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Database: PDB
Entry: 4UM9
LinkDB: 4UM9
Original site: 4UM9 
HEADER    IMMUNE SYSTEM                           15-MAY-14   4UM9              
TITLE     CRYSTAL STRUCTURE OF ALPHA V BETA 6 WITH PEPTIDE                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-V;                                          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: HEADPIECE, RESIDUES 31-625;                                
COMPND   5 SYNONYM: VITRONECTIN RECEPTOR SUBUNIT ALPHA, INTEGRIN ALPHA V;       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTEGRIN BETA-6;                                           
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: INTEGRIN BETA 6;                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: TRANSFORMING GROWTH FACTOR BETA 3;                         
COMPND  15 CHAIN: E, F;                                                         
COMPND  16 FRAGMENT: RESIDUES 7-17;                                             
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: INTEGRIN BETA-6;                                           
COMPND  20 CHAIN: D;                                                            
COMPND  21 SYNONYM: INTEGRIN BETA 6;                                            
COMPND  22 ENGINEERED: YES                                                      
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: HEK293S GNT I- CELL;                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCDNA 3.1 AND ET10;                       
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  16 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNT I- CELL;                    
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PCDNA 3.1 AND ET10;                       
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  26 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  28 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNT I- CELL;                    
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PCDNA 3.1 AND ET10;                       
SOURCE  31 MOL_ID: 4;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  33 ORGANISM_COMMON: HUMAN;                                              
SOURCE  34 ORGANISM_TAXID: 9606;                                                
SOURCE  35 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  36 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  37 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  38 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNT I- CELL;                    
SOURCE  39 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  40 EXPRESSION_SYSTEM_PLASMID: PCDNA 3.1 AND ET10                        
KEYWDS    IMMUNE SYSTEM, CELL SURFACE RECEPTOR                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.DONG,T.A.SPRINGER                                                   
REVDAT   4   16-MAR-16 4UM9    1       REMARK DBREF  SEQADV SEQRES              
REVDAT   4 2                           SITE   MASTER                            
REVDAT   3   17-DEC-14 4UM9    1       JRNL                                     
REVDAT   2   19-NOV-14 4UM9    1       JRNL                                     
REVDAT   1   12-NOV-14 4UM9    0                                                
JRNL        AUTH   X.DONG,N.E.HUDSON,C.LU,T.A.SPRINGER                          
JRNL        TITL   STRUCTURAL DETERMINANTS OF INTEGRIN BETA-SUBUNIT             
JRNL        TITL 2 SPECIFICITY FOR LATENT TGF-BETA                              
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  21  1091 2014              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   25383667                                                     
JRNL        DOI    10.1038/NSMB.2905                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT 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,3             
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 : N/A                                           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.5                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50                             
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.99                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 100024                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.4                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1415                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3     1 48.4014 -  5.3840    0.93     9823   143  0.1811 0.2151        
REMARK   3     2  5.3840 -  4.2743    0.95     9977   144  0.1581 0.2135        
REMARK   3     3  4.2743 -  3.7342    0.96    10022   137  0.1828 0.2316        
REMARK   3     4  3.7342 -  3.3929    0.96     9995   143  0.2258 0.2758        
REMARK   3     5  3.3929 -  3.1497    0.98    10222   147  0.2580 0.3342        
REMARK   3     6  3.1497 -  2.9641    0.98    10239   148  0.2894 0.3251        
REMARK   3     7  2.9641 -  2.8156    0.98    10142   147  0.3133 0.3535        
REMARK   3     8  2.8156 -  2.6931    0.98    10154   148  0.3375 0.3815        
REMARK   3     9  2.6931 -  2.5894    0.97    10056   139  0.3720 0.3781        
REMARK   3    10  2.5894 -  2.5001    0.77     7979   119  0.3974 0.4490        
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 1                                             
REMARK   3   B_SOL              : 1                                             
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.53             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.39            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 54.54                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 74.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           NULL                                  
REMARK   3   ANGLE     :  1.258           NULL                                  
REMARK   3   CHIRALITY :  0.056           NULL                                  
REMARK   3   PLANARITY :  0.005           NULL                                  
REMARK   3   DIHEDRAL  : 11.821           NULL                                  
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 : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: N/A                                       
REMARK   4                                                                      
REMARK   4 4UM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAY-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-60643.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-AUG-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9796                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 100024                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.35                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 2.3                                
REMARK 200  R MERGE                    (I) : 0.12                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.90                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.1                                
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.35                               
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 4G1M                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.6                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4000, 0.1 M                      
REMARK 280  NACACODYLATE, PH 6.0                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       92.51000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       84.04500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       92.51000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       84.04500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10560 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 45650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F                               
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10820 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 46590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375  S   SO4 A1595   LIES ON A SPECIAL POSITION.                         
REMARK 375      HOH A4072   LIES ON A SPECIAL POSITION.                         
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     ASP A   595                                                      
REMARK 465     THR A   596                                                      
REMARK 465     GLY A   597                                                      
REMARK 465     GLY A   598                                                      
REMARK 465     LEU A   599                                                      
REMARK 465     GLU A   600                                                      
REMARK 465     VAL A   601                                                      
REMARK 465     LEU A   602                                                      
REMARK 465     PHE A   603                                                      
REMARK 465     GLN A   604                                                      
REMARK 465     HIS B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     GLU B    12                                                      
REMARK 465     ALA B    28                                                      
REMARK 465     GLN B    29                                                      
REMARK 465     GLU B    30                                                      
REMARK 465     ASN B    31                                                      
REMARK 465     PHE B    32                                                      
REMARK 465     THR B    33                                                      
REMARK 465     HIS B    34                                                      
REMARK 465     PRO B    35                                                      
REMARK 465     SER B    36                                                      
REMARK 465     GLY B    37                                                      
REMARK 465     VAL B    38                                                      
REMARK 465     GLY B    39                                                      
REMARK 465     GLU B    40                                                      
REMARK 465     LYS B   441                                                      
REMARK 465     GLU B   442                                                      
REMARK 465     VAL B   443                                                      
REMARK 465     GLU B   444                                                      
REMARK 465     GLY B   467                                                      
REMARK 465     HIS B   468                                                      
REMARK 465     MET B   469                                                      
