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PDBsum entry 1ew2

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Hydrolase PDB id
1ew2
Jmol
Contents
Protein chain
479 a.a. *
Ligands
NAG
PO4
Metals
_ZN ×2
_MG ×2
Waters ×602
* Residue conservation analysis
HEADER    HYDROLASE                               21-APR-00   1EW2
TITLE     CRYSTAL STRUCTURE OF A HUMAN PHOSPHATASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PHOSPHATASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.1.3.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 ORGAN: PLACENTA
KEYWDS    PHOSPHATASE, NON COVALENT COMPLEX, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.H.LE DU,T.STIGBRAND,M.J.TAUSSIG,A.MENEZ,E.A.STURA
REVDAT   3   13-JUL-11 1EW2    1       VERSN
REVDAT   2   24-FEB-09 1EW2    1       VERSN
REVDAT   1   04-APR-01 1EW2    0
JRNL        AUTH   M.H.LE DU,T.STIGBRAND,M.J.TAUSSIG,A.MENEZ,E.A.STURA
JRNL        TITL   CRYSTAL STRUCTURE OF ALKALINE PHOSPHATASE FROM HUMAN
JRNL        TITL 2 PLACENTA AT 1.8 A RESOLUTION. IMPLICATION FOR A SUBSTRATE
JRNL        TITL 3 SPECIFICITY.
JRNL        REF    J.BIOL.CHEM.                  V. 276  9158 2001
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   11124260
JRNL        DOI    10.1074/JBC.M009250200
REMARK   2
REMARK   2 RESOLUTION.    1.82 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 41585
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
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185
REMARK   3   R VALUE            (WORKING SET) : 0.185
REMARK   3   FREE R VALUE                     : 0.242
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 2050
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3652
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 23
REMARK   3   SOLVENT ATOMS            : 602
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 18.00
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1EW2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-00.
REMARK 100 THE RCSB ID CODE IS RCSB010947.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 24-APR-97
REMARK 200  TEMPERATURE           (KELVIN) : 80.0
REMARK 200  PH                             : 6.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : LURE
REMARK 200  BEAMLINE                       : D41A
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                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49278
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 79.6
REMARK 200  DATA REDUNDANCY                : 2.340
REMARK 200  R MERGE                    (I) : 0.08500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74
REMARK 200  COMPLETENESS FOR SHELL     (%) : 66.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.32
REMARK 200  R MERGE FOR SHELL          (I) : 0.68600
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, PH 6.0, VAPOR DIFFUSION,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-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        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.45000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.45000
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  1.000000  0.000000  0.000000       44.40000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       57.25000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       44.40000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       57.25000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       53.45000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       44.40000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       57.25000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       53.45000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       44.40000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       57.25000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 9970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -268.0 KCAL/MOL
