longtext: 2OCG-pdb

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HEADER    HYDROLASE                               20-DEC-06   2OCG
TITLE     CRYSTAL STRUCTURE OF HUMAN VALACYCLOVIR HYDROLASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: VALACYCLOVIR HYDROLASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 38-291;
COMPND   5 SYNONYM: VACVASE, BIPHENYL HYDROLASE-LIKE PROTEIN,
COMPND   6 BIPHENYL HYDROLASE-RELATED PROTEIN, BPH-RP, BREAST
COMPND   7 EPITHELIAL MUCIN-ASSOCIATED ANTIGEN, MCNAA;
COMPND   8 EC: 3.1.-.-;
COMPND   9 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 GENE: BPHL;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET17B
KEYWDS    ALPHA BETA HYDROLASE FOLD
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.LAI,Z.XU,G.L.AMIDON
REVDAT   1   05-FEB-08 2OCG    0
JRNL        AUTH   L.LAI,Z.XU,J.ZHOU,G.L.AMIDON
JRNL        TITL   MOLECULAR BASIS OF PRODRUG ACTIVATION BY HUMAN
JRNL        TITL 2 VALACYCLOVIR HYDROLASE: A NEW DRUG DELIVERY TARGET
JRNL        TITL 3 FOR IMPROVING ORAL ABSORPTION
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. 1.75 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) : 1.75
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.49
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)   (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 76825
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.182
REMARK   3   FREE R VALUE                     : 0.201
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 3765
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            : 2032
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 308
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.33700
REMARK   3    B22 (A**2) : 0.20300
REMARK   3    B33 (A**2) : -0.54000
REMARK   3    B12 (A**2) : -0.30300
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
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) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
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) : 1.044 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.501 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.927 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.825 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 57.76
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : ION.PARAM
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  4  : GOL_XPLOR_FLEX_PAR.TXT
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: FRIEDEL PAIRS WERE USED IN REFINEMENT
REMARK   4
REMARK   4 2OCG COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB040960.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-JUL-2004
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 32-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0029, 0.9791, 0.9793, 0.9565
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : DTREK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39135
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.490
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 11.290
REMARK 200  R MERGE                    (I) : 0.06500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 18.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.93
REMARK 200  R MERGE FOR SHELL          (I) : 0.33100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 6.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 63.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4,000, 0.1 M MOPS, 0.1 M
REMARK 280  MNSO4, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,2/3+Z
REMARK 290       3555   -X+Y,-X,1/3+Z
REMARK 290       4555   -X,-Y,Z
REMARK 290       5555   Y,-X+Y,2/3+Z
REMARK 290       6555   X-Y,X,1/3+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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.56000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       28.78000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       57.56000
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       28.78000
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. THE BIOLOGICAL UNIT OF THE
REMARK 300 PROTEIN IS NOT KNOWN
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 MG    MG A 402   LIES ON A SPECIAL POSITION.
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ARG A 187    CG    CD    NE    CZ    NH1   NH2
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    LEU A  53       18.51     54.34
REMARK 500    ASN A  68      107.09    -51.06
REMARK 500    SER A 122     -121.79     56.54
REMARK 500    CYS A 208       28.44   -147.47
REMARK 500    LYS A 254     -154.72   -115.08
REMARK 500    ASN A 256       39.08    -96.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A 401  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A  57   OE1
REMARK 620 2 GLU A  57   OE2  56.7
REMARK 620 3 ASP A  78   OD2 103.1 159.5
REMARK 620 4 HOH A 588   O    84.3  85.5  89.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 402  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 204   OD2
REMARK 620 2 HOH A 636   O    85.0
REMARK 620 3 HOH A 635   O   100.7  77.9
REMARK 620 N                    1     2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: MN BINDING SITE FOR RESIDUE A 401
