HEADER TRANSFERASE 24-OCT-05 2BED
TITLE STRUCTURE OF FPT BOUND TO INHIBITOR SCH207736
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN FARNESYLTRANSFERASE/GERANYLGERANYLTRANSFERASE TYPE
COMPND 3 I ALPHA SUBUNIT;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: CAAX FARNESYLTRANSFERASE ALPHA SUBUNIT, RAS PROTEINS
COMPND 6 PRENYLTRANSFERASE ALPHA, FTASE-ALPHA, TYPE I PROTEIN GERANYL-
COMPND 7 GERANYLTRANSFERASE ALPHA SUBUNIT, GGTASE-I-ALPHA;
COMPND 8 EC: 2.5.1.58, 2.5.1.59;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: PROTEIN FARNESYLTRANSFERASE BETA SUBUNIT;
COMPND 12 CHAIN: B;
COMPND 13 SYNONYM: CAAX FARNESYLTRANSFERASE BETA SUBUNIT, RAS PROTEINS
COMPND 14 PRENYLTRANSFERASE BETA, FTASE-BETA;
COMPND 15 EC: 2.5.1.58;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: FNTA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 10 ORGANISM_COMMON: NORWAY RAT;
SOURCE 11 ORGANISM_TAXID: 10116;
SOURCE 12 GENE: FNTB;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FPT, PTASE, FARNESYL, DRUG DESIGN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.STRICKLAND
REVDAT 5 14-FEB-24 2BED 1 REMARK LINK
REVDAT 4 24-JAN-18 2BED 1 AUTHOR
REVDAT 3 18-OCT-17 2BED 1 REMARK
REVDAT 2 24-FEB-09 2BED 1 VERSN
REVDAT 1 08-AUG-06 2BED 0
JRNL AUTH F.G.NJOROGE,B.VIBULBHAN,P.PINTO,C.STRICKLAND,W.R.BISHOP,
JRNL AUTH 2 A.NOMEIR,V.GIRIJAVALLABHAN
JRNL TITL ENHANCED FTASE ACTIVITY ACHIEVED VIA PIPERAZINE INTERACTION
JRNL TITL 2 WITH CATALYTIC ZINC.
JRNL REF BIOORG.MED.CHEM.LETT. V. 16 984 2006
JRNL REFN ISSN 0960-894X
JRNL PMID 16298128
JRNL DOI 10.1016/J.BMCL.2005.10.090
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 32803
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1662
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5819
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 57
REMARK 3 SOLVENT ATOMS : 388
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.08200
REMARK 3 B22 (A**2) : -1.08200
REMARK 3 B33 (A**2) : 2.16300
REMARK 3 B12 (A**2) : -3.17500
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : PAR207736.PRO
REMARK 3 PARAMETER FILE 2 : PARAFPP.PRO
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOP207736.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPFPP.PRO
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2BED COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034995.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32808
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
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 (%) : 98.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06600
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) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.48700
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 23.24333
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 46.48667
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 34.86500
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 58.10833
