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PDBsum entry 1p15

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Hydrolase PDB id
1p15
Jmol
Contents
Protein chains
245 a.a. *
Waters ×115
* Residue conservation analysis
HEADER    HYDROLASE                               11-APR-03   1P15
TITLE     CRYSTAL STRUCTURE OF THE D2 DOMAIN OF RPTPA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN-TYROSINE PHOSPHATASE ALPHA;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: D2 DOMAIN;
COMPND   5 SYNONYM: R-PTP- ALPHA, LCA-RELATED PHOSPHATASE;
COMPND   6 EC: 3.1.3.48;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 GENE: PTPRA OR LRP OR PTPA;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    TRANSMEMBRANE, HYDROLASE, PHOSPHORYLATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.D.SONNENBURG,A.BILWES,T.HUNTER,J.P.NOEL
REVDAT   2   24-FEB-09 1P15    1       VERSN
REVDAT   1   19-AUG-03 1P15    0
JRNL        AUTH   E.D.SONNENBURG,A.BILWES,T.HUNTER,J.P.NOEL
JRNL        TITL   THE STRUCTURE OF THE MEMBRANE DISTAL PHOSPHATASE
JRNL        TITL 2 DOMAIN OF RPTPALPHA REVEALS INTERDOMAIN
JRNL        TITL 3 FLEXIBILITY AND AN SH2 DOMAIN INTERACTION REGION.
JRNL        REF    BIOCHEMISTRY                  V.  42  7904 2003
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   12834342
JRNL        DOI    10.1021/BI0340503
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 51.18
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.6
REMARK   3   NUMBER OF REFLECTIONS             : 38121
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.203
REMARK   3   FREE R VALUE                     : 0.255
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 3468
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5766
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3490
REMARK   3   BIN FREE R VALUE                    : 0.3270
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.80
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 630
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3974
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 115
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 24.30
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.80
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.45000
REMARK   3    B22 (A**2) : 0.45000
REMARK   3    B33 (A**2) : -0.90000
REMARK   3    B12 (A**2) : 2.83000
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) : 0.42
REMARK   3   ESD FROM SIGMAA              (A) : 0.45
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.47
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.39
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.010
REMARK   3   BOND ANGLES            (DEGREES) : 2.10
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.20
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.94
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.460 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.560 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.620 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.560 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.38
REMARK   3   BSOL        : 53.83
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  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1P15 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-03.
REMARK 100 THE RCSB ID CODE IS RCSB018885.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 105
REMARK 200  PH                             : 5.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL7-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40834
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 51.100
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.13