REMARK 465     SER B   475                                                      
REMARK 465     ARG B   476                                                      
REMARK 465     GLY B   477                                                      
REMARK 465     LEU B   478                                                      
REMARK 465     GLN B   479                                                      
REMARK 465     THR B   480                                                      
REMARK 465     LEU B   481                                                      
REMARK 465     PHE B   482                                                      
REMARK 465     GLN B   483                                                      
REMARK 465     SER C    29                                                      
REMARK 465     ALA C    30                                                      
REMARK 465     SER C    31                                                      
REMARK 465     GLN C   504                                                      
REMARK 465     LYS C   505                                                      
REMARK 465     ASP C   595                                                      
REMARK 465     THR C   596                                                      
REMARK 465     GLY C   597                                                      
REMARK 465     GLY C   598                                                      
REMARK 465     LEU C   599                                                      
REMARK 465     GLU C   600                                                      
REMARK 465     VAL C   601                                                      
REMARK 465     LEU C   602                                                      
REMARK 465     PHE C   603                                                      
REMARK 465     GLN C   604                                                      
REMARK 465     HIS D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     GLN D     3                                                      
REMARK 465     GLY D     4                                                      
REMARK 465     PHE D    32                                                      
REMARK 465     THR D    33                                                      
REMARK 465     HIS D    34                                                      
REMARK 465     PRO D    35                                                      
REMARK 465     SER D    36                                                      
REMARK 465     GLY D    37                                                      
REMARK 465     VAL D    38                                                      
REMARK 465     GLY D    39                                                      
REMARK 465     GLU D   442                                                      
REMARK 465     HIS D   465                                                      
REMARK 465     PRO D   466                                                      
REMARK 465     GLY D   467                                                      
REMARK 465     HIS D   468                                                      
REMARK 465     MET D   469                                                      
REMARK 465     GLY D   470                                                      
REMARK 465     SER D   475                                                      
REMARK 465     ARG D   476                                                      
REMARK 465     GLY D   477                                                      
REMARK 465     LEU D   478                                                      
REMARK 465     GLN D   479                                                      
REMARK 465     THR D   480                                                      
REMARK 465     LEU D   481                                                      
REMARK 465     PHE D   482                                                      
REMARK 465     GLN D   483                                                      
REMARK 465     ACE E   238                                                      
REMARK 465     HIS E   239                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU D  30    CG   CD   OE1  OE2                                  
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   NE2  GLN A   494     OD1  ASN A   524              2.11            
REMARK 500   O    ARG A   509     NH1  ARG A   543              2.03            
REMARK 500   OD2  ASP B   129     OH   TYR B   185              2.11            
REMARK 500   O    GLU B   208     ND2  ASN B   212              2.19            
REMARK 500   OD2  ASP C   415     O    HOH C  4040              2.12            
REMARK 500   OD1  ASP E   243     O    HOH B  4014              2.00            
REMARK 500   O    HOH D  4013     O    HOH D  4015              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OG   SER A   452     OG   SER C   452     4555     2.19            
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    LEU A 502   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    PRO A 583   C   -  N   -  CA  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    PRO A 583   C   -  N   -  CD  ANGL. DEV. = -12.6 DEGREES          
REMARK 500    PRO C 464   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    PRO C 583   C   -  N   -  CA  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    PHE D 186   CB  -  CG  -  CD1 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    PHE D 186   CB  -  CG  -  CD2 ANGL. DEV. =   4.9 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    SER A  63     -135.21     48.91                                   
REMARK 500    GLN A 102     -116.00     59.72                                   
REMARK 500    THR A 116      164.95     69.21                                   
REMARK 500    MET A 118      -74.36    -98.13                                   
REMARK 500    SER A 144     -165.17   -124.79                                   
REMARK 500    ASP A 148      172.01     66.10                                   
REMARK 500    SER A 399      -53.44   -135.12                                   
REMARK 500    LYS A 505      109.10    -58.72                                   
REMARK 500    LEU A 593      -78.98    -53.57                                   
REMARK 500    ARG B  77      150.08     71.01                                   
REMARK 500    VAL B 161      -68.71   -135.00                                   
REMARK 500    ASN B 218     -157.62   -157.10                                   
REMARK 500    ILE B 219      -71.95   -100.54                                   
REMARK 500    ASP B 244       71.45   -105.63                                   
REMARK 500    CYS B 377      -84.50    -76.64                                   
REMARK 500    HIS B 451       88.91    -69.38                                   
REMARK 500    CYS B 459     -110.39     59.39                                   
REMARK 500    SER C  63     -130.76     50.76                                   
REMARK 500    GLN C 102     -115.51     59.20                                   
REMARK 500    MET C 118      -69.73    -98.98                                   
REMARK 500    SER C 144     -165.24   -124.09                                   
REMARK 500    ASP C 148      172.30     65.48                                   
REMARK 500    SER C 399      -54.30   -129.81                                   
REMARK 500    LYS C 459       85.01     40.78                                   
REMARK 500    THR C 460      -64.41    -92.97                                   
REMARK 500    PHE C 581      -17.87     71.40                                   
REMARK 500    ALA D   7     -167.39    -74.00                                   
REMARK 500    LEU D   8        5.83     51.67                                   
REMARK 500    ARG D  77      104.93     67.84                                   
REMARK 500    VAL D 161      -69.06   -135.11                                   
REMARK 500    ASN D 218     -157.81   -157.37                                   
REMARK 500    ILE D 219      -73.90   -100.98                                   
REMARK 500    ASP D 244       71.35   -105.37                                   
REMARK 500    ILE D 376       79.56   -102.77                                   
REMARK 500    ASN D 378     -118.45     48.05                                   
REMARK 500    CYS D 450       67.15   -111.63                                   
REMARK 500    HIS D 451       82.20     50.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     ACE F  238                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 243   OD1                                                    
REMARK 620 2 GLU B 223   OE2 107.5                                              
REMARK 620 3 HOH B4013   O   153.6  93.7                                        
REMARK 620 4 HOH B4014   O    56.4 145.6  97.3                                  
REMARK 620 5 HOH B4027   O    95.6  69.3  76.9  81.6                            
REMARK 620 6 SER B 125   OG  107.5 119.7  73.5  94.7 149.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER D 125   OG                                                     
REMARK 620 2 GLU D 223   OE2 122.4                                              
REMARK 620 3 ASP F 243   OD1 104.5  68.0                                        
REMARK 620 4 HOH D4004   O    80.9 106.5 173.7                                  
REMARK 620 5 HOH D4005   O    97.4 129.0  72.4 110.4                            
REMARK 620 6 HOH D4011   O   162.4  75.3  81.5  94.2  68.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 234   OD1                                                    
REMARK 620 2 HOH A4030   O    68.3                                              
REMARK 620 3 ILE A 236   O    95.5 100.1                                        
REMARK 620 4 ASN A 232   OD1  85.5  91.9 167.4                                  
REMARK 620 5 ASP A 238   OD1 142.4  74.2  88.6  98.2                            
REMARK 620 6 ASP A 238   OD2 158.1 120.6 101.9  74.6  52.2                      
REMARK 620 7 ASP A 230   OD1  85.1 153.0  86.4  81.2 132.5  82.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 421   OD1                                                    
REMARK 620 2 ASP C 421   OD2  44.6                                              
REMARK 620 3 HOH C4040   O    67.0  95.5                                        
REMARK 620 4 ASN C 417   OD1 158.8 128.3 131.7                                  
REMARK 620 5 TYR C 419   O    93.4  81.5 152.7  65.5                            
REMARK 620 6 ASP C 415   OD1 100.1  63.8  94.4  89.3 108.2                      
