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PDBsum entry 2cfv

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Hydrolase PDB id
2cfv
Jmol
Contents
Protein chain
268 a.a.
Metals
_NI ×4
_CL
Waters ×25
HEADER    HYDROLASE                               23-FEB-06   2CFV
TITLE     CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE
TITLE    2 RECEPTOR TYPE J
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HUMAN PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE J;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 1019-1311;
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, CD14 8 ANTIGEN;
COMPND   8 EC: 3.1.3.48;
COMPND   9 ENGINEERED: 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: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PNIC28-BSA4
KEYWDS    HYDROLASE, RECEPTOR TYPE TYROSINE PHOSPHATASE J, PTPRJ,
KEYWDS   2 GLYCOPROTEIN, PROTEIN PHOSPHATASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.E.DEBRECZENI,A.J.BARR,J.ESWARAN,E.UGOCHUKWU,M.SUNDSTROM,J.WEIGELT,
AUTHOR   2 C.ARROWSMITH,A.EDWARDS,S.KNAPP
REVDAT   4   20-JUN-12 2CFV    1       JRNL   REMARK
REVDAT   3   13-JUL-11 2CFV    1       VERSN
REVDAT   2   03-FEB-09 2CFV    1       VERSN  SOURCE AUTHOR JRNL
REVDAT   2 2                           REMARK SITE
REVDAT   1   09-MAR-06 2CFV    0
JRNL        AUTH   A.J.BARR,E.UGOCHUKWU,W.H.LEE,O.N.F.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.    2.50 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) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 63.25
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 10857
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) : 0.203
REMARK   3   R VALUE            (WORKING SET) : 0.201
REMARK   3   FREE R VALUE                     : 0.250
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800
REMARK   3   FREE R VALUE TEST SET COUNT      : 547
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) : 2.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 788
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640
REMARK   3   BIN FREE R VALUE SET COUNT          : 38
REMARK   3   BIN FREE R VALUE                    : 0.3380
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2130
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 5
REMARK   3   SOLVENT ATOMS            : 25
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) : 29.51
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.23000
REMARK   3    B22 (A**2) : 1.23000
REMARK   3    B33 (A**2) : -1.85000
REMARK   3    B12 (A**2) : 0.62000
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): 0.513
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.285
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.221
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.803
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2193 ; 0.012 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  1418 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2979 ; 1.296 ; 1.926
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3440 ; 0.915 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   264 ; 6.914 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   107 ;37.141 ;23.832
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   342 ;16.956 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;18.465 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   333 ; 0.072 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2441 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   467 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   464 ; 0.229 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1358 ; 0.197 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1049 ; 0.190 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1101 ; 0.086 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    58 ; 0.155 ; 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):    30 ; 0.245 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    24 ; 0.170 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.163 ; 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):  1374 ; 0.485 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2159 ; 0.846 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   947 ; 1.148 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   820 ; 1.683 ; 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   -19        A  1301
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.0540  28.5200 -14.3810
REMARK   3    T TENSOR
REMARK   3      T11:   0.2010 T22:  -0.1333
REMARK   3      T33:  -0.0929 T12:  -0.1140
REMARK   3      T13:   0.0393 T23:   0.0230
REMARK   3    L TENSOR
REMARK   3      L11:   1.7566 L22:   3.2916
REMARK   3      L33:   3.5090 L12:  -0.4098
REMARK   3      L13:  -0.0498 L23:  -0.7789
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1634 S12:  -0.0701 S13:  -0.2750
REMARK   3      S21:   0.2248 S22:   0.1076 S23:   0.2215
REMARK   3      S31:   0.8140 S32:  -0.3864 S33:   0.0558
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
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 2CFV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-FEB-06.
