HEADER TRANSFERASE 16-JAN-14 4OGU
TITLE THE EFFECTS OF LYSINE 200 AND PHENYLALANINE 239 FARNESYL PYROPHOSPHATE
TITLE 2 SYNTHASE (FPPS) MUTATIONS ON THE CATALYTIC ACTIVITY, CRYSTAL
TITLE 3 STRUCTURE AND INHIBITION BY NITROGEN 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 (DE);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET 11 DERIVATIVE
KEYWDS ALL ALPHA-HELICAL, PRENYLTRANSFERASE, TRANSFERASE, ISOPRENE
KEYWDS 2 BIOSYNTHESIS, LIPID BIOSYNTHESIS, STEROID BIOSYNTHESIS, ISOPRENOID
KEYWDS 3 PATHWAY, CHOLESTEROL SYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR M.K.TSOUMPRA,B.L.BARNETT,J.R.C.MUNIZ,R.L.WALTER,F.H.EBETINO,F.VON
AUTHOR 2 DELFT,R.G.G.RUSSELL,U.OPPERMANN,J.E.DUNFORD
REVDAT 3 20-SEP-23 4OGU 1 REMARK SEQADV LINK
REVDAT 2 31-JAN-18 4OGU 1 AUTHOR JRNL
REVDAT 1 21-JAN-15 4OGU 0
JRNL AUTH M.K.TSOUMPRA,B.L.BARNETT,J.R.C.MUNIZ,R.L.WALTER,F.H.EBETINO,
JRNL AUTH 2 F.VON DELFT,R.G.G.RUSSELL,U.OPPERMANN,J.E.DUNFORD
JRNL TITL THE EFFECTS OF LYSINE 200 AND PHENYLALANINE 239 FARNESYL
JRNL TITL 2 PYROPHOSPHATE SYNTHASE (FPPS) MUTATIONS ON THE CATALYTIC
JRNL TITL 3 ACTIVITY, CRYSTAL STRUCTURE AND INHIBITION BY NITROGEN
JRNL TITL 4 CONTAINING BISPHOSPHONATES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 25116
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1284
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.83
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2776
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2351
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2638
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE : 0.2748
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.97
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 138
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 : 2636
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 109
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.24
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.57580
REMARK 3 B22 (A**2) : 1.57580
REMARK 3 B33 (A**2) : -3.15160
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) : 0.355
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) : 0.187
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 : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2769 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3776 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1293 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 67 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 402 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2769 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 2 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 359 ; 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 : 3474 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.96
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.63
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.81
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|8 - 28}
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4512 30.4439 8.4617
REMARK 3 T TENSOR
REMARK 3 T11: -0.3032 T22: -0.0909
REMARK 3 T33: 0.2375 T12: 0.1520
REMARK 3 T13: 0.1520 T23: -0.0905
REMARK 3 L TENSOR
REMARK 3 L11: 2.0068 L22: 3.8177
REMARK 3 L33: 1.0337 L12: 1.5104
REMARK 3 L13: 0.5334 L23: -0.6367
REMARK 3 S TENSOR
REMARK 3 S11: 0.0500 S12: -0.0877 S13: -0.0111
REMARK 3 S21: 0.0341 S22: -0.1280 S23: 0.1506
REMARK 3 S31: -0.1297 S32: -0.3425 S33: 0.0780
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|29 - 52}
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0080 25.7691 15.9039
REMARK 3 T TENSOR
REMARK 3 T11: -0.2227 T22: -0.1946
REMARK 3 T33: 0.3040 T12: 0.0911
REMARK 3 T13: 0.1011 T23: -0.0369
REMARK 3 L TENSOR
REMARK 3 L11: 2.3137 L22: 0.6002
REMARK 3 L33: 4.6370 L12: 1.6511