REMARK 620 7 ASP C 415   OD2  99.9  95.0  49.8 100.8 157.2  51.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 288   OD1                                                    
REMARK 620 2 TYR A 290   O   108.3                                              
REMARK 620 3 HOH A4045   O    88.1 107.7                                        
REMARK 620 4 ASP A 292   OD1 161.8  77.9  73.7                                  
REMARK 620 5 ASP A 292   OD2 137.6  99.6 113.3  54.2                            
REMARK 620 6 ASP A 284   OD1  63.5  81.7 151.5 134.6  90.7                      
REMARK 620 7 ASN A 286   OD1  63.7 156.0  95.0 117.1  77.8  74.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 218   OD1                                                    
REMARK 620 2 ASP B 220   O    81.1                                              
REMARK 620 3 GLU B 162   OE2 107.7 159.7                                        
REMARK 620 4 ASP B 220   OD1  80.6  70.0  93.1                                  
REMARK 620 5 PRO B 222   O   160.4  89.8  86.6 112.7                            
REMARK 620 6 GLU B 223   OE1  84.9  98.0 100.9 162.3  79.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 357   OD1                                                    
REMARK 620 2 ASP C 357   OD2  53.6                                              
REMARK 620 3 ASP C 353   OD1 145.5 144.5                                        
REMARK 620 4 ASP C 349   OD1 140.5  96.0  73.9                                  
REMARK 620 5 ASP C 351   OD1  97.3  62.7  82.5  87.1                            
REMARK 620 6 PHE C 355   O    88.7 110.4 101.0  78.7 163.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER D 127   O                                                      
REMARK 620 2 ASP D 130   OD1  98.7                                              
REMARK 620 3 LYS D 338   O   148.9  83.5                                        
REMARK 620 4 HOH D4006   O    91.1 113.0  60.2                                  
REMARK 620 5 ASP D 130   OD2 130.5  54.4  75.7 135.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 349   OD1                                                    
REMARK 620 2 PHE A 355   O    79.3                                              
REMARK 620 3 ASP A 357   OD1 139.0  84.3                                        
REMARK 620 4 ASP A 357   OD2  95.8 106.8  53.6                                  
REMARK 620 5 HOH A4064   O   138.7  84.1  75.3 125.2                            
REMARK 620 6 ASP A 353   OD1  74.4  97.6 145.5 151.7  70.7                      
REMARK 620 7 ASP A 351   OD1  89.7 168.5 102.1  70.7 106.6  82.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 127   O                                                      
REMARK 620 2 ASP B 130   OD1  96.4                                              
REMARK 620 3 ASP B 130   OD2 141.0  44.6                                        
REMARK 620 4 HOH B4016   O    99.8 159.7 117.9                                  
REMARK 620 5 ASP B 131   OD1 106.4  91.4  78.1  72.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 230   OD1                                                    
REMARK 620 2 ASN C 232   OD1  75.0                                              
REMARK 620 3 ASP C 238   OD2  81.9  73.4                                        
REMARK 620 4 ASP C 238   OD1 133.0 102.5  53.7                                  
REMARK 620 5 ASP C 234   OD1  82.5  82.4 153.9 144.5                            
REMARK 620 6 ILE C 236   O    85.9 160.6 100.8  87.8  98.8                      
REMARK 620 7 HOH C4019   O   155.8  90.9 113.3  68.7  76.1 108.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 223   OE1                                                    
REMARK 620 2 GLU D 162   OE2 101.2                                              
REMARK 620 3 ASP D 220   OD1 157.7  99.7                                        
REMARK 620 4 PRO D 222   O    80.0  87.6 108.8                                  
REMARK 620 5 ASN D 218   OD1  82.9 112.3  82.0 156.0                            
REMARK 620 6 ASP D 220   O    92.6 164.0  68.0  87.0  77.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 413   OD1                                                    
REMARK 620 2 ASP A 415   OD1  73.9                                              
REMARK 620 3 ASN A 417   OD1  73.9  87.6                                        
REMARK 620 4 TYR A 419   O    69.9 143.5  78.3                                  
REMARK 620 5 ASP A 421   OD2  93.8  88.1 167.7  98.6                            
REMARK 620 6 HOH A4071   O   140.2  72.0  84.7 138.3 104.9                      
REMARK 620 7 ASP A 421   OD1 144.9 112.0 138.9 100.4  53.2  69.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C 286   OD1                                                    
REMARK 620 2 ASP C 292   OD1 117.9                                              
REMARK 620 3 ASP C 292   OD2  78.7  53.8                                        
REMARK 620 4 HOH C4027   O    98.1  70.0 110.9                                  
REMARK 620 5 ASP C 284   OD1  77.6 131.7  90.3 157.4                            
REMARK 620 6 ASP C 288   OD1  63.4 167.5 135.5  97.5  60.6                      
REMARK 620 7 TYR C 290   O   153.4  78.0  97.5 107.7  76.1 106.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN C3461                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG D2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA D2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA D2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1595                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1595                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1596                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1596                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1597                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG A3044  THROUGH NAG A3045  BOUND TO ASN A  44           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG A3260  THROUGH MAN A3263  BOUND TO ASN A 260           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG A3266  THROUGH MAN A3271  BOUND TO ASN A 266           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG A3458  THROUGH NAG A3459  BOUND TO ASN A 458           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG A3524  THROUGH NAG A3525  BOUND TO ASN A 524           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG A3585  THROUGH NAG A3586  BOUND TO ASN A 585           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG B3080  BOUND TO ASN B  80                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG B3243  BOUND TO ASN B 243                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG B3370  BOUND TO ASN B 370                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG C3044  BOUND TO ASN C  44                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG C3260  THROUGH NAG C3261  BOUND TO ASN C 260           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG C3266  THROUGH MAN C3271  BOUND TO ASN C 266           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG C3458  THROUGH BMA C3460  BOUND TO ASN C 458           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG C3524  BOUND TO ASN C 524                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG C3585  THROUGH NAG C3586  BOUND TO ASN C 585           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG D3031  BOUND TO ASN D  31                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG D3080  BOUND TO ASN D  80                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG D3243  BOUND TO ASN D 243                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UM8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ALPHA V BETA 6                                 
DBREF  4UM9 A    1   595  UNP    P06756   ITAV_HUMAN      31    625             
DBREF  4UM9 B    1   474  UNP    P18564   ITB6_HUMAN      18    491             
DBREF  4UM9 C    1   595  UNP    P06756   ITAV_HUMAN      31    625             
DBREF  4UM9 D    1   474  UNP    P18564   ITB6_HUMAN      18    491             
DBREF  4UM9 E  239   249  UNP    Q6TV15   Q6TV15_HUMAN     7     17             
DBREF  4UM9 F  239   249  UNP    Q6TV15   Q6TV15_HUMAN     7     17             
SEQADV 4UM9 THR A  596  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 GLY A  597  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 GLY A  598  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 LEU A  599  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 GLU A  600  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 VAL A  601  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 LEU A  602  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 PHE A  603  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 GLN A  604  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 CYS A  400  UNP  P06756    MET   430 ENGINEERED MUTATION            
SEQADV 4UM9 SER B  475  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 ARG B  476  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 GLY B  477  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 LEU B  478  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 GLN B  479  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 THR B  480  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 LEU B  481  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 PHE B  482  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 GLN B  483  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 CYS B  270  UNP  P18564    ILE   287 CONFLICT                       
SEQADV 4UM9 ASN B  452  UNP  P18564    HIS   469 CONFLICT                       
SEQADV 4UM9 THR C  596  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 GLY C  597  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 GLY C  598  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 LEU C  599  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 GLU C  600  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 VAL C  601  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 LEU C  602  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 PHE C  603  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 GLN C  604  UNP  P06756              EXPRESSION TAG                 
SEQADV 4UM9 CYS C  400  UNP  P06756    MET   430 ENGINEERED MUTATION            
SEQADV 4UM9 SER D  475  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 ARG D  476  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 GLY D  477  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 LEU D  478  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 GLN D  479  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 THR D  480  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 LEU D  481  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 PHE D  482  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 GLN D  483  UNP  P18564              EXPRESSION TAG                 