REMARK 100 THE PDBE ID CODE IS EBI-27927.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 09-FEB-06
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : NULL
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                  : SI
REMARK 200  OPTICS                         : MIRROS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11491
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.600
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8
REMARK 200  DATA REDUNDANCY                : 3.760
REMARK 200  R MERGE                    (I) : 0.06000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 15.2500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.13
REMARK 200  R MERGE FOR SHELL          (I) : 0.27000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.180
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2AHS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 43.1
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M NICL2,0.1M TRIS PH 8.5,
REMARK 280  1M LI2SO4,150 UL SITTING DROPS
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       43.03000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.84338
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       39.84667
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       43.03000
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       24.84338
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       39.84667
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       43.03000
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       24.84338
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       39.84667
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.68676
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       79.69333
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       49.68676
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       79.69333
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       49.68676
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       79.69333
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -212.0 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      -43.03000
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000       74.53015
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -0.500000 -0.866025  0.000000       43.03000
REMARK 350   BIOMT2   3  0.866025 -0.500000  0.000000       74.53015
REMARK 350   BIOMT3   3  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   -22
REMARK 465     HIS A   -21
REMARK 465     HIS A   -20
REMARK 465     LYS A  1140
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  1156
REMARK 465     GLN A  1157
REMARK 465     PRO A  1175
REMARK 465     GLU A  1176
REMARK 465     THR A  1189
REMARK 465     SER A  1190
REMARK 465     SER A  1202
REMARK 465     ALA A  1203
REMARK 465     PRO A  1204
REMARK 465     ASP A  1205
REMARK 465     HIS A  1206
REMARK 465     GLY A  1207
REMARK 465     VAL A  1208
REMARK 465     PRO A  1209
REMARK 465     ASP A  1210
REMARK 465     MET A  1226
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     GLU A  1232
REMARK 465     SER A  1233
REMARK 465     SER A  1301
REMARK 465     GLN A  1302
REMARK 465     LYS A  1303
REMARK 465     ASP A  1304
REMARK 465     SER A  1305
REMARK 465     LYS A  1306
REMARK 465     VAL A  1307
REMARK 465     ASP A  1308
REMARK 465     LEU A  1309
REMARK 465     ILE A  1310
REMARK 465     TYR A  1311
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     ASN A  -6    CG   OD1  ND2
REMARK 470     PHE A  -3    CD1  CD2  CE1  CE2  CZ
REMARK 470     GLN A  -2    CG   CD   OE1  NE2
REMARK 470     LYS A1019    CE   NZ
REMARK 470     ARG A1022    NE   CZ   NH1  NH2
REMARK 470     GLU A1027    CG   CD   OE1  OE2
REMARK 470     LYS A1031    CG   CD   CE   NZ
REMARK 470     LYS A1032    CE   NZ
REMARK 470     GLN A1034    CD   OE1  NE2
REMARK 470     ASP A1036    CG   OD1  OD2
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    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU A1120    CG   CD1  CD2
REMARK 470     LYS A1121    CE   NZ
REMARK 470     TYR A1133    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LYS A1185    CG   CD   CE   NZ
REMARK 470     ILE A1187    CG1  CG2  CD1
REMARK 470     GLU A1191    CG   CD   OE1  OE2
REMARK 470     LEU A1214    CG   CD1  CD2
REMARK 470     ASP A1224    CG   OD1  OD2
REMARK 470     ILE A1298    CG1  CG2  CD1
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    MET A   0      142.24   -174.23
REMARK 500    SER A1037       74.94     54.30
REMARK 500    GLN A1087      -62.19   -154.15
REMARK 500    ASN A1096       84.02    -69.28
REMARK 500    CYS A1239     -118.67   -113.58
REMARK 500    VAL A1243      -57.89   -140.09
REMARK 500    VAL A1282       95.32     57.29
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 ASP A 1224     TYR A 1225                 -147.79
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 A2302  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A -18   NE2
