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Database: PDB
Entry: 6P7S
LinkDB: 6P7S
Original site: 6P7S 
HEADER    VIRAL PROTEIN                           06-JUN-19   6P7S              
TITLE     CRYSTAL STRUCTURE OF THE CEDAR HENIPAVIRUS ATTACHMENT G GLYCOPROTEIN  
TITLE    2 GLOBULAR DOMAIN IN COMPLEX WITH THE RECEPTOR EPHRIN-B1               
CAVEAT     6P7S    NAG G 1 HAS WRONG CHIRALITY AT ATOM C1 NAG A 702 HAS WRONG   
CAVEAT   2 6P7S    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATTACHMENT GLYCOPROTEIN;                                   
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: GLOBULAR DOMAIN (UNP RESIDUES 193-622);                    
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: EPHRIN-B1;                                                 
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 FRAGMENT: UNP RESIDUES 29-170;                                       
COMPND  10 SYNONYM: CEK5 RECEPTOR LIGAND,CEK5-L,EFL-3,ELK LIGAND,ELK-L,EPH-     
COMPND  11 RELATED RECEPTOR TYROSINE KINASE LIGAND 2,LERK-2,STIMULATED BY       
COMPND  12 RETINOIC ACID GENE 1 PROTEIN;                                        
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CEDAR VIRUS;                                    
SOURCE   3 ORGANISM_TAXID: 1221391;                                             
SOURCE   4 EXPRESSION_SYSTEM: INSECT CELL EXPRESSION VECTOR PTIE1;              
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 266783;                                     
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   8 ORGANISM_COMMON: MOUSE;                                              
SOURCE   9 ORGANISM_TAXID: 10090;                                               
SOURCE  10 GENE: EFNB1, EPL2, EPLG2, LERK2, STRA1;                              
SOURCE  11 EXPRESSION_SYSTEM: INSECT CELL EXPRESSION VECTOR PTIE1;              
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 266783                                      
KEYWDS    CEDAR VIRUS, ATTACHMENT, GLYCOPROTEIN, G PROTEIN, VIRAL PROTEIN,      
KEYWDS   2 RECEPTOR, EPHRIN-B1, HENIPAVIRUS                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.XU,D.B.NIKOLOV,Y.XU                                                 
REVDAT   4   29-JUL-20 6P7S    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   23-OCT-19 6P7S    1       JRNL                                     
REVDAT   2   09-OCT-19 6P7S    1       JRNL                                     
REVDAT   1   25-SEP-19 6P7S    0                                                
JRNL        AUTH   E.D.LAING,C.K.NAVARATNARAJAH,S.CHELIOUT DA SILVA,            
JRNL        AUTH 2 S.R.PETZING,Y.XU,S.L.STERLING,G.A.MARSH,L.F.WANG,M.AMAYA,    
JRNL        AUTH 3 D.B.NIKOLOV,R.CATTANEO,C.C.BRODER,K.XU                       
JRNL        TITL   STRUCTURAL AND FUNCTIONAL ANALYSES REVEAL PROMISCUOUS AND    
JRNL        TITL 2 SPECIES SPECIFIC USE OF EPHRIN RECEPTORS BY CEDAR VIRUS.     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 116 20707 2019              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   31548390                                                     
JRNL        DOI    10.1073/PNAS.1911773116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.49 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.2_1309                                    
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.94                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 37244                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.390                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2007                            
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 44.9439 -  8.3943    0.99     2583   143  0.1892 0.1887        
REMARK   3     2  8.3943 -  6.6698    1.00     2540   143  0.1976 0.2334        
REMARK   3     3  6.6698 -  5.8287    1.00     2532   144  0.1820 0.2704        
