HEADER TRANSFERASE/TRANSFERASE INHIBITOR 14-JUN-11 3SFX
TITLE CRYPTOCOCCUS NEOFORMANS PROTEIN FARNESYLTRANSFERASE IN COMPLEX WITH
TITLE 2 FPT-II AND TIPIFARNIB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CRYPTOCOCCUS NEOFORMANS PROTEIN FARNESYLTRANSFERASE ALPHA
COMPND 3 SUBUNIT;
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CRYPTOCOCCUS NEOFORMANS PROTEIN FARNESYLTRANSFERASE BETA
COMPND 8 SUBUNIT;
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRYPTOCOCCUS NEOFORMANS;
SOURCE 3 ORGANISM_TAXID: 235443;
SOURCE 4 STRAIN: H99;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: CRYPTOCOCCUS NEOFORMANS;
SOURCE 9 ORGANISM_TAXID: 235443;
SOURCE 10 STRAIN: H99;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PRENYLTRANSFERASE, PROTEIN FARNESYLTRANSFERASE, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.HAST,L.S.BEESE
REVDAT 3 28-FEB-24 3SFX 1 REMARK LINK
REVDAT 2 19-OCT-11 3SFX 1 JRNL
REVDAT 1 03-AUG-11 3SFX 0
JRNL AUTH M.A.HAST,C.B.NICHOLS,S.M.ARMSTRONG,S.M.KELLY,H.W.HELLINGA,
JRNL AUTH 2 J.A.ALSPAUGH,L.S.BEESE
JRNL TITL STRUCTURES OF CRYPTOCOCCUS NEOFORMANS PROTEIN
JRNL TITL 2 FARNESYLTRANSFERASE REVEAL STRATEGIES FOR DEVELOPING
JRNL TITL 3 INHIBITORS THAT TARGET FUNGAL PATHOGENS.
JRNL REF J.BIOL.CHEM. V. 286 35149 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21816822
JRNL DOI 10.1074/JBC.M111.250506
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 85314
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4538
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6207
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE SET COUNT : 338
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6346
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 109
REMARK 3 SOLVENT ATOMS : 669
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.162
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6638 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9029 ; 1.264 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 796 ; 5.338 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 302 ;33.429 ;23.377
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1050 ;14.239 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 47 ;15.035 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 961 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5097 ; 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): 3997 ; 0.591 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6448 ; 1.121 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2641 ; 1.797 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2580 ; 2.924 ; 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): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 5 A 334
REMARK 3 ORIGIN FOR THE GROUP (A): 34.5823 -30.3482 8.3903
REMARK 3 T TENSOR
REMARK 3 T11: 0.0543 T22: 0.0521
REMARK 3 T33: 0.0978 T12: -0.0310
REMARK 3 T13: -0.0195 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.3164 L22: 0.9693
REMARK 3 L33: 1.2698 L12: 0.0604
REMARK 3 L13: -0.0029 L23: -0.1505
REMARK 3 S TENSOR
REMARK 3 S11: 0.0031 S12: -0.0905 S13: 0.0338
REMARK 3 S21: 0.1054 S22: -0.0279 S23: -0.0891
REMARK 3 S31: -0.1148 S32: 0.1506 S33: 0.0247
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 519
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0698 -32.1147 -10.3360
REMARK 3 T TENSOR
REMARK 3 T11: 0.0245 T22: 0.0207
REMARK 3 T33: 0.0718 T12: -0.0190
REMARK 3 T13: -0.0006 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.5237 L22: 0.5538
REMARK 3 L33: 1.3945 L12: 0.1161
REMARK 3 L13: 0.0326 L23: -0.1617
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: -0.0099 S13: 0.0197
REMARK 3 S21: -0.0497 S22: 0.0057 S23: 0.0097
REMARK 3 S31: 0.0080 S32: -0.0614 S33: 0.0056
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 3SFX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1000066154.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 12.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85314
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4K, CAPSO PH 9.5, LITHIUM SULFATE,
REMARK 280 SODIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 65.04800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 71.08800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 71.08800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 97.57200
