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HEADER HYDROLASE 09-OCT-03 1R50
TITLE BACILLUS SUBTILIS LIPASE A WITH COVALENTLY BOUND SC-IPG-
TITLE 2 PHOSPHONATE-INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-181;
COMPND 5 SYNONYM: LIPASE A;
COMPND 6 EC: 3.1.1.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: LIPA;
SOURCE 5 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BCL1051;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMA5LIP
KEYWDS LIPASE, ALPHA/BETA HYDROLASE, PHOSPHONATE INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.DROEGE,G.VAN POUDEROYEN,T.E.VRENKEN,C.J.RUEGGEBERG,
AUTHOR 2 M.T.REETZ,B.W.DIJKSTRA,W.J.QUAX
REVDAT 1 19-OCT-04 1R50 0
JRNL AUTH M.J.DROEGE,G.VAN POUDEROYEN,T.E.VRENKEN,
JRNL AUTH 2 C.J.RUEGGEBERG,M.T.REETZ,B.W.DIJKSTRA,W.J.QUAX
JRNL TITL DIRECTED EVOLUTION OF BACILLUS SUBTILIS LIPASE A
JRNL TITL 2 USING ENANTIOMERIC PHOSPHONATE INHIBITORS: CRYSTAL
JRNL TITL 3 STRUCTURES AND PHAGE DISPLAY SELECTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.45 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
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) (%) : 85.8
REMARK 3 NUMBER OF REFLECTIONS : 48747
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) : 0.196
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2467
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 : 2702
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 245
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.72200
REMARK 3 B22 (A**2) : -0.85700
REMARK 3 B33 (A**2) : 0.13500
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) : 0.00
REMARK 3 ESD FROM SIGMAA (A) : 0.00
REMARK 3 LOW RESOLUTION CUTOFF (A) : 0.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.00
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.00
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.23
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R50 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-OCT-2003.
REMARK 100 THE RCSB ID CODE IS RCSB020444.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-2001
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 10.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9330
REMARK 200 MONOCHROMATOR : SI111 OR SI311 CRYSTALS, LN2
REMARK 200 COOLED
REMARK 200 OPTICS : MIRRORS
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 : TRUNCATE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48857
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.6
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.00000
REMARK 200 R SYM (I) : 0.04200
REMARK 200 FOR THE DATA SET : 27.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 35.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.00000
REMARK 200 R SYM FOR SHELL (I) : 0.30500
REMARK 200 FOR SHELL : 2.200
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: BACILLUS SUBTILIS LIPASE A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, ETHANOL AMINE, SODIUM
REMARK 280 SULPHATE, CADMIUM CHLORIDE, PH 10, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 19.79700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.54100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.79550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.54100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.79700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.79550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
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 ALA A 1
REMARK 465 GLU A 2
REMARK 465 ALA B 1
REMARK 465 GLU B 2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 77 CB SER A 77 OG 0.043
REMARK 500 MET A 134 SD MET A 134 CE -0.029
REMARK 500 SER B 77 CB SER B 77 OG 0.037
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 72 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 VAL A 74 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 ALA A 105 N - CA - C ANGL. DEV. = -8.8 DEGREES
REMARK 500 ALA A 113 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 THR A 126 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 ARG A 147 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 ASN B 18 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 GLY B 46 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 ASP B 72 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 VAL B 74 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 ALA B 105 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 ASN B 106 N - CA - C ANGL. DEV. = 7.3 DEGREES