REMARK   3     4  5.8287 -  5.2967    1.00     2544   145  0.1622 0.1917        
REMARK   3     5  5.2967 -  4.9176    1.00     2523   144  0.1581 0.1843        
REMARK   3     6  4.9176 -  4.6280    1.00     2520   144  0.1528 0.2002        
REMARK   3     7  4.6280 -  4.3964    1.00     2514   142  0.1721 0.2248        
REMARK   3     8  4.3964 -  4.2052    1.00     2513   144  0.1999 0.2253        
REMARK   3     9  4.2052 -  4.0434    1.00     2518   146  0.2262 0.2583        
REMARK   3    10  4.0434 -  3.9039    1.00     2497   144  0.2366 0.2688        
REMARK   3    11  3.9039 -  3.7819    1.00     2524   147  0.2498 0.2861        
REMARK   3    12  3.7819 -  3.6739    1.00     2503   142  0.2639 0.3242        
REMARK   3    13  3.6739 -  3.5772    1.00     2498   140  0.2985 0.3236        
REMARK   3    14  3.5772 -  3.4900    0.96     2428   139  0.3393 0.3762        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.510            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.560           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 132.6                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.91                          
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      :  0.011           9371                                  
REMARK   3   ANGLE     :  1.522          12689                                  
REMARK   3   CHIRALITY :  0.066           1414                                  
REMARK   3   PLANARITY :  0.009           1597                                  
REMARK   3   DIHEDRAL  : 19.190           3480                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN C                                     
REMARK   3     ATOM PAIRS NUMBER  : 3720                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 1183                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6P7S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000242066.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9192                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37299                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.10                              
REMARK 200  R MERGE                    (I) : 0.15000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.73400                            
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 78.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS, PH 8.5, 20% PEG6000,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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       79.58467            
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       39.79233            
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       59.68850            
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       19.89617            
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       99.48083            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 19.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, G                         
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 20.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, H                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A   194                                                      
REMARK 465     MET A   195                                                      
REMARK 465     TYR A   196                                                      
REMARK 465     SER A   197                                                      
REMARK 465     THR A   198                                                      
REMARK 465     ASN A   199                                                      
REMARK 465     ALA A   200                                                      
REMARK 465     TYR A   201                                                      
REMARK 465     ALA A   202                                                      
