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HEADER HYDROLASE 27-MAR-04 1VE7
TITLE CRYSTAL STRUCTURE OF AN ACYLPEPTIDE HYDROLASE/ESTERASE FROM
TITLE 2 AEROPYRUM PERNIX K1 IN COMPLEX WITH P-NITROPHENYL PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYLAMINO-ACID-RELEASING ENZYME;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: AARE, ACYL-PEPTIDE HYDROLASE, APH, ACYLAMINOACYL-
COMPND 5 PEPTIDASE;
COMPND 6 EC: 3.4.19.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;
SOURCE 3 ORGANISM_COMMON: ARCHAEA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA
KEYWDS BETA PROPELLER DOMAIN, ALPHA/BETA HYDROLASE DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BARTLAM,G.WANG,R.GAO,H.YANG,X.ZHAO,G.XIE,S.CAO,Y.FENG,
AUTHOR 2 Z.RAO
REVDAT 1 02-NOV-04 1VE7 0
JRNL AUTH M.BARTLAM,G.WANG,H.YANG,R.GAO,X.ZHAO,G.XIE,S.CAO,
JRNL AUTH 2 Y.FENG,Z.RAO
JRNL TITL CRYSTAL STRUCTURE OF AN ACYLPEPTIDE
JRNL TITL 2 HYDROLASE/ESTERASE FROM AEROPYRUM PERNIX K1
JRNL REF STRUCTURE V. 12 1481 2004
JRNL REFN ASTM STRUE6 UK ISSN 0969-2126
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 30134
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) : 0.207
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1555
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2760
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 254
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8730
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 193
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.25
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.45
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.70
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.04
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) : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 1VE7 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-APR-2004.
REMARK 100 THE RCSB ID CODE IS RCSB006517.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-SEP-2003
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
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 : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31768
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : 0.10000
REMARK 200 FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.37700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1VE6
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: PEG 4000, NAAC, DTT, EDTA, PH 4.6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-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 31.94150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.00200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.31100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.00200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.94150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.31100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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
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 350 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 ARG A 2
REMARK 465 ILE A 3
REMARK 465 ILE A 4
REMARK 465 MET A 5
REMARK 465 PRO A 6
REMARK 465 VAL A 7
REMARK 465 GLU A 8
REMARK 465 ARG A 582
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 ILE B 3
REMARK 465 ILE B 4
REMARK 465 MET B 5
REMARK 465 PRO B 6
REMARK 465 VAL B 7
REMARK 465 GLU B 8
REMARK 465 ARG B 582
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 394 SD MET A 394 CE -0.064
REMARK 500 MET A 477 SD MET A 477 CE -0.065
REMARK 500 ARG A 526 CG ARG A 526 CD -0.063
REMARK 500 MET A 561 SD MET A 561 CE 0.130
REMARK 500 MET B 477 SD MET B 477 CE -0.125
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 PHE A 41 N - CA - C ANGL. DEV. =-13.5 DEGREES
REMARK 500 LEU A 50 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 GLN A 89 N - CA - C ANGL. DEV. =-13.0 DEGREES
REMARK 500 ALA A 91 N - CA - C ANGL. DEV. =-12.5 DEGREES
REMARK 500 VAL A 134 N - CA - C ANGL. DEV. =-16.3 DEGREES
