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Database: PDB
Entry: 2QEP
LinkDB: 2QEP
Original site: 2QEP 
HEADER    HYDROLASE                               26-JUN-07   2QEP              
TITLE     CRYSTAL STRUCTURE OF THE D1 DOMAIN OF PTPRN2 (IA2BETA)                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE N2;             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: D1 DOMAIN;                                                 
COMPND   5 SYNONYM: R-PTP-N2, ISLET CELL AUTOANTIGEN-RELATED PROTEIN, ICAAR,    
COMPND   6 IAR, PHOGRIN;                                                        
COMPND   7 EC: 3.1.3.48;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PTPRN2;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: PHAGE-RESISTANT DERIVATIVE OF BL21(DE3);   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC-CH                                   
KEYWDS    PTPRN2, PTPRP, PHOGRIN, IA-2 BETA, AUTOANTIGEN, STRUCTURAL GENOMICS,  
KEYWDS   2 STRUCTURAL GENOMICS CONSORTIUM, SGC, HYDROLASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.UGOCHUKWU,A.BARR,I.ALFANO,G.BERRIDGE,N.BURGESS-BROWN,S.DAS,         
AUTHOR   2 O.FEDOROV,O.KING,F.NIESEN,S.WATT,P.SAVITSKY,E.SALAH,A.C.W.PIKE,      
AUTHOR   3 G.BUNKOCZI,F.VON DELFT,M.SUNDSTROM,A.EDWARDS,C.H.ARROWSMITH,         
AUTHOR   4 J.WEIGELT,S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM (SGC)               
REVDAT   6   18-OCT-17 2QEP    1       REMARK                                   
REVDAT   5   13-JUL-11 2QEP    1       VERSN                                    
REVDAT   4   09-JUN-09 2QEP    1       REVDAT                                   
REVDAT   3   24-FEB-09 2QEP    1       VERSN                                    
REVDAT   2   03-FEB-09 2QEP    1       JRNL                                     
REVDAT   1   24-JUL-07 2QEP    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.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0037                                      
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) : 59.23                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 21905                          
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) : 0.239                           
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1187                            
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) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1605                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.24                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 100                          
REMARK   3   BIN FREE R VALUE                    : 0.3590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4413                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 39                                      
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) : 31.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.70000                                              
REMARK   3    B22 (A**2) : -2.97000                                             
REMARK   3    B33 (A**2) : 1.28000                                              
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): 0.629         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.329         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.266         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.532        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.916                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.874                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4522 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2869 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6175 ; 1.310 ; 1.929       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6984 ; 0.882 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   570 ; 6.512 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   205 ;33.720 ;23.951       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   663 ;15.183 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;12.526 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   695 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5131 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   936 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1018 ; 0.218 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2953 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2199 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2280 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   116 ; 0.150 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.016 ; 0.200       
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):    12 ; 0.264 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    33 ; 0.291 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.177 ; 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):  2937 ; 0.467 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1148 ; 0.090 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4594 ; 0.789 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1843 ; 1.069 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1581 ; 1.556 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 4                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    724       A     771      4                      
REMARK   3           1     B    724       B     771      4                      
REMARK   3           2     A    776       A     898      4                      