SEQADV 4UM9 THR D   29  UNP  P18564    GLN    46 CONFLICT                       
SEQADV 4UM9 CYS D  270  UNP  P18564    ILE   287 CONFLICT                       
SEQADV 4UM9 ASN D  452  UNP  P18564    HIS   469 CONFLICT                       
SEQADV 4UM9 ACE E  238  UNP  Q6TV15              EXPRESSION TAG                 
SEQADV 4UM9 ACE F  238  UNP  Q6TV15              EXPRESSION TAG                 
SEQRES   1 A  604  PHE ASN LEU ASP VAL ASP SER PRO ALA GLU TYR SER GLY          
SEQRES   2 A  604  PRO GLU GLY SER TYR PHE GLY PHE ALA VAL ASP PHE PHE          
SEQRES   3 A  604  VAL PRO SER ALA SER SER ARG MET PHE LEU LEU VAL GLY          
SEQRES   4 A  604  ALA PRO LYS ALA ASN THR THR GLN PRO GLY ILE VAL GLU          
SEQRES   5 A  604  GLY GLY GLN VAL LEU LYS CYS ASP TRP SER SER THR ARG          
SEQRES   6 A  604  ARG CYS GLN PRO ILE GLU PHE ASP ALA THR GLY ASN ARG          
SEQRES   7 A  604  ASP TYR ALA LYS ASP ASP PRO LEU GLU PHE LYS SER HIS          
SEQRES   8 A  604  GLN TRP PHE GLY ALA SER VAL ARG SER LYS GLN ASP LYS          
SEQRES   9 A  604  ILE LEU ALA CYS ALA PRO LEU TYR HIS TRP ARG THR GLU          
SEQRES  10 A  604  MET LYS GLN GLU ARG GLU PRO VAL GLY THR CYS PHE LEU          
SEQRES  11 A  604  GLN ASP GLY THR LYS THR VAL GLU TYR ALA PRO CYS ARG          
SEQRES  12 A  604  SER GLN ASP ILE ASP ALA ASP GLY GLN GLY PHE CYS GLN          
SEQRES  13 A  604  GLY GLY PHE SER ILE ASP PHE THR LYS ALA ASP ARG VAL          
SEQRES  14 A  604  LEU LEU GLY GLY PRO GLY SER PHE TYR TRP GLN GLY GLN          
SEQRES  15 A  604  LEU ILE SER ASP GLN VAL ALA GLU ILE VAL SER LYS TYR          
SEQRES  16 A  604  ASP PRO ASN VAL TYR SER ILE LYS TYR ASN ASN GLN LEU          
SEQRES  17 A  604  ALA THR ARG THR ALA GLN ALA ILE PHE ASP ASP SER TYR          
SEQRES  18 A  604  LEU GLY TYR SER VAL ALA VAL GLY ASP PHE ASN GLY ASP          
SEQRES  19 A  604  GLY ILE ASP ASP PHE VAL SER GLY VAL PRO ARG ALA ALA          
SEQRES  20 A  604  ARG THR LEU GLY MET VAL TYR ILE TYR ASP GLY LYS ASN          
SEQRES  21 A  604  MET SER SER LEU TYR ASN PHE THR GLY GLU GLN MET ALA          
SEQRES  22 A  604  ALA TYR PHE GLY PHE SER VAL ALA ALA THR ASP ILE ASN          
SEQRES  23 A  604  GLY ASP ASP TYR ALA ASP VAL PHE ILE GLY ALA PRO LEU          
SEQRES  24 A  604  PHE MET ASP ARG GLY SER ASP GLY LYS LEU GLN GLU VAL          
SEQRES  25 A  604  GLY GLN VAL SER VAL SER LEU GLN ARG ALA SER GLY ASP          
SEQRES  26 A  604  PHE GLN THR THR LYS LEU ASN GLY PHE GLU VAL PHE ALA          
SEQRES  27 A  604  ARG PHE GLY SER ALA ILE ALA PRO LEU GLY ASP LEU ASP          
SEQRES  28 A  604  GLN ASP GLY PHE ASN ASP ILE ALA ILE ALA ALA PRO TYR          
SEQRES  29 A  604  GLY GLY GLU ASP LYS LYS GLY ILE VAL TYR ILE PHE ASN          
SEQRES  30 A  604  GLY ARG SER THR GLY LEU ASN ALA VAL PRO SER GLN ILE          
SEQRES  31 A  604  LEU GLU GLY GLN TRP ALA ALA ARG SER CYS PRO PRO SER          
SEQRES  32 A  604  PHE GLY TYR SER MET LYS GLY ALA THR ASP ILE ASP LYS          
SEQRES  33 A  604  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA PHE GLY VAL          
SEQRES  34 A  604  ASP ARG ALA ILE LEU TYR ARG ALA ARG PRO VAL ILE THR          
SEQRES  35 A  604  VAL ASN ALA GLY LEU GLU VAL TYR PRO SER ILE LEU ASN          
SEQRES  36 A  604  GLN ASP ASN LYS THR CYS SER LEU PRO GLY THR ALA LEU          
SEQRES  37 A  604  LYS VAL SER CYS PHE ASN VAL ARG PHE CYS LEU LYS ALA          
SEQRES  38 A  604  ASP GLY LYS GLY VAL LEU PRO ARG LYS LEU ASN PHE GLN          
SEQRES  39 A  604  VAL GLU LEU LEU LEU ASP LYS LEU LYS GLN LYS GLY ALA          
SEQRES  40 A  604  ILE ARG ARG ALA LEU PHE LEU TYR SER ARG SER PRO SER          
SEQRES  41 A  604  HIS SER LYS ASN MET THR ILE SER ARG GLY GLY LEU MET          
SEQRES  42 A  604  GLN CYS GLU GLU LEU ILE ALA TYR LEU ARG ASP GLU SER          
SEQRES  43 A  604  GLU PHE ARG ASP LYS LEU THR PRO ILE THR ILE PHE MET          
SEQRES  44 A  604  GLU TYR ARG LEU ASP TYR ARG THR ALA ALA ASP THR THR          
SEQRES  45 A  604  GLY LEU GLN PRO ILE LEU ASN GLN PHE THR PRO ALA ASN          
SEQRES  46 A  604  ILE SER ARG GLN ALA HIS ILE LEU LEU ASP THR GLY GLY          
SEQRES  47 A  604  LEU GLU VAL LEU PHE GLN                                      
SEQRES   1 C  604  PHE ASN LEU ASP VAL ASP SER PRO ALA GLU TYR SER GLY          
SEQRES   2 C  604  PRO GLU GLY SER TYR PHE GLY PHE ALA VAL ASP PHE PHE          
SEQRES   3 C  604  VAL PRO SER ALA SER SER ARG MET PHE LEU LEU VAL GLY          
SEQRES   4 C  604  ALA PRO LYS ALA ASN THR THR GLN PRO GLY ILE VAL GLU          
SEQRES   5 C  604  GLY GLY GLN VAL LEU LYS CYS ASP TRP SER SER THR ARG          
SEQRES   6 C  604  ARG CYS GLN PRO ILE GLU PHE ASP ALA THR GLY ASN ARG          
SEQRES   7 C  604  ASP TYR ALA LYS ASP ASP PRO LEU GLU PHE LYS SER HIS          
SEQRES   8 C  604  GLN TRP PHE GLY ALA SER VAL ARG SER LYS GLN ASP LYS          
SEQRES   9 C  604  ILE LEU ALA CYS ALA PRO LEU TYR HIS TRP ARG THR GLU          
SEQRES  10 C  604  MET LYS GLN GLU ARG GLU PRO VAL GLY THR CYS PHE LEU          
SEQRES  11 C  604  GLN ASP GLY THR LYS THR VAL GLU TYR ALA PRO CYS ARG          
SEQRES  12 C  604  SER GLN ASP ILE ASP ALA ASP GLY GLN GLY PHE CYS GLN          
SEQRES  13 C  604  GLY GLY PHE SER ILE ASP PHE THR LYS ALA ASP ARG VAL          
SEQRES  14 C  604  LEU LEU GLY GLY PRO GLY SER PHE TYR TRP GLN GLY GLN          
SEQRES  15 C  604  LEU ILE SER ASP GLN VAL ALA GLU ILE VAL SER LYS TYR          
SEQRES  16 C  604  ASP PRO ASN VAL TYR SER ILE LYS TYR ASN ASN GLN LEU          
SEQRES  17 C  604  ALA THR ARG THR ALA GLN ALA ILE PHE ASP ASP SER TYR          
SEQRES  18 C  604  LEU GLY TYR SER VAL ALA VAL GLY ASP PHE ASN GLY ASP          
SEQRES  19 C  604  GLY ILE ASP ASP PHE VAL SER GLY VAL PRO ARG ALA ALA          
SEQRES  20 C  604  ARG THR LEU GLY MET VAL TYR ILE TYR ASP GLY LYS ASN          
SEQRES  21 C  604  MET SER SER LEU TYR ASN PHE THR GLY GLU GLN MET ALA          
SEQRES  22 C  604  ALA TYR PHE GLY PHE SER VAL ALA ALA THR ASP ILE ASN          
SEQRES  23 C  604  GLY ASP ASP TYR ALA ASP VAL PHE ILE GLY ALA PRO LEU          
SEQRES  24 C  604  PHE MET ASP ARG GLY SER ASP GLY LYS LEU GLN GLU VAL          
SEQRES  25 C  604  GLY GLN VAL SER VAL SER LEU GLN ARG ALA SER GLY ASP          
SEQRES  26 C  604  PHE GLN THR THR LYS LEU ASN GLY PHE GLU VAL PHE ALA          
SEQRES  27 C  604  ARG PHE GLY SER ALA ILE ALA PRO LEU GLY ASP LEU ASP          
SEQRES  28 C  604  GLN ASP GLY PHE ASN ASP ILE ALA ILE ALA ALA PRO TYR          
SEQRES  29 C  604  GLY GLY GLU ASP LYS LYS GLY ILE VAL TYR ILE PHE ASN          
SEQRES  30 C  604  GLY ARG SER THR GLY LEU ASN ALA VAL PRO SER GLN ILE          
SEQRES  31 C  604  LEU GLU GLY GLN TRP ALA ALA ARG SER CYS PRO PRO SER          
SEQRES  32 C  604  PHE GLY TYR SER MET LYS GLY ALA THR ASP ILE ASP LYS          
SEQRES  33 C  604  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA PHE GLY VAL          
SEQRES  34 C  604  ASP ARG ALA ILE LEU TYR ARG ALA ARG PRO VAL ILE THR          
SEQRES  35 C  604  VAL ASN ALA GLY LEU GLU VAL TYR PRO SER ILE LEU ASN          
SEQRES  36 C  604  GLN ASP ASN LYS THR CYS SER LEU PRO GLY THR ALA LEU          
SEQRES  37 C  604  LYS VAL SER CYS PHE ASN VAL ARG PHE CYS LEU LYS ALA          
SEQRES  38 C  604  ASP GLY LYS GLY VAL LEU PRO ARG LYS LEU ASN PHE GLN          
SEQRES  39 C  604  VAL GLU LEU LEU LEU ASP LYS LEU LYS GLN LYS GLY ALA          
SEQRES  40 C  604  ILE ARG ARG ALA LEU PHE LEU TYR SER ARG SER PRO SER          
SEQRES  41 C  604  HIS SER LYS ASN MET THR ILE SER ARG GLY GLY LEU MET          
SEQRES  42 C  604  GLN CYS GLU GLU LEU ILE ALA TYR LEU ARG ASP GLU SER          
SEQRES  43 C  604  GLU PHE ARG ASP LYS LEU THR PRO ILE THR ILE PHE MET          
SEQRES  44 C  604  GLU TYR ARG LEU ASP TYR ARG THR ALA ALA ASP THR THR          
SEQRES  45 C  604  GLY LEU GLN PRO ILE LEU ASN GLN PHE THR PRO ALA ASN          
SEQRES  46 C  604  ILE SER ARG GLN ALA HIS ILE LEU LEU ASP THR GLY GLY          
SEQRES  47 C  604  LEU GLU VAL LEU PHE GLN                                      
SEQRES   1 B  483  HIS VAL GLN GLY GLY CYS ALA LEU GLY GLY ALA GLU THR          
SEQRES   2 B  483  CYS GLU ASP CYS LEU LEU ILE GLY PRO GLN CYS ALA TRP          
SEQRES   3 B  483  CYS ALA GLN GLU ASN PHE THR HIS PRO SER GLY VAL GLY          
SEQRES   4 B  483  GLU ARG CYS ASP THR PRO ALA ASN LEU LEU ALA LYS GLY          
SEQRES   5 B  483  CYS GLN LEU ASN PHE ILE GLU ASN PRO VAL SER GLN VAL          
SEQRES   6 B  483  GLU ILE LEU LYS ASN LYS PRO LEU SER VAL GLY ARG GLN          
SEQRES   7 B  483  LYS ASN SER SER ASP ILE VAL GLN ILE ALA PRO GLN SER          
SEQRES   8 B  483  LEU ILE LEU LYS LEU ARG PRO GLY GLY ALA GLN THR LEU          
SEQRES   9 B  483  GLN VAL HIS VAL ARG GLN THR GLU ASP TYR PRO VAL ASP          
SEQRES  10 B  483  LEU TYR TYR LEU MET ASP LEU SER ALA SER MET ASP ASP          
SEQRES  11 B  483  ASP LEU ASN THR ILE LYS GLU LEU GLY SER ARG LEU SER          
SEQRES  12 B  483  LYS GLU MET SER LYS LEU THR SER ASN PHE ARG LEU GLY          
SEQRES  13 B  483  PHE GLY SER PHE VAL GLU LYS PRO VAL SER PRO PHE VAL          
SEQRES  14 B  483  LYS THR THR PRO GLU GLU ILE ALA ASN PRO CYS SER SER          
SEQRES  15 B  483  ILE PRO TYR PHE CYS LEU PRO THR PHE GLY PHE LYS HIS          
SEQRES  16 B  483  ILE LEU PRO LEU THR ASN ASP ALA GLU ARG PHE ASN GLU          
SEQRES  17 B  483  ILE VAL LYS ASN GLN LYS ILE SER ALA ASN ILE ASP THR          
SEQRES  18 B  483  PRO GLU GLY GLY PHE ASP ALA ILE MET GLN ALA ALA VAL          
SEQRES  19 B  483  CYS LYS GLU LYS ILE GLY TRP ARG ASN ASP SER LEU HIS          
SEQRES  20 B  483  LEU LEU VAL PHE VAL SER ASP ALA ASP SER HIS PHE GLY          
SEQRES  21 B  483  MET ASP SER LYS LEU ALA GLY ILE VAL CYS PRO ASN ASP          
SEQRES  22 B  483  GLY LEU CYS HIS LEU ASP SER LYS ASN GLU TYR SER MET          
SEQRES  23 B  483  SER THR VAL LEU GLU TYR PRO THR ILE GLY GLN LEU ILE          
SEQRES  24 B  483  ASP LYS LEU VAL GLN ASN ASN VAL LEU LEU ILE PHE ALA          
SEQRES  25 B  483  VAL THR GLN GLU GLN VAL HIS LEU TYR GLU ASN TYR ALA          
SEQRES  26 B  483  LYS LEU ILE PRO GLY ALA THR VAL GLY LEU LEU GLN LYS          
SEQRES  27 B  483  ASP SER GLY ASN ILE LEU GLN LEU ILE ILE SER ALA TYR          
SEQRES  28 B  483  GLU GLU LEU ARG SER GLU VAL GLU LEU GLU VAL LEU GLY          
SEQRES  29 B  483  ASP THR GLU GLY LEU ASN LEU SER PHE THR ALA ILE CYS          
SEQRES  30 B  483  ASN ASN GLY THR LEU PHE GLN HIS GLN LYS LYS CYS SER          
SEQRES  31 B  483  HIS MET LYS VAL GLY ASP THR ALA SER PHE SER VAL THR          
SEQRES  32 B  483  VAL ASN ILE PRO HIS CYS GLU ARG ARG SER ARG HIS ILE          
SEQRES  33 B  483  ILE ILE LYS PRO VAL GLY LEU GLY ASP ALA LEU GLU LEU          
SEQRES  34 B  483  LEU VAL SER PRO GLU CYS ASN CYS ASP CYS GLN LYS GLU          
SEQRES  35 B  483  VAL GLU VAL ASN SER SER LYS CYS HIS ASN GLY ASN GLY          
