HEADER TRANSFERASE 07-JUL-13 3WEF
TITLE CRYSTAL STRUCTURE OF THE HUMAN SQUALENE SYNTHASE IN COMPLEX WITH
TITLE 2 FARNESYL THIOPYROPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SQUALENE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: UNP RESIDUES 31-370;
COMPND 5 SYNONYM: SQS, SS, FPP:FPP FARNESYLTRANSFERASE, FARNESYL-DIPHOSPHATE
COMPND 6 FARNESYLTRANSFERASE;
COMPND 7 EC: 2.5.1.21;
COMPND 8 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: FDFT1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS FARNESYL-DIPHOSPHATE FARNESYLTRANSFERASE, HEAD-TO-HEAD SYNTHASES,
KEYWDS 2 CHOLESTEROL BIOSYNTHESIS, OXIDOREDUCTASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.I.LIU,W.Y.JENG,A.H.J.WANG
REVDAT 3 08-NOV-23 3WEF 1 REMARK
REVDAT 2 25-DEC-19 3WEF 1 JRNL SEQADV
REVDAT 1 12-FEB-14 3WEF 0
JRNL AUTH C.I.LIU,W.Y.JENG,W.J.CHANG,M.F.SHIH,T.P.KO,A.H.J.WANG
JRNL TITL STRUCTURAL INSIGHTS INTO THE CATALYTIC MECHANISM OF HUMAN
JRNL TITL 2 SQUALENE SYNTHASE.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 231 2014
JRNL REFN ESSN 1399-0047
JRNL PMID 24531458
JRNL DOI 10.1107/S1399004713026230
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 97681
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) : 0.190
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4876
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.47
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13094
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.42
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 714
REMARK 3 BIN FREE R VALUE : 0.3290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15961
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 192
REMARK 3 SOLVENT ATOMS : 352
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.40000
REMARK 3 B22 (A**2) : 0.49000
REMARK 3 B33 (A**2) : -0.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.15000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.260
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.200
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.685
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16471 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 22271 ; 1.417 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1963 ; 5.213 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 803 ;38.265 ;24.147
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2921 ;18.717 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 112 ;16.836 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2462 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12412 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 9847 ; 1.549 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15956 ; 2.902 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6624 ; 3.457 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6315 ; 5.780 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 16471 ; 1.804 ; 3.000
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 : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 36 A 369
REMARK 3 RESIDUE RANGE : A 401 A 402
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7128 59.2592 49.4836
REMARK 3 T TENSOR
REMARK 3 T11: 0.1028 T22: 0.0865
REMARK 3 T33: 0.1540 T12: -0.0098
REMARK 3 T13: 0.0239 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: -0.0394 L22: 0.2432
REMARK 3 L33: -0.0689 L12: 0.0568
REMARK 3 L13: 0.0909 L23: 0.0845
REMARK 3 S TENSOR
REMARK 3 S11: -0.0220 S12: -0.0295 S13: -0.0370
REMARK 3 S21: 0.0556 S22: 0.0112 S23: 0.0063
REMARK 3 S31: 0.0523 S32: 0.0067 S33: 0.0109
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 37 B 369
REMARK 3 RESIDUE RANGE : B 401 B 402
REMARK 3 ORIGIN FOR THE GROUP (A): 51.4188 44.1191 45.2793
REMARK 3 T TENSOR