REMARK 500 ALA B 113 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 THR B 126 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 ARG B 147 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 ASN B 179 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I6W RELATED DB: PDB
REMARK 900 BACILLUS SUBTILIS LIPASE A
REMARK 900 RELATED ID: 1R4Z RELATED DB: PDB
REMARK 900 BACILLUS SUBTILIS LIPASE A WITH COVALENTLY BOUND RC-IPG-
REMARK 900 PHOSPHONATE-INHIBITOR
DBREF 1R50 A 1 181 SWS P37957 LIP_BACSU 32 212
DBREF 1R50 B 1 181 SWS P37957 LIP_BACSU 32 212
SEQRES 1 A 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 A 181 GLY ALA SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU
SEQRES 3 A 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 A 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 A 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 A 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 A 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP
SEQRES 8 A 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 A 181 ALA ASN ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR
SEQRES 10 A 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 A 181 SER ALA ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 A 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 A 181 ILE GLY LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE
SEQRES 14 A 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 B 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 B 181 GLY ALA SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU
SEQRES 3 B 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 B 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 B 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 B 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 B 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP
SEQRES 8 B 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 B 181 ALA ASN ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR
SEQRES 10 B 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 B 181 SER ALA ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 B 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 B 181 ILE GLY LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE
SEQRES 14 B 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
HET SIL A 277 17
HET SIL B 277 17
HETNAM SIL [(4S)-2,2-DIMETHYL-1,3-DIOXOLAN-4-YL]METHYL HYDROGEN
HETNAM 2 SIL HEX-5-ENYLPHOSPHONATE
HETSYN SIL O-[(S)-1,2-O-ISOPROPYLIDENE-SN-GLYCEROL]6-HEXENYL
HETSYN 2 SIL PHOSPHONATE, O-[(S)-IPG] 6-HEXENYL PHOSPHONATE
FORMUL 3 SIL 2(C12 H23 O5 P1)
FORMUL 5 HOH *245(H2 O1)
HELIX 1 1 ALA A 15 ASN A 18 5 4
HELIX 2 2 PHE A 19 GLN A 29 1 11
HELIX 3 3 SER A 32 ASP A 34 5 3
HELIX 4 4 THR A 47 GLY A 67 1 21
HELIX 5 5 MET A 78 LEU A 90 1 13
HELIX 6 6 ASP A 91 ASN A 94 5 4
HELIX 7 7 ALA A 105 THR A 109 5 5
HELIX 8 8 MET A 137 ARG A 142 1 6
HELIX 9 9 HIS A 156 TYR A 161 5 6
HELIX 10 10 SER A 162 ASN A 174 1 13
HELIX 11 11 ALA B 15 ASN B 18 5 4
HELIX 12 12 PHE B 19 GLN B 29 1 11
HELIX 13 13 SER B 32 ASP B 34 5 3
HELIX 14 14 THR B 47 GLY B 67 1 21
HELIX 15 15 MET B 78 LEU B 90 1 13
HELIX 16 16 ASP B 91 ASN B 94 5 4
HELIX 17 17 ALA B 105 THR B 109 5 5
HELIX 18 18 MET B 137 ARG B 142 1 6
HELIX 19 19 HIS B 156 TYR B 161 5 6
HELIX 20 20 SER B 162 ASN B 174 1 13
SHEET 1 A 6 LEU A 36 ALA A 38 0
SHEET 2 A 6 VAL A 6 VAL A 9 1 N VAL A 6 O TYR A 37
SHEET 3 A 6 VAL A 71 HIS A 76 1 O ASP A 72 N VAL A 7
SHEET 4 A 6 VAL A 96 LEU A 102 1 O LEU A 102 N ALA A 75
SHEET 5 A 6 LEU A 124 SER A 130 1 O LEU A 124 N VAL A 99
SHEET 6 A 6 ARG A 147 ILE A 151 1 O VAL A 149 N SER A 127
SHEET 1 B 6 LEU B 36 ALA B 38 0
SHEET 2 B 6 VAL B 6 VAL B 9 1 N MET B 8 O TYR B 37
SHEET 3 B 6 VAL B 71 HIS B 76 1 O ASP B 72 N VAL B 7
SHEET 4 B 6 VAL B 96 LEU B 102 1 O LEU B 102 N ALA B 75
SHEET 5 B 6 LEU B 124 SER B 130 1 O LEU B 124 N VAL B 99
SHEET 6 B 6 ARG B 147 ILE B 151 1 O ILE B 151 N TYR B 129
LINK OG SER A 77 P16 SIL A 277
LINK OG SER B 77 P16 SIL B 277
CRYST1 39.594 83.591 95.082 90.00 90.00 90.00 P 21 21 21 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 0.025256 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011963 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010517 0.00000
TER 1352 ASN A 181
TER 2704 ASN B 181
MASTER 281 0 2 20 12 0 0 6 2981 2 36 28
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