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Database: PDB
Entry: 2QT7
LinkDB: 2QT7
Original site: 2QT7 
HEADER    HYDROLASE                               01-AUG-07   2QT7              
TITLE     CRYSTALLOGRAPHIC STRUCTURE OF THE MATURE ECTODOMAIN OF THE HUMAN      
TITLE    2 RECEPTOR-TYPE PROTEIN-TYROSINE PHOSPHATASE IA-2 AT 1.30 ANGSTROMS    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE-LIKE N;         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SEQUENCE DATABASE RESIDUES 468-558;                        
COMPND   5 SYNONYM: R-PTP-N, PTP IA-2, ISLET CELL ANTIGEN 512, ICA 512, ISLET   
COMPND   6 CELL AUTOANTIGEN 3;                                                  
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: PTPRN, ICA3, ICA512;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET9B                                     
KEYWDS    IA-2, ICA-512, PROTEIN-TYROSINE PHOSPHATASE, TRANSMEMBRANE PROTEIN,   
KEYWDS   2 DIABETES, AUTOIMMUNITY, PROTEOLYSIS, GLYCOPROTEIN, RECEPTOR,         
KEYWDS   3 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.E.PRIMO,S.KLINKE,M.P.SICA,F.A.GOLDBAUM,J.JAKONCIC,E.POSKUS,         
AUTHOR   2 M.R.ERMACORA                                                         
REVDAT   4   25-OCT-17 2QT7    1       REMARK                                   
REVDAT   3   24-FEB-09 2QT7    1       VERSN                                    
REVDAT   2   04-MAR-08 2QT7    1       JRNL                                     
REVDAT   1   11-DEC-07 2QT7    0                                                
JRNL        AUTH   M.E.PRIMO,S.KLINKE,M.P.SICA,F.A.GOLDBAUM,J.JAKONCIC,         
JRNL        AUTH 2 E.POSKUS,M.R.ERMACORA                                        
JRNL        TITL   STRUCTURE OF THE MATURE ECTODOMAIN OF THE HUMAN              
JRNL        TITL 2 RECEPTOR-TYPE PROTEIN-TYROSINE PHOSPHATASE IA-2              
JRNL        REF    J.BIOL.CHEM.                  V. 283  4674 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18048354                                                     
JRNL        DOI    10.1074/JBC.M708144200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 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) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 36265                          
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) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1922                            
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) : 1.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.33                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2238                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.99                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2670                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 129                          
REMARK   3   BIN FREE R VALUE                    : 0.3450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1326                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 176                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.74000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.74000                                             
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): 0.067         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.067         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.041         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.937         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1408 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1927 ; 1.161 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   195 ; 5.370 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    57 ;39.001 ;25.789       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   240 ;11.001 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     5 ;20.521 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   239 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1047 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   679 ; 0.214 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1045 ; 0.301 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   118 ; 0.131 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     6 ; 0.099 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    56 ; 0.159 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    28 ; 0.145 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):     2 ; 0.040 ; 0.200       
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):   937 ; 0.884 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1479 ; 1.479 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   508 ; 2.001 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   441 ; 3.001 ; 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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2QT7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044024.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-NOV-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               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793, 1.5895                     
REMARK 200  MONOCHROMATOR                  : SI (111) CHANNEL CUT               
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : TOROIDAL FOCUSING MIRROR           
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38269                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 7.600                              
REMARK 200  R MERGE                    (I) : 0.03000                            
REMARK 200  R SYM                      (I) : 0.03000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 43.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.21300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXDE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (W/V) PEG 4000, 0.1 M TRIS PH 8.5,   
REMARK 280  0.2 M CACL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       15.87800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.56550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.39950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.56550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       15.87800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.39950            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1330 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350   BIOMT1   2 -1.000000  0.000000  0.000000       15.87800            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000       36.56550            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     ALA A    20                                                      
REMARK 465     GLU A   110                                                      
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     GLU A  21    CG   CD   OE1  OE2                                  
REMARK 470     HIS A  72    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 108    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  21    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  31    CG   CD   CE   NZ                                   