REMARK 3 T11: 0.1246 T22: 0.1124
REMARK 3 T33: 0.1679 T12: -0.0009
REMARK 3 T13: 0.0281 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.0111 L22: 0.0226
REMARK 3 L33: 0.0158 L12: -0.0081
REMARK 3 L13: 0.0136 L23: 0.0049
REMARK 3 S TENSOR
REMARK 3 S11: -0.0004 S12: -0.0008 S13: 0.0039
REMARK 3 S21: 0.0061 S22: 0.0020 S23: 0.0034
REMARK 3 S31: 0.0031 S32: 0.0021 S33: -0.0016
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 36 C 368
REMARK 3 RESIDUE RANGE : C 401 C 401
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4232 16.9458 43.2646
REMARK 3 T TENSOR
REMARK 3 T11: 0.0830 T22: 0.0732
REMARK 3 T33: 0.1397 T12: 0.0193
REMARK 3 T13: 0.0154 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: -0.1575 L22: 0.1302
REMARK 3 L33: -0.0634 L12: 0.0926
REMARK 3 L13: -0.0202 L23: 0.0274
REMARK 3 S TENSOR
REMARK 3 S11: -0.0129 S12: 0.0040 S13: 0.0618
REMARK 3 S21: 0.0043 S22: 0.0273 S23: -0.0780
REMARK 3 S31: -0.0555 S32: 0.0423 S33: -0.0144
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 37 D 369
REMARK 3 RESIDUE RANGE : D 401 D 401
REMARK 3 ORIGIN FOR THE GROUP (A): 27.5917 68.0304 -2.2264
REMARK 3 T TENSOR
REMARK 3 T11: 0.1789 T22: 0.1393
REMARK 3 T33: 0.2136 T12: -0.0277
REMARK 3 T13: 0.0421 T23: -0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.2311 L22: -0.0089
REMARK 3 L33: 0.6634 L12: 0.0703
REMARK 3 L13: -0.3370 L23: -0.1577
REMARK 3 S TENSOR
REMARK 3 S11: 0.0706 S12: -0.0706 S13: 0.0565
REMARK 3 S21: 0.0848 S22: -0.0170 S23: -0.0150
REMARK 3 S31: -0.1575 S32: 0.0477 S33: -0.0536
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 37 E 369
REMARK 3 RESIDUE RANGE : E 401 E 402
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3699 48.4650 10.0786
REMARK 3 T TENSOR
REMARK 3 T11: 0.1235 T22: 0.1124
REMARK 3 T33: 0.1750 T12: 0.0012
REMARK 3 T13: 0.0286 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.0698 L22: 0.1251
REMARK 3 L33: 0.0292 L12: 0.0108
REMARK 3 L13: -0.0159 L23: -0.0593
REMARK 3 S TENSOR
REMARK 3 S11: 0.0021 S12: 0.0072 S13: 0.0090
REMARK 3 S21: -0.0066 S22: 0.0026 S23: 0.0099
REMARK 3 S31: 0.0037 S32: -0.0043 S33: -0.0047
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 38 F 369
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5988 24.3638 -1.9186
REMARK 3 T TENSOR
REMARK 3 T11: 0.1696 T22: 0.1476
REMARK 3 T33: 0.2178 T12: 0.0133
REMARK 3 T13: 0.0492 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 0.2734 L22: 0.1064
REMARK 3 L33: 0.1336 L12: 0.2166
REMARK 3 L13: -0.0322 L23: -0.0616
REMARK 3 S TENSOR
REMARK 3 S11: -0.0115 S12: 0.0239 S13: -0.0877
REMARK 3 S21: -0.0556 S22: -0.0221 S23: -0.1264
REMARK 3 S31: 0.0481 S32: 0.0360 S33: 0.0335
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3WEF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000096231.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : VARIMAXHF
REMARK 200 OPTICS : VARIMAXHF
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 97910
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.65500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3VJB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% PEG 400, 2M K2HPO4/NAH2PO4, 3MM
REMARK 280 FARNESYL THIOPYROPHOSPHATE, PH 6.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 76.87600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, 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 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 28
REMARK 465 SER A 29
REMARK 465 HIS A 30
REMARK 465 MET A 31
REMARK 465 ASP A 32
REMARK 465 GLN A 33
REMARK 465 ASP A 34
REMARK 465 SER A 35
REMARK 465 LYS A 318
REMARK 465 GLY A 319
REMARK 465 GLN A 320
REMARK 465 ALA A 321
REMARK 465 VAL A 322
REMARK 465 THR A 323
REMARK 465 LEU A 324
REMARK 465 ASN A 370