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM SUCCINATE, LITHIUM
REMARK 280  SULFATE, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
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       50.88567
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      101.77133
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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     PHE A   787
REMARK 465     SER A   788
REMARK 465     ASP A   789
REMARK 465     TYR A   790
REMARK 465     ALA A   791
REMARK 465     ASN A   792
REMARK 465     PHE A   793
REMARK 465     LYS A   794
REMARK 465     ARG B   674
REMARK 465     ASP B   789
REMARK 465     TYR B   790
REMARK 465     ALA B   791
REMARK 465     ASN B   792
REMARK 465     PHE B   793
REMARK 465     LYS B   794
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    GLU A   633     N    CYS A   635              1.74
REMARK 500   O    ARG A   679     N    ILE A   681              2.08
REMARK 500   O    GLN A   632     N    LYS A   634              2.16
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    HIS A 604   N   -  CA  -  C   ANGL. DEV. = -19.7 DEGREES
REMARK 500    GLU A 629   N   -  CA  -  C   ANGL. DEV. = -28.3 DEGREES
REMARK 500    ARG A 630   N   -  CA  -  C   ANGL. DEV. =  21.1 DEGREES
REMARK 500    GLY A 631   N   -  CA  -  C   ANGL. DEV. = -33.0 DEGREES
REMARK 500    ALA A 636   N   -  CA  -  C   ANGL. DEV. =  23.0 DEGREES
REMARK 500    GLN A 637   N   -  CA  -  C   ANGL. DEV. = -23.7 DEGREES
REMARK 500    ARG A 674   N   -  CA  -  C   ANGL. DEV. = -24.5 DEGREES
REMARK 500    GLU A 675   N   -  CA  -  C   ANGL. DEV. =  20.1 DEGREES
REMARK 500    SER A 715   N   -  CA  -  C   ANGL. DEV. = -16.7 DEGREES
REMARK 500    GLN A 772   N   -  CA  -  C   ANGL. DEV. = -22.0 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    ARG A 573      -71.28     18.52
REMARK 500    GLU A 576      114.38     74.24
REMARK 500    ASN A 582       87.77    -65.54
REMARK 500    PRO A 601     -173.95    -56.02
REMARK 500    LEU A 603        1.89     80.90
REMARK 500    THR A 605       -4.26   -166.66
REMARK 500    GLU A 633       31.93      7.67
REMARK 500    LYS A 634      -22.43      5.29
REMARK 500    CYS A 635     -142.96   -178.44
REMARK 500    ALA A 636     -142.45    -45.01
REMARK 500    GLN A 637       48.20     96.38
REMARK 500    ASP A 642       84.19     82.33
REMARK 500    LEU A 644       75.19    110.40
REMARK 500    LEU A 654      179.26    -39.44
REMARK 500    LYS A 655      -31.36    104.31
REMARK 500    LYS A 656       38.58    -63.74
REMARK 500    CYS A 660     -165.26    -79.97
REMARK 500    GLU A 661      -78.88    -56.78
REMARK 500    ARG A 674       53.57    155.72
REMARK 500    GLU A 675      131.61    -19.56
REMARK 500    ASN A 676      109.23   -175.67
REMARK 500    ARG A 679       82.54     -4.67
REMARK 500    GLN A 680       76.49    -15.88
REMARK 500    PRO A 695      153.67    -18.85
REMARK 500    SER A 696      -95.09    -71.85
REMARK 500    GLN A 713      -82.22    -65.08
REMARK 500    SER A 715      -21.40    171.27
REMARK 500    CYS A 724      -89.90   -118.72
REMARK 500    SER A 725      -34.84   -135.86
REMARK 500    ALA A 728      -59.96   -137.00
REMARK 500    ALA A 746       -0.47   -146.97
REMARK 500    GLU A 747       -7.90   -159.18
REMARK 500    ASP A 751       57.47    -90.29
REMARK 500    VAL A 752       17.89    -59.94
REMARK 500    PHE A 753      -54.93   -134.96
REMARK 500    VAL A 767       75.63     79.16
REMARK 500    GLN A 768      -93.45    -77.90
REMARK 500    THR A 769      108.37    -39.71
REMARK 500    GLU A 771      -53.80   -147.08
REMARK 500    TYR A 773      -68.36    136.99
REMARK 500    ASP A 785       41.77    -85.17
REMARK 500    ALA B 549      -36.65    115.96