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 71.08800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 71.08800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 32.52400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 71.08800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 71.08800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 97.57200
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 71.08800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 71.08800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 32.52400
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 65.04800
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: 9560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 B2738 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 -12
REMARK 465 GLY A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 SER A -2
REMARK 465 GLN A -1
REMARK 465 LEU A 0
REMARK 465 MET A 1
REMARK 465 VAL A 2
REMARK 465 THR A 3
REMARK 465 SER A 4
REMARK 465 SER A 258
REMARK 465 LYS A 259
REMARK 465 LEU A 260
REMARK 465 ASN A 261
REMARK 465 PRO A 262
REMARK 465 ASP A 263
REMARK 465 ILE A 264
REMARK 465 GLU A 265
REMARK 465 THR A 266
REMARK 465 VAL A 267
REMARK 465 GLU A 268
REMARK 465 ALA A 269
REMARK 465 PHE A 270
REMARK 465 GLY A 271
REMARK 465 ASP A 277
REMARK 465 GLU A 335
REMARK 465 GLU A 336
REMARK 465 MET B 1
REMARK 465 SER B 243
REMARK 465 VAL B 244
REMARK 465 VAL B 245
REMARK 465 PRO B 246
REMARK 465 SER B 247
REMARK 465 THR B 248
REMARK 465 SER B 249
REMARK 465 ALA B 250
REMARK 465 PHE B 251
REMARK 465 PRO B 252
REMARK 465 THR B 253
REMARK 465 SER B 254
REMARK 465 LYS B 350
REMARK 465 LYS B 351
REMARK 465 SER B 352
REMARK 465 ARG B 353
REMARK 465 ILE B 354
REMARK 465 GLU B 355
REMARK 465 VAL B 356
REMARK 465 PHE B 357
REMARK 465 GLU B 358
REMARK 465 GLU B 359
REMARK 465 GLU B 360
REMARK 465 LYS B 361
REMARK 465 GLU B 362
REMARK 465 GLY B 363
REMARK 465 ASP B 364
REMARK 465 TRP B 365
REMARK 465 GLU B 366
REMARK 465 ASP B 367
REMARK 465 VAL B 368
REMARK 465 PRO B 369
REMARK 465 PRO B 370
REMARK 465 ASN B 520
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1889 O HOH A 2912 8555 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 315 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG B 315 NE - CZ - NH2 ANGL. DEV. = -6.0 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 VAL A 31 47.06 35.71
REMARK 500 VAL A 198 -58.25 -121.90
REMARK 500 GLU A 317 -55.89 -126.24
REMARK 500 VAL B 51 67.42 -68.87
REMARK 500 SER B 52 107.30 -54.49
REMARK 500 GLN B 76 119.92 -173.14
REMARK 500 ASN B 219 -5.94 69.82
REMARK 500 ALA B 263 -169.43 -170.87
REMARK 500 SER B 394 -136.69 -127.45
REMARK 500 VAL B 500 -56.09 75.35
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 ZN B 521 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 323 OD2
REMARK 620 2 ASP B 323 OD1 54.4
REMARK 620 3 CYS B 325 SG 105.6 89.6
REMARK 620 4 HIS B 410 NE2 124.9 91.9 117.6
REMARK 620 5 JAN B 526 N2 101.6 156.0 98.2 104.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3FX B 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3FX B 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3FX B 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FII B 525
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JAN B 526
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 527
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3Q73 RELATED DB: PDB
REMARK 900 RELATED ID: 3Q75 RELATED DB: PDB
REMARK 900 RELATED ID: 3Q78 RELATED DB: PDB
REMARK 900 RELATED ID: 3Q79 RELATED DB: PDB
REMARK 900 RELATED ID: 3Q7A RELATED DB: PDB
REMARK 900 RELATED ID: 3Q7F RELATED DB: PDB
REMARK 900 RELATED ID: 3SFY RELATED DB: PDB
REMARK 999
REMARK 999 THERE IS NO UNIPORT DATABASE REFERENCE SEQUENCE AVAILABLE AT THE
REMARK 999 TIME OF THE DEPOSITION. THE SEQUENCES PRESENTED HERE ARE OF
REMARK 999 FARNESYLTRANSFERASE ALPHA SUBUNIT(RESIDUES 15-349) AND BETA
REMARK 999 SUBUNIT FROM CRYPTOCOCCUS NEOFORMANS VAR. GRUBII STRAIN H99. THE
REMARK 999 FIRST 14 RESIDUES IN THE ALPHA SUBUNIT(CHAIN A) REPRESENT
REMARK 999 EXPRESSION TAG.