REMARK 465 GLY B 28
REMARK 465 SER B 29
REMARK 465 HIS B 30
REMARK 465 MET B 31
REMARK 465 ASP B 32
REMARK 465 GLN B 33
REMARK 465 ASP B 34
REMARK 465 SER B 35
REMARK 465 LEU B 36
REMARK 465 ASN B 370
REMARK 465 GLY C 28
REMARK 465 SER C 29
REMARK 465 HIS C 30
REMARK 465 MET C 31
REMARK 465 ASP C 32
REMARK 465 GLN C 33
REMARK 465 ASP C 34
REMARK 465 SER C 35
REMARK 465 GLN C 369
REMARK 465 ASN C 370
REMARK 465 GLY D 28
REMARK 465 SER D 29
REMARK 465 HIS D 30
REMARK 465 MET D 31
REMARK 465 ASP D 32
REMARK 465 GLN D 33
REMARK 465 ASP D 34
REMARK 465 SER D 35
REMARK 465 LEU D 36
REMARK 465 LYS D 318
REMARK 465 GLY D 319
REMARK 465 GLN D 320
REMARK 465 ALA D 321
REMARK 465 ASN D 370
REMARK 465 GLY E 28
REMARK 465 SER E 29
REMARK 465 HIS E 30
REMARK 465 MET E 31
REMARK 465 ASP E 32
REMARK 465 GLN E 33
REMARK 465 ASP E 34
REMARK 465 SER E 35
REMARK 465 LEU E 36
REMARK 465 ARG E 317
REMARK 465 LYS E 318
REMARK 465 GLY E 319
REMARK 465 GLN E 320
REMARK 465 ASN E 370
REMARK 465 GLY F 28
REMARK 465 SER F 29
REMARK 465 HIS F 30
REMARK 465 MET F 31
REMARK 465 ASP F 32
REMARK 465 GLN F 33
REMARK 465 ASP F 34
REMARK 465 SER F 35
REMARK 465 LEU F 36
REMARK 465 SER F 37
REMARK 465 LYS F 315
REMARK 465 ILE F 316
REMARK 465 ARG F 317
REMARK 465 LYS F 318
REMARK 465 GLY F 319
REMARK 465 GLN F 320
REMARK 465 ALA F 321
REMARK 465 VAL F 322
REMARK 465 THR F 323
REMARK 465 LEU F 324
REMARK 465 ASN F 370
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O PHE D 132 NE2 GLN D 140 2.13
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 LEU E 97 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 MET E 207 CG - SD - CE ANGL. DEV. = -9.9 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 THR A 163 -76.91 -95.49
REMARK 500 ALA A 176 -46.70 -141.39
REMARK 500 GLU A 191 -5.75 84.67
REMARK 500 ASP A 219 30.58 -96.04
REMARK 500 SER A 237 1.33 -69.24
REMARK 500 ASN A 305 17.32 49.83
REMARK 500 ALA A 328 45.78 -89.25
REMARK 500 THR B 163 -77.12 -100.71
REMARK 500 ALA B 176 -46.93 -141.34
REMARK 500 ARG B 317 172.20 -58.22
REMARK 500 SER C 53 -71.09 -62.53
REMARK 500 THR C 163 -86.68 -86.72
REMARK 500 ALA C 176 -45.92 -137.63
REMARK 500 ASN C 305 17.35 59.98
REMARK 500 LYS C 315 99.72 -56.15
REMARK 500 ARG C 367 28.97 -76.97
REMARK 500 PRO D 107 8.60 -67.73
REMARK 500 THR D 163 -84.01 -95.82
REMARK 500 ALA D 176 -40.77 -145.98
REMARK 500 GLU D 191 -3.07 74.39
REMARK 500 MET D 325 61.44 -119.75
REMARK 500 ALA D 328 35.87 -90.42
REMARK 500 THR E 163 -91.66 -106.06
REMARK 500 ALA E 176 -44.82 -136.41
REMARK 500 ASP E 219 21.51 -75.92
REMARK 500 VAL E 235 -61.27 -98.82
REMARK 500 PRO E 354 27.97 -74.05
REMARK 500 SER E 355 -4.86 -151.08
REMARK 500 THR E 368 -70.19 -53.75
REMARK 500 ARG F 66 -73.53 -37.48
REMARK 500 LYS F 115 49.07 -104.40
REMARK 500 THR F 163 -88.20 -92.95
REMARK 500 ALA F 176 -47.49 -134.55
REMARK 500 ASP F 219 31.58 -83.56
REMARK 500 MET F 326 160.85 169.39
REMARK 500 ALA F 328 49.12 -73.75
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 FPS A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPS A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPS B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPS B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPS C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPS D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPS E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPS E 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VJ8 RELATED DB: PDB
REMARK 900 RELATED ID: 3VJ9 RELATED DB: PDB
REMARK 900 RELATED ID: 3VJA RELATED DB: PDB
REMARK 900 RELATED ID: 3VJB RELATED DB: PDB
REMARK 900 RELATED ID: 3VJC RELATED DB: PDB
REMARK 900 RELATED ID: 3VJD RELATED DB: PDB
REMARK 900 RELATED ID: 3WEG RELATED DB: PDB
