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HEADER HYDROLASE 28-JAN-09 3G0I
TITLE COMPLEX OF ASPERGILLUS NIGER EPOXIDE HYDROLASE WITH
TITLE 2 VALPROMIDE (2-PROPYLPENTANAMIDE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 5-396;
COMPND 5 EC: 3.3.2.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 ORGANISM_TAXID: 5061;
SOURCE 4 STRAIN: LCP521;
SOURCE 5 GENE: HYL1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEF-ANEH336
KEYWDS EPOXIDE HYDROLASE, ALPHA/BETA HYDROLASE FOLD, VALPROMIDE, 2-
KEYWDS 2 PROPYLPENTANAMIDE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ZOU,S.L.MOWBRAY
REVDAT 1 09-JUN-09 3G0I 0
JRNL AUTH M.T.REETZ,M.BOCOLA,L.W.WANG,J.SANCHIS,A.CRONIN,
JRNL AUTH 2 M.ARAND,J.ZOU,A.ARCHELAS,A.L.BOTTALLA,A.NAWORYTA,
JRNL AUTH 3 S.L.MOWBRAY
JRNL TITL DIRECTED EVOLUTION OF AN ENANTIOSELECTIVE EPOXIDE
JRNL TITL 2 HYDROLASE: UNCOVERING THE SOURCE OF
JRNL TITL 3 ENANTIOSELECTIVITY AT EACH EVOLUTIONARY STAGE
JRNL REF J.AM.CHEM.SOC. V. 131 7334 2009
JRNL REFN ISSN 0002-7863
JRNL PMID 19469578
JRNL DOI 10.1021/JA809673D
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.ZOU,B.M.HALLBERG,T.BERGFORS,F.OESCH,M.ARAND,
REMARK 1 AUTH 2 S.L.MOWBRAY,T.A.JONES
REMARK 1 TITL STRUCTURE OF ASPERGILLUS NIGER EPOXIDE HYDROLASE AT
REMARK 1 TITL 2 1.8 A RESOLUTION: IMPLICATIONS FOR THE STRUCTURE
REMARK 1 TITL 3 AND FUNCTION OF THE MAMMALIAN MICROSOMAL CLASS OF
REMARK 1 TITL 4 EPOXIDE HYDROLASES
REMARK 1 REF STRUCTURE V. 8 111 2000
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 10673439
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 47296
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1214
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3226
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.1820
REMARK 3 BIN FREE R VALUE SET COUNT : 78
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6218
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 454
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : 0.10000
REMARK 3 B33 (A**2) : -0.10000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.218
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.179
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.231
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6439 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8771 ; 1.189 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 788 ; 5.862 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 280 ;35.419 ;23.214
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1031 ;13.657 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 37 ;17.375 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 940 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4979 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3144 ; 0.187 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4431 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 517 ; 0.134 ; 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): 43 ; 0.158 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.128 ; 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): 4041 ; 0.563 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6379 ; 0.931 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2767 ; 1.441 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2392 ; 2.283 ; 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 : 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 : 1.40