REMARK 500 ARG A 188 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 LYS A 207 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 LEU A 335 N - CA - C ANGL. DEV. =-10.1 DEGREES
REMARK 500 GLN B 89 N - CA - C ANGL. DEV. =-14.2 DEGREES
REMARK 500 THR B 130 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 VAL B 134 N - CA - C ANGL. DEV. =-15.2 DEGREES
REMARK 500 GLU B 231 N - CA - C ANGL. DEV. =-10.3 DEGREES
REMARK 500 GLY B 257 N - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500 VAL B 471 N - CA - C ANGL. DEV. =-11.0 DEGREES
REMARK 500 GLU B 547 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 GLU B 580 N - CA - C ANGL. DEV. =-10.8 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
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 SER B 445 -115.46 61.12
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VE6 RELATED DB: PDB
REMARK 900 NATIVE ENZYME
DBREF 1VE7 A 1 582 SWS Q9YBQ2 APEH_AERPE 1 582
DBREF 1VE7 B 1 582 SWS Q9YBQ2 APEH_AERPE 1 582
SEQRES 1 A 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 A 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 A 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 A 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 A 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 A 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 A 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 A 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 A 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 A 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 A 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 A 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 A 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 A 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 A 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 A 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 A 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 A 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 A 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 A 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 A 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 A 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 A 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 A 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 A 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 A 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 A 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 A 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 A 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 A 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 A 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 A 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 A 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 A 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 A 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 A 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 A 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 A 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 A 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 A 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 A 582 PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 A 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 A 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 A 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 A 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
