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HEADER HYDROLASE 05-MAR-01 1I6W
TITLE THE CRYSTAL STRUCTURE OF BACILLUS SUBTILIS LIPASE: A
TITLE 2 MINIMAL ALPHA/BETA HYDROLASE ENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE A;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 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 ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.VAN POUDEROYEN,T.EGGERT,K.-E.JAEGER,B.W.DIJKSTRA
REVDAT 1 23-MAY-01 1I6W 0
JRNL AUTH G.VAN POUDEROYEN,T.EGGERT,K.-E.JAEGER,B.W.DIJKSTRA
JRNL TITL THE CRYSTAL STRUCTURE OF BACILLUS SUBTILIS LIPASE:
JRNL TITL 2 A MINIMAL ALPHA/BETA HYDROLASE FOLD ENZYME
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.50 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_TOPPAR:PROTEIN_REP.PARAM
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 81.0
REMARK 3 NUMBER OF REFLECTIONS : 41796
REMARK 3
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : R-FREE
REMARK 3 FREE R VALUE TEST SET SELECTION : 5%
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2099
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 : 41
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.51
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 116
REMARK 3 BIN R VALUE (WORKING SET) : 0.3344
REMARK 3 BIN FREE R VALUE : 0.3854
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 5
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 : 2711
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 517
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.39
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.15
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) : 0.18
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.24
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.70
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
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS ANISOTROPIC
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 1I6W COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-2001.
REMARK 100 THE RCSB ID CODE IS RCSB012979.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-1999
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 : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9393 ANGSTROM
REMARK 200 MONOCHROMATOR : SI111 OR SI311 CRYSTALS,
REMARK 200 LN2 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 : 689356
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.4
REMARK 200 DATA REDUNDANCY : 16.500
REMARK 200 R MERGE (I) : 0.00000
REMARK 200 R SYM (I) : 7.60000
REMARK 200 FOR THE DATA SET : 20.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 30.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.00000
REMARK 200 R SYM FOR SHELL (I) : 28.00000
REMARK 200 FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: DM
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, ETHANOL AMINE,
REMARK 280 SODIUM SULPHATE, CADMIUM CHLORIDE
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 19.81950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.87600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.60050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.87600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.81950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.60050
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 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, 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 ALA A 1
REMARK 465 GLU A 2
REMARK 465 ALA B 1
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 HIS A 3 CA HIS A 3 N 0.038
REMARK 500 MET A 134 CE MET A 134 SD 0.034
REMARK 500 GLU B 2 CA GLU B 2 N 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. =-10.0 DEGREES
REMARK 500 VAL A 74 N - CA - C ANGL. DEV. = -8.0 DEGREES
REMARK 500 ALA A 105 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 ASN A 106 N - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 ARG A 147 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 GLY B 13 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 PHE B 17 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 PHE B 19 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 GLY B 30 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 GLY B 46 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 ASP B 72 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 VAL B 74 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 THR B 126 N - CA - C ANGL. DEV. = -7.4 DEGREES
REMARK 500 ARG B 147 N - CA - C ANGL. DEV. = -9.8 DEGREES
DBREF 1I6W A 1 181 SWS P37957 LIP_BACSU 32 212
DBREF 1I6W 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 CD 518 1
HETNAM CD CADMIUM ION
FORMUL 3 CD CD1 2+
FORMUL 4 HOH *517(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 PHE B 19 GLN B 29 1 11
HELIX 12 12 SER B 32 ASP B 34 5 3
HELIX 13 13 THR B 47 GLY B 67 1 21
HELIX 14 14 MET B 78 LEU B 90 1 13
HELIX 15 15 ASP B 91 ASN B 94 5 4
HELIX 16 16 ALA B 105 THR B 109 5 5
HELIX 17 17 MET B 137 SER B 141 5 5
HELIX 18 18 HIS B 156 TYR B 161 5 6
HELIX 19 19 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 O VAL A 6 N 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 N ALA A 97 O VAL A 71
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 ARG A 147 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 O VAL B 6 N 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 N ALA B 97 O VAL B 71
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 ARG B 147 N SER B 127
CRYST1 39.639 83.201 95.752 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 0.025228 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012019 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010444 0.00000
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