DBREF 3SFX A -12 336 PDB 3SFX 3SFX -12 336
DBREF 3SFX B 1 520 PDB 3SFX 3SFX 1 520
SEQRES 1 A 349 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN LEU
SEQRES 2 A 349 MET VAL THR SER THR TYR ILE PRO MET SER GLN ARG ARG
SEQRES 3 A 349 SER TRP ALA ASP VAL LYS PRO ILE MET GLN ASP ASP GLY
SEQRES 4 A 349 PRO ASN PRO VAL VAL PRO ILE MET TYR SER GLU GLU TYR
SEQRES 5 A 349 LYS ASP ALA MET ASP TYR PHE ARG ALA ILE ALA ALA LYS
SEQRES 6 A 349 GLU GLU LYS SER GLU ARG ALA LEU GLU LEU THR GLU ILE
SEQRES 7 A 349 ILE VAL ARG MET ASN PRO ALA HIS TYR THR VAL TRP GLN
SEQRES 8 A 349 TYR ARG PHE SER LEU LEU THR SER LEU ASN LYS SER LEU
SEQRES 9 A 349 GLU ASP GLU LEU ARG LEU MET ASN GLU PHE ALA VAL GLN
SEQRES 10 A 349 ASN LEU LYS SER TYR GLN VAL TRP HIS HIS ARG LEU LEU
SEQRES 11 A 349 LEU LEU ASP ARG ILE SER PRO GLN ASP PRO VAL SER GLU
SEQRES 12 A 349 ILE GLU TYR ILE HIS GLY SER LEU LEU PRO ASP PRO LYS
SEQRES 13 A 349 ASN TYR HIS THR TRP ALA TYR LEU HIS TRP LEU TYR SER
SEQRES 14 A 349 HIS PHE SER THR LEU GLY ARG ILE SER GLU ALA GLN TRP
SEQRES 15 A 349 GLY SER GLU LEU ASP TRP CYS ASN GLU MET LEU ARG VAL
SEQRES 16 A 349 ASP GLY ARG ASN ASN SER ALA TRP GLY TRP ARG TRP TYR
SEQRES 17 A 349 LEU ARG VAL SER ARG PRO GLY ALA GLU THR SER SER ARG
SEQRES 18 A 349 SER LEU GLN ASP GLU LEU ILE TYR ILE LEU LYS SER ILE
SEQRES 19 A 349 HIS LEU ILE PRO HIS ASN VAL SER ALA TRP ASN TYR LEU
SEQRES 20 A 349 ARG GLY PHE LEU LYS HIS PHE SER LEU PRO LEU VAL PRO
SEQRES 21 A 349 ILE LEU PRO ALA ILE LEU PRO TYR THR ALA SER LYS LEU
SEQRES 22 A 349 ASN PRO ASP ILE GLU THR VAL GLU ALA PHE GLY PHE PRO
SEQRES 23 A 349 MET PRO SER ASP PRO LEU PRO GLU ASP THR PRO LEU PRO
SEQRES 24 A 349 VAL PRO LEU ALA LEU GLU TYR LEU ALA ASP SER PHE ILE
SEQRES 25 A 349 GLU GLN ASN ARG VAL ASP ASP ALA ALA LYS VAL PHE GLU
SEQRES 26 A 349 LYS LEU SER SER GLU TYR ASP GLN MET ARG ALA GLY TYR
SEQRES 27 A 349 TRP GLU PHE ARG ARG ARG GLU CYS ALA GLU GLU
SEQRES 1 B 520 MET ALA THR GLU PHE THR PRO SER VAL TYR SER LEU VAL
SEQRES 2 B 520 SER LYS PRO LEU PRO SER ASN SER ARG PRO SER ALA THR
SEQRES 3 B 520 LEU ASP GLU GLN ALA GLU THR GLU ASP LEU ILE SER GLN
