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Database: PDB
Entry: 5E5R
LinkDB: 5E5R
Original site: 5E5R 
HEADER    HYDROLASE/CELL ADHESION                 09-OCT-15   5E5R              
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBONIC ANHYDRASE-LIKE      
TITLE    2 DOMAIN OF PTPRG AND IMMUNOGLOBULIN DOMAINS 2-3 OF CNTN3              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE GAMMA;          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: CA DOMAIN, UNP RESIDUES 56-320;                            
COMPND   5 SYNONYM: R-PTP-GAMMA;                                                
COMPND   6 EC: 3.1.3.48;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CONTACTIN-3;                                               
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: IMMUNOGLOBULIN DOMAINS 2-3, UNP RESIDUES 124-316;          
COMPND  12 SYNONYM: BRAIN-DERIVED IMMUNOGLOBULIN SUPERFAMILY PROTEIN 1,BIG-1,   
COMPND  13 PLASMACYTOMA-ASSOCIATED NEURONAL GLYCOPROTEIN;                       
COMPND  14 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: PTPRG, PTPG;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI2(DE3);                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET32HP;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: MOUSE;                                              
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 GENE: CNTN3, PANG, PCS;                                              
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: T7 SHUFFLE EXPRESS;                        
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PT7HMP                                    
KEYWDS    NEURAL CELL ADHESION MOLECULE, RECEPTOR-TYPE PROTEIN TYROSINE         
KEYWDS   2 PHOSPHATASE, IMMUNOGLOBULIN DOMAINS, CARBONIC ANHYDRASE-LIKE DOMAIN, 
KEYWDS   3 HYDROLASE-CELL ADHESION COMPLEX                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.M.NIKOLAIENKO,S.BOUYAIN                                             
REVDAT   3   27-SEP-17 5E5R    1       JRNL                                     
REVDAT   2   23-NOV-16 5E5R    1       JRNL                                     
REVDAT   1   31-AUG-16 5E5R    0                                                
JRNL        AUTH   R.M.NIKOLAIENKO,M.HAMMEL,V.DUBREUIL,R.ZALMAI,D.R.HALL,       
JRNL        AUTH 2 N.MEHZABEEN,S.J.KARUPPAN,S.HARROCH,S.L.STELLA,S.BOUYAIN      
JRNL        TITL   STRUCTURAL BASIS FOR INTERACTIONS BETWEEN CONTACTIN FAMILY   
JRNL        TITL 2 MEMBERS AND PROTEIN-TYROSINE PHOSPHATASE RECEPTOR TYPE G IN  
JRNL        TITL 3 NEURAL TISSUES.                                              
JRNL        REF    J.BIOL.CHEM.                  V. 291 21335 2016              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   27539848                                                     
JRNL        DOI    10.1074/JBC.M116.742163                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.15                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 31039                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1553                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.1581 -  5.7792    0.99     2871   152  0.1587 0.1968        
REMARK   3     2  5.7792 -  4.5882    1.00     2731   144  0.1445 0.1683        
REMARK   3     3  4.5882 -  4.0085    0.99     2702   141  0.1529 0.2329        
REMARK   3     4  4.0085 -  3.6422    0.99     2688   142  0.1932 0.2821        
REMARK   3     5  3.6422 -  3.3812    1.00     2673   140  0.2037 0.2656        
REMARK   3     6  3.3812 -  3.1819    1.00     2686   142  0.2300 0.3300        
REMARK   3     7  3.1819 -  3.0225    1.00     2662   139  0.2375 0.3152        
REMARK   3     8  3.0225 -  2.8910    1.00     2655   141  0.2432 0.3049        
REMARK   3     9  2.8910 -  2.7797    1.00     2656   140  0.2520 0.3394        
REMARK   3    10  2.7797 -  2.6838    0.99     2633   139  0.2477 0.3738        
