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HEADER HYDROLASE 21-FEB-00 1C7J
TITLE PNB ESTERASE 56C8
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 MUTATION: YES
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
KEYWDS ALPHA-BETA HYDROLASE, DIRECTED EVOLUTION, ORGANIC ACTIVITY,
KEYWDS 2 PNB ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.SPILLER,A.GERSHENSON,F.ARNOLD,R.C.STEVENS
REVDAT 1 29-MAR-00 1C7J 0
SPRSDE 29-MAR-00 1C7J 1QE8
JRNL AUTH B.SPILLER,A.GERSHENSON,F.H.ARNOLD,R.C.STEVENS
JRNL TITL A STRUCTURAL VIEW OF EVOLUTIONARY DIVERGENCE
JRNL REF PROC.NAT.ACAD.SCI.USA V. 96 12305 1999
JRNL REFN ASTM PNASA6 US ISSN 0027-8424
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.6 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
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) (%) : 89.0
REMARK 3 NUMBER OF REFLECTIONS : 64813
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) : 0.214
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 6566
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 : 3774
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.70
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.80
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 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 1C7J COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-2000.
REMARK 100 THE RCSB ID CODE IS RCSB001432.
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 : 8.40
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 : 67818
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
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 (%) : 93.0
REMARK 200 DATA REDUNDANCY : 8.900
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 40.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 61.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.31800
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: 29% PEG 4000, 100MM TRIS, 175
REMARK 280 LISO4, 10MM DMF
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 33.75350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.41850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.91650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.41850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.75350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.91650
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 1 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 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 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 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 THR A 2 CA THR A 2 N 0.030
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 GLN A 4 N - CA - C ANGL. DEV. = 11.2 DEGREES
REMARK 500 PRO A 64 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASP A 81 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 MET A 144 N - CA - C ANGL. DEV. =-12.2 DEGREES
REMARK 500 ASN A 172 N - CA - C ANGL. DEV. = 8.7 DEGREES
REMARK 500 MET A 221 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 500 THR A 283 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 GLY A 295 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 LEU A 303 N - CA - C ANGL. DEV. =-10.2 DEGREES
REMARK 500 GLY A 311 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 ARG A 384 N - CA - C ANGL. DEV. = -9.4 DEGREES
REMARK 500 THR A 442 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASN A 451 N - CA - C ANGL. DEV. =-10.7 DEGREES
REMARK 500 GLU A 457 N - CA - C ANGL. DEV. = 8.2 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 A 189 58.86 -119.53
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QE3 RELATED DB: PDB
REMARK 900 WILD TYPE PNB ESTERASE
REMARK 900 RELATED ID: 1C7I RELATED DB: PDB
REMARK 900 PNB ESTERASE, 13 MUTATIONS
DBREF 1C7J A 1 489 SWS P37967 PNBA_BACSU 1 489
SEQADV 1C7J VAL A 60 SWS P37967 ILE 60 ENGINEERED
SEQADV 1C7J MET A 144 SWS P37967 LEU 144 ENGINEERED
SEQADV 1C7J SER A 317 SWS P37967 PRO 317 ENGINEERED
SEQADV 1C7J ARG A 322 SWS P37967 HIS 322 ENGINEERED
SEQADV 1C7J SER A 334 SWS P37967 LEU 334 ENGINEERED
SEQADV 1C7J VAL A 358 SWS P37967 MET 358 ENGINEERED
SEQADV 1C7J PHE A 370 SWS P37967 TYR 370 ENGINEERED
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 VAL 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 MET 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 SER ASP SER ASP VAL ARG SER GLN GLU
SEQRES 26 A 489 THR LEU ASP ALA ALA LEU GLU TYR SER 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 VAL THR ASP LEU LEU PHE TRP
SEQRES 29 A 489 ARG PRO ALA VAL ALA PHE 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 487 5
HET K A 500 1
HETNAM SO4 SULFATE ION
HETNAM K POTASSIUM ION
FORMUL 2 SO4 O4 S1 2-
FORMUL 3 K K1 1+
FORMUL 4 HOH *270(H2 O1)
HELIX 1 1 VAL A 34 ARG A 38 5 5
HELIX 2 2 LEU A 67 TYR A 72 1 6
HELIX 3 3 GLU A 115 ASP A 119 5 5
HELIX 4 4 GLY A 120 GLU A 128 1 9
HELIX 5 5 LEU A 138 PHE A 143 1 6
HELIX 6 6 ASN A 156 ILE A 173 1 18
HELIX 7 7 SER A 174 PHE A 176 5 3
HELIX 8 8 SER A 189 LEU A 199 1 11
HELIX 9 9 MET A 201 LYS A 205 5 5
HELIX 10 10 THR A 222 GLY A 238 1 17
HELIX 11 11 GLN A 243 THR A 249 5 7
HELIX 12 12 ALA A 251 GLU A 266 1 16
HELIX 13 13 GLU A 287 GLU A 294 1 8
HELIX 14 14 ASP A 309 PHE A 314 5 6
HELIX 15 15 SER A 323 LEU A 335 1 13
HELIX 16 16 LYS A 337 LYS A 342 1 6
HELIX 17 17 ALA A 343 TYR A 347 5 5
HELIX 18 18 SER A 350 PHE A 363 1 14
HELIX 19 19 PHE A 363 SER A 375 1 13
HELIX 20 20 GLU A 402 GLY A 408 1 7
HELIX 21 21 ASP A 411 LYS A 418 1 8
HELIX 22 22 THR A 422 GLY A 443 1 22
HELIX 23 23 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 N LEU A 52 O LYS A 12
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 N VAL A 463 O 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 0.03
CRYST1 67.507 81.833 98.837 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 0.014810 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012220 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010120 0.00000 |