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HEADER HYDROLASE 11-DEC-06 2O7R
TITLE PLANT CARBOXYLESTERASE AECXE1 FROM ACTINIDIA ERIANTHA WITH
TITLE 2 ACYL ADDUCT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CXE CARBOXYLESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACTINIDIA ERIANTHA;
SOURCE 3 GENE: CXE1;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS CARBOXYLESTERASE, ACTINIDIA ERIANTHA, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.R.ILEPERUMA,S.D.MARSHALL,C.J.SQUIRE,H.M.BAKER,
AUTHOR 2 J.G.OAKESHOTT,R.J.RUSSELL,K.M.PLUMMER,R.D.NEWCOMB,E.N.BAKER
REVDAT 1 27-FEB-07 2O7R 0
JRNL AUTH N.R.ILEPERUMA,S.D.MARSHALL,C.J.SQUIRE,H.M.BAKER,
JRNL AUTH 2 J.G.OAKESHOTT,R.J.RUSSELL,K.M.PLUMMER,R.D.NEWCOMB,
JRNL AUTH 3 E.N.BAKER
JRNL TITL HIGH-RESOLUTION CRYSTAL STRUCTURE OF PLANT
JRNL TITL 2 CARBOXYLESTERASE AECXE1, FROM ACTINIDIA ERIANTHA,
JRNL TITL 3 AND ITS COMPLEX WITH A HIGH-AFFINITY INHIBITOR
JRNL TITL 4 PARAOXON.
JRNL REF BIOCHEMISTRY V. 46 1851 2007
JRNL REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 3 NUMBER OF REFLECTIONS : 61167
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 + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3305
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.38
REMARK 3 BIN RESOLUTION RANGE LOW : 1.42
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2543
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 51.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 137
REMARK 3 BIN FREE R VALUE : 0.3410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2627
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.42000
REMARK 3 B22 (A**2) : -0.40000
REMARK 3 B33 (A**2) : 1.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.42000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.066
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.065
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2470 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3352 ; 1.923 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 303 ; 5.514 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 107 ;32.583 ;23.271
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 400 ;11.228 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;14.281 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 373 ; 0.132 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1863 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1199 ; 0.238 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1698 ; 0.316 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 181 ; 0.129 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 52 ; 0.208 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.092 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1574 ; 1.395 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2463 ; 1.963 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1019 ; 2.856 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 889 ; 4.004 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2O7R COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-2007.
REMARK 100 THE RCSB ID CODE IS RCSB040793.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-2006
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97907
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63214
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 31.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.43300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% MPEG 5000, 0.2M MALIC/KOH, PH
REMARK 280 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 1/2+X,1/2+Y,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 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 78.28250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.91000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 78.28250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.91000
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 1 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH 30 LIES ON A SPECIAL POSITION.
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 MET A 1
REMARK 465 SER A 2
REMARK 465 ASN A 3
REMARK 465 ASP A 4
REMARK 465 HIS A 5
REMARK 465 LEU A 6
REMARK 465 GLU A 7
REMARK 465 THR A 8