SEQRES 1 B 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 B 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 B 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 B 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 B 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 B 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 B 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 B 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 B 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 B 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 B 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 B 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 B 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 B 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 B 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 B 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 B 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 B 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 B 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 B 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 B 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 B 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 B 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 B 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 B 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 B 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 B 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 B 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 B 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 B 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 B 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 B 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 B 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 B 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 B 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 B 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 B 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 B 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 B 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 B 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 B 582 PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 B 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 B 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 B 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 B 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
HET 4NP 701 14
HET 4NP 1701 14
HET GOL 751 6
HETNAM 4NP 4-NITROPHENYL PHOSPHATE
HETNAM GOL GLYCEROL
FORMUL 3 4NP 2(C6 H6 N1 O6 P1)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *187(H2 O1)
HELIX 1 1 SER A 10 VAL A 22 1 13
HELIX 2 2 ASP A 239 TYR A 243 5 5
HELIX 3 3 PRO A 323 SER A 329 1 7
HELIX 4 4 ASP A 379 ALA A 388 1 10
HELIX 5 5 GLY A 404 LYS A 410 1 7
HELIX 6 6 GLY A 417 SER A 433 1 17
HELIX 7 7 SER A 445 LYS A 458 1 14
HELIX 8 8 ASP A 473 LEU A 480 1 8
HELIX 9 9 ASP A 482 GLY A 494 1 13
HELIX 10 10 SER A 496 ARG A 503 1 8
HELIX 11 11 SER A 504 ILE A 512 5 9
HELIX 12 12 PRO A 528 ARG A 542 1 15
HELIX 13 13 THR A 560 GLU A 580 1 21
HELIX 14 14 SER B 10 VAL B 22 1 13
HELIX 15 15 LYS B 238 ARG B 244 1 7
HELIX 16 16 PRO B 323 ARG B 328 1 6
HELIX 17 17 ASP B 379 ALA B 388 1 10
HELIX 18 18 GLY B 404 LYS B 410 1 7
HELIX 19 19 GLY B 417 SER B 433 1 17
HELIX 20 20 SER B 445 LYS B 458 1 14
HELIX 21 21 ASP B 473 SER B 481 1 9
HELIX 22 22 ASP B 482 GLY B 494 1 13
HELIX 23 23 SER B 496 ARG B 503 1 8
HELIX 24 24 SER B 504 ILE B 512 5 9
HELIX 25 25 LEU B 529 ARG B 542 1 14
HELIX 26 26 THR B 560 ARG B 579 1 20
SHEET 1 A 4 LYS A 24 VAL A 31 0
SHEET 2 A 4 LYS A 35 PHE A 41 -1 O LEU A 37 N GLY A 29
SHEET 3 A 4 VAL A 46 TYR A 51 -1 O TYR A 49 N VAL A 38
SHEET 4 A 4 THR A 56 LYS A 58 -1 O VAL A 57 N LEU A 50
SHEET 1 B 4 SER A 66 VAL A 67 0
SHEET 2 B 4 ARG A 76 ASP A 82 -1 O VAL A 80 N SER A 66
SHEET 3 B 4 HIS A 90 ASN A 96 -1 O PHE A 93 N LEU A 79
SHEET 4 B 4 GLN A 104 ARG A 105 -1 O GLN A 104 N LYS A 94
SHEET 1 C 5 ASP A 69 PRO A 70 0
SHEET 2 C 5 ARG A 113 ASP A 119 1 O ASP A 119 N ASP A 69
SHEET 3 C 5 VAL A 124 ALA A 129 -1 O VAL A 125 N VAL A 118
SHEET 4 C 5 VAL A 134 ASP A 140 -1 O TYR A 137 N PHE A 126
SHEET 5 C 5 GLY A 143 LEU A 150 -1 O LEU A 150 N VAL A 134
SHEET 1 D 4 GLY A 154 ARG A 160 0
SHEET 2 D 4 LEU A 163 GLY A 171 -1 O ALA A 165 N SER A 157
SHEET 3 D 4 ARG A 174 ASN A 181 -1 O SER A 176 N GLY A 168
SHEET 4 D 4 GLY A 185 PHE A 190 -1 O PHE A 190 N LEU A 177