REMARK 900 RELATED ID: 3WEH RELATED DB: PDB
REMARK 900 RELATED ID: 3WEI RELATED DB: PDB
REMARK 900 RELATED ID: 3WEJ RELATED DB: PDB
REMARK 900 RELATED ID: 3WEK RELATED DB: PDB
DBREF 3WEF A 31 370 UNP P37268 FDFT_HUMAN 31 370
DBREF 3WEF B 31 370 UNP P37268 FDFT_HUMAN 31 370
DBREF 3WEF C 31 370 UNP P37268 FDFT_HUMAN 31 370
DBREF 3WEF D 31 370 UNP P37268 FDFT_HUMAN 31 370
DBREF 3WEF E 31 370 UNP P37268 FDFT_HUMAN 31 370
DBREF 3WEF F 31 370 UNP P37268 FDFT_HUMAN 31 370
SEQADV 3WEF GLY A 28 UNP P37268 EXPRESSION TAG
SEQADV 3WEF SER A 29 UNP P37268 EXPRESSION TAG
SEQADV 3WEF HIS A 30 UNP P37268 EXPRESSION TAG
SEQADV 3WEF GLY B 28 UNP P37268 EXPRESSION TAG
SEQADV 3WEF SER B 29 UNP P37268 EXPRESSION TAG
SEQADV 3WEF HIS B 30 UNP P37268 EXPRESSION TAG
SEQADV 3WEF GLY C 28 UNP P37268 EXPRESSION TAG
SEQADV 3WEF SER C 29 UNP P37268 EXPRESSION TAG
SEQADV 3WEF HIS C 30 UNP P37268 EXPRESSION TAG
SEQADV 3WEF GLY D 28 UNP P37268 EXPRESSION TAG
SEQADV 3WEF SER D 29 UNP P37268 EXPRESSION TAG
SEQADV 3WEF HIS D 30 UNP P37268 EXPRESSION TAG
SEQADV 3WEF GLY E 28 UNP P37268 EXPRESSION TAG
SEQADV 3WEF SER E 29 UNP P37268 EXPRESSION TAG
SEQADV 3WEF HIS E 30 UNP P37268 EXPRESSION TAG
SEQADV 3WEF GLY F 28 UNP P37268 EXPRESSION TAG
SEQADV 3WEF SER F 29 UNP P37268 EXPRESSION TAG
SEQADV 3WEF HIS F 30 UNP P37268 EXPRESSION TAG
SEQRES 1 A 343 GLY SER HIS MET ASP GLN ASP SER LEU SER SER SER LEU
SEQRES 2 A 343 LYS THR CYS TYR LYS TYR LEU ASN GLN THR SER ARG SER
SEQRES 3 A 343 PHE ALA ALA VAL ILE GLN ALA LEU ASP GLY GLU MET ARG
SEQRES 4 A 343 ASN ALA VAL CYS ILE PHE TYR LEU VAL LEU ARG ALA LEU
SEQRES 5 A 343 ASP THR LEU GLU ASP ASP MET THR ILE SER VAL GLU LYS
SEQRES 6 A 343 LYS VAL PRO LEU LEU HIS ASN PHE HIS SER PHE LEU TYR
SEQRES 7 A 343 GLN PRO ASP TRP ARG PHE MET GLU SER LYS GLU LYS ASP
SEQRES 8 A 343 ARG GLN VAL LEU GLU ASP PHE PRO THR ILE SER LEU GLU
SEQRES 9 A 343 PHE ARG ASN LEU ALA GLU LYS TYR GLN THR VAL ILE ALA
SEQRES 10 A 343 ASP ILE CYS ARG ARG MET GLY ILE GLY MET ALA GLU PHE
SEQRES 11 A 343 LEU ASP LYS HIS VAL THR SER GLU GLN GLU TRP ASP LYS
SEQRES 12 A 343 TYR CYS HIS TYR VAL ALA GLY LEU VAL GLY ILE GLY LEU
SEQRES 13 A 343 SER ARG LEU PHE SER ALA SER GLU PHE GLU ASP PRO LEU
SEQRES 14 A 343 VAL GLY GLU ASP THR GLU ARG ALA ASN SER MET GLY LEU
SEQRES 15 A 343 PHE LEU GLN LYS THR ASN ILE ILE ARG ASP TYR LEU GLU
SEQRES 16 A 343 ASP GLN GLN GLY GLY ARG GLU PHE TRP PRO GLN GLU VAL
SEQRES 17 A 343 TRP SER ARG TYR VAL LYS LYS LEU GLY ASP PHE ALA LYS
SEQRES 18 A 343 PRO GLU ASN ILE ASP LEU ALA VAL GLN CYS LEU ASN GLU
SEQRES 19 A 343 LEU ILE THR ASN ALA LEU HIS HIS ILE PRO ASP VAL ILE
SEQRES 20 A 343 THR TYR LEU SER ARG LEU ARG ASN GLN SER VAL PHE ASN
SEQRES 21 A 343 PHE CYS ALA ILE PRO GLN VAL MET ALA ILE ALA THR LEU
SEQRES 22 A 343 ALA ALA CYS TYR ASN ASN GLN GLN VAL PHE LYS GLY ALA
SEQRES 23 A 343 VAL LYS ILE ARG LYS GLY GLN ALA VAL THR LEU MET MET
SEQRES 24 A 343 ASP ALA THR ASN MET PRO ALA VAL LYS ALA ILE ILE TYR
SEQRES 25 A 343 GLN TYR MET GLU GLU ILE TYR HIS ARG ILE PRO ASP SER
SEQRES 26 A 343 ASP PRO SER SER SER LYS THR ARG GLN ILE ILE SER THR
SEQRES 27 A 343 ILE ARG THR GLN ASN
SEQRES 1 B 343 GLY SER HIS MET ASP GLN ASP SER LEU SER SER SER LEU
SEQRES 2 B 343 LYS THR CYS TYR LYS TYR LEU ASN GLN THR SER ARG SER
SEQRES 3 B 343 PHE ALA ALA VAL ILE GLN ALA LEU ASP GLY GLU MET ARG
SEQRES 4 B 343 ASN ALA VAL CYS ILE PHE TYR LEU VAL LEU ARG ALA LEU
SEQRES 5 B 343 ASP THR LEU GLU ASP ASP MET THR ILE SER VAL GLU LYS
SEQRES 6 B 343 LYS VAL PRO LEU LEU HIS ASN PHE HIS SER PHE LEU TYR
SEQRES 7 B 343 GLN PRO ASP TRP ARG PHE MET GLU SER LYS GLU LYS ASP
SEQRES 8 B 343 ARG GLN VAL LEU GLU ASP PHE PRO THR ILE SER LEU GLU
SEQRES 9 B 343 PHE ARG ASN LEU ALA GLU LYS TYR GLN THR VAL ILE ALA
