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HEADER EPOXIDE HYDROLASE 04-NOV-99 1QO7
TITLE STRUCTURE OF ASPERGILLUS NIGER EPOXIDE HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 3-396;
COMPND 5 SYNONYM: EH;
COMPND 6 EC: 3.3.2.3;
COMPND 7 MUTATION: YES;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 STRAIN: LCP521;
SOURCE 4 TISSUE: MYCELIUM;
SOURCE 5 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PGEF+;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEF-ANEH336;
SOURCE 11 EXPRESSION_SYSTEM_GENE: AJ238460 (EMBL DATABASE ENTRY);
SOURCE 12 OTHER_DETAILS: MUSEUM OF NATURAL HISTORY, PARIS, FRANCE.
SOURCE 13 MODIFIED N-TERMINUS
KEYWDS EPOXIDE HYDROLASE, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.-Y.ZOU,B.M.HALLBERG,T.BERGFORS,F.OESCH,M.ARAND,
AUTHOR 2 S.L.MOWBRAY,T.A.JONES
REVDAT 1 10-FEB-00 1QO7 0
JRNL AUTH J.-Y.ZOU,B.M.HALLBERG,T.BERGFORS,F.OESCH,M.ARAND,
JRNL AUTH 2 S.L.MOWBRAY,T.A.JONES
JRNL TITL STRUCTURE OF ASPERGILLUS NIGER EPOXIDE HYDROLASE AT
JRNL TITL 2 1.8A RESOLUTION: IMPLICATIONS FOR THE STRUCTURE AND
JRNL TITL 3 FUNCTION OF THE MAMMALIAN MICROSOMAL CLASS OF
JRNL TITL 4 EPOXIDE HYDROLASES
JRNL REF STRUCTURE (LONDON) V. 8 111 2000
JRNL REFN ASTM STRUE6 UK ISSN 0969-2126
REMARK 2
REMARK 2 RESOLUTION. 1.8 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,
REMARK 3 GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,
REMARK 3 PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 1636344.02
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 74309
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 SET) : 0.224
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1524
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 11975
REMARK 3 BIN R VALUE (WORKING SET) : 0.251
REMARK 3 BIN FREE R VALUE : 0.263
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.2
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 268
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6128
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 374
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.1
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.4
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.01
REMARK 3 B22 (A**2) : 3.23
REMARK 3 B33 (A**2) : -4.25
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.77
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.14
REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.3
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.3
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.83
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.49 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 0.88 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.58 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 0.95 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.355619
REMARK 3 BSOL : 39.2403
REMARK 3
REMARK 3 NCS MODEL : NONE
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1QO7 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 4-NOV-1999.
REMARK 100 THE EBI ID CODE IS EBI-4325.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-1999
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 BEAMLINE ID14
REMARK 200 BEAMLINE : ID14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.937
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74416
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.80
REMARK 200 RESOLUTION RANGE LOW (A) : 38.3
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.5
REMARK 200 R MERGE (I) : 0.073
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.5
REMARK 200 R MERGE FOR SHELL (I) : 0.321
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE,DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG6000, 0.1M MES BUFFER PH 6.0,
REMARK 280 0.1M NAAC.
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 44.66000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 A 3 .. 396 B 3 .. 396 0.02
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 THE ASYMMETRIC UNIT CONTAINS 1 COPY OF A HOMO-DIMERIC-COMPLEX
REMARK 300 OF BIOPOLYMERS
REMARK 300
REMARK 300 FOR THE HOMO-ASSEMBLY DESCRIBED BY REMARK 350
REMARK 300 THE DIFFERENCE IN ACCESSIBLE SURFACE AREA PER