SHEET 1 E 4 GLY A 195 ILE A 202 0
SHEET 2 E 4 VAL A 208 THR A 214 -1 O GLU A 213 N SER A 196
SHEET 3 E 4 ALA A 218 VAL A 223 -1 O ARG A 219 N LEU A 212
SHEET 4 E 4 VAL A 230 ASP A 232 -1 O GLU A 231 N THR A 222
SHEET 1 F 4 ALA A 247 TYR A 253 0
SHEET 2 F 4 LEU A 259 ARG A 265 -1 O ALA A 260 N GLY A 252
SHEET 3 F 4 ARG A 268 ILE A 273 -1 O PHE A 272 N VAL A 261
SHEET 4 F 4 GLU A 276 VAL A 278 -1 O VAL A 278 N VAL A 271
SHEET 1 G 3 ASN A 284 HIS A 285 0
SHEET 2 G 3 LYS A 294 SER A 301 -1 O THR A 300 N ASN A 284
SHEET 3 G 3 VAL A 289 TRP A 291 -1 N TRP A 291 O LYS A 294
SHEET 1 H 4 ASN A 284 HIS A 285 0
SHEET 2 H 4 LYS A 294 SER A 301 -1 O THR A 300 N ASN A 284
SHEET 3 H 4 THR A 304 LEU A 311 -1 O THR A 304 N SER A 301
SHEET 4 H 4 PRO A 316 LEU A 318 -1 O LEU A 317 N ILE A 308
SHEET 1 I16 ILE A 330 GLU A 339 0
SHEET 2 I16 ARG A 345 SER A 353 -1 O THR A 348 N VAL A 336
SHEET 3 I16 HIS A 391 PRO A 395 -1 O MET A 394 N TYR A 349
SHEET 4 I16 GLY A 360 VAL A 366 1 N PRO A 361 O HIS A 391
SHEET 5 I16 ALA A 436 TYR A 444 1 O TYR A 440 N VAL A 364
SHEET 6 I16 ALA A 464 GLY A 468 1 O GLY A 468 N GLY A 443
SHEET 7 I16 LEU A 516 PRO A 521 1 O ILE A 519 N ALA A 467
SHEET 8 I16 PHE A 546 ILE A 551 1 O HIS A 549 N LEU A 518
SHEET 9 I16 PHE B 546 ILE B 551 -1 O ILE B 550 N ALA A 548
SHEET 10 I16 LEU B 516 PRO B 521 1 N LEU B 518 O GLU B 547
SHEET 11 I16 GLY B 465 GLY B 468 1 N GLY B 465 O ALA B 517
SHEET 12 I16 ALA B 436 TYR B 444 1 N ILE B 441 O VAL B 466
SHEET 13 I16 GLY B 360 VAL B 366 1 N THR B 362 O GLU B 438
SHEET 14 I16 HIS B 391 PRO B 395 1 O HIS B 391 N VAL B 363
SHEET 15 I16 ARG B 345 SER B 353 -1 N TYR B 349 O MET B 394
SHEET 16 I16 ILE B 330 GLU B 339 -1 N VAL B 336 O THR B 348
SHEET 1 J 4 LYS B 24 VAL B 31 0
SHEET 2 J 4 LYS B 35 PHE B 41 -1 O LYS B 35 N VAL B 31
SHEET 3 J 4 VAL B 46 TYR B 51 -1 O TYR B 49 N VAL B 38
SHEET 4 J 4 THR B 56 LYS B 58 -1 O VAL B 57 N LEU B 50
SHEET 1 K 4 SER B 66 VAL B 67 0
SHEET 2 K 4 ARG B 76 ASP B 82 -1 O VAL B 80 N SER B 66
SHEET 3 K 4 HIS B 90 ASN B 96 -1 O PHE B 93 N LEU B 79
SHEET 4 K 4 ARG B 99 ARG B 105 -1 O GLN B 104 N LYS B 94
SHEET 1 L 5 ASP B 69 PRO B 70 0
SHEET 2 L 5 ARG B 113 ASP B 119 1 O ASP B 119 N ASP B 69
SHEET 3 L 5 VAL B 124 THR B 130 -1 O VAL B 125 N VAL B 118
SHEET 4 L 5 ARG B 133 ASP B 140 -1 O TYR B 137 N PHE B 126
SHEET 5 L 5 GLY B 143 LEU B 150 -1 O ALA B 148 N LEU B 136
SHEET 1 M 4 GLY B 154 ARG B 160 0
SHEET 2 M 4 LEU B 163 GLY B 171 -1 O LEU B 167 N PHE B 155
SHEET 3 M 4 ARG B 174 ASN B 181 -1 O PHE B 178 N GLY B 166
SHEET 4 M 4 GLY B 185 PHE B 190 -1 O PHE B 190 N LEU B 177
SHEET 1 N 4 GLY B 195 ILE B 202 0
SHEET 2 N 4 VAL B 208 THR B 214 -1 O GLU B 213 N SER B 196
SHEET 3 N 4 ALA B 218 VAL B 223 -1 O VAL B 223 N VAL B 208
SHEET 4 N 4 VAL B 230 ASP B 232 -1 O GLU B 231 N THR B 222
SHEET 1 O 4 ALA B 247 TYR B 253 0
SHEET 2 O 4 LEU B 259 ARG B 265 -1 O ARG B 264 N ALA B 247
SHEET 3 O 4 ARG B 268 ILE B 273 -1 O ARG B 268 N ARG B 265
SHEET 4 O 4 GLU B 276 VAL B 278 -1 O GLU B 276 N ILE B 273
SHEET 1 P 3 ASN B 284 HIS B 285 0
SHEET 2 P 3 LEU B 295 SER B 301 -1 O THR B 300 N ASN B 284
SHEET 3 P 3 VAL B 289 LEU B 290 -1 N VAL B 289 O VAL B 296
SHEET 1 Q 4 ASN B 284 HIS B 285 0
SHEET 2 Q 4 LEU B 295 SER B 301 -1 O THR B 300 N ASN B 284
SHEET 3 Q 4 THR B 304 LEU B 311 -1 O LEU B 311 N LEU B 295
SHEET 4 Q 4 PRO B 316 LEU B 318 -1 O LEU B 318 N ILE B 308
SSBOND 1 CYS A 416 CYS A 453
SSBOND 2 CYS B 416 CYS B 453
CISPEP 1 LEU A 311 PRO A 312 0 0.35
CISPEP 2 THR A 358 PRO A 359 0 0.23
CISPEP 3 GLY A 369 PRO A 370 0 0.50
CISPEP 4 LEU B 311 PRO B 312 0 0.69
CISPEP 5 THR B 358 PRO B 359 0 -0.33
CISPEP 6 GLY B 369 PRO B 370 0 0.46
CRYST1 63.883 104.622 168.004 90.00 90.00 90.00 P 21 21 21 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 0.015654 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009558 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005952 0.00000
TER 4366 ARG A 581
TER 8732 ARG B 581
MASTER 305 0 3 26 80 0 0 6 8951 2 38 90
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