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HEADER HYDROLASE 12-AUG-99 1CQZ
TITLE CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.3.2.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGAN: LIVER;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: INSECT;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR: BACCULOVIRUS
KEYWDS HOMODIMER, ALPHA/BETA HYDROLASE FOLD, DOMAIN-SWAPPING
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.ARGIRIADI,C.MORISSEAU,B.D.HAMMOCK,D.W.CHRISTIANSON
REVDAT 1 19-NOV-99 1CQZ 0
JRNL AUTH M.A.ARGIRIADI,C.MORISSEAU,B.D.HAMMOCK,
JRNL AUTH 2 D.W.CHRISTIANSON
JRNL TITL DETOXIFICATION OF ENVIRONMENTAL MUTAGENS AND
JRNL TITL 2 CARCINOGENS: STRUCTURE-BASED MECHANISM AND
JRNL TITL 3 EVOLUTION OF LIVER EPOXIDE HYDROLASE
JRNL REF PROC.NAT.ACAD.SCI.USA V. 96 10637 1999
JRNL REFN ASTM PNASA6 US ISSN 0027-8424
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.F.GRANT,D.H.STORMS,B.D.HAMMOCK
REMARK 1 TITL MOLECULAR CLONING AND EXPRESSION OF MURINE LIVER
REMARK 1 TITL 2 SOLUBLE EPOXIDE HYDROLASE
REMARK 1 REF J.BIOL.CHEM. V. 268 17628 1993
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.K.BEETHAM,D.GRANT,M.ARAND,J.GARBARINO,T.KIYOSUE,
REMARK 1 AUTH 2 F.PINOT,F.OESCH,W.R.BELKNAP,K.SHINOZAKI,B.D.HAMMOCK
REMARK 1 TITL GENE EVOLUTION OF EPOXIDE HYDROLASES AND
REMARK 1 TITL 2 RECOMMENDED NOMENCLATURE
REMARK 1 REF DNA CELL BIOL. V. 14 61 1995
REMARK 1 REFN ISSN 1044-5498
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 32278
REMARK 3
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM 5%
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.309
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1598
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8178
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 40
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.90
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.00
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3
REMARK 3 NCS MODEL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CQZ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-1999.
REMARK 100 THE RCSB ID CODE IS RCSB009504.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUL-1997
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.908
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : OTHER
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32278
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 9.400
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 50.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.35700
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: NULL
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, MES,
REMARK 280 ETHANOL, DITHIOTHREITOL
