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PDBsum entry 1d5r

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Hydrolase PDB id
1d5r
Jmol
Contents
Protein chain
307 a.a. *
Ligands
TLA
Waters ×382
* Residue conservation analysis
HEADER    HYDROLASE                               11-OCT-99   1D5R
TITLE     CRYSTAL STRUCTURE OF THE PTEN TUMOR SUPPRESSOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PHOSPHOINOSITIDE PHOSPHOTASE PTEN;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 7-353;
COMPND   5 EC: 3.1.3.48;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PVL1393
KEYWDS    C2 DOMAIN, PHOSPHOTIDYLINOSITOL, PHOSPHOTASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.O.LEE,H.YANG,M.-M.GEORGESCU,A.DI CRISTOFANO,N.P.PAVLETICH
REVDAT   3   24-FEB-09 1D5R    1       VERSN
REVDAT   2   01-APR-03 1D5R    1       JRNL
REVDAT   1   04-NOV-99 1D5R    0
JRNL        AUTH   J.O.LEE,H.YANG,M.M.GEORGESCU,A.DI CRISTOFANO,
JRNL        AUTH 2 T.MAEHAMA,Y.SHI,J.E.DIXON,P.PANDOLFI,N.P.PAVLETICH
JRNL        TITL   CRYSTAL STRUCTURE OF THE PTEN TUMOR SUPPRESSOR:
JRNL        TITL 2 IMPLICATIONS FOR ITS PHOSPHOINOSITIDE PHOSPHATASE
JRNL        TITL 3 ACTIVITY AND MEMBRANE ASSOCIATION.
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V.  99   323 1999
JRNL        REFN                   ISSN 0092-8674
JRNL        PMID   10555148
JRNL        DOI    10.1016/S0092-8674(00)81663-3
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.10 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) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
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)   (%) : 95.8
REMARK   3   NUMBER OF REFLECTIONS             : 20302
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 SET) : 0.224
REMARK   3   FREE R VALUE                     : 0.276
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 960
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            : 2576
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 10
REMARK   3   SOLVENT ATOMS            : 382
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 25.50
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) : 0.009
REMARK   3   BOND ANGLES            (DEGREES) : 1.66
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) : 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  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 1D5R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-99.
REMARK 100 THE RCSB ID CODE IS RCSB009817.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-DEC-98
REMARK 200  TEMPERATURE           (KELVIN) : 130.0
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : F2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20302
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8
REMARK 200  DATA REDUNDANCY                : 3.500
REMARK 200  R MERGE                    (I) : 0.03700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 42.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.16300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA/K TARTRATE, 5% GLYCEROL, 100MM
REMARK 280  TRIS-CL, 10MM DTT, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -Y,X,Z
REMARK 290       4555   Y,-X,Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2
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        0.00000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  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       56.57000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.57000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       29.27500
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       56.57000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.57000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       29.27500