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 11.62167
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: FPT IS A DIMER OF THE ALPHA AND BETA SUBUNITS. THERE IS 1
REMARK 300 ALPHA AND 1 BETA IN THE ASYMMETRIC UNIT AND TOGETHER THESE FORM THE
REMARK 300 BIOLOGICAL 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: 8480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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 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 PRO A 163 C - N - CA ANGL. DEV. = 12.9 DEGREES
REMARK 500 LEU B 308 CA - CB - CG ANGL. DEV. = -15.9 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 SER A 85 65.96 -119.05
REMARK 500 VAL A 88 39.30 36.13
REMARK 500 ASN A 127 72.33 -157.30
REMARK 500 ALA A 128 -12.09 -47.36
REMARK 500 GLN A 145 65.49 36.99
REMARK 500 GLN A 162 76.90 -172.18
REMARK 500 LYS A 164 62.44 -108.56
REMARK 500 LEU A 215 67.37 -112.98
REMARK 500 ASP A 217 -37.03 -19.47
REMARK 500 ASP A 230 87.18 -173.52
REMARK 500 THR A 247 -80.55 -96.11
REMARK 500 ASP A 252 109.45 -52.01
REMARK 500 PRO A 271 -39.70 -34.46
REMARK 500 ARG A 287 -22.42 150.89
REMARK 500 ASN A 325 43.82 -109.14
REMARK 500 GLN A 326 61.66 39.05
REMARK 500 ASN A 329 42.04 96.11
REMARK 500 ASP A 332 -72.49 -51.66
REMARK 500 GLU A 347 -71.82 -123.11
REMARK 500 LEU A 363 2.50 -64.90
REMARK 500 PRO B 28 -71.69 -33.50
REMARK 500 GLU B 33 40.74 -91.27
REMARK 500 LYS B 63 40.13 -75.19
REMARK 500 ASN B 65 33.87 15.12
REMARK 500 HIS B 66 -119.26 -121.42
REMARK 500 GLN B 74 55.12 -63.21
REMARK 500 ASP B 91 0.39 -64.02
REMARK 500 PRO B 119 130.03 -26.44
REMARK 500 VAL B 201 -19.81 -46.55
REMARK 500 ASN B 234 -161.82 -113.11
REMARK 500 LYS B 264 31.51 -141.71
REMARK 500 ASP B 297 124.34 -172.79
REMARK 500 SER B 326 -28.25 -156.71
REMARK 500 CYS B 343 45.23 -109.80
REMARK 500 ASP B 352 -79.11 -48.79
REMARK 500 SER B 378 68.88 158.35
REMARK 500 PRO B 399 8.42 -63.49
REMARK 500 PRO B 421 84.88 -41.16
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 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 297 OD2
REMARK 620 2 ASP B 297 OD1 53.1
REMARK 620 3 CYS B 299 SG 104.5 68.9
REMARK 620 4 HIS B 362 NE2 109.9 93.5 118.1
REMARK 620 N 1 2 3
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPP B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 736 B 2001
DBREF 2BED A 54 366 UNP Q04631 PFTA_RAT 54 366
DBREF 2BED B 23 423 UNP Q02293 PFTB_RAT 23 423
SEQRES 1 A 313 GLY PHE LEU SER LEU ASP SER PRO THR TYR VAL LEU TYR
SEQRES 2 A 313 ARG ASP ARG ALA GLU TRP ALA ASP ILE ASP PRO VAL PRO
SEQRES 3 A 313 GLN ASN ASP GLY PRO SER PRO VAL VAL GLN ILE ILE TYR
SEQRES 4 A 313 SER GLU LYS PHE ARG ASP VAL TYR ASP TYR PHE ARG ALA
SEQRES 5 A 313 VAL LEU GLN ARG ASP GLU ARG SER GLU ARG ALA PHE LYS
SEQRES 6 A 313 LEU THR ARG ASP ALA ILE GLU LEU ASN ALA ALA ASN TYR
SEQRES 7 A 313 THR VAL TRP HIS PHE ARG ARG VAL LEU LEU ARG SER LEU
