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PDBsum entry 2nz6

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Hydrolase PDB id
2nz6
Jmol
Contents
Protein chain
296 a.a.
Ligands
PO4
Metals
_CL
_NI ×5
Waters ×94
HEADER    HYDROLASE                               22-NOV-06   2NZ6
TITLE     CRYSTAL STRUCTURE OF THE PTPRJ INACTIVATING MUTANT C1239S
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE ETA;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: TYROSINE-PROTEIN PHOSPHATASE;
COMPND   5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE ETA, R-PTP-ETA, HPTP ETA,
COMPND   6 PROTEIN- TYROSINE PHOSPHATASE RECEPTOR TYPE J, DENSITY-ENHANCED
COMPND   7 PHOSPHATASE 1, DEP-1, CD148 ANTIGEN;
COMPND   8 EC: 3.1.3.48;
COMPND   9 ENGINEERED: YES;
COMPND  10 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: PTPRJ;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS    HYDROLASE RECEPTOR TYPE TYROSINE PHOSPHATASE J, PTPRJ, GLYCOPROTEIN,
KEYWDS   2 PROTEIN PHOSPHATASE, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS
KEYWDS   3 CONSORTIUM, SGC, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.UGOCHUKWU,A.BARR,P.SAVITSKY,A.C.W.PIKE,G.BUNKOCZI,M.SUNDSTROM,
AUTHOR   2 J.WEIGELT,C.H.ARROWSMITH,A.EDWARDS,F.VON DELFT,S.KNAPP,STRUCTURAL
AUTHOR   3 GENOMICS CONSORTIUM (SGC)
REVDAT   5   13-JUL-11 2NZ6    1       VERSN
REVDAT   4   09-JUN-09 2NZ6    1       REVDAT
REVDAT   3   24-FEB-09 2NZ6    1       VERSN
REVDAT   2   03-FEB-09 2NZ6    1       JRNL
REVDAT   1   12-DEC-06 2NZ6    0
JRNL        AUTH   A.J.BARR,E.UGOCHUKWU,W.H.LEE,O.N.KING,P.FILIPPAKOPOULOS,
JRNL        AUTH 2 I.ALFANO,P.SAVITSKY,N.A.BURGESS-BROWN,S.MULLER,S.KNAPP
JRNL        TITL   LARGE-SCALE STRUCTURAL ANALYSIS OF THE CLASSICAL HUMAN
JRNL        TITL 2 PROTEIN TYROSINE PHOSPHATOME.
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 136   352 2009
JRNL        REFN                   ISSN 0092-8674
JRNL        PMID   19167335
JRNL        DOI    10.1016/J.CELL.2008.11.038
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
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) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.98
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2
REMARK   3   NUMBER OF REFLECTIONS             : 14581
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) : 0.184
REMARK   3   R VALUE            (WORKING SET) : 0.182
REMARK   3   FREE R VALUE                     : 0.228
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800
REMARK   3   FREE R VALUE TEST SET COUNT      : 738
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) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 968
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.60
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270
REMARK   3   BIN FREE R VALUE SET COUNT          : 57
REMARK   3   BIN FREE R VALUE                    : 0.3840
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2380
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 11
REMARK   3   SOLVENT ATOMS            : 94
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) : 22.44
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.31000
REMARK   3    B22 (A**2) : 0.31000
REMARK   3    B33 (A**2) : -0.47000
REMARK   3    B12 (A**2) : 0.16000
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): 0.315
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.221
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.158
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.948
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2458 ; 0.011 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  1594 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3345 ; 1.291 ; 1.929
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3880 ; 1.314 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   292 ; 6.569 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   125 ;38.257 ;24.240
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   392 ;14.494 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;16.095 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   366 ; 0.077 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2736 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   511 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   444 ; 0.199 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1603 ; 0.198 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1202 ; 0.175 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1217 ; 0.087 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   106 ; 0.147 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.042 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    39 ; 0.180 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    38 ; 0.173 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.078 ; 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):  1533 ; 0.596 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   592 ; 0.107 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2398 ; 0.978 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1087 ; 1.391 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   947 ; 1.901 ; 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  : 1
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   -21        A  1303
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.3409  29.3880 -13.9498
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0848 T22:  -0.1260
REMARK   3      T33:  -0.1298 T12:  -0.0195
REMARK   3      T13:   0.0105 T23:   0.0067
REMARK   3    L TENSOR
REMARK   3      L11:   0.9952 L22:   1.9150
REMARK   3      L33:   1.4601 L12:  -0.2978
REMARK   3      L13:  -0.1515 L23:  -0.6791
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0626 S12:  -0.1023 S13:  -0.1365
REMARK   3      S21:   0.1607 S22:   0.0587 S23:   0.0983
REMARK   3      S31:   0.1221 S32:  -0.0931 S33:   0.0039
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
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 RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 2NZ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-06.