REMARK 470     GLU B  74    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  75    CG   CD   OE1  NE2                                  
REMARK 470     ASN B  76    CG   OD1  ND2                                       
REMARK 470     ARG B 109    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 110    CG   CD   OE1  OE2                                  
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                              CA A 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  76   O                                                      
REMARK 620 2 ASP A  81   OD2  90.0                                              
REMARK 620 3 HOH A 369   O   149.5  85.2                                        
REMARK 620 4 HOH A 329   O   136.7  85.2  72.9                                  
REMARK 620 5 HOH A 359   O    70.2  96.9  80.5 153.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  94   OE1                                                    
REMARK 620 2 GLU A  94   OE2  55.0                                              
REMARK 620 3 GLN A 100   OE1  99.3  90.4                                        
REMARK 620 4 HOH A 390   O    78.1  95.9 169.8                                  
REMARK 620 5 HOH A 424   O   142.5 157.1  98.2  78.9                            
REMARK 620 6 HOH A 425   O   124.2  73.5 101.2  88.3  84.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  94   OE1                                                    
REMARK 620 2 GLU B  94   OE2  51.9                                              
REMARK 620 3 GLN B 100   OE1  89.8  84.1                                        
REMARK 620 4 HOH B 304   O   129.7  78.1  90.9                                  
REMARK 620 5 HOH B 440   O    87.8  94.8 177.6  91.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 201                  
DBREF  2QT7 A   20   110  UNP    Q16849   PTPRN_HUMAN    468    558             
DBREF  2QT7 B   20   110  UNP    Q16849   PTPRN_HUMAN    468    558             
SEQRES   1 A   91  ALA GLU GLU TYR GLY TYR ILE VAL THR ASP GLN LYS PRO          
SEQRES   2 A   91  LEU SER LEU ALA ALA GLY VAL LYS LEU LEU GLU ILE LEU          
SEQRES   3 A   91  ALA GLU HIS VAL HIS MET SER SER GLY SER PHE ILE ASN          
SEQRES   4 A   91  ILE SER VAL VAL GLY PRO ALA LEU THR PHE ARG ILE ARG          
SEQRES   5 A   91  HIS ASN GLU GLN ASN LEU SER LEU ALA ASP VAL THR GLN          
SEQRES   6 A   91  GLN ALA GLY LEU VAL LYS SER GLU LEU GLU ALA GLN THR          
SEQRES   7 A   91  GLY LEU GLN ILE LEU GLN THR GLY VAL GLY GLN ARG GLU          
SEQRES   1 B   91  ALA GLU GLU TYR GLY TYR ILE VAL THR ASP GLN LYS PRO          
SEQRES   2 B   91  LEU SER LEU ALA ALA GLY VAL LYS LEU LEU GLU ILE LEU          
SEQRES   3 B   91  ALA GLU HIS VAL HIS MET SER SER GLY SER PHE ILE ASN          
SEQRES   4 B   91  ILE SER VAL VAL GLY PRO ALA LEU THR PHE ARG ILE ARG          
SEQRES   5 B   91  HIS ASN GLU GLN ASN LEU SER LEU ALA ASP VAL THR GLN          
SEQRES   6 B   91  GLN ALA GLY LEU VAL LYS SER GLU LEU GLU ALA GLN THR          
SEQRES   7 B   91  GLY LEU GLN ILE LEU GLN THR GLY VAL GLY GLN ARG GLU          
HET     CA  A 202       1                                                       
HET     CA  A 203       1                                                       
HET     CA  B 201       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    3(CA 2+)                                                     
FORMUL   6  HOH   *176(H2 O)                                                    
HELIX    1   1 LEU A   35  VAL A   49  1                                  15    
HELIX    2   2 LEU A   79  LEU A   88  1                                  10    
HELIX    3   3 LYS A   90  THR A   97  1                                   8    
HELIX    4   4 LEU B   35  VAL B   49  1                                  15    
HELIX    5   5 LEU B   79  LEU B   88  1                                  10    
HELIX    6   6 LYS B   90  THR B   97  1                                   8    
SHEET    1   A 8 PHE A  56  VAL A  62  0                                        
SHEET    2   A 8 ALA A  65  ILE A  70 -1  O  ARG A  69   N  ILE A  57           
SHEET    3   A 8 TYR A  23  THR A  28 -1  N  GLY A  24   O  PHE A  68           
SHEET    4   A 8 ILE A 101  GLY A 107 -1  O  LEU A 102   N  VAL A  27           
SHEET    5   A 8 ILE B 101  GLY B 107 -1  O  THR B 104   N  VAL A 106           
SHEET    6   A 8 TYR B  23  THR B  28 -1  N  VAL B  27   O  GLN B 103           
SHEET    7   A 8 ALA B  65  ILE B  70 -1  O  PHE B  68   N  GLY B  24           
SHEET    8   A 8 PHE B  56  VAL B  62 -1  N  ILE B  57   O  ARG B  69           
LINK         O   ASN A  76                CA    CA A 202     1555   1555  2.54  
LINK         OD2 ASP A  81                CA    CA A 202     1555   1555  2.26  
LINK         OE1 GLU A  94                CA    CA A 203     1555   1555  2.34  
LINK         OE2 GLU A  94                CA    CA A 203     1555   1555  2.40  
LINK         OE1 GLN A 100                CA    CA A 203     1555   1555  2.32  
LINK         OE1 GLU B  94                CA    CA B 201     1555   1555  2.50  
LINK         OE2 GLU B  94                CA    CA B 201     1555   1555  2.52  
LINK         OE1 GLN B 100                CA    CA B 201     1555   1555  2.36  
LINK        CA    CA B 201                 O   HOH B 304     1555   1555  2.43  
LINK        CA    CA B 201                 O   HOH B 440     1555   1555  2.43  
LINK        CA    CA A 202                 O   HOH A 369     1555   1555  2.44  
LINK        CA    CA A 202                 O   HOH A 329     1555   1555  2.51  
LINK        CA    CA A 202                 O   HOH A 359     1555   1555  2.46  
LINK        CA    CA A 203                 O   HOH A 390     1555   1555  2.51  
LINK        CA    CA A 203                 O   HOH A 424     1555   1555  2.52  
LINK        CA    CA A 203                 O   HOH A 425     1555   1555  2.31  
CISPEP   1 LYS A   31    PRO A   32          0        -6.56                     
CISPEP   2 LYS B   31    PRO B   32          0        -4.44                     
SITE     1 AC1  7 ASN A  76  ASP A  81  GLY A  98  HOH A 329                    
SITE     2 AC1  7 HOH A 336  HOH A 359  HOH A 369                               
SITE     1 AC2  5 GLU A  94  GLN A 100  HOH A 390  HOH A 424                    
SITE     2 AC2  5 HOH A 425                                                     
SITE     1 AC3  6 HIS A  50  HOH A 307  GLU B  94  GLN B 100                    
SITE     2 AC3  6 HOH B 304  HOH B 440                                          
CRYST1   31.756   66.799   73.131  90.00  90.00  90.00 P 21 21 21    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      0.031490  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014970  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013674        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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