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   BIOMT1   2 -1.000000  0.000000  0.000000       88.80000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       53.45000
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     ALA A   480
REMARK 465     GLY A   481
REMARK 465     THR A   482
REMARK 465     THR A   483
REMARK 465     ASP A   484
REMARK 465     ALA A   485
REMARK 465     ALA A   486
REMARK 465     HIS A   487
REMARK 465     PRO A   488
REMARK 465     GLY A   489
REMARK 465     ARG A   490
REMARK 465     SER A   491
REMARK 465     VAL A   492
REMARK 465     VAL A   493
REMARK 465     PRO A   494
REMARK 465     ALA A   495
REMARK 465     LEU A   496
REMARK 465     LEU A   497
REMARK 465     PRO A   498
REMARK 465     LEU A   499
REMARK 465     LEU A   500
REMARK 465     ALA A   501
REMARK 465     GLY A   502
REMARK 465     THR A   503
REMARK 465     LEU A   504
REMARK 465     LEU A   505
REMARK 465     LEU A   506
REMARK 465     LEU A   507
REMARK 465     GLU A   508
REMARK 465     THR A   509
REMARK 465     ALA A   510
REMARK 465     THR A   511
REMARK 465     ALA A   512
REMARK 465     PRO A   513
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     ILE A   1    CG1  CG2  CD1
REMARK 470     GLU A   5    CG   CD   OE1  OE2
REMARK 470     GLU A  18    CG   CD   OE1  OE2
REMARK 470     GLN A  30    CG   CD   OE1  NE2
REMARK 470     ASP A  61    CG   OD1  OD2
REMARK 470     LYS A  62    CG   CD   CE   NZ
REMARK 470     GLU A 469    CG   CD   OE1  OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OE1  GLN A   242     O    HOH A  1601              0.53
REMARK 500   C7   NAG A  1000     O    HOH A  1136              0.72
REMARK 500   O    HOH A  1117     O    HOH A  1353              0.90
REMARK 500   CD   GLN A   242     O    HOH A  1113              1.01
REMARK 500   NE2  GLN A   242     O    HOH A  1113              1.11
REMARK 500   N2   NAG A  1000     O    HOH A  1136              1.13
REMARK 500   O7   NAG A  1000     O    HOH A  1136              1.33
REMARK 500   CD   GLN A   242     O    HOH A  1601              1.68
REMARK 500   CG   GLN A   242     O    HOH A  1113              1.78
REMARK 500   CD2  LEU A    26     O    HOH A  1556              2.00
REMARK 500   C8   NAG A  1000     O    HOH A  1136              2.02
REMARK 500   OE1  GLN A   242     O    HOH A  1113              2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A  1598     O    HOH A  1598     3655     0.80
REMARK 500   O    HOH A  1133     O    HOH A  1222     4555     1.91
REMARK 500   O    HOH A  1035     O    HOH A  1399     3655     2.12
REMARK 500   O    HOH A  1133     O    HOH A  1137     4555     2.19
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A  42   CB  -  CG  -  OD2 ANGL. DEV. =  13.5 DEGREES
REMARK 500    ARG A  53   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    LYS A  60   CA  -  C   -  N   ANGL. DEV. =  16.2 DEGREES
REMARK 500    TYR A  76   CB  -  CG  -  CD1 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    THR A  82   CB  -  CA  -  C   ANGL. DEV. = -22.0 DEGREES
REMARK 500    THR A  82   CA  -  CB  -  OG1 ANGL. DEV. =  16.4 DEGREES
REMARK 500    ARG A 125   CD  -  NE  -  CZ  ANGL. DEV. =  20.3 DEGREES
REMARK 500    ARG A 125   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ARG A 135   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG A 166   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    GLN A 180   CA  -  CB  -  CG  ANGL. DEV. =  13.5 DEGREES
REMARK 500    GLN A 180   CB  -  CG  -  CD  ANGL. DEV. =  17.5 DEGREES