REMARK 100 THE RCSB ID CODE IS RCSB040484.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 06-MAY-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X10SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15274
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.980
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2
REMARK 200  DATA REDUNDANCY                : 3.300
REMARK 200  R MERGE                    (I) : 0.08900
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) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.38700
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: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2CFV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M NICL2, 0.1M TRIS, PH 8.5, 1M
REMARK 280  LI2SO4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290       9555   -X+Y+1/3,-X+2/3,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        0.00000
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        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.26050
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       25.55381
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       39.65000
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       44.26050
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       25.55381
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       39.65000
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       44.26050
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       25.55381
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       39.65000
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       51.10762
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       79.30000
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       51.10762
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       79.30000
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       51.10762
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       79.30000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 10470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -168.0 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 -0.500000 -0.866025  0.000000       44.26050
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       76.66143
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      -44.26050
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000       76.66143
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 NI    NI A 201  LIES ON A SPECIAL POSITION.
REMARK 375 NI    NI A 206  LIES ON A SPECIAL POSITION.
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   -22
REMARK 465     CYS A  1141
REMARK 465     VAL A  1142
REMARK 465     GLU A  1143
REMARK 465     GLN A  1144
REMARK 465     GLY A  1145
REMARK 465     ARG A  1146
REMARK 465     THR A  1147
REMARK 465     LYS A  1148
REMARK 465     CYS A  1149
REMARK 465     GLU A  1150
REMARK 465     LYS A  1227
REMARK 465     GLN A  1228
REMARK 465     SER A  1229
REMARK 465     PRO A  1230
REMARK 465     PRO A  1231
REMARK 465     ASP A  1304
REMARK 465     SER A  1305
REMARK 465     LYS A  1306
REMARK 465     VAL A  1307
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     GLN A  -2    CG   CD   OE1  NE2
REMARK 470     ARG A1022    NE   CZ   NH1  NH2
REMARK 470     LYS A1031    CE   NZ
REMARK 470     LYS A1032    CE   NZ
REMARK 470     SER A1037    OG
REMARK 470     GLU A1043    CD   OE1  OE2
REMARK 470     GLU A1046    CD   OE1  OE2
REMARK 470     LYS A1049    CD   CE   NZ
REMARK 470     ARG A1066    NE   CZ   NH1  NH2
REMARK 470     LYS A1083    CE   NZ
REMARK 470     LYS A1121    CE   NZ
REMARK 470     TYR A1133    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LYS A1140    CD   CE   NZ
REMARK 470     GLU A1151    OE1  OE2
REMARK 470     LYS A1156    CG   CD   CE   NZ
REMARK 470     GLU A1176    CG   CD   OE1  OE2
REMARK 470     ILE A1187    CG1  CG2  CD1
REMARK 470     ASP A1224    OD1  OD2
REMARK 470     GLU A1232    CG   CD   OE1  OE2
REMARK 470     LYS A1303    CG   CD   CE   NZ
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    LYS A1057       48.36   -148.80
REMARK 500    SER A1155      -42.79   -133.72
REMARK 500    SER A1190       -0.76     79.43
REMARK 500    VAL A1243      -55.76   -127.23
