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Database: PDB
Entry: 1TYE
LinkDB: 1TYE
Original site: 1TYE 
HEADER    CELL ADHESION                           07-JUL-04   1TYE              
TITLE     STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS AND BINDING OF LIGAND-    
TITLE    2 MIMETIC THERAPEUTICS TO THE PLATELET RECEPTOR FOR FIBRINOGEN         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-IIB;                                        
COMPND   3 CHAIN: A, C, E;                                                      
COMPND   4 FRAGMENT: RESIDUES 1-452;                                            
COMPND   5 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIB; GPALPHA IIB; GPIIB; CD41
COMPND   6 ANTIGEN;                                                             
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTEGRIN BETA-3;                                           
COMPND  10 CHAIN: B, D, F;                                                      
COMPND  11 FRAGMENT: RESIDUES 1-440;                                            
COMPND  12 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA; GPIIIA; CD61 ANTIGEN;  
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ITGAB;                                                         
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: LEC 3.2.8.1;                               
SOURCE  10 EXPRESSION_SYSTEM_CELL: HAMPSTER OVARY CELLS;                        
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: ITGAB;                                                         
SOURCE  17 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  18 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: LEC 3.2.8.1;                               
SOURCE  21 EXPRESSION_SYSTEM_CELL: HAMPSTER OVARY CELLS;                        
SOURCE  22 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    CRYSTAL STRUCTURE; PLATELET INTEGRIN ALPHAIIBBETA3; FIBRINOGEN        
KEYWDS   2 BINDING; ALLOSTERY; THERAPEUTIC ANTAGONISM, CELL ADHESION            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.XIAO,J.TAKAGI,B.S.COLLER,J.-H.WANG,T.A.SPRINGER                     
REVDAT   5   10-SEP-14 1TYE    1       JRNL                                     
REVDAT   4   13-JUL-11 1TYE    1       VERSN                                    
REVDAT   3   24-FEB-09 1TYE    1       VERSN                                    
REVDAT   2   09-NOV-04 1TYE    1       JRNL                                     
REVDAT   1   12-OCT-04 1TYE    0                                                
JRNL        AUTH   T.XIAO,J.TAKAGI,B.S.COLLER,J.-H.WANG,T.A.SPRINGER            
JRNL        TITL   STRUCTURAL BASIS FOR ALLOSTERY IN INTEGRINS AND BINDING TO   
JRNL        TITL 2 FIBRINOGEN-MIMETIC THERAPEUTICS                              
JRNL        REF    NATURE                        V. 432    59 2004              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   15378069                                                     
JRNL        DOI    10.1038/NATURE02976                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 118381                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5971                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 20604                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 295                                     
REMARK   3   SOLVENT ATOMS            : 120                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 74.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.21500                                              
REMARK   3    B22 (A**2) : 0.21500                                              
REMARK   3    B33 (A**2) : -0.43000                                             
REMARK   3    B12 (A**2) : -10.34300                                            
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.42                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.700                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1TYE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023029.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-OCT-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9760                             
REMARK 200  MONOCHROMATOR                  : RH-COATED SI                       
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 121498                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 10.000                             
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : 0.09700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.60200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1TVX                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 0.4 M MAGNESIUM ACETATE,   
REMARK 280  0.1 M SODIUM CACODYLATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.85867            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       29.42933            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       58.85867            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       29.42933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 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   C    SER B    84     CD   PRO B    85              1.51            
REMARK 500   O    SER C   101     N    ASP C   102              1.56            
REMARK 500   O    GLU E   123     N    LYS E   124              1.62            
REMARK 500   O    ALA A   122     N    GLU A   123              1.77            
REMARK 500   O    TRP E   100     N    SER E   101              1.80            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASP A  28   CB    ASP A  28   CG     -0.130                       
REMARK 500    SER A 101   CB    SER A 101   OG      0.287                       
REMARK 500    GLU A 123   CB    GLU A 123   CG      0.324                       
REMARK 500    ALA A 122   C     GLU A 123   N      -0.292                       
REMARK 500    GLU A 123   C     LYS A 124   N       0.157                       
REMARK 500    TRP C 100   C     SER C 101   N      -0.244                       
REMARK 500    SER C 101   C     ASP C 102   N      -0.271                       
REMARK 500    GLU C 117   CA    GLU C 117   C       0.317                       
REMARK 500    LYS C 118   N     LYS C 118   CA     -0.162                       
REMARK 500    ALA C 122   C     ALA C 122   O      -0.119                       
REMARK 500    GLU C 123   N     GLU C 123   CA      0.129                       
REMARK 500    ARG D   8   CB    ARG D   8   CG     -0.181                       
REMARK 500    THR D   7   C     ARG D   8   N      -0.142                       
REMARK 500    PRO D  85   CD    PRO D  85   N       0.395                       
REMARK 500    SER D  84   C     PRO D  85   N      -0.173                       
REMARK 500    TRP E 100   C     SER E 101   N      -0.271                       
REMARK 500    ALA E 122   C     GLU E 123   N       0.300                       
REMARK 500    GLU E 123   C     LYS E 124   N      -0.377                       
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    ASP A 102   N   -  CA  -  CB  ANGL. DEV. = -12.9 DEGREES          
REMARK 500    ASP A 102   N   -  CA  -  C   ANGL. DEV. =  20.2 DEGREES          
REMARK 500    ALA A 122   N   -  CA  -  C   ANGL. DEV. = -18.2 DEGREES          
REMARK 500    ALA A 122   CA  -  C   -  O   ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ALA A 122   CA  -  C   -  N   ANGL. DEV. =  33.9 DEGREES          
REMARK 500    ALA A 122   O   -  C   -  N   ANGL. DEV. = -25.0 DEGREES          
REMARK 500    GLU A 123   C   -  N   -  CA  ANGL. DEV. =  25.4 DEGREES          
REMARK 500    PRO A 334   N   -  CA  -  CB  ANGL. DEV. =   8.0 DEGREES          
REMARK 500    PRO A 337   CA  -  N   -  CD  ANGL. DEV. = -15.6 DEGREES          
REMARK 500    PRO A 452   C   -  N   -  CD  ANGL. DEV. = -13.2 DEGREES          
REMARK 500    ARG B   8   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    GLN B  79   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    PRO B  85   C   -  N   -  CD  ANGL. DEV. = -65.2 DEGREES          
REMARK 500    GLU B 409   N   -  CA  -  C   ANGL. DEV. = -17.9 DEGREES          
REMARK 500    TRP C 100   CA  -  C   -  N   ANGL. DEV. =  15.4 DEGREES          
REMARK 500    TRP C 100   O   -  C   -  N   ANGL. DEV. = -19.0 DEGREES          
REMARK 500    SER C 101   C   -  N   -  CA  ANGL. DEV. =  25.1 DEGREES          
REMARK 500    ASP C 102   N   -  CA  -  C   ANGL. DEV. =  19.6 DEGREES          
REMARK 500    SER C 101   CA  -  C   -  N   ANGL. DEV. =  31.6 DEGREES          
REMARK 500    SER C 101   O   -  C   -  N   ANGL. DEV. = -39.9 DEGREES          
REMARK 500    ASP C 102   C   -  N   -  CA  ANGL. DEV. =  24.5 DEGREES          
REMARK 500    GLU C 117   O   -  C   -  N   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    ALA C 122   CB  -  CA  -  C   ANGL. DEV. =  14.8 DEGREES          
REMARK 500    ALA C 122   CA  -  C   -  N   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ALA C 122   O   -  C   -  N   ANGL. DEV. =   9.8 DEGREES          
REMARK 500    GLU C 123   C   -  N   -  CA  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    GLU C 123   O   -  C   -  N   ANGL. DEV. = -11.4 DEGREES          
REMARK 500    PRO C 334   CA  -  N   -  CD  ANGL. DEV. = -22.8 DEGREES          
REMARK 500    PRO C 337   CA  -  N   -  CD  ANGL. DEV. = -12.9 DEGREES          
REMARK 500    PRO C 337   C   -  N   -  CD  ANGL. DEV. = -25.4 DEGREES          
REMARK 500    PRO D  85   CA  -  N   -  CD  ANGL. DEV. = -20.1 DEGREES          
REMARK 500    PRO D  85   N   -  CA  -  CB  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO D  85   N   -  CD  -  CG  ANGL. DEV. = -11.7 DEGREES          
REMARK 500    SER D  84   CA  -  C   -  N   ANGL. DEV. =  20.2 DEGREES          
REMARK 500    SER D  84   O   -  C   -  N   ANGL. DEV. = -20.3 DEGREES          
REMARK 500    PRO D  85   C   -  N   -  CA  ANGL. DEV. =  30.5 DEGREES          