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: MG BINDING SITE FOR RESIDUE A 402
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR RESIDUE A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OCI   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VALACYCLOVIR HYDROLASE COMPLEXED WITH
REMARK 900 A PRODUCT ANALOGUE
REMARK 900 RELATED ID: 2OCK   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VALACYCLOVIR HYDROLASE D123N MUTANT
REMARK 900 RELATED ID: 2OCL   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VALACYCLOVIR HYDROLASE S122A MUTANT
DBREF  2OCG A   21   274  UNP    Q86WA6   BPHL_HUMAN      38    291
SEQRES   1 A  254  SER VAL THR SER ALA LYS VAL ALA VAL ASN GLY VAL GLN
SEQRES   2 A  254  LEU HIS TYR GLN GLN THR GLY GLU GLY ASP HIS ALA VAL
SEQRES   3 A  254  LEU LEU LEU PRO GLY MET LEU GLY SER GLY GLU THR ASP
SEQRES   4 A  254  PHE GLY PRO GLN LEU LYS ASN LEU ASN LYS LYS LEU PHE
SEQRES   5 A  254  THR VAL VAL ALA TRP ASP PRO ARG GLY TYR GLY HIS SER
SEQRES   6 A  254  ARG PRO PRO ASP ARG ASP PHE PRO ALA ASP PHE PHE GLU
SEQRES   7 A  254  ARG ASP ALA LYS ASP ALA VAL ASP LEU MET LYS ALA LEU
SEQRES   8 A  254  LYS PHE LYS LYS VAL SER LEU LEU GLY TRP SER ASP GLY
SEQRES   9 A  254  GLY ILE THR ALA LEU ILE ALA ALA ALA LYS TYR PRO SER
SEQRES  10 A  254  TYR ILE HIS LYS MET VAL ILE TRP GLY ALA ASN ALA TYR
SEQRES  11 A  254  VAL THR ASP GLU ASP SER MET ILE TYR GLU GLY ILE ARG
SEQRES  12 A  254  ASP VAL SER LYS TRP SER GLU ARG THR ARG LYS PRO LEU
SEQRES  13 A  254  GLU ALA LEU TYR GLY TYR ASP TYR PHE ALA ARG THR CYS
SEQRES  14 A  254  GLU LYS TRP VAL ASP GLY ILE ARG GLN PHE LYS HIS LEU
SEQRES  15 A  254  PRO ASP GLY ASN ILE CYS ARG HIS LEU LEU PRO ARG VAL
SEQRES  16 A  254  GLN CYS PRO ALA LEU ILE VAL HIS GLY GLU LYS ASP PRO
SEQRES  17 A  254  LEU VAL PRO ARG PHE HIS ALA ASP PHE ILE HIS LYS HIS
SEQRES  18 A  254  VAL LYS GLY SER ARG LEU HIS LEU MET PRO GLU GLY LYS
SEQRES  19 A  254  HIS ASN LEU HIS LEU ARG PHE ALA ASP GLU PHE ASN LYS
SEQRES  20 A  254  LEU ALA GLU ASP PHE LEU GLN
HET     MN  A 401       1
HET     MG  A 402       1
HET    GOL  A 501       6
HETNAM      MN MANGANESE (II) ION
HETNAM      MG MAGNESIUM ION
HETNAM     GOL GLYCEROL
FORMUL   2   MN    MN 2+
FORMUL   3   MG    MG 2+
FORMUL   4  GOL    C3 H8 O3
FORMUL   5  HOH   *302(H2 O)
HELIX    1   1 SER A   55  PHE A   60  1                                   6
HELIX    2   2 PHE A   60  LEU A   67  1                                   8
HELIX    3   3 ASP A   95  LEU A  111  1                                  17
HELIX    4   4 SER A  122  TYR A  135  1                                  14
HELIX    5   5 THR A  152  GLY A  161  1                                  10
HELIX    6   6 ASP A  164  TRP A  168  5                                   5
HELIX    7   7 SER A  169  GLY A  181  1                                  13
HELIX    8   8 GLY A  181  GLN A  198  1                                  18
HELIX    9   9 PHE A  199  ASN A  206  5                                   8
HELIX   10  10 CYS A  208  VAL A  215  5                                   8
HELIX   11  11 PRO A  231  VAL A  242  1                                  12
HELIX   12  12 ASN A  256  PHE A  261  1                                   6
HELIX   13  13 PHE A  261  GLN A  274  1                                  14
SHEET    1   A 8 THR A  23  VAL A  29  0
SHEET    2   A 8 VAL A  32  GLY A  40 -1  O  VAL A  32   N  VAL A  29
SHEET    3   A 8 PHE A  72  TRP A  77 -1  O  VAL A  74   N  THR A  39
SHEET    4   A 8 HIS A  44  LEU A  49  1  N  LEU A  48   O  VAL A  75
SHEET    5   A 8 VAL A 116  TRP A 121  1  O  LEU A 119   N  LEU A  47
SHEET    6   A 8 ILE A 139  TRP A 145  1  O  VAL A 143   N  LEU A 118
SHEET    7   A 8 ALA A 219  GLY A 224  1  O  LEU A 220   N  MET A 142
SHEET    8   A 8 ARG A 246  MET A 250  1  O  ARG A 246   N  ILE A 221
LINK         OE1 GLU A  57                MN    MN A 401   1555   1555    2.36
LINK         OE2 GLU A  57                MN    MN A 401   1555   1555    2.27
LINK         OD2 ASP A  78                MN    MN A 401   1555   1555    2.12
LINK         OD2 ASP A 204                MG    MG A 402   1555   1555    2.09
LINK        MN    MN A 401                 O   HOH A 588   1555   1555    2.30
LINK        MG    MG A 402                 O   HOH A 636   1555   1555    2.07
LINK        MG    MG A 402                 O   HOH A 635   1555   1555    2.04
CISPEP   1 ARG A   86    PRO A   87          0        -0.25
CISPEP   2 PRO A   87    PRO A   88          0         0.12
SITE     1 AC1  5 HIS A  35  GLU A  57  ASP A  78  HIS A  84
SITE     2 AC1  5 HOH A 588
SITE     1 AC2  3 ASP A 204  HOH A 635  HOH A 636
SITE     1 AC3 10 SER A 122  ASP A 123  ILE A 126  GLY A 146
SITE     2 AC3 10 ALA A 147  ASN A 148  TRP A 192  HIS A 255
SITE     3 AC3 10 HOH A 607  HOH A 750
CRYST1   88.970   88.970   86.340  90.00  90.00 120.00 P 62          6
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      0.011240  0.006489  0.000000        0.00000
SCALE2      0.000000  0.012979  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011582        0.00000
TER    2033      GLN A 274
MASTER      287    0    3   13    8    0    6    6 2342    1   15   20
END