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 3G0I COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JAN-09.
REMARK 100 THE RCSB ID CODE IS RCSB051268.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-SEP-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
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) : 0.9763
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47596
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.9470
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.21300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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 1QO7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG6000, 0.1M MES, PH6.0, 0.1M
REMARK 280 UNBUFFERED SODIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 44.82750
REMARK 290 SMTRY3 2 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 300 REMARK: N/A
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
REMARK 350 TOTAL BURIED SURFACE AREA: 5620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
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 THR A 320
REMARK 465 ALA A 321
REMARK 465 SER A 322
REMARK 465 ALA A 323
REMARK 465 PRO A 324
REMARK 465 ASN A 325
REMARK 465 GLY A 326
REMARK 465 ALA A 327
REMARK 465 THR A 328
REMARK 465 THR B 320
REMARK 465 ALA B 321
REMARK 465 SER B 322
REMARK 465 ALA B 323
REMARK 465 PRO B 324
REMARK 465 ASN B 325
REMARK 465 GLY B 326
REMARK 465 ALA B 327
REMARK 465 THR B 328
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 118 41.06 -94.39
REMARK 500 THR A 153 -115.46 43.45
REMARK 500 ASP A 192 -137.83 53.15
REMARK 500 ASP A 286 -73.39 -83.20
REMARK 500 LYS A 332 -88.25 -120.02
REMARK 500 PRO B 118 39.25 -94.48
REMARK 500 SER B 120 -177.71 -173.13
REMARK 500 THR B 153 -113.00 45.44
REMARK 500 ASP B 192 -138.48 56.12
REMARK 500 ASP B 286 -77.75 -83.27
REMARK 500 LYS B 332 -90.81 -123.93
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 VPR A 1
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VPR B 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QO7 RELATED DB: PDB
REMARK 900 STRUCTURE OF ASPERGILLUS NIGER EPOXIDE HYDROLASE
DBREF 3G0I A 5 396 UNP Q9UR30 Q9UR30_ASPNG 5 396
DBREF 3G0I B 5 396 UNP Q9UR30 Q9UR30_ASPNG 5 396
SEQADV 3G0I LYS A 3 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G0I ALA A 4 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G0I LYS B 3 UNP Q9UR30 EXPRESSION TAG
SEQADV 3G0I ALA B 4 UNP Q9UR30 EXPRESSION TAG
SEQRES 1 A 394 LYS ALA PHE ALA LYS PHE PRO SER SER ALA SER ILE SER
SEQRES 2 A 394 PRO ASN PRO PHE THR VAL SER ILE PRO ASP GLU GLN LEU
SEQRES 3 A 394 ASP ASP LEU LYS THR LEU VAL ARG LEU SER LYS ILE ALA
SEQRES 4 A 394 PRO PRO THR TYR GLU SER LEU GLN ALA ASP GLY ARG PHE
SEQRES 5 A 394 GLY ILE THR SER GLU TRP LEU THR THR MET ARG GLU LYS
SEQRES 6 A 394 TRP LEU SER GLU PHE ASP TRP ARG PRO PHE GLU ALA ARG
SEQRES 7 A 394 LEU ASN SER PHE PRO GLN PHE THR THR GLU ILE GLU GLY
SEQRES 8 A 394 LEU THR ILE HIS PHE ALA ALA LEU PHE SER GLU ARG GLU
SEQRES 9 A 394 ASP ALA VAL PRO ILE ALA LEU LEU HIS GLY TRP PRO GLY
SEQRES 10 A 394 SER PHE VAL GLU PHE TYR PRO ILE LEU GLN LEU PHE ARG
