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HEADER HYDROLASE 28-AUG-07 2V9Z
TITLE STRUCTURE OF THE RHODOCOCCUS HALOALKANE DEHALOGENASE MUTANT
TITLE 2 WITH ENHANCED ENANTIOSELECTIVITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HALOALKANE DEHALOGENASE DHAA12;
COMPND 5 EC: 3.8.1.5;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RHODOCHROUS;
SOURCE 3 STRAIN: NCIMB13064;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_VECTOR: PET21B
KEYWDS PLASMID, HYDROLASE, DETOXIFICATION
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KOUDELAKOVA,Z.PROKOP,Y.SATO,M.LAPKOUSKI,E.CHOVANCOVA,
AUTHOR 2 M.MONINCOVA,A.JESENSKA,J.EMMER,T.SENDA,Y.NAGATA,
AUTHOR 3 I.KUTA SMATANOVA,J.DAMBORSKY
REVDAT 1 16-SEP-08 2V9Z 0
JRNL AUTH T.KOUDELAKOVA,Z.PROKOP,Y.SATO,M.LAPKOUSKI,
JRNL AUTH 2 E.CHOVANCOVA,M.MONINCOVA,A.JESENSKA,J.EMMER,
JRNL AUTH 3 T.SENDA,Y.NAGATA,I.KUTA SMATANOVA,J.DAMBORSKY
JRNL TITL RATIONAL ENGINEERING OF RHODOCOCCUS HALOALKANE
JRNL TITL 2 DEHALOGENASE WITH ENHANCED ENANTIOSELECTIVITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.0 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.13
REMARK 3 NUMBER OF REFLECTIONS : 5648
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) : 0.20252
REMARK 3 R VALUE (WORKING SET) : 0.19456
REMARK 3 FREE R VALUE : 0.26745
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 11.2
REMARK 3 FREE R VALUE TEST SET COUNT : 712
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) : 3.002
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.080
REMARK 3 REFLECTION IN BIN (WORKING SET) : 384
REMARK 3 BIN R VALUE (WORKING SET) : 0.251
REMARK 3 BIN FREE R VALUE SET COUNT : 51
REMARK 3 BIN FREE R VALUE : 0.379
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2415
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.456
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.602
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.422
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.618
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.796
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 2497 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 3416 ; 1.601 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 302 ;22.208 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 122 ;37.308 ;23.361
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 370 ;25.372 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;23.471 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 360 ; 0.281 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 1987 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 1330 ; 0.304 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): 1664 ; 0.340 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 104 ; 0.224 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 26 ; 0.169 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED (A): 5 ; 0.239 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 1537 ; 1.039 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 2466 ; 1.833 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 1058 ; 2.786 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 950 ; 4.396 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF 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. RESIDUES MET A 1 AND SER A 2 ARE
REMARK 3 DISORDERED. GLU A 3 DUE TO DISORDERED SIDE CHAIN IS
REMARK 3 SUBSTITUTED BY ALA. SIDE CHAINS OF ASP A 167 AND VAL
REMARK 3 A 168 WERE MODELLED STEREOCHEMICALLY
REMARK 4
REMARK 4 2V9Z COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 28-AUG-2007.
REMARK 100 THE EBI ID CODE IS EBI-33584.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-APR-2007
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NONIUS FR591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6389
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.00
REMARK 200 RESOLUTION RANGE LOW (A) : 53.45
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.7
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.4
REMARK 200 R MERGE (I) : 0.14
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.1
REMARK 200 R MERGE FOR SHELL (I) : 0.43
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1BN6
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL OF PROTEIN (5 MG/ML IN 25
REMARK 280 MM TRIS-HCL PH 7.5, 150 MM AMMONIUM SULPHATE, 1 MM EDTA)
REMARK 280 WAS MIXED 1:1 WITH THE RESERVOIR (1 ML) CONSISTED OF 20 %
REMARK 280 PEG 6000, 0.1 M SODIUM ACETATE, 0.2 M AMMONIUM SULPHATE,
REMARK 280 0.1 M TRIS-HCL PH 8.5-9.0. SITTING-DROP 281K.