REMARK 465     GLU A   203                                                      
REMARK 465     LEU A   204                                                      
REMARK 465     ALA A   205                                                      
REMARK 465     GLY A   206                                                      
REMARK 465     PRO A   207                                                      
REMARK 465     PRO B   168                                                      
REMARK 465     ASN B   169                                                      
REMARK 465     ALA B   170                                                      
REMARK 465     ALA C   194                                                      
REMARK 465     MET C   195                                                      
REMARK 465     TYR C   196                                                      
REMARK 465     SER C   197                                                      
REMARK 465     THR C   198                                                      
REMARK 465     ASN C   199                                                      
REMARK 465     ALA C   200                                                      
REMARK 465     TYR C   201                                                      
REMARK 465     ALA C   202                                                      
REMARK 465     GLU C   203                                                      
REMARK 465     LEU C   204                                                      
REMARK 465     ALA C   205                                                      
REMARK 465     GLY C   206                                                      
REMARK 465     PRO C   207                                                      
REMARK 465     ALA D    29                                                      
REMARK 465     PRO D   168                                                      
REMARK 465     ASN D   169                                                      
REMARK 465     ALA D   170                                                      
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     ASP B 167    CG   OD1  OD2                                       
REMARK 470     ASP D 167    CG   OD1  OD2                                       
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   ND2  ASN A   311     C2   NAG A   701              1.80            
REMARK 500   ND2  ASN C   425     C2   NAG H     1              2.00            
REMARK 500   OG   SER C   573     NH1  ARG C   603              2.14            
REMARK 500   ND2  ASN C   311     C2   NAG C   701              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B  42   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO B  95   C   -  N   -  CA  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    CYS C 239   CA  -  CB  -  SG  ANGL. DEV. =   8.5 DEGREES          
REMARK 500    PRO C 354   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
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    ASP A 218       70.31     45.64                                   
REMARK 500    LYS A 456       70.03     51.31                                   
REMARK 500    SER A 480     -161.12   -124.18                                   
REMARK 500    LEU A 535      -67.11   -101.43                                   
REMARK 500    GLU A 554     -178.52   -172.57                                   
REMARK 500    THR A 564      -60.13   -101.81                                   
REMARK 500    ARG A 580      -80.85   -114.76                                   
REMARK 500    ASN A 605       46.07     34.48                                   
REMARK 500    PRO B 119       47.58    -86.46                                   
REMARK 500    THR B 155      -72.40    -83.54                                   
REMARK 500    ASP C 218       70.56     46.98                                   
