REMARK 3 L33: 3.7954 L12: 2.9104
REMARK 3 L13: 0.5707 L23: -0.5546
REMARK 3 S TENSOR
REMARK 3 S11: 0.0433 S12: -0.0927 S13: 0.1463
REMARK 3 S21: 0.2802 S22: -0.0702 S23: 0.0378
REMARK 3 S31: -0.5387 S32: -0.0088 S33: 0.0269
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|79 - 152}
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4723 -11.6884 21.3491
REMARK 3 T TENSOR
REMARK 3 T11: -0.2505 T22: -0.3040
REMARK 3 T33: 0.3040 T12: -0.0655
REMARK 3 T13: -0.0077 T23: -0.0320
REMARK 3 L TENSOR
REMARK 3 L11: 1.8243 L22: 4.5538
REMARK 3 L33: 1.8464 L12: -0.2554
REMARK 3 L13: 0.0108 L23: -0.3711
REMARK 3 S TENSOR
REMARK 3 S11: 0.1222 S12: -0.1033 S13: 0.1171
REMARK 3 S21: 0.3912 S22: -0.0428 S23: 0.0487
REMARK 3 S31: -0.3177 S32: 0.1093 S33: -0.0794
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {A|153 - 177}
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0775 -13.4569 8.9971
REMARK 3 T TENSOR
REMARK 3 T11: -0.3040 T22: -0.3040
REMARK 3 T33: 0.3040 T12: -0.0516
REMARK 3 T13: -0.0300 T23: 0.0328
REMARK 3 L TENSOR
REMARK 3 L11: 2.0453 L22: 2.6551
REMARK 3 L33: 1.6182 L12: -0.1798
REMARK 3 L13: -0.4572 L23: -0.2639
REMARK 3 S TENSOR
REMARK 3 S11: -0.0709 S12: 0.1881 S13: 0.3543
REMARK 3 S21: -0.0544 S22: 0.0774 S23: 0.2517
REMARK 3 S31: -0.1822 S32: -0.1262 S33: -0.0065
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {A|178 - 294}
REMARK 3 ORIGIN FOR THE GROUP (A): 33.5699 -13.8991 0.6439
REMARK 3 T TENSOR
REMARK 3 T11: -0.2432 T22: -0.3040
REMARK 3 T33: 0.3040 T12: -0.0382
REMARK 3 T13: -0.0083 T23: 0.0515
REMARK 3 L TENSOR
REMARK 3 L11: 1.7585 L22: 3.6344
REMARK 3 L33: 1.2170 L12: -0.4681
REMARK 3 L13: 0.0619 L23: 0.0474
REMARK 3 S TENSOR
REMARK 3 S11: 0.0461 S12: 0.3536 S13: 0.1039
REMARK 3 S21: -0.3756 S22: -0.0478 S23: -0.2251
REMARK 3 S31: 0.0161 S32: 0.0919 S33: 0.0017
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {A|295 - 332}
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4552 -8.0932 -4.4737
REMARK 3 T TENSOR
REMARK 3 T11: -0.2103 T22: -0.3040
REMARK 3 T33: 0.3040 T12: -0.0643
REMARK 3 T13: 0.0838 T23: 0.0789
REMARK 3 L TENSOR
REMARK 3 L11: 2.3698 L22: 5.0923
REMARK 3 L33: 1.1839 L12: -0.6142
REMARK 3 L13: 0.9599 L23: -0.7172
REMARK 3 S TENSOR
REMARK 3 S11: -0.2189 S12: 0.3922 S13: 0.0819
REMARK 3 S21: -0.5252 S22: 0.0765 S23: -0.4673
REMARK 3 S31: 0.0200 S32: 0.3201 S33: 0.1424
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {A|333 - 349}
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5765 6.5356 4.3729
REMARK 3 T TENSOR
REMARK 3 T11: -0.1434 T22: -0.3040
REMARK 3 T33: 0.3040 T12: 0.0008
REMARK 3 T13: -0.0574 T23: 0.1255
REMARK 3 L TENSOR
REMARK 3 L11: 1.2985 L22: 7.1886
REMARK 3 L33: 0.3889 L12: 2.7087
REMARK 3 L13: 1.2512 L23: 1.8359
REMARK 3 S TENSOR
REMARK 3 S11: 0.0393 S12: 0.0128 S13: 0.1276
REMARK 3 S21: 0.1556 S22: -0.0120 S23: 0.0654
REMARK 3 S31: -0.0985 S32: -0.0608 S33: -0.0272
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4N9U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000082933.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25619
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.110
REMARK 200 RESOLUTION RANGE LOW (A) : 52.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : 0.09100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 3CP6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NH4CL, PEG6000, 10% ETHYLENE
REMARK 280 GLYCOL, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 34.79000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 55.55500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 55.55500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.39500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 55.55500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 55.55500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 52.18500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 55.55500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.55500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 17.39500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 55.55500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.55500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 52.18500
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 34.79000
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: 7090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL
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 BIOMT1 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 34.79000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 600 LIES ON A SPECIAL POSITION.
