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HEADER HYDROLASE 18-SEP-13 4C6H
TITLE HALOALKANE DEHALOGENASE WITH 1-HEXANOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: 1-HEXANOL PRODUCT IN ACTIVE SITE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTERACEAE;
SOURCE 3 ORGANISM_TAXID: 31989;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: ROSETTA2;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-28A;
SOURCE 10 OTHER_DETAILS: CATALYSES BREAKDOWN OF HALOGENATED ALKANES TO THEIR
SOURCE 11 CORRESPONDING HYDROGEN HALIDES AND ALCOHOL COMPOUNDS
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.R.NOVAK,C.SAYER,M.ISUPOV,D.GOTZ,A.M.SPRAGG,J.A.LITTLECHILD
REVDAT 1 14-MAY-14 4C6H 0
JRNL AUTH H.R.NOVAK,C.SAYER,M.N.ISUPOV,D.GOTZ,A.M.SPRAGG,
JRNL AUTH 2 J.A.LITTLECHILD
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERISATION OF A HALOALKANE
JRNL TITL 2 DEHALOGENASE FROM A MARINE RHODOBACTERACEAE.
JRNL REF FEBS LETT. V. 588 1616 2014
JRNL REFN ISSN 0014-5793
JRNL PMID 24613925
JRNL DOI 10.1016/J.FEBSLET.2014.02.056
REMARK 2
REMARK 2 RESOLUTION. 1.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.86
REMARK 3 NUMBER OF REFLECTIONS : 34350
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) : 0.15460
REMARK 3 R VALUE (WORKING SET) : 0.15286
REMARK 3 FREE R VALUE : 0.18703
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1803
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.613
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.655
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2486
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.248
REMARK 3 BIN FREE R VALUE SET COUNT : 131
REMARK 3 BIN FREE R VALUE : 0.300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2399
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 331
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.604
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.52
REMARK 3 B22 (A**2) : -0.79
REMARK 3 B33 (A**2) : 1.31
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.086
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.087
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.609
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2497 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3410 ; 1.438 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 324 ; 5.536 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 126 ;32.191 ;23.730
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 414 ;12.466 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;17.638 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 368 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1953 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1199 ; 2.420 ; 4.680
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1505 ; 3.130 ; 7.861
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1296 ; 3.894 ; 5.490
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4C6H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-SEP-13.
REMARK 100 THE PDBE ID CODE IS EBI-58403.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 287
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36192
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.61
REMARK 200 RESOLUTION RANGE LOW (A) : 47.84
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 12.8
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 26.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.6
REMARK 200 R MERGE FOR SHELL (I) : 0.20
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.60
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1CV2
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.1
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1
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 32.22500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.70500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.22500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.70500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 A2012 LIES ON A SPECIAL POSITION.
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 NH1A ARG A 6 O HOH A 2004 0.98
REMARK 500 NH2A ARG A 6 O HOH A 2005 1.67
REMARK 500 OE1B GLU A 137 O HOH A 2177 2.18
REMARK 500 OD1 ASP A 254 O HOH A 2296 2.13
REMARK 500 CZ B ARG A 286 O HOH A 2061 1.76
REMARK 500 NH1B ARG A 286 O HOH A 2061 0.92
