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Database: PDB
Entry: 2WO3
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Original site: 2WO3 
HEADER    TRANSFERASE/SIGNALING PROTEIN           21-JUL-09   2WO3              
TITLE     CRYSTAL STRUCTURE OF THE EPHA4-EPHRINA2 COMPLEX                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPHRIN TYPE-A RECEPTOR;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EPHRIN LIGAND BINDING DOMAIN, RESIDUES 30-202;             
COMPND   5 SYNONYM: TYROSINE-PROTEIN KINASE RECEPTOR SEK, RECEPTOR PROTEIN-     
COMPND   6 TYROSINE KINASE HEK8, TYROSINE-PROTEIN KINASE TYRO1;                 
COMPND   7 EC: 2.7.10.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: EPHRIN-A2;                                                 
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: EPH RECEPTOR BINDING DOMAIN, RESIDUES 33-177;              
COMPND  13 SYNONYM: EPH-RELATED RECEPTOR TYROSINE KINASE LIGAND 6, HEK7-LIGAND, 
COMPND  14 LERK-6, HEK7-L;                                                      
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MUTATION: YES;                                                       
COMPND  17 OTHER_DETAILS: N-ACETYLGLUCOSAMINE LINKAGES OBSERVED IN STRUCTURE AT 
COMPND  18 ASN 42                                                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;                                
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PHLSEC;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  15 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;                                
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PHLSEC                                    
KEYWDS    TRANSFERASE-SIGNALING PROTEIN COMPLEX, EFN, EPH, EPHA4, KINASE,       
KEYWDS   2 EPHRIN, COMPLEX, MEMBRANE, CELL SURFACE RECEPTOR, TYROSINE-PROTEIN   
KEYWDS   3 KINASE, GLYCOPROTEIN, EPHRINA2                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.A.BOWDEN,A.R.ARICESCU,J.E.NETTLESHIP,C.SIEBOLD,N.RAHMAN-HUQ,        
AUTHOR   2 R.J.OWENS,D.I.STUART,E.Y.JONES                                       
REVDAT   4   28-FEB-18 2WO3    1       SOURCE                                   
REVDAT   3   23-NOV-11 2WO3    1       JRNL                                     
REVDAT   2   13-JUL-11 2WO3    1       VERSN                                    
REVDAT   1   27-OCT-09 2WO3    0                                                
JRNL        AUTH   T.A.BOWDEN,A.R.ARICESCU,J.E.NETTLESHIP,C.SIEBOLD,            
JRNL        AUTH 2 N.RAHMAN-HUQ,R.J.OWENS,D.I.STUART,E.Y.JONES                  
JRNL        TITL   STRUCTURAL PLASTICITY OF EPH-RECEPTOR A4 FACILITATES         
JRNL        TITL 2 CROSS-CLASS EPHRIN SIGNALLING                                
JRNL        REF    STRUCTURE                     V.  17  1386 2009              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   19836338                                                     
JRNL        DOI    10.1016/J.STR.2009.07.018                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
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) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 17987                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 954                             
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) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1295                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.78                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4420                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 80                           
REMARK   3   BIN FREE R VALUE                    : 0.4230                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2576                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 136                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 58.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.19000                                              
REMARK   3    B22 (A**2) : 1.19000                                              
REMARK   3    B33 (A**2) : -1.78000                                             
REMARK   3    B12 (A**2) : 0.59000                                              
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): 0.295         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.229         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.148         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.556        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2680 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1858 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3639 ; 1.287 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4463 ; 0.807 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   316 ; 6.389 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   139 ;30.513 ;23.165       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   425 ;15.017 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;13.384 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   376 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2998 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   593 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1582 ; 0.750 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   640 ; 0.099 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2557 ; 1.409 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1098 ; 1.560 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1082 ; 2.644 ; 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  : 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 :   B    32        B   173                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.8600 -44.8480  27.8600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0583 T22:   0.1686                                     
