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PDBsum entry 2ixn

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Top Page protein Protein-protein interface(s) links
Isomerase PDB id
2ixn
Jmol
Contents
Protein chains
292 a.a.
HEADER    ISOMERASE                               09-JUL-06   2IXN
TITLE     CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE ACTIVATOR YPA2
TITLE    2 PTPA2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE 2A ACTIVATOR 2;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: RESIDUES 1-304;
COMPND   5 SYNONYM: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE PTPA-2, PPIASE PTPA-2,
COMPND   6  ROTAMASE PTPA-2, PTPA2, PHOSPHOTYROSYL PHOSPHATASE ACTIVATOR 2;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE   4 ORGANISM_TAXID: 4932;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: GOLD (DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET9
KEYWDS    PP2A PHOSPHATASE ACTIVATOR PROLYL ISOMERASE PTPA, ISOMERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    N.LEULLIOT,G.VICENTINI,J.JORDENS,S.QUEVILLON-CHERUEL,M.SCHILTZ,
AUTHOR   2 D.BARFORD,H.VAN TILBEURGH,J.GORIS
REVDAT   4   13-JUL-11 2IXN    1       VERSN
REVDAT   3   24-FEB-09 2IXN    1       VERSN
REVDAT   2   09-AUG-06 2IXN    1       JRNL
REVDAT   1   31-JUL-06 2IXN    0
JRNL        AUTH   N.LEULLIOT,G.VICENTINI,J.JORDENS,S.QUEVILLON-CHERUEL,
JRNL        AUTH 2 M.SCHILTZ,D.BARFORD,H.VAN TILBEURGH,J.GORIS
JRNL        TITL   CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE ACTIVATOR:
JRNL        TITL 2 IMPLICATIONS FOR ITS PP2A-SPECIFIC PPIASE ACTIVITY
JRNL        REF    MOL.CELL                      V.  23   413 2006
JRNL        REFN                   ISSN 1097-2765
JRNL        PMID   16885030
JRNL        DOI    10.1016/J.MOLCEL.2006.07.008
REMARK   2
REMARK   2 RESOLUTION.    2.8  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.3
REMARK   3   NUMBER OF REFLECTIONS             : 16283
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 + TEST SET) : 0.202
REMARK   3   R VALUE            (WORKING SET) : 0.199
REMARK   3   FREE R VALUE                     : 0.273
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 897
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1201
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3120
REMARK   3   BIN FREE R VALUE SET COUNT          : 64
REMARK   3   BIN FREE R VALUE                    : 0.3250
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4792
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          :
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.48
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.38000
REMARK   3    B22 (A**2) : 2.13000
REMARK   3    B33 (A**2) : -0.75000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
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): 0.432
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.323
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 36.688
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4920 ; 0.022 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6628 ; 2.226 ; 1.954
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   572 ; 8.678 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   234 ;37.582 ;23.675
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   902 ;24.950 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;22.792 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   702 ; 0.160 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3674 ; 0.007 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2453 ; 0.280 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3362 ; 0.337 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   203 ; 0.185 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    29 ; 0.274 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.326 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2939 ; 0.751 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4660 ; 1.369 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2264 ; 2.129 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1968 ; 3.338 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 2
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     3        A   299
REMARK   3    ORIGIN FOR THE GROUP (A):  56.9640  28.2260   1.0910
REMARK   3    T TENSOR
REMARK   3      T11:   0.0885 T22:   0.4011
REMARK   3      T33:   0.0698 T12:  -0.0627
REMARK   3      T13:  -0.0650 T23:   0.0778
REMARK   3    L TENSOR
REMARK   3      L11:   5.4437 L22:   1.8848
REMARK   3      L33:   2.0819 L12:   1.7840
REMARK   3      L13:  -0.2208 L23:  -0.4497
REMARK   3    S TENSOR
REMARK   3      S11:   0.1960 S12:  -0.6641 S13:  -0.0837
REMARK   3      S21:   0.0696 S22:  -0.0068 S23:   0.1278
REMARK   3      S31:   0.0920 S32:  -0.1800 S33:  -0.1891
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     3        B   299
REMARK   3    ORIGIN FOR THE GROUP (A):  20.5510  16.7040 -22.2240
REMARK   3    T TENSOR
REMARK   3      T11:   0.0034 T22:   0.3554
REMARK   3      T33:   0.0212 T12:  -0.0437
REMARK   3      T13:   0.0145 T23:   0.0629
REMARK   3    L TENSOR
REMARK   3      L11:   2.2523 L22:   2.4630
REMARK   3      L33:   5.0630 L12:   0.7868
REMARK   3      L13:   0.7246 L23:  -0.9988
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1708 S12:   0.2932 S13:  -0.0674
REMARK   3      S21:  -0.0491 S22:  -0.1792 S23:   0.0224
REMARK   3      S31:  -0.3281 S32:   0.2722 S33:   0.3500
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 2IXN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUL-06.