REMARK 500    PRO D  85   C   -  N   -  CD  ANGL. DEV. = -18.4 DEGREES          
REMARK 500    SER E 101   N   -  CA  -  CB  ANGL. DEV. = -13.1 DEGREES          
REMARK 500    TRP E 100   CA  -  C   -  N   ANGL. DEV. =  18.0 DEGREES          
REMARK 500    TRP E 100   O   -  C   -  N   ANGL. DEV. = -20.3 DEGREES          
REMARK 500    SER E 101   C   -  N   -  CA  ANGL. DEV. =  30.5 DEGREES          
REMARK 500    GLU E 123   CA  -  CB  -  CG  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    ALA E 122   CA  -  C   -  N   ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ALA E 122   O   -  C   -  N   ANGL. DEV. =   9.7 DEGREES          
REMARK 500    GLU E 123   CA  -  C   -  N   ANGL. DEV. =  24.8 DEGREES          
REMARK 500    GLU E 123   O   -  C   -  N   ANGL. DEV. = -29.6 DEGREES          
REMARK 500    PRO E 334   CA  -  N   -  CD  ANGL. DEV. = -13.5 DEGREES          
REMARK 500    PRO E 334   C   -  N   -  CD  ANGL. DEV. = -14.2 DEGREES          
REMARK 500    PRO E 337   CA  -  N   -  CD  ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    PRO E 337   C   -  N   -  CD  ANGL. DEV. = -13.1 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      58 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A   6      -47.87   -131.24                                   
REMARK 500    GLN A   7       34.83    -90.60                                   
REMARK 500    HIS A  30      -98.45    -92.66                                   
REMARK 500    ARG A  32     -178.45    -66.22                                   
REMARK 500    PRO A  40        1.79    -65.47                                   
REMARK 500    PRO A  45       -9.44    -58.10                                   
REMARK 500    ARG A  59      115.31   -165.57                                   
REMARK 500    SER A  96      115.77   -163.08                                   
REMARK 500    SER A 101      -97.77      3.03                                   
REMARK 500    LYS A 118     -126.25     64.75                                   
REMARK 500    ALA A 122      -70.33   -124.79                                   
REMARK 500    GLU A 168       40.72     70.62                                   
REMARK 500    SER A 218       32.56    -92.72                                   
REMARK 500    SER A 222     -168.94    -65.61                                   
REMARK 500    SER A 261       65.69     38.50                                   
REMARK 500    TYR A 288       43.63     70.98                                   
REMARK 500    THR A 296      160.04    179.95                                   
REMARK 500    ASP A 319       35.59     84.79                                   
REMARK 500    PRO A 337       59.44    -61.13                                   
REMARK 500    ALA A 342      170.67    -56.74                                   
REMARK 500    GLN A 395     -148.08   -100.99                                   
REMARK 500    PRO A 412     -167.96    -70.56                                   
REMARK 500    SER B  11      -16.72   -168.41                                   
REMARK 500    CYS B  26      103.32   -165.61                                   
REMARK 500    SER B  27       32.23    -90.78                                   
REMARK 500    ALA B  30        3.62    -60.03                                   
REMARK 500    LEU B  33       48.43    -70.00                                   
REMARK 500    PRO B  51        9.97    -57.90                                   
REMARK 500    GLU B  60      -51.20   -128.11                                   
REMARK 500    ALA B  61       90.20     61.17                                   
REMARK 500    LEU B  64      -78.06    -77.84                                   
REMARK 500    ASP B  66       70.86   -162.06                                   
REMARK 500    PRO B  68      167.07    -48.26                                   
REMARK 500    ASP B  76      112.92   -170.10                                   
REMARK 500    GLN B  79      115.88   -167.58                                   
REMARK 500    VAL B 157      -68.52   -141.57                                   
REMARK 500    ASP B 158     -178.90    177.86                                   
REMARK 500    PRO B 160       63.16    -67.78                                   
REMARK 500    SER B 213     -164.06   -125.67                                   
REMARK 500    CYS B 232       73.88   -100.97                                   
REMARK 500    ASP B 233      -73.89    -40.45                                   
REMARK 500    ASN B 240      -40.08    -27.80                                   
REMARK 500    LYS B 253     -175.42    -62.46                                   
REMARK 500    LEU B 258       -5.71     86.05                                   
REMARK 500    SER B 334     -168.71   -168.89                                   
REMARK 500    ASP B 361       74.96     43.33                                   
REMARK 500    GLU B 365       31.33    -86.82                                   
REMARK 500    CYS B 374     -151.63    -76.35                                   
REMARK 500    ASN B 376        3.14    -65.63                                   
REMARK 500    ASN B 377       17.10     57.83                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     172 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA A  122     GLU A  123                  127.70                    
REMARK 500 TRP C  100     SER C  101                 -131.39                    
REMARK 500 SER C  101     ASP C  102                  118.79                    
REMARK 500 SER D   84     PRO D   85                 -142.84                    
REMARK 500 TRP E  100     SER E  101                 -132.67                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ASP A  28        -11.71                                           
REMARK 500    TRP A 100        -11.88                                           
REMARK 500    ALA A 122         24.43                                           
REMARK 500    TRP C 100        -12.88                                           
REMARK 500    SER C 101         32.04                                           
REMARK 500    GLU C 123        -16.11                                           
REMARK 500    SER D  11        -10.36                                           
REMARK 500    SER D  84        -14.66                                           
REMARK 500    TRP E 100        -11.14                                           
REMARK 500    GLU E 123        -19.66                                           
REMARK 500    ASP F 361        -10.54                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PRO B   2        46.8      L          L   OUTSIDE RANGE           
REMARK 500    ASP C 102        16.9      L          L   OUTSIDE RANGE           
REMARK 500    PHE C 191        24.2      L          L   OUTSIDE RANGE           
REMARK 500    THR F   7        25.0      L          L   OUTSIDE RANGE           
REMARK 500    SER F  11        23.4      L          L   OUTSIDE RANGE           
REMARK 500    LYS F  72        23.6      L          L   OUTSIDE RANGE           
REMARK 500    ASP F 361        20.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1404  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 243   OE1                                                    
REMARK 620 2 ASP A 247   O    75.0                                              
REMARK 620 3 THR A 250   O    71.9  90.6                                        
REMARK 620 4 ASP A 245   OD1 119.8 102.3 164.4                                  
REMARK 620 5 THR A 250   OG1 143.9  84.7  79.0  93.2                            
REMARK 620 6 GLU A 252   OE1 120.0 163.5  88.4  76.7  79.0                      
REMARK 620 7 GLU A 252   OE2  82.8 152.8  97.5  75.1 122.4  43.4                
REMARK 620 8 GLU A 243   OE2  51.0  80.7 122.6  69.0 153.7 113.6  73.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1405  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 299   OD1                                                    
REMARK 620 2 ASP A 305   OD1 117.0                                              
REMARK 620 3 ASP A 305   OD2  89.3  53.0                                        
REMARK 620 4 ASP A 297   OD1  72.1 135.5  85.5                                  
REMARK 620 5 ASP A 301   OD1  74.1 143.9 160.7  80.1                            
REMARK 620 6 ASP A 301   OD2  53.5 112.5 131.3 107.0  44.0                      
REMARK 620 7 ARG A 303   O   148.6  93.1 103.3  80.2  87.0 125.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1406  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 373   OD1                                                    
REMARK 620 2 ASP A 367   OD1  97.9                                              
REMARK 620 3 ASP A 365   OD1 147.0  98.7                                        
REMARK 620 4 TYR A 371   O    87.4 164.0  84.4                                  
REMARK 620 5 ASP A 373   OD2  48.1 104.0 100.1  90.7                            
REMARK 620 6 ASP A 369   OD1 124.2  72.4  88.0  92.1 171.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1407  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 434   OD1                                                    
REMARK 620 2 ASP A 428   OD1 103.2                                              
REMARK 620 3 ASP A 434   OD2  49.3  91.6                                        
REMARK 620 4 ASP A 426   OD1 141.6  72.0  92.3                                  
REMARK 620 5 ASP A 428   OD2  74.9  45.1  98.7 116.1                            
REMARK 620 6 ASN A 430   OD1 139.7  81.3 169.6  78.4  81.6                      
REMARK 620 7 TYR A 432   O   103.8 141.7  86.0  69.9 172.0  95.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAC B1301   O2                                                     
REMARK 620 2 HOH B1405   O   152.7                                              
REMARK 620 3 GLU B 220   OE1  99.1 104.4                                        