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 A -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 ARG A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 GLY A 3
REMARK 465 ASP A 4
REMARK 465 GLN A 5
REMARK 465 ASN A 6
REMARK 465 SER A 7
REMARK 465 ASP A 31
REMARK 465 GLU A 32
REMARK 465 MET A 33
REMARK 465 GLY A 34
REMARK 465 LYS A 350
REMARK 465 ARG A 351
REMARK 465 ARG A 352
REMARK 465 LYS A 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 ASP A 8 CG OD1 OD2
REMARK 470 GLN A 12 CG CD OE1 NE2
REMARK 470 GLN A 15 CG CD OE1 NE2
REMARK 470 GLN A 19 CG CD OE1 NE2
REMARK 470 ARG A 26 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 35 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 54 CG1 CG2 CD1
REMARK 470 GLU A 73 OE1 OE2
REMARK 470 LYS A 121 CE NZ
REMARK 470 GLU A 149 OE1 OE2
REMARK 470 GLN A 180 CG CD OE1 NE2
REMARK 470 VAL A 183 CG1 CG2
REMARK 470 VAL A 186 CG1 CG2
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 GLU A 222 CG CD OE1 OE2
REMARK 470 LYS A 223 CG CD CE NZ
REMARK 470 GLU A 281 CG CD OE1 OE2
REMARK 470 ARG A 300 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 346 NE CZ NH1 NH2
REMARK 470 LYS A 347 CE NZ
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 VAL A 124 -74.68 -100.93
REMARK 500 ALA A 178 61.06 -113.68
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 MG A 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 103 OD1
REMARK 620 2 ASP A 107 OD2 87.2
REMARK 620 3 RIS A 404 O12 101.6 163.7
REMARK 620 4 RIS A 404 O15 87.3 79.5 87.2
REMARK 620 5 HOH A 553 O 84.3 99.0 95.6 171.5
REMARK 620 6 HOH A 554 O 157.0 91.6 85.6 115.1 73.1
REMARK 620 7 HOH A 581 O 145.8 79.7 85.5 59.4 128.7 55.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 103 OD2
REMARK 620 2 ASP A 107 OD2 90.5
REMARK 620 3 RIS A 404 O15 98.4 85.1
REMARK 620 4 HOH A 556 O 84.8 100.6 173.5
REMARK 620 5 HOH A 557 O 163.5 105.8 86.0 89.4
REMARK 620 6 HOH A 558 O 86.2 172.8 89.1 85.5 78.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 243 OD2
REMARK 620 2 RIS A 404 O11 98.8
REMARK 620 3 RIS A 404 O16 90.0 112.5
REMARK 620 4 HOH A 550 O 81.7 95.8 151.4
REMARK 620 5 HOH A 551 O 68.7 164.2 78.2 73.3
REMARK 620 6 HOH A 552 O 134.5 122.9 89.9 77.2 66.8
REMARK 620 7 HOH A 582 O 160.0 65.5 107.2 87.4 124.0 57.7
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 MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RIS A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KFA RELATED DB: PDB