REMARK   3    11  2.6838 -  2.6000    0.95     2529   133  0.2666 0.3391        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.060           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 56.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           7425                                  
REMARK   3   ANGLE     :  1.101          10054                                  
REMARK   3   CHIRALITY :  0.043           1054                                  
REMARK   3   PLANARITY :  0.005           1325                                  
REMARK   3   DIHEDRAL  : 14.013           2730                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND ((RESSEQ 56:320))                        
REMARK   3    ORIGIN FOR THE GROUP (A): -50.8968 -30.1627  26.6603              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5856 T22:   0.6535                                     
REMARK   3      T33:   0.3219 T12:  -0.1063                                     
REMARK   3      T13:   0.1227 T23:  -0.1415                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6285 L22:   8.6906                                     
REMARK   3      L33:   5.7250 L12:   1.6527                                     
REMARK   3      L13:   0.7752 L23:  -1.3528                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5948 S12:  -1.0018 S13:   0.5469                       
REMARK   3      S21:   1.2093 S22:  -0.6945 S23:   0.4008                       
REMARK   3      S31:  -0.7238 S32:  -0.0995 S33:   0.1015                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND ((RESSEQ 125:221))                       
REMARK   3    ORIGIN FOR THE GROUP (A): -59.1349 -62.0775   8.0005              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7823 T22:   0.4516                                     
REMARK   3      T33:   0.4836 T12:  -0.1177                                     
REMARK   3      T13:   0.1296 T23:   0.0555                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0585 L22:   8.4455                                     
REMARK   3      L33:   8.5221 L12:  -1.8588                                     
REMARK   3      L13:  -2.0720 L23:  -0.4639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6550 S12:  -0.3695 S13:  -1.3076                       
REMARK   3      S21:   0.5627 S22:   0.0813 S23:   0.3603                       
REMARK   3      S31:   1.6062 S32:  -0.0560 S33:   0.5597                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND ((RESSEQ 222:316))                       
REMARK   3    ORIGIN FOR THE GROUP (A): -53.3906 -46.0216  -7.1526              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6385 T22:   0.4954                                     
REMARK   3      T33:   0.3857 T12:  -0.2102                                     
REMARK   3      T13:  -0.1806 T23:   0.0595                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6105 L22:   2.8320                                     
REMARK   3      L33:   8.9292 L12:   0.1366                                     
REMARK   3      L13:  -4.6610 L23:   1.7228                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5929 S12:   1.1433 S13:   0.2597                       
REMARK   3      S21:  -0.6984 S22:   0.2089 S23:   0.1894                       
REMARK   3      S31:  -0.1797 S32:  -0.6112 S33:   0.4157                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'C' AND ((RESSEQ 57:320))                        
REMARK   3    ORIGIN FOR THE GROUP (A): -15.1068 -20.7316  45.2127              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3818 T22:   0.4762                                     
REMARK   3      T33:   0.2915 T12:  -0.1012                                     
REMARK   3      T13:   0.0477 T23:  -0.0466                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5280 L22:   6.1894                                     
REMARK   3      L33:   4.9602 L12:   2.3702                                     