REMARK   3      T33:   0.0319 T12:  -0.0532                                     
REMARK   3      T13:   0.0152 T23:  -0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8431 L22:   0.8936                                     
REMARK   3      L33:   4.3541 L12:  -0.1820                                     
REMARK   3      L13:   0.3498 L23:   0.4448                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0767 S12:  -0.0517 S13:   0.0468                       
REMARK   3      S21:   0.1288 S22:  -0.2086 S23:  -0.0673                       
REMARK   3      S31:   0.2520 S32:  -0.2501 S33:   0.1319                       
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 :   A    28        A   203                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.1370 -40.8940   9.6280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0886 T22:   0.1142                                     
REMARK   3      T33:   0.0082 T12:   0.0215                                     
REMARK   3      T13:   0.0053 T23:   0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4989 L22:   1.1352                                     
REMARK   3      L33:   0.9061 L12:  -0.3875                                     
REMARK   3      L13:  -0.2482 L23:   0.1455                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0713 S12:  -0.1605 S13:  -0.1446                       
REMARK   3      S21:   0.0326 S22:   0.0255 S23:  -0.0169                       
REMARK   3      S31:  -0.0320 S32:   0.0740 S33:   0.0458                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2WO3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JUL-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290040471.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.81                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18961                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 16.00                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.75000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
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 1KGY                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 200 MM KNO3, PH 8.0        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+1/3                                            
REMARK 290       6555   X-Y,X,Z+2/3                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       19.78467            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       39.56933            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       19.78467            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       39.56933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.8 KCAL/MOL                         
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 174 TO GLN                        
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     GLU A    27                                                      
REMARK 465     THR A   204                                                      
REMARK 465     LYS A   205                                                      
REMARK 465     HIS A   206                                                      
REMARK 465     HIS A   207                                                      
REMARK 465     HIS A   208                                                      
REMARK 465     HIS A   209                                                      
REMARK 465     HIS A   210                                                      
REMARK 465     HIS A   211                                                      
REMARK 465     GLU B    30                                                      
REMARK 465     THR B    31                                                      
REMARK 465     GLY B    32                                                      
REMARK 465     GLU B   175                                                      
REMARK 465     THR B   176                                                      
REMARK 465     LEU B   177                                                      
REMARK 465     GLY B   178                                                      
REMARK 465     THR B   179                                                      
REMARK 465     LYS B   180                                                      
REMARK 465     HIS B   181                                                      