REMARK 620 4 HOH B1404   O   100.6  95.7  83.9                                  
REMARK 620 5 SER B 121   OG   82.5  84.8  87.4 171.1                            
REMARK 620 6 SER B 123   OG   75.4  88.4 155.1  73.5 115.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 127   OD1                                                    
REMARK 620 2 ASP B 127   OD2  40.8                                              
REMARK 620 3 SER B 123   O    80.4 118.4                                        
REMARK 620 4 ASP B 126   OD1  99.4  97.5  70.9                                  
REMARK 620 5 ASP B 126   OD2  92.9  65.7 113.0  44.3                            
REMARK 620 6 ASP B 251   OD2  88.5 112.5  72.7 140.8 174.3                      
REMARK 620 7 HOH B1406   O   156.1 160.8  80.8  88.1 107.9  72.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1403  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 158   OD2                                                    
REMARK 620 2 ASN B 215   OD1  96.3                                              
REMARK 620 3 ASP B 217   O   170.5  90.8                                        
REMARK 620 4 ASP B 217   OD1  99.0  95.4  74.1                                  
REMARK 620 5 GLU B 220   OE2  89.8  78.4  97.7 169.8                            
REMARK 620 6 PRO B 219   O    92.6 159.0  82.7 101.9  82.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1411  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 252   OE1                                                    
REMARK 620 2 ASP C 245   OD1  73.9                                              
REMARK 620 3 ASP C 247   O   150.9 100.4                                        
REMARK 620 4 THR C 250   OG1  75.6  80.1  75.3                                  
REMARK 620 5 GLU C 243   OE1 118.2  89.9  89.9 160.2                            
REMARK 620 6 GLU C 243   OE2 115.7 141.3  86.9 137.9  51.9                      
REMARK 620 7 THR C 250   O    84.4 148.7  87.8  72.8 120.5  68.6                
REMARK 620 8 GLU C 252   OE2  39.5  88.9 167.9 114.2  82.4  81.1  88.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1412  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 305   OD2                                                    
REMARK 620 2 ASN C 299   OD1  81.7                                              
REMARK 620 3 ASP C 301   OD2 155.6  82.6                                        
REMARK 620 4 ASP C 301   OD1 142.4  70.5  44.8                                  
REMARK 620 5 ASP C 297   OD1  75.1  68.7 116.0  71.5                            
REMARK 620 6 ASP C 305   OD1  56.2 109.2 112.7 157.4 130.3                      
REMARK 620 7 ARG C 303   O    96.4 140.3 107.6  89.7  72.5 102.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1413  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 365   OD1                                                    
REMARK 620 2 ASP C 367   OD1  92.3                                              
REMARK 620 3 ASP C 369   OD1  84.9  73.8                                        
REMARK 620 4 TYR C 371   O    91.1 162.0  88.9                                  
REMARK 620 5 ASP C 373   OD2 103.9  84.5 157.0 111.7                            
REMARK 620 6 ASP C 373   OD1 146.7 102.4 127.8  84.0  49.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1414  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 434   OD1                                                    
REMARK 620 2 ASP C 434   OD2  48.8                                              
REMARK 620 3 TYR C 432   O    98.3  96.1                                        
REMARK 620 4 ASN C 430   OD1 143.4 160.7  95.8                                  
REMARK 620 5 ASP C 428   OD1 100.1  85.0 156.3  78.1                            
REMARK 620 6 ASP C 426   OD1 136.7  87.9  84.3  78.2  72.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1408  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAC D1302   O2                                                     
REMARK 620 2 SER D 123   OG   80.6                                              
REMARK 620 3 SER D 121   OG   71.7  96.5                                        
REMARK 620 4 GLU D 220   OE1  93.7 163.7  96.2                                  
REMARK 620 5 HOH D1412   O   154.0  83.0  90.4 107.1                            
REMARK 620 6 HOH D1411   O   105.3  82.4 177.0  84.5  92.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D1409  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 126   OD1                                                    
REMARK 620 2 ASP D 126   OD2  43.7                                              
REMARK 620 3 SER D 123   O    76.2 118.5                                        
REMARK 620 4 ASP D 127   OD1  88.2 102.0  84.5                                  
REMARK 620 5 ASP D 251   OD2 148.3 167.1  72.3  85.5                            
REMARK 620 6 HOH D1413   O   122.8 106.6  94.3 147.9  63.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D1410  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 220   OE2                                                    
REMARK 620 2 ASN D 215   OD1  84.8                                              
REMARK 620 3 ASP D 217   O    97.6  93.3                                        
REMARK 620 4 PRO D 219   O    92.3 169.9  77.5                                  
REMARK 620 5 ASP D 217   OD1 163.3  86.9  68.4  93.4                            
REMARK 620 6 ASP D 158   OD2  98.0 102.9 158.4  87.1  98.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E1418  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR E 250   OG1                                                    
REMARK 620 2 GLU E 243   OE1 145.9                                              
REMARK 620 3 ASP E 247   O    91.1  70.4                                        
REMARK 620 4 THR E 250   O    77.2  72.3  82.8                                  
REMARK 620 5 ASP E 245   OD1  87.7 124.5 106.6 162.4                            
REMARK 620 6 GLU E 243   OE2 157.0  51.4  82.8 123.6  73.1                      
REMARK 620 7 GLU E 252   OE2 110.2  88.0 157.8  95.7  81.1  79.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E1419  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN E 299   OD1                                                    
REMARK 620 2 ASP E 305   OD2  85.9                                              
REMARK 620 3 ASP E 297   OD1  72.3  82.8                                        
REMARK 620 4 ASP E 305   OD1 109.2  57.3 139.3                                  
REMARK 620 5 ASP E 301   OD2  81.9 153.1 115.8 104.5                            
REMARK 620 6 ARG E 303   O   153.5  99.8  82.7  95.4 101.8                      
REMARK 620 7 ASP E 301   OD1  73.6 150.7  71.3 149.4  44.9  90.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E1420  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 373   OD2                                                    
REMARK 620 2 ASP E 365   OD1  97.7                                              
REMARK 620 3 TYR E 371   O   104.2  94.1                                        
REMARK 620 4 ASP E 369   OD1 167.2  78.0  88.3                                  
REMARK 620 5 ASP E 367   OD1  91.1  76.8 163.3  76.2                            
REMARK 620 6 ASP E 373   OD1  50.7 148.2  91.6 133.5 103.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E1421  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 426   OD1                                                    
REMARK 620 2 ASP E 428   OD1  92.9                                              
REMARK 620 3 ASN E 430   OD1  80.6  79.8                                        
REMARK 620 4 TYR E 432   O    70.2 162.9  94.4                                  
REMARK 620 5 ASP E 434   OD1 146.5  99.3 132.1  96.5                            
REMARK 620 6 ASP E 434   OD2  95.9  92.0 170.9  92.3  53.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F1415  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAC F1303   O2                                                     
REMARK 620 2 HOH F1419   O   151.8                                              
REMARK 620 3 GLU F 220   OE1 104.4 103.7                                        
REMARK 620 4 SER F 123   OG   76.3  80.7 150.6                                  
REMARK 620 5 SER F 121   OG   81.9  90.1 100.9 108.2                            
REMARK 620 6 HOH F1418   O    97.5  91.5  77.0  73.9 177.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F1416  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 126   OD1                                                    
REMARK 620 2 SER F 123   O    94.2                                              
REMARK 620 3 ASP F 127   OD1  93.8  82.6                                        
REMARK 620 4 ASP F 251   OD2 155.3  62.5  75.9                                  
REMARK 620 5 HOH F1420   O   101.3  82.7 159.6  84.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F1417  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 217   O                                                      
REMARK 620 2 ASP F 217   OD1  72.0                                              
REMARK 620 3 PRO F 219   O    82.5  93.1                                        
REMARK 620 4 ASP F 158   OD2 159.8  89.7  90.3                                  
REMARK 620 5 GLU F 220   OE2 103.6 173.1  91.4  95.4                            