REMARK   3      L13:  -1.9941 L23:  -0.4220                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4434 S12:   0.9460 S13:  -0.0926                       
REMARK   3      S21:  -0.7902 S22:   0.4963 S23:  -0.6132                       
REMARK   3      S31:   0.0381 S32:   0.0242 S33:  -0.0618                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'D' AND ((RESSEQ 124:221))                       
REMARK   3    ORIGIN FOR THE GROUP (A): -25.9765  -7.5001  79.5404              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5033 T22:   0.2381                                     
REMARK   3      T33:   0.3290 T12:  -0.0097                                     
REMARK   3      T13:   0.0958 T23:  -0.0447                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1294 L22:   6.9970                                     
REMARK   3      L33:   8.2253 L12:   0.5034                                     
REMARK   3      L13:   3.5043 L23:   0.6640                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2538 S12:  -0.1499 S13:   0.5514                       
REMARK   3      S21:   0.4235 S22:  -0.0788 S23:  -0.1909                       
REMARK   3      S31:  -1.0936 S32:   0.0514 S33:   0.3293                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'D' AND ((RESSEQ 222:316))                       
REMARK   3    ORIGIN FOR THE GROUP (A): -21.6258 -29.8919  81.0980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4422 T22:   0.2954                                     
REMARK   3      T33:   0.3969 T12:  -0.0845                                     
REMARK   3      T13:   0.1638 T23:  -0.1155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8729 L22:   7.5844                                     
REMARK   3      L33:   8.7254 L12:  -4.9212                                     
REMARK   3      L13:   5.5912 L23:  -7.1076                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0259 S12:  -0.1330 S13:   0.0500                       
REMARK   3      S21:  -0.0420 S22:  -0.0639 S23:  -0.2441                       
REMARK   3      S31:   0.2498 S32:  -0.0085 S33:   0.0625                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5E5R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214401.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-11                          
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               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE-CRYSTAL      
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31166                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 11.40                              
REMARK 200  R MERGE                    (I) : 0.13400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3JXH, 5E4I                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1% (V/V) TACSIMATE PH 7.0, 20% (W/V)     
REMARK 280  PEG 3350, 50MM IMIDAZOLE-HCL PH 6.5, VAPOR DIFFUSION, HANGING       
REMARK 280  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       37.06900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.26300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.06900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.26300            
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: 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     VAL A    95                                                      
REMARK 465     GLY A    96                                                      
REMARK 465     GLU A    97                                                      
REMARK 465     GLU A    98                                                      
REMARK 465     TYR A    99                                                      
REMARK 465     GLN A   100                                                      
REMARK 465     ILE A   165                                                      
REMARK 465     PHE B   124                                                      
REMARK 465     PRO B   148                                                      
