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HEADER HYDROLASE 12-JUL-99 1QE3
TITLE PNB ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PARA-NITROBENZYL ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PNB ESTERASE;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 BIOLOGICAL_UNIT: MONOMER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 OTHER_DETAILS: TEMPERATURE INDUCED
KEYWDS ALPHA-BETA HYDROLASE DIRECTED EVOLUTION
EXPDTA X-RAY DIFFRACTION
AUTHOR B.SPILLER,A.GERSHENSON,F.ARNOLD,R.STEVENS
REVDAT 2 27-OCT-99 1QE3 1 JRNL
REVDAT 1 21-JUL-99 1QE3 0
JRNL AUTH B.SPILLER,A.GERSHENSON,F.H.ARNOLD,R.C.STEVENS
JRNL TITL A STRUCTURAL ANALYSIS OF EVOLUTIONARY DIVERGENCE
JRNL REF PROC.NAT.ACAD.SCI.USA V. 96 12305 1999
JRNL REFN ASTM PNASA6 US ISSN 0027-8424 0040
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 83.7
REMARK 3 NUMBER OF REFLECTIONS : 73015
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, THROUGHOUT
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 7353
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 : 3643
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 352
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.10
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) : 1.300
REMARK 3 BOND ANGLES (DEGREES) : 0.01
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 0.37 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 0.36 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.68 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 0.60 ; 2.500
REMARK 3
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 1QE3 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-1999.
REMARK 100 THE RCSB ID CODE IS RCSB009331.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-1998
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.25
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : QUANTA
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86234
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
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: SOLVE
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: 28% PEG 4000, 150 LIS04,100MM
REMARK 280 TRIS
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 33.62050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.78750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.35700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.78750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.62050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.35700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 ASP A 66
REMARK 465 LEU A 67
REMARK 465 LEU A 68
REMARK 465 SER A 69
REMARK 465 LEU A 70
REMARK 465 SER A 71
REMARK 465 TYR A 72
REMARK 465 THR A 73
REMARK 465 GLU A 74
REMARK 465 GLU A 414
REMARK 465 ARG A 415
REMARK 465 MET A 416
REMARK 465 ALA A 417
REMARK 465 LYS A 418
REMARK 465 ALA A 419
REMARK 465 GLU A 420
REMARK 465 PRO A 485
REMARK 465 SER A 486
REMARK 465 LYS A 487
REMARK 465 GLY A 488
REMARK 465 GLU A 489
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 4*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 2 N - CA - C ANGL. DEV. = 6.6 DEGREES
REMARK 500 GLN A 4 N - CA - C ANGL. DEV. = 11.5 DEGREES
REMARK 500 ILE A 5 N - CA - C ANGL. DEV. = -7.8 DEGREES
REMARK 500 THR A 8 N - CA - C ANGL. DEV. = -6.7 DEGREES
REMARK 500 HIS A 22 N - CA - C ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP A 24 N - CA - C ANGL. DEV. = -7.1 DEGREES
REMARK 500 ARG A 38 N - CA - C ANGL. DEV. = -6.3 DEGREES
REMARK 500 LEU A 75 CA - CB - CG ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 81 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 PRO A 98 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 PHE A 108 N - CA - C ANGL. DEV. = 5.6 DEGREES
REMARK 500 GLY A 111 N - CA - C ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP A 119 N - CA - C ANGL. DEV. = -5.4 DEGREES