SEQRES  36 B  483  SER PHE GLN CYS GLY VAL CYS ALA CYS HIS PRO GLY HIS          
SEQRES  37 B  483  MET GLY PRO ARG CYS GLU SER ARG GLY LEU GLN THR LEU          
SEQRES  38 B  483  PHE GLN                                                      
SEQRES   1 D  483  HIS VAL GLN GLY GLY CYS ALA LEU GLY GLY ALA GLU THR          
SEQRES   2 D  483  CYS GLU ASP CYS LEU LEU ILE GLY PRO GLN CYS ALA TRP          
SEQRES   3 D  483  CYS ALA THR GLU ASN PHE THR HIS PRO SER GLY VAL GLY          
SEQRES   4 D  483  GLU ARG CYS ASP THR PRO ALA ASN LEU LEU ALA LYS GLY          
SEQRES   5 D  483  CYS GLN LEU ASN PHE ILE GLU ASN PRO VAL SER GLN VAL          
SEQRES   6 D  483  GLU ILE LEU LYS ASN LYS PRO LEU SER VAL GLY ARG GLN          
SEQRES   7 D  483  LYS ASN SER SER ASP ILE VAL GLN ILE ALA PRO GLN SER          
SEQRES   8 D  483  LEU ILE LEU LYS LEU ARG PRO GLY GLY ALA GLN THR LEU          
SEQRES   9 D  483  GLN VAL HIS VAL ARG GLN THR GLU ASP TYR PRO VAL ASP          
SEQRES  10 D  483  LEU TYR TYR LEU MET ASP LEU SER ALA SER MET ASP ASP          
SEQRES  11 D  483  ASP LEU ASN THR ILE LYS GLU LEU GLY SER ARG LEU SER          
SEQRES  12 D  483  LYS GLU MET SER LYS LEU THR SER ASN PHE ARG LEU GLY          
SEQRES  13 D  483  PHE GLY SER PHE VAL GLU LYS PRO VAL SER PRO PHE VAL          
SEQRES  14 D  483  LYS THR THR PRO GLU GLU ILE ALA ASN PRO CYS SER SER          
SEQRES  15 D  483  ILE PRO TYR PHE CYS LEU PRO THR PHE GLY PHE LYS HIS          
SEQRES  16 D  483  ILE LEU PRO LEU THR ASN ASP ALA GLU ARG PHE ASN GLU          
SEQRES  17 D  483  ILE VAL LYS ASN GLN LYS ILE SER ALA ASN ILE ASP THR          
SEQRES  18 D  483  PRO GLU GLY GLY PHE ASP ALA ILE MET GLN ALA ALA VAL          
SEQRES  19 D  483  CYS LYS GLU LYS ILE GLY TRP ARG ASN ASP SER LEU HIS          
SEQRES  20 D  483  LEU LEU VAL PHE VAL SER ASP ALA ASP SER HIS PHE GLY          
SEQRES  21 D  483  MET ASP SER LYS LEU ALA GLY ILE VAL CYS PRO ASN ASP          
SEQRES  22 D  483  GLY LEU CYS HIS LEU ASP SER LYS ASN GLU TYR SER MET          
SEQRES  23 D  483  SER THR VAL LEU GLU TYR PRO THR ILE GLY GLN LEU ILE          
SEQRES  24 D  483  ASP LYS LEU VAL GLN ASN ASN VAL LEU LEU ILE PHE ALA          
SEQRES  25 D  483  VAL THR GLN GLU GLN VAL HIS LEU TYR GLU ASN TYR ALA          
SEQRES  26 D  483  LYS LEU ILE PRO GLY ALA THR VAL GLY LEU LEU GLN LYS          
SEQRES  27 D  483  ASP SER GLY ASN ILE LEU GLN LEU ILE ILE SER ALA TYR          
SEQRES  28 D  483  GLU GLU LEU ARG SER GLU VAL GLU LEU GLU VAL LEU GLY          
SEQRES  29 D  483  ASP THR GLU GLY LEU ASN LEU SER PHE THR ALA ILE CYS          
SEQRES  30 D  483  ASN ASN GLY THR LEU PHE GLN HIS GLN LYS LYS CYS SER          
SEQRES  31 D  483  HIS MET LYS VAL GLY ASP THR ALA SER PHE SER VAL THR          
SEQRES  32 D  483  VAL ASN ILE PRO HIS CYS GLU ARG ARG SER ARG HIS ILE          
SEQRES  33 D  483  ILE ILE LYS PRO VAL GLY LEU GLY ASP ALA LEU GLU LEU          
SEQRES  34 D  483  LEU VAL SER PRO GLU CYS ASN CYS ASP CYS GLN LYS GLU          
SEQRES  35 D  483  VAL GLU VAL ASN SER SER LYS CYS HIS ASN GLY ASN GLY          
SEQRES  36 D  483  SER PHE GLN CYS GLY VAL CYS ALA CYS HIS PRO GLY HIS          
SEQRES  37 D  483  MET GLY PRO ARG CYS GLU SER ARG GLY LEU GLN THR LEU          
SEQRES  38 D  483  PHE GLN                                                      
SEQRES   1 E   13  ACE HIS GLY ARG GLY ASP LEU GLY ARG LEU LYS LYS NHH          
SEQRES   1 F   13  ACE HIS GLY ARG GLY ASP LEU GLY ARG LEU LYS LYS NHH          
HET     CA  A2001       1                                                       
HET     CA  A2002       1                                                       
HET     CA  A2003       1                                                       
HET     CA  A2004       1                                                       
HET    NAG  A3044      14                                                       
HET    NAG  A3045      14                                                       
HET    NAG  A3260      14                                                       
HET    NAG  A3261      14                                                       
HET    BMA  A3262      11                                                       
HET    MAN  A3263      11                                                       
HET    NAG  A3266      14                                                       
HET    NAG  A3267      14                                                       
HET    BMA  A3268      11                                                       
HET    MAN  A3269      11                                                       
HET    MAN  A3270      11                                                       
HET    MAN  A3271      11                                                       
HET    NAG  A3458      14                                                       
HET    NAG  A3459      14                                                       
HET    NAG  A3524      14                                                       
HET    NAG  A3525      14                                                       
HET    NAG  A3585      14                                                       
HET    NAG  A3586      14                                                       
HET     MG  B2001       1                                                       
HET     CA  B2002       1                                                       
HET     CA  B2003       1                                                       
HET    NAG  B3080      14                                                       
HET    NAG  B3243      14                                                       
HET    NAG  B3370      14                                                       
HET     CA  C2001       1                                                       
HET     CA  C2002       1                                                       
HET     CA  C2003       1                                                       
HET     CA  C2004       1                                                       
HET    NAG  C3044      14                                                       
HET    NAG  C3260      14                                                       
HET    NAG  C3261      14                                                       
HET    NAG  C3266      14                                                       
HET    NAG  C3267      14                                                       
HET    BMA  C3268      11                                                       
HET    MAN  C3269      11                                                       
HET    MAN  C3270      11                                                       
HET    MAN  C3271      11                                                       
HET    NAG  C3458      14                                                       
HET    NAG  C3459      14                                                       
HET    BMA  C3460      11                                                       
HET    MAN  C3461      11                                                       
HET    NAG  C3524      14                                                       
HET    NAG  C3585      14                                                       
HET    NAG  C3586      14                                                       
HET     MG  D2001       1                                                       
HET     CA  D2002       1                                                       
HET     CA  D2003       1                                                       
HET    NAG  D3031      14                                                       
HET    NAG  D3080      14                                                       
HET    NAG  D3243      14                                                       
HET    NHH  E 250       1                                                       
HET    ACE  F 238       2                                                       
HET    NHH  F 250       1                                                       
HET    SO4  A1595       5                                                       
HET    SO4  C1595       5                                                       
HET    SO4  C1596       5                                                       
HET    SO4  B1475       5                                                       
HET    SO4  A1596       5                                                       
HET    SO4  A1597       5                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     SO4 SULFATE ION                                                      
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     NHH N'-{4-[2-(DIAMINOMETHYLIDENE)HYDRAZONO]                          
HETNAM   2 NHH  CYCLOHEXYLIDEN}AMINOMETHANEHYDRAZONAMIDE                        
HETNAM      CA CALCIUM ION                                                      
HETNAM     ACE ACETYL GROUP                                                     
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  NAG    28(C8 H15 N O6)                                              
FORMUL   6  SO4    6(O4 S 2-)                                                   
FORMUL   7  MAN    8(C6 H12 O6)                                                 
FORMUL   8  BMA    4(C6 H12 O6)                                                 
FORMUL   9  NHH    2(C8 H16 N8)                                                 
FORMUL  10   CA    12(CA 2+)                                                    
FORMUL  11  ACE    C2 H4 O                                                      
FORMUL  12  HOH   *230(H2 O)                                                    
HELIX    1   1 GLY A  175  GLN A  180  1                                   6    
HELIX    2   2 VAL A  188  LYS A  194  1                                   7    
HELIX    3   3 GLN A  214  ASP A  218  5                                   5    
HELIX    4   4 ARG A  245  LEU A  250  1                                   6    
HELIX    5   5 GLY A  366  LYS A  370  5                                   5    
HELIX    6   6 ASP A  544  PHE A  548  5                                   5    
HELIX    7   7 THR B   13  LEU B   18  1                                   6    
HELIX    8   8 THR B   44  GLY B   52  1                                   9    
HELIX    9   9 ASN B   80  ILE B   84  5                                   5    
HELIX   10  10 SER B  125  SER B  127  5                                   3    
HELIX   11  11 MET B  128  ILE B  135  1                                   8    
HELIX   12  12 GLU B  137  THR B  150  1                                  14    
HELIX   13  13 THR B  172  ASN B  178  1                                   7    
HELIX   14  14 ASP B  202  ASN B  212  1                                  11    
HELIX   15  15 GLY B  224  CYS B  235  1                                  12    