REMARK 465     HIS B   182                                                      
REMARK 465     HIS B   183                                                      
REMARK 465     HIS B   184                                                      
REMARK 465     HIS B   185                                                      
REMARK 465     HIS B   186                                                      
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   O    HOH A  2039     O    HOH A  2039     4445     2.14            
REMARK 500   O    HOH B  2064     O    HOH B  2064     4545     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    VAL A  39      130.78    -37.40                                   
REMARK 500    GLU A  62      -60.10    -26.74                                   
REMARK 500    CYS A  73       53.96   -154.64                                   
REMARK 500    GLU A  92     -113.31     49.83                                   
REMARK 500    LYS A 133       53.19   -151.89                                   
REMARK 500    ASP B  54       98.10   -164.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED (DSSP).                        
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED (DSSP).                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1175                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1176                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WO1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE EPHA4 LIGAND BINDING DOMAIN                 
REMARK 900 RELATED ID: 2WO2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE EPHA4-EPHRINB2 COMPLEX                      
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 Q174N SITE-DIRECTED MUTATION TO PROMOTE CRYSTALLOGENESIS             
DBREF  2WO3 A   30   202  UNP    P54764   EPHA4_HUMAN     30    202             
DBREF  2WO3 B   33   173  UNP    O43921   EFNA2_HUMAN     33    173             
SEQADV 2WO3 GLU A   27  UNP  P54764              EXPRESSION TAG                 
SEQADV 2WO3 THR A   28  UNP  P54764              EXPRESSION TAG                 
SEQADV 2WO3 GLY A   29  UNP  P54764              EXPRESSION TAG                 
SEQADV 2WO3 ARG A  203  UNP  P54764              EXPRESSION TAG                 
SEQADV 2WO3 THR A  204  UNP  P54764              EXPRESSION TAG                 
SEQADV 2WO3 LYS A  205  UNP  P54764              EXPRESSION TAG                 
SEQADV 2WO3 HIS A  206  UNP  P54764              EXPRESSION TAG                 
SEQADV 2WO3 HIS A  207  UNP  P54764              EXPRESSION TAG                 
SEQADV 2WO3 HIS A  208  UNP  P54764              EXPRESSION TAG                 
SEQADV 2WO3 HIS A  209  UNP  P54764              EXPRESSION TAG                 
SEQADV 2WO3 HIS A  210  UNP  P54764              EXPRESSION TAG                 
SEQADV 2WO3 HIS A  211  UNP  P54764              EXPRESSION TAG                 
SEQADV 2WO3 GLU B   30  UNP  O43921              EXPRESSION TAG                 
SEQADV 2WO3 THR B   31  UNP  O43921              EXPRESSION TAG                 
SEQADV 2WO3 GLY B   32  UNP  O43921              EXPRESSION TAG                 
SEQADV 2WO3 GLN B  174  UNP  O43921    ASN   174 ENGINEERED MUTATION            
SEQADV 2WO3 GLU B  175  UNP  O43921              EXPRESSION TAG                 
SEQADV 2WO3 THR B  176  UNP  O43921              EXPRESSION TAG                 
SEQADV 2WO3 LEU B  177  UNP  O43921              EXPRESSION TAG                 
SEQADV 2WO3 GLY B  178  UNP  O43921              EXPRESSION TAG                 
SEQADV 2WO3 THR B  179  UNP  O43921              EXPRESSION TAG                 
SEQADV 2WO3 LYS B  180  UNP  O43921              EXPRESSION TAG                 
SEQADV 2WO3 HIS B  181  UNP  O43921              EXPRESSION TAG                 
SEQADV 2WO3 HIS B  182  UNP  O43921              EXPRESSION TAG                 
SEQADV 2WO3 HIS B  183  UNP  O43921              EXPRESSION TAG                 
SEQADV 2WO3 HIS B  184  UNP  O43921              EXPRESSION TAG                 
SEQADV 2WO3 HIS B  185  UNP  O43921              EXPRESSION TAG                 
SEQADV 2WO3 HIS B  186  UNP  O43921              EXPRESSION TAG                 
SEQRES   1 A  185  GLU THR GLY GLU VAL THR LEU LEU ASP SER ARG SER VAL          
SEQRES   2 A  185  GLN GLY GLU LEU GLY TRP ILE ALA SER PRO LEU GLU GLY          
SEQRES   3 A  185  GLY TRP GLU GLU VAL SER ILE MET ASP GLU LYS ASN THR          
SEQRES   4 A  185  PRO ILE ARG THR TYR GLN VAL CYS ASN VAL MET GLU PRO          
SEQRES   5 A  185  SER GLN ASN ASN TRP LEU ARG THR ASP TRP ILE THR ARG          
SEQRES   6 A  185  GLU GLY ALA GLN ARG VAL TYR ILE GLU ILE LYS PHE THR          
SEQRES   7 A  185  LEU ARG ASP CYS ASN SER LEU PRO GLY VAL MET GLY THR          
SEQRES   8 A  185  CYS LYS GLU THR PHE ASN LEU TYR TYR TYR GLU SER ASP          
SEQRES   9 A  185  ASN ASP LYS GLU ARG PHE ILE ARG GLU ASN GLN PHE VAL          
SEQRES  10 A  185  LYS ILE ASP THR ILE ALA ALA ASP GLU SER PHE THR GLN          
SEQRES  11 A  185  VAL ASP ILE GLY ASP ARG ILE MET LYS LEU ASN THR GLU          
SEQRES  12 A  185  ILE ARG ASP VAL GLY PRO LEU SER LYS LYS GLY PHE TYR          