REMARK 500    ASN B 565       42.31   -158.07
REMARK 500    GLU B 576     -113.58    162.60
REMARK 500    ASN B 577      111.72   -170.55
REMARK 500    THR B 578       44.66   -175.19
REMARK 500    ASN B 582       84.93    -64.94
REMARK 500    TRP B 616       31.00    -93.85
REMARK 500    ARG B 630       25.43     43.24
REMARK 500    CYS B 635      147.04    162.99
REMARK 500    ASP B 642      -33.27   -158.05
REMARK 500    ASN B 672     -110.75   -119.15
REMARK 500    LYS B 677     -177.18     11.59
REMARK 500    SER B 678     -164.49   -112.88
REMARK 500    ARG B 679      137.64   -170.58
REMARK 500    VAL B 692      108.55    115.49
REMARK 500    SER B 696       23.16    -65.79
REMARK 500    GLN B 713      -71.28    -67.26
REMARK 500    SER B 715      -27.89   -155.09
REMARK 500    CYS B 724      -97.28   -134.41
REMARK 500    ALA B 728      -69.66   -129.28
REMARK 500    ASP B 751       60.17   -112.35
REMARK 500    VAL B 767       78.82     81.53
REMARK 500    GLN B 768      -83.98    -65.25
REMARK 500    ALA B 786      -49.03    134.10
REMARK 500    PHE B 787     -124.59    -70.86
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 B  17        DISTANCE =  5.84 ANGSTROMS
REMARK 525    HOH A  28        DISTANCE =  6.17 ANGSTROMS
REMARK 525    HOH A  38        DISTANCE =  5.97 ANGSTROMS
REMARK 525    HOH B  53        DISTANCE =  5.94 ANGSTROMS
REMARK 525    HOH B  57        DISTANCE =  8.97 ANGSTROMS
REMARK 525    HOH A  47        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH A  88        DISTANCE =  5.67 ANGSTROMS
REMARK 525    HOH A  89        DISTANCE =  7.20 ANGSTROMS
REMARK 525    HOH A  93        DISTANCE =  6.57 ANGSTROMS
REMARK 525    HOH A 106        DISTANCE =  6.02 ANGSTROMS
REMARK 525    HOH A 109        DISTANCE =  5.33 ANGSTROMS
REMARK 525    HOH A 113        DISTANCE =  5.04 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P13   RELATED DB: PDB
DBREF  1P15 A  542   794  UNP    P18052   PTPRA_MOUSE    577    829
DBREF  1P15 B  542   794  UNP    P18052   PTPRA_MOUSE    577    829
SEQRES   1 A  253  MET ARG THR GLY ASN LEU PRO ALA ASN MET LYS LYS ASN
SEQRES   2 A  253  ARG VAL LEU GLN ILE ILE PRO TYR GLU PHE ASN ARG VAL
SEQRES   3 A  253  ILE ILE PRO VAL LYS ARG GLY GLU GLU ASN THR ASP TYR
SEQRES   4 A  253  VAL ASN ALA SER PHE ILE ASP GLY TYR ARG GLN LYS ASP
SEQRES   5 A  253  SER TYR ILE ALA SER GLN GLY PRO LEU LEU HIS THR ILE
SEQRES   6 A  253  GLU ASP PHE TRP ARG MET ILE TRP GLU TRP LYS SER CYS
SEQRES   7 A  253  SER ILE VAL MET LEU THR GLU LEU GLU GLU ARG GLY GLN
SEQRES   8 A  253  GLU LYS CYS ALA GLN TYR TRP PRO SER ASP GLY LEU VAL
SEQRES   9 A  253  SER TYR GLY ASP ILE THR VAL GLU LEU LYS LYS GLU GLU
SEQRES  10 A  253  GLU CYS GLU SER TYR THR VAL ARG ASP LEU LEU VAL THR
SEQRES  11 A  253  ASN THR ARG GLU ASN LYS SER ARG GLN ILE ARG GLN PHE
SEQRES  12 A  253  HIS PHE HIS GLY TRP PRO GLU VAL GLY ILE PRO SER ASP
SEQRES  13 A  253  GLY LYS GLY MET ILE ASN ILE ILE ALA ALA VAL GLN LYS
SEQRES  14 A  253  GLN GLN GLN GLN SER GLY ASN HIS PRO ILE THR VAL HIS
SEQRES  15 A  253  CYS SER ALA GLY ALA GLY ARG THR GLY THR PHE CYS ALA
SEQRES  16 A  253  LEU SER THR VAL LEU GLU ARG VAL LYS ALA GLU GLY ILE
SEQRES  17 A  253  LEU ASP VAL PHE GLN THR VAL LYS SER LEU ARG LEU GLN
SEQRES  18 A  253  ARG PRO HIS MET VAL GLN THR LEU GLU GLN TYR GLU PHE
SEQRES  19 A  253  CYS TYR LYS VAL VAL GLN GLU TYR ILE ASP ALA PHE SER
SEQRES  20 A  253  ASP TYR ALA ASN PHE LYS
SEQRES   1 B  253  MET ARG THR GLY ASN LEU PRO ALA ASN MET LYS LYS ASN
SEQRES   2 B  253  ARG VAL LEU GLN ILE ILE PRO TYR GLU PHE ASN ARG VAL
SEQRES   3 B  253  ILE ILE PRO VAL LYS ARG GLY GLU GLU ASN THR ASP TYR
SEQRES   4 B  253  VAL ASN ALA SER PHE ILE ASP GLY TYR ARG GLN LYS ASP