HELIX   16  16 CYS B  235  GLY B  240  1                                   6    
HELIX   17  17 PHE B  259  GLY B  267  5                                   9    
HELIX   18  18 THR B  294  ASN B  305  1                                  12    
HELIX   19  19 THR B  314  LYS B  326  1                                  13    
HELIX   20  20 ASN B  342  ARG B  355  1                                  14    
HELIX   21  21 GLY C  175  GLN C  180  1                                   6    
HELIX   22  22 VAL C  188  LYS C  194  1                                   7    
HELIX   23  23 GLN C  214  ASP C  218  5                                   5    
HELIX   24  24 ARG C  245  LEU C  250  1                                   6    
HELIX   25  25 GLY C  366  LYS C  370  5                                   5    
HELIX   26  26 PHE C  427  VAL C  429  5                                   3    
HELIX   27  27 ASP C  544  PHE C  548  5                                   5    
HELIX   28  28 ASP C  564  ALA C  569  1                                   6    
HELIX   29  29 THR D   13  ILE D   20  1                                   8    
HELIX   30  30 THR D   44  GLY D   52  1                                   9    
HELIX   31  31 ASN D   80  ILE D   84  5                                   5    
HELIX   32  32 SER D  125  SER D  127  5                                   3    
HELIX   33  33 MET D  128  LYS D  136  1                                   9    
HELIX   34  34 GLU D  137  THR D  150  1                                  14    
HELIX   35  35 THR D  172  ASN D  178  1                                   7    
HELIX   36  36 ASP D  202  ASN D  212  1                                  11    
HELIX   37  37 GLY D  224  CYS D  235  1                                  12    
HELIX   38  38 CYS D  235  GLY D  240  1                                   6    
HELIX   39  39 PHE D  259  GLY D  267  5                                   9    
HELIX   40  40 THR D  294  ASN D  305  1                                  12    
HELIX   41  41 THR D  314  ILE D  328  1                                  15    
HELIX   42  42 ASN D  342  ARG D  355  1                                  14    
HELIX   43  43 LEU E  244  LYS E  249  1                                   6    
HELIX   44  44 LEU F  244  LYS F  249  1                                   6    
SHEET    1  AA 4 ALA A   9  SER A  12  0                                        
SHEET    2  AA 4 ARG A 431  TYR A 435 -1  O  ALA A 432   N  TYR A  11           
SHEET    3  AA 4 ASP A 421  ALA A 426 -1  O  LEU A 422   N  TYR A 435           
SHEET    4  AA 4 PHE A 404  THR A 412 -1  N  GLY A 405   O  GLY A 425           
SHEET    1  AB 4 VAL A  23  PHE A  26  0                                        
SHEET    2  AB 4 PHE A  35  ALA A  40 -1  O  PHE A  35   N  PHE A  26           
SHEET    3  AB 4 GLN A  55  ASP A  60 -1  O  GLN A  55   N  ALA A  40           
SHEET    4  AB 4 CYS A  67  PRO A  69 -1  O  GLN A  68   N  LYS A  58           
SHEET    1  AC 2 ASP A  79  ALA A  81  0                                        
SHEET    2  AC 2 ASP A  84  PRO A  85 -1  O  ASP A  84   N  TYR A  80           
SHEET    1  AD 2 GLU A  87  PHE A  88  0                                        
SHEET    2  AD 2 HIS A 113  TRP A 114 -1  O  HIS A 113   N  PHE A  88           
SHEET    1  AE 4 VAL A  98  LYS A 101  0                                        
SHEET    2  AE 4 LYS A 104  ALA A 109 -1  O  LYS A 104   N  LYS A 101           
SHEET    3  AE 4 THR A 127  ASP A 132 -1  O  THR A 127   N  ALA A 109           
SHEET    4  AE 4 LYS A 135  TYR A 139 -1  O  LYS A 135   N  ASP A 132           
SHEET    1  AF 4 ILE A 161  PHE A 163  0                                        
SHEET    2  AF 4 ARG A 168  GLY A 173 -1  O  LEU A 170   N  ASP A 162           
SHEET    3  AF 4 GLN A 182  GLN A 187 -1  O  GLN A 182   N  GLY A 173           
SHEET    4  AF 4 LEU A 208  ALA A 209 -1  O  LEU A 208   N  SER A 185           
SHEET    1  AG 4 VAL A 226  GLY A 229  0                                        
SHEET    2  AG 4 ASP A 238  VAL A 243 -1  O  ASP A 238   N  GLY A 229           
SHEET    3  AG 4 MET A 252  TYR A 256 -1  O  MET A 252   N  VAL A 243           
SHEET    4  AG 4 SER A 263  THR A 268 -1  N  LEU A 264   O  ILE A 255           
SHEET    1  AH 4 VAL A 280  THR A 283  0                                        
SHEET    2  AH 4 ASP A 292  ALA A 297 -1  O  ASP A 292   N  THR A 283           
SHEET    3  AH 4 GLN A 314  GLN A 320 -1  O  GLN A 314   N  ALA A 297           
SHEET    4  AH 4 PHE A 326  ASN A 332 -1  O  GLN A 327   N  LEU A 319           
SHEET    1  AI 2 MET A 301  ARG A 303  0                                        
SHEET    2  AI 2 LEU A 309  GLU A 311 -1  O  GLN A 310   N  ASP A 302           
SHEET    1  AJ 4 ILE A 344  GLY A 348  0                                        
SHEET    2  AJ 4 ASP A 357  ALA A 362 -1  O  ASP A 357   N  LEU A 347           
SHEET    3  AJ 4 ILE A 372  ARG A 379 -1  O  ILE A 372   N  ALA A 362           
SHEET    4  AJ 4 GLY A 382  LEU A 383  1  O  GLY A 382   N  ARG A 379           
SHEET    1  AK 4 ILE A 344  GLY A 348  0                                        
SHEET    2  AK 4 ASP A 357  ALA A 362 -1  O  ASP A 357   N  LEU A 347           
SHEET    3  AK 4 ILE A 372  ARG A 379 -1  O  ILE A 372   N  ALA A 362           
SHEET    4  AK 4 GLN A 389  GLU A 392 -1  O  GLN A 389   N  ILE A 375           
SHEET    1  AL 2 GLY A 382  LEU A 383  0                                        
SHEET    2  AL 2 ILE A 372  ARG A 379  1  O  ARG A 379   N  GLY A 382           
SHEET    1  AM 5 ALA A 511  PHE A 513  0                                        
SHEET    2  AM 5 GLN A 534  LEU A 542 -1  O  TYR A 541   N  LEU A 512           
SHEET    3  AM 5 CYS A 472  GLY A 483 -1  O  PHE A 473   N  ALA A 540           
SHEET    4  AM 5 VAL A 440  TYR A 450 -1  O  THR A 442   N  ASP A 482           
SHEET    5  AM 5 ILE A 577  LEU A 578  1  O  ILE A 577   N  ILE A 441           
SHEET    1  AN 5 ILE A 453  LEU A 454  0                                        
SHEET    2  AN 5 ASN A 585  ILE A 592  1  O  HIS A 591   N  LEU A 454           
SHEET    3  AN 5 ILE A 555  LEU A 563 -1  O  ILE A 555   N  ALA A 590           
SHEET    4  AN 5 LYS A 490  LEU A 498 -1  O  GLN A 494   N  ARG A 562           
SHEET    5  AN 5 SER A 520  SER A 528 -1  O  HIS A 521   N  LEU A 497           
SHEET    1  BA 2 ALA B  25  TRP B  26  0                                        
SHEET    2  BA 2 CYS B  42  ASP B  43 -1  O  ASP B  43   N  ALA B  25           
SHEET    1  BB 6 GLN B  64  LYS B  69  0                                        
SHEET    2  BB 6 SER B  91  LEU B  96 -1  O  SER B  91   N  LEU B  68           
SHEET    3  BB 6 LEU B 427  PRO B 433  1  O  GLU B 428   N  LEU B  92           
SHEET    4  BB 6 ARG B 414  PRO B 420 -1  O  ARG B 414   N  VAL B 431           
SHEET    5  BB 6 VAL B 358  GLY B 364 -1  O  GLU B 361   N  LYS B 419           
SHEET    6  BB 6 LYS B 388  CYS B 389 -1  O  CYS B 389   N  VAL B 358           
SHEET    1  BC 5 ILE B  87  ALA B  88  0                                        
SHEET    2  BC 5 GLN B 102  ARG B 109 -1  O  HIS B 107   N  ALA B  88           
SHEET    3  BC 5 THR B 397  ASN B 405 -1  O  ALA B 398   N  VAL B 108           
SHEET    4  BC 5 ASN B 370  ILE B 376 -1  O  ASN B 370   N  ASN B 405           
SHEET    5  BC 5 PHE B 383  GLN B 384 -1  O  PHE B 383   N  ALA B 375           
SHEET    1  BD 6 PHE B 193  THR B 200  0                                        
SHEET    2  BD 6 PHE B 153  PHE B 160 -1  O  LEU B 155   N  THR B 200           
SHEET    3  BD 6 VAL B 116  ASP B 123  1  O  VAL B 116   N  ARG B 154           
SHEET    4  BD 6 LEU B 246  SER B 253  1  O  LEU B 246   N  ASP B 117           
SHEET    5  BD 6 VAL B 307  VAL B 313  1  O  LEU B 308   N  LEU B 249           
SHEET    6  BD 6 THR B 332  LEU B 335  1  O  THR B 332   N  PHE B 311           
SHEET    1  BE 2 GLY B 455  GLN B 458  0                                        
SHEET    2  BE 2 VAL B 461  CYS B 464 -1  O  VAL B 461   N  GLN B 458           
SHEET    1  CA 4 LEU C   3  SER C  12  0                                        
SHEET    2  CA 4 ARG C 431  ALA C 437 -1  O  ALA C 432   N  TYR C  11           
SHEET    3  CA 4 ASP C 421  ALA C 426 -1  O  LEU C 422   N  TYR C 435           
SHEET    4  CA 4 SER C 407  THR C 412 -1  O  SER C 407   N  GLY C 425           
SHEET    1  CB 4 VAL C  23  PHE C  26  0                                        
SHEET    2  CB 4 PHE C  35  ALA C  40 -1  O  PHE C  35   N  PHE C  26           
SHEET    3  CB 4 GLN C  55  ASP C  60 -1  O  GLN C  55   N  ALA C  40           
SHEET    4  CB 4 CYS C  67  PRO C  69 -1  O  GLN C  68   N  LYS C  58           
SHEET    1  CC 2 ASP C  79  ALA C  81  0                                        
SHEET    2  CC 2 ASP C  84  PRO C  85 -1  O  ASP C  84   N  TYR C  80           
SHEET    1  CD 2 GLU C  87  PHE C  88  0                                        
SHEET    2  CD 2 HIS C 113  TRP C 114 -1  O  HIS C 113   N  PHE C  88           
SHEET    1  CE 4 VAL C  98  LYS C 101  0                                        
SHEET    2  CE 4 LYS C 104  ALA C 109 -1  O  LYS C 104   N  LYS C 101           
SHEET    3  CE 4 THR C 127  ASP C 132 -1  O  THR C 127   N  ALA C 109           
SHEET    4  CE 4 LYS C 135  TYR C 139 -1  O  LYS C 135   N  ASP C 132           
SHEET    1  CF 4 ILE C 161  PHE C 163  0                                        
SHEET    2  CF 4 ARG C 168  GLY C 173 -1  O  LEU C 170   N  ASP C 162           
SHEET    3  CF 4 GLN C 182  GLN C 187 -1  O  GLN C 182   N  GLY C 173           
SHEET    4  CF 4 LEU C 208  ALA C 209 -1  O  LEU C 208   N  SER C 185           
SHEET    1  CG 4 VAL C 226  GLY C 229  0                                        
SHEET    2  CG 4 ASP C 238  VAL C 243 -1  O  ASP C 238   N  GLY C 229           
SHEET    3  CG 4 MET C 252  TYR C 256 -1  O  MET C 252   N  VAL C 243           
SHEET    4  CG 4 SER C 263  THR C 268 -1  N  LEU C 264   O  ILE C 255           
SHEET    1  CH 4 VAL C 280  THR C 283  0                                        
SHEET    2  CH 4 ASP C 292  ALA C 297 -1  O  ASP C 292   N  THR C 283           
SHEET    3  CH 4 GLN C 314  GLN C 320 -1  O  GLN C 314   N  ALA C 297           
SHEET    4  CH 4 PHE C 326  ASN C 332 -1  O  GLN C 327   N  LEU C 319           
SHEET    1  CI 2 MET C 301  ARG C 303  0                                        
SHEET    2  CI 2 LEU C 309  GLU C 311 -1  O  GLN C 310   N  ASP C 302           
SHEET    1  CJ 4 ILE C 344  GLY C 348  0                                        
SHEET    2  CJ 4 ASP C 357  ALA C 362 -1  O  ASP C 357   N  LEU C 347           
SHEET    3  CJ 4 ILE C 372  ARG C 379 -1  O  ILE C 372   N  ALA C 362           
SHEET    4  CJ 4 GLY C 382  LEU C 383  1  O  GLY C 382   N  ARG C 379           
SHEET    1  CK 4 ILE C 344  GLY C 348  0                                        