SEQRES 10 B 343 ASP ILE CYS ARG ARG MET GLY ILE GLY MET ALA GLU PHE
SEQRES 11 B 343 LEU ASP LYS HIS VAL THR SER GLU GLN GLU TRP ASP LYS
SEQRES 12 B 343 TYR CYS HIS TYR VAL ALA GLY LEU VAL GLY ILE GLY LEU
SEQRES 13 B 343 SER ARG LEU PHE SER ALA SER GLU PHE GLU ASP PRO LEU
SEQRES 14 B 343 VAL GLY GLU ASP THR GLU ARG ALA ASN SER MET GLY LEU
SEQRES 15 B 343 PHE LEU GLN LYS THR ASN ILE ILE ARG ASP TYR LEU GLU
SEQRES 16 B 343 ASP GLN GLN GLY GLY ARG GLU PHE TRP PRO GLN GLU VAL
SEQRES 17 B 343 TRP SER ARG TYR VAL LYS LYS LEU GLY ASP PHE ALA LYS
SEQRES 18 B 343 PRO GLU ASN ILE ASP LEU ALA VAL GLN CYS LEU ASN GLU
SEQRES 19 B 343 LEU ILE THR ASN ALA LEU HIS HIS ILE PRO ASP VAL ILE
SEQRES 20 B 343 THR TYR LEU SER ARG LEU ARG ASN GLN SER VAL PHE ASN
SEQRES 21 B 343 PHE CYS ALA ILE PRO GLN VAL MET ALA ILE ALA THR LEU
SEQRES 22 B 343 ALA ALA CYS TYR ASN ASN GLN GLN VAL PHE LYS GLY ALA
SEQRES 23 B 343 VAL LYS ILE ARG LYS GLY GLN ALA VAL THR LEU MET MET
SEQRES 24 B 343 ASP ALA THR ASN MET PRO ALA VAL LYS ALA ILE ILE TYR
SEQRES 25 B 343 GLN TYR MET GLU GLU ILE TYR HIS ARG ILE PRO ASP SER
SEQRES 26 B 343 ASP PRO SER SER SER LYS THR ARG GLN ILE ILE SER THR
SEQRES 27 B 343 ILE ARG THR GLN ASN
SEQRES 1 C 343 GLY SER HIS MET ASP GLN ASP SER LEU SER SER SER LEU
SEQRES 2 C 343 LYS THR CYS TYR LYS TYR LEU ASN GLN THR SER ARG SER
SEQRES 3 C 343 PHE ALA ALA VAL ILE GLN ALA LEU ASP GLY GLU MET ARG
SEQRES 4 C 343 ASN ALA VAL CYS ILE PHE TYR LEU VAL LEU ARG ALA LEU
SEQRES 5 C 343 ASP THR LEU GLU ASP ASP MET THR ILE SER VAL GLU LYS
SEQRES 6 C 343 LYS VAL PRO LEU LEU HIS ASN PHE HIS SER PHE LEU TYR
SEQRES 7 C 343 GLN PRO ASP TRP ARG PHE MET GLU SER LYS GLU LYS ASP
SEQRES 8 C 343 ARG GLN VAL LEU GLU ASP PHE PRO THR ILE SER LEU GLU
SEQRES 9 C 343 PHE ARG ASN LEU ALA GLU LYS TYR GLN THR VAL ILE ALA
SEQRES 10 C 343 ASP ILE CYS ARG ARG MET GLY ILE GLY MET ALA GLU PHE
SEQRES 11 C 343 LEU ASP LYS HIS VAL THR SER GLU GLN GLU TRP ASP LYS
SEQRES 12 C 343 TYR CYS HIS TYR VAL ALA GLY LEU VAL GLY ILE GLY LEU
SEQRES 13 C 343 SER ARG LEU PHE SER ALA SER GLU PHE GLU ASP PRO LEU
SEQRES 14 C 343 VAL GLY GLU ASP THR GLU ARG ALA ASN SER MET GLY LEU
SEQRES 15 C 343 PHE LEU GLN LYS THR ASN ILE ILE ARG ASP TYR LEU GLU
SEQRES 16 C 343 ASP GLN GLN GLY GLY ARG GLU PHE TRP PRO GLN GLU VAL
SEQRES 17 C 343 TRP SER ARG TYR VAL LYS LYS LEU GLY ASP PHE ALA LYS
SEQRES 18 C 343 PRO GLU ASN ILE ASP LEU ALA VAL GLN CYS LEU ASN GLU
SEQRES 19 C 343 LEU ILE THR ASN ALA LEU HIS HIS ILE PRO ASP VAL ILE
SEQRES 20 C 343 THR TYR LEU SER ARG LEU ARG ASN GLN SER VAL PHE ASN
SEQRES 21 C 343 PHE CYS ALA ILE PRO GLN VAL MET ALA ILE ALA THR LEU
SEQRES 22 C 343 ALA ALA CYS TYR ASN ASN GLN GLN VAL PHE LYS GLY ALA
SEQRES 23 C 343 VAL LYS ILE ARG LYS GLY GLN ALA VAL THR LEU MET MET
SEQRES 24 C 343 ASP ALA THR ASN MET PRO ALA VAL LYS ALA ILE ILE TYR
SEQRES 25 C 343 GLN TYR MET GLU GLU ILE TYR HIS ARG ILE PRO ASP SER
SEQRES 26 C 343 ASP PRO SER SER SER LYS THR ARG GLN ILE ILE SER THR
SEQRES 27 C 343 ILE ARG THR GLN ASN
SEQRES 1 D 343 GLY SER HIS MET ASP GLN ASP SER LEU SER SER SER LEU
SEQRES 2 D 343 LYS THR CYS TYR LYS TYR LEU ASN GLN THR SER ARG SER
SEQRES 3 D 343 PHE ALA ALA VAL ILE GLN ALA LEU ASP GLY GLU MET ARG
SEQRES 4 D 343 ASN ALA VAL CYS ILE PHE TYR LEU VAL LEU ARG ALA LEU
SEQRES 5 D 343 ASP THR LEU GLU ASP ASP MET THR ILE SER VAL GLU LYS
SEQRES 6 D 343 LYS VAL PRO LEU LEU HIS ASN PHE HIS SER PHE LEU TYR
SEQRES 7 D 343 GLN PRO ASP TRP ARG PHE MET GLU SER LYS GLU LYS ASP
SEQRES 8 D 343 ARG GLN VAL LEU GLU ASP PHE PRO THR ILE SER LEU GLU
SEQRES 9 D 343 PHE ARG ASN LEU ALA GLU LYS TYR GLN THR VAL ILE ALA
SEQRES 10 D 343 ASP ILE CYS ARG ARG MET GLY ILE GLY MET ALA GLU PHE
SEQRES 11 D 343 LEU ASP LYS HIS VAL THR SER GLU GLN GLU TRP ASP LYS