REMARK 620 6 ASN F 215   OD1  93.4  86.4 175.8  93.8  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 1008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D 1010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D 1012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 1013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E 1014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F 1015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F 1016                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F 1017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN F 1018                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA F 1019                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F 1020                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC B 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC D 1302                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC F 1303                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 1409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 1410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 1415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 1416                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 1417                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 1418                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 1419                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 1420                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 1421                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1TXV   RELATED DB: PDB                                   
REMARK 900 NON-DRUG BOUND HIGHER RESOLUTION STRUCTURE COMPLEXED WITH            
REMARK 900 10E5 FAB                                                             
REMARK 900 RELATED ID: 1TY3   RELATED DB: PDB                                   
REMARK 900 NON-DRUG BOUND STRUCTURE COMPLEXED WITH 10E5 FAB                     
REMARK 900 RELATED ID: 1TY5   RELATED DB: PDB                                   
REMARK 900 TIROFIBAN BOUND STRUCTURE COMPLEXED WITH 10E5 FAB                    
REMARK 900 RELATED ID: 1TY6   RELATED DB: PDB                                   
REMARK 900 EPTIFIBATIDE BOUND STRUCTURE COMPLEXED WITH 10E5 FAB                 
REMARK 900 RELATED ID: 1TY7   RELATED DB: PDB                                   
REMARK 900 MERCK COMPOUND L739758 BOUND STRUCTURE COMPLEXED WITH 10E5           
REMARK 900 FAB                                                                  
DBREF  1TYE A    1   452  UNP    P08514   ITAB_HUMAN      32    483             
DBREF  1TYE C    1   452  UNP    P08514   ITAB_HUMAN      32    483             
DBREF  1TYE E    1   452  UNP    P08514   ITAB_HUMAN      32    483             
DBREF  1TYE B    1   440  UNP    P05106   ITB3_HUMAN      27    466             
DBREF  1TYE D    1   440  UNP    P05106   ITB3_HUMAN      27    466             
DBREF  1TYE F    1   440  UNP    P05106   ITB3_HUMAN      27    466             
SEQRES   1 A  452  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  452  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  452  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  452  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  452  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  452  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  452  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  452  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  452  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  452  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  452  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  452  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  452  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  452  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  452  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  452  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  452  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  452  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  452  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  452  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  452  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  452  TYR GLN ARG LEU HIS ARG LEU ARG ALA GLU GLN MET ALA          
SEQRES  23 A  452  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  452  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  452  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  452  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  452  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  452  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  452  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  452  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  452  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  452  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  452  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  452  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  452  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO                      
SEQRES   1 B  440  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  440  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  440  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  440  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  440  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  440  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  440  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  440  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  440  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  440  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  440  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  440  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  440  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  440  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  440  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  440  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  440  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  440  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  440  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  440  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  440  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  440  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  440  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  440  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  440  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  440  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  440  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  440  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  440  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  440  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  440  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  440  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  440  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  440  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN                  
SEQRES   1 C  452  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 C  452  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 C  452  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 C  452  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 C  452  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 C  452  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 C  452  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 C  452  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 C  452  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 C  452  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 C  452  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 C  452  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 C  452  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 C  452  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 C  452  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 C  452  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 C  452  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 C  452  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 C  452  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 C  452  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 C  452  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 C  452  TYR GLN ARG LEU HIS ARG LEU ARG ALA GLU GLN MET ALA          
SEQRES  23 C  452  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 C  452  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 C  452  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 C  452  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 C  452  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 C  452  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 C  452  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 C  452  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 C  452  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 C  452  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 C  452  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 C  452  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 C  452  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO                      
SEQRES   1 D  440  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 D  440  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 D  440  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 D  440  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 D  440  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 D  440  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 D  440  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 D  440  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 D  440  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 D  440  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 D  440  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 D  440  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 D  440  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 D  440  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 D  440  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 D  440  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 D  440  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 D  440  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 D  440  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 D  440  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 D  440  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 D  440  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 D  440  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 D  440  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 D  440  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 D  440  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 D  440  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 D  440  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 D  440  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 D  440  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 D  440  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 D  440  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 D  440  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 D  440  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN                  