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 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 75.95000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 75.95000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 71.50000
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 2 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, 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 LEU A 3
REMARK 465 ALA A 20
REMARK 465 GLY A 21
REMARK 465 ALA A 22
REMARK 465 PHE A 23
REMARK 465 ARG A 24
REMARK 465 ARG A 25
REMARK 465 SER A 26
REMARK 465 GLU A 27
REMARK 465 GLU A 28
REMARK 465 ALA A 29
REMARK 465 LEU A 30
REMARK 465 ALA A 31
REMARK 465 LEU A 32
REMARK 465 PRO A 33
REMARK 465 ARG A 34
REMARK 465 ASP A 35
REMARK 465 PHE A 36
REMARK 465 LEU A 37
REMARK 465 LEU A 38
REMARK 465 GLY A 39
REMARK 465 ALA A 40
REMARK 465 TYR A 41
REMARK 465 GLN A 42
REMARK 465 THR A 43
REMARK 465 GLU A 44
REMARK 465 PHE A 45
REMARK 465 PRO A 46
REMARK 465 GLU A 47
REMARK 465 VAL A 64
REMARK 465 PRO A 65
REMARK 465 LEU A 66
REMARK 465 MET A 67
REMARK 465 ASP A 68
REMARK 465 GLU A 69
REMARK 465 SER A 70
REMARK 465 TYR A 71
REMARK 465 ARG A 72
REMARK 465 LYS A 73
REMARK 465 SER A 74
REMARK 465 SER A 75
REMARK 465 LYS A 76
REMARK 465 ALA A 77
REMARK 465 CYS A 78
REMARK 465 GLY A 79
REMARK 465 ALA A 80
REMARK 465 ASN A 81
REMARK 465 LEU A 82
REMARK 465 PRO A 83
REMARK 465 GLU A 84
REMARK 465 ASN A 85
REMARK 465 PHE A 86
REMARK 465 SER A 87
REMARK 465 ILE A 88
REMARK 465 SER A 89
REMARK 465 VAL A 545
REMARK 465 GLN A 546
REMARK 465 ASN A 547
REMARK 465 PRO A 548
REMARK 465 SER A 549
REMARK 465 VAL A 550
REMARK 465 THR A 551
REMARK 465 SER A 552
REMARK 465 LYS A 553
REMARK 465 ILE A 554
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 LEU B 3
REMARK 465 VAL B 545
REMARK 465 GLN B 546
REMARK 465 ASN B 547
REMARK 465 PRO B 548
REMARK 465 SER B 549
REMARK 465 VAL B 550
REMARK 465 THR B 551
REMARK 465 SER B 552
REMARK 465 LYS B 553
REMARK 465 ILE B 554
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 OD1 ASP A 320 NH2 ARG A 349 2.06
REMARK 500 OD1 ASP B 320 NH2 ARG B 349 2.07
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 291 SD MET A 291 CE 0.179
REMARK 500 MET B 291 SD MET B 291 CE 0.161
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 THR A 118 N - CA - C ANGL. DEV. =-11.5 DEGREES
REMARK 500 PRO A 232 C - N - CA ANGL. DEV. = 36.7 DEGREES
REMARK 500 GLU A 423 N - CA - C ANGL. DEV. =-13.1 DEGREES
REMARK 500 PRO A 435 C - N - CA ANGL. DEV. =-12.2 DEGREES
REMARK 500 ASN A 436 N - CA - C ANGL. DEV. =-14.6 DEGREES
REMARK 500 GLY A 457 N - CA - C ANGL. DEV. =-12.1 DEGREES
REMARK 500 LEU A 484 CA - CB - CG ANGL. DEV. =-11.6 DEGREES
REMARK 500 ASP B 9 N - CA - C ANGL. DEV. =-13.0 DEGREES
REMARK 500 GLU B 44 N - CA - C ANGL. DEV. =-12.9 DEGREES