SEQRES 4 B 520 LEU PHE ASP LEU THR ALA ASP PRO ASN ALA LEU VAL SER
SEQRES 5 B 520 GLU HIS GLY LYS ARG TYR SER GLY LEU ARG LYS GLN GLU
SEQRES 6 B 520 HIS THR GLN PHE LEU ALA SER SER PHE PHE GLN LEU PRO
SEQRES 7 B 520 GLY LYS PHE VAL SER LEU ASP ALA SER ARG PRO TRP LEU
SEQRES 8 B 520 VAL PHE TRP THR VAL HIS SER LEU ASP LEU LEU GLY VAL
SEQRES 9 B 520 ALA LEU ASP GLN GLY THR LYS ASP ARG VAL VAL SER THR
SEQRES 10 B 520 LEU LEU HIS PHE LEU SER PRO LYS GLY GLY PHE GLY GLY
SEQRES 11 B 520 GLY PRO ALA ASN SER GLN ILE PRO HIS LEU LEU PRO THR
SEQRES 12 B 520 TYR ALA SER VAL CYS SER LEU ALA ILE ALA GLY ASN ASP
SEQRES 13 B 520 SER SER THR GLY GLY TRP LYS ASP LEU ALA ALA ALA ARG
SEQRES 14 B 520 GLN SER ILE TYR GLU PHE PHE MET ARG CYS LYS ARG PRO
SEQRES 15 B 520 ASP GLY GLY PHE VAL VAL CYS GLU GLY GLY GLU VAL ASP
SEQRES 16 B 520 VAL ARG GLY THR TYR CYS LEU LEU VAL VAL ALA THR LEU
SEQRES 17 B 520 LEU ASP ILE ILE THR PRO GLU LEU LEU HIS ASN VAL ASP
SEQRES 18 B 520 LYS PHE VAL SER ALA CYS GLN THR TYR GLU GLY GLY PHE
SEQRES 19 B 520 ALA CYS ALA SER PHE PRO PHE PRO SER VAL VAL PRO SER
SEQRES 20 B 520 THR SER ALA PHE PRO THR SER GLU PRO SER CYS ARG VAL
SEQRES 21 B 520 SER MET ALA GLU ALA HIS GLY GLY TYR THR SER CYS SER
SEQRES 22 B 520 LEU ASN SER HIS PHE LEU LEU THR SER VAL PRO LEU PRO
SEQRES 23 B 520 SER PHE PRO LEU SER ILE ASP ALA ASN ALA ALA LEU ARG
SEQRES 24 B 520 TRP THR VAL LEU GLN GLN GLY GLU PRO ILE GLU GLY GLY
SEQRES 25 B 520 GLY PHE ARG GLY ARG THR ASN LYS LEU VAL ASP GLY CYS
SEQRES 26 B 520 TYR SER TRP TRP VAL GLY GLY GLY ALA PRO VAL ALA GLU
SEQRES 27 B 520 GLU LEU VAL ARG ARG GLU LYS SER ARG LYS VAL LYS LYS
SEQRES 28 B 520 SER ARG ILE GLU VAL PHE GLU GLU GLU LYS GLU GLY ASP
SEQRES 29 B 520 TRP GLU ASP VAL PRO PRO ILE PRO PRO ILE PHE ASN ARG
SEQRES 30 B 520 VAL ALA LEU GLN GLU PHE THR LEU VAL ALA ALA GLN GLN
SEQRES 31 B 520 ASP PRO GLY SER THR GLY GLY LEU ARG ASP LYS PRO GLY
SEQRES 32 B 520 LYS ARG PRO ASP GLN TYR HIS THR CYS ASN ASN LEU SER
SEQRES 33 B 520 GLY LEU SER ILE ALA GLN HIS LYS MET SER HIS SER PRO
SEQRES 34 B 520 SER THR VAL SER SER ASN ARG LEU LYS PHE ASP ALA SER
SEQRES 35 B 520 LYS GLY LEU PRO ALA VAL LYS PRO VAL ALA PRO GLY GLY