REMARK   3           2     B    776       B     898      4                      
REMARK   3           3     A    903       A     930      4                      
REMARK   3           3     B    903       B     930      4                      
REMARK   3           4     A    936       A     976      4                      
REMARK   3           4     B    936       B     976      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3422 ;  0.36 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   3422 ;  0.33 ;  2.00           
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   724        A   974                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.3406   5.0593   2.7838              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1115 T22:  -0.0444                                     
REMARK   3      T33:  -0.0955 T12:   0.0184                                     
REMARK   3      T13:  -0.0123 T23:  -0.0297                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9619 L22:   1.2678                                     
REMARK   3      L33:   1.1316 L12:   0.6301                                     
REMARK   3      L13:  -0.1756 L23:  -0.1881                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0282 S12:   0.1594 S13:  -0.0099                       
REMARK   3      S21:  -0.0283 S22:   0.0050 S23:   0.1193                       
REMARK   3      S31:   0.0830 S32:  -0.0961 S33:  -0.0332                       
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   724        B   974                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3999  37.6760  -2.8659              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0483 T22:  -0.0268                                     
REMARK   3      T33:  -0.1238 T12:   0.0327                                     
REMARK   3      T13:   0.0400 T23:   0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4172 L22:   3.0110                                     
REMARK   3      L33:   1.2949 L12:   0.9311                                     
REMARK   3      L13:   0.2706 L23:   0.1542                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0168 S12:  -0.0207 S13:  -0.0974                       
REMARK   3      S21:   0.1193 S22:  -0.0310 S23:  -0.0138                       
REMARK   3      S31:   0.1756 S32:  -0.0499 S33:   0.0143                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2QEP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000043504.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAY-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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) : 0.99990                            
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          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23096                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 59.230                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.13900                            
REMARK 200  R SYM                      (I) : 0.13900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
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) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.46500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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 2I1Y                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NA/KPO4, 0.1 M BIS-TRIS-PROPANE    
REMARK 280  PH 6.5, 20.0% PEG 3350, 10.0% ETHYLENE GLYCOL, VAPOR DIFFUSION,     
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       65.77050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       68.27750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       65.77050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       68.27750            
REMARK 290   SMTRY3   4  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 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     MET A   714                                                      
REMARK 465     SER A   715                                                      
REMARK 465     GLU A   716                                                      
REMARK 465     GLU A   717                                                      
REMARK 465     PRO A   718                                                      
REMARK 465     VAL A   719                                                      
REMARK 465     GLN A   720                                                      
REMARK 465     SER A   721                                                      
REMARK 465     ASN A   722                                                      
REMARK 465     MET A   723                                                      
REMARK 465     ALA A   969                                                      
REMARK 465     HIS A  1013                                                      
REMARK 465     HIS A  1014                                                      
REMARK 465     HIS A  1015                                                      
REMARK 465     HIS A  1016                                                      
REMARK 465     HIS A  1017                                                      
REMARK 465     MET B   714                                                      
REMARK 465     SER B   715                                                      
REMARK 465     GLU B   716                                                      
REMARK 465     GLU B   717                                                      
REMARK 465     PRO B   718                                                      