REMARK 500    LEU C 327      -17.24     80.59                                   
REMARK 500    ASP C 328      -67.94   -100.13                                   
REMARK 500    THR C 424      -62.38    -98.68                                   
REMARK 500    THR C 443      -63.59   -120.48                                   
REMARK 500    SER C 480     -163.47   -123.62                                   
REMARK 500    VAL C 505      -54.88   -128.16                                   
REMARK 500    LEU C 535      -66.46   -105.16                                   
REMARK 500    ARG C 580      -75.75   -120.19                                   
REMARK 500    ASN C 605       47.27     33.47                                   
REMARK 500    PRO D  42     -168.86    -74.58                                   
REMARK 500    LYS D  43       -8.04     70.07                                   
REMARK 500    HIS D 105      -17.57     67.04                                   
REMARK 500    ARG D 156       -8.80     70.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6P7S A  194   622  UNP    J7H333   J7H333_9MONO   194    622             
DBREF  6P7S B   29   170  UNP    P52795   EFNB1_MOUSE     29    170             
DBREF  6P7S C  194   622  UNP    J7H333   J7H333_9MONO   194    622             
DBREF  6P7S D   29   170  UNP    P52795   EFNB1_MOUSE     29    170             
SEQRES   1 A  429  ALA MET TYR SER THR ASN ALA TYR ALA GLU LEU ALA GLY          
SEQRES   2 A  429  PRO PRO LYS ILE PHE CYS LYS SER VAL SER LYS ASP PRO          
SEQRES   3 A  429  ASP PHE ARG LEU LYS GLN ILE ASP TYR VAL ILE PRO VAL          
SEQRES   4 A  429  GLN GLN ASP ARG SER ILE CYS MET ASN ASN PRO LEU LEU          
SEQRES   5 A  429  ASP ILE SER ASP GLY PHE PHE THR TYR ILE HIS TYR GLU          
SEQRES   6 A  429  GLY ILE ASN SER CYS LYS LYS SER ASP SER PHE LYS VAL          
SEQRES   7 A  429  LEU LEU SER HIS GLY GLU ILE VAL ASP ARG GLY ASP TYR          
SEQRES   8 A  429  ARG PRO SER LEU TYR LEU LEU SER SER HIS TYR HIS PRO          
SEQRES   9 A  429  TYR SER MET GLN VAL ILE ASN CYS VAL PRO VAL THR CYS          
SEQRES  10 A  429  ASN GLN SER SER PHE VAL PHE CYS HIS ILE SER ASN ASN          
SEQRES  11 A  429  THR LYS THR LEU ASP ASN SER ASP TYR SER SER ASP GLU          
SEQRES  12 A  429  TYR TYR ILE THR TYR PHE ASN GLY ILE ASP ARG PRO LYS          
SEQRES  13 A  429  THR LYS LYS ILE PRO ILE ASN ASN MET THR ALA ASP ASN          
SEQRES  14 A  429  ARG TYR ILE HIS PHE THR PHE SER GLY GLY GLY GLY VAL          
SEQRES  15 A  429  CYS LEU GLY GLU GLU PHE ILE ILE PRO VAL THR THR VAL          
SEQRES  16 A  429  ILE ASN THR ASP VAL PHE THR HIS ASP TYR CYS GLU SER          
SEQRES  17 A  429  PHE ASN CYS SER VAL GLN THR GLY LYS SER LEU LYS GLU          
SEQRES  18 A  429  ILE CYS SER GLU SER LEU ARG SER PRO THR ASN SER SER          
SEQRES  19 A  429  ARG TYR ASN LEU ASN GLY ILE MET ILE ILE SER GLN ASN          
SEQRES  20 A  429  ASN MET THR ASP PHE LYS ILE GLN LEU ASN GLY ILE THR          
SEQRES  21 A  429  TYR ASN LYS LEU SER PHE GLY SER PRO GLY ARG LEU SER          
SEQRES  22 A  429  LYS THR LEU GLY GLN VAL LEU TYR TYR GLN SER SER MET          
SEQRES  23 A  429  SER TRP ASP THR TYR LEU LYS ALA GLY PHE VAL GLU LYS          
SEQRES  24 A  429  TRP LYS PRO PHE THR PRO ASN TRP MET ASN ASN THR VAL          
SEQRES  25 A  429  ILE SER ARG PRO ASN GLN GLY ASN CYS PRO ARG TYR HIS          
SEQRES  26 A  429  LYS CYS PRO GLU ILE CYS TYR GLY GLY THR TYR ASN ASP          
SEQRES  27 A  429  ILE ALA PRO LEU ASP LEU GLY LYS ASP MET TYR VAL SER          
SEQRES  28 A  429  VAL ILE LEU ASP SER ASP GLN LEU ALA GLU ASN PRO GLU          
SEQRES  29 A  429  ILE THR VAL PHE ASN SER THR THR ILE LEU TYR LYS GLU          
SEQRES  30 A  429  ARG VAL SER LYS ASP GLU LEU ASN THR ARG SER THR THR          
SEQRES  31 A  429  THR SER CYS PHE LEU PHE LEU ASP GLU PRO TRP CYS ILE          
SEQRES  32 A  429  SER VAL LEU GLU THR ASN ARG PHE ASN GLY LYS SER ILE          