SEQRES 36 B 520 GLY TRP LYS ASN GLU ASP GLU ARG GLN ASN ALA ARG ARG
SEQRES 37 B 520 GLU ILE TRP ALA ASN ALA LEU GLY TRP ILE GLU GLU GLU
SEQRES 38 B 520 GLY GLY GLU ILE ILE VAL GLY GLY LYS ASP ASN ARG ILE
SEQRES 39 B 520 ASN THR THR THR PRO VAL PHE ASN ILE LEU GLY LEU ARG
SEQRES 40 B 520 LEU LYS PRO PHE ILE ASN TYR PHE TYR CYS GLN GLU ASN
HET ZN B 521 1
HET 3FX B 522 15
HET 3FX B 523 15
HET 3FX B 524 15
HET FII B 525 24
HET JAN B 526 34
HET SO4 B 527 5
HETNAM ZN ZINC ION
HETNAM 3FX (2R)-3-(CYCLOHEXYLAMINO)-2-HYDROXYPROPANE-1-SULFONIC
HETNAM 2 3FX ACID
HETNAM FII [(3,7,11-TRIMETHYL-DODECA-2,6,10-TRIENYLOXYCARBAMOYL)-
HETNAM 2 FII METHYL]-PHOSPHONIC ACID
HETNAM JAN 6-[(S)-AMINO(4-CHLOROPHENYL)(1-METHYL-1H-IMIDAZOL-5-
HETNAM 2 JAN YL)METHYL]-4-(3-CHLOROPHENYL)-1-METHYLQUINOLIN-2(1H)-
HETNAM 3 JAN ONE
HETNAM SO4 SULFATE ION
HETSYN FII FPP ANALOG
HETSYN JAN R115777; TIPIFARNIB
FORMUL 3 ZN ZN 2+
FORMUL 4 3FX 3(C9 H19 N O4 S)
FORMUL 7 FII C17 H30 N O5 P
FORMUL 8 JAN C27 H22 CL2 N4 O
FORMUL 9 SO4 O4 S 2-
FORMUL 10 HOH *669(H2 O)
HELIX 1 1 PRO A 8 ALA A 16 5 9
HELIX 2 2 SER A 36 LYS A 52 1 17
HELIX 3 3 SER A 56 ASN A 70 1 15
HELIX 4 4 HIS A 73 LEU A 87 1 15
HELIX 5 5 SER A 90 GLN A 104 1 15
HELIX 6 6 SER A 108 SER A 123 1 16
HELIX 7 7 PRO A 127 LEU A 139 1 13
HELIX 8 8 ASN A 144 LEU A 161 1 18
HELIX 9 9 SER A 165 ASP A 183 1 19
HELIX 10 10 ASN A 186 VAL A 198 1 13
HELIX 11 11 SER A 206 ILE A 224 1 19
HELIX 12 12 ASN A 227 PHE A 241 1 15
HELIX 13 13 LEU A 245 PRO A 247 5 3
HELIX 14 14 ILE A 248 LEU A 253 1 6
HELIX 15 15 PRO A 254 THR A 256 5 3
HELIX 16 16 VAL A 287 GLN A 301 1 15
HELIX 17 17 ARG A 303 GLU A 317 1 15
HELIX 18 18 ASP A 319 MET A 321 5 3
HELIX 19 19 ARG A 322 ALA A 334 1 13
HELIX 20 20 SER B 8 LEU B 12 5 5
HELIX 21 21 SER B 24 THR B 44 1 21
HELIX 22 22 ARG B 62 GLN B 76 1 15
HELIX 23 23 PRO B 78 ASP B 85 5 8
HELIX 24 24 SER B 87 GLY B 103 1 17
HELIX 25 25 ASP B 107 HIS B 120 1 14
HELIX 26 26 HIS B 139 GLY B 154 1 16
HELIX 27 27 GLY B 161 ALA B 168 1 8
HELIX 28 28 ALA B 168 LYS B 180 1 13
HELIX 29 29 ASP B 195 ASP B 210 1 16
HELIX 30 30 THR B 213 HIS B 218 1 6
HELIX 31 31 ASN B 219 CYS B 227 1 9