REMARK 465     HIS B   149                                                      
REMARK 465     SER B   150                                                      
REMARK 465     GLY B   151                                                      
REMARK 465     SER B   164                                                      
REMARK 465     GLY C    56                                                      
REMARK 465     HIS D   149                                                      
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 156    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH2  ARG C   169     O    HOH C   501              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OH   TYR A   278     OE1  GLN C   100     1455     2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 228      -12.88     94.06                                   
REMARK 500    ASP A 294     -131.51     52.76                                   
REMARK 500    HIS A 295       40.23   -104.98                                   
REMARK 500    ASN A 305       58.74    -93.29                                   
REMARK 500    HIS A 313     -127.34     54.10                                   
REMARK 500    ASN B 160      -52.69     66.21                                   
REMARK 500    ASP B 169     -161.58   -165.38                                   
REMARK 500    THR B 203     -158.58   -143.61                                   
REMARK 500    GLU B 226      151.64    -44.34                                   
REMARK 500    ALA C  93     -156.77    -79.17                                   
REMARK 500    GLU C  98       28.83     46.73                                   
REMARK 500    HIS C 154      -57.30   -126.79                                   
REMARK 500    PRO C 181     -168.87    -68.90                                   
REMARK 500    ASP C 182      -18.33     66.74                                   
REMARK 500    HIS C 227      129.31    -34.20                                   
REMARK 500    GLU C 228       -2.80     77.77                                   
REMARK 500    ILE C 264       15.32   -144.09                                   
REMARK 500    ASP C 294       73.58     46.24                                   
REMARK 500    HIS C 313     -123.47     52.46                                   
REMARK 500    CYS D 144      -68.58    -92.13                                   
REMARK 500    ASN D 160     -119.36     58.14                                   
REMARK 500    PRO D 163       48.75   -102.63                                   
REMARK 500    ASP D 169     -153.27   -151.15                                   
REMARK 500    VAL D 202      -75.23    -78.41                                   
REMARK 500    CYS D 249      114.73   -162.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT C 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI D 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5E4Q   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E4I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E4S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E52   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E53   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E55   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E5U   RELATED DB: PDB                                   
DBREF  5E5R A   56   320  UNP    P23470   PTPRG_HUMAN     56    320             
DBREF  5E5R B  124   316  UNP    Q07409   CNTN3_MOUSE    124    316             
DBREF  5E5R C   56   320  UNP    P23470   PTPRG_HUMAN     56    320             
DBREF  5E5R D  124   316  UNP    Q07409   CNTN3_MOUSE    124    316             
SEQRES   1 A  265  GLY ASP PRO TYR TRP ALA TYR SER GLY ALA TYR GLY PRO          
SEQRES   2 A  265  GLU HIS TRP VAL THR SER SER VAL SER CYS GLY GLY ARG          
SEQRES   3 A  265  HIS GLN SER PRO ILE ASP ILE LEU ASP GLN TYR ALA ARG          
SEQRES   4 A  265  VAL GLY GLU GLU TYR GLN GLU LEU GLN LEU ASP GLY PHE          
SEQRES   5 A  265  ASP ASN GLU SER SER ASN LYS THR TRP MET LYS ASN THR          