SEQRES   1 E  452  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 E  452  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 E  452  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 E  452  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 E  452  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 E  452  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 E  452  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 E  452  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 E  452  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 E  452  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 E  452  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 E  452  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 E  452  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 E  452  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 E  452  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 E  452  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 E  452  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 E  452  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 E  452  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 E  452  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 E  452  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 E  452  TYR GLN ARG LEU HIS ARG LEU ARG ALA GLU GLN MET ALA          
SEQRES  23 E  452  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 E  452  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 E  452  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 E  452  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 E  452  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 E  452  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 E  452  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 E  452  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 E  452  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 E  452  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 E  452  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 E  452  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 E  452  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO                      
SEQRES   1 F  440  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 F  440  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 F  440  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 F  440  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 F  440  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 F  440  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 F  440  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 F  440  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 F  440  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 F  440  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 F  440  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 F  440  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 F  440  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 F  440  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 F  440  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 F  440  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 F  440  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 F  440  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 F  440  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 F  440  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 F  440  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 F  440  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 F  440  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 F  440  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 F  440  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 F  440  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 F  440  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 F  440  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 F  440  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 F  440  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 F  440  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 F  440  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 F  440  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 F  440  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN                  
MODRES 1TYE ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 1TYE ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 1TYE ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 1TYE ASN D   99  ASN  GLYCOSYLATION SITE                                 
MODRES 1TYE ASN D  320  ASN  GLYCOSYLATION SITE                                 
MODRES 1TYE ASN D  371  ASN  GLYCOSYLATION SITE                                 
MODRES 1TYE ASN E   15  ASN  GLYCOSYLATION SITE                                 
MODRES 1TYE ASN F   99  ASN  GLYCOSYLATION SITE                                 
MODRES 1TYE ASN F  320  ASN  GLYCOSYLATION SITE                                 
MODRES 1TYE ASN F  371  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B1001      14                                                       
HET    NAG  B1002      14                                                       
HET    NAG  B1003      14                                                       
HET    MAN  B1004      11                                                       
HET    BMA  B1005      11                                                       
HET    NAG  B1006      14                                                       
HET    NAG  D1007      14                                                       
HET    NAG  D1008      14                                                       
HET    NAG  D1009      14                                                       
HET    MAN  D1010      11                                                       
HET    BMA  D1011      11                                                       
HET    MAN  D1012      11                                                       
HET    NAG  D1013      14                                                       
HET    NAG  E1014      14                                                       
HET    NAG  F1015      14                                                       
HET    NAG  F1016      14                                                       
HET    NAG  F1017      14                                                       
HET    MAN  F1018      11                                                       
HET    BMA  F1019      11                                                       
HET    NAG  F1020      14                                                       
HET    CAC  B1301       5                                                       
HET    CAC  D1302       5                                                       
HET    CAC  F1303       5                                                       
HET     MG  B1401       1                                                       
HET     CA  B1402       1                                                       
HET     CA  B1403       1                                                       
HET     CA  A1404       1                                                       
HET     CA  A1405       1                                                       
HET     CA  A1406       1                                                       
HET     CA  A1407       1                                                       
HET     MG  D1408       1                                                       
HET     CA  D1409       1                                                       
HET     CA  D1410       1                                                       
HET     CA  C1411       1                                                       
HET     CA  C1412       1                                                       
HET     CA  C1413       1                                                       
HET     CA  C1414       1                                                       
HET     MG  F1415       1                                                       
HET     CA  F1416       1                                                       
HET     CA  F1417       1                                                       
HET     CA  E1418       1                                                       
HET     CA  E1419       1                                                       
HET     CA  E1420       1                                                       
HET     CA  E1421       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     CAC CACODYLATE ION                                                   
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CA CALCIUM ION                                                      
HETSYN     CAC DIMETHYLARSINATE                                                 
FORMUL   7  NAG    13(C8 H15 N O6)                                              
FORMUL   8  MAN    4(C6 H12 O6)                                                 
