HEADER TRANSFERASE 11-JUN-01 1JCQ
TITLE CRYSTAL STRUCTURE OF HUMAN PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH
TITLE 2 FARNESYL DIPHOSPHATE AND THE PEPTIDOMIMETIC INHIBITOR L-739,750
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN FARNESYLTRANSFERASE, ALPHA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ALPHA SUBUNIT;
COMPND 5 SYNONYM: CAAX FARNESYLTRANSFERASE ALPHA SUBUNIT; RAS PROTEINS
COMPND 6 PRENYLTRANSFERASE ALPHA; FTASE-ALPHA; PRENYL-PROTEIN TRANSFERASE RAM2
COMPND 7 HOMOLOG;
COMPND 8 EC: 2.5.1.-;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: PROTEIN FARNESYLTRANSFERASE, BETA SUBUNIT;
COMPND 13 CHAIN: B;
COMPND 14 FRAGMENT: BETA SUBUNIT;
COMPND 15 SYNONYM: CAAX FARNESYLTRANSFERASE BETA SUBUNIT; RAS PROTEINS
COMPND 16 PRENYLTRANSFERASE BETA; FTASE-BETA; PRENYL-PROTEIN TRANSFERASE
COMPND 17 DPR1/RAM1 SUBUNIT;
COMPND 18 EC: 2.5.1.-;
COMPND 19 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FTASE, PFT, PFTASE, FT, FPT, FARNESYLTRANSFERASE, FARNESYL
KEYWDS 2 TRANSFERASE, FARNESYL PROTEIN TRANSFERASE, CAAX, RAS, CANCER, TUMOR
KEYWDS 3 REGRESSION, L-739, 750, PEPTIDOMIMETIC, INHIBITOR, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.B.LONG,P.J.CASEY,L.S.BEESE
REVDAT 4 16-AUG-23 1JCQ 1 HETSYN
REVDAT 3 29-JUL-20 1JCQ 1 COMPND REMARK SEQADV HET
REVDAT 3 2 1 HETNAM FORMUL LINK SITE
REVDAT 3 3 1 ATOM
REVDAT 2 24-FEB-09 1JCQ 1 VERSN
REVDAT 1 02-NOV-01 1JCQ 0
JRNL AUTH S.B.LONG,P.J.HANCOCK,A.M.KRAL,H.W.HELLINGA,L.S.BEESE
JRNL TITL THE CRYSTAL STRUCTURE OF HUMAN PROTEIN FARNESYLTRANSFERASE
JRNL TITL 2 REVEALS THE BASIS FOR INHIBITION BY CAAX TETRAPEPTIDES AND
JRNL TITL 3 THEIR MIMETICS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 98 12948 2001
JRNL REFN ISSN 0027-8424
JRNL PMID 11687658
JRNL DOI 10.1073/PNAS.241407898
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.B.LONG,P.J.CASEY,L.S.BEESE
REMARK 1 TITL THE BASIS FOR K-RAS4B BINDING SPECIFICITY TO PROTEIN
REMARK 1 TITL 2 FARNESYLTRANSFERASE REVEALED BY 2A RESOLUTION TERNARY
REMARK 1 TITL 3 COMPLEX STRUCTURES
REMARK 1 REF STRUCTURE V. 8 209 2000
REMARK 1 REFN ISSN 0969-2126
REMARK 1 DOI 10.1016/S0969-2126(00)00096-4
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.-W.PARK,S.R.BODULURI,J.F.MOOMAW,P.J.CASEY,L.S.BEESE
REMARK 1 TITL CRYSTAL STRUCTURE OF PROTEIN FARNESYLTRANSFERASE AT 2.25A
REMARK 1 TITL 2 RESOLUTION
REMARK 1 REF SCIENCE V. 275 1800 1997
REMARK 1 REFN ISSN 0036-8075
REMARK 1 DOI 10.1126/SCIENCE.275.5307.1800
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.0
REMARK 3 NUMBER OF REFLECTIONS : 46863
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 SET) : 0.179
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2341
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4305
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 238
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5898
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 334
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.29
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.24
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.300
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.210 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.080 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.030 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.240 ; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PR
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : ACE
REMARK 3 PARAMETER FILE 4 : FPP
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PR
REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 3 : ACE
REMARK 3 TOPOLOGY FILE 4 : FPP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1JCQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013630.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.7
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46302
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.5
REMARK 200 DATA REDUNDANCY : 5.590
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.95
REMARK 200 R MERGE FOR SHELL (I) : 0.19300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.130
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1D8D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, AMMONIUM ACETATE, DTT, TRIS
REMARK 280 -HCL, PH 5.7, VAPOR DIFFUSION, HANGING DROP AT 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 21.61400
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 43.22800
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 32.42100
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 54.03500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 10.80700
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 300 REMARK: THE BIOLOGICAL UNIT OF PROTEIN FARNESYLTRANSFERASE (FTASE)
REMARK 300 IS A HETERODIMER OF ALPHA AND BETA SUBUNITS. THERE IS ONE FTASE
REMARK 300 HETERODIMER PER ASYMMETRIC UNIT.