REMARK 100 THE PDBE ID CODE IS EBI-29332.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 5.60
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 176445
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.4
REMARK 200  DATA REDUNDANCY                : 9.300
REMARK 200  R MERGE                    (I) : 0.19000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.87
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
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: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX, HYSS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG4000, 0.4M KCL, PH 5.6,
REMARK 280  0.1M TRIS-HCL PH 8.5
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       26.86750
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       26.86750
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       78.96500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       85.52100
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       78.96500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       85.52100
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       26.86750
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       78.96500
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       85.52100
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       26.86750
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       78.96500
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       85.52100
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 BIOMOLECULE:  2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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     MET A     1
REMARK 465     LEU A     2
REMARK 465     ASP A    74
REMARK 465     ALA A    75
REMARK 465     ASP A    76
REMARK 465     SER A    77
REMARK 465     SER A    78
REMARK 465     PRO A   300
REMARK 465     ASP A   301
REMARK 465     GLY A   302
REMARK 465     VAL A   303
REMARK 465     SER A   304
REMARK 465     HIS A   305
REMARK 465     HIS A   306
REMARK 465     HIS A   307
REMARK 465     HIS A   308
REMARK 465     HIS A   309
REMARK 465     HIS A   310
REMARK 465     MET B     1
REMARK 465     LEU B     2
REMARK 465     ASP B    74
REMARK 465     ALA B    75
REMARK 465     ASP B    76
REMARK 465     SER B    77
REMARK 465     HIS B   188
REMARK 465     GLY B   189
REMARK 465     VAL B   190
REMARK 465     TRP B   191
REMARK 465     SER B   246
REMARK 465     SER B   247
REMARK 465     ALA B   248
REMARK 465     PRO B   300
REMARK 465     ASP B   301
REMARK 465     GLY B   302
REMARK 465     VAL B   303
REMARK 465     SER B   304
REMARK 465     HIS B   305
REMARK 465     HIS B   306
REMARK 465     HIS B   307
REMARK 465     HIS B   308
REMARK 465     HIS B   309
REMARK 465     HIS B   310
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     PRO A   3    CG   CD
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    TRP A    16     OG   SER A    19              2.13
REMARK 500   O    THR B    66     N    LYS B    68              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A 223   CG    GLU A 223   CD      0.105
REMARK 500    THR B   9   N     THR B   9   CA      0.138
REMARK 500    GLU B 121   CB    GLU B 121   CG     -0.115
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    LEU A   7   CA  -  CB  -  CG  ANGL. DEV. =  16.7 DEGREES