REMARK 3 L13: 0.0926 L23: -0.4542
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: -0.1958 S13: 0.0295
REMARK 3 S21: 0.2307 S22: -0.0545 S23: 0.1089
REMARK 3 S31: 0.0935 S32: -0.0967 S33: 0.0529
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|53 - 78}
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3050 26.0847 0.1502
REMARK 3 T TENSOR
REMARK 3 T11: -0.3040 T22: 0.0383
REMARK 3 T33: 0.3040 T12: 0.1004
REMARK 3 T13: 0.0606 T23: 0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 5.1811 L22: 0.6536
REMARK 3 L33: 2.6143 L12: -1.9218
REMARK 3 L13: 1.5270 L23: 0.9246
REMARK 3 S TENSOR
REMARK 3 S11: 0.0137 S12: 0.0135 S13: -0.0638
REMARK 3 S21: 0.2207 S22: -0.0272 S23: 0.1954
REMARK 3 S31: -0.0083 S32: -0.4806 S33: 0.0135
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|79 - 152}
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2351 25.3705 4.0537
REMARK 3 T TENSOR
REMARK 3 T11: -0.3040 T22: -0.2608
REMARK 3 T33: 0.3037 T12: 0.0729
REMARK 3 T13: 0.0474 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 3.0634 L22: 2.7846
REMARK 3 L33: 2.2380 L12: -0.0546
REMARK 3 L13: 0.7355 L23: 0.8315
REMARK 3 S TENSOR
REMARK 3 S11: -0.0177 S12: -0.3966 S13: -0.1226
REMARK 3 S21: 0.1234 S22: 0.0122 S23: 0.1183
REMARK 3 S31: -0.1424 S32: -0.3784 S33: 0.0055
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {A|153 - 206}
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0724 24.5100 -13.8620
REMARK 3 T TENSOR
REMARK 3 T11: -0.3040 T22: -0.1615
REMARK 3 T33: 0.3040 T12: 0.0627
REMARK 3 T13: -0.0448 T23: -0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 3.2173 L22: 1.9780
REMARK 3 L33: 2.6717 L12: 0.2622
REMARK 3 L13: -0.7745 L23: -1.5654
REMARK 3 S TENSOR
REMARK 3 S11: -0.0121 S12: 0.3190 S13: -0.1208
REMARK 3 S21: -0.3016 S22: 0.0157 S23: 0.2508
REMARK 3 S31: 0.1755 S32: -0.0598 S33: -0.0037
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {A|207 - 294}
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1143 34.8176 -16.2734
REMARK 3 T TENSOR
REMARK 3 T11: -0.3040 T22: -0.1391
REMARK 3 T33: 0.3040 T12: 0.0457
REMARK 3 T13: -0.0513 T23: -0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 4.1372 L22: 1.8982
REMARK 3 L33: 1.0633 L12: 0.4695
REMARK 3 L13: 0.1231 L23: 0.2833
REMARK 3 S TENSOR
REMARK 3 S11: -0.0467 S12: 0.5372 S13: 0.2931
REMARK 3 S21: -0.4066 S22: 0.0260 S23: 0.1989
REMARK 3 S31: -0.1716 S32: -0.0119 S33: 0.0207
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {A|295 - 350}
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9424 37.9296 -18.9170
REMARK 3 T TENSOR
REMARK 3 T11: -0.3040 T22: -0.1343
REMARK 3 T33: 0.3040 T12: 0.0918
REMARK 3 T13: -0.0893 T23: -0.0575
REMARK 3 L TENSOR
REMARK 3 L11: 4.0158 L22: 2.3223
REMARK 3 L33: 1.2688 L12: -0.6065
REMARK 3 L13: 0.0091 L23: 0.3327
REMARK 3 S TENSOR
REMARK 3 S11: 0.1816 S12: 0.2518 S13: 0.4017
REMARK 3 S21: -0.4163 S22: -0.3370 S23: 0.3262
REMARK 3 S31: -0.2527 S32: -0.1078 S33: 0.1554
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4OGU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000084475.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-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 : 25116
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 51.120
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.60