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       56.57000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       56.57000
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       29.27500
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       56.57000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       56.57000
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       29.27500
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: MONOMERIC
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     7
REMARK 465     ILE A     8
REMARK 465     VAL A     9
REMARK 465     SER A    10
REMARK 465     ARG A    11
REMARK 465     ASN A    12
REMARK 465     LYS A    13
REMARK 465     GLY A   282
REMARK 465     PRO A   283
REMARK 465     GLU A   284
REMARK 465     GLU A   285
REMARK 465     VAL A   309
REMARK 465     ASP A   310
REMARK 465     ASN A   311
REMARK 465     ASP A   312
REMARK 465     GLU A   352
REMARK 465     GLU A   353
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   O    HOH A  1503     O    HOH A  1690              2.15
REMARK 500   O    HOH A  1433     O    HOH A  1633              2.15
REMARK 500   O    ASP A    24     O    HOH A  1706              2.17
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    GLY A  20   N   -  CA  -  C   ANGL. DEV. = -15.1 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    TYR A  16      -21.68    171.13
REMARK 500    GLN A  17      137.04   -175.89
REMARK 500    PHE A  21     -105.38   -117.07
REMARK 500    ASP A  22       61.30    173.58
REMARK 500    LEU A  42      154.21    -42.42
REMARK 500    GLU A  43      152.98    174.12
REMARK 500    ARG A  47      -45.04   -134.51
REMARK 500    LYS A  62      -90.35    -40.31
REMARK 500    GLU A  73     -116.07    -63.00
REMARK 500    THR A  78       30.40    -58.52
REMARK 500    SER A 113       36.82    -80.95
REMARK 500    ASP A 116      -47.85   -141.69
REMARK 500    ASN A 117     -154.78   -153.28
REMARK 500    HIS A 118       16.81   -146.88
REMARK 500    CYS A 124     -126.31   -129.29
REMARK 500    LYS A 128     -102.44   -121.10
REMARK 500    THR A 210     -167.71   -128.54
REMARK 500    LEU A 220     -135.42     61.37
REMARK 500    ASP A 236      106.83     29.63
REMARK 500    LYS A 237      -23.01     77.38
REMARK 500    MET A 270      -64.17    -92.91
REMARK 500    GLU A 314      -44.84   -142.54
REMARK 500    ASN A 334       49.48     36.04
REMARK 500    ASN A 340      -18.07     82.76
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 A1421        DISTANCE =  6.14 ANGSTROMS
REMARK 525    HOH A1436        DISTANCE =  5.18 ANGSTROMS
REMARK 525    HOH A1438        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH A1480        DISTANCE =  5.35 ANGSTROMS
REMARK 525    HOH A1510        DISTANCE =  5.28 ANGSTROMS
REMARK 525    HOH A1588        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH A1618        DISTANCE =  7.22 ANGSTROMS
REMARK 525    HOH A1624        DISTANCE =  5.52 ANGSTROMS
REMARK 525    HOH A1632        DISTANCE =  6.51 ANGSTROMS
REMARK 525    HOH A1662        DISTANCE =  6.97 ANGSTROMS
REMARK 525    HOH A1663        DISTANCE =  6.49 ANGSTROMS
REMARK 525    HOH A1667        DISTANCE =  6.86 ANGSTROMS
REMARK 525    HOH A1671        DISTANCE =  5.29 ANGSTROMS
REMARK 525    HOH A1691        DISTANCE =  7.32 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TLA A 1352
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 286-309 ARE REPLACED BY VAL
DBREF  1D5R A    7   285  UNP    P60484   PTEN_HUMAN       7    285
DBREF  1D5R A  310   353  UNP    P60484   PTEN_HUMAN     310    353
SEQADV 1D5R MET A    7  UNP  P60484    GLU     7 CONFLICT
SEQADV 1D5R VAL A  309  UNP  P60484          309 SEE REMARK 999
SEQRES   1 A  324  MET ILE VAL SER ARG ASN LYS ARG ARG TYR GLN GLU ASP
SEQRES   2 A  324  GLY PHE ASP LEU ASP LEU THR TYR ILE TYR PRO ASN ILE