FORMUL   8  BMA    3(C6 H12 O6)                                                 
FORMUL  17  CAC    3(C2 H6 AS O2 1-)                                            
FORMUL  20   MG    3(MG 2+)                                                     
FORMUL  21   CA    18(CA 2+)                                                    
FORMUL  41  HOH   *120(H2 O)                                                    
HELIX    1   1 LEU A  151  ASP A  159  1                                   9    
HELIX    2   2 GLY A  187  LEU A  192  1                                   6    
HELIX    3   3 VAL A  200  TYR A  207  1                                   8    
HELIX    4   4 ASN A  227  PHE A  231  5                                   5    
HELIX    5   5 THR A  259  LEU A  264  1                                   6    
HELIX    6   6 TYR A  440  ALA A  442  5                                   3    
HELIX    7   7 SER B   12  ALA B   18  1                                   7    
HELIX    8   8 LEU B   40  ASP B   47  1                                   8    
HELIX    9   9 SER B  121  ASP B  126  5                                   6    
HELIX   10  10 ASP B  127  THR B  146  1                                  20    
HELIX   11  11 PRO B  169  GLU B  174  5                                   6    
HELIX   12  12 ASN B  175  LYS B  181  5                                   7    
HELIX   13  13 GLN B  199  LYS B  208  1                                  10    
HELIX   14  14 GLY B  221  CYS B  232  1                                  12    
HELIX   15  15 CYS B  232  GLY B  237  1                                   6    
HELIX   16  16 LEU B  258  GLY B  264  5                                   7    
HELIX   17  17 TYR B  281  THR B  286  5                                   6    
HELIX   18  18 SER B  291  LYS B  302  1                                  12    
HELIX   19  19 VAL B  314  LEU B  324  1                                  11    
HELIX   20  20 SER B  337  LYS B  350  1                                  14    
HELIX   21  21 LEU C  151  ASP C  159  1                                   9    
HELIX   22  22 GLY C  187  LEU C  192  1                                   6    
HELIX   23  23 VAL C  200  TYR C  207  1                                   8    
HELIX   24  24 THR C  259  LEU C  264  1                                   6    
HELIX   25  25 SER D   12  SER D   20  1                                   9    
HELIX   26  26 LYS D   41  ASP D   47  1                                   7    
HELIX   27  27 ALA D   50  GLU D   52  5                                   3    
HELIX   28  28 SER D  121  LYS D  125  5                                   5    
HELIX   29  29 ASP D  127  LYS D  144  1                                  18    
HELIX   30  30 PRO D  169  GLU D  174  5                                   6    
HELIX   31  31 CYS D  177  LYS D  181  5                                   5    
HELIX   32  32 GLN D  199  LYS D  209  1                                  11    
HELIX   33  33 GLY D  221  CYS D  232  1                                  12    
HELIX   34  34 CYS D  232  GLY D  237  1                                   6    
HELIX   35  35 ASP D  259  GLY D  264  5                                   6    
HELIX   36  36 TYR D  281  THR D  286  5                                   6    
HELIX   37  37 SER D  291  LYS D  302  1                                  12    
HELIX   38  38 VAL D  314  GLU D  323  1                                  10    
HELIX   39  39 SER D  337  GLY D  349  1                                  13    
HELIX   40  40 GLY E   44  GLU E   48  5                                   5    
HELIX   41  41 LEU E  151  ASP E  159  1                                   9    
HELIX   42  42 GLY E  187  LEU E  192  1                                   6    
HELIX   43  43 VAL E  200  TYR E  207  1                                   8    
HELIX   44  44 ASN E  227  PHE E  231  5                                   5    
HELIX   45  45 THR E  259  LEU E  264  1                                   6    
HELIX   46  46 ASN F    3  ARG F    8  1                                   6    
HELIX   47  47 SER F   12  LEU F   17  1                                   6    
HELIX   48  48 SER F  121  ASP F  126  5                                   6    
HELIX   49  49 ASP F  127  LYS F  144  1                                  18    
HELIX   50  50 PRO F  169  GLU F  174  5                                   6    
HELIX   51  51 CYS F  177  LYS F  181  5                                   5    
HELIX   52  52 GLN F  199  LYS F  208  1                                  10    
HELIX   53  53 GLY F  221  CYS F  232  1                                  12    
HELIX   54  54 CYS F  232  GLY F  237  1                                   6    
HELIX   55  55 LEU F  258  GLY F  264  5                                   7    
HELIX   56  56 SER F  291  LYS F  302  1                                  12    
HELIX   57  57 VAL F  314  ILE F  325  1                                  12    
HELIX   58  58 SER F  337  GLY F  349  1                                  13    
SHEET    1   A 5 GLY A  62  GLY A  63  0                                        
SHEET    2   A 5 THR A   9  ALA A  12  1  N  PHE A  10   O  GLY A  63           
SHEET    3   A 5 GLN A 444  TYR A 448 -1  O  VAL A 447   N  THR A   9           
SHEET    4   A 5 ASP A 434  ALA A 439 -1  N  VAL A 437   O  ALA A 446           
SHEET    5   A 5 SER A 420  VAL A 425 -1  N  ARG A 422   O  ILE A 436           
SHEET    1   B 4 LEU A  23  HIS A  26  0                                        
SHEET    2   B 4 ALA A  34  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3   B 4 GLY A  52  PRO A  57 -1  O  PHE A  54   N  VAL A  37           
SHEET    4   B 4 SER A  67  LEU A  68 -1  O  LEU A  68   N  VAL A  53           
SHEET    1   C 4 GLU A  75  VAL A  79  0                                        
SHEET    2   C 4 GLN A  82  PHE A  87 -1  O  LEU A  84   N  ARG A  77           
SHEET    3   C 4 HIS A 112  GLU A 117 -1  O  ASN A 114   N  GLN A  85           
SHEET    4   C 4 GLU A 120  GLU A 121 -1  O  GLU A 120   N  GLU A 117           
SHEET    1   D 4 GLU A  75  VAL A  79  0                                        
SHEET    2   D 4 GLN A  82  PHE A  87 -1  O  LEU A  84   N  ARG A  77           
SHEET    3   D 4 HIS A 112  GLU A 117 -1  O  ASN A 114   N  GLN A  85           
SHEET    4   D 4 THR A 125  PRO A 126 -1  O  THR A 125   N  TRP A 113           
SHEET    1   E 4 VAL A  97  TRP A 100  0                                        
SHEET    2   E 4 VAL A 103  ALA A 108 -1  O  VAL A 103   N  TRP A 100           
SHEET    3   E 4 SER A 129  GLN A 134 -1  O  PHE A 131   N  ALA A 106           
SHEET    4   E 4 ARG A 139  TYR A 143 -1  O  TYR A 143   N  CYS A 130           
SHEET    1   F 4 SER A 172  VAL A 175  0                                        
SHEET    2   F 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3   F 4 LEU A 194  PRO A 199 -1  O  ALA A 196   N  LEU A 183           
SHEET    4   F 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1   G 4 VAL A 239  GLY A 242  0                                        
SHEET    2   G 4 GLU A 252  ALA A 257 -1  O  VAL A 254   N  ALA A 240           
SHEET    3   G 4 ALA A 266  LEU A 270 -1  O  LEU A 270   N  TYR A 253           
SHEET    4   G 4 ARG A 276  ARG A 281 -1  O  LEU A 277   N  ILE A 269           
SHEET    1   H 4 VAL A 293  THR A 296  0                                        
SHEET    2   H 4 ASP A 305  GLY A 309 -1  O  LEU A 307   N  ALA A 294           
SHEET    3   H 4 ARG A 327  PHE A 331 -1  O  PHE A 331   N  LEU A 306           
SHEET    4   H 4 LEU A 345  THR A 348 -1  O  LEU A 347   N  VAL A 328           
SHEET    1   I 2 MET A 314  ARG A 317  0                                        
SHEET    2   I 2 LYS A 321  GLU A 324 -1  O  ALA A 323   N  GLU A 315           
SHEET    1   J 4 ILE A 360  PRO A 362  0                                        
SHEET    2   J 4 ILE A 374  ALA A 378 -1  O  ALA A 375   N  ALA A 361           
SHEET    3   J 4 GLN A 388  PHE A 392 -1  O  LEU A 390   N  VAL A 376           
SHEET    4   J 4 GLN A 405  ASP A 408 -1  O  GLN A 405   N  VAL A 391           
SHEET    1   K 6 ARG B  62  GLU B  65  0                                        
SHEET    2   K 6 ARG B  87  LEU B  92 -1  O  ALA B  89   N  ARG B  62           
SHEET    3   K 6 LEU B 425  PHE B 431  1  O  GLN B 428   N  LEU B  90           
SHEET    4   K 6 GLU B 411  PRO B 418 -1  N  PHE B 414   O  VAL B 427           
SHEET    5   K 6 SER B 353  ARG B 360 -1  N  ARG B 360   O  THR B 415           
SHEET    6   K 6 SER B 385  LEU B 389 -1  O  LEU B 389   N  SER B 353           
SHEET    1   L 4 SER B  97  ARG B 105  0                                        
SHEET    2   L 4 THR B 394  VAL B 403 -1  O  VAL B 395   N  VAL B 104           
SHEET    3   L 4 LEU B 366  THR B 373 -1  N  SER B 367   O  LYS B 402           
SHEET    4   L 4 VAL B 379  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1   M 6 TYR B 190  THR B 197  0                                        
SHEET    2   M 6 LEU B 149  PHE B 156 -1  N  ALA B 155   O  LYS B 191           
SHEET    3   M 6 VAL B 112  ASP B 119  1  N  MET B 118   O  GLY B 154           
SHEET    4   M 6 SER B 243  THR B 250  1  O  LEU B 245   N  ASP B 113           
SHEET    5   M 6 ILE B 304  VAL B 310  1  O  ALA B 309   N  PHE B 248           
SHEET    6   M 6 THR B 329  VAL B 332  1  O  GLY B 331   N  PHE B 308           
SHEET    1   N 4 LEU C   8  ALA C  12  0                                        
SHEET    2   N 4 GLN C 444  TYR C 448 -1  O  VAL C 445   N  TYR C  11           
SHEET    3   N 4 ASP C 434  ALA C 439 -1  N  LEU C 435   O  TYR C 448           
SHEET    4   N 4 SER C 420  VAL C 425 -1  N  ARG C 422   O  ILE C 436           
SHEET    1   O 3 LEU C  23  LYS C  27  0                                        
SHEET    2   O 3 VAL C  33  GLY C  38 -1  O  VAL C  36   N  ASP C  24           
SHEET    3   O 3 VAL C  53  PRO C  57 -1  O  CYS C  56   N  ILE C  35           