SEQRES 12 D 343 TYR CYS HIS TYR VAL ALA GLY LEU VAL GLY ILE GLY LEU
SEQRES 13 D 343 SER ARG LEU PHE SER ALA SER GLU PHE GLU ASP PRO LEU
SEQRES 14 D 343 VAL GLY GLU ASP THR GLU ARG ALA ASN SER MET GLY LEU
SEQRES 15 D 343 PHE LEU GLN LYS THR ASN ILE ILE ARG ASP TYR LEU GLU
SEQRES 16 D 343 ASP GLN GLN GLY GLY ARG GLU PHE TRP PRO GLN GLU VAL
SEQRES 17 D 343 TRP SER ARG TYR VAL LYS LYS LEU GLY ASP PHE ALA LYS
SEQRES 18 D 343 PRO GLU ASN ILE ASP LEU ALA VAL GLN CYS LEU ASN GLU
SEQRES 19 D 343 LEU ILE THR ASN ALA LEU HIS HIS ILE PRO ASP VAL ILE
SEQRES 20 D 343 THR TYR LEU SER ARG LEU ARG ASN GLN SER VAL PHE ASN
SEQRES 21 D 343 PHE CYS ALA ILE PRO GLN VAL MET ALA ILE ALA THR LEU
SEQRES 22 D 343 ALA ALA CYS TYR ASN ASN GLN GLN VAL PHE LYS GLY ALA
SEQRES 23 D 343 VAL LYS ILE ARG LYS GLY GLN ALA VAL THR LEU MET MET
SEQRES 24 D 343 ASP ALA THR ASN MET PRO ALA VAL LYS ALA ILE ILE TYR
SEQRES 25 D 343 GLN TYR MET GLU GLU ILE TYR HIS ARG ILE PRO ASP SER
SEQRES 26 D 343 ASP PRO SER SER SER LYS THR ARG GLN ILE ILE SER THR
SEQRES 27 D 343 ILE ARG THR GLN ASN
SEQRES 1 E 343 GLY SER HIS MET ASP GLN ASP SER LEU SER SER SER LEU
SEQRES 2 E 343 LYS THR CYS TYR LYS TYR LEU ASN GLN THR SER ARG SER
SEQRES 3 E 343 PHE ALA ALA VAL ILE GLN ALA LEU ASP GLY GLU MET ARG
SEQRES 4 E 343 ASN ALA VAL CYS ILE PHE TYR LEU VAL LEU ARG ALA LEU
SEQRES 5 E 343 ASP THR LEU GLU ASP ASP MET THR ILE SER VAL GLU LYS
SEQRES 6 E 343 LYS VAL PRO LEU LEU HIS ASN PHE HIS SER PHE LEU TYR
SEQRES 7 E 343 GLN PRO ASP TRP ARG PHE MET GLU SER LYS GLU LYS ASP
SEQRES 8 E 343 ARG GLN VAL LEU GLU ASP PHE PRO THR ILE SER LEU GLU
SEQRES 9 E 343 PHE ARG ASN LEU ALA GLU LYS TYR GLN THR VAL ILE ALA
SEQRES 10 E 343 ASP ILE CYS ARG ARG MET GLY ILE GLY MET ALA GLU PHE
SEQRES 11 E 343 LEU ASP LYS HIS VAL THR SER GLU GLN GLU TRP ASP LYS
SEQRES 12 E 343 TYR CYS HIS TYR VAL ALA GLY LEU VAL GLY ILE GLY LEU
SEQRES 13 E 343 SER ARG LEU PHE SER ALA SER GLU PHE GLU ASP PRO LEU
SEQRES 14 E 343 VAL GLY GLU ASP THR GLU ARG ALA ASN SER MET GLY LEU
SEQRES 15 E 343 PHE LEU GLN LYS THR ASN ILE ILE ARG ASP TYR LEU GLU
SEQRES 16 E 343 ASP GLN GLN GLY GLY ARG GLU PHE TRP PRO GLN GLU VAL
SEQRES 17 E 343 TRP SER ARG TYR VAL LYS LYS LEU GLY ASP PHE ALA LYS
SEQRES 18 E 343 PRO GLU ASN ILE ASP LEU ALA VAL GLN CYS LEU ASN GLU
SEQRES 19 E 343 LEU ILE THR ASN ALA LEU HIS HIS ILE PRO ASP VAL ILE
SEQRES 20 E 343 THR TYR LEU SER ARG LEU ARG ASN GLN SER VAL PHE ASN
SEQRES 21 E 343 PHE CYS ALA ILE PRO GLN VAL MET ALA ILE ALA THR LEU
SEQRES 22 E 343 ALA ALA CYS TYR ASN ASN GLN GLN VAL PHE LYS GLY ALA
SEQRES 23 E 343 VAL LYS ILE ARG LYS GLY GLN ALA VAL THR LEU MET MET
SEQRES 24 E 343 ASP ALA THR ASN MET PRO ALA VAL LYS ALA ILE ILE TYR
SEQRES 25 E 343 GLN TYR MET GLU GLU ILE TYR HIS ARG ILE PRO ASP SER
SEQRES 26 E 343 ASP PRO SER SER SER LYS THR ARG GLN ILE ILE SER THR
SEQRES 27 E 343 ILE ARG THR GLN ASN
SEQRES 1 F 343 GLY SER HIS MET ASP GLN ASP SER LEU SER SER SER LEU
SEQRES 2 F 343 LYS THR CYS TYR LYS TYR LEU ASN GLN THR SER ARG SER
SEQRES 3 F 343 PHE ALA ALA VAL ILE GLN ALA LEU ASP GLY GLU MET ARG
SEQRES 4 F 343 ASN ALA VAL CYS ILE PHE TYR LEU VAL LEU ARG ALA LEU
SEQRES 5 F 343 ASP THR LEU GLU ASP ASP MET THR ILE SER VAL GLU LYS
SEQRES 6 F 343 LYS VAL PRO LEU LEU HIS ASN PHE HIS SER PHE LEU TYR
SEQRES 7 F 343 GLN PRO ASP TRP ARG PHE MET GLU SER LYS GLU LYS ASP
SEQRES 8 F 343 ARG GLN VAL LEU GLU ASP PHE PRO THR ILE SER LEU GLU
SEQRES 9 F 343 PHE ARG ASN LEU ALA GLU LYS TYR GLN THR VAL ILE ALA
SEQRES 10 F 343 ASP ILE CYS ARG ARG MET GLY ILE GLY MET ALA GLU PHE
SEQRES 11 F 343 LEU ASP LYS HIS VAL THR SER GLU GLN GLU TRP ASP LYS
SEQRES 12 F 343 TYR CYS HIS TYR VAL ALA GLY LEU VAL GLY ILE GLY LEU
SEQRES 13 F 343 SER ARG LEU PHE SER ALA SER GLU PHE GLU ASP PRO LEU