REMARK 900 FARNESYL PYROPHOSPHATE SYNTHASE MUTANT
REMARK 900 RELATED ID: 4KPD RELATED DB: PDB
REMARK 900 FARNESYL PYROPHOSPHATE SYNTHASE MUTANT
REMARK 900 RELATED ID: 4KPJ RELATED DB: PDB
REMARK 900 FARNESYL PYROPHOSPHATE SYNTHASE MUTANT
REMARK 900 RELATED ID: 4KQ5 RELATED DB: PDB
REMARK 900 FARNESYL PYROPHOSPHATE SYNTHASE MUTANT
REMARK 900 RELATED ID: 4KQS RELATED DB: PDB
REMARK 900 FARNESYL PYROPHOSPHATE SYNTHASE MUTANT
REMARK 900 RELATED ID: 4KQU RELATED DB: PDB
REMARK 900 FARNESYL PYROPHOSPHATE SYNTHASE MUTANT
REMARK 900 RELATED ID: 1YQ7 RELATED DB: PDB
REMARK 900 FARNESYL PYROPHOSPHATE SYNTHASE NATIVE COMPLEX
REMARK 900 RELATED ID: 4NUA RELATED DB: PDB
REMARK 900 RELATED ID: 4NG6 RELATED DB: PDB
REMARK 900 RELATED ID: 4NKE RELATED DB: PDB
REMARK 900 RELATED ID: 4NKF RELATED DB: PDB
DBREF 4N9U A 1 353 UNP P14324 FPPS_HUMAN 67 419
SEQADV 4N9U MET A -21 UNP P14324 EXPRESSION TAG
SEQADV 4N9U GLY A -20 UNP P14324 EXPRESSION TAG
SEQADV 4N9U SER A -19 UNP P14324 EXPRESSION TAG
SEQADV 4N9U SER A -18 UNP P14324 EXPRESSION TAG
SEQADV 4N9U HIS A -17 UNP P14324 EXPRESSION TAG
SEQADV 4N9U HIS A -16 UNP P14324 EXPRESSION TAG
SEQADV 4N9U HIS A -15 UNP P14324 EXPRESSION TAG
SEQADV 4N9U HIS A -14 UNP P14324 EXPRESSION TAG
SEQADV 4N9U HIS A -13 UNP P14324 EXPRESSION TAG
SEQADV 4N9U HIS A -12 UNP P14324 EXPRESSION TAG
SEQADV 4N9U SER A -11 UNP P14324 EXPRESSION TAG
SEQADV 4N9U SER A -10 UNP P14324 EXPRESSION TAG
SEQADV 4N9U GLY A -9 UNP P14324 EXPRESSION TAG
SEQADV 4N9U ARG A -8 UNP P14324 EXPRESSION TAG
SEQADV 4N9U GLU A -7 UNP P14324 EXPRESSION TAG
SEQADV 4N9U ASN A -6 UNP P14324 EXPRESSION TAG
SEQADV 4N9U LEU A -5 UNP P14324 EXPRESSION TAG
SEQADV 4N9U TYR A -4 UNP P14324 EXPRESSION TAG
SEQADV 4N9U PHE A -3 UNP P14324 EXPRESSION TAG
SEQADV 4N9U GLN A -2 UNP P14324 EXPRESSION TAG
SEQADV 4N9U GLY A -1 UNP P14324 EXPRESSION TAG
SEQADV 4N9U HIS A 0 UNP P14324 EXPRESSION TAG
SEQADV 4N9U THR A 53 UNP P14324 ALA 119 CONFLICT
SEQADV 4N9U GLY A 200 UNP P14324 LYS 266 ENGINEERED MUTATION
SEQRES 1 A 375 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 375 ARG GLU ASN LEU TYR PHE GLN GLY HIS MET ASN GLY ASP
SEQRES 3 A 375 GLN ASN SER ASP VAL TYR ALA GLN GLU LYS GLN ASP PHE
SEQRES 4 A 375 VAL GLN HIS PHE SER GLN ILE VAL ARG VAL LEU THR GLU
SEQRES 5 A 375 ASP GLU MET GLY HIS PRO GLU ILE GLY ASP ALA ILE ALA