SHEET    1   P 4 THR C  76  VAL C  79  0                                        
SHEET    2   P 4 GLN C  82  PHE C  87 -1  O  LEU C  84   N  ARG C  77           
SHEET    3   P 4 HIS C 112  GLU C 117 -1  O  HIS C 112   N  PHE C  87           
SHEET    4   P 4 GLU C 120  GLU C 121 -1  O  GLU C 120   N  GLU C 117           
SHEET    1   Q 4 VAL C  97  TRP C 100  0                                        
SHEET    2   Q 4 VAL C 103  ALA C 108 -1  O  VAL C 105   N  VAL C  98           
SHEET    3   Q 4 SER C 129  ALA C 133 -1  O  PHE C 131   N  ALA C 106           
SHEET    4   Q 4 ARG C 140  TYR C 143 -1  O  ALA C 141   N  LEU C 132           
SHEET    1   R 4 SER C 172  VAL C 175  0                                        
SHEET    2   R 4 GLU C 180  ALA C 185 -1  O  VAL C 182   N  VAL C 174           
SHEET    3   R 4 LEU C 194  PRO C 199 -1  O  ALA C 196   N  LEU C 183           
SHEET    4   R 4 SER C 220  LEU C 221 -1  O  SER C 220   N  GLN C 197           
SHEET    1   S 4 VAL C 239  GLY C 242  0                                        
SHEET    2   S 4 GLU C 252  ALA C 257 -1  O  VAL C 254   N  ALA C 240           
SHEET    3   S 4 ALA C 266  ASP C 271 -1  O  LEU C 270   N  TYR C 253           
SHEET    4   S 4 ARG C 276  ARG C 281 -1  O  LEU C 277   N  ILE C 269           
SHEET    1   T 4 VAL C 293  THR C 296  0                                        
SHEET    2   T 4 ASP C 305  ALA C 310 -1  O  ASP C 305   N  THR C 296           
SHEET    3   T 4 ARG C 327  PHE C 331 -1  O  PHE C 331   N  LEU C 306           
SHEET    4   T 4 LEU C 345  THR C 348 -1  O  LEU C 347   N  VAL C 328           
SHEET    1   U 2 MET C 314  ARG C 317  0                                        
SHEET    2   U 2 LYS C 321  GLU C 324 -1  O  ALA C 323   N  GLU C 315           
SHEET    1   V 4 ILE C 360  PRO C 362  0                                        
SHEET    2   V 4 ILE C 374  ALA C 378 -1  O  ALA C 375   N  ALA C 361           
SHEET    3   V 4 GLN C 388  PHE C 392 -1  O  LEU C 390   N  VAL C 376           
SHEET    4   V 4 VAL C 406  ASP C 408 -1  O  LEU C 407   N  VAL C 389           
SHEET    1   W 2 GLY C 394  GLN C 395  0                                        
SHEET    2   W 2 GLY C 398  LEU C 399 -1  O  GLY C 398   N  GLN C 395           
SHEET    1   X 3 CYS D  38  LEU D  40  0                                        
SHEET    2   X 3 CYS D  23  CYS D  26 -1  N  ALA D  24   O  ASP D  39           
SHEET    3   X 3 ILE D  54  GLU D  55 -1  O  GLU D  55   N  TRP D  25           
SHEET    1   Y 6 ARG D  62  GLU D  65  0                                        
SHEET    2   Y 6 ARG D  87  LEU D  92 -1  O  ALA D  89   N  ARG D  62           
SHEET    3   Y 6 LEU D 425  PHE D 431  1  O  GLN D 428   N  ILE D  88           
SHEET    4   Y 6 GLU D 411  PRO D 418 -1  N  PHE D 414   O  VAL D 427           
SHEET    5   Y 6 SER D 353  ARG D 360 -1  N  ARG D 360   O  THR D 415           
SHEET    6   Y 6 SER D 385  LEU D 389 -1  O  LEU D 389   N  SER D 353           
SHEET    1   Z 4 SER D  97  ARG D 105  0                                        
SHEET    2   Z 4 THR D 394  VAL D 403 -1  O  VAL D 395   N  VAL D 104           
SHEET    3   Z 4 LEU D 366  THR D 373 -1  N  SER D 367   O  LYS D 402           
SHEET    4   Z 4 VAL D 379  PRO D 381 -1  O  ILE D 380   N  ALA D 372           
SHEET    1  AA 6 TYR D 190  THR D 197  0                                        
SHEET    2  AA 6 LEU D 149  PHE D 156 -1  N  ILE D 151   O  THR D 197           
SHEET    3  AA 6 VAL D 112  ASP D 119  1  N  MET D 118   O  GLY D 154           
SHEET    4  AA 6 SER D 243  THR D 250  1  O  SER D 243   N  ASP D 113           
SHEET    5  AA 6 ILE D 304  THR D 311  1  O  ALA D 309   N  PHE D 248           
SHEET    6  AA 6 THR D 329  LEU D 333  1  O  THR D 329   N  PHE D 308           
SHEET    1  AB 5 GLY E  63  GLN E  64  0                                        
SHEET    2  AB 5 THR E   9  ALA E  12  1  N  PHE E  10   O  GLY E  63           
SHEET    3  AB 5 GLN E 444  TYR E 448 -1  O  VAL E 447   N  THR E   9           
SHEET    4  AB 5 ASP E 434  ALA E 439 -1  N  LEU E 435   O  TYR E 448           
SHEET    5  AB 5 SER E 420  VAL E 425 -1  N  ARG E 422   O  ILE E 436           
SHEET    1  AC 3 LEU E  23  LYS E  27  0                                        
SHEET    2  AC 3 VAL E  33  GLY E  38 -1  O  ALA E  34   N  HIS E  26           
SHEET    3  AC 3 VAL E  53  PRO E  57 -1  O  CYS E  56   N  ILE E  35           
SHEET    1  AD 4 GLU E  75  VAL E  79  0                                        
SHEET    2  AD 4 GLN E  82  PHE E  87 -1  O  LEU E  84   N  ARG E  77           
SHEET    3  AD 4 HIS E 112  GLU E 117 -1  O  HIS E 112   N  PHE E  87           
SHEET    4  AD 4 GLU E 120  GLU E 121 -1  O  GLU E 120   N  GLU E 117           
SHEET    1  AE 4 GLU E  75  VAL E  79  0                                        
SHEET    2  AE 4 GLN E  82  PHE E  87 -1  O  LEU E  84   N  ARG E  77           
SHEET    3  AE 4 HIS E 112  GLU E 117 -1  O  HIS E 112   N  PHE E  87           
SHEET    4  AE 4 THR E 125  PRO E 126 -1  O  THR E 125   N  TRP E 113           
SHEET    1  AF 4 VAL E  97  TRP E 100  0                                        
SHEET    2  AF 4 VAL E 103  ALA E 108 -1  O  VAL E 103   N  TRP E 100           
SHEET    3  AF 4 SER E 129  ALA E 133 -1  O  SER E 129   N  ALA E 108           
SHEET    4  AF 4 ARG E 140  TYR E 143 -1  O  ALA E 141   N  LEU E 132           
SHEET    1  AG 4 SER E 173  VAL E 175  0                                        
SHEET    2  AG 4 GLU E 180  ALA E 185 -1  O  VAL E 182   N  VAL E 174           
SHEET    3  AG 4 LEU E 194  PRO E 199 -1  O  ALA E 196   N  LEU E 183           
SHEET    4  AG 4 SER E 220  LEU E 221 -1  O  SER E 220   N  GLN E 197           
SHEET    1  AH 4 VAL E 239  GLY E 242  0                                        
SHEET    2  AH 4 GLU E 252  ALA E 257 -1  O  VAL E 254   N  ALA E 240           
SHEET    3  AH 4 ALA E 266  LEU E 270 -1  O  ALA E 266   N  ALA E 257           
SHEET    4  AH 4 ARG E 276  ARG E 281 -1  O  LEU E 277   N  ILE E 269           
SHEET    1  AI 4 VAL E 293  THR E 296  0                                        
SHEET    2  AI 4 ASP E 305  ALA E 310 -1  O  LEU E 307   N  ALA E 294           
SHEET    3  AI 4 ARG E 327  PHE E 331 -1  O  PHE E 331   N  LEU E 306           
SHEET    4  AI 4 LEU E 345  THR E 348 -1  O  LEU E 347   N  VAL E 328           
SHEET    1  AJ 2 MET E 314  ARG E 317  0                                        
SHEET    2  AJ 2 LYS E 321  GLU E 324 -1  O  ALA E 323   N  GLU E 315           
SHEET    1  AK 4 ILE E 360  PRO E 362  0                                        
SHEET    2  AK 4 ILE E 374  ALA E 378 -1  O  ALA E 375   N  ALA E 361           
SHEET    3  AK 4 GLN E 388  PHE E 392 -1  O  PHE E 392   N  ILE E 374           
SHEET    4  AK 4 GLN E 405  ASP E 408 -1  O  LEU E 407   N  VAL E 389           
SHEET    1  AL 2 GLY E 394  GLN E 395  0                                        
SHEET    2  AL 2 GLY E 398  LEU E 399 -1  O  GLY E 398   N  GLN E 395           
SHEET    1  AM 6 ARG F  62  GLU F  65  0                                        
SHEET    2  AM 6 ARG F  87  LEU F  92 -1  O  ALA F  89   N  ARG F  62           
SHEET    3  AM 6 ILE F 426  PHE F 431  1  O  THR F 430   N  LEU F  90           
SHEET    4  AM 6 GLU F 411  VAL F 419 -1  N  PHE F 414   O  VAL F 427           
SHEET    5  AM 6 SER F 353  ARG F 360 -1  N  GLU F 356   O  VAL F 419           
SHEET    6  AM 6 SER F 385  LEU F 389 -1  O  CYS F 386   N  VAL F 355           
SHEET    1  AN 4 SER F  97  ARG F 105  0                                        
SHEET    2  AN 4 THR F 394  VAL F 403 -1  O  VAL F 395   N  VAL F 104           
SHEET    3  AN 4 LEU F 366  THR F 373 -1  N  THR F 373   O  SER F 396           
SHEET    4  AN 4 VAL F 379  PRO F 381 -1  O  ILE F 380   N  ALA F 372           
SHEET    1  AO 6 TYR F 190  THR F 197  0                                        
SHEET    2  AO 6 LEU F 149  PHE F 156 -1  N  ALA F 155   O  LYS F 191           
SHEET    3  AO 6 VAL F 112  ASP F 119  1  N  TYR F 116   O  GLY F 152           
SHEET    4  AO 6 SER F 243  THR F 250  1  O  SER F 243   N  ASP F 113           
SHEET    5  AO 6 ASN F 305  THR F 311  1  O  ALA F 309   N  PHE F 248           
SHEET    6  AO 6 THR F 329  LEU F 333  1  O  GLY F 331   N  PHE F 308           
SSBOND   1 CYS A   56    CYS A   65                          1555   1555  2.04  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.05  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.03  
SSBOND   4 CYS B    5    CYS B   23                          1555   1555  2.03  
SSBOND   5 CYS B   13    CYS B  435                          1555   1555  2.04  
SSBOND   6 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND   7 CYS B   26    CYS B   49                          1555   1555  2.03  
SSBOND   8 CYS B  177    CYS B  184                          1555   1555  2.04  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.04  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.04  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.06  
SSBOND  12 CYS C   56    CYS C   65                          1555   1555  2.03  
SSBOND  13 CYS C  107    CYS C  130                          1555   1555  2.05  
SSBOND  14 CYS C  146    CYS C  167                          1555   1555  2.04  
SSBOND  15 CYS D    5    CYS D   23                          1555   1555  2.03  
SSBOND  16 CYS D   13    CYS D  435                          1555   1555  2.03  
SSBOND  17 CYS D   16    CYS D   38                          1555   1555  2.04  
SSBOND  18 CYS D   26    CYS D   49                          1555   1555  2.02  
SSBOND  19 CYS D  177    CYS D  184                          1555   1555  2.05  
SSBOND  20 CYS D  232    CYS D  273                          1555   1555  2.04  
SSBOND  21 CYS D  374    CYS D  386                          1555   1555  2.03  
SSBOND  22 CYS D  406    CYS D  433                          1555   1555  2.02  
SSBOND  23 CYS E   56    CYS E   65                          1555   1555  2.03  
SSBOND  24 CYS E  107    CYS E  130                          1555   1555  2.05  