REMARK 500    ARG A 101   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG A 101   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    LEU A 154   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES
REMARK 500    LEU A 161   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES
REMARK 500    CYS A 299   CA  -  CB  -  SG  ANGL. DEV. =  -7.1 DEGREES
REMARK 500    PRO B  10   C   -  N   -  CA  ANGL. DEV. =  23.4 DEGREES
REMARK 500    PRO B  10   C   -  N   -  CD  ANGL. DEV. = -20.4 DEGREES
REMARK 500    LEU B 193   CA  -  CB  -  CG  ANGL. DEV. =  14.6 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    LEU A   7       31.78   -148.39
REMARK 500    THR A   9     -142.96   -155.63
REMARK 500    ASP A  11       15.05   -140.89
REMARK 500    THR A  21      -72.05    -60.07
REMARK 500    ARG A  22      -66.63    -21.02
REMARK 500    GLU A  46     -134.29    -56.19
REMARK 500    PRO A  47      103.63    -31.77
REMARK 500    SER A 158      -72.12      7.10
REMARK 500    SER A 187       30.51    -88.18
REMARK 500    PHE A 198      -64.40   -122.75
REMARK 500    LEU A 202      -74.89    -40.82
REMARK 500    HIS A 213      -43.38   -138.33
REMARK 500    ILE A 217      -19.56    -43.56
REMARK 500    LYS A 243      -71.10    -58.76
REMARK 500    VAL A 244      -62.29    -27.83
REMARK 500    LYS A 245       45.19    -97.12
REMARK 500    SER A 246      127.85    -39.01
REMARK 500    SER A 247        3.58     44.69
REMARK 500    SER A 254       92.67   -161.36
REMARK 500    SER A 283       33.80   -141.60
REMARK 500    LEU A 285      -70.37    -34.79
REMARK 500    LEU A 297       76.23   -117.33
REMARK 500    ASN B  41      -32.22    -28.14
REMARK 500    GLN B  43       54.39   -150.30
REMARK 500    ASN B  57       47.79    -99.40
REMARK 500    THR B  66      -72.42    -51.43
REMARK 500    GLN B  67       28.41    -57.41
REMARK 500    LYS B  68       18.90   -140.61
REMARK 500    GLU B  84      -31.51    -36.51
REMARK 500    SER B  96      -49.17    -28.16
REMARK 500    LYS B 164      -73.97    -83.57
REMARK 500    TRP B 181       46.96     71.38
REMARK 500    PHE B 198      -69.32   -127.79
REMARK 500    GLN B 207      -39.73    -35.90
REMARK 500    HIS B 213      -42.28   -133.49
REMARK 500    SER B 254       76.92   -116.37
REMARK 500    VAL B 281      -62.90   -106.98
REMARK 500    PRO B 286      -32.43    -25.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 GLU A    4     LYS A    5                 -138.36
REMARK 500 THR A    9     PRO A   10                 -139.80
REMARK 500 ASP A   11     ASP A   12                  148.16
REMARK 500 GLY B   38     HIS B   39                 -147.32
REMARK 500 PRO B  298     CYS B  299                  149.01
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    GLU A   4        23.9      L          L   OUTSIDE RANGE
REMARK 500    LEU A   8        23.7      L          L   OUTSIDE RANGE
REMARK 500    THR A   9        21.5      L          L   OUTSIDE RANGE
REMARK 500    GLU A  46        12.4      L          L   OUTSIDE RANGE
REMARK 500    ASN A  57        23.7      L          L   OUTSIDE RANGE
REMARK 500    SER A 247        24.1      L          L   OUTSIDE RANGE
REMARK 500    LEU B   7        24.4      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2IXO   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE
REMARK 900  ACTIVATOR YPA1 PTPA1