SEQRES   3 A  324  ILE ALA MET GLY PHE PRO ALA GLU ARG LEU GLU GLY VAL
SEQRES   4 A  324  TYR ARG ASN ASN ILE ASP ASP VAL VAL ARG PHE LEU ASP
SEQRES   5 A  324  SER LYS HIS LYS ASN HIS TYR LYS ILE TYR ASN LEU CYS
SEQRES   6 A  324  ALA GLU ARG HIS TYR ASP THR ALA LYS PHE ASN CYS ARG
SEQRES   7 A  324  VAL ALA GLN TYR PRO PHE GLU ASP HIS ASN PRO PRO GLN
SEQRES   8 A  324  LEU GLU LEU ILE LYS PRO PHE CYS GLU ASP LEU ASP GLN
SEQRES   9 A  324  TRP LEU SER GLU ASP ASP ASN HIS VAL ALA ALA ILE HIS
SEQRES  10 A  324  CYS LYS ALA GLY LYS GLY ARG THR GLY VAL MET ILE CYS
SEQRES  11 A  324  ALA TYR LEU LEU HIS ARG GLY LYS PHE LEU LYS ALA GLN
SEQRES  12 A  324  GLU ALA LEU ASP PHE TYR GLY GLU VAL ARG THR ARG ASP
SEQRES  13 A  324  LYS LYS GLY VAL THR ILE PRO SER GLN ARG ARG TYR VAL
SEQRES  14 A  324  TYR TYR TYR SER TYR LEU LEU LYS ASN HIS LEU ASP TYR
SEQRES  15 A  324  ARG PRO VAL ALA LEU LEU PHE HIS LYS MET MET PHE GLU
SEQRES  16 A  324  THR ILE PRO MET PHE SER GLY GLY THR CYS ASN PRO GLN
SEQRES  17 A  324  PHE VAL VAL CYS GLN LEU LYS VAL LYS ILE TYR SER SER
SEQRES  18 A  324  ASN SER GLY PRO THR ARG ARG GLU ASP LYS PHE MET TYR
SEQRES  19 A  324  PHE GLU PHE PRO GLN PRO LEU PRO VAL CYS GLY ASP ILE
SEQRES  20 A  324  LYS VAL GLU PHE PHE HIS LYS GLN ASN LYS MET LEU LYS
SEQRES  21 A  324  LYS ASP LYS MET PHE HIS PHE TRP VAL ASN THR PHE PHE
SEQRES  22 A  324  ILE PRO GLY PRO GLU GLU VAL ASP ASN ASP LYS GLU TYR
SEQRES  23 A  324  LEU VAL LEU THR LEU THR LYS ASN ASP LEU ASP LYS ALA
SEQRES  24 A  324  ASN LYS ASP LYS ALA ASN ARG TYR PHE SER PRO ASN PHE
SEQRES  25 A  324  LYS VAL LYS LEU TYR PHE THR LYS THR VAL GLU GLU
HET    TLA  A1352      10
HETNAM     TLA L(+)-TARTARIC ACID
FORMUL   2  TLA    C4 H6 O6
FORMUL   3  HOH   *382(H2 O)
HELIX    1   1 ASN A   49  HIS A   61  1                                  13
HELIX    2   2 GLN A   97  GLU A   99  5                                   3
HELIX    3   3 LEU A  100  SER A  113  1                                  14
HELIX    4   4 LYS A  128  ARG A  142  1                                  15
HELIX    5   5 LYS A  147  THR A  160  1                                  14
HELIX    6   6 ILE A  168  HIS A  185  1                                  18
HELIX    7   7 PHE A  278  ILE A  280  5                                   3
HELIX    8   8 ASN A  323  LEU A  325  5                                   3
HELIX    9   9 LYS A  327  ASP A  331  5                                   5
SHEET    1   A 5 LEU A  25  TYR A  29  0
SHEET    2   A 5 ILE A  32  MET A  35 -1  O  ILE A  32   N  ILE A  28
SHEET    3   A 5 VAL A 119  HIS A 123  1  O  ALA A 120   N  ILE A  33
SHEET    4   A 5 TYR A  65  CYS A  71  1  O  LYS A  66   N  ALA A 121
SHEET    5   A 5 VAL A  85  PHE A  90  1  O  ALA A  86   N  ASN A  69
SHEET    1   B 5 ARG A 233  GLU A 235  0
SHEET    2   B 5 PHE A 238  CYS A 250 -1  O  PHE A 238   N  GLU A 235
SHEET    3   B 5 ALA A 192  PHE A 200 -1  O  LEU A 193   N  VAL A 249
SHEET    4   B 5 LYS A 342  LYS A 349 -1  N  LYS A 344   O  MET A 199
SHEET    5   B 5 LEU A 316  THR A 321 -1  O  LEU A 316   N  PHE A 347
SHEET    1   C 4 VAL A 222  SER A 226  0
SHEET    2   C 4 PRO A 213  GLN A 219 -1  N  VAL A 217   O  TYR A 225
SHEET    3   C 4 ASP A 252  HIS A 259 -1  N  LYS A 254   O  CYS A 218
SHEET    4   C 4 ASP A 268  ASN A 276 -1  O  ASP A 268   N  HIS A 259
SITE     1 AC1 10 ASP A  92  HIS A  93  CYS A 124  LYS A 125
SITE     2 AC1 10 ALA A 126  GLY A 129  ARG A 130  GLN A 171
SITE     3 AC1 10 HOH A1381  HOH A1439
CRYST1  113.140  113.140   58.550  90.00  90.00  90.00 I 4           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      0.008839  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008839  0.000000        0.00000
SCALE3      0.000000  0.000000  0.017079        0.00000
      
PROCHECK
Go to PROCHECK summary
 References