SEQRES 8 A 313 GLN LYS ASP LEU GLN GLU GLU MET ASN TYR ILE THR ALA
SEQRES 9 A 313 ILE ILE GLU GLU GLN PRO LYS ASN TYR GLN VAL TRP HIS
SEQRES 10 A 313 HIS ARG ARG VAL LEU VAL GLU TRP LEU LYS ASP PRO SER
SEQRES 11 A 313 GLN GLU LEU GLU PHE ILE ALA ASP ILE LEU ASN GLN ASP
SEQRES 12 A 313 ALA LYS ASN TYR HIS ALA TRP GLN HIS ARG GLN TRP VAL
SEQRES 13 A 313 ILE GLN GLU PHE ARG LEU TRP ASP ASN GLU LEU GLN TYR
SEQRES 14 A 313 VAL ASP GLN LEU LEU LYS GLU ASP VAL ARG ASN ASN SER
SEQRES 15 A 313 VAL TRP ASN GLN ARG HIS PHE VAL ILE SER ASN THR THR
SEQRES 16 A 313 GLY TYR SER ASP ARG ALA VAL LEU GLU ARG GLU VAL GLN
SEQRES 17 A 313 TYR THR LEU GLU MET ILE LYS LEU VAL PRO HIS ASN GLU
SEQRES 18 A 313 SER ALA TRP ASN TYR LEU LYS GLY ILE LEU GLN ASP ARG
SEQRES 19 A 313 GLY LEU SER ARG TYR PRO ASN LEU LEU ASN GLN LEU LEU
SEQRES 20 A 313 ASP LEU GLN PRO SER HIS SER SER PRO TYR LEU ILE ALA
SEQRES 21 A 313 PHE LEU VAL ASP ILE TYR GLU ASP MET LEU GLU ASN GLN
SEQRES 22 A 313 CYS ASP ASN LYS GLU ASP ILE LEU ASN LYS ALA LEU GLU
SEQRES 23 A 313 LEU CYS GLU ILE LEU ALA LYS GLU LYS ASP THR ILE ARG
SEQRES 24 A 313 LYS GLU TYR TRP ARG TYR ILE GLY ARG SER LEU GLN SER
SEQRES 25 A 313 LYS
SEQRES 1 B 401 LEU TYR SER LEU ARG PRO GLU HIS ALA ARG GLU ARG LEU
SEQRES 2 B 401 GLN ASP ASP SER VAL GLU THR VAL THR SER ILE GLU GLN
SEQRES 3 B 401 ALA LYS VAL GLU GLU LYS ILE GLN GLU VAL PHE SER SER
SEQRES 4 B 401 TYR LYS PHE ASN HIS LEU VAL PRO ARG LEU VAL LEU GLN
SEQRES 5 B 401 ARG GLU LYS HIS PHE HIS TYR LEU LYS ARG GLY LEU ARG
SEQRES 6 B 401 GLN LEU THR ASP ALA TYR GLU CYS LEU ASP ALA SER ARG
SEQRES 7 B 401 PRO TRP LEU CYS TYR TRP ILE LEU HIS SER LEU GLU LEU
SEQRES 8 B 401 LEU ASP GLU PRO ILE PRO GLN ILE VAL ALA THR ASP VAL
SEQRES 9 B 401 CYS GLN PHE LEU GLU LEU CYS GLN SER PRO ASP GLY GLY
SEQRES 10 B 401 PHE GLY GLY GLY PRO GLY GLN TYR PRO HIS LEU ALA PRO
SEQRES 11 B 401 THR TYR ALA ALA VAL ASN ALA LEU CYS ILE ILE GLY THR
SEQRES 12 B 401 GLU GLU ALA TYR ASN VAL ILE ASN ARG GLU LYS LEU LEU
SEQRES 13 B 401 GLN TYR LEU TYR SER LEU LYS GLN PRO ASP GLY SER PHE
SEQRES 14 B 401 LEU MET HIS VAL GLY GLY GLU VAL ASP VAL ARG SER ALA
SEQRES 15 B 401 TYR CYS ALA ALA SER VAL ALA SER LEU THR ASN ILE ILE
SEQRES 16 B 401 THR PRO ASP LEU PHE GLU GLY THR ALA GLU TRP ILE ALA
SEQRES 17 B 401 ARG CYS GLN ASN TRP GLU GLY GLY ILE GLY GLY VAL PRO
SEQRES 18 B 401 GLY MET GLU ALA HIS GLY GLY TYR THR PHE CYS GLY LEU
SEQRES 19 B 401 ALA ALA LEU VAL ILE LEU LYS LYS GLU ARG SER LEU ASN
SEQRES 20 B 401 LEU LYS SER LEU LEU GLN TRP VAL THR SER ARG GLN MET
SEQRES 21 B 401 ARG PHE GLU GLY GLY PHE GLN GLY ARG CYS ASN LYS LEU
SEQRES 22 B 401 VAL ASP GLY CYS TYR SER PHE TRP GLN ALA GLY LEU LEU
SEQRES 23 B 401 PRO LEU LEU HIS ARG ALA LEU HIS ALA GLN GLY ASP PRO
SEQRES 24 B 401 ALA LEU SER MET SER HIS TRP MET PHE HIS GLN GLN ALA
SEQRES 25 B 401 LEU GLN GLU TYR ILE LEU MET CYS CYS GLN CYS PRO ALA
SEQRES 26 B 401 GLY GLY LEU LEU ASP LYS PRO GLY LYS SER ARG ASP PHE