REMARK 500 LEU B 112 CA - CB - CG ANGL. DEV. =-11.3 DEGREES
REMARK 500 LYS B 215 N - CA - C ANGL. DEV. =-11.5 DEGREES
REMARK 500 ASN B 231 N - CA - C ANGL. DEV. = 14.5 DEGREES
REMARK 500 PRO B 232 C - N - CA ANGL. DEV. = 21.9 DEGREES
REMARK 500 ASN B 436 N - CA - C ANGL. DEV. =-14.4 DEGREES
REMARK 500 GLY B 457 N - CA - C ANGL. DEV. =-12.5 DEGREES
REMARK 500 LEU B 484 CA - CB - CG ANGL. DEV. =-11.8 DEGREES
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 ALA A 207 126.94 -34.73
REMARK 500 ASN A 357 64.63 -48.28
REMARK 500 GLU A 423 128.65 -69.48
REMARK 500 GLU B 44 149.72 -64.34
REMARK 500 ASN B 205 119.19 -113.02
REMARK 500 ALA B 207 144.26 -114.12
REMARK 500 ASN B 357 63.78 -47.54
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CR6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE
REMARK 900 COMPLEXED WITH CPU INHIBITOR
DBREF 1CQZ A 1 554 SWS P34914 HYES_MOUSE 1 554
DBREF 1CQZ B 1 554 SWS P34914 HYES_MOUSE 1 554
SEQRES 1 A 554 MET ALA LEU ARG VAL ALA ALA PHE ASP LEU ASP GLY VAL
SEQRES 2 A 554 LEU ALA LEU PRO SER ILE ALA GLY ALA PHE ARG ARG SER
SEQRES 3 A 554 GLU GLU ALA LEU ALA LEU PRO ARG ASP PHE LEU LEU GLY
SEQRES 4 A 554 ALA TYR GLN THR GLU PHE PRO GLU GLY PRO THR GLU GLN
SEQRES 5 A 554 LEU MET LYS GLY LYS ILE THR PHE SER GLN TRP VAL PRO
SEQRES 6 A 554 LEU MET ASP GLU SER TYR ARG LYS SER SER LYS ALA CYS
SEQRES 7 A 554 GLY ALA ASN LEU PRO GLU ASN PHE SER ILE SER GLN ILE
SEQRES 8 A 554 PHE SER GLN ALA MET ALA ALA ARG SER ILE ASN ARG PRO
SEQRES 9 A 554 MET LEU GLN ALA ALA ILE ALA LEU LYS LYS LYS GLY PHE
SEQRES 10 A 554 THR THR CYS ILE VAL THR ASN ASN TRP LEU ASP ASP GLY
SEQRES 11 A 554 ASP LYS ARG ASP SER LEU ALA GLN MET MET CYS GLU LEU
SEQRES 12 A 554 SER GLN HIS PHE ASP PHE LEU ILE GLU SER CYS GLN VAL
SEQRES 13 A 554 GLY MET ILE LYS PRO GLU PRO GLN ILE TYR ASN PHE LEU
SEQRES 14 A 554 LEU ASP THR LEU LYS ALA LYS PRO ASN GLU VAL VAL PHE
SEQRES 15 A 554 LEU ASP ASP PHE GLY SER ASN LEU LYS PRO ALA ARG ASP
SEQRES 16 A 554 MET GLY MET VAL THR ILE LEU VAL HIS ASN THR ALA SER
SEQRES 17 A 554 ALA LEU ARG GLU LEU GLU LYS VAL THR GLY THR GLN PHE
SEQRES 18 A 554 PRO GLU ALA PRO LEU PRO VAL PRO CYS ASN PRO ASN ASP
SEQRES 19 A 554 VAL SER HIS GLY TYR VAL THR VAL LYS PRO GLY ILE ARG
SEQRES 20 A 554 LEU HIS PHE VAL GLU MET GLY SER GLY PRO ALA LEU CYS
SEQRES 21 A 554 LEU CYS HIS GLY PHE PRO GLU SER TRP PHE SER TRP ARG
SEQRES 22 A 554 TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY PHE ARG VAL
SEQRES 23 A 554 LEU ALA ILE ASP MET LYS GLY TYR GLY ASP SER SER SER
SEQRES 24 A 554 PRO PRO GLU ILE GLU GLU TYR ALA MET GLU LEU LEU CYS
SEQRES 25 A 554 LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY ILE PRO
SEQRES 26 A 554 GLN ALA VAL PHE ILE GLY HIS ASP TRP ALA GLY VAL MET
SEQRES 27 A 554 VAL TRP ASN MET ALA LEU PHE TYR PRO GLU ARG VAL ARG