SEQRES 6 A 375 ARG LEU LYS GLU VAL LEU GLU TYR ASN THR ILE GLY GLY
SEQRES 7 A 375 LYS TYR ASN ARG GLY LEU THR VAL VAL VAL ALA PHE ARG
SEQRES 8 A 375 GLU LEU VAL GLU PRO ARG LYS GLN ASP ALA ASP SER LEU
SEQRES 9 A 375 GLN ARG ALA TRP THR VAL GLY TRP CYS VAL GLU LEU LEU
SEQRES 10 A 375 GLN ALA PHE PHE LEU VAL ALA ASP ASP ILE MET ASP SER
SEQRES 11 A 375 SER LEU THR ARG ARG GLY GLN ILE CYS TRP TYR GLN LYS
SEQRES 12 A 375 PRO GLY VAL GLY LEU ASP ALA ILE ASN ASP ALA ASN LEU
SEQRES 13 A 375 LEU GLU ALA CYS ILE TYR ARG LEU LEU LYS LEU TYR CYS
SEQRES 14 A 375 ARG GLU GLN PRO TYR TYR LEU ASN LEU ILE GLU LEU PHE
SEQRES 15 A 375 LEU GLN SER SER TYR GLN THR GLU ILE GLY GLN THR LEU
SEQRES 16 A 375 ASP LEU LEU THR ALA PRO GLN GLY ASN VAL ASP LEU VAL
SEQRES 17 A 375 ARG PHE THR GLU LYS ARG TYR LYS SER ILE VAL LYS TYR
SEQRES 18 A 375 GLY THR ALA PHE TYR SER PHE TYR LEU PRO ILE ALA ALA
SEQRES 19 A 375 ALA MET TYR MET ALA GLY ILE ASP GLY GLU LYS GLU HIS
SEQRES 20 A 375 ALA ASN ALA LYS LYS ILE LEU LEU GLU MET GLY GLU PHE
SEQRES 21 A 375 PHE GLN ILE GLN ASP ASP TYR LEU ASP LEU PHE GLY ASP
SEQRES 22 A 375 PRO SER VAL THR GLY LYS ILE GLY THR ASP ILE GLN ASP
SEQRES 23 A 375 ASN LYS CYS SER TRP LEU VAL VAL GLN CYS LEU GLN ARG
SEQRES 24 A 375 ALA THR PRO GLU GLN TYR GLN ILE LEU LYS GLU ASN TYR
SEQRES 25 A 375 GLY GLN LYS GLU ALA GLU LYS VAL ALA ARG VAL LYS ALA
SEQRES 26 A 375 LEU TYR GLU GLU LEU ASP LEU PRO ALA VAL PHE LEU GLN
SEQRES 27 A 375 TYR GLU GLU ASP SER TYR SER HIS ILE MET ALA LEU ILE
SEQRES 28 A 375 GLU GLN TYR ALA ALA PRO LEU PRO PRO ALA VAL PHE LEU
SEQRES 29 A 375 GLY LEU ALA ARG LYS ILE TYR LYS ARG ARG LYS
HET MG A 401 1
HET MG A 402 1
HET MG A 403 1
HET RIS A 404 17
HET EDO A 405 4
HET EDO A 406 4
HETNAM MG MAGNESIUM ION
HETNAM RIS 1-HYDROXY-2-(3-PYRIDINYL)ETHYLIDENE BIS-PHOSPHONIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN RIS RISEDRONATE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 MG 3(MG 2+)
FORMUL 5 RIS C7 H11 N O7 P2
FORMUL 6 EDO 2(C2 H6 O2)
FORMUL 8 HOH *121(H2 O)
HELIX 1 1 TYR A 10 HIS A 20 1 11
HELIX 2 2 HIS A 20 GLU A 30 1 11
HELIX 3 3 HIS A 35 GLU A 37 5 3
HELIX 4 4 ILE A 38 THR A 53 1 16
HELIX 5 5 TYR A 58 VAL A 72 1 15
HELIX 6 6 GLU A 73 GLN A 77 5 5
HELIX 7 7 ASP A 78 ASP A 107 1 30
HELIX 8 8 TRP A 118 LYS A 121 5 4
HELIX 9 9 VAL A 124 LEU A 126 5 3
HELIX 10 10 ASP A 127 ARG A 148 1 22
HELIX 11 11 TYR A 152 ALA A 178 1 27
HELIX 12 12 ASP A 184 PHE A 188 5 5