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : 0.11400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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 (%): 49.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NH4CL, PEG 6000, 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 33.63500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 55.60500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 55.60500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 16.81750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 55.60500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 55.60500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 50.45250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 55.60500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.60500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 16.81750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 55.60500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.60500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 50.45250
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 33.63500
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: 7040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 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 0.00000
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 607 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 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 TYR A 10 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 12 CG CD OE1 NE2
REMARK 470 GLU A 13 CG CD OE1 OE2
REMARK 470 ASP A 16 CG OD1 OD2
REMARK 470 GLN A 19 CG CD OE1 NE2
REMARK 470 ARG A 26 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 30 CD OE1 OE2
REMARK 470 HIS A 35 CG ND1 CD2 CE1 NE2
REMARK 470 THR A 53 OG1 CG2
REMARK 470 GLU A 73 CG CD OE1 OE2
REMARK 470 ARG A 75 CD NE CZ NH1 NH2
REMARK 470 LYS A 121 CE NZ
REMARK 470 GLN A 162 CG CD OE1 NE2
REMARK 470 GLN A 180 CG CD OE1 NE2
REMARK 470 VAL A 183 CG1 CG2
REMARK 470 ASP A 184 CG OD1 OD2
REMARK 470 ARG A 187 NE CZ NH1 NH2
REMARK 470 GLU A 222 CG CD OE1 OE2
REMARK 470 LYS A 223 CG CD CE NZ
REMARK 470 LYS A 230 CE NZ
REMARK 470 SER A 253 OG
REMARK 470 GLU A 281 CG CD OE1 OE2
REMARK 470 LYS A 293 CG CD CE NZ
REMARK 470 GLU A 296 CD OE1 OE2
REMARK 470 ARG A 300 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 307 CG CD OE1 OE2
REMARK 470 LYS A 350 CG CD 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 -71.31 -100.10
REMARK 500 ALA A 178 60.39 -112.58
REMARK 500 THR A 201 -51.14 -128.60
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 OD2
REMARK 620 2 ASP A 107 OD2 93.7
REMARK 620 3 210 A 405 O2 93.3 172.2
REMARK 620 4 210 A 405 O10 94.6 85.7 97.2
REMARK 620 5 HOH A 504 O 142.1 65.8 110.2 54.3
REMARK 620 6 HOH A 593 O 79.2 97.6 80.3 173.2 132.5
REMARK 620 7 HOH A 594 O 158.7 86.0 86.3 106.6 56.1 79.7
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 OD1
REMARK 620 2 ASP A 107 OD2 95.6
REMARK 620 3 210 A 405 O10 101.4 89.0
REMARK 620 4 HOH A 586 O 90.7 173.5 88.1
REMARK 620 5 HOH A 587 O 88.3 99.1 166.7 82.7
REMARK 620 6 HOH A 588 O 162.6 100.8 84.8 73.1 83.5
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 2 210 A 405 O9 101.8
REMARK 620 3 210 A 405 O5 94.5 89.2
REMARK 620 4 HOH A 590 O 90.6 94.6 172.9
REMARK 620 5 HOH A 591 O 81.3 172.7 84.0 91.9
REMARK 620 6 HOH A 592 O 168.6 87.9 79.6 94.5 88.4
REMARK 620 N 1 2 3 4 5
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 IPE A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 210 A 405
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4N9U RELATED DB: PDB
REMARK 900 RELATED ID: 4NG6 RELATED DB: PDB
REMARK 900 RELATED ID: 1ZW5 RELATED DB: PDB
REMARK 900 NATIVE STRUCTURE COMPLEXED WITH TWO LIGANDS.
REMARK 900 RELATED ID: 4NUA RELATED DB: PDB
DBREF 4OGU A 1 353 UNP P14324 FPPS_HUMAN 67 419
SEQADV 4OGU MET A -21 UNP P14324 EXPRESSION TAG
SEQADV 4OGU GLY A -20 UNP P14324 EXPRESSION TAG
SEQADV 4OGU SER A -19 UNP P14324 EXPRESSION TAG
SEQADV 4OGU SER A -18 UNP P14324 EXPRESSION TAG
SEQADV 4OGU HIS A -17 UNP P14324 EXPRESSION TAG
SEQADV 4OGU HIS A -16 UNP P14324 EXPRESSION TAG
SEQADV 4OGU HIS A -15 UNP P14324 EXPRESSION TAG
SEQADV 4OGU HIS A -14 UNP P14324 EXPRESSION TAG
SEQADV 4OGU HIS A -13 UNP P14324 EXPRESSION TAG