REMARK 300 CHAIN BETWEEN THE ISOLATED CHAIN AND THAT FOR
REMARK 300 THE CHAIN IN THE COMPLEX IS 2398.4 ANGSTROM**2
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, 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: 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, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ALA A 99 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 LEU A 101 N - CA - C ANGL. DEV. = -10.2 DEGREES
REMARK 500 PRO A 118 C - N - CA ANGL. DEV. = 7.9 DEGREES
REMARK 500 THR A 136 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 HIS A 143 N - CA - C ANGL. DEV. = -13.0 DEGREES
REMARK 500 SER A 148 N - CA - C ANGL. DEV. = -10.0 DEGREES
REMARK 500 GLN A 189 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 GLY A 204 N - CA - C ANGL. DEV. = 10.0 DEGREES
REMARK 500 PHE A 307 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 PHE A 345 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 VAL A 395 N - CA - C ANGL. DEV. = 8.2 DEGREES
REMARK 500 ALA B 99 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 LEU B 101 N - CA - C ANGL. DEV. = -10.1 DEGREES
REMARK 500 THR B 136 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 HIS B 143 N - CA - C ANGL. DEV. = -12.8 DEGREES
REMARK 500 SER B 148 N - CA - C ANGL. DEV. = -10.3 DEGREES
REMARK 500 GLN B 189 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 GLY B 204 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 PHE B 307 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 PHE B 345 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 VAL B 395 N - CA - C ANGL. DEV. = 8.2 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 M RES CSSEQI PSI PHI
REMARK 500
REMARK 500 THR A 153 38.72 -112.38
REMARK 500 THR B 153 38.05 -111.79
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A V
REMARK 525 B W
REMARK 525
DBREF 1QO7 A 3 396 EMBL AJ238460 ANI238460 3 396
SEQADV 1QO7 LYS A 3 EMBL AJ238460 ALA 3 ENGINEERED
SEQADV 1QO7 ALA A 4 EMBL AJ238460 PRO 4 ENGINEERED
SEQADV 1QO7 LYS B 3 EMBL AJ238460 ALA 3 ENGINEERED
SEQADV 1QO7 ALA B 4 EMBL AJ238460 PRO 4 ENGINEERED
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
FORMUL 3 HOH *374(H2 O1)
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 269 1 12
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 SER A 306 ILE A 311 1 6
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 226 LEU B 230 5 5
HELIX 29 29 SER B 231 GLY B 248 1 18
HELIX 30 30 LEU B 249 ARG B 258 1 10
HELIX 31 31 ARG B 258 SER B 269 1 12
HELIX 32 32 SER B 269 TRP B 284 1 16
HELIX 33 33 PRO B 290 THR B 304 1 15
HELIX 34 34 SER B 306 ILE B 311 1 6
HELIX 35 35 THR B 313 THR B 318 1 6
HELIX 36 36 PRO B 353 ALA B 358 1 6
HELIX 37 37 PHE B 375 ARG B 380 1 6
HELIX 38 38 ARG B 380 TRP B 396 1 17
SHEET 1 A 8 PRO A 85 ILE A 91 0
SHEET 2 A 8 LEU A 94 LEU A 101 -1 N ALA A 100 O PRO A 85
SHEET 3 A 8 PHE A 142 PRO A 147 -1 N VAL A 146 O ALA A 99
SHEET 4 A 8 VAL A 109 LEU A 114 1 N VAL A 109 O HIS A 143
SHEET 5 A 8 TYR A 186 GLY A 190 1 N ILE A 187 O ALA A 112
SHEET 6 A 8 CYS A 208 LEU A 213 1 N LYS A 209 O TYR A 186
SHEET 7 A 8 PRO A 339 PHE A 345 1 N PRO A 339 O VAL A 211
SHEET 8 A 8 LEU A 363 HIS A 369 1 N VAL A 364 O PHE A 340
SHEET 1 B 8 PRO B 85 ILE B 91 0
SHEET 2 B 8 LEU B 94 LEU B 101 -1 N ALA B 100 O PRO B 85
SHEET 3 B 8 PHE B 142 PRO B 147 -1 N VAL B 146 O ALA B 99
SHEET 4 B 8 VAL B 109 LEU B 114 1 N VAL B 109 O HIS B 143
SHEET 5 B 8 TYR B 186 GLY B 190 1 N ILE B 187 O ALA B 112
SHEET 6 B 8 CYS B 208 LEU B 213 1 N LYS B 209 O TYR B 186
SHEET 7 B 8 PRO B 339 PHE B 345 1 N PRO B 339 O VAL B 211
SHEET 8 B 8 LEU B 363 HIS B 369 1 N VAL B 364 O PHE B 340
CISPEP 1 TRP A 117 PRO A 118 0 0.03
CISPEP 2 GLY A 157 PRO A 158 0 0.17
CISPEP 3 TRP B 117 PRO B 118 0 0.33
CISPEP 4 GLY B 157 PRO B 158 0 0.19
CRYST1 62.690 89.320 75.770 90.00 105.37 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 0.015951 0.000000 0.004385 0.00000
SCALE2 0.000000 0.011196 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013687 0.00000
MTRIX1 1 -0.999000 -0.043000 -0.022000 58.82900 1
MTRIX2 1 -0.048000 0.927000 0.373000 -23.39300 1
MTRIX3 1 0.005000 0.374000 -0.928000 127.74000 1
END |