REMARK 500    ARG A 204   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG A 245   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG A 245   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    SER A 261   N   -  CA  -  CB  ANGL. DEV. =  10.2 DEGREES
REMARK 500    VAL A 262   CA  -  C   -  N   ANGL. DEV. =  22.4 DEGREES
REMARK 500    VAL A 262   O   -  C   -  N   ANGL. DEV. = -14.2 DEGREES
REMARK 500    TYR A 276   CB  -  CG  -  CD2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ASP A 285   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ARG A 301   CD  -  NE  -  CZ  ANGL. DEV. =  14.8 DEGREES
REMARK 500    ARG A 301   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ARG A 314   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ASP A 316   CB  -  CG  -  OD1 ANGL. DEV. =  -6.8 DEGREES
REMARK 500    ASP A 316   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES
REMARK 500    HIS A 320   CE1 -  NE2 -  CD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    LEU A 353   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES
REMARK 500    ASP A 357   CB  -  CG  -  OD1 ANGL. DEV. =  17.0 DEGREES
REMARK 500    ASP A 357   CB  -  CG  -  OD2 ANGL. DEV. = -13.6 DEGREES
REMARK 500    HIS A 358   ND1 -  CE1 -  NE2 ANGL. DEV. =   9.7 DEGREES
REMARK 500    ARG A 370   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG A 370   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ASP A 384   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG A 385   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG A 420   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    THR A 431   N   -  CA  -  CB  ANGL. DEV. = -16.1 DEGREES
REMARK 500    HIS A 432   CE1 -  NE2 -  CD2 ANGL. DEV. =   8.1 DEGREES
REMARK 500    THR A 472   N   -  CA  -  CB  ANGL. DEV. =  35.6 DEGREES
REMARK 500    THR A 472   CA  -  CB  -  CG2 ANGL. DEV. =  13.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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    ASP A  61       40.46   -100.73
REMARK 500    SER A 261      -32.78    101.15
REMARK 500    VAL A 262      -79.86    -75.11
REMARK 500    THR A 263      -39.51     81.83
REMARK 500    HIS A 358     -176.41   -172.18
REMARK 500    SER A 359     -166.90   -112.68
REMARK 500    VAL A 361       45.26    -85.47
REMARK 500    LEU A 468     -148.42   -102.37
REMARK 500    GLU A 469     -137.41     36.34
REMARK 500    ALA A 473       21.94     92.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    THR A  82         10.22
REMARK 500    LEU A 468        -11.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    THR A 263        23.8      L          L   OUTSIDE RANGE
REMARK 500    THR A 472        18.1      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A1188        DISTANCE =  6.77 ANGSTROMS
REMARK 525    HOH A1206        DISTANCE =  5.55 ANGSTROMS
REMARK 525    HOH A1233        DISTANCE =  5.18 ANGSTROMS
REMARK 525    HOH A1234        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH A1247        DISTANCE =  6.84 ANGSTROMS
REMARK 525    HOH A1263        DISTANCE =  5.45 ANGSTROMS
REMARK 525    HOH A1269        DISTANCE =  5.82 ANGSTROMS
REMARK 525    HOH A1302        DISTANCE =  8.16 ANGSTROMS
REMARK 525    HOH A1319        DISTANCE =  5.13 ANGSTROMS
REMARK 525    HOH A1338        DISTANCE =  6.14 ANGSTROMS
REMARK 525    HOH A1357        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH A1389        DISTANCE =  6.16 ANGSTROMS
REMARK 525    HOH A1390        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH A1397        DISTANCE =  6.77 ANGSTROMS
REMARK 525    HOH A1407        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH A1409        DISTANCE =  8.28 ANGSTROMS
REMARK 525    HOH A1416        DISTANCE =  5.72 ANGSTROMS
REMARK 525    HOH A1438        DISTANCE =  6.03 ANGSTROMS
REMARK 525    HOH A1461        DISTANCE =  7.91 ANGSTROMS