SEQRES  33 A  429  ARG PRO GLU ILE TYR SER TYR LYS ILE PRO LYS TYR CYS          
SEQRES   1 B  142  ALA LYS ASN LEU GLU PRO VAL SER TRP SER SER LEU ASN          
SEQRES   2 B  142  PRO LYS PHE LEU SER GLY LYS GLY LEU VAL ILE TYR PRO          
SEQRES   3 B  142  LYS ILE GLY ASP LYS LEU ASP ILE ILE CYS PRO ARG ALA          
SEQRES   4 B  142  GLU ALA GLY ARG PRO TYR GLU TYR TYR LYS LEU TYR LEU          
SEQRES   5 B  142  VAL ARG PRO GLU GLN ALA ALA ALA CYS SER THR VAL LEU          
SEQRES   6 B  142  ASP PRO ASN VAL LEU VAL THR CYS ASN LYS PRO HIS GLN          
SEQRES   7 B  142  GLU ILE ARG PHE THR ILE LYS PHE GLN GLU PHE SER PRO          
SEQRES   8 B  142  ASN TYR MET GLY LEU GLU PHE LYS LYS TYR HIS ASP TYR          
SEQRES   9 B  142  TYR ILE THR SER THR SER ASN GLY SER LEU GLU GLY LEU          
SEQRES  10 B  142  GLU ASN ARG GLU GLY GLY VAL CYS ARG THR ARG THR MET          
SEQRES  11 B  142  LYS ILE VAL MET LYS VAL GLY GLN ASP PRO ASN ALA              
SEQRES   1 C  429  ALA MET TYR SER THR ASN ALA TYR ALA GLU LEU ALA GLY          
SEQRES   2 C  429  PRO PRO LYS ILE PHE CYS LYS SER VAL SER LYS ASP PRO          
SEQRES   3 C  429  ASP PHE ARG LEU LYS GLN ILE ASP TYR VAL ILE PRO VAL          
SEQRES   4 C  429  GLN GLN ASP ARG SER ILE CYS MET ASN ASN PRO LEU LEU          
SEQRES   5 C  429  ASP ILE SER ASP GLY PHE PHE THR TYR ILE HIS TYR GLU          
SEQRES   6 C  429  GLY ILE ASN SER CYS LYS LYS SER ASP SER PHE LYS VAL          
SEQRES   7 C  429  LEU LEU SER HIS GLY GLU ILE VAL ASP ARG GLY ASP TYR          
SEQRES   8 C  429  ARG PRO SER LEU TYR LEU LEU SER SER HIS TYR HIS PRO          
SEQRES   9 C  429  TYR SER MET GLN VAL ILE ASN CYS VAL PRO VAL THR CYS          
SEQRES  10 C  429  ASN GLN SER SER PHE VAL PHE CYS HIS ILE SER ASN ASN          
SEQRES  11 C  429  THR LYS THR LEU ASP ASN SER ASP TYR SER SER ASP GLU          
SEQRES  12 C  429  TYR TYR ILE THR TYR PHE ASN GLY ILE ASP ARG PRO LYS          
SEQRES  13 C  429  THR LYS LYS ILE PRO ILE ASN ASN MET THR ALA ASP ASN          
SEQRES  14 C  429  ARG TYR ILE HIS PHE THR PHE SER GLY GLY GLY GLY VAL          
SEQRES  15 C  429  CYS LEU GLY GLU GLU PHE ILE ILE PRO VAL THR THR VAL          
SEQRES  16 C  429  ILE ASN THR ASP VAL PHE THR HIS ASP TYR CYS GLU SER          
SEQRES  17 C  429  PHE ASN CYS SER VAL GLN THR GLY LYS SER LEU LYS GLU          
SEQRES  18 C  429  ILE CYS SER GLU SER LEU ARG SER PRO THR ASN SER SER          
SEQRES  19 C  429  ARG TYR ASN LEU ASN GLY ILE MET ILE ILE SER GLN ASN          
SEQRES  20 C  429  ASN MET THR ASP PHE LYS ILE GLN LEU ASN GLY ILE THR          
SEQRES  21 C  429  TYR ASN LYS LEU SER PHE GLY SER PRO GLY ARG LEU SER          
SEQRES  22 C  429  LYS THR LEU GLY GLN VAL LEU TYR TYR GLN SER SER MET          
SEQRES  23 C  429  SER TRP ASP THR TYR LEU LYS ALA GLY PHE VAL GLU LYS          
SEQRES  24 C  429  TRP LYS PRO PHE THR PRO ASN TRP MET ASN ASN THR VAL          
SEQRES  25 C  429  ILE SER ARG PRO ASN GLN GLY ASN CYS PRO ARG TYR HIS          
SEQRES  26 C  429  LYS CYS PRO GLU ILE CYS TYR GLY GLY THR TYR ASN ASP          
SEQRES  27 C  429  ILE ALA PRO LEU ASP LEU GLY LYS ASP MET TYR VAL SER          
SEQRES  28 C  429  VAL ILE LEU ASP SER ASP GLN LEU ALA GLU ASN PRO GLU          
SEQRES  29 C  429  ILE THR VAL PHE ASN SER THR THR ILE LEU TYR LYS GLU          
SEQRES  30 C  429  ARG VAL SER LYS ASP GLU LEU ASN THR ARG SER THR THR          
SEQRES  31 C  429  THR SER CYS PHE LEU PHE LEU ASP GLU PRO TRP CYS ILE          
SEQRES  32 C  429  SER VAL LEU GLU THR ASN ARG PHE ASN GLY LYS SER ILE          
SEQRES  33 C  429  ARG PRO GLU ILE TYR SER TYR LYS ILE PRO LYS TYR CYS          
SEQRES   1 D  142  ALA LYS ASN LEU GLU PRO VAL SER TRP SER SER LEU ASN          
SEQRES   2 D  142  PRO LYS PHE LEU SER GLY LYS GLY LEU VAL ILE TYR PRO          
SEQRES   3 D  142  LYS ILE GLY ASP LYS LEU ASP ILE ILE CYS PRO ARG ALA          
SEQRES   4 D  142  GLU ALA GLY ARG PRO TYR GLU TYR TYR LYS LEU TYR LEU          