REMARK 900 RELATED ID: 2IXP   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE
REMARK 900  ACTIVATOR YPA1 PTPA1 IN COMPLEX WITH MODEL
REMARK 900  SUBSTRATE
DBREF  2IXN A    1   304  UNP    Q12461   PTPA2_YEAST      1    304
DBREF  2IXN A  305   310  PDB    2IXN     2IXN           305    310
DBREF  2IXN B    1   304  UNP    Q12461   PTPA2_YEAST      1    304
DBREF  2IXN B  305   310  PDB    2IXN     2IXN           305    310
SEQRES   1 A  310  MET LEU PRO GLU LYS ARG LEU LEU THR PRO ASP ASP MET
SEQRES   2 A  310  LYS LEU TRP GLU GLU SER PRO THR ARG ALA HIS PHE THR
SEQRES   3 A  310  LYS PHE ILE ILE ASP LEU ALA GLU SER VAL LYS GLY HIS
SEQRES   4 A  310  GLU ASN SER GLN TYR LYS GLU PRO ILE SER GLU SER ILE
SEQRES   5 A  310  ASN SER MET MET ASN LEU LEU SER GLN ILE LYS ASP ILE
SEQRES   6 A  310  THR GLN LYS HIS PRO VAL ILE LYS ASP ALA ASP SER SER
SEQRES   7 A  310  ARG PHE GLY LYS VAL GLU PHE ARG ASP PHE TYR ASP GLU
SEQRES   8 A  310  VAL SER ARG ASN SER ARG LYS ILE LEU ARG SER GLU PHE
SEQRES   9 A  310  PRO SER LEU THR ASP GLU GLN LEU GLU GLN LEU SER ILE
SEQRES  10 A  310  TYR LEU ASP GLU SER TRP GLY ASN LYS ARG ARG ILE ASP
SEQRES  11 A  310  TYR GLY SER GLY HIS GLU LEU ASN PHE MET CYS LEU LEU
SEQRES  12 A  310  TYR GLY LEU TYR SER TYR GLY ILE PHE ASN LEU SER ASN
SEQRES  13 A  310  ASP SER THR ASN LEU VAL LEU LYS VAL PHE ILE GLU TYR
SEQRES  14 A  310  LEU LYS ILE MET ARG ILE LEU GLU THR LYS TYR TRP LEU
SEQRES  15 A  310  GLU PRO ALA GLY SER HIS GLY VAL TRP GLY LEU ASP ASP
SEQRES  16 A  310  TYR HIS PHE LEU PRO PHE LEU PHE GLY ALA PHE GLN LEU
SEQRES  17 A  310  THR THR HIS LYS HIS LEU LYS PRO ILE SER ILE HIS ASN
SEQRES  18 A  310  ASN GLU LEU VAL GLU MET PHE ALA HIS ARG TYR LEU TYR
SEQRES  19 A  310  PHE GLY CYS ILE ALA PHE ILE ASN LYS VAL LYS SER SER
SEQRES  20 A  310  ALA SER LEU ARG TRP HIS SER PRO MET LEU ASP ASP ILE
SEQRES  21 A  310  SER GLY VAL LYS THR TRP SER LYS VAL ALA GLU GLY MET
SEQRES  22 A  310  ILE LYS MET TYR LYS ALA GLU VAL LEU SER LYS LEU PRO
SEQRES  23 A  310  ILE MET GLN HIS PHE TYR PHE SER GLU PHE LEU PRO CYS
SEQRES  24 A  310  PRO ASP GLY VAL SER HIS HIS HIS HIS HIS HIS
SEQRES   1 B  310  MET LEU PRO GLU LYS ARG LEU LEU THR PRO ASP ASP MET
SEQRES   2 B  310  LYS LEU TRP GLU GLU SER PRO THR ARG ALA HIS PHE THR
SEQRES   3 B  310  LYS PHE ILE ILE ASP LEU ALA GLU SER VAL LYS GLY HIS
SEQRES   4 B  310  GLU ASN SER GLN TYR LYS GLU PRO ILE SER GLU SER ILE
SEQRES   5 B  310  ASN SER MET MET ASN LEU LEU SER GLN ILE LYS ASP ILE
SEQRES   6 B  310  THR GLN LYS HIS PRO VAL ILE LYS ASP ALA ASP SER SER
SEQRES   7 B  310  ARG PHE GLY LYS VAL GLU PHE ARG ASP PHE TYR ASP GLU
SEQRES   8 B  310  VAL SER ARG ASN SER ARG LYS ILE LEU ARG SER GLU PHE
SEQRES   9 B  310  PRO SER LEU THR ASP GLU GLN LEU GLU GLN LEU SER ILE
SEQRES  10 B  310  TYR LEU ASP GLU SER TRP GLY ASN LYS ARG ARG ILE ASP
SEQRES  11 B  310  TYR GLY SER GLY HIS GLU LEU ASN PHE MET CYS LEU LEU
SEQRES  12 B  310  TYR GLY LEU TYR SER TYR GLY ILE PHE ASN LEU SER ASN
SEQRES  13 B  310  ASP SER THR ASN LEU VAL LEU LYS VAL PHE ILE GLU TYR
SEQRES  14 B  310  LEU LYS ILE MET ARG ILE LEU GLU THR LYS TYR TRP LEU
SEQRES  15 B  310  GLU PRO ALA GLY SER HIS GLY VAL TRP GLY LEU ASP ASP
SEQRES  16 B  310  TYR HIS PHE LEU PRO PHE LEU PHE GLY ALA PHE GLN LEU
SEQRES  17 B  310  THR THR HIS LYS HIS LEU LYS PRO ILE SER ILE HIS ASN
SEQRES  18 B  310  ASN GLU LEU VAL GLU MET PHE ALA HIS ARG TYR LEU TYR