REMARK 465     VAL B   719                                                      
REMARK 465     GLN B   720                                                      
REMARK 465     SER B   721                                                      
REMARK 465     ASN B   722                                                      
REMARK 465     MET B   723                                                      
REMARK 465     HIS B   809                                                      
REMARK 465     ALA B   969                                                      
REMARK 465     HIS B  1013                                                      
REMARK 465     HIS B  1014                                                      
REMARK 465     HIS B  1015                                                      
REMARK 465     HIS B  1016                                                      
REMARK 465     HIS B  1017                                                      
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     ILE A 725    CD1                                                 
REMARK 470     LYS A 742    CG   CD   CE   NZ                                   
REMARK 470     ARG A 744    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 747    CG   CD   CE   NZ                                   
REMARK 470     GLU A 750    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 777    CG   CD1  CD2                                       
REMARK 470     LYS A 790    NZ                                                  
REMARK 470     GLU A 792    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 809    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 812    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 854    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP A 862    CG   OD1  OD2                                       
REMARK 470     GLU A 863    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 883    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 896    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 921    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 929    CD   CE   NZ                                        
REMARK 470     LYS A 932    CD   CE   NZ                                        
REMARK 470     ARG A 935    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 938    OG                                                  
REMARK 470     LYS A 964    CG   CD   CE   NZ                                   
REMARK 470     LYS A 970    CG   CD   CE   NZ                                   
REMARK 470     GLU A 971    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 972    CD1                                                 
REMARK 470     GLN A 990    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 992    NZ                                                  
REMARK 470     LEU A1010    CG   CD1  CD2                                       
REMARK 470     HIS A1012    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE B 725    CD1                                                 
REMARK 470     MET B 730    SD   CE                                             
REMARK 470     ILE B 731    CG1  CG2  CD1                                       
REMARK 470     LYS B 740    CG   CD   CE   NZ                                   
REMARK 470     ASN B 743    CG   OD1  ND2                                       
REMARK 470     LYS B 747    CG   CD   CE   NZ                                   
REMARK 470     GLU B 750    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 756    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 768    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 769    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 777    CG   CD1  CD2                                       
REMARK 470     LYS B 790    NZ                                                  
REMARK 470     GLU B 792    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 808    CG   OD1  OD2                                       
REMARK 470     ARG B 812    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 837    OG                                                  
REMARK 470     ARG B 854    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP B 862    CG   OD1  OD2                                       
REMARK 470     GLU B 863    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 883    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 914    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 921    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 928    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 932    CG   CD   CE   NZ                                   
REMARK 470     ARG B 935    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 938    OG                                                  
REMARK 470     LYS B 964    CG   CD   CE   NZ                                   
REMARK 470     LYS B 967    CG   CD   CE   NZ                                   
REMARK 470     LYS B 970    CG   CD   CE   NZ                                   
REMARK 470     GLU B 971    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 972    CD1                                                 
REMARK 470     GLN B 990    CG   CD   OE1  NE2                                  
REMARK 470     ILE B1009    CD1                                                 
REMARK 470     HIS B1012    CG   ND1  CD2  CE1  NE2                             
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    ASN A 760       16.94   -148.35                                   
