longtext: 1C7J-pdb

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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