SEQRES 14 F 343 VAL GLY GLU ASP THR GLU ARG ALA ASN SER MET GLY LEU
SEQRES 15 F 343 PHE LEU GLN LYS THR ASN ILE ILE ARG ASP TYR LEU GLU
SEQRES 16 F 343 ASP GLN GLN GLY GLY ARG GLU PHE TRP PRO GLN GLU VAL
SEQRES 17 F 343 TRP SER ARG TYR VAL LYS LYS LEU GLY ASP PHE ALA LYS
SEQRES 18 F 343 PRO GLU ASN ILE ASP LEU ALA VAL GLN CYS LEU ASN GLU
SEQRES 19 F 343 LEU ILE THR ASN ALA LEU HIS HIS ILE PRO ASP VAL ILE
SEQRES 20 F 343 THR TYR LEU SER ARG LEU ARG ASN GLN SER VAL PHE ASN
SEQRES 21 F 343 PHE CYS ALA ILE PRO GLN VAL MET ALA ILE ALA THR LEU
SEQRES 22 F 343 ALA ALA CYS TYR ASN ASN GLN GLN VAL PHE LYS GLY ALA
SEQRES 23 F 343 VAL LYS ILE ARG LYS GLY GLN ALA VAL THR LEU MET MET
SEQRES 24 F 343 ASP ALA THR ASN MET PRO ALA VAL LYS ALA ILE ILE TYR
SEQRES 25 F 343 GLN TYR MET GLU GLU ILE TYR HIS ARG ILE PRO ASP SER
SEQRES 26 F 343 ASP PRO SER SER SER LYS THR ARG GLN ILE ILE SER THR
SEQRES 27 F 343 ILE ARG THR GLN ASN
HET FPS A 401 24
HET FPS A 402 24
HET FPS B 401 24
HET FPS B 402 24
HET FPS C 401 24
HET FPS D 401 24
HET FPS E 401 24
HET FPS E 402 24
HETNAM FPS S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL]
HETNAM 2 FPS TRIHYDROGEN THIODIPHOSPHATE
HETSYN FPS FARNESYL THIOPYROPHOSPHATE
FORMUL 7 FPS 8(C15 H28 O6 P2 S)
FORMUL 15 HOH *352(H2 O)
HELIX 1 1 SER A 37 SER A 51 1 15
HELIX 2 2 PHE A 54 ALA A 60 1 7
HELIX 3 3 GLU A 64 ASP A 85 1 22
HELIX 4 4 SER A 89 LEU A 104 1 16
HELIX 5 5 ARG A 119 ASP A 124 1 6
HELIX 6 6 ASP A 124 ASN A 134 1 11
HELIX 7 7 ALA A 136 LEU A 158 1 23
HELIX 8 8 SER A 164 ALA A 176 1 13
HELIX 9 9 ALA A 176 SER A 190 1 15
HELIX 10 10 ASP A 194 ASP A 200 1 7
HELIX 11 11 ASP A 200 ASP A 219 1 20
HELIX 12 12 ASP A 219 GLN A 225 1 7
HELIX 13 13 PRO A 232 SER A 237 1 6
HELIX 14 14 LYS A 242 GLU A 250 5 9
HELIX 15 15 ASN A 251 HIS A 268 1 18
HELIX 16 16 HIS A 269 LEU A 280 1 12
HELIX 17 17 ASN A 282 TYR A 304 1 23
HELIX 18 18 ASN A 306 LYS A 311 5 6
HELIX 19 19 ASN A 330 ILE A 349 1 20
HELIX 20 20 SER A 355 GLN A 369 1 15
HELIX 21 21 SER B 38 SER B 51 1 14
HELIX 22 22 PHE B 54 ALA B 60 1 7
HELIX 23 23 GLU B 64 ASP B 85 1 22
HELIX 24 24 SER B 89 LEU B 104 1 16
HELIX 25 25 ARG B 119 ASP B 124 1 6
HELIX 26 26 ASP B 124 ASN B 134 1 11
HELIX 27 27 ALA B 136 ASP B 159 1 24
HELIX 28 28 SER B 164 ALA B 176 1 13
HELIX 29 29 ALA B 176 SER B 190 1 15
HELIX 30 30 PRO B 195 ASP B 200 1 6
HELIX 31 31 ASP B 200 ASP B 219 1 20
HELIX 32 32 ASP B 219 GLN B 225 1 7
HELIX 33 33 PRO B 232 SER B 237 1 6
HELIX 34 34 LYS B 242 GLU B 250 5 9
HELIX 35 35 ASN B 251 HIS B 268 1 18
HELIX 36 36 HIS B 269 LEU B 280 1 12
HELIX 37 37 ASN B 282 TYR B 304 1 23
HELIX 38 38 ASN B 306 LYS B 311 5 6
HELIX 39 39 VAL B 322 MET B 326 5 5
HELIX 40 40 ASN B 330 ILE B 349 1 20
HELIX 41 41 SER B 355 GLN B 369 1 15
HELIX 42 42 SER C 37 SER C 51 1 15
HELIX 43 43 PHE C 54 ALA C 60 1 7
HELIX 44 44 GLU C 64 ASP C 85 1 22
HELIX 45 45 SER C 89 LEU C 104 1 16
HELIX 46 46 ARG C 119 ASP C 124 1 6
HELIX 47 47 ASP C 124 LEU C 135 1 12
HELIX 48 48 ALA C 136 PHE C 157 1 22
HELIX 49 49 SER C 164 ALA C 176 1 13
HELIX 50 50 ALA C 176 SER C 190 1 15
HELIX 51 51 ASP C 194 ASP C 200 1 7
HELIX 52 52 ASP C 200 ASP C 219 1 20
HELIX 53 53 ASP C 219 GLN C 225 1 7
HELIX 54 54 PRO C 232 SER C 237 1 6
HELIX 55 55 LYS C 242 GLU C 250 5 9
HELIX 56 56 ASN C 251 LEU C 267 1 17
HELIX 57 57 HIS C 269 ARG C 279 1 11
HELIX 58 58 ASN C 282 TYR C 304 1 23
HELIX 59 59 ASN C 306 LYS C 311 5 6
HELIX 60 60 GLN C 320 MET C 325 1 6
HELIX 61 61 ASN C 330 ARG C 348 1 19
HELIX 62 62 SER C 355 ARG C 367 1 13
HELIX 63 63 SER D 38 SER D 51 1 14
HELIX 64 64 PHE D 54 ALA D 60 1 7
HELIX 65 65 GLU D 64 ASP D 85 1 22
HELIX 66 66 SER D 89 ASN D 99 1 11
HELIX 67 67 ASN D 99 LEU D 104 1 6
HELIX 68 68 ARG D 119 ASP D 124 1 6