SEQRES   5 B  253  SER TYR ILE ALA SER GLN GLY PRO LEU LEU HIS THR ILE
SEQRES   6 B  253  GLU ASP PHE TRP ARG MET ILE TRP GLU TRP LYS SER CYS
SEQRES   7 B  253  SER ILE VAL MET LEU THR GLU LEU GLU GLU ARG GLY GLN
SEQRES   8 B  253  GLU LYS CYS ALA GLN TYR TRP PRO SER ASP GLY LEU VAL
SEQRES   9 B  253  SER TYR GLY ASP ILE THR VAL GLU LEU LYS LYS GLU GLU
SEQRES  10 B  253  GLU CYS GLU SER TYR THR VAL ARG ASP LEU LEU VAL THR
SEQRES  11 B  253  ASN THR ARG GLU ASN LYS SER ARG GLN ILE ARG GLN PHE
SEQRES  12 B  253  HIS PHE HIS GLY TRP PRO GLU VAL GLY ILE PRO SER ASP
SEQRES  13 B  253  GLY LYS GLY MET ILE ASN ILE ILE ALA ALA VAL GLN LYS
SEQRES  14 B  253  GLN GLN GLN GLN SER GLY ASN HIS PRO ILE THR VAL HIS
SEQRES  15 B  253  CYS SER ALA GLY ALA GLY ARG THR GLY THR PHE CYS ALA
SEQRES  16 B  253  LEU SER THR VAL LEU GLU ARG VAL LYS ALA GLU GLY ILE
SEQRES  17 B  253  LEU ASP VAL PHE GLN THR VAL LYS SER LEU ARG LEU GLN
SEQRES  18 B  253  ARG PRO HIS MET VAL GLN THR LEU GLU GLN TYR GLU PHE
SEQRES  19 B  253  CYS TYR LYS VAL VAL GLN GLU TYR ILE ASP ALA PHE SER
SEQRES  20 B  253  ASP TYR ALA ASN PHE LYS
FORMUL   3  HOH   *115(H2 O)
HELIX    1   1 ARG A  543  LEU A  547  5                                   5
HELIX    2   2 THR A  605  TRP A  616  1                                  12
HELIX    3   3 GLY A  700  GLN A  712  1                                  13
HELIX    4   4 ALA A  728  GLY A  748  1                                  21
HELIX    5   5 PHE A  753  LEU A  761  1                                   9
HELIX    6   6 TYR A  773  TYR A  783  1                                  11
HELIX    7   7 ASN B  550  ASN B  554  5                                   5
HELIX    8   8 TYR B  562  ARG B  566  5                                   5
HELIX    9   9 LEU B  602  HIS B  604  5                                   3
HELIX   10  10 THR B  605  TRP B  616  1                                  12
HELIX   11  11 GLY B  698  GLN B  712  1                                  15
HELIX   12  12 ALA B  728  GLU B  747  1                                  20
HELIX   13  13 ASP B  751  LEU B  761  1                                  11
HELIX   14  14 THR B  769  ASP B  785  1                                  17
SHEET    1   A 7 ALA A 583  ILE A 586  0
SHEET    2   A 7 TYR A 595  SER A 598 -1  O  TYR A 595   N  ILE A 586
SHEET    3   A 7 ILE A 720  HIS A 723  1  O  VAL A 722   N  SER A 598
SHEET    4   A 7 SER A 620  MET A 623  1  N  VAL A 622   O  THR A 721
SHEET    5   A 7 LYS A 677  PHE A 686  1  O  PHE A 684   N  ILE A 621
SHEET    6   A 7 TYR A 663  THR A 671 -1  N  ARG A 666   O  GLN A 683
SHEET    7   A 7 GLU A 658  GLU A 659 -1  N  GLU A 658   O  VAL A 665
SHEET    1   B 2 SER A 646  TYR A 647  0
SHEET    2   B 2 ILE A 650  THR A 651 -1  O  ILE A 650   N  TYR A 647
SHEET    1   C 8 ALA B 583  GLY B 588  0
SHEET    2   C 8 GLN B 591  SER B 598 -1  O  GLN B 591   N  GLY B 588
SHEET    3   C 8 ILE B 720  HIS B 723  1  O  VAL B 722   N  SER B 598
SHEET    4   C 8 SER B 620  MET B 623  1  N  VAL B 622   O  THR B 721
SHEET    5   C 8 SER B 678  PHE B 686  1  O  PHE B 684   N  ILE B 621
SHEET    6   C 8 TYR B 663  THR B 671 -1  N  THR B 664   O  HIS B 685
SHEET    7   C 8 ILE B 650  GLU B 659 -1  N  THR B 651   O  THR B 671
SHEET    8   C 8 LEU B 644  TYR B 647 -1  N  TYR B 647   O  ILE B 650
SHEET    1   D 2 GLU B 628  GLU B 629  0
SHEET    2   D 2 GLN B 632  GLU B 633 -1  O  GLN B 632   N  GLU B 629
CRYST1   59.101   59.101  152.657  90.00  90.00 120.00 P 31          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      0.016920  0.009769  0.000000        0.00000
SCALE2      0.000000  0.019538  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006551        0.00000
      
PROCHECK
Go to PROCHECK summary
 References