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: 9610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 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 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 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 THR A 4
REMARK 465 GLU A 5
REMARK 465 GLY A 6
REMARK 465 VAL A 7
REMARK 465 GLY A 8
REMARK 465 GLU A 9
REMARK 465 ALA A 10
REMARK 465 ALA A 11
REMARK 465 GLN A 12
REMARK 465 GLY A 13
REMARK 465 GLY A 14
REMARK 465 GLU A 15
REMARK 465 PRO A 16
REMARK 465 GLY A 17
REMARK 465 GLN A 18
REMARK 465 PRO A 19
REMARK 465 ALA A 20
REMARK 465 GLN A 21
REMARK 465 PRO A 22
REMARK 465 PRO A 23
REMARK 465 PRO A 24
REMARK 465 GLN A 25
REMARK 465 PRO A 26
REMARK 465 HIS A 27
REMARK 465 PRO A 28
REMARK 465 PRO A 29
REMARK 465 PRO A 30
REMARK 465 PRO A 31
REMARK 465 GLN A 32
REMARK 465 GLN A 33
REMARK 465 GLN A 34
REMARK 465 HIS A 35
REMARK 465 LYS A 36
REMARK 465 GLU A 37
REMARK 465 GLU A 38
REMARK 465 MET A 39
REMARK 465 ALA A 40
REMARK 465 ALA A 41
REMARK 465 GLU A 42
REMARK 465 ALA A 43
REMARK 465 GLY A 44
REMARK 465 GLU A 45
REMARK 465 ALA A 46
REMARK 465 VAL A 47
REMARK 465 ALA A 48
REMARK 465 SER A 49
REMARK 465 PRO A 50
REMARK 465 MET A 51
REMARK 465 ASP A 52
REMARK 465 ASP A 53
REMARK 465 GLY A 54
REMARK 465 SER A 368
REMARK 465 THR A 369
REMARK 465 GLU A 370
REMARK 465 ASN A 371
REMARK 465 ASP A 372
REMARK 465 SER A 373
REMARK 465 PRO A 374
REMARK 465 THR A 375
REMARK 465 ASN A 376
REMARK 465 VAL A 377
REMARK 465 GLN A 378
REMARK 465 GLN A 379
REMARK 465 GLU A 380
REMARK 465 GLU A 381
REMARK 465 PHE A 382
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 PRO B 4
REMARK 465 SER B 5
REMARK 465 SER B 6
REMARK 465 PHE B 7
REMARK 465 THR B 8
REMARK 465 TYR B 9
REMARK 465 TYR B 10
REMARK 465 CYS B 11
REMARK 465 PRO B 12
REMARK 465 PRO B 13
REMARK 465 SER B 14
REMARK 465 GLU B 425
REMARK 465 LEU B 426
REMARK 465 LYS B 427
REMARK 465 ASP B 428
REMARK 465 GLU B 429
REMARK 465 THR B 430
REMARK 465 SER B 431
REMARK 465 ALA B 432
REMARK 465 GLU B 433
REMARK 465 PRO B 434
REMARK 465 ALA B 435
REMARK 465 THR B 436
REMARK 465 ASP B 437
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 B 308 CA - CB - CG ANGL. DEV. = -14.4 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 GLU A 71 0.09 -64.05