SEQRES 28 A 554 ALA VAL ALA SER LEU ASN THR PRO PHE MET PRO PRO ASP
SEQRES 29 A 554 PRO ASP VAL SER PRO MET LYS VAL ILE ARG SER ILE PRO
SEQRES 30 A 554 VAL PHE ASN TYR GLN LEU TYR PHE GLN GLU PRO GLY VAL
SEQRES 31 A 554 ALA GLU ALA GLU LEU GLU LYS ASN MET SER ARG THR PHE
SEQRES 32 A 554 LYS SER PHE PHE ARG ALA SER ASP GLU THR GLY PHE ILE
SEQRES 33 A 554 ALA VAL HIS LYS ALA THR GLU ILE GLY GLY ILE LEU VAL
SEQRES 34 A 554 ASN THR PRO GLU ASP PRO ASN LEU SER LYS ILE THR THR
SEQRES 35 A 554 GLU GLU GLU ILE GLU PHE TYR ILE GLN GLN PHE LYS LYS
SEQRES 36 A 554 THR GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN THR
SEQRES 37 A 554 GLU ARG ASN TRP LYS TRP SER CYS LYS GLY LEU GLY ARG
SEQRES 38 A 554 LYS ILE LEU VAL PRO ALA LEU MET VAL THR ALA GLU LYS
SEQRES 39 A 554 ASP ILE VAL LEU ARG PRO GLU MET SER LYS ASN MET GLU
SEQRES 40 A 554 LYS TRP ILE PRO PHE LEU LYS ARG GLY HIS ILE GLU ASP
SEQRES 41 A 554 CYS GLY HIS TRP THR GLN ILE GLU LYS PRO THR GLU VAL
SEQRES 42 A 554 ASN GLN ILE LEU ILE LYS TRP LEU GLN THR GLU VAL GLN
SEQRES 43 A 554 ASN PRO SER VAL THR SER LYS ILE
SEQRES 1 B 554 MET ALA LEU ARG VAL ALA ALA PHE ASP LEU ASP GLY VAL
SEQRES 2 B 554 LEU ALA LEU PRO SER ILE ALA GLY ALA PHE ARG ARG SER
SEQRES 3 B 554 GLU GLU ALA LEU ALA LEU PRO ARG ASP PHE LEU LEU GLY
SEQRES 4 B 554 ALA TYR GLN THR GLU PHE PRO GLU GLY PRO THR GLU GLN
SEQRES 5 B 554 LEU MET LYS GLY LYS ILE THR PHE SER GLN TRP VAL PRO
SEQRES 6 B 554 LEU MET ASP GLU SER TYR ARG LYS SER SER LYS ALA CYS
SEQRES 7 B 554 GLY ALA ASN LEU PRO GLU ASN PHE SER ILE SER GLN ILE
SEQRES 8 B 554 PHE SER GLN ALA MET ALA ALA ARG SER ILE ASN ARG PRO
SEQRES 9 B 554 MET LEU GLN ALA ALA ILE ALA LEU LYS LYS LYS GLY PHE
SEQRES 10 B 554 THR THR CYS ILE VAL THR ASN ASN TRP LEU ASP ASP GLY
SEQRES 11 B 554 ASP LYS ARG ASP SER LEU ALA GLN MET MET CYS GLU LEU
SEQRES 12 B 554 SER GLN HIS PHE ASP PHE LEU ILE GLU SER CYS GLN VAL
SEQRES 13 B 554 GLY MET ILE LYS PRO GLU PRO GLN ILE TYR ASN PHE LEU
SEQRES 14 B 554 LEU ASP THR LEU LYS ALA LYS PRO ASN GLU VAL VAL PHE
SEQRES 15 B 554 LEU ASP ASP PHE GLY SER ASN LEU LYS PRO ALA ARG ASP
SEQRES 16 B 554 MET GLY MET VAL THR ILE LEU VAL HIS ASN THR ALA SER
SEQRES 17 B 554 ALA LEU ARG GLU LEU GLU LYS VAL THR GLY THR GLN PHE
SEQRES 18 B 554 PRO GLU ALA PRO LEU PRO VAL PRO CYS ASN PRO ASN ASP
SEQRES 19 B 554 VAL SER HIS GLY TYR VAL THR VAL LYS PRO GLY ILE ARG
SEQRES 20 B 554 LEU HIS PHE VAL GLU MET GLY SER GLY PRO ALA LEU CYS
SEQRES 21 B 554 LEU CYS HIS GLY PHE PRO GLU SER TRP PHE SER TRP ARG
SEQRES 22 B 554 TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY PHE ARG VAL
SEQRES 23 B 554 LEU ALA ILE ASP MET LYS GLY TYR GLY ASP SER SER SER
SEQRES 24 B 554 PRO PRO GLU ILE GLU GLU TYR ALA MET GLU LEU LEU CYS