REMARK 500 GLY A 120 N - CA - C ANGL. DEV. = 6.8 DEGREES
REMARK 500 PHE A 143 N - CA - C ANGL. DEV. = 5.4 DEGREES
REMARK 500 LEU A 144 N - CA - C ANGL. DEV. =-12.9 DEGREES
REMARK 500 LEU A 146 N - CA - C ANGL. DEV. = 5.9 DEGREES
REMARK 500 GLU A 171 N - CA - C ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASN A 172 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 ILE A 173 N - CA - C ANGL. DEV. = 6.4 DEGREES
REMARK 500 VAL A 185 N - CA - C ANGL. DEV. = -5.4 DEGREES
REMARK 500 MET A 201 N - CA - C ANGL. DEV. = 6.6 DEGREES
REMARK 500 MET A 201 CB - CG - SD ANGL. DEV. = -7.6 DEGREES
REMARK 500 GLN A 209 N - CA - C ANGL. DEV. = 6.6 DEGREES
REMARK 500 MET A 221 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 GLU A 241 N - CA - C ANGL. DEV. = 5.8 DEGREES
REMARK 500 LEU A 279 N - CA - C ANGL. DEV. = -5.3 DEGREES
REMARK 500 LYS A 282 N - CA - C ANGL. DEV. = 5.6 DEGREES
REMARK 500 THR A 283 N - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 PRO A 285 N - CA - C ANGL. DEV. = 6.6 DEGREES
REMARK 500 GLY A 295 N - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 GLY A 299 N - CA - C ANGL. DEV. = 6.0 DEGREES
REMARK 500 LEU A 303 N - CA - C ANGL. DEV. =-10.0 DEGREES
REMARK 500 THR A 307 N - CA - C ANGL. DEV. = -7.2 DEGREES
REMARK 500 GLY A 311 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 HIS A 322 N - CA - C ANGL. DEV. = 6.9 DEGREES
REMARK 500 SER A 323 N - CA - C ANGL. DEV. =-11.3 DEGREES
REMARK 500 GLY A 336 N - CA - C ANGL. DEV. = -7.1 DEGREES
REMARK 500 TYR A 347 N - CA - C ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 360 N - CA - C ANGL. DEV. = 6.3 DEGREES
REMARK 500 LEU A 361 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 PHE A 363 N - CA - C ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 384 N - CA - C ANGL. DEV. = -9.6 DEGREES
REMARK 500 ASP A 386 N - CA - C ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 387 N - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 PRO A 393 C - N - CA ANGL. DEV. = 5.4 DEGREES
REMARK 500 ALA A 397 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 HIS A 399 N - CA - C ANGL. DEV. = -6.1 DEGREES
REMARK 500 ALA A 400 N - CA - C ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASN A 409 N - CA - C ANGL. DEV. = -5.6 DEGREES
REMARK 500 LEU A 410 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 THR A 442 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASN A 444 N - CA - C ANGL. DEV. = -7.1 DEGREES
REMARK 500 THR A 447 N - CA - C ANGL. DEV. = -5.4 DEGREES
REMARK 500 ASN A 451 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 GLU A 457 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 ASP A 466 N - CA - C ANGL. DEV. = -5.5 DEGREES
REMARK 500 GLU A 468 N - CA - C ANGL. DEV. = -6.1 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 SER A 323 144.19 87.41
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QE3 RELATED DB: PDB
REMARK 900 WILD TYPE PNB ESTERASE
REMARK 900 RELATED ID: 1QE8 RELATED DB: PDB
REMARK 900 PNB ESTERASE, 9 MUTATIONS
REMARK 900 RELATED ID: 1C00 RELATED DB: PDB
REMARK 900 PNB ESTERASE, 13 MUTATIONS
DBREF 1QE3 A 1 489 SWS P37967 PNBA_BACSU 1 489
SEQRES 1 A 489 MET THR HIS GLN ILE VAL THR THR GLN TYR GLY LYS VAL
SEQRES 2 A 489 LYS GLY THR THR GLU ASN GLY VAL HIS LYS TRP LYS GLY
SEQRES 3 A 489 ILE PRO TYR ALA LYS PRO PRO VAL GLY GLN TRP ARG PHE
SEQRES 4 A 489 LYS ALA PRO GLU PRO PRO GLU VAL TRP GLU ASP VAL LEU
SEQRES 5 A 489 ASP ALA THR ALA TYR GLY PRO ILE CYS PRO GLN PRO SER
SEQRES 6 A 489 ASP LEU LEU SER LEU SER TYR THR GLU LEU PRO ARG GLN
SEQRES 7 A 489 SER GLU ASP CYS LEU TYR VAL ASN VAL PHE ALA PRO ASP
SEQRES 8 A 489 THR PRO SER GLN ASN LEU PRO VAL MET VAL TRP ILE HIS
SEQRES 9 A 489 GLY GLY ALA PHE TYR LEU GLY ALA GLY SER GLU PRO LEU