REMARK 500 VAL A 88 36.61 38.40
REMARK 500 LYS A 164 71.19 -102.32
REMARK 500 ALA A 197 -1.71 -58.77
REMARK 500 THR A 247 -89.88 -114.77
REMARK 500 HIS A 306 11.50 -147.81
REMARK 500 ASN A 325 43.55 -109.26
REMARK 500 GLU A 347 -61.81 -124.09
REMARK 500 ASP A 349 47.88 -157.96
REMARK 500 ASN B 65 -124.98 59.39
REMARK 500 GLN B 74 60.04 -64.45
REMARK 500 GLN B 318 31.20 -87.33
REMARK 500 SER B 326 -5.57 -149.89
REMARK 500 HIS B 383 113.80 -163.75
REMARK 500 PRO B 421 113.41 -36.90
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 B1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 297 OD1
REMARK 620 2 ASP B 297 OD2 53.3
REMARK 620 3 CYS B 299 SG 92.0 104.0
REMARK 620 4 HIS B 362 NE2 79.8 115.8 120.5
REMARK 620 5 739 B3012 SCC 150.2 102.3 112.5 100.4
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JCR RELATED DB: PDB
REMARK 900 RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH THE NON-SUBSTRATE
REMARK 900 TETRAPEPTIDE INHIBITOR CVFM AND FARNESYL DIPHOSPHATE SUBSTRATE
REMARK 900 RELATED ID: 1JCS RELATED DB: PDB
REMARK 900 RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH THE PEPTIDE
REMARK 900 SUBSTRATE TKCVFM AND AN ANALOG OF FARNESYL DIPHOSPHATE
REMARK 900 RELATED ID: 1D8D RELATED DB: PDB
REMARK 900 PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A K-RAS4B PEPTIDE
REMARK 900 SUBSTRATE AND FARNESYL DIPHOSPHATE ANALOG
REMARK 900 RELATED ID: 1FT1 RELATED DB: PDB
REMARK 900 UNLIGANDED PROTEIN FARENESYLTRANSFERASE
DBREF 1JCQ A 1 379 UNP P49354 PFTA_HUMAN 1 379
DBREF 1JCQ B 1 437 UNP P49356 PFTB_HUMAN 1 437
SEQADV 1JCQ GLU A 380 UNP P49354 INSERTION
SEQADV 1JCQ GLU A 381 UNP P49354 INSERTION
SEQADV 1JCQ PHE A 382 UNP P49354 INSERTION
SEQRES 1 A 382 MET ALA ALA THR GLU GLY VAL GLY GLU ALA ALA GLN GLY
SEQRES 2 A 382 GLY GLU PRO GLY GLN PRO ALA GLN PRO PRO PRO GLN PRO
SEQRES 3 A 382 HIS PRO PRO PRO PRO GLN GLN GLN HIS LYS GLU GLU MET
SEQRES 4 A 382 ALA ALA GLU ALA GLY GLU ALA VAL ALA SER PRO MET ASP
SEQRES 5 A 382 ASP GLY PHE VAL SER LEU ASP SER PRO SER TYR VAL LEU
SEQRES 6 A 382 TYR ARG ASP ARG ALA GLU TRP ALA ASP ILE ASP PRO VAL
SEQRES 7 A 382 PRO GLN ASN ASP GLY PRO ASN PRO VAL VAL GLN ILE ILE