REMARK 525    HOH A1479        DISTANCE =  7.13 ANGSTROMS
REMARK 525    HOH A1489        DISTANCE =  6.31 ANGSTROMS
REMARK 525    HOH A1509        DISTANCE =  5.38 ANGSTROMS
REMARK 525    HOH A1513        DISTANCE =  7.43 ANGSTROMS
REMARK 525    HOH A1540        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH A1554        DISTANCE =  6.57 ANGSTROMS
REMARK 525    HOH A1561        DISTANCE =  6.83 ANGSTROMS
REMARK 525    HOH A1573        DISTANCE =  5.77 ANGSTROMS
REMARK 525    HOH A1586        DISTANCE =  6.73 ANGSTROMS
REMARK 525    HOH A1591        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH A1593        DISTANCE =  5.18 ANGSTROMS
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                              ZN A1001  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PO4 A1005   O1
REMARK 620 2 PO4 A1005   O2   57.3
REMARK 620 3 HIS A 432   NE2  90.4  88.1
REMARK 620 4 HIS A 320   NE2 117.7 170.2 100.7
REMARK 620 5 ASP A 316   OD1 111.8  87.6 150.1  86.9
REMARK 620 6 ASP A 316   OD2 146.6  90.6  97.9  92.5  52.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1002  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A  92   OG
REMARK 620 2 PO4 A1005   O2   64.6
REMARK 620 3 ASP A 357   OD2  82.4 146.0
REMARK 620 4 ASP A  42   OD1 115.8 102.9  98.5
REMARK 620 5 ASP A  42   OD2  69.8 100.4  73.9  50.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A1003  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 155   OG
REMARK 620 2 HOH A1426   O   171.7
REMARK 620 3 HOH A1006   O    93.8  90.3
REMARK 620 4 ASP A  42   OD2  85.3  90.3 178.0
REMARK 620 5 GLU A 311   OE2  92.9  94.6  85.3  96.6
REMARK 620 6 HOH A1115   O    85.0  88.1  85.1  93.0 170.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A1004  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 269   O
REMARK 620 2 HOH A1428   O    91.0
REMARK 620 3 GLU A 270   OE2  91.4 177.0
REMARK 620 4 ASP A 285   OD1  85.6  94.4  84.0
REMARK 620 5 GLU A 216   OE2 138.6  85.9  93.5 135.8
REMARK 620 6 ASP A 285   OD2 135.5  85.6  91.4  50.6  85.4
REMARK 620 7 GLU A 216   OE1  86.9  87.5  94.4 172.3  51.8 137.1
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1005
DBREF  1EW2 A    1   513  UNP    P05187   PPB1_HUMAN      23    535
SEQRES   1 A  513  ILE ILE PRO VAL GLU GLU GLU ASN PRO ASP PHE TRP ASN
SEQRES   2 A  513  ARG GLU ALA ALA GLU ALA LEU GLY ALA ALA LYS LYS LEU
SEQRES   3 A  513  GLN PRO ALA GLN THR ALA ALA LYS ASN LEU ILE ILE PHE
SEQRES   4 A  513  LEU GLY ASP GLY MET GLY VAL SER THR VAL THR ALA ALA
SEQRES   5 A  513  ARG ILE LEU LYS GLY GLN LYS LYS ASP LYS LEU GLY PRO
SEQRES   6 A  513  GLU ILE PRO LEU ALA MET ASP ARG PHE PRO TYR VAL ALA
SEQRES   7 A  513  LEU SER LYS THR TYR ASN VAL ASP LYS HIS VAL PRO ASP
SEQRES   8 A  513  SER GLY ALA THR ALA THR ALA TYR LEU CYS GLY VAL LYS
SEQRES   9 A  513  GLY ASN PHE GLN THR ILE GLY LEU SER ALA ALA ALA ARG
SEQRES  10 A  513  PHE ASN GLN CYS ASN THR THR ARG GLY ASN GLU VAL ILE
SEQRES  11 A  513  SER VAL MET ASN ARG ALA LYS LYS ALA GLY LYS SER VAL
SEQRES  12 A  513  GLY VAL VAL THR THR THR ARG VAL GLN HIS ALA SER PRO
SEQRES  13 A  513  ALA GLY THR TYR ALA HIS THR VAL ASN ARG ASN TRP TYR
SEQRES  14 A  513  SER ASP ALA ASP VAL PRO ALA SER ALA ARG GLN GLU GLY
SEQRES  15 A  513  CYS GLN ASP ILE ALA THR GLN LEU ILE SER ASN MET ASP
SEQRES  16 A  513  ILE ASP VAL ILE LEU GLY GLY GLY ARG LYS TYR MET PHE
SEQRES  17 A  513  ARG MET GLY THR PRO ASP PRO GLU TYR PRO ASP ASP TYR
SEQRES  18 A  513  SER GLN GLY GLY THR ARG LEU ASP GLY LYS ASN LEU VAL
SEQRES  19 A  513  GLN GLU TRP LEU ALA LYS ARG GLN GLY ALA ARG TYR VAL
SEQRES  20 A  513  TRP ASN ARG THR GLU LEU MET GLN ALA SER LEU ASP PRO
SEQRES  21 A  513  SER VAL THR HIS LEU MET GLY LEU PHE GLU PRO GLY ASP
