HEADER HYDROLASE (ORGANOPHOSPHATE-DEGRADING) 07-JUL-94 1PTA
TITLE THREE-DIMENSIONAL STRUCTURE OF PHOSPHOTRIESTERASE: AN ENZYME CAPABLE
TITLE 2 OF DETOXIFYING ORGANOPHOSPHATE NERVE AGENTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOTRIESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.5.-.-
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BREVUNDIMONAS DIMINUTA;
SOURCE 3 ORGANISM_TAXID: 293
KEYWDS HYDROLASE (ORGANOPHOSPHATE-DEGRADING)
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BENNING,H.M.HOLDEN
REVDAT 5 14-FEB-24 1PTA 1 REMARK
REVDAT 4 29-NOV-17 1PTA 1 HELIX
REVDAT 3 13-JUL-11 1PTA 1 VERSN
REVDAT 2 24-FEB-09 1PTA 1 VERSN
REVDAT 1 01-DEC-95 1PTA 0
JRNL AUTH M.M.BENNING,J.M.KUO,F.M.RAUSHEL,H.M.HOLDEN
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF PHOSPHOTRIESTERASE: AN ENZYME
JRNL TITL 2 CAPABLE OF DETOXIFYING ORGANOPHOSPHATE NERVE AGENTS.
JRNL REF BIOCHEMISTRY V. 33 15001 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 7999757
JRNL DOI 10.1021/BI00254A008
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.M.BENNING,J.M.KUO,F.M.RAUSHEL,H.M.HOLDEN
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE BINUCLEAR METAL CENTER OF
REMARK 1 TITL 2 PHOSPHOTRIESTERASE
REMARK 1 REF BIOCHEMISTRY V. 34 7973 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 20330
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2439
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 129
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.014 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.320 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : 17.100; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.006 ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : 0.012 ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : 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 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PTA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175838.
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) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 48.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 40.10000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.10000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.85000
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 80.20000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 93.70000
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 GLY A 261
REMARK 465 LEU A 262
REMARK 465 GLU A 263
REMARK 465 ASP A 264
REMARK 465 ASN A 265
REMARK 465 ALA A 266
REMARK 465 SER A 267
REMARK 465 ALA A 268
REMARK 465 SER A 269
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 NZ LYS A 169 NE2 HIS A 201 2.12
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 81 CD GLU A 81 OE1 0.072
REMARK 500 GLU A 115 CD GLU A 115 OE2 0.078
REMARK 500 GLU A 144 CD GLU A 144 OE1 0.076
REMARK 500 GLU A 344 CD GLU A 344 OE1 0.071
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 85 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 96 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 96 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 100 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 109 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 109 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP A 121 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 133 CB - CG - OD1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 164 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 207 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP A 235 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 246 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 LEU A 252 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 ASP A 253 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 315 CB - CG - OD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ASP A 323 CB - CG - OD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 337 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 356 NE - CZ - NH2 ANGL. DEV. = -3.3 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 CYS A 59 -159.55 -141.42