SEQRES 8 A 382 TYR SER ASP LYS PHE ARG ASP VAL TYR ASP TYR PHE ARG
SEQRES 9 A 382 ALA VAL LEU GLN ARG ASP GLU ARG SER GLU ARG ALA PHE
SEQRES 10 A 382 LYS LEU THR ARG ASP ALA ILE GLU LEU ASN ALA ALA ASN
SEQRES 11 A 382 TYR THR VAL TRP HIS PHE ARG ARG VAL LEU LEU LYS SER
SEQRES 12 A 382 LEU GLN LYS ASP LEU HIS GLU GLU MET ASN TYR ILE THR
SEQRES 13 A 382 ALA ILE ILE GLU GLU GLN PRO LYS ASN TYR GLN VAL TRP
SEQRES 14 A 382 HIS HIS ARG ARG VAL LEU VAL GLU TRP LEU ARG ASP PRO
SEQRES 15 A 382 SER GLN GLU LEU GLU PHE ILE ALA ASP ILE LEU ASN GLN
SEQRES 16 A 382 ASP ALA LYS ASN TYR HIS ALA TRP GLN HIS ARG GLN TRP
SEQRES 17 A 382 VAL ILE GLN GLU PHE LYS LEU TRP ASP ASN GLU LEU GLN
SEQRES 18 A 382 TYR VAL ASP GLN LEU LEU LYS GLU ASP VAL ARG ASN ASN
SEQRES 19 A 382 SER VAL TRP ASN GLN ARG TYR PHE VAL ILE SER ASN THR
SEQRES 20 A 382 THR GLY TYR ASN ASP ARG ALA VAL LEU GLU ARG GLU VAL
SEQRES 21 A 382 GLN TYR THR LEU GLU MET ILE LYS LEU VAL PRO HIS ASN
SEQRES 22 A 382 GLU SER ALA TRP ASN TYR LEU LYS GLY ILE LEU GLN ASP
SEQRES 23 A 382 ARG GLY LEU SER LYS TYR PRO ASN LEU LEU ASN GLN LEU
SEQRES 24 A 382 LEU ASP LEU GLN PRO SER HIS SER SER PRO TYR LEU ILE
SEQRES 25 A 382 ALA PHE LEU VAL ASP ILE TYR GLU ASP MET LEU GLU ASN
SEQRES 26 A 382 GLN CYS ASP ASN LYS GLU ASP ILE LEU ASN LYS ALA LEU
SEQRES 27 A 382 GLU LEU CYS GLU ILE LEU ALA LYS GLU LYS ASP THR ILE
SEQRES 28 A 382 ARG LYS GLU TYR TRP ARG TYR ILE GLY ARG SER LEU GLN
SEQRES 29 A 382 SER LYS HIS SER THR GLU ASN ASP SER PRO THR ASN VAL
SEQRES 30 A 382 GLN GLN GLU GLU PHE
SEQRES 1 B 437 MET ALA SER PRO SER SER PHE THR TYR TYR CYS PRO PRO
SEQRES 2 B 437 SER SER SER PRO VAL TRP SER GLU PRO LEU TYR SER LEU
SEQRES 3 B 437 ARG PRO GLU HIS ALA ARG GLU ARG LEU GLN ASP ASP SER
SEQRES 4 B 437 VAL GLU THR VAL THR SER ILE GLU GLN ALA LYS VAL GLU
SEQRES 5 B 437 GLU LYS ILE GLN GLU VAL PHE SER SER TYR LYS PHE ASN
SEQRES 6 B 437 HIS LEU VAL PRO ARG LEU VAL LEU GLN ARG GLU LYS HIS
SEQRES 7 B 437 PHE HIS TYR LEU LYS ARG GLY LEU ARG GLN LEU THR ASP
SEQRES 8 B 437 ALA TYR GLU CYS LEU ASP ALA SER ARG PRO TRP LEU CYS
SEQRES 9 B 437 TYR TRP ILE LEU HIS SER LEU GLU LEU LEU ASP GLU PRO
SEQRES 10 B 437 ILE PRO GLN ILE VAL ALA THR ASP VAL CYS GLN PHE LEU