SEQRES  19 B  310  PHE GLY CYS ILE ALA PHE ILE ASN LYS VAL LYS SER SER
SEQRES  20 B  310  ALA SER LEU ARG TRP HIS SER PRO MET LEU ASP ASP ILE
SEQRES  21 B  310  SER GLY VAL LYS THR TRP SER LYS VAL ALA GLU GLY MET
SEQRES  22 B  310  ILE LYS MET TYR LYS ALA GLU VAL LEU SER LYS LEU PRO
SEQRES  23 B  310  ILE MET GLN HIS PHE TYR PHE SER GLU PHE LEU PRO CYS
SEQRES  24 B  310  PRO ASP GLY VAL SER HIS HIS HIS HIS HIS HIS
HELIX    1   1 MET A   13  GLU A   18  1                                   6
HELIX    2   2 SER A   19  SER A   35  1                                  17
HELIX    3   3 SER A   49  GLN A   67  1                                  19
HELIX    4   4 VAL A   83  PHE A  104  1                                  22
HELIX    5   5 THR A  108  GLU A  121  1                                  14
HELIX    6   6 GLY A  132  TYR A  149  1                                  18
HELIX    7   7 ASN A  153  TRP A  181  1                                  29
HELIX    8   8 PHE A  198  LEU A  208  1                                  11
HELIX    9   9 LYS A  215  HIS A  220  5                                   6
HELIX   10  10 ASN A  221  ALA A  229  1                                   9
HELIX   11  11 TYR A  232  LYS A  245  1                                  14
HELIX   12  12 SER A  249  SER A  254  1                                   6
HELIX   13  13 SER A  254  SER A  261  1                                   8
HELIX   14  14 THR A  265  VAL A  281  1                                  17
HELIX   15  15 LYS A  284  GLN A  289  1                                   6
HELIX   16  16 ASP B   11  GLU B   18  1                                   8
HELIX   17  17 SER B   19  VAL B   36  1                                  18
HELIX   18  18 SER B   49  GLN B   67  1                                  19
HELIX   19  19 VAL B   83  PHE B  104  1                                  22
HELIX   20  20 THR B  108  GLU B  121  1                                  14
HELIX   21  21 GLY B  132  TYR B  149  1                                  18
HELIX   22  22 ASN B  153  TYR B  180  1                                  28
HELIX   23  23 PHE B  198  GLN B  207  1                                  10
HELIX   24  24 LYS B  215  ASN B  221  5                                   7
HELIX   25  25 GLU B  223  ALA B  229  1                                   7
HELIX   26  26 TYR B  232  LYS B  245  1                                  14
HELIX   27  27 SER B  249  SER B  254  1                                   6
HELIX   28  28 SER B  254  ILE B  260  1                                   7
HELIX   29  29 THR B  265  VAL B  281  1                                  17
HELIX   30  30 LYS B  284  GLN B  289  1                                   6
SHEET    1  AA 2 ASP A 130  TYR A 131  0
SHEET    2  AA 2 GLU A 183  PRO A 184  1  O  GLU A 183   N  TYR A 131
SHEET    1  BA 2 ASP B 130  TYR B 131  0
SHEET    2  BA 2 GLU B 183  PRO B 184  1  O  GLU B 183   N  TYR B 131
CISPEP   1 THR B    9    PRO B   10          0       -27.09
CRYST1  157.930  171.042   53.735  90.00  90.00  90.00 C 2 2 21     16
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      0.006332  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005847  0.000000        0.00000
SCALE3      0.000000  0.000000  0.018610        0.00000
      
PROCHECK
Go to PROCHECK summary
 References