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 26.36950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.34750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.45000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.34750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.36950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.45000
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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, TRP 141 TO PHE
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, PRO 142 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, PHE 144 TO ALA
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLY 171 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ALA 172 TO VAL
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LYS 175 TO GLY
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 176 TO GLY
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, VAL 245 TO ALA
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 3 CB CG CD OE1 OE2
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, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 221 CA - CB - CG ANGL. DEV. = 14.6 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 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 LEU A 18 49.09 39.86
REMARK 500 ARG A 30 35.52 105.03
REMARK 500 ASP A 31 -135.09 -176.22
REMARK 500 PRO A 42 64.48 -103.34
REMARK 500 THR A 43 -142.00 -104.55
REMARK 500 SER A 44 -165.64 174.23
REMARK 500 SER A 72 -173.57 -65.74
REMARK 500 LYS A 74 58.97 -107.53
REMARK 500 PHE A 80 -159.76 -58.42
REMARK 500 GLU A 98 -89.37 -94.61
REMARK 500 HIS A 105 -145.58 -106.98
REMARK 500 ASP A 106 -109.69 -42.15
REMARK 500 ASN A 119 47.26 -143.00
REMARK 500 GLU A 130 77.51 26.62
REMARK 500 ASP A 139 0.06 -53.34
REMARK 500 GLU A 141G -4.61 -55.72
REMARK 500 ASP A 156 95.78 39.77
REMARK 500 VAL A 157 -33.74 165.63
REMARK 500 ARG A 171 -52.61 -135.09
REMARK 500 LEU A 173 -70.43 -52.90
REMARK 500 PRO A 192 20.15 -71.92
REMARK 500 PHE A 193 21.57 -148.08
REMARK 500 ALA A 212 1.52 86.46
REMARK 500 ALA A 216 -38.74 -20.88
REMARK 500 ALA A 245 -86.35 -147.10
REMARK 500 GLU A 257 -36.29 -137.29
REMARK 500 LEU A 271 -103.53 -106.52
REMARK 500 ALA A 292 26.20 -70.50
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2V9Z A 1 141 UNP P0A3G2 DHAA_RHORH 1 141
DBREF 2V9Z A 141A 141K PDB 2V9Z 2V9Z 141A 141K
DBREF 2V9Z A 142 293 UNP P0A3G2 DHAA_RHORH 142 293
SEQADV 2V9Z PHE A 141 UNP P0A3G2 TRP 141 ENGINEERED MUTATION
SEQADV 2V9Z ALA A 142 UNP P0A3G2 PRO 142 ENGINEERED MUTATION
SEQADV 2V9Z ALA A 144 UNP P0A3G2 PHE 144 ENGINEERED MUTATION
SEQADV 2V9Z ARG A 171 UNP P0A3G2 GLY 171 ENGINEERED MUTATION
SEQADV 2V9Z VAL A 172 UNP P0A3G2 ALA 172 ENGINEERED MUTATION
SEQADV 2V9Z GLY A 175 UNP P0A3G2 LYS 175 ENGINEERED MUTATION
SEQADV 2V9Z GLY A 176 UNP P0A3G2 CYS 176 ENGINEERED MUTATION
SEQADV 2V9Z ALA A 245 UNP P0A3G2 VAL 245 ENGINEERED MUTATION
SEQRES 1 A 304 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 A 304 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 A 304 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 304 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 A 304 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 304 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 A 304 TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 A 304 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 A 304 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 A 304 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU
SEQRES 11 A 304 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU PHE HIS HIS
SEQRES 12 A 304 THR GLU VAL ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA
SEQRES 13 A 304 ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP VAL GLY
SEQRES 14 A 304 ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU ARG
SEQRES 15 A 304 VAL LEU PRO GLY GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 16 A 304 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL
SEQRES 17 A 304 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 18 A 304 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 19 A 304 ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 20 A 304 LEU LEU PHE TRP GLY THR PRO GLY ALA LEU ILE PRO PRO
SEQRES 21 A 304 ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN CYS
SEQRES 22 A 304 LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR LEU GLN
SEQRES 23 A 304 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 24 A 304 TRP LEU PRO ALA LEU
HELIX 1 1 SER A 44 ARG A 49 5 6
HELIX 2 2 ILE A 51 ALA A 56 1 6
HELIX 3 3 PHE A 81 LEU A 95 1 15
HELIX 4 4 TRP A 107 ARG A 118 1 12
HELIX 5 5 ASN A 119 GLU A 121 5 3
HELIX 6 6 VAL A 141E GLU A 141G 5 3
HELIX 7 7 GLU A 141H ARG A 153 1 16
HELIX 8 8 VAL A 157 ILE A 163 1 7
HELIX 9 9 ASN A 166 ARG A 171 1 6
HELIX 10 10 ARG A 171 GLY A 176 1 6
HELIX 11 11 THR A 182 GLU A 191 1 10
HELIX 12 12 PRO A 192 LEU A 194 5 3
HELIX 13 13 LYS A 195 ASP A 198 5 4
HELIX 14 14 ARG A 199 LEU A 209 1 11
HELIX 15 15 PRO A 215 SER A 232 1 18
HELIX 16 16 PRO A 248 LEU A 259 1 12
HELIX 17 17 TYR A 273 ASP A 277 5 5
HELIX 18 18 ASN A 278 LEU A 290 1 13
SHEET 1 AA 2 HIS A 13 GLU A 16 0
SHEET 2 AA 2 ARG A 21 TYR A 24 -1 O MET A 22 N VAL A 15
SHEET 1 AB 7 ASP A 26 VAL A 27 0
SHEET 2 AB 7 CYS A 61 ILE A 62 -1 O CYS A 61 N VAL A 27
SHEET 3 AB 7 VAL A 35 LEU A 38 1 O VAL A 35 N ILE A 62
SHEET 4 AB 7 VAL A 100 ILE A 104 1 O VAL A 101 N LEU A 36
SHEET 5 AB 7 VAL A 123 MET A 129 1 N LYS A 124 O VAL A 100
SHEET 6 AB 7 LYS A 236 PRO A 243 1 O LEU A 237 N CYS A 128
SHEET 7 AB 7 CYS A 262 GLY A 270 1 O LYS A 263 N LEU A 238
CISPEP 1 ASN A 41 PRO A 42 0 -6.98
CISPEP 2 GLU A 214 PRO A 215 0 -8.08
CISPEP 3 THR A 242 PRO A 243 0 11.92
CRYST1 52.739 68.900 84.695 90.00 90.00 90.00 P 21 21 21 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 0.018961 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014514 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011807 0.00000
TER 2416 LEU A 293
MASTER 312 0 0 18 9 0 0 6 2415 1 0 24
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