SEQRES   6 A  265  GLY LYS THR VAL ALA ILE LEU LEU LYS ASP ASP TYR PHE          
SEQRES   7 A  265  VAL SER GLY ALA GLY LEU PRO GLY ARG PHE LYS ALA GLU          
SEQRES   8 A  265  LYS VAL GLU PHE HIS TRP GLY HIS SER ASN GLY SER ALA          
SEQRES   9 A  265  GLY SER GLU HIS SER ILE ASN GLY ARG ARG PHE PRO VAL          
SEQRES  10 A  265  GLU MET GLN ILE PHE PHE TYR ASN PRO ASP ASP PHE ASP          
SEQRES  11 A  265  SER PHE GLN THR ALA ILE SER GLU ASN ARG ILE ILE GLY          
SEQRES  12 A  265  ALA MET ALA ILE PHE PHE GLN VAL SER PRO ARG ASP ASN          
SEQRES  13 A  265  SER ALA LEU ASP PRO ILE ILE HIS GLY LEU LYS GLY VAL          
SEQRES  14 A  265  VAL HIS HIS GLU LYS GLU THR PHE LEU ASP PRO PHE VAL          
SEQRES  15 A  265  LEU ARG ASP LEU LEU PRO ALA SER LEU GLY SER TYR TYR          
SEQRES  16 A  265  ARG TYR THR GLY SER LEU THR THR PRO PRO CYS SER GLU          
SEQRES  17 A  265  ILE VAL GLU TRP ILE VAL PHE ARG ARG PRO VAL PRO ILE          
SEQRES  18 A  265  SER TYR HIS GLN LEU GLU ALA PHE TYR SER ILE PHE THR          
SEQRES  19 A  265  THR GLU GLN GLN ASP HIS VAL LYS SER VAL GLU TYR LEU          
SEQRES  20 A  265  ARG ASN ASN PHE ARG PRO GLN GLN ARG LEU HIS ASP ARG          
SEQRES  21 A  265  VAL VAL SER LYS SER                                          
SEQRES   1 B  193  PHE LYS THR ARG MET ARG SER THR VAL SER VAL ARG GLU          
SEQRES   2 B  193  GLY GLN GLY VAL VAL LEU LEU CYS GLY PRO PRO PRO HIS          
SEQRES   3 B  193  SER GLY GLU LEU SER TYR ALA TRP VAL PHE ASN GLU TYR          
SEQRES   4 B  193  PRO SER PHE VAL GLU GLU ASP SER ARG ARG PHE VAL SER          
SEQRES   5 B  193  GLN GLU THR GLY HIS LEU TYR ILE ALA LYS VAL GLU PRO          
SEQRES   6 B  193  SER ASP VAL GLY ASN TYR THR CYS VAL VAL THR SER THR          
SEQRES   7 B  193  VAL THR ASN THR ARG VAL LEU GLY SER PRO THR PRO LEU          
SEQRES   8 B  193  VAL LEU ARG SER ASP GLY VAL MET GLY GLU TYR GLU PRO          
SEQRES   9 B  193  LYS ILE GLU VAL GLN PHE PRO GLU THR LEU PRO ALA ALA          
SEQRES  10 B  193  LYS GLY SER THR VAL ARG LEU GLU CYS PHE ALA LEU GLY          
SEQRES  11 B  193  ASN PRO VAL PRO GLN ILE ASN TRP ARG ARG SER ASP GLY          
SEQRES  12 B  193  MET PRO PHE PRO ASN LYS ILE LYS LEU ARG LYS PHE ASN          
SEQRES  13 B  193  GLY MET LEU GLU ILE GLN ASN PHE GLN GLN GLU ASP THR          
SEQRES  14 B  193  GLY SER TYR GLU CYS ILE ALA GLU ASN SER ARG GLY LYS          
SEQRES  15 B  193  ASN VAL ALA ARG GLY ARG LEU THR TYR TYR ALA                  
SEQRES   1 C  265  GLY ASP PRO TYR TRP ALA TYR SER GLY ALA TYR GLY PRO          
SEQRES   2 C  265  GLU HIS TRP VAL THR SER SER VAL SER CYS GLY GLY ARG          
SEQRES   3 C  265  HIS GLN SER PRO ILE ASP ILE LEU ASP GLN TYR ALA ARG          
SEQRES   4 C  265  VAL GLY GLU GLU TYR GLN GLU LEU GLN LEU ASP GLY PHE          
SEQRES   5 C  265  ASP ASN GLU SER SER ASN LYS THR TRP MET LYS ASN THR          
SEQRES   6 C  265  GLY LYS THR VAL ALA ILE LEU LEU LYS ASP ASP TYR PHE          
SEQRES   7 C  265  VAL SER GLY ALA GLY LEU PRO GLY ARG PHE LYS ALA GLU          
SEQRES   8 C  265  LYS VAL GLU PHE HIS TRP GLY HIS SER ASN GLY SER ALA          
SEQRES   9 C  265  GLY SER GLU HIS SER ILE ASN GLY ARG ARG PHE PRO VAL          
SEQRES  10 C  265  GLU MET GLN ILE PHE PHE TYR ASN PRO ASP ASP PHE ASP          
SEQRES  11 C  265  SER PHE GLN THR ALA ILE SER GLU ASN ARG ILE ILE GLY          
SEQRES  12 C  265  ALA MET ALA ILE PHE PHE GLN VAL SER PRO ARG ASP ASN          
SEQRES  13 C  265  SER ALA LEU ASP PRO ILE ILE HIS GLY LEU LYS GLY VAL          
SEQRES  14 C  265  VAL HIS HIS GLU LYS GLU THR PHE LEU ASP PRO PHE VAL          
SEQRES  15 C  265  LEU ARG ASP LEU LEU PRO ALA SER LEU GLY SER TYR TYR          
SEQRES  16 C  265  ARG TYR THR GLY SER LEU THR THR PRO PRO CYS SER GLU          
SEQRES  17 C  265  ILE VAL GLU TRP ILE VAL PHE ARG ARG PRO VAL PRO ILE          
SEQRES  18 C  265  SER TYR HIS GLN LEU GLU ALA PHE TYR SER ILE PHE THR          
SEQRES  19 C  265  THR GLU GLN GLN ASP HIS VAL LYS SER VAL GLU TYR LEU          
