HEADER TRANSFERASE 29-NOV-05 2F6X
TITLE CRYSTAL STRUCTURE OF (S)-3-O-GERANYLGERANYLGLYCERYL PHOSPHATE SYNTHASE
TITLE 2 COMPLEXED WITH SN-G1P AND MPD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: (S)-3-O-GERANYLGERANYLGLYCERYL PHOSPHATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: GGGPS;
COMPND 5 SYNONYM: GGGPS; PROTEIN PCRB HOMOLOG;
COMPND 6 EC: 2.5.1.42;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 2234;
SOURCE 4 GENE: PCRB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 10 OTHER_DETAILS: THREE AMINO ACIDS REMAIN AFTER REMOVAL OF THE HIS-
SOURCE 11 TAG, GSH
KEYWDS NON-CANONICAL TIM-BARREL; PRENYLTRANSFERASE; ARCHAEAL LIPID
KEYWDS 2 SYNTHESIS; SN-GLYCEROL-1-PHOSPHATE; 2-METHYL-2, 4-PENTANEDIOL;
KEYWDS 3 DIMER, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.PAYANDEH
REVDAT 6 03-APR-24 2F6X 1 REMARK
REVDAT 5 14-FEB-24 2F6X 1 REMARK SEQADV
REVDAT 4 18-OCT-17 2F6X 1 REMARK
REVDAT 3 24-FEB-09 2F6X 1 VERSN
REVDAT 2 28-MAR-06 2F6X 1 JRNL
REVDAT 1 24-JAN-06 2F6X 0
JRNL AUTH J.PAYANDEH,M.FUJIHASHI,W.GILLON,E.F.PAI
JRNL TITL THE CRYSTAL STRUCTURE OF (S)-3-O-GERANYLGERANYLGLYCERYL
JRNL TITL 2 PHOSPHATE SYNTHASE REVEALS AN ANCIENT FOLD FOR AN ANCIENT
JRNL TITL 3 ENZYME
JRNL REF J.BIOL.CHEM. V. 281 6070 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16377641
JRNL DOI 10.1074/JBC.M509377200
REMARK 2
REMARK 2 RESOLUTION. 2.00 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 : CNS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 35498
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1868
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 : 3689
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 222
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.89500
REMARK 3 B22 (A**2) : -0.89500
REMARK 3 B33 (A**2) : 1.79000
REMARK 3 B12 (A**2) : -2.37400
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.390
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) : 4.012 ; 3.218
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.968 ; 4.262
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.481 ; 5.018
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.132 ; 6.605
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 49.65
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : G1P.PAR
REMARK 3 PARAMETER FILE 4 : MPD.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2F6X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000035526.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR, BENT-FLAT SI-
REMARK 200 MIRROR (RH COATED)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37366
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04200
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) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.25800
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: CNS
REMARK 200 STARTING MODEL: DETERMINED FROM A SEMET MAD EXPERIMENT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNESIUM CHLORIDE, SODIUM
REMARK 280 CITRATE, SN-GLYCEROL-1-PHOSPHATE (ADDED DURING CRYOPROTECTION),
REMARK 280 2-METHYL-2,4-PENTANEDIOL (ADDED DURING CRYOPROTECTION), PH 6.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.94000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.67817
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 55.43333
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 47.94000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 27.67817
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 55.43333
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 47.94000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 27.67817
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 55.43333