SHEET    2  CK 4 ASP C 357  ALA C 362 -1  O  ASP C 357   N  LEU C 347           
SHEET    3  CK 4 ILE C 372  ARG C 379 -1  O  ILE C 372   N  ALA C 362           
SHEET    4  CK 4 GLN C 389  GLU C 392 -1  O  GLN C 389   N  ILE C 375           
SHEET    1  CL 2 GLY C 382  LEU C 383  0                                        
SHEET    2  CL 2 ILE C 372  ARG C 379  1  O  ARG C 379   N  GLY C 382           
SHEET    1  CM 5 ALA C 511  PHE C 513  0                                        
SHEET    2  CM 5 GLN C 534  LEU C 542 -1  O  TYR C 541   N  LEU C 512           
SHEET    3  CM 5 CYS C 472  GLY C 483 -1  O  PHE C 473   N  ALA C 540           
SHEET    4  CM 5 VAL C 440  TYR C 450 -1  O  THR C 442   N  ASP C 482           
SHEET    5  CM 5 ILE C 577  LEU C 578  1  O  ILE C 577   N  ILE C 441           
SHEET    1  CN 5 ILE C 453  LEU C 454  0                                        
SHEET    2  CN 5 ASN C 585  ILE C 592  1  O  HIS C 591   N  LEU C 454           
SHEET    3  CN 5 ILE C 555  LEU C 563 -1  O  ILE C 555   N  ALA C 590           
SHEET    4  CN 5 LYS C 490  LEU C 498 -1  O  GLN C 494   N  ARG C 562           
SHEET    5  CN 5 SER C 520  SER C 528 -1  O  HIS C 521   N  LEU C 497           
SHEET    1  DA 2 TRP D  26  CYS D  27  0                                        
SHEET    2  DA 2 ILE D  58  GLU D  59 -1  O  GLU D  59   N  TRP D  26           
SHEET    1  DB 6 GLN D  64  LYS D  69  0                                        
SHEET    2  DB 6 SER D  91  LEU D  96 -1  O  SER D  91   N  LEU D  68           
SHEET    3  DB 6 LEU D 427  PRO D 433  1  O  GLU D 428   N  LEU D  92           
SHEET    4  DB 6 ARG D 414  PRO D 420 -1  O  ARG D 414   N  VAL D 431           
SHEET    5  DB 6 VAL D 358  GLY D 364 -1  O  GLU D 361   N  LYS D 419           
SHEET    6  DB 6 LYS D 388  CYS D 389 -1  O  CYS D 389   N  VAL D 358           
SHEET    1  DC 5 ILE D  87  ALA D  88  0                                        
SHEET    2  DC 5 GLN D 102  ARG D 109 -1  O  HIS D 107   N  ALA D  88           
SHEET    3  DC 5 THR D 397  ASN D 405 -1  O  ALA D 398   N  VAL D 108           
SHEET    4  DC 5 ASN D 370  ILE D 376 -1  O  ASN D 370   N  ASN D 405           
SHEET    5  DC 5 LEU D 382  GLN D 384 -1  O  PHE D 383   N  ALA D 375           
SHEET    1  DD 6 PHE D 193  THR D 200  0                                        
SHEET    2  DD 6 PHE D 153  PHE D 160 -1  O  LEU D 155   N  THR D 200           
SHEET    3  DD 6 VAL D 116  ASP D 123  1  O  VAL D 116   N  ARG D 154           
SHEET    4  DD 6 LEU D 246  SER D 253  1  O  LEU D 246   N  ASP D 117           
SHEET    5  DD 6 VAL D 307  VAL D 313  1  O  LEU D 308   N  LEU D 249           
SHEET    6  DD 6 THR D 332  LEU D 335  1  O  THR D 332   N  PHE D 311           
SHEET    1  DE 2 SER D 456  GLN D 458  0                                        
SHEET    2  DE 2 VAL D 461  ALA D 463 -1  O  VAL D 461   N  GLN D 458           
SSBOND   1 CYS A   59    CYS A   67                          1555   1555  2.03  
SSBOND   2 CYS A  108    CYS A  128                          1555   1555  2.03  
SSBOND   3 CYS A  142    CYS A  155                          1555   1555  2.03  
SSBOND   4 CYS A  400    CYS B  270                          1555   1555  2.05  
SSBOND   5 CYS A  461    CYS A  472                          1555   1555  2.03  
SSBOND   6 CYS A  478    CYS A  535                          1555   1555  2.03  
SSBOND   7 CYS B    6    CYS B   24                          1555   1555  2.03  
SSBOND   8 CYS B   14    CYS B  437                          1555   1555  2.03  
SSBOND   9 CYS B   17    CYS B   42                          1555   1555  2.03  
SSBOND  10 CYS B   27    CYS B   53                          1555   1555  2.03  
SSBOND  11 CYS B  180    CYS B  187                          1555   1555  2.04  
SSBOND  12 CYS B  235    CYS B  276                          1555   1555  2.03  
SSBOND  13 CYS B  377    CYS B  389                          1555   1555  2.03  
SSBOND  14 CYS B  409    CYS B  435                          1555   1555  2.03  
SSBOND  15 CYS B  439    CYS B  459                          1555   1555  2.03  
SSBOND  16 CYS B  450    CYS B  462                          1555   1555  2.03  
SSBOND  17 CYS B  464    CYS B  473                          1555   1555  2.03  
SSBOND  18 CYS C   59    CYS C   67                          1555   1555  2.04  
SSBOND  19 CYS C  108    CYS C  128                          1555   1555  2.03  
SSBOND  20 CYS C  142    CYS C  155                          1555   1555  2.03  
SSBOND  21 CYS C  400    CYS D  270                          1555   1555  2.04  
SSBOND  22 CYS C  461    CYS C  472                          1555   1555  2.02  
SSBOND  23 CYS C  478    CYS C  535                          1555   1555  2.03  
SSBOND  24 CYS D    6    CYS D   24                          1555   1555  2.04  
SSBOND  25 CYS D   14    CYS D  437                          1555   1555  2.03  
SSBOND  26 CYS D   17    CYS D   42                          1555   1555  2.03  
SSBOND  27 CYS D   27    CYS D   53                          1555   1555  2.03  
SSBOND  28 CYS D  180    CYS D  187                          1555   1555  2.04  
SSBOND  29 CYS D  235    CYS D  276                          1555   1555  2.02  
SSBOND  30 CYS D  377    CYS D  389                          1555   1555  2.03  
SSBOND  31 CYS D  409    CYS D  435                          1555   1555  2.03  
SSBOND  32 CYS D  439    CYS D  459                          1555   1555  2.03  
SSBOND  33 CYS D  450    CYS D  462                          1555   1555  2.03  
SSBOND  34 CYS D  464    CYS D  473                          1555   1555  2.03  
LINK         ND2 ASN A  44                 C1  NAG A3044     1555   1555  1.44  
LINK         ND2 ASN A 260                 C1  NAG A3260     1555   1555  1.44  
LINK         ND2 ASN A 266                 C1  NAG A3266     1555   1555  1.43  
LINK         ND2 ASN A 458                 C1  NAG A3458     1555   1555  1.45  
LINK         ND2 ASN A 524                 C1  NAG A3524     1555   1555  1.44  
LINK         ND2 ASN A 585                 C1  NAG A3585     1555   1555  1.45  
LINK        CA    CA A2001                 OD1 ASP A 234     1555   1555  2.40  
LINK        CA    CA A2001                 O   HOH A4030     1555   1555  2.39  
LINK        CA    CA A2001                 O   ILE A 236     1555   1555  2.19  
LINK        CA    CA A2001                 OD1 ASN A 232     1555   1555  2.29  
LINK        CA    CA A2001                 OD1 ASP A 238     1555   1555  2.50  
LINK        CA    CA A2001                 OD2 ASP A 238     1555   1555  2.49  
LINK        CA    CA A2001                 OD1 ASP A 230     1555   1555  2.39  
LINK        CA    CA A2002                 OD1 ASP A 288     1555   1555  2.46  
LINK        CA    CA A2002                 O   TYR A 290     1555   1555  2.29  
LINK        CA    CA A2002                 O   HOH A4045     1555   1555  2.36  
LINK        CA    CA A2002                 OD1 ASP A 292     1555   1555  2.40  
LINK        CA    CA A2002                 OD2 ASP A 292     1555   1555  2.42  
LINK        CA    CA A2002                 OD1 ASP A 284     1555   1555  2.36  
LINK        CA    CA A2002                 OD1 ASN A 286     1555   1555  2.32  
LINK        CA    CA A2003                 OD1 ASP A 349     1555   1555  2.38  
LINK        CA    CA A2003                 O   PHE A 355     1555   1555  2.21  
LINK        CA    CA A2003                 OD1 ASP A 357     1555   1555  2.43  
LINK        CA    CA A2003                 OD2 ASP A 357     1555   1555  2.44  
LINK        CA    CA A2003                 O   HOH A4064     1555   1555  2.33  
LINK        CA    CA A2003                 OD1 ASP A 353     1555   1555  2.33  
LINK        CA    CA A2003                 OD1 ASP A 351     1555   1555  2.31  
LINK        CA    CA A2004                 OD1 ASP A 415     1555   1555  2.25  
LINK        CA    CA A2004                 OD1 ASP A 413     1555   1555  2.33  
LINK        CA    CA A2004                 OD1 ASN A 417     1555   1555  2.46  
LINK        CA    CA A2004                 OD1 ASP A 421     1555   1555  2.45  
LINK        CA    CA A2004                 O   HOH A4071     1555   1555  2.36  
LINK        CA    CA A2004                 OD2 ASP A 421     1555   1555  2.44  
LINK        CA    CA A2004                 O   TYR A 419     1555   1555  2.23  
LINK         O4  NAG A3044                 C1  NAG A3045     1555   1555  1.44  
LINK         O4  NAG A3260                 C1  NAG A3261     1555   1555  1.44  
LINK         O4  NAG A3261                 C1  BMA A3262     1555   1555  1.44  
LINK         O6  BMA A3262                 C1  MAN A3263     1555   1555  1.44  
LINK         O4  NAG A3266                 C1  NAG A3267     1555   1555  1.43  
LINK         O4  NAG A3267                 C1  BMA A3268     1555   1555  1.43  
LINK         O3  BMA A3268                 C1  MAN A3269     1555   1555  1.44  
LINK         O6  BMA A3268                 C1  MAN A3270     1555   1555  1.44  
LINK         O3  MAN A3270                 C1  MAN A3271     1555   1555  1.44  
LINK         O4  NAG A3458                 C1  NAG A3459     1555   1555  1.44  
LINK         O4  NAG A3524                 C1  NAG A3525     1555   1555  1.44  
LINK         O4  NAG A3585                 C1  NAG A3586     1555   1555  1.45  
LINK         ND2 ASN B  80                 C1  NAG B3080     1555   1555  1.45  
LINK         ND2 ASN B 243                 C1  NAG B3243     1555   1555  1.44  
LINK         ND2 ASN B 370                 C1  NAG B3370     1555   1555  1.45  
LINK        MG    MG B2001                 O   HOH B4013     1555   1555  2.07  
LINK        MG    MG B2001                 O   HOH B4014     1555   1555  2.05  
LINK        MG    MG B2001                 O   HOH B4027     1555   1555  2.07  
LINK        MG    MG B2001                 OD1 ASP E 243     1555   1555  2.17  
LINK        MG    MG B2001                 OG  SER B 125     1555   1555  2.10  
LINK        MG    MG B2001                 OE2 GLU B 223     1555   1555  2.07  
LINK        CA    CA B2002                 OE1 GLU B 223     1555   1555  2.45  
LINK        CA    CA B2002                 O   PRO B 222     1555   1555  2.17  
LINK        CA    CA B2002                 OD1 ASP B 220     1555   1555  2.28  
LINK        CA    CA B2002                 OE2 GLU B 162     1555   1555  2.36  
LINK        CA    CA B2002                 O   ASP B 220     1555   1555  2.44  
LINK        CA    CA B2002                 OD1 ASN B 218     1555   1555  2.33  
LINK        CA    CA B2003                 OD1 ASP B 130     1555   1555  2.37  
LINK        CA    CA B2003                 OD1 ASP B 131     1555   1555  2.33  
LINK        CA    CA B2003                 OD2 ASP B 130     1555   1555  3.12  
LINK        CA    CA B2003                 O   SER B 127     1555   1555  2.40  