SEQRES  13 A  185  LEU ALA PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU VAL          
SEQRES  14 A  185  SER VAL ARG VAL PHE TYR LYS ARG THR LYS HIS HIS HIS          
SEQRES  15 A  185  HIS HIS HIS                                                  
SEQRES   1 B  157  GLU THR GLY ASN SER ASP ARG TYR ALA VAL TYR TRP ASN          
SEQRES   2 B  157  ARG SER ASN PRO ARG PHE HIS ALA GLY ALA GLY ASP ASP          
SEQRES   3 B  157  GLY GLY GLY TYR THR VAL GLU VAL SER ILE ASN ASP TYR          
SEQRES   4 B  157  LEU ASP ILE TYR CYS PRO HIS TYR GLY ALA PRO LEU PRO          
SEQRES   5 B  157  PRO ALA GLU ARG MET GLU HIS TYR VAL LEU TYR MET VAL          
SEQRES   6 B  157  ASN GLY GLU GLY HIS ALA SER CYS ASP HIS ARG GLN ARG          
SEQRES   7 B  157  GLY PHE LYS ARG TRP GLU CYS ASN ARG PRO ALA ALA PRO          
SEQRES   8 B  157  GLY GLY PRO LEU LYS PHE SER GLU LYS PHE GLN LEU PHE          
SEQRES   9 B  157  THR PRO PHE SER LEU GLY PHE GLU PHE ARG PRO GLY HIS          
SEQRES  10 B  157  GLU TYR TYR TYR ILE SER ALA THR PRO PRO ASN ALA VAL          
SEQRES  11 B  157  ASP ARG PRO CYS LEU ARG LEU LYS VAL TYR VAL ARG PRO          
SEQRES  12 B  157  THR GLN GLU THR LEU GLY THR LYS HIS HIS HIS HIS HIS          
SEQRES  13 B  157  HIS                                                          
MODRES 2WO3 ASN B   42  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B1175      14                                                       
HET    NAG  B1176      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4  HOH   *136(H2 O)                                                    
HELIX    1   1 CYS A  108  SER A  110  5                                   3    
HELIX    2   2 GLU A  139  GLN A  141  5                                   3    
HELIX    3   3 GLN A  156  ASP A  161  1                                   6    
HELIX    4   4 ALA B   83  ARG B   85  5                                   3    
HELIX    5   5 GLY B   96  SER B  101  1                                   6    
SHEET    1   A 5 ILE A  46  SER A  48  0                                        
SHEET    2   A 5 ASN A  82  ARG A  85 -1  N  ARG A  85   O  ILE A  46           
SHEET    3   A 5 GLY A 180  ASP A 187 -1  N  ASP A 187   O  ASN A  82           
SHEET    4   A 5 THR A 121  SER A 129 -1  N  SER A 129   O  GLY A 180           
SHEET    5   A 5 VAL A 143  ALA A 149 -1  N  ILE A 148   O  PHE A 122           
SHEET    1   B 5 GLU A  55  MET A  60  0                                        
SHEET    2   B 5 PRO A  66  CYS A  73 -1  N  GLN A  71   O  GLU A  55           
SHEET    3   B 5 CYS A 191  TYR A 201 -1  N  LEU A 194   O  TYR A  70           
SHEET    4   B 5 VAL A  97  LEU A 105 -1  N  THR A 104   O  ALA A 193           
SHEET    5   B 5 ASN A 167  VAL A 173 -1  N  VAL A 173   O  VAL A  97           
SHEET    1   C 2 GLU A  30  ASP A  35  0                                        
SHEET    2   C 2 ARG A 198  LYS A 202 -1  N  TYR A 201   O  VAL A  31           
SHEET    1   D 3 ARG B  36  TRP B  41  0                                        
SHEET    2   D 3 TYR B  68  CYS B  73  1  N  TYR B  68   O  TYR B  37           
SHEET    3   D 3 LYS B 125  LYS B 129 -1  N  GLU B 128   O  LEU B  69           
SHEET    1   E 5 TYR B  59  VAL B  63  0                                        
SHEET    2   E 5 ARG B 165  VAL B 170  1  N  LYS B 167   O  TYR B  59           
SHEET    3   E 5 GLU B 147  ALA B 153 -1  N  TYR B 150   O  LEU B 166           
SHEET    4   E 5 TYR B  89  VAL B  94 -1  N  VAL B  94   O  TYR B 149           
SHEET    5   E 5 GLY B 108  CYS B 114 -1  N  CYS B 114   O  TYR B  89           
SSBOND   1 CYS A   73    CYS A  191                          1555   1555  2.05  
SSBOND   2 CYS A  108    CYS A  118                          1555   1555  2.04  
SSBOND   3 CYS B   73    CYS B  114                          1555   1555  2.04  
SSBOND   4 CYS B  102    CYS B  163                          1555   1555  2.05  
LINK         ND2 ASN B  42                 C1  NAG B1175     1555   1555  1.45  
LINK         O4  NAG B1175                 C1  NAG B1176     1555   1555  1.45  
CISPEP   1 SER A   48    PRO A   49          0         2.02                     
CISPEP   2 GLY A  174    PRO A  175          0         2.89                     
CISPEP   3 ALA B   78    PRO B   79          0         1.90                     
CISPEP   4 PRO B  155    PRO B  156          0         2.16                     
CISPEP   5 ARG B  161    PRO B  162          0        -1.00                     
SITE     1 AC1  7 TYR B  40  ASN B  42  ASN B  45  PRO B  74                    
SITE     2 AC1  7 HIS B  75  TYR B  76  NAG B1176                               
SITE     1 AC2  1 NAG B1175                                                     
CRYST1  115.412  115.412   59.354  90.00  90.00 120.00 P 64          6          
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      0.008665  0.005002  0.000000        0.00000                         
SCALE2      0.000000  0.010005  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016848        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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