SEQRES 10 A 489 TYR ASP GLY SER LYS LEU ALA ALA GLN GLY GLU VAL ILE
SEQRES 11 A 489 VAL VAL THR LEU ASN TYR ARG LEU GLY PRO PHE GLY PHE
SEQRES 12 A 489 LEU HIS LEU SER SER PHE ASP GLU ALA TYR SER ASP ASN
SEQRES 13 A 489 LEU GLY LEU LEU ASP GLN ALA ALA ALA LEU LYS TRP VAL
SEQRES 14 A 489 ARG GLU ASN ILE SER ALA PHE GLY GLY ASP PRO ASP ASN
SEQRES 15 A 489 VAL THR VAL PHE GLY GLU SER ALA GLY GLY MET SER ILE
SEQRES 16 A 489 ALA ALA LEU LEU ALA MET PRO ALA ALA LYS GLY LEU PHE
SEQRES 17 A 489 GLN LYS ALA ILE MET GLU SER GLY ALA SER ARG THR MET
SEQRES 18 A 489 THR LYS GLU GLN ALA ALA SER THR ALA ALA ALA PHE LEU
SEQRES 19 A 489 GLN VAL LEU GLY ILE ASN GLU SER GLN LEU ASP ARG LEU
SEQRES 20 A 489 HIS THR VAL ALA ALA GLU ASP LEU LEU LYS ALA ALA ASP
SEQRES 21 A 489 GLN LEU ARG ILE ALA GLU LYS GLU ASN ILE PHE GLN LEU
SEQRES 22 A 489 PHE PHE GLN PRO ALA LEU ASP PRO LYS THR LEU PRO GLU
SEQRES 23 A 489 GLU PRO GLU LYS SER ILE ALA GLU GLY ALA ALA SER GLY
SEQRES 24 A 489 ILE PRO LEU LEU ILE GLY THR THR ARG ASP GLU GLY TYR
SEQRES 25 A 489 LEU PHE PHE THR PRO ASP SER ASP VAL HIS SER GLN GLU
SEQRES 26 A 489 THR LEU ASP ALA ALA LEU GLU TYR LEU LEU GLY LYS PRO
SEQRES 27 A 489 LEU ALA GLU LYS ALA ALA ASP LEU TYR PRO ARG SER LEU
SEQRES 28 A 489 GLU SER GLN ILE HIS MET MET THR ASP LEU LEU PHE TRP
SEQRES 29 A 489 ARG PRO ALA VAL ALA TYR ALA SER ALA GLN SER HIS TYR
SEQRES 30 A 489 ALA PRO VAL TRP MET TYR ARG PHE ASP TRP HIS PRO GLU
SEQRES 31 A 489 LYS PRO PRO TYR ASN LYS ALA PHE HIS ALA LEU GLU LEU
SEQRES 32 A 489 PRO PHE VAL PHE GLY ASN LEU ASP GLY LEU GLU ARG MET
SEQRES 33 A 489 ALA LYS ALA GLU ILE THR ASP GLU VAL LYS GLN LEU SER
SEQRES 34 A 489 HIS THR ILE GLN SER ALA TRP ILE THR PHE ALA LYS THR
SEQRES 35 A 489 GLY ASN PRO SER THR GLU ALA VAL ASN TRP PRO ALA TYR
SEQRES 36 A 489 HIS GLU GLU THR ARG GLU THR VAL ILE LEU ASP SER GLU
SEQRES 37 A 489 ILE THR ILE GLU ASN ASP PRO GLU SER GLU LYS ARG GLN
SEQRES 38 A 489 LYS LEU PHE PRO SER LYS GLY GLU
HET SO4 485 5
HET ZN A 500 1
HETNAM SO4 SULFATE ION
HETNAM ZN ZINC ION
FORMUL 2 SO4 O4 S1 2-
FORMUL 3 ZN ZN1 2+
FORMUL 4 HOH *352(H2 O1)
HELIX 1 1 VAL A 34 ARG A 38 5 5
HELIX 2 2 GLU A 115 ASP A 119 5 5
HELIX 3 3 GLY A 120 GLU A 128 1 9
HELIX 4 4 LEU A 138 PHE A 143 1 6
HELIX 5 5 ASN A 156 ILE A 173 1 18
HELIX 6 6 SER A 174 PHE A 176 5 3
HELIX 7 7 SER A 189 LEU A 199 1 11
HELIX 8 8 MET A 201 LYS A 205 5 5
HELIX 9 9 THR A 222 GLY A 238 1 17
HELIX 10 10 GLN A 243 THR A 249 5 7
HELIX 11 11 ALA A 251 ILE A 264 1 14
HELIX 12 12 GLU A 287 GLU A 294 1 8
HELIX 13 13 ASP A 309 PHE A 314 5 6
HELIX 14 14 SER A 323 GLY A 336 1 14
HELIX 15 15 GLY A 336 ALA A 344 1 9
HELIX 16 16 ASP A 345 TYR A 347 5 3
HELIX 17 17 SER A 350 PHE A 363 1 14
HELIX 18 18 PHE A 363 SER A 375 1 13
HELIX 19 19 GLU A 402 GLY A 408 1 7
HELIX 20 20 THR A 422 GLY A 443 1 22
HELIX 21 21 GLU A 476 PHE A 484 1 9
SHEET 1 A 3 ILE A 5 THR A 8 0
SHEET 2 A 3 GLY A 11 LYS A 14 -1 O GLY A 11 N THR A 8
SHEET 3 A 3 VAL A 51 ASP A 53 1 O LEU A 52 N LYS A 14
SHEET 1 B11 THR A 16 GLU A 18 0
SHEET 2 B11 VAL A 21 PRO A 28 -1 O VAL A 21 N GLU A 18
SHEET 3 B11 TYR A 84 PRO A 90 -1 N VAL A 85 O ILE A 27
SHEET 4 B11 ILE A 130 LEU A 134 -1 N VAL A 131 O PHE A 88
SHEET 5 B11 LEU A 97 ILE A 103 1 O PRO A 98 N ILE A 130
SHEET 6 B11 GLY A 178 GLU A 188 1 N ASP A 179 O LEU A 97
SHEET 7 B11 LYS A 210 GLU A 214 1 O LYS A 210 N VAL A 185
SHEET 8 B11 LEU A 302 THR A 307 1 O LEU A 303 N MET A 213
SHEET 9 B11 VAL A 380 PHE A 385 1 O TRP A 381 N ILE A 304
SHEET 10 B11 GLU A 461 LEU A 465 1 O GLU A 461 N MET A 382
SHEET 11 B11 THR A 470 ASN A 473 -1 O THR A 470 N ILE A 464
CISPEP 1 PRO A 392 PRO A 393 0 0.71
CRYST1 67.241 80.714 99.575 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 0.014870 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012390 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010040 0.00000 |