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.35634
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 110.86667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 55.35634
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 110.86667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 55.35634
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 110.86667
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: 4560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 998
REMARK 465 SER A 999
REMARK 465 HIS A 1000
REMARK 465 GLY B 1998
REMARK 465 SER B 1999
REMARK 465 HIS B 2000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 218 O HOH A 222 1.95
REMARK 500 O HOH A 220 O HOH A 221 1.96
REMARK 500 O HOH A 216 O HOH A 217 2.02
REMARK 500 O ILE B 2114 O HOH B 3 2.19
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 ARG A1004 3.31 -69.95
REMARK 500 ASN A1041 -3.95 72.49
REMARK 500 ASN A1106 70.45 -150.91
REMARK 500 SER A1169 106.81 -10.93
REMARK 500 ASP A1186 -72.39 -140.13
REMARK 500 GLN B2040 13.60 -64.24
REMARK 500 VAL B2042 109.35 -46.83
REMARK 500 SER B2069 -162.08 173.81
REMARK 500 ASN B2070 25.12 -158.54
REMARK 500 SER B2169 108.03 2.89
REMARK 500 ASP B2186 -80.51 -111.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1GP A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1GP B 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 4001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 4002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VIZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PCRB, A BACTERIAL PROTEIN OF UNKNOWN FUNCTION
REMARK 900 RELATED ID: 2F6U RELATED DB: PDB
DBREF 2F6X A 1001 1231 UNP O29844 PCRB_ARCFU 1 231
DBREF 2F6X B 2001 2231 UNP O29844 PCRB_ARCFU 1 231
SEQADV 2F6X GLY A 998 UNP O29844 CLONING ARTIFACT
SEQADV 2F6X SER A 999 UNP O29844 CLONING ARTIFACT
SEQADV 2F6X HIS A 1000 UNP O29844 CLONING ARTIFACT
SEQADV 2F6X GLY B 1998 UNP O29844 CLONING ARTIFACT
SEQADV 2F6X SER B 1999 UNP O29844 CLONING ARTIFACT
SEQADV 2F6X HIS B 2000 UNP O29844 CLONING ARTIFACT
SEQRES 1 A 234 GLY SER HIS MET ARG TRP ARG LYS TRP ARG HIS ILE THR
SEQRES 2 A 234 LYS LEU ASP PRO ASP ARG THR ASN THR ASP GLU ILE ILE
SEQRES 3 A 234 LYS ALA VAL ALA ASP SER GLY THR ASP ALA VAL MET ILE
SEQRES 4 A 234 SER GLY THR GLN ASN VAL THR TYR GLU LYS ALA ARG THR
SEQRES 5 A 234 LEU ILE GLU LYS VAL SER GLN TYR GLY LEU PRO ILE VAL
SEQRES 6 A 234 VAL GLU PRO SER ASP PRO SER ASN VAL VAL TYR ASP VAL
SEQRES 7 A 234 ASP TYR LEU PHE VAL PRO THR VAL LEU ASN SER ALA ASP
SEQRES 8 A 234 GLY ASP TRP ILE THR GLY LYS HIS ALA GLN TRP VAL ARG
SEQRES 9 A 234 MET HIS TYR GLU ASN LEU GLN LYS PHE THR GLU ILE ILE
SEQRES 10 A 234 GLU SER GLU PHE ILE GLN ILE GLU GLY TYR ILE VAL LEU
SEQRES 11 A 234 ASN PRO ASP SER ALA VAL ALA ARG VAL THR LYS ALA LEU
SEQRES 12 A 234 CYS ASN ILE ASP LYS GLU LEU ALA ALA SER TYR ALA LEU
SEQRES 13 A 234 VAL GLY GLU LYS LEU PHE ASN LEU PRO ILE ILE TYR ILE
SEQRES 14 A 234 GLU TYR SER GLY THR TYR GLY ASN PRO GLU LEU VAL ALA
SEQRES 15 A 234 GLU VAL LYS LYS VAL LEU ASP LYS ALA ARG LEU PHE TYR
SEQRES 16 A 234 GLY GLY GLY ILE ASP SER ARG GLU LYS ALA ARG GLU MET
SEQRES 17 A 234 LEU ARG TYR ALA ASP THR ILE ILE VAL GLY ASN VAL ILE
SEQRES 18 A 234 TYR GLU LYS GLY ILE ASP ALA PHE LEU GLU THR LEU PRO
SEQRES 1 B 234 GLY SER HIS MET ARG TRP ARG LYS TRP ARG HIS ILE THR
SEQRES 2 B 234 LYS LEU ASP PRO ASP ARG THR ASN THR ASP GLU ILE ILE
SEQRES 3 B 234 LYS ALA VAL ALA ASP SER GLY THR ASP ALA VAL MET ILE
SEQRES 4 B 234 SER GLY THR GLN ASN VAL THR TYR GLU LYS ALA ARG THR
SEQRES 5 B 234 LEU ILE GLU LYS VAL SER GLN TYR GLY LEU PRO ILE VAL
SEQRES 6 B 234 VAL GLU PRO SER ASP PRO SER ASN VAL VAL TYR ASP VAL