SEQRES 11 A 394 GLU GLU TYR THR PRO GLU THR LEU PRO PHE HIS LEU VAL
SEQRES 12 A 394 VAL PRO SER LEU PRO GLY TYR THR PHE SER SER GLY PRO
SEQRES 13 A 394 PRO LEU ASP LYS ASP PHE GLY LEU MET ASP ASN ALA ARG
SEQRES 14 A 394 VAL VAL ASP GLN LEU MET LYS ASP LEU GLY PHE GLY SER
SEQRES 15 A 394 GLY TYR ILE ILE GLN GLY GLY ASP ILE GLY SER PHE VAL
SEQRES 16 A 394 GLY ARG LEU LEU GLY VAL GLY PHE ASP ALA CYS LYS ALA
SEQRES 17 A 394 VAL HIS LEU ASN LEU CYS ALA MET ARG ALA PRO PRO GLU
SEQRES 18 A 394 GLY PRO SER ILE GLU SER LEU SER ALA ALA GLU LYS GLU
SEQRES 19 A 394 GLY ILE ALA ARG MET GLU LYS PHE MET THR ASP GLY LEU
SEQRES 20 A 394 ALA TYR ALA MET GLU HIS SER THR ARG PRO SER THR ILE
SEQRES 21 A 394 GLY HIS VAL LEU SER SER SER PRO ILE ALA LEU LEU ALA
SEQRES 22 A 394 TRP ILE GLY GLU LYS TYR LEU GLN TRP VAL ASP LYS PRO
SEQRES 23 A 394 LEU PRO SER GLU THR ILE LEU GLU MET VAL SER LEU TYR
SEQRES 24 A 394 TRP LEU THR GLU SER PHE PRO ARG ALA ILE HIS THR TYR
SEQRES 25 A 394 ARG GLU THR THR PRO THR ALA SER ALA PRO ASN GLY ALA
SEQRES 26 A 394 THR MET LEU GLN LYS GLU LEU TYR ILE HIS LYS PRO PHE
SEQRES 27 A 394 GLY PHE SER PHE PHE PRO LYS ASP LEU CYS PRO VAL PRO
SEQRES 28 A 394 ARG SER TRP ILE ALA THR THR GLY ASN LEU VAL PHE PHE
SEQRES 29 A 394 ARG ASP HIS ALA GLU GLY GLY HIS PHE ALA ALA LEU GLU
SEQRES 30 A 394 ARG PRO ARG GLU LEU LYS THR ASP LEU THR ALA PHE VAL
SEQRES 31 A 394 GLU GLN VAL TRP
SEQRES 1 B 394 LYS ALA PHE ALA LYS PHE PRO SER SER ALA SER ILE SER
SEQRES 2 B 394 PRO ASN PRO PHE THR VAL SER ILE PRO ASP GLU GLN LEU
SEQRES 3 B 394 ASP ASP LEU LYS THR LEU VAL ARG LEU SER LYS ILE ALA
SEQRES 4 B 394 PRO PRO THR TYR GLU SER LEU GLN ALA ASP GLY ARG PHE
SEQRES 5 B 394 GLY ILE THR SER GLU TRP LEU THR THR MET ARG GLU LYS
SEQRES 6 B 394 TRP LEU SER GLU PHE ASP TRP ARG PRO PHE GLU ALA ARG
SEQRES 7 B 394 LEU ASN SER PHE PRO GLN PHE THR THR GLU ILE GLU GLY
SEQRES 8 B 394 LEU THR ILE HIS PHE ALA ALA LEU PHE SER GLU ARG GLU
SEQRES 9 B 394 ASP ALA VAL PRO ILE ALA LEU LEU HIS GLY TRP PRO GLY
SEQRES 10 B 394 SER PHE VAL GLU PHE TYR PRO ILE LEU GLN LEU PHE ARG
SEQRES 11 B 394 GLU GLU TYR THR PRO GLU THR LEU PRO PHE HIS LEU VAL
SEQRES 12 B 394 VAL PRO SER LEU PRO GLY TYR THR PHE SER SER GLY PRO
SEQRES 13 B 394 PRO LEU ASP LYS ASP PHE GLY LEU MET ASP ASN ALA ARG
SEQRES 14 B 394 VAL VAL ASP GLN LEU MET LYS ASP LEU GLY PHE GLY SER
SEQRES 15 B 394 GLY TYR ILE ILE GLN GLY GLY ASP ILE GLY SER PHE VAL
SEQRES 16 B 394 GLY ARG LEU LEU GLY VAL GLY PHE ASP ALA CYS LYS ALA
SEQRES 17 B 394 VAL HIS LEU ASN LEU CYS ALA MET ARG ALA PRO PRO GLU
SEQRES 18 B 394 GLY PRO SER ILE GLU SER LEU SER ALA ALA GLU LYS GLU
SEQRES 19 B 394 GLY ILE ALA ARG MET GLU LYS PHE MET THR ASP GLY LEU
SEQRES 20 B 394 ALA TYR ALA MET GLU HIS SER THR ARG PRO SER THR ILE
SEQRES 21 B 394 GLY HIS VAL LEU SER SER SER PRO ILE ALA LEU LEU ALA
SEQRES 22 B 394 TRP ILE GLY GLU LYS TYR LEU GLN TRP VAL ASP LYS PRO
SEQRES 23 B 394 LEU PRO SER GLU THR ILE LEU GLU MET VAL SER LEU TYR
SEQRES 24 B 394 TRP LEU THR GLU SER PHE PRO ARG ALA ILE HIS THR TYR
SEQRES 25 B 394 ARG GLU THR THR PRO THR ALA SER ALA PRO ASN GLY ALA
SEQRES 26 B 394 THR MET LEU GLN LYS GLU LEU TYR ILE HIS LYS PRO PHE
SEQRES 27 B 394 GLY PHE SER PHE PHE PRO LYS ASP LEU CYS PRO VAL PRO
SEQRES 28 B 394 ARG SER TRP ILE ALA THR THR GLY ASN LEU VAL PHE PHE