REMARK 500 TRP A 69 67.19 -151.52
REMARK 500 GLU A 159 -129.10 50.92
REMARK 500 ALA A 203 -164.17 -71.15
REMARK 500 LEU A 252 77.32 -114.92
REMARK 500 VAL A 351 -57.84 -120.90
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PTA A 36 362 UNP P0A434 OPD_BREDI 36 362
SEQRES 1 A 327 ARG ILE ASN THR VAL ARG GLY PRO ILE THR ILE SER GLU
SEQRES 2 A 327 ALA GLY PHE THR LEU THR HIS GLU HIS ILE CYS GLY SER
SEQRES 3 A 327 SER ALA GLY PHE LEU ARG ALA TRP PRO GLU PHE PHE GLY
SEQRES 4 A 327 SER ARG LYS ALA LEU ALA GLU LYS ALA VAL ARG GLY LEU
SEQRES 5 A 327 ARG ARG ALA ARG ALA ALA GLY VAL ARG THR ILE VAL ASP
SEQRES 6 A 327 VAL SER THR PHE ASP ILE GLY ARG ASP VAL SER LEU LEU
SEQRES 7 A 327 ALA GLU VAL SER ARG ALA ALA ASP VAL HIS ILE VAL ALA
SEQRES 8 A 327 ALA THR GLY LEU TRP PHE ASP PRO PRO LEU SER MET ARG
SEQRES 9 A 327 LEU ARG SER VAL GLU GLU LEU THR GLN PHE PHE LEU ARG
SEQRES 10 A 327 GLU ILE GLN TYR GLY ILE GLU ASP THR GLY ILE ARG ALA
SEQRES 11 A 327 GLY ILE ILE LYS VAL ALA THR THR GLY LYS ALA THR PRO
SEQRES 12 A 327 PHE GLN GLU LEU VAL LEU LYS ALA ALA ALA ARG ALA SER
SEQRES 13 A 327 LEU ALA THR GLY VAL PRO VAL THR THR HIS THR ALA ALA
SEQRES 14 A 327 SER GLN ARG ASP GLY GLU GLN GLN ALA ALA ILE PHE GLU
SEQRES 15 A 327 SER GLU GLY LEU SER PRO SER ARG VAL CYS ILE GLY HIS
SEQRES 16 A 327 SER ASP ASP THR ASP ASP LEU SER TYR LEU THR ALA LEU
SEQRES 17 A 327 ALA ALA ARG GLY TYR LEU ILE GLY LEU ASP HIS ILE PRO
SEQRES 18 A 327 HIS SER ALA ILE GLY LEU GLU ASP ASN ALA SER ALA SER
SEQRES 19 A 327 ALA LEU LEU GLY ILE ARG SER TRP GLN THR ARG ALA LEU
SEQRES 20 A 327 LEU ILE LYS ALA LEU ILE ASP GLN GLY TYR MET LYS GLN
SEQRES 21 A 327 ILE LEU VAL SER ASN ASP TRP LEU PHE GLY PHE SER SER
SEQRES 22 A 327 TYR VAL THR ASN ILE MET ASP VAL MET ASP ARG VAL ASN
SEQRES 23 A 327 PRO ASP GLY MET ALA PHE ILE PRO LEU ARG VAL ILE PRO
SEQRES 24 A 327 PHE LEU ARG GLU LYS GLY VAL PRO GLN GLU THR LEU ALA
SEQRES 25 A 327 GLY ILE THR VAL THR ASN PRO ALA ARG PHE LEU SER PRO
SEQRES 26 A 327 THR LEU
FORMUL 2 HOH *129(H2 O)
HELIX 1 H1 ILE A 46 ALA A 49 1 4
HELIX 2 H2 PRO A 70 PHE A 73 1 4
HELIX 3 H3 ARG A 76 ALA A 93 1 18
HELIX 4 H4 VAL A 110 SER A 117 1 8
HELIX 5 H5 LEU A 136 MET A 138 1 3
HELIX 6 H6 VAL A 143 GLN A 155 1 13
HELIX 7 H7 PRO A 178 THR A 194 1 17
HELIX 8 H8 ASP A 208 PHE A 216 1 9
HELIX 9 H9 LEU A 237 LEU A 243 1 7
HELIX 10 H10 TRP A 277 LEU A 287 1 11
HELIX 11 H11 ASN A 300 PHE A 304 1 5
HELIX 12 H12 SER A 308 VAL A 310 1 3
HELIX 13 H13 PHE A 327 LEU A 336 1 10
HELIX 14 H14 GLN A 343 LEU A 358 1 16
SHEET 1 S1 2 ARG A 36 ASN A 38 0
SHEET 2 S1 2 PRO A 43 THR A 45 -1
SHEET 1 S2 8 PHE A 51 GLU A 56 0
SHEET 2 S2 8 THR A 97 ASP A 100 1
SHEET 3 S2 8 VAL A 122 TRP A 131 1
SHEET 4 S2 8 ILE A 167 THR A 173 1
SHEET 5 S2 8 PRO A 197 HIS A 201 1
SHEET 6 S2 8 VAL A 226 HIS A 230 1
SHEET 7 S2 8 LEU A 249 LEU A 252 1
SHEET 8 S2 8 ILE A 296 SER A 299 1
CRYST1 80.200 93.700 45.000 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 0.012469 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010672 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022222 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