REMARK 500 NH2B ARG A 286 O HOH A 2061 2.20
REMARK 500 O HOH A 2054 O HOH A 2055 2.18
REMARK 500 O HOH A 2137 O HOH A 2141 2.18
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 145 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 145 NE - CZ - NH2 ANGL. DEV. = -3.5 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 PRO A 37 50.46 -105.52
REMARK 500 MET A 38 -162.22 -102.78
REMARK 500 ASN A 72 60.05 33.16
REMARK 500 ASP A 106 -134.48 54.76
REMARK 500 VAL A 246 -62.70 -138.62
REMARK 500 LEU A 270 -95.90 -94.61
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 CL A1293
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A1294
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HE2 A1295
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 GB KF032932
DBREF 4C6H A 2 292 PDB 4C6H 4C6H 2 292
SEQRES 1 A 291 THR THR SER PHE ARG ASP LYS LYS LYS PHE ALA THR VAL
SEQRES 2 A 291 HIS GLY LYS GLN MET ALA TYR ILE GLU GLU GLY THR GLY
SEQRES 3 A 291 ASP PRO ILE VAL PHE LEU HIS GLY ASN PRO MET SER SER
SEQRES 4 A 291 TYR LEU TRP ARG ASN ILE MET PRO HIS LEU ALA GLY LYS
SEQRES 5 A 291 GLY ARG LEU ILE ALA PRO ASP LEU ILE GLY MET GLY ASP
SEQRES 6 A 291 SER ASP LYS LEU ASP ASN SER GLY PRO ASP SER TYR THR
SEQRES 7 A 291 PHE ALA GLU HIS CYS THR TYR LEU PHE ALA LEU LEU GLU
SEQRES 8 A 291 GLN LEU GLY VAL THR GLU ASN VAL THR LEU VAL ILE HIS
SEQRES 9 A 291 ASP TRP GLY SER GLY LEU GLY PHE HIS TRP ALA HIS THR
SEQRES 10 A 291 HIS SER ASP ALA VAL LYS GLY ILE ALA PHE MET GLU ALA
SEQRES 11 A 291 ILE VAL GLU THR ARG GLU SER TRP ASP ALA PHE PRO GLU
SEQRES 12 A 291 ARG ALA ARG GLU MET PHE GLN ALA LEU ARG SER PRO ALA
SEQRES 13 A 291 GLY GLU GLU MET VAL LEU GLU LYS ASN LEU PHE VAL GLU
SEQRES 14 A 291 ALA LEU VAL PRO GLY SER ILE LEU ARG ASP LEU THR GLU
SEQRES 15 A 291 GLU GLU MET ASN GLU TYR ARG ARG PRO PHE ALA ASN ALA
SEQRES 16 A 291 GLY GLU ASP ARG ARG PRO THR LEU THR PHE PRO ARG GLN
SEQRES 17 A 291 VAL PRO ILE GLU GLY GLN PRO LYS ASP VAL THR GLU LEU
SEQRES 18 A 291 VAL ASP ALA TYR VAL ASP TRP LEU GLY GLN THR SER ILE
SEQRES 19 A 291 PRO LYS LEU PHE ILE ASN ALA ASP PRO GLY VAL LEU ILE
SEQRES 20 A 291 THR GLY GLU VAL ARG ASP ARG VAL ARG SER TRP PRO ASN
SEQRES 21 A 291 LEU THR GLU VAL THR VAL ALA GLY LEU HIS PHE ILE GLN
SEQRES 22 A 291 GLU ASP SER PRO ASP GLU ILE GLY ALA ALA VAL ARG ASP
SEQRES 23 A 291 TRP HIS ALA SER LEU
HET CL A1293 1
HET PGE A1294 10
HET HE2 A1295 14
HETNAM CL CHLORIDE ION
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM HE2 HEXAN-1-OL
FORMUL 2 CL CL 1-
FORMUL 3 PGE C6 H14 O4
FORMUL 4 HE2 C6 H14 O
FORMUL 5 HOH *331(H2 O)
HELIX 1 1 PHE A 5 LYS A 9 5 5
HELIX 2 2 SER A 39 ARG A 44 5 6
HELIX 3 3 ILE A 46 ALA A 51 5 6
HELIX 4 4 THR A 79 LEU A 94 1 16
HELIX 5 5 ASP A 106 HIS A 119 1 14
HELIX 6 6 SER A 138 PHE A 142 5 5
HELIX 7 7 PRO A 143 ARG A 145 5 3
HELIX 8 8 ALA A 146 ARG A 154 1 9
HELIX 9 9 ALA A 157 GLU A 164 1 8
HELIX 10 10 ASN A 166 ALA A 171 1 6
HELIX 11 11 ALA A 171 SER A 176 1 6
HELIX 12 12 THR A 182 ARG A 191 1 10
HELIX 13 13 PRO A 192 ALA A 194 5 3
HELIX 14 14 GLY A 197 ARG A 200 5 4
HELIX 15 15 ARG A 201 VAL A 210 1 10
HELIX 16 16 PRO A 216 GLY A 231 1 16
HELIX 17 17 THR A 249 ARG A 257 1 9
HELIX 18 18 PHE A 272 ASP A 276 5 5
HELIX 19 19 SER A 277 SER A 291 1 15
SHEET 1 AA 8 LYS A 10 VAL A 14 0
SHEET 2 AA 8 LYS A 17 GLU A 24 -1 O LYS A 17 N VAL A 14
SHEET 3 AA 8 ARG A 55 PRO A 59 -1 O LEU A 56 N GLU A 24
SHEET 4 AA 8 PRO A 29 LEU A 33 1 O ILE A 30 N ILE A 57
SHEET 5 AA 8 VAL A 100 HIS A 105 1 O THR A 101 N VAL A 31
SHEET 6 AA 8 VAL A 123 MET A 129 1 N LYS A 124 O VAL A 100
SHEET 7 AA 8 LYS A 237 PRO A 244 1 O LEU A 238 N PHE A 128
SHEET 8 AA 8 LEU A 262 GLY A 269 1 O THR A 263 N PHE A 239
CISPEP 1 ASN A 36 PRO A 37 0 -2.53
CISPEP 2 GLN A 215 PRO A 216 0 -4.05
CISPEP 3 ASP A 243 PRO A 244 0 6.53
SITE 1 AC1 6 ASN A 36 TRP A 107 PHE A 168 PRO A 207
SITE 2 AC1 6 HE2 A1295 HOH A2144
SITE 1 AC2 2 MET A 149 HOH A2186
SITE 1 AC3 8 ASP A 106 TRP A 107 ILE A 132 PHE A 142
SITE 2 AC3 8 PHE A 150 LEU A 247 CL A1293 HOH A2144
CRYST1 64.450 71.410 59.750 90.00 90.00 90.00 P 21 21 2 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 0.015516 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014004 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016736 0.00000
TER 2400 LEU A 292
MASTER 315 0 3 19 8 0 5 6 2755 1 24 23
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