REMARK 500    VAL A1282       90.73     64.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI A 201  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A -16   NE2
REMARK 620 2 HIS A -18   NE2  87.0
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI A 204  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A -20   N
REMARK 620 2 HIS A -21   N    85.8
REMARK 620 3 HIS A -20   ND1  97.7 176.5
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI A 205  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A -19   NE2
REMARK 620 2 HIS A -17   NE2 100.6
REMARK 620 3 HIS A1277   NE2 164.7  92.7
REMARK 620 4 LYS A1106   NZ   80.0 167.3  85.4
REMARK 620 5 HIS A -21   NE2  85.2  88.7 102.7 103.9
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI A 206  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A  96   O
REMARK 620 2 HIS A -20   NE2  94.8
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 207
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CFV   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE
REMARK 900 RECEPTOR TYPE J
DBREF  2NZ6 A 1019  1311  UNP    Q12913   PTPRJ_HUMAN   1019   1311
SEQADV 2NZ6 MET A  -22  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 HIS A  -21  UNP  Q12913              EXPRESSION TAG
SEQADV 2NZ6 HIS A  -20  UNP  Q12913              EXPRESSION TAG
SEQADV 2NZ6 HIS A  -19  UNP  Q12913              EXPRESSION TAG
SEQADV 2NZ6 HIS A  -18  UNP  Q12913              EXPRESSION TAG
SEQADV 2NZ6 HIS A  -17  UNP  Q12913              EXPRESSION TAG
SEQADV 2NZ6 HIS A  -16  UNP  Q12913              EXPRESSION TAG
SEQADV 2NZ6 SER A  -15  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 SER A  -14  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 GLY A  -13  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 VAL A  -12  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 ASP A  -11  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 LEU A  -10  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 GLY A   -9  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 THR A   -8  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 GLU A   -7  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 ASN A   -6  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 LEU A   -5  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 TYR A   -4  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 PHE A   -3  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 GLN A   -2  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 SER A   -1  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 MET A    0  UNP  Q12913              CLONING ARTIFACT
SEQADV 2NZ6 SER A 1239  UNP  Q12913    CYS  1239 ENGINEERED
SEQRES   1 A  316  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES   2 A  316  GLY THR GLU ASN LEU TYR PHE GLN SER MET LYS LEU ILE
SEQRES   3 A  316  ARG VAL GLU ASN PHE GLU ALA TYR PHE LYS LYS GLN GLN
SEQRES   4 A  316  ALA ASP SER ASN CYS GLY PHE ALA GLU GLU TYR GLU ASP
SEQRES   5 A  316  LEU LYS LEU VAL GLY ILE SER GLN PRO LYS TYR ALA ALA
SEQRES   6 A  316  GLU LEU ALA GLU ASN ARG GLY LYS ASN ARG TYR ASN ASN
SEQRES   7 A  316  VAL LEU PRO TYR ASP ILE SER ARG VAL LYS LEU SER VAL
SEQRES   8 A  316  GLN THR HIS SER THR ASP ASP TYR ILE ASN ALA ASN TYR
SEQRES   9 A  316  MET PRO GLY TYR HIS SER LYS LYS ASP PHE ILE ALA THR
SEQRES  10 A  316  GLN GLY PRO LEU PRO ASN THR LEU LYS ASP PHE TRP ARG
SEQRES  11 A  316  MET VAL TRP GLU LYS ASN VAL TYR ALA ILE ILE MET LEU
SEQRES  12 A  316  THR LYS CYS VAL GLU GLN GLY ARG THR LYS CYS GLU GLU
SEQRES  13 A  316  TYR TRP PRO SER LYS GLN ALA GLN ASP TYR GLY ASP ILE
SEQRES  14 A  316  THR VAL ALA MET THR SER GLU ILE VAL LEU PRO GLU TRP
SEQRES  15 A  316  THR ILE ARG ASP PHE THR VAL LYS ASN ILE GLN THR SER
SEQRES  16 A  316  GLU SER HIS PRO LEU ARG GLN PHE HIS PHE THR SER TRP
SEQRES  17 A  316  PRO ASP HIS GLY VAL PRO ASP THR THR ASP LEU LEU ILE
SEQRES  18 A  316  ASN PHE ARG TYR LEU VAL ARG ASP TYR MET LYS GLN SER
SEQRES  19 A  316  PRO PRO GLU SER PRO ILE LEU VAL HIS SER SER ALA GLY
SEQRES  20 A  316  VAL GLY ARG THR GLY THR PHE ILE ALA ILE ASP ARG LEU
SEQRES  21 A  316  ILE TYR GLN ILE GLU ASN GLU ASN THR VAL ASP VAL TYR
SEQRES  22 A  316  GLY ILE VAL TYR ASP LEU ARG MET HIS ARG PRO LEU MET