HELIX 69 69 ASP D 124 ASN D 134 1 11
HELIX 70 70 ALA D 136 LEU D 158 1 23
HELIX 71 71 SER D 164 ALA D 176 1 13
HELIX 72 72 ALA D 176 GLU D 191 1 16
HELIX 73 73 PRO D 195 ASP D 200 1 6
HELIX 74 74 ASP D 200 ASP D 219 1 20
HELIX 75 75 ASP D 219 GLY D 226 1 8
HELIX 76 76 PRO D 232 SER D 237 1 6
HELIX 77 77 LYS D 242 GLU D 250 5 9
HELIX 78 78 ASN D 251 HIS D 268 1 18
HELIX 79 79 HIS D 269 LEU D 280 1 12
HELIX 80 80 ASN D 282 TYR D 304 1 23
HELIX 81 81 ASN D 306 LYS D 311 5 6
HELIX 82 82 ASN D 330 ILE D 349 1 20
HELIX 83 83 SER D 355 GLN D 369 1 15
HELIX 84 84 SER E 38 SER E 51 1 14
HELIX 85 85 PHE E 54 ALA E 60 1 7
HELIX 86 86 GLU E 64 ASP E 85 1 22
HELIX 87 87 SER E 89 LEU E 104 1 16
HELIX 88 88 ARG E 119 ASP E 124 1 6
HELIX 89 89 ASP E 124 ASN E 134 1 11
HELIX 90 90 ALA E 136 PHE E 157 1 22
HELIX 91 91 SER E 164 ALA E 176 1 13
HELIX 92 92 ALA E 176 SER E 190 1 15
HELIX 93 93 ASP E 194 ASP E 200 1 7
HELIX 94 94 ASP E 200 ASP E 219 1 20
HELIX 95 95 ASP E 219 GLY E 227 1 9
HELIX 96 96 PRO E 232 SER E 237 1 6
HELIX 97 97 LYS E 242 GLU E 250 5 9
HELIX 98 98 ASN E 251 HIS E 268 1 18
HELIX 99 99 HIS E 269 ARG E 279 1 11
HELIX 100 100 ASN E 282 TYR E 304 1 23
HELIX 101 101 ASN E 306 LYS E 311 5 6
HELIX 102 102 VAL E 322 MET E 326 5 5
HELIX 103 103 ASN E 330 ARG E 348 1 19
HELIX 104 104 SER E 355 ARG E 367 1 13
HELIX 105 105 SER F 39 SER F 51 1 13
HELIX 106 106 SER F 53 ALA F 60 1 8
HELIX 107 107 GLU F 64 ASP F 84 1 21
HELIX 108 108 SER F 89 LEU F 104 1 16
HELIX 109 109 ARG F 119 ASP F 124 1 6
HELIX 110 110 PHE F 125 ARG F 133 1 9
HELIX 111 111 ALA F 136 PHE F 157 1 22
HELIX 112 112 SER F 164 ALA F 176 1 13
HELIX 113 113 ALA F 176 SER F 190 1 15
HELIX 114 114 ASP F 194 ASP F 200 1 7
HELIX 115 115 ASP F 200 ASP F 219 1 20
HELIX 116 116 ASP F 219 GLN F 225 1 7
HELIX 117 117 PRO F 232 SER F 237 1 6
HELIX 118 118 LYS F 242 LYS F 248 5 7
HELIX 119 119 ASN F 251 HIS F 268 1 18
HELIX 120 120 HIS F 269 LEU F 280 1 12
HELIX 121 121 ASN F 282 TYR F 304 1 23
HELIX 122 122 ASN F 306 LYS F 311 5 6
HELIX 123 123 ASN F 330 HIS F 347 1 18
HELIX 124 124 SER F 355 GLN F 369 1 15
SITE 1 AC1 13 THR A 50 SER A 51 ARG A 52 SER A 53
SITE 2 AC1 13 PHE A 54 ARG A 77 GLY A 180 MET A 207
SITE 3 AC1 13 LEU A 211 GLN A 212 ASN A 215 CYS A 289
SITE 4 AC1 13 FPS A 402
SITE 1 AC2 8 ILE A 58 TYR A 73 ARG A 77 ASP A 80
SITE 2 AC2 8 ASP A 84 VAL A 175 PHE A 288 FPS A 401
SITE 1 AC3 14 THR B 50 ARG B 52 SER B 53 PHE B 54
SITE 2 AC3 14 TYR B 73 ARG B 77 VAL B 179 GLY B 180
SITE 3 AC3 14 MET B 207 LEU B 211 GLN B 212 TYR B 276
SITE 4 AC3 14 CYS B 289 FPS B 402
SITE 1 AC4 13 TYR B 73 ARG B 77 ASP B 80 GLU B 83
SITE 2 AC4 13 ASP B 84 MET B 150 MET B 154 TYR B 171
SITE 3 AC4 13 VAL B 175 VAL B 179 GLN B 212 PHE B 288
SITE 4 AC4 13 FPS B 401
SITE 1 AC5 12 THR C 50 SER C 51 ARG C 52 SER C 53
SITE 2 AC5 12 PHE C 54 ARG C 77 GLY C 180 MET C 207
SITE 3 AC5 12 LEU C 211 GLN C 212 ASN C 215 CYS C 289
SITE 1 AC6 16 THR D 50 SER D 51 SER D 53 PHE D 54
SITE 2 AC6 16 TYR D 73 ARG D 77 GLY D 180 LEU D 183
SITE 3 AC6 16 MET D 207 GLN D 212 ASN D 215 PHE D 288
SITE 4 AC6 16 CYS D 289 HOH D 505 HOH D 516 HOH D 520
SITE 1 AC7 13 THR E 50 SER E 51 ARG E 52 SER E 53
SITE 2 AC7 13 PHE E 54 TYR E 73 GLY E 180 MET E 207
SITE 3 AC7 13 LEU E 211 GLN E 212 ASN E 215 CYS E 289
SITE 4 AC7 13 FPS E 402
SITE 1 AC8 11 TYR E 73 ARG E 77 ASP E 80 GLU E 83
SITE 2 AC8 11 ASP E 84 TYR E 171 VAL E 175 GLN E 212
SITE 3 AC8 11 ARG E 228 PHE E 230 FPS E 401
CRYST1 85.888 153.752 91.613 90.00 91.06 90.00 P 1 21 1 12
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 0.011643 0.000000 0.000215 0.00000
SCALE2 0.000000 0.006504 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010917 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