SEQRES 25 B 554 LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY ILE PRO
SEQRES 26 B 554 GLN ALA VAL PHE ILE GLY HIS ASP TRP ALA GLY VAL MET
SEQRES 27 B 554 VAL TRP ASN MET ALA LEU PHE TYR PRO GLU ARG VAL ARG
SEQRES 28 B 554 ALA VAL ALA SER LEU ASN THR PRO PHE MET PRO PRO ASP
SEQRES 29 B 554 PRO ASP VAL SER PRO MET LYS VAL ILE ARG SER ILE PRO
SEQRES 30 B 554 VAL PHE ASN TYR GLN LEU TYR PHE GLN GLU PRO GLY VAL
SEQRES 31 B 554 ALA GLU ALA GLU LEU GLU LYS ASN MET SER ARG THR PHE
SEQRES 32 B 554 LYS SER PHE PHE ARG ALA SER ASP GLU THR GLY PHE ILE
SEQRES 33 B 554 ALA VAL HIS LYS ALA THR GLU ILE GLY GLY ILE LEU VAL
SEQRES 34 B 554 ASN THR PRO GLU ASP PRO ASN LEU SER LYS ILE THR THR
SEQRES 35 B 554 GLU GLU GLU ILE GLU PHE TYR ILE GLN GLN PHE LYS LYS
SEQRES 36 B 554 THR GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN THR
SEQRES 37 B 554 GLU ARG ASN TRP LYS TRP SER CYS LYS GLY LEU GLY ARG
SEQRES 38 B 554 LYS ILE LEU VAL PRO ALA LEU MET VAL THR ALA GLU LYS
SEQRES 39 B 554 ASP ILE VAL LEU ARG PRO GLU MET SER LYS ASN MET GLU
SEQRES 40 B 554 LYS TRP ILE PRO PHE LEU LYS ARG GLY HIS ILE GLU ASP
SEQRES 41 B 554 CYS GLY HIS TRP THR GLN ILE GLU LYS PRO THR GLU VAL
SEQRES 42 B 554 ASN GLN ILE LEU ILE LYS TRP LEU GLN THR GLU VAL GLN
SEQRES 43 B 554 ASN PRO SER VAL THR SER LYS ILE
FORMUL 3 HOH *40(H2 O1)
HELIX 1 1 SER A 93 ALA A 98 1 6
HELIX 2 2 ASN A 102 LYS A 115 1 14
HELIX 3 3 ARG A 133 SER A 144 1 12
HELIX 4 4 GLN A 145 PHE A 147 5 3
HELIX 5 5 SER A 153 GLY A 157 1 5
HELIX 6 6 GLU A 162 LYS A 174 1 13
HELIX 7 7 LEU A 190 MET A 196 1 7
HELIX 8 8 ALA A 207 VAL A 216 1 10
HELIX 9 9 SER A 268 ARG A 273 5 6
HELIX 10 10 TYR A 274 ALA A 282 1 9
HELIX 11 11 ILE A 303 TYR A 306 5 4
HELIX 12 12 ALA A 307 GLY A 323 1 17
HELIX 13 13 ASP A 333 TYR A 346 1 14
HELIX 14 14 SER A 368 ILE A 376 1 9
HELIX 15 15 PHE A 379 GLN A 386 1 8
HELIX 16 16 GLY A 389 ASN A 398 1 10
HELIX 17 17 ASN A 398 PHE A 407 1 10
HELIX 18 18 LYS A 420 GLY A 425 1 6
HELIX 19 19 THR A 442 GLY A 457 1 16
HELIX 20 20 PHE A 458 ASN A 463 1 6
HELIX 21 21 TRP A 464 ARG A 466 5 3
HELIX 22 22 ASN A 467 CYS A 476 1 10
HELIX 23 23 LYS A 477 LEU A 479 5 3
HELIX 24 24 ARG A 499 LYS A 504 5 6
HELIX 25 25 ASN A 505 TRP A 509 5 5
HELIX 26 26 TRP A 524 LYS A 529 1 6
HELIX 27 27 LYS A 529 GLU A 544 1 16
HELIX 28 28 SER B 18 ALA B 29 1 12
HELIX 29 29 LEU B 37 GLN B 42 1 6
HELIX 30 30 GLU B 47 MET B 54 1 8
HELIX 31 31 THR B 59 SER B 75 1 17
HELIX 32 32 ILE B 88 SER B 93 1 6
HELIX 33 33 SER B 93 ALA B 98 1 6
HELIX 34 34 ASN B 102 LYS B 115 1 14
HELIX 35 35 ARG B 133 SER B 144 1 12
HELIX 36 36 SER B 153 GLY B 157 1 5
HELIX 37 37 PRO B 163 LYS B 174 1 12
HELIX 38 38 LEU B 190 ASP B 195 1 6
HELIX 39 39 SER B 208 VAL B 216 1 9
HELIX 40 40 SER B 268 ARG B 273 5 6
HELIX 41 41 TYR B 274 ALA B 282 1 9