SEQRES   5 D  142  VAL ARG PRO GLU GLN ALA ALA ALA CYS SER THR VAL LEU          
SEQRES   6 D  142  ASP PRO ASN VAL LEU VAL THR CYS ASN LYS PRO HIS GLN          
SEQRES   7 D  142  GLU ILE ARG PHE THR ILE LYS PHE GLN GLU PHE SER PRO          
SEQRES   8 D  142  ASN TYR MET GLY LEU GLU PHE LYS LYS TYR HIS ASP TYR          
SEQRES   9 D  142  TYR ILE THR SER THR SER ASN GLY SER LEU GLU GLY LEU          
SEQRES  10 D  142  GLU ASN ARG GLU GLY GLY VAL CYS ARG THR ARG THR MET          
SEQRES  11 D  142  LYS ILE VAL MET LYS VAL GLY GLN ASP PRO ASN ALA              
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    BMA  F   3      11                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    NAG  A 701      14                                                       
HET    NAG  A 702      14                                                       
HET    NAG  A 705      14                                                       
HET    NAG  C 701      14                                                       
HET    NAG  C 702      14                                                       
HET    NAG  C 705      14                                                       
HET    NAG  C 706      14                                                       
HET    NAG  D 201      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
FORMUL   5  NAG    16(C8 H15 N O6)                                              
FORMUL   6  BMA    C6 H12 O6                                                    
HELIX    1 AA1 TYR A  298  MET A  300  5                                   3    
HELIX    2 AA2 HIS A  396  SER A  401  1                                   6    
HELIX    3 AA3 SER A  411  SER A  419  1                                   9    
HELIX    4 AA4 ARG B   82  CYS B   89  1                                   8    
HELIX    5 AA5 GLY B  150  ARG B  154  5                                   5    
HELIX    6 AA6 TYR C  298  MET C  300  5                                   3    
HELIX    7 AA7 HIS C  396  SER C  401  1                                   6    
HELIX    8 AA8 SER C  411  SER C  419  1                                   9    
HELIX    9 AA9 ARG D   82  CYS D   89  1                                   8    
HELIX   10 AB1 GLY D  150  ARG D  154  5                                   5    
SHEET    1 AA1 4 LYS A 224  ILE A 226  0                                        
SHEET    2 AA1 4 GLU A 612  LYS A 617 -1  O  SER A 615   N  LYS A 224           
SHEET    3 AA1 4 PRO A 593  ASN A 602 -1  N  CYS A 595   O  TYR A 616           
SHEET    4 AA1 4 ASN A 578  LEU A 588 -1  N  PHE A 587   O  TRP A 594           
SHEET    1 AA2 4 ILE A 238  SER A 248  0                                        
SHEET    2 AA2 4 PHE A 251  ILE A 260 -1  O  TYR A 257   N  ASN A 241           
SHEET    3 AA2 4 LYS A 270  ASP A 280 -1  O  SER A 274   N  TYR A 254           
SHEET    4 AA2 4 PRO A 286  TYR A 295 -1  O  TYR A 289   N  GLU A 277           
SHEET    1 AA3 4 VAL A 302  CYS A 310  0                                        
SHEET    2 AA3 4 SER A 313  ILE A 320 -1  O  HIS A 319   N  ILE A 303           
SHEET    3 AA3 4 GLU A 336  PHE A 342 -1  O  GLU A 336   N  ILE A 320           
SHEET    4 AA3 4 LYS A 349  LYS A 352 -1  O  LYS A 349   N  TYR A 341           
SHEET    1 AA4 5 THR A 359  ALA A 360  0                                        
SHEET    2 AA4 5 ASP A 444  GLY A 451  1  O  ILE A 447   N  THR A 359           
SHEET    3 AA4 5 TYR A 429  ASN A 440 -1  N  SER A 438   O  LYS A 446           
SHEET    4 AA4 5 GLU A 380  ILE A 389 -1  N  ILE A 389   O  TYR A 429           
SHEET    5 AA4 5 HIS A 366  PHE A 369 -1  N  HIS A 366   O  VAL A 388           
SHEET    1 AA5 5 THR A 359  ALA A 360  0                                        
SHEET    2 AA5 5 ASP A 444  GLY A 451  1  O  ILE A 447   N  THR A 359           
SHEET    3 AA5 5 TYR A 429  ASN A 440 -1  N  SER A 438   O  LYS A 446           
SHEET    4 AA5 5 GLU A 380  ILE A 389 -1  N  ILE A 389   O  TYR A 429           