SEQRES 29 B 394 ARG ASP HIS ALA GLU GLY GLY HIS PHE ALA ALA LEU GLU
SEQRES 30 B 394 ARG PRO ARG GLU LEU LYS THR ASP LEU THR ALA PHE VAL
SEQRES 31 B 394 GLU GLN VAL TRP
HET VPR A 1 10
HET VPR B 1 10
HETNAM VPR 2-PROPYLPENTANAMIDE
HETSYN VPR VALPROMIDE
FORMUL 3 VPR 2(C8 H17 N O)
FORMUL 5 HOH *454(H2 O)
HELIX 1 1 PRO A 24 SER A 38 1 15
HELIX 2 2 TYR A 45 GLN A 49 5 5
HELIX 3 3 THR A 57 GLU A 71 1 15
HELIX 4 4 ASP A 73 ASN A 82 1 10
HELIX 5 5 SER A 120 GLU A 123 5 4
HELIX 6 6 PHE A 124 TYR A 135 1 12
HELIX 7 7 GLY A 165 LEU A 180 1 16
HELIX 8 8 ASP A 192 PHE A 205 1 14
HELIX 9 9 SER A 226 LEU A 230 5 5
HELIX 10 10 SER A 231 GLY A 248 1 18
HELIX 11 11 LEU A 249 ARG A 258 1 10
HELIX 12 12 ARG A 258 SER A 268 1 11
HELIX 13 13 SER A 269 TRP A 284 1 16
HELIX 14 14 PRO A 290 THR A 304 1 15
HELIX 15 15 GLU A 305 ILE A 311 1 7
HELIX 16 16 THR A 313 THR A 318 1 6
HELIX 17 17 PRO A 353 ALA A 358 1 6
HELIX 18 18 PHE A 375 ARG A 380 1 6
HELIX 19 19 ARG A 380 TRP A 396 1 17
HELIX 20 20 PRO B 24 SER B 38 1 15
HELIX 21 21 TYR B 45 GLN B 49 5 5
HELIX 22 22 THR B 57 GLU B 71 1 15
HELIX 23 23 ASP B 73 ASN B 82 1 10
HELIX 24 24 SER B 120 GLU B 123 5 4
HELIX 25 25 PHE B 124 TYR B 135 1 12
HELIX 26 26 GLY B 165 LEU B 180 1 16
HELIX 27 27 ASP B 192 PHE B 205 1 14
HELIX 28 28 SER B 231 GLY B 248 1 18
HELIX 29 29 LEU B 249 ARG B 258 1 10
HELIX 30 30 ARG B 258 SER B 269 1 12
HELIX 31 31 SER B 269 TRP B 284 1 16
HELIX 32 32 PRO B 290 THR B 304 1 15
HELIX 33 33 GLU B 305 ILE B 311 1 7
HELIX 34 34 THR B 313 THR B 318 1 6
HELIX 35 35 PRO B 353 ALA B 358 1 6
HELIX 36 36 PHE B 375 ARG B 380 1 6
HELIX 37 37 ARG B 380 TRP B 396 1 17
SHEET 1 A 8 GLN A 86 ILE A 91 0
SHEET 2 A 8 LEU A 94 LEU A 101 -1 O ILE A 96 N THR A 89
SHEET 3 A 8 PHE A 142 PRO A 147 -1 O VAL A 146 N ALA A 99
SHEET 4 A 8 VAL A 109 LEU A 114 1 N ILE A 111 O VAL A 145
SHEET 5 A 8 TYR A 186 GLY A 190 1 O GLN A 189 N LEU A 114
SHEET 6 A 8 CYS A 208 LEU A 213 1 O LYS A 209 N TYR A 186
SHEET 7 A 8 ILE A 336 PHE A 344 1 O GLY A 341 N VAL A 211
SHEET 8 A 8 GLY A 361 ASP A 368 1 O ARG A 367 N PHE A 344
SHEET 1 B 8 GLN B 86 ILE B 91 0
SHEET 2 B 8 LEU B 94 LEU B 101 -1 O ILE B 96 N THR B 89
SHEET 3 B 8 PHE B 142 PRO B 147 -1 O VAL B 146 N ALA B 99
SHEET 4 B 8 VAL B 109 LEU B 114 1 N ILE B 111 O VAL B 145
SHEET 5 B 8 TYR B 186 GLY B 190 1 O GLN B 189 N LEU B 114
SHEET 6 B 8 CYS B 208 LEU B 213 1 O HIS B 212 N ILE B 188
SHEET 7 B 8 ILE B 336 PHE B 344 1 O GLY B 341 N LEU B 213
SHEET 8 B 8 GLY B 361 ASP B 368 1 O ARG B 367 N PHE B 344
CISPEP 1 TRP A 117 PRO A 118 0 3.83
CISPEP 2 GLY A 157 PRO A 158 0 -2.88
CISPEP 3 GLY A 224 PRO A 225 0 2.73
CISPEP 4 TRP B 117 PRO B 118 0 2.80
CISPEP 5 GLY B 157 PRO B 158 0 1.38
CISPEP 6 GLY B 224 PRO B 225 0 -4.36
SITE 1 AC1 6 TRP A 117 ASP A 192 ILE A 193 PHE A 196
SITE 2 AC1 6 TYR A 251 TYR A 314
SITE 1 AC2 8 TRP B 117 ASP B 192 ILE B 193 PHE B 244
SITE 2 AC2 8 TYR B 251 TRP B 284 TYR B 314 THR B 317
CRYST1 62.985 89.655 75.812 90.00 105.31 90.00 P 1 21 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 0.015877 0.000000 0.004345 0.00000
SCALE2 0.000000 0.011154 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013676 0.00000
TER 3103 TRP A 396
TER 6220 TRP B 396
MASTER 303 0 2 37 16 0 4 6 6692 2 20 62
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