HEADER TRANSFERASE 30-AUG-07 2R42
TITLE THE BIOCHEMICAL AND STRUCTURAL BASIS FOR FEEDBACK INHIBITION OF
TITLE 2 MEVALONATE KINASE AND ISOPRENOID METABOLISM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MEVALONATE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MK;
COMPND 5 EC: 2.7.1.36;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 GENE: MVK;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-3D
KEYWDS MEVALONATE KINASE, FARNESYL THIODIPHOSPHATE, ATP-BINDING, CHOLESTEROL
KEYWDS 2 BIOSYNTHESIS, CYTOPLASM, LIPID SYNTHESIS, NUCLEOTIDE-BINDING,
KEYWDS 3 PEROXISOME, STEROID BIOSYNTHESIS, STEROL BIOSYNTHESIS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.FU,N.E.VOYNOVA,H.M.MIZIORKO,J.P.KIM
REVDAT 3 21-FEB-24 2R42 1 REMARK
REVDAT 2 24-FEB-09 2R42 1 VERSN
REVDAT 1 24-JUN-08 2R42 0
JRNL AUTH Z.FU,N.E.VOYNOVA,T.J.HERDENDORF,H.M.MIZIORKO,J.J.KIM
JRNL TITL BIOCHEMICAL AND STRUCTURAL BASIS FOR FEEDBACK INHIBITION OF
JRNL TITL 2 MEVALONATE KINASE AND ISOPRENOID METABOLISM.
JRNL REF BIOCHEMISTRY V. 47 3715 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18302342
JRNL DOI 10.1021/BI7024386
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1072536.650
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.4
REMARK 3 NUMBER OF REFLECTIONS : 13651
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) : 0.235
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1391
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 52.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 740
REMARK 3 BIN R VALUE (WORKING SET) : 0.3870
REMARK 3 BIN FREE R VALUE : 0.3790
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 11.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 91
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2804
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 73
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.59000
REMARK 3 B22 (A**2) : -2.83000
REMARK 3 B33 (A**2) : -6.76000
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) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.52
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) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.58
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.980
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) : 1.490 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.570 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.190 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.330 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.28
REMARK 3 BSOL : 45.81
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : FSP.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : FSP.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 2R42 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000044398.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
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 : GRAPHITE
REMARK 200 OPTICS : NULL
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 : 13785
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 28.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.4
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.32700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES BUFFER, PEG5000 MME, MGCL2, PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K, PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 38.99500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.21500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.99500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.21500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 3760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 77.99000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 LEU A 75