REMARK 500    ASP A 808      -90.44   -113.31                                   
REMARK 500    ASN A 851       44.00     36.99                                   
REMARK 500    HIS A 869     -111.96     69.47                                   
REMARK 500    GLU A 878      116.74   -160.76                                   
REMARK 500    ASP A 913      129.75    -37.65                                   
REMARK 500    CYS A 945     -101.60   -140.15                                   
REMARK 500    SER A 946      -84.95   -116.91                                   
REMARK 500    ALA A 949      -56.26   -125.65                                   
REMARK 500    VAL A 989      103.83     68.63                                   
REMARK 500    ASN B 760       32.74   -141.61                                   
REMARK 500    THR B 781      135.24    -38.39                                   
REMARK 500    SER B 785       65.77   -157.06                                   
REMARK 500    ALA B 803      133.40   -170.73                                   
REMARK 500    ASN B 851       66.45     39.16                                   
REMARK 500    HIS B 869     -109.76     57.29                                   
REMARK 500    CYS B 882     -179.66   -171.38                                   
REMARK 500    ARG B 914       29.30     49.31                                   
REMARK 500    ARG B 937       64.25   -111.31                                   
REMARK 500    SER B 938      -71.58     58.06                                   
REMARK 500    CYS B 945     -102.90   -142.93                                   
REMARK 500    SER B 946      -77.86   -125.74                                   
REMARK 500    ALA B 949      -61.97   -129.94                                   
REMARK 500    ASP B 973       83.59   -153.02                                   
REMARK 500    VAL B 989      102.12     65.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2I1Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE PHOSPHATASE DOMAIN OF HUMAN PTP IA-2        
DBREF  2QEP A  715  1010  UNP    Q92932   PTPR2_HUMAN    715   1010             
DBREF  2QEP B  715  1010  UNP    Q92932   PTPR2_HUMAN    715   1010             
SEQADV 2QEP MET A  714  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP ALA A 1011  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP HIS A 1012  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP HIS A 1013  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP HIS A 1014  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP HIS A 1015  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP HIS A 1016  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP HIS A 1017  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP MET B  714  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP ALA B 1011  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP HIS B 1012  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP HIS B 1013  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP HIS B 1014  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP HIS B 1015  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP HIS B 1016  UNP  Q92932              CLONING ARTIFACT               
SEQADV 2QEP HIS B 1017  UNP  Q92932              CLONING ARTIFACT               
SEQRES   1 A  304  MET SER GLU GLU PRO VAL GLN SER ASN MET ASP ILE SER          
SEQRES   2 A  304  THR GLY HIS MET ILE LEU SER TYR MET GLU ASP HIS LEU          
SEQRES   3 A  304  LYS ASN LYS ASN ARG LEU GLU LYS GLU TRP GLU ALA LEU          
SEQRES   4 A  304  CYS ALA TYR GLN ALA GLU PRO ASN SER SER PHE VAL ALA          
SEQRES   5 A  304  GLN ARG GLU GLU ASN VAL PRO LYS ASN ARG SER LEU ALA          
SEQRES   6 A  304  VAL LEU THR TYR ASP HIS SER ARG VAL LEU LEU LYS ALA          
SEQRES   7 A  304  GLU ASN SER HIS SER HIS SER ASP TYR ILE ASN ALA SER          
SEQRES   8 A  304  PRO ILE MET ASP HIS ASP PRO ARG ASN PRO ALA TYR ILE          
SEQRES   9 A  304  ALA THR GLN GLY PRO LEU PRO ALA THR VAL ALA ASP PHE          
SEQRES  10 A  304  TRP GLN MET VAL TRP GLU SER GLY CYS VAL VAL ILE VAL          
SEQRES  11 A  304  MET LEU THR PRO LEU ALA GLU ASN GLY VAL ARG GLN CYS          
SEQRES  12 A  304  TYR HIS TYR TRP PRO ASP GLU GLY SER ASN LEU TYR HIS          
SEQRES  13 A  304  ILE TYR GLU VAL ASN LEU VAL SER GLU HIS ILE TRP CYS          
SEQRES  14 A  304  GLU ASP PHE LEU VAL ARG SER PHE TYR LEU LYS ASN LEU          
SEQRES  15 A  304  GLN THR ASN GLU THR ARG THR VAL THR GLN PHE HIS PHE          
SEQRES  16 A  304  LEU SER TRP TYR ASP ARG GLY VAL PRO SER SER SER ARG          
SEQRES  17 A  304  SER LEU LEU ASP PHE ARG ARG LYS VAL ASN LYS CYS TYR          
SEQRES  18 A  304  ARG GLY ARG SER CYS PRO ILE ILE VAL HIS CYS SER ASP          
SEQRES  19 A  304  GLY ALA GLY ARG SER GLY THR TYR VAL LEU ILE ASP MET          
SEQRES  20 A  304  VAL LEU ASN LYS MET ALA LYS GLY ALA LYS GLU ILE ASP          
SEQRES  21 A  304  ILE ALA ALA THR LEU GLU HIS LEU ARG ASP GLN ARG PRO          
SEQRES  22 A  304  GLY MET VAL GLN THR LYS GLU GLN PHE GLU PHE ALA LEU          
SEQRES  23 A  304  THR ALA VAL ALA GLU GLU VAL ASN ALA ILE LEU ALA HIS          
SEQRES  24 A  304  HIS HIS HIS HIS HIS                                          
SEQRES   1 B  304  MET SER GLU GLU PRO VAL GLN SER ASN MET ASP ILE SER          
SEQRES   2 B  304  THR GLY HIS MET ILE LEU SER TYR MET GLU ASP HIS LEU          
SEQRES   3 B  304  LYS ASN LYS ASN ARG LEU GLU LYS GLU TRP GLU ALA LEU          
SEQRES   4 B  304  CYS ALA TYR GLN ALA GLU PRO ASN SER SER PHE VAL ALA          