SEQRES  23 A  316  VAL GLN THR GLU ASP GLN TYR VAL PHE LEU ASN GLN CYS
SEQRES  24 A  316  VAL LEU ASP ILE VAL ARG SER GLN LYS ASP SER LYS VAL
SEQRES  25 A  316  ASP LEU ILE TYR
HET     NI  A 201       1
HET     NI  A 203       1
HET     NI  A 204       1
HET     NI  A 205       1
HET     NI  A 206       1
HET    PO4  A 207       5
HET     CL  A 208       1
HETNAM      NI NICKEL (II) ION
HETNAM     PO4 PHOSPHATE ION
HETNAM      CL CHLORIDE ION
FORMUL   2   NI    5(NI 2+)
FORMUL   7  PO4    O4 P 3-
FORMUL   8   CL    CL 1-
FORMUL   9  HOH   *94(H2 O)
HELIX    1   1 ASP A  -11  GLN A   -2  1                                  10
HELIX    2   2 VAL A 1023  LEU A 1048  1                                  26
HELIX    3   3 LEU A 1062  ASN A 1069  5                                   8
HELIX    4   4 HIS A 1089  TYR A 1094  5                                   6
HELIX    5   5 THR A 1119  LYS A 1130  1                                  12
HELIX    6   6 THR A 1211  MET A 1226  1                                  16
HELIX    7   7 VAL A 1243  GLU A 1262  1                                  20
HELIX    8   8 ASP A 1266  MET A 1276  1                                  11
HELIX    9   9 THR A 1284  LYS A 1303  1                                  20
SHEET    1   A 2 ILE A1021  ARG A1022  0
SHEET    2   A 2 THR A1264  VAL A1265 -1  O  VAL A1265   N  ILE A1021
SHEET    1   B 8 ALA A1097  MET A1100  0
SHEET    2   B 8 PHE A1109  GLN A1113 -1  O  ALA A1111   N  ASN A1098
SHEET    3   B 8 ILE A1235  SER A1239  1  O  VAL A1237   N  ILE A1110
SHEET    4   B 8 ALA A1134  LEU A1138  1  N  ILE A1136   O  LEU A1236
SHEET    5   B 8 SER A1192  PHE A1200  1  O  PHE A1198   N  ILE A1135
SHEET    6   B 8 TRP A1177  ASN A1186 -1  N  ARG A1180   O  GLN A1197
SHEET    7   B 8 ILE A1164  VAL A1173 -1  N  THR A1169   O  ASP A1181
SHEET    8   B 8 GLN A1159  TYR A1161 -1  N  TYR A1161   O  ILE A1164
LINK        NI    NI A 201                 NE2 HIS A -16     1555   1555  2.16
LINK        NI    NI A 201                 NE2 HIS A -18     1555   1555  2.28
LINK        NI    NI A 203                 NE2 HIS A1206     1555   1555  2.28
LINK        NI    NI A 204                 N   HIS A -20     1555   1555  2.02
LINK        NI    NI A 204                 N   HIS A -21     1555   1555  2.10
LINK        NI    NI A 204                 ND1 HIS A -20     1555   1555  1.91
LINK        NI    NI A 205                 NE2 HIS A -19     1555   1555  2.39
LINK        NI    NI A 205                 NE2 HIS A -17     1555   1555  2.22
LINK        NI    NI A 206                 O   HOH A  96     1555   1555  2.55
LINK        NI    NI A 206                 NE2 HIS A -20     1555   1555  2.04
LINK        NI    NI A 201                 NE2 HIS A -18     1555   2665  2.28
LINK        NI    NI A 201                 NE2 HIS A -18     1555   3565  2.28
LINK        NI    NI A 201                 NE2 HIS A -16     1555   2665  2.16
LINK        NI    NI A 201                 NE2 HIS A -16     1555   3565  2.16
LINK        NI    NI A 205                 NE2 HIS A1277     1555   3565  2.29
LINK        NI    NI A 205                 NZ  LYS A1106     1555   3565  2.09
LINK        NI    NI A 205                 NE2 HIS A -21     1555   2665  2.11
LINK        NI    NI A 206                 NE2 HIS A -20     1555   2665  2.13
LINK        NI    NI A 206                 NE2 HIS A -20     1555   3565  2.02
LINK        NI    NI A 206                 O   HOH A  96     1555   2665  2.62
LINK        NI    NI A 206                 O   HOH A  96     1555   3565  2.60
SITE     1 AC1  2 HIS A -18  HIS A -16
SITE     1 AC2  1 HIS A1206
SITE     1 AC3  3 HIS A -19  HIS A -20  HIS A -21
SITE     1 AC4  5 HIS A -21  HIS A -19  HIS A -17  LYS A1106
SITE     2 AC4  5 HIS A1277
SITE     1 AC5  2 HIS A -20  HOH A  96
SITE     1 AC6 10 HOH A  45  ASP A1205  SER A1239  SER A1240
SITE     2 AC6 10 ALA A1241  GLY A1242  VAL A1243  GLY A1244
SITE     3 AC6 10 ARG A1245  TYR A1311
CRYST1   88.521   88.521  118.950  90.00  90.00 120.00 H 3           9
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      0.011297  0.006522  0.000000        0.00000
SCALE2      0.000000  0.013044  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008407        0.00000
      
PROCHECK
Go to PROCHECK summary
 References