REMARK 465 GLU A 76
REMARK 465 GLN A 77
REMARK 465 GLY A 78
REMARK 465 ASP A 79
REMARK 465 VAL A 80
REMARK 465 PRO A 81
REMARK 465 ALA A 82
REMARK 465 PRO A 83
REMARK 465 THR A 84
REMARK 465 LEU A 85
REMARK 465 GLU A 86
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 87 CG CD OE1 NE2
REMARK 470 LEU A 88 CG CD1 CD2
REMARK 470 GLU A 89 CG CD OE1 OE2
REMARK 470 LYS A 90 CG CD CE NZ
REMARK 470 LEU A 91 CG CD1 CD2
REMARK 470 LYS A 92 CG CD CE NZ
REMARK 470 LYS A 93 CG CD CE NZ
REMARK 470 VAL A 94 CG1 CG2
REMARK 470 LEU A 97 CB CG CD1 CD2
REMARK 470 PRO A 98 CG CD
REMARK 470 ARG A 99 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 100 CG OD1 OD2
REMARK 470 CYS A 101 SG
REMARK 470 VAL A 102 CG1 CG2
REMARK 470 ASN A 104 CG OD1 ND2
REMARK 470 GLU A 105 CG CD OE1 OE2
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 A 115 CA - C - N ANGL. DEV. = -20.7 DEGREES
REMARK 500 LEU A 115 O - C - N ANGL. DEV. = 13.8 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 19 -76.35 -24.39
REMARK 500 HIS A 24 31.78 -97.86
REMARK 500 ASN A 34 41.62 -76.21
REMARK 500 ASN A 46 -163.05 -61.58
REMARK 500 ASN A 55 -75.37 -50.59
REMARK 500 VAL A 56 22.35 -66.94
REMARK 500 THR A 66 -70.30 -50.33
REMARK 500 LEU A 69 45.91 -83.78
REMARK 500 ASP A 71 57.43 -67.01
REMARK 500 LEU A 88 128.65 -172.28
REMARK 500 GLU A 89 92.92 -58.13
REMARK 500 ARG A 99 -145.40 -117.62
REMARK 500 ASP A 100 -31.85 -160.08
REMARK 500 PHE A 112 -70.71 -56.09
REMARK 500 LYS A 122 -4.70 -56.19
REMARK 500 LEU A 168 50.85 -101.44
REMARK 500 ARG A 171 18.10 57.10
REMARK 500 GLN A 217 -69.96 -131.75
REMARK 500 LYS A 238 10.72 54.58
REMARK 500 ALA A 284 -89.96 -76.91
REMARK 500 PRO A 286 73.71 -62.32
REMARK 500 LEU A 348 -152.73 -72.07
REMARK 500 GLU A 349 72.09 -169.00
REMARK 500 ARG A 350 -62.43 -4.48
REMARK 500 THR A 370 -156.46 -113.36
REMARK 500 PRO A 375 -84.49 -43.50
REMARK 500 ALA A 382 5.36 -53.47
REMARK 500 SER A 384 42.27 -107.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LEU A 115 -12.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 FPS A 400
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FPS A 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2R3V RELATED DB: PDB
REMARK 900 DIFFERENT SOURCE
DBREF 2R42 A 1 395 UNP P17256 KIME_RAT 1 395
SEQRES 1 A 395 MET LEU SER GLU VAL LEU LEU VAL SER ALA PRO GLY LYS
SEQRES 2 A 395 VAL ILE LEU HIS GLY GLU HIS ALA VAL VAL HIS GLY LYS
SEQRES 3 A 395 VAL ALA LEU ALA VAL ALA LEU ASN LEU ARG THR PHE LEU
SEQRES 4 A 395 VAL LEU ARG PRO GLN SER ASN GLY LYS VAL SER LEU ASN
SEQRES 5 A 395 LEU PRO ASN VAL GLY ILE LYS GLN VAL TRP ASP VAL ALA
SEQRES 6 A 395 THR LEU GLN LEU LEU ASP THR GLY PHE LEU GLU GLN GLY
SEQRES 7 A 395 ASP VAL PRO ALA PRO THR LEU GLU GLN LEU GLU LYS LEU
SEQRES 8 A 395 LYS LYS VAL ALA GLY LEU PRO ARG ASP CYS VAL GLY ASN
SEQRES 9 A 395 GLU GLY LEU SER LEU LEU ALA PHE LEU TYR LEU TYR LEU
SEQRES 10 A 395 ALA ILE CYS ARG LYS GLN ARG THR LEU PRO SER LEU ASP
SEQRES 11 A 395 ILE MET VAL TRP SER GLU LEU PRO PRO GLY ALA GLY LEU
SEQRES 12 A 395 GLY SER SER ALA ALA TYR SER VAL CYS VAL ALA ALA ALA
SEQRES 13 A 395 LEU LEU THR ALA CYS GLU GLU VAL THR ASN PRO LEU LYS