HELIX 32 32 HIS B 266 SER B 282 1 17
HELIX 33 33 ASP B 293 GLN B 304 1 12
HELIX 34 34 GLU B 307 GLY B 311 5 5
HELIX 35 35 CYS B 325 VAL B 330 1 6
HELIX 36 36 GLY B 333 VAL B 349 1 17
HELIX 37 37 ASN B 376 ALA B 387 1 12
HELIX 38 38 ASP B 407 HIS B 423 1 17
HELIX 39 39 SER B 428 PHE B 439 1 12
HELIX 40 40 ASN B 459 LEU B 475 1 17
HELIX 41 41 GLY B 489 ARG B 493 5 5
HELIX 42 42 LEU B 504 TYR B 516 1 13
SHEET 1 A 2 SER B 238 PHE B 241 0
SHEET 2 A 2 CYS B 258 SER B 261 -1 O VAL B 260 N PHE B 239
SHEET 1 B 2 MET B 425 HIS B 427 0
SHEET 2 B 2 TRP B 477 GLU B 479 -1 O ILE B 478 N SER B 426
LINK OD2 ASP B 323 ZN ZN B 521 1555 1555 2.05
LINK OD1 ASP B 323 ZN ZN B 521 1555 1555 2.61
LINK SG CYS B 325 ZN ZN B 521 1555 1555 2.30
LINK NE2 HIS B 410 ZN ZN B 521 1555 1555 2.10
LINK ZN ZN B 521 N2 JAN B 526 1555 1555 2.18
CISPEP 1 LEU A 285 PRO A 286 0 -1.33
CISPEP 2 PHE B 288 PRO B 289 0 -1.93
SITE 1 AC1 4 ASP B 323 CYS B 325 HIS B 410 JAN B 526
SITE 1 AC2 10 TYR B 58 ASP B 100 GLY B 489 LYS B 490
SITE 2 AC2 10 ASP B 491 ARG B 493 ASN B 495 HOH B1774
SITE 3 AC2 10 HOH B1900 HOH B2460
SITE 1 AC3 10 ARG B 62 LYS B 63 GLN B 64 GLU B 65
SITE 2 AC3 10 PHE B 74 PHE B 75 HOH B1877 HOH B1972
SITE 3 AC3 10 HOH B1994 HOH B2102
SITE 1 AC4 7 SER B 123 PRO B 124 LYS B 125 ALA B 133
SITE 2 AC4 7 ASN B 134 SER B 135 GLN B 136
SITE 1 AC5 17 HOH A2096 TRP B 90 LEU B 141 ARG B 197
SITE 2 AC5 17 HIS B 266 GLY B 268 TYR B 269 CYS B 272
SITE 3 AC5 17 ARG B 317 LYS B 320 TYR B 326 TRP B 329
SITE 4 AC5 17 JAN B 526 HOH B2087 HOH B2092 HOH B2101
SITE 5 AC5 17 HOH B2547
SITE 1 AC6 14 LEU B 84 TRP B 94 ARG B 197 ASP B 323
SITE 2 AC6 14 CYS B 325 TYR B 326 ASP B 407 TYR B 409
SITE 3 AC6 14 HIS B 410 ZN B 521 FII B 525 HOH B2588
SITE 4 AC6 14 HOH B2773 HOH B2869
SITE 1 AC7 8 TYR A 74 ALA B 86 SER B 87 TRP B 90
SITE 2 AC7 8 HIS B 139 LEU B 141 PRO B 142 HOH B2111
CRYST1 142.176 142.176 130.096 90.00 90.00 90.00 P 43 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 0.007034 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007034 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007687 0.00000
(ATOM LINES ARE NOT SHOWN.)
END