SEQRES 27 B 401 TYR HIS THR CYS TYR CYS LEU SER GLY LEU SER ILE ALA
SEQRES 28 B 401 GLN HIS PHE GLY SER GLY ALA MET LEU HIS ASP VAL VAL
SEQRES 29 B 401 MET GLY VAL PRO GLU ASN VAL LEU GLN PRO THR HIS PRO
SEQRES 30 B 401 VAL TYR ASN ILE GLY PRO ASP LYS VAL ILE GLN ALA THR
SEQRES 31 B 401 THR HIS PHE LEU GLN LYS PRO VAL PRO GLY PHE
HET ZN B 1 1
HET FPP B1001 24
HET 736 B2001 32
HETNAM ZN ZINC ION
HETNAM FPP FARNESYL DIPHOSPHATE
HETNAM 736 (11S)-8-CHLORO-11-[1-(METHYLSULFONYL)PIPERIDIN-4-YL]-6-
HETNAM 2 736 PIPERAZIN-1-YL-11H-BENZO[5,6]CYCLOHEPTA[1,2-B]PYRIDINE
FORMUL 3 ZN ZN 2+
FORMUL 4 FPP C15 H28 O7 P2
FORMUL 5 736 C24 H29 CL N4 O2 S
FORMUL 6 HOH *388(H2 O)
HELIX 1 1 LEU A 65 ALA A 73 5 9
HELIX 2 2 SER A 93 ARG A 109 1 17
HELIX 3 3 SER A 113 ASN A 127 1 15
HELIX 4 4 ASN A 130 LEU A 144 1 15
HELIX 5 5 ASP A 147 GLN A 162 1 16
HELIX 6 6 ASN A 165 LYS A 180 1 16
HELIX 7 7 GLN A 184 ASP A 196 1 13
HELIX 8 8 ASN A 199 PHE A 213 1 15
HELIX 9 9 ASN A 218 ASP A 230 1 13
HELIX 10 10 ASN A 233 THR A 247 1 15
HELIX 11 11 ASP A 252 VAL A 270 1 19
HELIX 12 12 ASN A 273 GLN A 285 1 13
HELIX 13 13 GLY A 288 ARG A 291 5 4
HELIX 14 14 TYR A 292 HIS A 306 1 15
HELIX 15 15 SER A 308 ASN A 325 1 18
HELIX 16 16 ASN A 329 GLU A 347 1 19
HELIX 17 17 ASP A 349 ILE A 351 5 3
HELIX 18 18 ARG A 352 LEU A 363 1 12
HELIX 19 19 ARG B 27 GLU B 33 5 7
HELIX 20 20 THR B 42 SER B 60 1 19
HELIX 21 21 GLN B 74 LEU B 86 1 13
HELIX 22 22 THR B 90 ASP B 97 5 8
HELIX 23 23 SER B 99 LEU B 114 1 16
HELIX 24 24 PRO B 119 GLN B 134 1 16
HELIX 25 25 HIS B 149 GLY B 164 1 16
HELIX 26 26 THR B 165 ILE B 172 1 8
HELIX 27 27 ASN B 173 LYS B 185 1 13
HELIX 28 28 ASP B 200 THR B 214 1 15
HELIX 29 29 GLY B 224 ARG B 231 1 8
HELIX 30 30 HIS B 248 LYS B 263 1 16
HELIX 31 31 LYS B 264 LEU B 268 5 5
HELIX 32 32 ASN B 269 ARG B 280 1 12
HELIX 33 33 CYS B 299 GLN B 304 1 6
HELIX 34 34 GLY B 306 ALA B 317 1 12
HELIX 35 35 HIS B 331 CYS B 343 1 13
HELIX 36 36 ASP B 359 GLN B 374 1 16
HELIX 37 37 VAL B 389 VAL B 393 5 5
HELIX 38 38 GLY B 404 LEU B 416 1 13
SHEET 1 A 2 GLN A 89 ILE A 90 0
SHEET 2 A 2 GLN B 88 LEU B 89 1 O LEU B 89 N 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 ZN ZN B 1 OD2 ASP B 297 1555 1555 2.43
LINK ZN ZN B 1 OD1 ASP B 297 1555 1555 2.49
LINK ZN ZN B 1 SG CYS B 299 1555 1555 2.68
LINK ZN ZN B 1 NE2 HIS B 362 1555 1555 2.71
SITE 1 AC1 4 ASP B 297 CYS B 299 HIS B 362 736 B2001
SITE 1 AC2 12 LYS A 164 TYR A 166 TYR B 205 HIS B 248
SITE 2 AC2 12 GLY B 250 TYR B 251 CYS B 254 ARG B 291
SITE 3 AC2 12 LYS B 294 TYR B 300 TRP B 303 736 B2001
SITE 1 AC3 12 LYS A 164 TYR A 166 HIS A 201 ZN B 1
SITE 2 AC3 12 CYS B 95 LEU B 96 TRP B 102 TRP B 106
SITE 3 AC3 12 TYR B 300 ASP B 359 TYR B 361 FPP B1001
CRYST1 174.020 174.020 69.730 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 0.005746 0.003318 0.000000 0.00000
SCALE2 0.000000 0.006635 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014341 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