SEQRES 14 A 395 ASP ARG GLY SER ILE GLY SER TRP PRO GLU GLU ASP LEU
SEQRES 15 A 395 LYS SER ILE ASN LYS TRP ALA TYR GLU GLY GLU ARG VAL
SEQRES 16 A 395 ILE HIS GLY ASN PRO SER GLY VAL ASP ASN SER VAL SER
SEQRES 17 A 395 THR TRP GLY GLY ALA LEU ARG TYR GLN GLN GLY LYS MET
SEQRES 18 A 395 SER SER LEU LYS ARG LEU PRO ALA LEU GLN ILE LEU LEU
SEQRES 19 A 395 THR ASN THR LYS VAL PRO ARG SER THR LYS ALA LEU VAL
SEQRES 20 A 395 ALA GLY VAL ARG SER ARG LEU ILE LYS PHE PRO GLU ILE
SEQRES 21 A 395 MET ALA PRO LEU LEU THR SER ILE ASP ALA ILE SER LEU
SEQRES 22 A 395 GLU CYS GLU ARG VAL LEU GLY GLU MET ALA ALA ALA PRO
SEQRES 23 A 395 VAL PRO GLU GLN TYR LEU VAL LEU GLU GLU LEU MET ASP
SEQRES 24 A 395 MET ASN GLN HIS HIS LEU ASN ALA LEU GLY VAL GLY HIS
SEQRES 25 A 395 ALA SER LEU ASP GLN LEU CYS GLN VAL THR ALA ALA HIS
SEQRES 26 A 395 GLY LEU HIS SER LYS LEU THR GLY ALA GLY GLY GLY GLY
SEQRES 27 A 395 CYS GLY ILE THR LEU LEU LYS PRO GLY LEU GLU ARG ALA
SEQRES 28 A 395 LYS VAL GLU ALA ALA LYS GLN ALA LEU THR GLY CYS GLY
SEQRES 29 A 395 PHE ASP CYS TRP GLU THR SER ILE GLY ALA PRO GLY VAL
SEQRES 30 A 395 SER MET HIS SER ALA THR SER ILE GLU ASP PRO VAL ARG
SEQRES 31 A 395 GLN ALA LEU GLY LEU
HET MG A 500 1
HET FPS A 400 20
HETNAM MG MAGNESIUM ION
HETNAM FPS S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL]
HETNAM 2 FPS TRIHYDROGEN THIODIPHOSPHATE
HETSYN FPS FARNESYL THIOPYROPHOSPHATE
FORMUL 2 MG MG 2+
FORMUL 3 FPS C15 H28 O6 P2 S
FORMUL 4 HOH *73(H2 O)
HELIX 1 1 HIS A 20 GLY A 25 5 6
HELIX 2 2 VAL A 64 LEU A 69 1 6
HELIX 3 3 LYS A 90 LEU A 97 1 8
HELIX 4 4 GLU A 105 ARG A 121 1 17
HELIX 5 5 GLY A 144 CYS A 161 1 18
HELIX 6 6 ASN A 166 ARG A 171 5 6
HELIX 7 7 PRO A 178 GLY A 198 1 21
HELIX 8 8 GLY A 202 GLY A 211 1 10
HELIX 9 9 SER A 242 PHE A 257 1 16
HELIX 10 10 PHE A 257 ALA A 283 1 27
HELIX 11 11 VAL A 287 GLY A 309 1 23
HELIX 12 12 HIS A 312 HIS A 325 1 14
HELIX 13 13 ARG A 350 CYS A 363 1 14
HELIX 14 14 GLU A 386 GLY A 394 1 9
SHEET 1 A 7 ILE A 58 ASP A 63 0
SHEET 2 A 7 LYS A 48 LEU A 53 -1 N LEU A 53 O ILE A 58
SHEET 3 A 7 ASP A 130 SER A 135 1 O VAL A 133 N ASN A 52
SHEET 4 A 7 ALA A 28 LEU A 41 -1 N PHE A 38 O TRP A 134
SHEET 5 A 7 LEU A 6 HIS A 17 -1 N HIS A 17 O LEU A 29
SHEET 6 A 7 SER A 378 HIS A 380 -1 O HIS A 380 N LEU A 7
SHEET 7 A 7 ILE A 174 GLY A 175 -1 N GLY A 175 O MET A 379
SHEET 1 B 6 ILE A 58 ASP A 63 0
SHEET 2 B 6 LYS A 48 LEU A 53 -1 N LEU A 53 O ILE A 58
SHEET 3 B 6 ASP A 130 SER A 135 1 O VAL A 133 N ASN A 52
SHEET 4 B 6 ALA A 28 LEU A 41 -1 N PHE A 38 O TRP A 134
SHEET 5 B 6 ALA A 213 TYR A 216 -1 O LEU A 214 N ALA A 30
SHEET 6 B 6 MET A 221 SER A 223 -1 O SER A 222 N ARG A 215
SHEET 1 C 4 HIS A 328 LEU A 331 0
SHEET 2 C 4 CYS A 339 LEU A 344 -1 O ILE A 341 N LYS A 330
SHEET 3 C 4 LEU A 230 ASN A 236 -1 N GLN A 231 O LEU A 344
SHEET 4 C 4 ASP A 366 ILE A 372 -1 O TRP A 368 N LEU A 234
SITE 1 AC1 5 GLY A 144 SER A 146 ALA A 147 GLU A 193
SITE 2 AC1 5 ASP A 204
SITE 1 AC2 13 LEU A 53 ASN A 55 SER A 108 SER A 135
SITE 2 AC2 13 GLY A 140 GLY A 142 LEU A 143 GLY A 144
SITE 3 AC2 13 SER A 145 SER A 146 TYR A 149 HOH A 502
SITE 4 AC2 13 HOH A 539
CRYST1 77.990 118.430 42.860 90.00 90.00 90.00 P 21 21 2 4
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 0.012822 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008444 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023332 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