REMARK 620 2 HIS A -18   NE2  89.5
REMARK 620 3 HIS A -18   NE2  96.0  83.4
REMARK 620 4 HIS A -16   NE2  97.8  84.6 161.5
REMARK 620 5 HIS A -16   NE2 168.9  79.5  84.0  80.0
REMARK 620 6 HIS A -16   NE2 106.3 164.1  96.0  91.8  84.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NI A2303  NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A -17   NE2
REMARK 620 2 LYS A1106   NZ  164.0
REMARK 620 3 HIS A1277   NE2  91.7  90.8
REMARK 620 4 HOH A2019   O    86.1  78.1  89.3
REMARK 620 5 HIS A -19   NE2  94.7  78.2 160.5  72.8
REMARK 620 6  CL A2304  CL    86.6 106.8 114.1 155.6  84.7
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NI A2302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NI A2303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A2304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NI A2305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NI A2306
DBREF  2CFV A  -22     0  PDB    2CFV     2CFV           -22      0
DBREF  2CFV A 1019  1311  UNP    Q12913   PTPRJ_HUMAN   1019   1311
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 ALA
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 CYS 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  A2302       1
HET     NI  A2303       1
HET     CL  A2304       1
HET     NI  A2305       1
HET     NI  A2306       1
HETNAM      NI NICKEL (II) ION
HETNAM      CL CHLORIDE ION
FORMUL   2   NI    4(NI 2+)
FORMUL   4   CL    CL 1-
FORMUL   7  HOH   *25(H2 O)
HELIX    1   1 ASP A  -11  GLN A   -2  1                                  10
HELIX    2   2 ASN A 1025  GLN A 1034  1                                  10
HELIX    3   3 ASN A 1038  LEU A 1048  1                                  11
HELIX    4   4 LYS A 1049  VAL A 1051  5                                   3
HELIX    5   5 LYS A 1057  LEU A 1062  1                                   6
HELIX    6   6 ALA A 1063  ASN A 1069  5                                   7
HELIX    7   7 TYR A 1077  SER A 1080  5                                   4
HELIX    8   8 HIS A 1089  TYR A 1094  5                                   6
HELIX    9   9 LEU A 1116  ASN A 1118  5                                   3
HELIX   10  10 THR A 1119  LYS A 1130  1                                  12
HELIX   11  11 THR A 1212  ARG A 1223  1                                  12
HELIX   12  12 VAL A 1243  GLU A 1262  1                                  20
HELIX   13  13 ASP A 1266  MET A 1276  1                                  11
HELIX   14  14 THR A 1284  VAL A 1299  1                                  16
SHEET    1  AA 2 ILE A1021  ARG A1022  0
SHEET    2  AA 2 THR A1264  VAL A1265 -1  O  VAL A1265   N  ILE A1021
SHEET    1  AB 8 ALA A1097  MET A1100  0
SHEET    2  AB 8 PHE A1109  THR A1112 -1  O  PHE A1109   N  MET A1100
SHEET    3  AB 8 ILE A1235  HIS A1238  1  O  ILE A1235   N  ILE A1110
SHEET    4  AB 8 ALA A1134  MET A1137  1  O  ALA A1134   N  LEU A1236
SHEET    5  AB 8 SER A1192  HIS A1199  1  O  ARG A1196   N  ILE A1135
SHEET    6  AB 8 THR A1178  ASN A1186 -1  O  THR A1178   N  HIS A1199
SHEET    7  AB 8 ILE A1164  VAL A1173 -1  O  THR A1165   N  LYS A1185
SHEET    8  AB 8 GLN A1159  TYR A1161 -1  O  GLN A1159   N  VAL A1166
LINK        NI    NI A2302                 NE2 HIS A -18     1555   1555  1.97
LINK        NI    NI A2302                 NE2 HIS A -18     1555   2665  2.47
LINK        NI    NI A2302                 NE2 HIS A -18     1555   3565  2.25
LINK        NI    NI A2302                 NE2 HIS A -16     1555   1555  2.19
LINK        NI    NI A2302                 NE2 HIS A -16     1555   2665  2.43
LINK        NI    NI A2302                 NE2 HIS A -16     1555   3565  1.96
LINK        NI    NI A2303                 NE2 HIS A -19     1555   2665  2.26
LINK        NI    NI A2303                 NZ  LYS A1106     1555   1555  1.83
LINK        NI    NI A2303                 NE2 HIS A1277     1555   1555  2.21
LINK        NI    NI A2303                 O   HOH A2019     1555   1555  1.96
LINK        NI    NI A2303                CL    CL A2304     1555   1555  2.36
LINK        NI    NI A2303                 NE2 HIS A -17     1555   2665  2.17
LINK        NI    NI A2305                 O   HOH A2005     1555   2665  2.54
LINK        NI    NI A2305                 O   HOH A2005     1555   3565  2.51
LINK        NI    NI A2305                 O   HOH A2005     1555   1555  2.60
LINK        NI    NI A2306                 O   HOH A2004     1555   1555  2.38
SITE     1 AC1  2 HIS A -16  HIS A -18
SITE     1 AC2  6 HIS A -17  HIS A -19  LYS A1106  HIS A1277
SITE     2 AC2  6 HOH A2019   CL A2304
SITE     1 AC3  4 HIS A -17  HIS A -19  LYS A1106   NI A2303
SITE     1 AC4  2 HOH A2002  HOH A2005
SITE     1 AC5  3 HIS A -19  HOH A2003  HOH A2004
CRYST1   86.060   86.060  119.540  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      0.011620  0.006709  0.000000        0.00000
SCALE2      0.000000  0.013417  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008365        0.00000
      
PROCHECK
Go to PROCHECK summary
 References