SEQRES  20 C  265  ARG ASN ASN PHE ARG PRO GLN GLN ARG LEU HIS ASP ARG          
SEQRES  21 C  265  VAL VAL SER LYS SER                                          
SEQRES   1 D  193  PHE LYS THR ARG MET ARG SER THR VAL SER VAL ARG GLU          
SEQRES   2 D  193  GLY GLN GLY VAL VAL LEU LEU CYS GLY PRO PRO PRO HIS          
SEQRES   3 D  193  SER GLY GLU LEU SER TYR ALA TRP VAL PHE ASN GLU TYR          
SEQRES   4 D  193  PRO SER PHE VAL GLU GLU ASP SER ARG ARG PHE VAL SER          
SEQRES   5 D  193  GLN GLU THR GLY HIS LEU TYR ILE ALA LYS VAL GLU PRO          
SEQRES   6 D  193  SER ASP VAL GLY ASN TYR THR CYS VAL VAL THR SER THR          
SEQRES   7 D  193  VAL THR ASN THR ARG VAL LEU GLY SER PRO THR PRO LEU          
SEQRES   8 D  193  VAL LEU ARG SER ASP GLY VAL MET GLY GLU TYR GLU PRO          
SEQRES   9 D  193  LYS ILE GLU VAL GLN PHE PRO GLU THR LEU PRO ALA ALA          
SEQRES  10 D  193  LYS GLY SER THR VAL ARG LEU GLU CYS PHE ALA LEU GLY          
SEQRES  11 D  193  ASN PRO VAL PRO GLN ILE ASN TRP ARG ARG SER ASP GLY          
SEQRES  12 D  193  MET PRO PHE PRO ASN LYS ILE LYS LEU ARG LYS PHE ASN          
SEQRES  13 D  193  GLY MET LEU GLU ILE GLN ASN PHE GLN GLN GLU ASP THR          
SEQRES  14 D  193  GLY SER TYR GLU CYS ILE ALA GLU ASN SER ARG GLY LYS          
SEQRES  15 D  193  ASN VAL ALA ARG GLY ARG LEU THR TYR TYR ALA                  
HET    MLI  A 401       7                                                       
HET    MLI  C 401       7                                                       
HET    FMT  C 402       3                                                       
HET    FMT  C 403       3                                                       
HET    MLI  D 401       7                                                       
HETNAM     MLI MALONATE ION                                                     
HETNAM     FMT FORMIC ACID                                                      
FORMUL   5  MLI    3(C3 H2 O4 2-)                                               
FORMUL   7  FMT    2(C H2 O2)                                                   
FORMUL  10  HOH   *59(H2 O)                                                     
HELIX    1 AA1 SER A   63  GLU A   69  5                                   7    
HELIX    2 AA2 HIS A   70  SER A   75  1                                   6    
HELIX    3 AA3 VAL A   76  GLY A   80  5                                   5    
HELIX    4 AA4 LEU A   89  ALA A   93  5                                   5    
HELIX    5 AA5 SER A  186  GLU A  193  1                                   8    
HELIX    6 AA6 ASN A  211  ALA A  213  5                                   3    
HELIX    7 AA7 LEU A  214  VAL A  224  1                                  11    
HELIX    8 AA8 VAL A  237  LEU A  242  5                                   6    
HELIX    9 AA9 SER A  277  SER A  286  1                                  10    
HELIX   10 AB1 GLU B  187  VAL B  191  5                                   5    
HELIX   11 AB2 LYS B  277  ASN B  279  5                                   3    
HELIX   12 AB3 GLN B  288  THR B  292  5                                   5    
HELIX   13 AB4 SER C   63  GLU C   69  5                                   7    
HELIX   14 AB5 HIS C   70  SER C   75  1                                   6    
HELIX   15 AB6 VAL C   76  GLY C   80  5                                   5    
HELIX   16 AB7 LEU C   89  ALA C   93  5                                   5    
HELIX   17 AB8 SER C  186  GLU C  193  1                                   8    
HELIX   18 AB9 LEU C  214  LYS C  222  1                                   9    
HELIX   19 AC1 VAL C  237  LEU C  242  5                                   6    
HELIX   20 AC2 SER C  277  GLU C  282  1                                   6    
HELIX   21 AC3 ALA C  283  SER C  286  5                                   4    
HELIX   22 AC4 GLU D  187  VAL D  191  5                                   5    