SEQRES  22 A  513  MET LYS TYR GLU ILE HIS ARG ASP SER THR LEU ASP PRO
SEQRES  23 A  513  SER LEU MET GLU MET THR GLU ALA ALA LEU ARG LEU LEU
SEQRES  24 A  513  SER ARG ASN PRO ARG GLY PHE PHE LEU PHE VAL GLU GLY
SEQRES  25 A  513  GLY ARG ILE ASP HIS GLY HIS HIS GLU SER ARG ALA TYR
SEQRES  26 A  513  ARG ALA LEU THR GLU THR ILE MET PHE ASP ASP ALA ILE
SEQRES  27 A  513  GLU ARG ALA GLY GLN LEU THR SER GLU GLU ASP THR LEU
SEQRES  28 A  513  SER LEU VAL THR ALA ASP HIS SER HIS VAL PHE SER PHE
SEQRES  29 A  513  GLY GLY TYR PRO LEU ARG GLY SER SER ILE PHE GLY LEU
SEQRES  30 A  513  ALA PRO GLY LYS ALA ARG ASP ARG LYS ALA TYR THR VAL
SEQRES  31 A  513  LEU LEU TYR GLY ASN GLY PRO GLY TYR VAL LEU LYS ASP
SEQRES  32 A  513  GLY ALA ARG PRO ASP VAL THR GLU SER GLU SER GLY SER
SEQRES  33 A  513  PRO GLU TYR ARG GLN GLN SER ALA VAL PRO LEU ASP GLU
SEQRES  34 A  513  GLU THR HIS ALA GLY GLU ASP VAL ALA VAL PHE ALA ARG
SEQRES  35 A  513  GLY PRO GLN ALA HIS LEU VAL HIS GLY VAL GLN GLU GLN
SEQRES  36 A  513  THR PHE ILE ALA HIS VAL MET ALA PHE ALA ALA CYS LEU
SEQRES  37 A  513  GLU PRO TYR THR ALA CYS ASP LEU ALA PRO PRO ALA GLY
SEQRES  38 A  513  THR THR ASP ALA ALA HIS PRO GLY ARG SER VAL VAL PRO
SEQRES  39 A  513  ALA LEU LEU PRO LEU LEU ALA GLY THR LEU LEU LEU LEU
SEQRES  40 A  513  GLU THR ALA THR ALA PRO
MODRES 1EW2 ASN A  122  ASN  GLYCOSYLATION SITE
HET    NAG  A1000      14
HET     ZN  A1001       1
HET     ZN  A1002       1
HET     MG  A1003       1
HET     MG  A1004       1
HET    PO4  A1005       5
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM      ZN ZINC ION
HETNAM      MG MAGNESIUM ION
HETNAM     PO4 PHOSPHATE ION
FORMUL   2  NAG    C8 H15 N O6
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5   MG    2(MG 2+)
FORMUL   7  PO4    O4 P 3-
FORMUL   8  HOH   *602(H2 O)
HELIX    1   1 PRO A    3  GLU A    7  5                                   5
HELIX    2   2 ASN A    8  LEU A   26  1                                  19
HELIX    3   3 GLY A   45  LYS A   60  1                                  16
HELIX    4   4 LEU A   69  PHE A   74  5                                   6
HELIX    5   5 ASP A   91  GLY A  102  1                                  12
HELIX    6   6 GLN A  120  THR A  124  5                                   5
HELIX    7   7 SER A  131  ALA A  139  1                                   9
HELIX    8   8 HIS A  153  GLY A  158  1                                   6
HELIX    9   9 SER A  170  VAL A  174  5                                   5
HELIX   10  10 PRO A  175  GLU A  181  1                                   7
HELIX   11  11 ASP A  185  ASN A  193  1                                   9
HELIX   12  12 ARG A  204  MET A  207  5                                   4
HELIX   13  13 ASP A  220  GLY A  224  5                                   5
HELIX   14  14 ASN A  232  LYS A  240  1                                   9
HELIX   15  15 ASN A  249  ASP A  259  1                                  11
HELIX   16  16 TYR A  276  ARG A  280  5                                   5
HELIX   17  17 SER A  287  SER A  300  1                                  14
HELIX   18  18 ARG A  314  GLU A  321  1                                   8
HELIX   19  19 ARG A  323  THR A  345  1                                  23
HELIX   20  20 THR A  410  GLY A  415  1                                   6
HELIX   21  21 GLN A  445  VAL A  449  5                                   5
HELIX   22  22 THR A  456  ALA A  466  1                                  11
SHEET    1   A10 ALA A 244  VAL A 247  0
SHEET    2   A10 HIS A 264  LEU A 268  1  O  HIS A 264   N  ARG A 245
SHEET    3   A10 VAL A 198  GLY A 202  1  O  ILE A 199   N  GLY A 267
SHEET    4   A10 SER A 142  ARG A 150  1  O  VAL A 143   N  VAL A 198
SHEET    5   A10 PHE A 306  GLY A 312  1  O  PHE A 307   N  GLY A 144