REMARK 465 THR A 9
REMARK 465 GLY A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 ASP A 13
REMARK 465 PRO A 14
REMARK 465 ASN A 15
REMARK 465 THR A 16
REMARK 465 ASN A 17
REMARK 465 ALA A 250
REMARK 465 GLU A 251
REMARK 465 SER A 252
REMARK 465 GLU A 253
REMARK 465 ASP A 329
REMARK 465 SER A 330
REMARK 465 CYS A 331
REMARK 465 THR A 332
REMARK 465 THR A 333
REMARK 465 LYS A 334
REMARK 465 LEU A 335
REMARK 465 LYS A 336
REMARK 465 LEU A 337
REMARK 465 ASN A 338
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
REMARK 500 O HOH 101 O HOH 217 2.18
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 M RES CSSEQI PSI PHI
REMARK 500 PHE A 97 166.24 76.29
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2O7V RELATED DB: PDB
DBREF 2O7R A 1 335 UNP Q0ZPV7 Q0ZPV7_9ERIC 1 335
SEQADV 2O7R LYS A 336 UNP Q0ZPV7 CLONING ARTIFACT
SEQADV 2O7R LEU A 337 UNP Q0ZPV7 CLONING ARTIFACT
SEQADV 2O7R ASN A 338 UNP Q0ZPV7 CLONING ARTIFACT
SEQRES 1 A 338 MET SER ASN ASP HIS LEU GLU THR THR GLY SER SER ASP
SEQRES 2 A 338 PRO ASN THR ASN LEU LEU LYS TYR LEU PRO ILE VAL LEU
SEQRES 3 A 338 ASN PRO ASP ARG THR ILE THR ARG PRO ILE GLN ILE PRO
SEQRES 4 A 338 SER THR ALA ALA SER PRO ASP PRO THR SER SER SER PRO
SEQRES 5 A 338 VAL LEU THR LYS ASP LEU ALA LEU ASN PRO LEU HIS ASN
SEQRES 6 A 338 THR PHE VAL ARG LEU PHE LEU PRO ARG HIS ALA LEU TYR
SEQRES 7 A 338 ASN SER ALA LYS LEU PRO LEU VAL VAL TYR PHE HIS GLY
SEQRES 8 A 338 GLY GLY PHE ILE LEU PHE SER ALA ALA SER THR ILE PHE
SEQRES 9 A 338 HIS ASP PHE CYS CYS GLU MET ALA VAL HIS ALA GLY VAL
SEQRES 10 A 338 VAL ILE ALA SER VAL ASP TYR ARG LEU ALA PRO GLU HIS
SEQRES 11 A 338 ARG LEU PRO ALA ALA TYR ASP ASP ALA MET GLU ALA LEU
SEQRES 12 A 338 GLN TRP ILE LYS ASP SER ARG ASP GLU TRP LEU THR ASN
SEQRES 13 A 338 PHE ALA ASP PHE SER ASN CYS PHE ILE MET GLY GLU SER
SEQRES 14 A 338 ALA GLY GLY ASN ILE ALA TYR HIS ALA GLY LEU ARG ALA
SEQRES 15 A 338 ALA ALA VAL ALA ASP GLU LEU LEU PRO LEU LYS ILE LYS
SEQRES 16 A 338 GLY LEU VAL LEU ASP GLU PRO GLY PHE GLY GLY SER LYS
SEQRES 17 A 338 ARG THR GLY SER GLU LEU ARG LEU ALA ASN ASP SER ARG
SEQRES 18 A 338 LEU PRO THR PHE VAL LEU ASP LEU ILE TRP GLU LEU SER
SEQRES 19 A 338 LEU PRO MET GLY ALA ASP ARG ASP HIS GLU TYR CYS ASN
SEQRES 20 A 338 PRO THR ALA GLU SER GLU PRO LEU TYR SER PHE ASP LYS
SEQRES 21 A 338 ILE ARG SER LEU GLY TRP ARG VAL MET VAL VAL GLY CYS
SEQRES 22 A 338 HIS GLY ASP PRO MET ILE ASP ARG GLN MET GLU LEU ALA
SEQRES 23 A 338 GLU ARG LEU GLU LYS LYS GLY VAL ASP VAL VAL ALA GLN
SEQRES 24 A 338 PHE ASP VAL GLY GLY TYR HIS ALA VAL LYS LEU GLU ASP
SEQRES 25 A 338 PRO GLU LYS ALA LYS GLN PHE PHE VAL ILE LEU LYS LYS
SEQRES 26 A 338 PHE VAL VAL ASP SER CYS THR THR LYS LEU LYS LEU ASN
HET 4PA A 369 7
HETNAM 4PA PROPYL ACETATE
FORMUL 2 4PA C5 H10 O2
FORMUL 3 HOH *217(H2 O1)
HELIX 1 1 HIS A 75 ASN A 79 5 5
HELIX 2 2 SER A 101 GLY A 116 1 16
HELIX 3 3 PRO A 133 ASP A 148 1 16
HELIX 4 4 ASP A 151 PHE A 157 1 7
HELIX 5 5 SER A 169 ALA A 184 1 16
HELIX 6 6 VAL A 185 LEU A 190 1 6
HELIX 7 7 THR A 210 LEU A 216 1 7
HELIX 8 8 PRO A 223 LEU A 235 1 13
HELIX 9 9 TYR A 256 GLY A 265 1 10
HELIX 10 10 MET A 278 LYS A 292 1 15
HELIX 11 11 ALA A 307 GLU A 311 5 5
HELIX 12 12 ASP A 312 VAL A 328 1 17
SHEET 1 A 2 VAL A 25 LEU A 26 0
SHEET 2 A 2 ILE A 32 THR A 33 -1 O THR A 33 N VAL A 25
SHEET 1 B 8 VAL A 53 ASN A 61 0
SHEET 2 B 8 THR A 66 PRO A 73 -1 O LEU A 72 N LEU A 54
SHEET 3 B 8 VAL A 118 ASP A 123 -1 O ASP A 123 N PHE A 67
SHEET 4 B 8 LEU A 83 PHE A 89 1 N VAL A 86 O VAL A 118
SHEET 5 B 8 ALA A 158 GLU A 168 1 O ASP A 159 N LEU A 83
SHEET 6 B 8 ILE A 194 ASP A 200 1 O LYS A 195 N CYS A 163
SHEET 7 B 8 ARG A 267 CYS A 273 1 O MET A 269 N LEU A 199
SHEET 8 B 8 ASP A 295 ASP A 301 1 O ASP A 295 N VAL A 268
LINK OG SER A 169 CAI 4PA A 369
CISPEP 1 ALA A 127 PRO A 128 0 1.61
CISPEP 2 LEU A 132 PRO A 133 0 11.73
CISPEP 3 LEU A 190 PRO A 191 0 13.11
CRYST1 156.565 53.820 42.328 90.00 102.48 90.00 C 1 2 1 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 0.006387 0.000000 0.001414 0.00000
SCALE2 0.000000 0.018580 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024197 0.00000
TER 2404 VAL A 328
MASTER 294 0 1 12 10 0 0 6 2627 1 8 26
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