SEQRES 11 B 437 GLU LEU CYS GLN SER PRO GLU GLY GLY PHE GLY GLY GLY
SEQRES 12 B 437 PRO GLY GLN TYR PRO HIS LEU ALA PRO THR TYR ALA ALA
SEQRES 13 B 437 VAL ASN ALA LEU CYS ILE ILE GLY THR GLU GLU ALA TYR
SEQRES 14 B 437 ASP ILE ILE ASN ARG GLU LYS LEU LEU GLN TYR LEU TYR
SEQRES 15 B 437 SER LEU LYS GLN PRO ASP GLY SER PHE LEU MET HIS VAL
SEQRES 16 B 437 GLY GLY GLU VAL ASP VAL ARG SER ALA TYR CYS ALA ALA
SEQRES 17 B 437 SER VAL ALA SER LEU THR ASN ILE ILE THR PRO ASP LEU
SEQRES 18 B 437 PHE GLU GLY THR ALA GLU TRP ILE ALA ARG CYS GLN ASN
SEQRES 19 B 437 TRP GLU GLY GLY ILE GLY GLY VAL PRO GLY MET GLU ALA
SEQRES 20 B 437 HIS GLY GLY TYR THR PHE CYS GLY LEU ALA ALA LEU VAL
SEQRES 21 B 437 ILE LEU LYS ARG GLU ARG SER LEU ASN LEU LYS SER LEU
SEQRES 22 B 437 LEU GLN TRP VAL THR SER ARG GLN MET ARG PHE GLU GLY
SEQRES 23 B 437 GLY PHE GLN GLY ARG CYS ASN LYS LEU VAL ASP GLY CYS
SEQRES 24 B 437 TYR SER PHE TRP GLN ALA GLY LEU LEU PRO LEU LEU HIS
SEQRES 25 B 437 ARG ALA LEU HIS ALA GLN GLY ASP PRO ALA LEU SER MET
SEQRES 26 B 437 SER HIS TRP MET PHE HIS GLN GLN ALA LEU GLN GLU TYR
SEQRES 27 B 437 ILE LEU MET CYS CYS GLN CYS PRO ALA GLY GLY LEU LEU
SEQRES 28 B 437 ASP LYS PRO GLY LYS SER ARG ASP PHE TYR HIS THR CYS
SEQRES 29 B 437 TYR CYS LEU SER GLY LEU SER ILE ALA GLN HIS PHE GLY
SEQRES 30 B 437 SER GLY ALA MET LEU HIS ASP VAL VAL LEU GLY VAL PRO
SEQRES 31 B 437 GLU ASN ALA LEU GLN PRO THR HIS PRO VAL TYR ASN ILE
SEQRES 32 B 437 GLY PRO ASP LYS VAL ILE GLN ALA THR THR TYR PHE LEU
SEQRES 33 B 437 GLN LYS PRO VAL PRO GLY PHE GLU GLU LEU LYS ASP GLU
SEQRES 34 B 437 THR SER ALA GLU PRO ALA THR ASP
HET GLC C 1 11
HET FRU C 2 12
HET ACY A3002 4
HET ZN B1001 1
HET FPP B3011 24
HET 739 B3012 34
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM FRU BETA-D-FRUCTOFURANOSE
HETNAM ACY ACETIC ACID
HETNAM ZN ZINC ION
HETNAM FPP FARNESYL DIPHOSPHATE
HETNAM 739 2(S)-{2(S)-[2(R)-AMINO-3-MERCAPTO]PROPYLAMINO-3(S)-
HETNAM 2 739 METHYL}PENTYLOXY-3-PHENYLPROPIONYLMETHIONINE SULFONE
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN FRU BETA-D-FRUCTOSE; D-FRUCTOSE; FRUCTOSE
HETSYN 739 L-739,750
FORMUL 3 GLC C6 H12 O6
FORMUL 3 FRU C6 H12 O6
FORMUL 4 ACY C2 H4 O2
FORMUL 5 ZN ZN 2+
FORMUL 6 FPP C15 H28 O7 P2