LINK        CA    CA B2003                 O   HOH B4016     1555   1555  2.41  
LINK         ND2 ASN C  44                 C1  NAG C3044     1555   1555  1.43  
LINK         ND2 ASN C 260                 C1  NAG C3260     1555   1555  1.43  
LINK         ND2 ASN C 266                 C1  NAG C3266     1555   1555  1.43  
LINK         ND2 ASN C 458                 C1  NAG C3458     1555   1555  1.44  
LINK         ND2 ASN C 524                 C1  NAG C3524     1555   1555  1.45  
LINK         ND2 ASN C 585                 C1  NAG C3585     1555   1555  1.45  
LINK        CA    CA C2001                 OD2 ASP C 415     1555   1555  2.68  
LINK        CA    CA C2001                 OD1 ASP C 415     1555   1555  2.24  
LINK        CA    CA C2001                 O   TYR C 419     1555   1555  2.49  
LINK        CA    CA C2001                 OD1 ASN C 417     1555   1555  2.17  
LINK        CA    CA C2001                 O   HOH C4040     1555   1555  2.27  
LINK        CA    CA C2001                 OD2 ASP C 421     1555   1555  3.10  
LINK        CA    CA C2001                 OD1 ASP C 421     1555   1555  2.47  
LINK        CA    CA C2002                 OD1 ASP C 353     1555   1555  2.29  
LINK        CA    CA C2002                 OD1 ASP C 349     1555   1555  2.41  
LINK        CA    CA C2002                 OD1 ASP C 351     1555   1555  2.38  
LINK        CA    CA C2002                 O   PHE C 355     1555   1555  2.06  
LINK        CA    CA C2002                 OD2 ASP C 357     1555   1555  2.46  
LINK        CA    CA C2002                 OD1 ASP C 357     1555   1555  2.40  
LINK        CA    CA C2003                 O   ILE C 236     1555   1555  2.27  
LINK        CA    CA C2003                 OD1 ASP C 234     1555   1555  2.37  
LINK        CA    CA C2003                 OD1 ASP C 230     1555   1555  2.49  
LINK        CA    CA C2003                 OD1 ASP C 238     1555   1555  2.41  
LINK        CA    CA C2003                 OD1 ASN C 232     1555   1555  2.32  
LINK        CA    CA C2003                 OD2 ASP C 238     1555   1555  2.44  
LINK        CA    CA C2003                 O   HOH C4019     1555   1555  2.32  
LINK        CA    CA C2004                 OD1 ASN C 286     1555   1555  2.30  
LINK        CA    CA C2004                 O   HOH C4027     1555   1555  2.41  
LINK        CA    CA C2004                 OD2 ASP C 292     1555   1555  2.44  
LINK        CA    CA C2004                 OD1 ASP C 292     1555   1555  2.39  
LINK        CA    CA C2004                 O   TYR C 290     1555   1555  2.30  
LINK        CA    CA C2004                 OD1 ASP C 284     1555   1555  2.41  
LINK        CA    CA C2004                 OD1 ASP C 288     1555   1555  2.44  
LINK         O4  NAG C3260                 C1  NAG C3261     1555   1555  1.44  
LINK         O4  NAG C3266                 C1  NAG C3267     1555   1555  1.43  
LINK         O4  NAG C3267                 C1  BMA C3268     1555   1555  1.43  
LINK         O6  BMA C3268                 C1  MAN C3270     1555   1555  1.44  
LINK         O3  BMA C3268                 C1  MAN C3269     1555   1555  1.44  
LINK         O3  MAN C3270                 C1  MAN C3271     1555   1555  1.44  
LINK         O4  NAG C3458                 C1  NAG C3459     1555   1555  1.45  
LINK         O4  NAG C3459                 C1  BMA C3460     1555   1555  1.45  
LINK         O4  NAG C3585                 C1  NAG C3586     1555   1555  1.45  
LINK         ND2 ASN D  31                 C1  NAG D3031     1555   1555  1.44  
LINK         ND2 ASN D  80                 C1  NAG D3080     1555   1555  1.44  
LINK         ND2 ASN D 243                 C1  NAG D3243     1555   1555  1.43  
LINK        MG    MG D2001                 O   HOH D4005     1555   1555  2.06  
LINK        MG    MG D2001                 O   HOH D4004     1555   1555  2.07  
LINK        MG    MG D2001                 OD1 ASP F 243     1555   1555  2.13  
LINK        MG    MG D2001                 OE2 GLU D 223     1555   1555  2.13  
LINK        MG    MG D2001                 OG  SER D 125     1555   1555  2.09  
LINK        MG    MG D2001                 O   HOH D4011     1555   1555  2.06  
LINK        CA    CA D2002                 OD2 ASP D 130     1555   1555  2.45  
LINK        CA    CA D2002                 O   HOH D4006     1555   1555  2.41  
LINK        CA    CA D2002                 O   LYS D 338     1555   1555  3.01  
LINK        CA    CA D2002                 OD1 ASP D 130     1555   1555  2.33  
LINK        CA    CA D2002                 O   SER D 127     1555   1555  2.49  
LINK        CA    CA D2003                 O   ASP D 220     1555   1555  2.48  
LINK        CA    CA D2003                 OD1 ASN D 218     1555   1555  2.42  
LINK        CA    CA D2003                 O   PRO D 222     1555   1555  2.14  
LINK        CA    CA D2003                 OD1 ASP D 220     1555   1555  2.30  
LINK        CA    CA D2003                 OE2 GLU D 162     1555   1555  2.45  
LINK        CA    CA D2003                 OE1 GLU D 223     1555   1555  2.41  
CISPEP   1 TYR A  450    PRO A  451          0        -4.08                     
CISPEP   2 ALA B   88    PRO B   89          0        -2.58                     
CISPEP   3 SER B  166    PRO B  167          0         4.82                     
CISPEP   4 ILE B  183    PRO B  184          0        -4.62                     
CISPEP   5 TYR C  450    PRO C  451          0        -3.94                     
CISPEP   6 ALA D   88    PRO D   89          0        -2.51                     
CISPEP   7 SER D  166    PRO D  167          0         5.02                     
CISPEP   8 ILE D  183    PRO D  184          0        -5.97                     
SITE     1 AC1  6 ASP A 230  ASN A 232  ASP A 234  ILE A 236                    
SITE     2 AC1  6 ASP A 238  HOH A4030                                          
SITE     1 AC2  6 ASP A 284  ASN A 286  ASP A 288  TYR A 290                    
SITE     2 AC2  6 ASP A 292  HOH A4045                                          
SITE     1 AC3  6 ASP A 349  ASP A 351  ASP A 353  PHE A 355                    
SITE     2 AC3  6 ASP A 357  HOH A4064                                          
SITE     1 AC4  6 ASP A 413  ASP A 415  ASN A 417  TYR A 419                    
SITE     2 AC4  6 ASP A 421  HOH A4071                                          
SITE     1 AC5  7 SER B 125  SER B 127  GLU B 223  HOH B4013                    
SITE     2 AC5  7 HOH B4014  HOH B4027  ASP E 243                               
SITE     1 AC6  5 GLU B 162  ASN B 218  ASP B 220  PRO B 222                    
SITE     2 AC6  5 GLU B 223                                                     
SITE     1 AC7  5 SER B 127  ASP B 130  ASP B 131  LYS B 338                    
SITE     2 AC7  5 HOH B4016                                                     
SITE     1 AC8  6 ASP C 413  ASP C 415  ASN C 417  TYR C 419                    
SITE     2 AC8  6 ASP C 421  HOH C4040                                          
SITE     1 AC9  5 ASP C 349  ASP C 351  ASP C 353  PHE C 355                    
SITE     2 AC9  5 ASP C 357                                                     
SITE     1 BC1  6 ASP C 230  ASN C 232  ASP C 234  ILE C 236                    
SITE     2 BC1  6 ASP C 238  HOH C4019                                          
SITE     1 BC2  6 ASP C 284  ASN C 286  ASP C 288  TYR C 290                    
SITE     2 BC2  6 ASP C 292  HOH C4027                                          
SITE     1 BC3  4 GLU C 448  TYR C 450  ARG C 476  BMA C3460                    
SITE     1 BC4  8 ASP D 123  SER D 125  SER D 127  GLU D 223                    
SITE     2 BC4  8 HOH D4004  HOH D4005  HOH D4011  ASP F 243                    
SITE     1 BC5  4 SER D 127  ASP D 130  LYS D 338  HOH D4006                    
SITE     1 BC6  5 GLU D 162  ASN D 218  ASP D 220  PRO D 222                    
SITE     2 BC6  5 GLU D 223                                                     
SITE     1 BC7  2 PRO A 488  ARG A 489                                          
SITE     1 BC8  4 ASN C  77  PHE C  88  LYS C  89  SER C  90                    
SITE     1 BC9  3 SER C 528  GLY C 531  LEU C 532                               
SITE     1 CC1  1 HIS B 277                                                     
SITE     1 CC2  3 GLY A  13  GLU A  15  ARG A 398                               
SITE     1 CC3  4 ASN A  77  PHE A  88  LYS A  89  SER A  90                    
SITE     1 CC4  8 GLU A  15  GLY A  16  LYS A  42  ASN A  44                    
SITE     2 CC4  8 GLU A  52  HOH A4004  HOH A4086  HOH A4087                    
SITE     1 CC5  6 ASN A 232  ASP A 257  LYS A 259  ASN A 260                    
SITE     2 CC5  6 HOH A4033  HOH A4088                                          
SITE     1 CC6  7 GLN A 214  PHE A 217  TYR A 254  SER A 263                    
SITE     2 CC6  7 LEU A 264  ASN A 266  HOH A4028                               
SITE     1 CC7  7 PRO A 451  ASN A 458  THR A 460  CYS A 472                    
SITE     2 CC7  7 PHE A 473  ASN A 474  HOH C4052                               
SITE     1 CC8  4 GLN A 494  SER A 522  ASN A 524  ASP A 564                    
SITE     1 CC9  3 PHE A 558  PRO A 583  ASN A 585                               
SITE     1 DC1  3 ASN B  80  SER B  82  ASP B  83                               
SITE     1 DC2  2 ASN B 243  HOH B4063                                          
SITE     1 DC3  5 SER A 305  GLY B 368  ASN B 370  HOH B4064                    
SITE     2 DC3  5 LYS D 214                                                     
SITE     1 DC4  6 GLU C  15  GLY C  16  LYS C  42  ASN C  44                    
SITE     2 DC4  6 GLU C  52  HOH C4051                                          
SITE     1 DC5  4 ASP C 234  ASP C 257  LYS C 259  ASN C 260                    
SITE     1 DC6  6 GLN C 214  PHE C 217  TYR C 254  SER C 263                    
SITE     2 DC6  6 LEU C 264  ASN C 266                                          
SITE     1 DC7  7 GLU A 448  ARG A 588  ASN C 458  THR C 460                    
SITE     2 DC7  7 CYS C 472  ASN C 474  MAN C3461                               
SITE     1 DC8  3 GLN C 494  SER C 522  ASN C 524                               
SITE     1 DC9  3 PHE C 558  PRO C 583  ASN C 585                               
SITE     1 EC1  2 ASN D  31  GLN D  54                                          
SITE     1 EC2  3 ASN D  80  SER D  82  HOH D4022                               
SITE     1 EC3  1 ASN D 243                                                     
CRYST1  185.020  168.090  101.800  90.00  98.95  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005405  0.000000  0.000851        0.00000                         
SCALE2      0.000000  0.005949  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009944        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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