SHEET    6   A10 ASN A  35  GLY A  41  1  O  LEU A  36   N  LEU A 308
SHEET    7   A10 THR A 350  ALA A 356  1  O  LEU A 351   N  ILE A  37
SHEET    8   A10 VAL A 437  ARG A 442 -1  O  ALA A 438   N  ALA A 356
SHEET    9   A10 TYR A  76  LYS A  81 -1  O  TYR A  76   N  ALA A 441
SHEET   10   A10 VAL A 452  GLU A 454  1  O  GLN A 453   N  LYS A  81
SHEET    1   B 2 SER A 359  HIS A 360  0
SHEET    2   B 2 HIS A 432  ALA A 433 -1  N  ALA A 433   O  SER A 359
SHEET    1   C 3 PHE A 362  PHE A 364  0
SHEET    2   C 3 LEU A 391  ASN A 395 -1  O  LEU A 392   N  SER A 363
SHEET    3   C 3 SER A 423  VAL A 425  1  N  ALA A 424   O  GLY A 394
SSBOND   1 CYS A  121    CYS A  183                          1555   1555  2.03
SSBOND   2 CYS A  467    CYS A  474                          1555   1555  2.05
LINK         ND2 ASN A 122                 C1  NAG A1000     1555   1555  1.02
LINK         ND2 ASN A 122                 C2  NAG A1000     1555   1555  1.94
LINK        ZN    ZN A1001                 O1  PO4 A1005     1555   1555  2.61
LINK        ZN    ZN A1001                 O2  PO4 A1005     1555   1555  2.44
LINK        ZN    ZN A1001                 NE2 HIS A 432     1555   1555  2.37
LINK        ZN    ZN A1001                 NE2 HIS A 320     1555   1555  2.38
LINK        ZN    ZN A1001                 OD1 ASP A 316     1555   1555  2.45
LINK        ZN    ZN A1001                 OD2 ASP A 316     1555   1555  2.61
LINK        ZN    ZN A1002                 OG  SER A  92     1555   1555  2.58
LINK        ZN    ZN A1002                 O2  PO4 A1005     1555   1555  2.25
LINK        ZN    ZN A1002                 OD2 ASP A 357     1555   1555  2.37
LINK        ZN    ZN A1002                 OD1 ASP A  42     1555   1555  2.26
LINK        ZN    ZN A1002                 OD2 ASP A  42     1555   1555  2.65
LINK        MG    MG A1003                 OG  SER A 155     1555   1555  2.45
LINK        MG    MG A1003                 O   HOH A1426     1555   1555  2.50
LINK        MG    MG A1003                 O   HOH A1006     1555   1555  2.42
LINK        MG    MG A1003                 OD2 ASP A  42     1555   1555  2.35
LINK        MG    MG A1003                 OE2 GLU A 311     1555   1555  2.30
LINK        MG    MG A1003                 O   HOH A1115     1555   1555  2.36
LINK        MG    MG A1004                 O   PHE A 269     1555   1555  2.39
LINK        MG    MG A1004                 O   HOH A1428     1555   1555  2.45
LINK        MG    MG A1004                 OE2 GLU A 270     1555   1555  2.36
LINK        MG    MG A1004                 OD1 ASP A 285     1555   1555  2.64
LINK        MG    MG A1004                 OE2 GLU A 216     1555   1555  2.63
LINK        MG    MG A1004                 OD2 ASP A 285     1555   1555  2.54
LINK        MG    MG A1004                 OE1 GLU A 216     1555   1555  2.40
SITE     1 AC1  6 ASN A 122  LEU A 258  ARG A 297  ARG A 301
SITE     2 AC1  6 HOH A1136  HOH A1266
SITE     1 AC2  4 ASP A 316  HIS A 320  HIS A 432  PO4 A1005
SITE     1 AC3  5 ASP A  42  SER A  92  ASP A 357  HIS A 358
SITE     2 AC3  5 PO4 A1005
SITE     1 AC4  6 ASP A  42  SER A 155  GLU A 311  HOH A1006
SITE     2 AC4  6 HOH A1115  HOH A1426
SITE     1 AC5  5 GLU A 216  PHE A 269  GLU A 270  ASP A 285
SITE     2 AC5  5 HOH A1428
SITE     1 AC6 12 ASP A  42  ASP A  91  SER A  92  HIS A 153
SITE     2 AC6 12 ARG A 166  ASP A 316  HIS A 432   ZN A1001
SITE     3 AC6 12  ZN A1002  HOH A1076  HOH A1115  HOH A1320
CRYST1   88.800  114.500  106.900  90.00  90.00  90.00 C 2 2 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      0.011260  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008730  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009350        0.00000
      
PROCHECK
Go to PROCHECK summary
 References