FORMUL 7 739 C23 H39 N3 O6 S2
FORMUL 8 HOH *334(H2 O)
HELIX 1 1 LEU A 65 ARG A 69 5 5
HELIX 2 2 ARG A 69 ALA A 73 5 5
HELIX 3 3 SER A 93 ASP A 110 1 18
HELIX 4 4 SER A 113 ASN A 127 1 15
HELIX 5 5 ASN A 130 LEU A 144 1 15
HELIX 6 6 ASP A 147 GLN A 162 1 16
HELIX 7 7 ASN A 165 ARG A 180 1 16
HELIX 8 8 GLN A 184 ASP A 196 1 13
HELIX 9 9 ASN A 199 PHE A 213 1 15
HELIX 10 10 ASN A 218 ASP A 230 1 13
HELIX 11 11 ASN A 233 THR A 247 1 15
HELIX 12 12 ASP A 252 VAL A 270 1 19
HELIX 13 13 ASN A 273 GLN A 285 1 13
HELIX 14 14 GLY A 288 LYS A 291 5 4
HELIX 15 15 TYR A 292 SER A 307 1 16
HELIX 16 16 SER A 308 ASN A 325 1 18
HELIX 17 17 ASN A 329 GLU A 347 1 19
HELIX 18 18 ASP A 349 ILE A 351 5 3
HELIX 19 19 ARG A 352 HIS A 367 1 16
HELIX 20 20 LEU B 23 ARG B 27 5 5
HELIX 21 21 ARG B 27 ARG B 34 5 8
HELIX 22 22 THR B 42 SER B 61 1 20
HELIX 23 23 GLN B 74 LEU B 86 1 13
HELIX 24 24 THR B 90 ASP B 97 5 8
HELIX 25 25 SER B 99 LEU B 114 1 16
HELIX 26 26 PRO B 119 GLN B 134 1 16
HELIX 27 27 HIS B 149 GLY B 164 1 16
HELIX 28 28 THR B 165 ILE B 172 1 8
HELIX 29 29 ASN B 173 LYS B 185 1 13
HELIX 30 30 ASP B 200 THR B 214 1 15
HELIX 31 31 GLY B 224 GLN B 233 1 10
HELIX 32 32 HIS B 248 LEU B 262 1 15
HELIX 33 33 ARG B 264 LEU B 268 5 5
HELIX 34 34 ASN B 269 ARG B 280 1 12
HELIX 35 35 CYS B 299 GLN B 304 1 6
HELIX 36 36 GLY B 306 GLN B 318 1 13
HELIX 37 37 HIS B 331 CYS B 343 1 13
HELIX 38 38 ASP B 359 GLN B 374 1 16
HELIX 39 39 VAL B 389 ALA B 393 5 5
HELIX 40 40 GLY B 404 GLN B 417 1 14
SHEET 1 A 2 GLN A 89 ILE A 90 0
SHEET 2 A 2 GLN B 88 LEU B 89 1 N LEU B 89 O GLN A 89
SHEET 1 B 2 HIS B 375 SER B 378 0
SHEET 2 B 2 MET B 381 ASP B 384 -1 O MET B 381 N SER B 378
LINK C1 GLC C 1 O2 FRU C 2 1555 1555 1.45
LINK OD1 ASP B 297 ZN ZN B1001 1555 1555 2.67
LINK OD2 ASP B 297 ZN ZN B1001 1555 1555 1.97
LINK SG CYS B 299 ZN ZN B1001 1555 1555 2.29
LINK NE2 HIS B 362 ZN ZN B1001 1555 1555 2.34
LINK ZN ZN B1001 SCC 739 B3012 1555 1555 2.36
CRYST1 178.476 178.476 64.842 90.00 90.00 120.00 P 61 6
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 0.005603 0.003235 0.000000 0.00000
SCALE2 0.000000 0.006470 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015422 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