HELIX 13 13 THR A 189 THR A 201 1 13
HELIX 14 14 THR A 201 PHE A 206 1 6
HELIX 15 15 PHE A 206 ALA A 217 1 12
HELIX 16 16 GLY A 221 GLY A 250 1 30
HELIX 17 17 ASP A 251 GLY A 256 1 6
HELIX 18 18 SER A 268 ALA A 278 1 11
HELIX 19 19 THR A 279 TYR A 290 1 12
HELIX 20 20 GLU A 294 LEU A 308 1 15
HELIX 21 21 ASP A 309 ALA A 333 1 25
HELIX 22 22 PRO A 337 TYR A 349 1 13
SHEET 1 A 2 THR A 111 ARG A 112 0
SHEET 2 A 2 GLN A 115 ILE A 116 -1 O GLN A 115 N ARG A 112
LINK OD1 ASP A 103 MG MG A 401 1555 1555 2.00
LINK OD2 ASP A 103 MG MG A 403 1555 1555 1.93
LINK OD2 ASP A 107 MG MG A 401 1555 1555 2.22
LINK OD2 ASP A 107 MG MG A 403 1555 1555 2.17
LINK OD2 ASP A 243 MG MG A 402 1555 1555 2.17
LINK MG MG A 401 O12 RIS A 404 1555 1555 2.02
LINK MG MG A 401 O15 RIS A 404 1555 1555 2.30
LINK MG MG A 401 O HOH A 553 1555 1555 2.28
LINK MG MG A 401 O HOH A 554 1555 1555 1.88
LINK MG MG A 401 O HOH A 581 1555 1555 2.73
LINK MG MG A 402 O11 RIS A 404 1555 1555 1.87
LINK MG MG A 402 O16 RIS A 404 1555 1555 2.02
LINK MG MG A 402 O HOH A 550 1555 1555 2.02
LINK MG MG A 402 O HOH A 551 1555 1555 2.27
LINK MG MG A 402 O HOH A 552 1555 1555 2.07
LINK MG MG A 402 O HOH A 582 1555 1555 2.78
LINK MG MG A 403 O15 RIS A 404 1555 1555 2.10
LINK MG MG A 403 O HOH A 556 1555 1555 2.42
LINK MG MG A 403 O HOH A 557 1555 1555 2.23
LINK MG MG A 403 O HOH A 558 1555 1555 2.05
CISPEP 1 ALA A 334 PRO A 335 0 3.85
SITE 1 AC1 7 ASP A 103 ASP A 107 MG A 403 RIS A 404
SITE 2 AC1 7 HOH A 553 HOH A 554 HOH A 581
SITE 1 AC2 6 ASP A 243 RIS A 404 HOH A 550 HOH A 551
SITE 2 AC2 6 HOH A 552 HOH A 582
SITE 1 AC3 7 ASP A 103 ASP A 107 MG A 401 RIS A 404
SITE 2 AC3 7 HOH A 556 HOH A 557 HOH A 558
SITE 1 AC4 26 LEU A 100 ASP A 103 ASP A 107 ARG A 112
SITE 2 AC4 26 GLN A 171 GLY A 200 THR A 201 GLN A 240
SITE 3 AC4 26 ASP A 243 LYS A 257 MG A 401 MG A 402
SITE 4 AC4 26 MG A 403 HOH A 540 HOH A 549 HOH A 550
SITE 5 AC4 26 HOH A 551 HOH A 552 HOH A 554 HOH A 557
SITE 6 AC4 26 HOH A 558 HOH A 562 HOH A 563 HOH A 579
SITE 7 AC4 26 HOH A 581 HOH A 582
SITE 1 AC5 7 GLU A 136 ALA A 137 TYR A 140 LEU A 161
SITE 2 AC5 7 SER A 164 HOH A 523 HOH A 564
SITE 1 AC6 4 ARG A 141 GLN A 162 HOH A 523 HOH A 608
CRYST1 111.110 111.110 69.580 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 0.009000 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014372 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