SHEET    5 AA5 5 VAL A 375  LEU A 377 -1  N  VAL A 375   O  ILE A 382           
SHEET    1 AA6 4 GLY A 463  THR A 468  0                                        
SHEET    2 AA6 4 GLN A 471  GLN A 476 -1  O  LEU A 473   N  SER A 466           
SHEET    3 AA6 4 ALA A 487  LYS A 492 -1  O  GLY A 488   N  TYR A 474           
SHEET    4 AA6 4 THR A 497  TRP A 500 -1  O  ASN A 499   N  PHE A 489           
SHEET    1 AA7 4 ILE A 532  PRO A 534  0                                        
SHEET    2 AA7 4 TYR A 542  LEU A 547 -1  O  VAL A 543   N  ALA A 533           
SHEET    3 AA7 4 PRO A 556  PHE A 561 -1  O  THR A 559   N  SER A 544           
SHEET    4 AA7 4 ILE A 566  ARG A 571 -1  O  TYR A 568   N  VAL A 560           
SHEET    1 AA8 3 VAL B  35  SER B  36  0                                        
SHEET    2 AA8 3 LYS B  59  CYS B  64  1  O  ASP B  61   N  VAL B  35           
SHEET    3 AA8 3 ILE B 108  LYS B 113 -1  O  ILE B 112   N  LEU B  60           
SHEET    1 AA9 5 LEU B  50  ILE B  52  0                                        
SHEET    2 AA9 5 LYS B 159  LYS B 163  1  O  VAL B 161   N  LEU B  50           
SHEET    3 AA9 5 ASP B 131  THR B 135 -1  N  ILE B 134   O  ILE B 160           
SHEET    4 AA9 5 TYR B  76  VAL B  81 -1  N  TYR B  79   O  THR B 135           
SHEET    5 AA9 5 ASN B  96  CYS B 101 -1  O  LEU B  98   N  LEU B  78           
SHEET    1 AB1 4 LYS C 224  ILE C 226  0                                        
SHEET    2 AB1 4 GLU C 612  LYS C 617 -1  O  SER C 615   N  LYS C 224           
SHEET    3 AB1 4 PRO C 593  ASN C 602 -1  N  CYS C 595   O  TYR C 616           
SHEET    4 AB1 4 ASN C 578  LEU C 588 -1  N  ASN C 578   O  ASN C 602           
SHEET    1 AB2 4 ILE C 238  SER C 248  0                                        
SHEET    2 AB2 4 PHE C 251  ILE C 260 -1  O  PHE C 251   N  SER C 248           
SHEET    3 AB2 4 LYS C 270  ASP C 280 -1  O  LYS C 270   N  GLU C 258           
SHEET    4 AB2 4 PRO C 286  TYR C 295 -1  O  TYR C 289   N  GLU C 277           
SHEET    1 AB3 4 VAL C 302  CYS C 310  0                                        
SHEET    2 AB3 4 SER C 313  ILE C 320 -1  O  HIS C 319   N  ILE C 303           
SHEET    3 AB3 4 GLU C 336  PHE C 342 -1  O  GLU C 336   N  ILE C 320           
SHEET    4 AB3 4 LYS C 349  LYS C 352 -1  O  LYS C 349   N  TYR C 341           
SHEET    1 AB4 5 THR C 359  ALA C 360  0                                        
SHEET    2 AB4 5 ASP C 444  GLY C 451  1  O  ILE C 447   N  THR C 359           
SHEET    3 AB4 5 TYR C 429  ASN C 440 -1  N  SER C 438   O  LYS C 446           
SHEET    4 AB4 5 GLU C 380  ILE C 389 -1  N  ILE C 389   O  TYR C 429           
SHEET    5 AB4 5 HIS C 366  PHE C 369 -1  N  HIS C 366   O  VAL C 388           
SHEET    1 AB5 5 THR C 359  ALA C 360  0                                        
SHEET    2 AB5 5 ASP C 444  GLY C 451  1  O  ILE C 447   N  THR C 359           
SHEET    3 AB5 5 TYR C 429  ASN C 440 -1  N  SER C 438   O  LYS C 446           
SHEET    4 AB5 5 GLU C 380  ILE C 389 -1  N  ILE C 389   O  TYR C 429           
SHEET    5 AB5 5 VAL C 375  LEU C 377 -1  N  VAL C 375   O  ILE C 382           
SHEET    1 AB6 4 GLY C 463  THR C 468  0                                        
SHEET    2 AB6 4 GLN C 471  GLN C 476 -1  O  LEU C 473   N  SER C 466           
SHEET    3 AB6 4 LYS C 486  LYS C 492 -1  O  GLY C 488   N  TYR C 474           
SHEET    4 AB6 4 THR C 497  PRO C 498 -1  O  THR C 497   N  LYS C 492           
SHEET    1 AB7 4 ILE C 532  PRO C 534  0                                        
SHEET    2 AB7 4 TYR C 542  LEU C 547 -1  O  VAL C 543   N  ALA C 533           
SHEET    3 AB7 4 PRO C 556  PHE C 561 -1  O  GLU C 557   N  ILE C 546           
SHEET    4 AB7 4 ILE C 566  ARG C 571 -1  O  GLU C 570   N  ILE C 558           
SHEET    1 AB8 3 VAL D  35  SER D  36  0                                        