SEQADV 4OGU HIS A -12 UNP P14324 EXPRESSION TAG
SEQADV 4OGU SER A -11 UNP P14324 EXPRESSION TAG
SEQADV 4OGU SER A -10 UNP P14324 EXPRESSION TAG
SEQADV 4OGU GLY A -9 UNP P14324 EXPRESSION TAG
SEQADV 4OGU ARG A -8 UNP P14324 EXPRESSION TAG
SEQADV 4OGU GLU A -7 UNP P14324 EXPRESSION TAG
SEQADV 4OGU ASN A -6 UNP P14324 EXPRESSION TAG
SEQADV 4OGU LEU A -5 UNP P14324 EXPRESSION TAG
SEQADV 4OGU TYR A -4 UNP P14324 EXPRESSION TAG
SEQADV 4OGU PHE A -3 UNP P14324 EXPRESSION TAG
SEQADV 4OGU GLN A -2 UNP P14324 EXPRESSION TAG
SEQADV 4OGU GLY A -1 UNP P14324 EXPRESSION TAG
SEQADV 4OGU HIS A 0 UNP P14324 EXPRESSION TAG
SEQADV 4OGU THR A 53 UNP P14324 ALA 119 CONFLICT
SEQADV 4OGU ALA A 239 UNP P14324 PHE 305 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 LYS 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 ALA 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 IPE A 404 14
HET 210 A 405 13
HETNAM MG MAGNESIUM ION
HETNAM IPE 3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE
HETNAM 210 PAMIDRONATE
HETSYN IPE ISOPENTENYL PYROPHOSPHATE
HETSYN 210 (3-AMINO-1-HYDROXY-1-PHOSPHONO-PROPYL)PHOSPHONIC ACID
FORMUL 2 MG 3(MG 2+)
FORMUL 5 IPE C5 H12 O7 P2
FORMUL 6 210 C3 H11 N O7 P2
FORMUL 7 HOH *109(H2 O)
HELIX 1 1 GLN A 12 HIS A 20 1 9
HELIX 2 2 HIS A 20 THR A 29 1 10
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 ASP A 78 ASP A 107 1 30
HELIX 7 7 TRP A 118 LYS A 121 5 4
HELIX 8 8 VAL A 124 LEU A 126 5 3
HELIX 9 9 ASP A 127 ARG A 148 1 22
HELIX 10 10 TYR A 152 ALA A 178 1 27
HELIX 11 11 THR A 189 THR A 201 1 13
HELIX 12 12 THR A 201 ALA A 217 1 17
HELIX 13 13 GLY A 221 GLY A 250 1 30
HELIX 14 14 ASP A 251 GLY A 256 1 6
HELIX 15 15 SER A 268 ALA A 278 1 11
HELIX 16 16 THR A 279 TYR A 290 1 12
HELIX 17 17 GLU A 294 LEU A 308 1 15
HELIX 18 18 ASP A 309 ALA A 333 1 25
HELIX 19 19 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 OD2 ASP A 103 MG MG A 401 1555 1555 2.13
LINK OD1 ASP A 103 MG MG A 403 1555 1555 1.93
LINK OD2 ASP A 107 MG MG A 401 1555 1555 2.14
LINK OD2 ASP A 107 MG MG A 403 1555 1555 2.11
LINK OD2 ASP A 243 MG MG A 402 1555 1555 2.06
LINK MG MG A 401 O2 210 A 405 1555 1555 2.11
LINK MG MG A 401 O10 210 A 405 1555 1555 2.11
LINK MG MG A 401 O HOH A 504 1555 1555 2.94
LINK MG MG A 401 O HOH A 593 1555 1555 2.23
LINK MG MG A 401 O HOH A 594 1555 1555 1.90
LINK MG MG A 402 O9 210 A 405 1555 1555 2.00
LINK MG MG A 402 O5 210 A 405 1555 1555 2.10
LINK MG MG A 402 O HOH A 590 1555 1555 2.07
LINK MG MG A 402 O HOH A 591 1555 1555 2.28
LINK MG MG A 402 O HOH A 592 1555 1555 2.43
LINK MG MG A 403 O10 210 A 405 1555 1555 2.01
LINK MG MG A 403 O HOH A 586 1555 1555 2.08
LINK MG MG A 403 O HOH A 587 1555 1555 1.97
LINK MG MG A 403 O HOH A 588 1555 1555 2.18
CISPEP 1 ALA A 334 PRO A 335 0 3.49
SITE 1 AC1 7 ASP A 103 ASP A 107 MG A 403 210 A 405
SITE 2 AC1 7 HOH A 504 HOH A 593 HOH A 594
SITE 1 AC2 5 ASP A 243 210 A 405 HOH A 590 HOH A 591
SITE 2 AC2 5 HOH A 592
SITE 1 AC3 7 ASP A 103 ASP A 107 MG A 401 210 A 405
SITE 2 AC3 7 HOH A 586 HOH A 587 HOH A 588
SITE 1 AC4 15 GLY A 56 LYS A 57 ARG A 60 GLN A 96
SITE 2 AC4 15 ARG A 113 THR A 201 TYR A 204 GLN A 240
SITE 3 AC4 15 ASP A 243 210 A 405 HOH A 505 HOH A 507
SITE 4 AC4 15 HOH A 596 HOH A 597 HOH A 600
SITE 1 AC5 23 ASP A 103 ASP A 107 ARG A 112 LYS A 200
SITE 2 AC5 23 THR A 201 GLN A 240 ASP A 243 LYS A 257
SITE 3 AC5 23 MG A 401 MG A 402 MG A 403 IPE A 404
SITE 4 AC5 23 HOH A 504 HOH A 546 HOH A 586 HOH A 588
SITE 5 AC5 23 HOH A 589 HOH A 590 HOH A 591 HOH A 592
SITE 6 AC5 23 HOH A 593 HOH A 594 HOH A 601
CRYST1 111.210 111.210 67.270 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 0.008992 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008992 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014865 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