HELIX   23 AC5 LYS D  277  ASN D  279  5                                   3    
HELIX   24 AC6 GLN D  288  THR D  292  5                                   5    
SHEET    1 AA1 6 GLN A 103  ASP A 105  0                                        
SHEET    2 AA1 6 PHE A 133  SER A 135 -1  O  SER A 135   N  GLN A 103           
SHEET    3 AA1 6 PHE A 143  TRP A 152 -1  O  PHE A 143   N  VAL A 134           
SHEET    4 AA1 6 VAL A 124  LEU A 127 -1  N  ILE A 126   O  VAL A 148           
SHEET    5 AA1 6 TRP A 116  ASN A 119 -1  N  LYS A 118   O  ALA A 125           
SHEET    6 AA1 6 GLU A 230  PHE A 232 -1  O  THR A 231   N  MET A 117           
SHEET    1 AA2 8 GLN A 103  ASP A 105  0                                        
SHEET    2 AA2 8 PHE A 133  SER A 135 -1  O  SER A 135   N  GLN A 103           
SHEET    3 AA2 8 PHE A 143  TRP A 152 -1  O  PHE A 143   N  VAL A 134           
SHEET    4 AA2 8 VAL A 172  TYR A 179 -1  O  PHE A 177   N  GLU A 146           
SHEET    5 AA2 8 ILE A 197  VAL A 206 -1  O  ILE A 202   N  MET A 174           
SHEET    6 AA2 8 VAL A 265  ILE A 276  1  O  ILE A 268   N  ALA A 201           
SHEET    7 AA2 8 TYR A 249  GLY A 254 -1  N  GLY A 254   O  VAL A 265           
SHEET    8 AA2 8 SER A 318  SER A 320 -1  O  SER A 320   N  TYR A 249           
SHEET    1 AA3 5 PHE A 288  GLN A 293  0                                        
SHEET    2 AA3 5 VAL A 296  TYR A 301 -1  O  GLU A 300   N  THR A 289           
SHEET    3 AA3 5 VAL B 140  LEU B 142 -1  O  VAL B 141   N  LYS A 297           
SHEET    4 AA3 5 LEU B 181  ILE B 183 -1  O  LEU B 181   N  LEU B 142           
SHEET    5 AA3 5 ARG B 172  VAL B 174 -1  N  PHE B 173   O  TYR B 182           
SHEET    1 AA4 4 VAL B 132  VAL B 134  0                                        
SHEET    2 AA4 4 THR B 212  LEU B 216  1  O  VAL B 215   N  VAL B 134           
SHEET    3 AA4 4 GLY B 192  SER B 200 -1  N  TYR B 194   O  THR B 212           
SHEET    4 AA4 4 LEU B 153  PHE B 159 -1  N  SER B 154   O  THR B 199           
SHEET    1 AA5 4 VAL B 132  VAL B 134  0                                        
SHEET    2 AA5 4 THR B 212  LEU B 216  1  O  VAL B 215   N  VAL B 134           
SHEET    3 AA5 4 GLY B 192  SER B 200 -1  N  TYR B 194   O  THR B 212           
SHEET    4 AA5 4 ARG B 206  LEU B 208 -1  O  VAL B 207   N  VAL B 198           
SHEET    1 AA6 4 TYR B 225  GLN B 232  0                                        
SHEET    2 AA6 4 VAL B 245  ASN B 254 -1  O  LEU B 252   N  LYS B 228           
SHEET    3 AA6 4 MET B 281  ILE B 284 -1  O  ILE B 284   N  VAL B 245           
SHEET    4 AA6 4 ILE B 273  ARG B 276 -1  N  LYS B 274   O  GLU B 283           
SHEET    1 AA7 4 THR B 236  ALA B 240  0                                        
SHEET    2 AA7 4 GLY B 304  TYR B 315  1  O  ARG B 311   N  LEU B 237           
SHEET    3 AA7 4 GLY B 293  ASN B 301 -1  N  CYS B 297   O  ALA B 308           
SHEET    4 AA7 4 GLN B 258  ARG B 263 -1  N  ASN B 260   O  ILE B 298           
SHEET    1 AA8 2 ASP C  87  ILE C  88  0                                        
SHEET    2 AA8 2 SER C 164  ILE C 165  1  O  SER C 164   N  ILE C  88           
SHEET    1 AA9 6 GLN C 103  ASP C 105  0                                        
SHEET    2 AA9 6 PHE C 133  GLY C 136 -1  O  SER C 135   N  GLN C 103           
SHEET    3 AA9 6 LEU C 139  TRP C 152 -1  O  PHE C 143   N  VAL C 134           
SHEET    4 AA9 6 VAL C 172  TYR C 179 -1  O  PHE C 177   N  GLU C 146           
SHEET    5 AA9 6 ILE C 197  VAL C 206 -1  O  ILE C 202   N  MET C 174           
SHEET    6 AA9 6 VAL C 274  ILE C 276  1  O  VAL C 274   N  PHE C 203           
SHEET    1 AB1 9 GLU C 230  PHE C 232  0                                        
SHEET    2 AB1 9 TRP C 116  ASN C 119 -1  N  MET C 117   O  THR C 231           
SHEET    3 AB1 9 VAL C 124  LEU C 127 -1  O  ALA C 125   N  LYS C 118           
SHEET    4 AB1 9 LEU C 139  TRP C 152 -1  O  VAL C 148   N  ILE C 126           
SHEET    5 AB1 9 VAL C 172  TYR C 179 -1  O  PHE C 177   N  GLU C 146           