SHEET    2 AB8 3 ASP D  61  CYS D  64  1  O  ASP D  61   N  VAL D  35           
SHEET    3 AB8 3 ILE D 108  THR D 111 -1  O  PHE D 110   N  ILE D  62           
SHEET    1 AB9 5 LEU D  50  ILE D  52  0                                        
SHEET    2 AB9 5 LYS D 159  LYS D 163  1  O  VAL D 161   N  LEU D  50           
SHEET    3 AB9 5 ASP D 131  SER D 136 -1  N  ILE D 134   O  ILE D 160           
SHEET    4 AB9 5 TYR D  76  VAL D  81 -1  N  VAL D  81   O  TYR D 133           
SHEET    5 AB9 5 VAL D  97  CYS D 101 -1  O  LEU D  98   N  LEU D  78           
SSBOND   1 CYS A  212    CYS A  622                          1555   1555  2.04  
SSBOND   2 CYS A  239    CYS A  263                          1555   1555  2.05  
SSBOND   3 CYS A  305    CYS A  318                          1555   1555  2.07  
SSBOND   4 CYS A  310    CYS A  376                          1555   1555  2.04  
SSBOND   5 CYS A  399    CYS A  416                          1555   1555  2.03  
SSBOND   6 CYS A  404    CYS A  520                          1555   1555  2.04  
SSBOND   7 CYS A  514    CYS A  524                          1555   1555  2.04  
SSBOND   8 CYS A  586    CYS A  595                          1555   1555  2.03  
SSBOND   9 CYS B   64    CYS B  101                          1555   1555  2.02  
SSBOND  10 CYS B   89    CYS B  153                          1555   1555  2.04  
SSBOND  11 CYS C  212    CYS C  622                          1555   1555  2.04  
SSBOND  12 CYS C  239    CYS C  263                          1555   1555  2.06  
SSBOND  13 CYS C  305    CYS C  318                          1555   1555  2.04  
SSBOND  14 CYS C  310    CYS C  376                          1555   1555  2.04  
SSBOND  15 CYS C  399    CYS C  416                          1555   1555  2.03  
SSBOND  16 CYS C  404    CYS C  520                          1555   1555  2.05  
SSBOND  17 CYS C  514    CYS C  524                          1555   1555  2.04  
SSBOND  18 CYS C  586    CYS C  595                          1555   1555  2.03  
SSBOND  19 CYS D   64    CYS D  101                          1555   1555  2.04  
SSBOND  20 CYS D   89    CYS D  153                          1555   1555  2.03  
LINK         ND2 ASN A 311                 C1  NAG A 701     1555   1555  1.44  
LINK         ND2 ASN A 322                 C1  NAG A 702     1555   1555  1.44  
LINK         ND2 ASN A 425                 C1  NAG E   1     1555   1555  1.45  
LINK         ND2 ASN A 502                 C1  NAG A 705     1555   1555  1.45  
LINK         ND2 ASN A 562                 C1  NAG F   1     1555   1555  1.45  
LINK         ND2 ASN B 139                 C1  NAG G   1     1555   1555  1.46  
LINK         ND2 ASN C 311                 C1  NAG C 701     1555   1555  1.44  
LINK         ND2 ASN C 322                 C1  NAG C 702     1555   1555  1.46  
LINK         ND2 ASN C 425                 C1  NAG H   1     1555   1555  1.46  
LINK         ND2 ASN C 502                 C1  NAG C 705     1555   1555  1.44  
LINK         ND2 ASN C 562                 C1  NAG C 706     1555   1555  1.44  
LINK         ND2 ASN D 139                 C1  NAG D 201     1555   1555  1.46  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.45  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.45  
LINK         O4  NAG F   2                 C1  BMA F   3     1555   1555  1.45  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.44  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.45  
CISPEP   1 LYS A  494    PRO A  495          0        -1.74                     
CISPEP   2 LYS C  494    PRO C  495          0         1.52                     
CRYST1  207.570  207.570  119.377  90.00  90.00 120.00 P 65         12          
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      0.004818  0.002781  0.000000        0.00000                         
SCALE2      0.000000  0.005563  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008377        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system