SEQRES 7 B 234 ASP TYR LEU PHE VAL PRO THR VAL LEU ASN SER ALA ASP
SEQRES 8 B 234 GLY ASP TRP ILE THR GLY LYS HIS ALA GLN TRP VAL ARG
SEQRES 9 B 234 MET HIS TYR GLU ASN LEU GLN LYS PHE THR GLU ILE ILE
SEQRES 10 B 234 GLU SER GLU PHE ILE GLN ILE GLU GLY TYR ILE VAL LEU
SEQRES 11 B 234 ASN PRO ASP SER ALA VAL ALA ARG VAL THR LYS ALA LEU
SEQRES 12 B 234 CYS ASN ILE ASP LYS GLU LEU ALA ALA SER TYR ALA LEU
SEQRES 13 B 234 VAL GLY GLU LYS LEU PHE ASN LEU PRO ILE ILE TYR ILE
SEQRES 14 B 234 GLU TYR SER GLY THR TYR GLY ASN PRO GLU LEU VAL ALA
SEQRES 15 B 234 GLU VAL LYS LYS VAL LEU ASP LYS ALA ARG LEU PHE TYR
SEQRES 16 B 234 GLY GLY GLY ILE ASP SER ARG GLU LYS ALA ARG GLU MET
SEQRES 17 B 234 LEU ARG TYR ALA ASP THR ILE ILE VAL GLY ASN VAL ILE
SEQRES 18 B 234 TYR GLU LYS GLY ILE ASP ALA PHE LEU GLU THR LEU PRO
HET 1GP A3001 10
HET MPD A4001 8
HET 1GP B3002 10
HET MPD B4002 8
HETNAM 1GP SN-GLYCEROL-1-PHOSPHATE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 3 1GP 2(C3 H9 O6 P)
FORMUL 4 MPD 2(C6 H14 O2)
FORMUL 7 HOH *222(H2 O)
HELIX 1 1 MET A 1001 TRP A 1006 5 6
HELIX 2 2 THR A 1019 SER A 1029 1 11
HELIX 3 3 THR A 1043 SER A 1055 1 13
HELIX 4 4 THR A 1093 MET A 1102 1 10
HELIX 5 5 HIS A 1103 GLU A 1105 5 3
HELIX 6 6 ASN A 1106 SER A 1116 1 11
HELIX 7 7 SER A 1131 THR A 1137 1 7
HELIX 8 8 ASP A 1144 LEU A 1158 1 15
HELIX 9 9 ASN A 1174 LEU A 1185 1 12
HELIX 10 10 SER A 1198 LEU A 1206 1 9
HELIX 11 11 ASN A 1216 LYS A 1221 1 6
HELIX 12 12 GLY A 1222 GLU A 1228 1 7
HELIX 13 13 ARG B 2002 TRP B 2006 5 5
HELIX 14 14 THR B 2019 ASP B 2028 1 10
HELIX 15 15 THR B 2043 GLN B 2056 1 14
HELIX 16 16 THR B 2093 HIS B 2103 1 11
HELIX 17 17 ASN B 2106 SER B 2116 1 11
HELIX 18 18 SER B 2131 THR B 2137 1 7
HELIX 19 19 ASP B 2144 LEU B 2158 1 15
HELIX 20 20 ASN B 2174 LEU B 2185 1 12
HELIX 21 21 SER B 2198 ALA B 2209 1 12
HELIX 22 22 GLY B 2215 GLY B 2222 1 8
HELIX 23 23 GLY B 2222 GLU B 2228 1 7
SHEET 1 A 9 HIS A1008 LEU A1012 0
SHEET 2 A 9 ALA A1033 ILE A1036 1 O ALA A1033 N THR A1010
SHEET 3 A 9 ILE A1061 VAL A1063 1 O VAL A1062 N ILE A1036
SHEET 4 A 9 TYR A1077 VAL A1083 1 O TYR A1077 N VAL A1063
SHEET 5 A 9 ILE A1119 VAL A1126 1 O GLU A1122 N VAL A1080
SHEET 6 A 9 ILE A1163 GLU A1167 1 O ILE A1163 N GLY A1123
SHEET 7 A 9 ARG A1189 GLY A1193 1 O PHE A1191 N ILE A1164
SHEET 8 A 9 THR A1211 VAL A1214 1 O ILE A1213 N TYR A1192
SHEET 9 A 9 HIS A1008 LEU A1012 1 N LYS A1011 O VAL A1214
SHEET 1 B 9 HIS B2008 LEU B2012 0
SHEET 2 B 9 ALA B2033 ILE B2036 1 O MET B2035 N THR B2010
SHEET 3 B 9 ILE B2061 VAL B2063 1 O VAL B2062 N ILE B2036
SHEET 4 B 9 TYR B2077 VAL B2083 1 O TYR B2077 N VAL B2063
SHEET 5 B 9 ILE B2119 VAL B2126 1 O TYR B2124 N THR B2082
SHEET 6 B 9 ILE B2163 GLU B2167 1 O ILE B2163 N GLY B2123
SHEET 7 B 9 ARG B2189 GLY B2193 1 O PHE B2191 N ILE B2164
SHEET 8 B 9 THR B2211 VAL B2214 1 O ILE B2213 N TYR B2192
SHEET 9 B 9 HIS B2008 LEU B2012 1 N ILE B2009 O VAL B2214
SITE 1 AC1 13 HOH A 6 HOH A 40 HOH A 185 HOH A 219
SITE 2 AC1 13 LYS A1011 TYR A1165 GLU A1167 GLY A1170
SITE 3 AC1 13 GLY A1193 GLY A1194 GLY A1195 GLY A1215
SITE 4 AC1 13 ASN A1216
SITE 1 AC2 10 HOH B 21 HOH B 43 LYS B2011 TYR B2165
SITE 2 AC2 10 GLU B2167 GLY B2170 GLY B2193 GLY B2194
SITE 3 AC2 10 GLY B2195 ASN B2216
SITE 1 AC3 8 HOH A 184 PRO A1065 SER A1066 ASP A1067
SITE 2 AC3 8 VAL A1080 PRO A1081 LYS A1095 TRP A1099
SITE 1 AC4 7 PRO B2065 SER B2066 ASP B2067 PRO B2081
SITE 2 AC4 7 LYS B2095 HIS B2096 TRP B2099
CRYST1 95.880 95.880 166.300 90.00 90.00 120.00 H 3 18
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 0.010430 0.006022 0.000000 0.00000
SCALE2 0.000000 0.012043 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006013 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