SHEET    6 AB1 9 ILE C 197  VAL C 206 -1  O  ILE C 202   N  MET C 174           
SHEET    7 AB1 9 VAL C 265  PHE C 270  1  O  ILE C 268   N  ALA C 201           
SHEET    8 AB1 9 TYR C 249  GLY C 254 -1  N  GLY C 254   O  VAL C 265           
SHEET    9 AB1 9 SER C 318  LYS C 319 -1  O  SER C 318   N  ARG C 251           
SHEET    1 AB2 5 PHE C 288  GLN C 293  0                                        
SHEET    2 AB2 5 VAL C 296  TYR C 301 -1  O  GLU C 300   N  THR C 289           
SHEET    3 AB2 5 VAL D 140  LEU D 142 -1  O  VAL D 141   N  LYS C 297           
SHEET    4 AB2 5 LEU D 181  ILE D 183 -1  O  ILE D 183   N  VAL D 140           
SHEET    5 AB2 5 ARG D 172  VAL D 174 -1  N  PHE D 173   O  TYR D 182           
SHEET    1 AB3 4 VAL D 132  VAL D 134  0                                        
SHEET    2 AB3 4 THR D 212  LEU D 216  1  O  VAL D 215   N  VAL D 134           
SHEET    3 AB3 4 GLY D 192  SER D 200 -1  N  GLY D 192   O  LEU D 214           
SHEET    4 AB3 4 LEU D 153  PHE D 159 -1  N  ALA D 156   O  VAL D 197           
SHEET    1 AB4 4 VAL D 132  VAL D 134  0                                        
SHEET    2 AB4 4 THR D 212  LEU D 216  1  O  VAL D 215   N  VAL D 134           
SHEET    3 AB4 4 GLY D 192  SER D 200 -1  N  GLY D 192   O  LEU D 214           
SHEET    4 AB4 4 VAL D 207  LEU D 208 -1  O  VAL D 207   N  VAL D 198           
SHEET    1 AB5 4 TYR D 225  GLN D 232  0                                        
SHEET    2 AB5 4 VAL D 245  ASN D 254 -1  O  LEU D 252   N  LYS D 228           
SHEET    3 AB5 4 MET D 281  ILE D 284 -1  O  ILE D 284   N  VAL D 245           
SHEET    4 AB5 4 LYS D 274  ARG D 276 -1  N  ARG D 276   O  MET D 281           
SHEET    1 AB6 4 THR D 236  ALA D 239  0                                        
SHEET    2 AB6 4 GLY D 304  TYR D 314  1  O  ARG D 311   N  LEU D 237           
SHEET    3 AB6 4 GLY D 293  ASN D 301 -1  N  TYR D 295   O  GLY D 310           
SHEET    4 AB6 4 GLN D 258  ARG D 263 -1  N  ASN D 260   O  ILE D 298           
SSBOND   1 CYS A   78    CYS A  261                          1555   1555  2.03  
SSBOND   2 CYS B  144    CYS B  196                          1555   1555  2.04  
SSBOND   3 CYS B  249    CYS B  297                          1555   1555  2.01  
SSBOND   4 CYS C   78    CYS C  261                          1555   1555  2.04  
SSBOND   5 CYS D  144    CYS D  196                          1555   1555  2.04  
SSBOND   6 CYS D  249    CYS D  297                          1555   1555  2.02  
CISPEP   1 SER A   84    PRO A   85          0         0.57                     
CISPEP   2 PRO A  259    PRO A  260          0        10.34                     
CISPEP   3 TYR B  162    PRO B  163          0        -5.01                     
CISPEP   4 ASN B  254    PRO B  255          0         2.15                     
CISPEP   5 SER C   84    PRO C   85          0        -1.05                     
CISPEP   6 PRO C  259    PRO C  260          0         8.60                     
CISPEP   7 TYR D  162    PRO D  163          0         7.12                     
CISPEP   8 ASN D  254    PRO D  255          0        -2.91                     
SITE     1 AC1  2 TRP A 116  PHE A 232                                          
SITE     1 AC2  2 GLU C 230  PHE C 232                                          
SITE     1 AC3  5 THR C 120  GLY C 121  LYS C 122  HIS C 227                    
SITE     2 AC3  5 THR C 290                                                     
SITE     1 AC4  3 THR C 120  LYS C 122  THR C 258                               
SITE     1 AC5  5 GLU D 177  PHE D 233  PRO D 234  ARG D 246                    
SITE     2 AC5  5 GLU D 248                                                     
CRYST1   74.138   90.526  147.448  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      0.013488  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011047  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006782        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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