HELIX 42 42 ILE B 303 TYR B 306 5 4
HELIX 43 43 ALA B 307 GLY B 323 1 17
HELIX 44 44 ASP B 333 TYR B 346 1 14
HELIX 45 45 SER B 368 ILE B 376 1 9
HELIX 46 46 PHE B 379 GLN B 386 1 8
HELIX 47 47 GLY B 389 ASN B 398 1 10
HELIX 48 48 ASN B 398 PHE B 407 1 10
HELIX 49 49 THR B 442 GLY B 457 1 16
HELIX 50 50 PHE B 458 ASN B 463 1 6
HELIX 51 51 TRP B 464 ARG B 466 5 3
HELIX 52 52 ASN B 467 CYS B 476 1 10
HELIX 53 53 LYS B 477 LEU B 479 5 3
HELIX 54 54 ARG B 499 LYS B 504 5 6
HELIX 55 55 ASN B 505 TRP B 509 5 5
HELIX 56 56 TRP B 524 LYS B 529 1 6
HELIX 57 57 LYS B 529 GLU B 544 1 16
SHEET 1 A 5 PHE A 149 GLU A 152 0
SHEET 2 A 5 THR A 118 THR A 123 1 O THR A 119 N PHE A 149
SHEET 3 A 5 VAL A 5 PHE A 8 1 O ALA A 6 N CYS A 120
SHEET 4 A 5 VAL A 180 ASP A 184 1 O VAL A 181 N ALA A 7
SHEET 5 A 5 VAL A 199 LEU A 202 1 O VAL A 199 N PHE A 182
SHEET 1 B 2 ALA A 15 LEU A 16 0
SHEET 2 B 2 SER A 100 ILE A 101 -1 N SER A 100 O LEU A 16
SHEET 1 C 8 SER A 236 THR A 241 0
SHEET 2 C 8 ARG A 247 MET A 253 -1 O LEU A 248 N VAL A 240
SHEET 3 C 8 ARG A 285 ASP A 290 -1 N VAL A 286 O MET A 253
SHEET 4 C 8 ALA A 258 CYS A 262 1 O LEU A 259 N LEU A 287
SHEET 5 C 8 ALA A 327 HIS A 332 1 N VAL A 328 O ALA A 258
SHEET 6 C 8 VAL A 350 LEU A 356 1 N ARG A 351 O ALA A 327
SHEET 7 C 8 ALA A 487 ALA A 492 1 N LEU A 488 O VAL A 353
SHEET 8 C 8 LYS A 514 ILE A 518 1 N LYS A 514 O ALA A 487
SHEET 1 D 5 PHE B 149 GLU B 152 0
SHEET 2 D 5 THR B 118 THR B 123 1 O THR B 119 N PHE B 149
SHEET 3 D 5 VAL B 5 PHE B 8 1 N ALA B 6 O THR B 118
SHEET 4 D 5 VAL B 180 ASP B 184 1 O VAL B 181 N ALA B 7
SHEET 5 D 5 VAL B 199 LEU B 202 1 O VAL B 199 N PHE B 182
SHEET 1 E 2 ALA B 15 LEU B 16 0
SHEET 2 E 2 SER B 100 ILE B 101 -1 N SER B 100 O LEU B 16
SHEET 1 F 8 SER B 236 THR B 241 0
SHEET 2 F 8 ARG B 247 MET B 253 -1 O LEU B 248 N VAL B 240
SHEET 3 F 8 ARG B 285 ASP B 290 -1 N VAL B 286 O MET B 253
SHEET 4 F 8 ALA B 258 CYS B 262 1 O LEU B 259 N LEU B 287
SHEET 5 F 8 ALA B 327 HIS B 332 1 N VAL B 328 O ALA B 258
SHEET 6 F 8 VAL B 350 LEU B 356 1 N ARG B 351 O ALA B 327
SHEET 7 F 8 ALA B 487 ALA B 492 1 N LEU B 488 O VAL B 353
SHEET 8 F 8 LYS B 514 ILE B 518 1 N LYS B 514 O ALA B 487
CISPEP 1 LEU A 16 PRO A 17 0 0.51
CISPEP 2 LYS A 160 PRO A 161 0 -0.18
CISPEP 3 ASN A 231 PRO A 232 0 -1.54
CISPEP 4 GLY A 256 PRO A 257 0 -0.28
CISPEP 5 PHE A 265 PRO A 266 0 -0.87
CISPEP 6 LEU B 16 PRO B 17 0 -0.54
CISPEP 7 LYS B 160 PRO B 161 0 -0.39
CISPEP 8 ASN B 231 PRO B 232 0 -1.89
CISPEP 9 GLY B 256 PRO B 257 0 0.18
CISPEP 10 PHE B 265 PRO B 266 0 -1.11
CRYST1 151.900 143.000 60.000 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 0.006583 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006993 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016667 0.00000
END |