SEQRES   5 B  304  GLN ARG GLU GLU ASN VAL PRO LYS ASN ARG SER LEU ALA          
SEQRES   6 B  304  VAL LEU THR TYR ASP HIS SER ARG VAL LEU LEU LYS ALA          
SEQRES   7 B  304  GLU ASN SER HIS SER HIS SER ASP TYR ILE ASN ALA SER          
SEQRES   8 B  304  PRO ILE MET ASP HIS ASP PRO ARG ASN PRO ALA TYR ILE          
SEQRES   9 B  304  ALA THR GLN GLY PRO LEU PRO ALA THR VAL ALA ASP PHE          
SEQRES  10 B  304  TRP GLN MET VAL TRP GLU SER GLY CYS VAL VAL ILE VAL          
SEQRES  11 B  304  MET LEU THR PRO LEU ALA GLU ASN GLY VAL ARG GLN CYS          
SEQRES  12 B  304  TYR HIS TYR TRP PRO ASP GLU GLY SER ASN LEU TYR HIS          
SEQRES  13 B  304  ILE TYR GLU VAL ASN LEU VAL SER GLU HIS ILE TRP CYS          
SEQRES  14 B  304  GLU ASP PHE LEU VAL ARG SER PHE TYR LEU LYS ASN LEU          
SEQRES  15 B  304  GLN THR ASN GLU THR ARG THR VAL THR GLN PHE HIS PHE          
SEQRES  16 B  304  LEU SER TRP TYR ASP ARG GLY VAL PRO SER SER SER ARG          
SEQRES  17 B  304  SER LEU LEU ASP PHE ARG ARG LYS VAL ASN LYS CYS TYR          
SEQRES  18 B  304  ARG GLY ARG SER CYS PRO ILE ILE VAL HIS CYS SER ASP          
SEQRES  19 B  304  GLY ALA GLY ARG SER GLY THR TYR VAL LEU ILE ASP MET          
SEQRES  20 B  304  VAL LEU ASN LYS MET ALA LYS GLY ALA LYS GLU ILE ASP          
SEQRES  21 B  304  ILE ALA ALA THR LEU GLU HIS LEU ARG ASP GLN ARG PRO          
SEQRES  22 B  304  GLY MET VAL GLN THR LYS GLU GLN PHE GLU PHE ALA LEU          
SEQRES  23 B  304  THR ALA VAL ALA GLU GLU VAL ASN ALA ILE LEU ALA HIS          
SEQRES  24 B  304  HIS HIS HIS HIS HIS                                          
HET     CL  A   1       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  HOH   *39(H2 O)                                                     
HELIX    1   1 ASP A  724  LEU A  739  1                                  16    
HELIX    2   2 ASN A  741  TYR A  755  1                                  15    
HELIX    3   3 ASN A  770  ASN A  774  5                                   5    
HELIX    4   4 TYR A  782  ARG A  786  5                                   5    
HELIX    5   5 LEU A  823  ALA A  825  5                                   3    
HELIX    6   6 THR A  826  SER A  837  1                                  12    
HELIX    7   7 SER A  919  ARG A  935  1                                  17    
HELIX    8   8 ALA A  949  LYS A  967  1                                  19    
HELIX    9   9 ASP A  973  ASP A  983  1                                  11    
HELIX   10  10 THR A  991  HIS A 1012  1                                  22    
HELIX   11  11 ASP B  724  LEU B  739  1                                  16    
HELIX   12  12 ASN B  741  TYR B  755  1                                  15    
HELIX   13  13 ARG B  767  ASN B  774  5                                   8    
HELIX   14  14 LYS B  790  SER B  794  5                                   5    
HELIX   15  15 LEU B  823  ALA B  825  5                                   3    
HELIX   16  16 THR B  826  GLY B  838  1                                  13    
HELIX   17  17 SER B  919  ARG B  935  1                                  17    
HELIX   18  18 ALA B  949  LYS B  964  1                                  16    
HELIX   19  19 ASP B  973  ARG B  985  1                                  13    
HELIX   20  20 THR B  991  HIS B 1012  1                                  22    
SHEET    1   A 8 ALA A 803  ILE A 806  0                                        
SHEET    2   A 8 TYR A 816  THR A 819 -1  O  TYR A 816   N  ILE A 806           
SHEET    3   A 8 ILE A 941  HIS A 944  1  O  ILE A 941   N  ILE A 817           
SHEET    4   A 8 VAL A 841  MET A 844  1  N  VAL A 843   O  ILE A 942           
SHEET    5   A 8 GLU A 899  PHE A 908  1  O  PHE A 906   N  MET A 844           
SHEET    6   A 8 PHE A 885  ASN A 894 -1  N  ARG A 888   O  GLN A 905           
SHEET    7   A 8 TYR A 871  CYS A 882 -1  N  HIS A 879   O  VAL A 887           
SHEET    8   A 8 SER A 865  TYR A 868 -1  N  ASN A 866   O  VAL A 873           
SHEET    1   B 2 ALA A 849  GLU A 850  0                                        
SHEET    2   B 2 VAL A 853  ARG A 854 -1  O  VAL A 853   N  GLU A 850           
SHEET    1   C 8 ALA B 803  ILE B 806  0                                        
SHEET    2   C 8 TYR B 816  THR B 819 -1  O  ALA B 818   N  SER B 804           
SHEET    3   C 8 ILE B 941  HIS B 944  1  O  ILE B 941   N  ILE B 817           
SHEET    4   C 8 VAL B 841  MET B 844  1  N  VAL B 843   O  HIS B 944           
SHEET    5   C 8 THR B 900  PHE B 908  1  O  PHE B 906   N  ILE B 842           
SHEET    6   C 8 PHE B 885  ASN B 894 -1  N  LEU B 886   O  HIS B 907           
SHEET    7   C 8 TYR B 871  CYS B 882 -1  N  GLU B 872   O  LYS B 893           
SHEET    8   C 8 SER B 865  TYR B 868 -1  N  TYR B 868   O  TYR B 871           
SHEET    1   D 2 ALA B 849  GLU B 850  0                                        
SHEET    2   D 2 VAL B 853  ARG B 854 -1  O  VAL B 853   N  GLU B 850           
CISPEP   1 GLU A  758    PRO A  759          0         6.63                     
CISPEP   2 ARG A  935    GLY A  936          0       -11.60                     
CISPEP   3 GLU B  758    PRO B  759          0        -2.07                     
CRYST1  131.541  136.555   35.752  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007602  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007323  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027971        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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