SSBOND  25 CYS E  146    CYS E  167                          1555   1555  2.04  
SSBOND  26 CYS F    5    CYS F   23                          1555   1555  1.96  
SSBOND  27 CYS F   13    CYS F  435                          1555   1555  2.05  
SSBOND  28 CYS F   16    CYS F   38                          1555   1555  2.03  
SSBOND  29 CYS F   26    CYS F   49                          1555   1555  2.03  
SSBOND  30 CYS F  177    CYS F  184                          1555   1555  2.05  
SSBOND  31 CYS F  232    CYS F  273                          1555   1555  2.04  
SSBOND  32 CYS F  374    CYS F  386                          1555   1555  2.04  
SSBOND  33 CYS F  406    CYS F  433                          1555   1555  2.03  
LINK         ND2 ASN B  99                 C1  NAG B1001     1555   1555  1.45  
LINK         ND2 ASN B 320                 C1  NAG B1002     1555   1555  1.45  
LINK         ND2 ASN B 371                 C1  NAG B1006     1555   1555  1.45  
LINK         ND2 ASN D  99                 C1  NAG D1007     1555   1555  1.45  
LINK         ND2 ASN D 320                 C1  NAG D1008     1555   1555  1.45  
LINK         ND2 ASN D 371                 C1  NAG D1013     1555   1555  1.45  
LINK         ND2 ASN E  15                 C1  NAG E1014     1555   1555  1.45  
LINK         ND2 ASN F  99                 C1  NAG F1015     1555   1555  1.45  
LINK         ND2 ASN F 320                 C1  NAG F1016     1555   1555  1.45  
LINK         ND2 ASN F 371                 C1  NAG F1020     1555   1555  1.45  
LINK         O4  NAG B1002                 C1  NAG B1003     1555   1555  1.39  
LINK         O4  NAG B1003                 C1  MAN B1004     1555   1555  1.40  
LINK         O3  MAN B1004                 C1  BMA B1005     1555   1555  1.40  
LINK         O4  NAG D1008                 C1  NAG D1009     1555   1555  1.38  
LINK         O4  NAG D1009                 C1  MAN D1010     1555   1555  1.39  
LINK         O3  MAN D1010                 C1  BMA D1011     1555   1555  1.40  
LINK         O6  MAN D1010                 C1  MAN D1012     1555   1555  1.41  
LINK         O4  NAG F1016                 C1  NAG F1017     1555   1555  1.38  
LINK         O4  NAG F1017                 C1  MAN F1018     1555   1555  1.40  
LINK         O3  MAN F1018                 C1  BMA F1019     1555   1555  1.40  
LINK        CA    CA A1404                 OE1 GLU A 243     1555   1555  2.63  
LINK        CA    CA A1404                 O   ASP A 247     1555   1555  2.09  
LINK        CA    CA A1404                 O   THR A 250     1555   1555  2.01  
LINK        CA    CA A1404                 OD1 ASP A 245     1555   1555  2.28  
LINK        CA    CA A1404                 OG1 THR A 250     1555   1555  2.60  
LINK        CA    CA A1404                 OE1 GLU A 252     1555   1555  3.20  
LINK        CA    CA A1404                 OE2 GLU A 252     1555   1555  2.27  
LINK        CA    CA A1404                 OE2 GLU A 243     1555   1555  2.47  
LINK        CA    CA A1405                 OD1 ASN A 299     1555   1555  2.65  
LINK        CA    CA A1405                 OD1 ASP A 305     1555   1555  2.53  
LINK        CA    CA A1405                 OD2 ASP A 305     1555   1555  2.40  
LINK        CA    CA A1405                 OD1 ASP A 297     1555   1555  2.41  
LINK        CA    CA A1405                 OD1 ASP A 301     1555   1555  2.38  
LINK        CA    CA A1405                 OD2 ASP A 301     1555   1555  3.18  
LINK        CA    CA A1405                 O   ARG A 303     1555   1555  2.43  
LINK        CA    CA A1406                 OD1 ASP A 373     1555   1555  2.64  
LINK        CA    CA A1406                 OD1 ASP A 367     1555   1555  2.07  
LINK        CA    CA A1406                 OD1 ASP A 365     1555   1555  2.06  
LINK        CA    CA A1406                 O   TYR A 371     1555   1555  2.12  
LINK        CA    CA A1406                 OD2 ASP A 373     1555   1555  2.76  
LINK        CA    CA A1406                 OD1 ASP A 369     1555   1555  2.65  
LINK        CA    CA A1407                 OD1 ASP A 434     1555   1555  2.67  
LINK        CA    CA A1407                 OD1 ASP A 428     1555   1555  2.20  
LINK        CA    CA A1407                 OD2 ASP A 434     1555   1555  2.62  
LINK        CA    CA A1407                 OD1 ASP A 426     1555   1555  2.67  
LINK        CA    CA A1407                 OD2 ASP A 428     1555   1555  3.10  
LINK        CA    CA A1407                 OD1 ASN A 430     1555   1555  2.35  
LINK        CA    CA A1407                 O   TYR A 432     1555   1555  2.12  
LINK         O2  CAC B1301                MG    MG B1401     1555   1555  1.94  
LINK        MG    MG B1401                 O   HOH B1405     1555   1555  1.92  
LINK        MG    MG B1401                 OE1 GLU B 220     1555   1555  2.12  
LINK        MG    MG B1401                 O   HOH B1404     1555   1555  2.19  
LINK        MG    MG B1401                 OG  SER B 121     1555   1555  2.17  
LINK        MG    MG B1401                 OG  SER B 123     1555   1555  2.17  
LINK        CA    CA B1402                 OD1 ASP B 127     1555   1555  2.22  
LINK        CA    CA B1402                 OD2 ASP B 127     1555   1555  3.33  
LINK        CA    CA B1402                 O   SER B 123     1555   1555  2.38  
LINK        CA    CA B1402                 OD1 ASP B 126     1555   1555  2.70  
LINK        CA    CA B1402                 OD2 ASP B 126     1555   1555  3.09  
LINK        CA    CA B1402                 OD2 ASP B 251     1555   1555  2.69  
LINK        CA    CA B1402                 O   HOH B1406     1555   1555  2.29  
LINK        CA    CA B1403                 OD2 ASP B 158     1555   1555  1.99  
LINK        CA    CA B1403                 OD1 ASN B 215     1555   1555  1.93  
LINK        CA    CA B1403                 O   ASP B 217     1555   1555  2.20  
LINK        CA    CA B1403                 OD1 ASP B 217     1555   1555  2.17  
LINK        CA    CA B1403                 OE2 GLU B 220     1555   1555  2.34  
LINK        CA    CA B1403                 O   PRO B 219     1555   1555  1.99  
LINK        CA    CA C1411                 OE1 GLU C 252     1555   1555  3.39  
LINK        CA    CA C1411                 OD1 ASP C 245     1555   1555  2.06  
LINK        CA    CA C1411                 O   ASP C 247     1555   1555  2.14  
LINK        CA    CA C1411                 OG1 THR C 250     1555   1555  2.69  
LINK        CA    CA C1411                 OE1 GLU C 243     1555   1555  2.73  
LINK        CA    CA C1411                 OE2 GLU C 243     1555   1555  2.15  
LINK        CA    CA C1411                 O   THR C 250     1555   1555  2.45  
LINK        CA    CA C1411                 OE2 GLU C 252     1555   1555  2.18  
LINK        CA    CA C1412                 OD2 ASP C 305     1555   1555  2.22  
LINK        CA    CA C1412                 OD1 ASN C 299     1555   1555  2.22  
LINK        CA    CA C1412                 OD2 ASP C 301     1555   1555  3.10  
LINK        CA    CA C1412                 OD1 ASP C 301     1555   1555  2.15  
LINK        CA    CA C1412                 OD1 ASP C 297     1555   1555  2.35  
LINK        CA    CA C1412                 OD1 ASP C 305     1555   1555  2.45  
LINK        CA    CA C1412                 O   ARG C 303     1555   1555  2.40  
LINK        CA    CA C1413                 OD1 ASP C 365     1555   1555  2.32  
LINK        CA    CA C1413                 OD1 ASP C 367     1555   1555  2.22  
LINK        CA    CA C1413                 OD1 ASP C 369     1555   1555  2.65  
LINK        CA    CA C1413                 O   TYR C 371     1555   1555  2.08  
LINK        CA    CA C1413                 OD2 ASP C 373     1555   1555  2.64  
LINK        CA    CA C1413                 OD1 ASP C 373     1555   1555  2.63  
LINK        CA    CA C1414                 OD1 ASP C 434     1555   1555  2.68  
LINK        CA    CA C1414                 OD2 ASP C 434     1555   1555  2.66  
LINK        CA    CA C1414                 O   TYR C 432     1555   1555  2.01  
LINK        CA    CA C1414                 OD1 ASN C 430     1555   1555  2.28  
LINK        CA    CA C1414                 OD1 ASP C 428     1555   1555  2.20  
LINK        CA    CA C1414                 OD1 ASP C 426     1555   1555  2.46  
LINK         O2  CAC D1302                MG    MG D1408     1555   1555  1.95  
LINK        MG    MG D1408                 OG  SER D 123     1555   1555  2.01  
LINK        MG    MG D1408                 OG  SER D 121     1555   1555  2.25  
LINK        MG    MG D1408                 OE1 GLU D 220     1555   1555  2.02  
LINK        MG    MG D1408                 O   HOH D1412     1555   1555  1.97  
LINK        MG    MG D1408                 O   HOH D1411     1555   1555  2.03  
LINK        CA    CA D1409                 OD1 ASP D 126     1555   1555  2.56  
LINK        CA    CA D1409                 OD2 ASP D 126     1555   1555  3.16  
LINK        CA    CA D1409                 O   SER D 123     1555   1555  2.10  
LINK        CA    CA D1409                 OD1 ASP D 127     1555   1555  2.24  
LINK        CA    CA D1409                 OD2 ASP D 251     1555   1555  2.69  
LINK        CA    CA D1409                 O   HOH D1413     1555   1555  2.64  
LINK        CA    CA D1410                 OE2 GLU D 220     1555   1555  2.49  
LINK        CA    CA D1410                 OD1 ASN D 215     1555   1555  1.98  
LINK        CA    CA D1410                 O   ASP D 217     1555   1555  2.45  
LINK        CA    CA D1410                 O   PRO D 219     1555   1555  1.96  
LINK        CA    CA D1410                 OD1 ASP D 217     1555   1555  2.37  
LINK        CA    CA D1410                 OD2 ASP D 158     1555   1555  2.11  
LINK        CA    CA E1418                 OG1 THR E 250     1555   1555  2.46  
LINK        CA    CA E1418                 OE1 GLU E 243     1555   1555  2.68  
LINK        CA    CA E1418                 O   ASP E 247     1555   1555  2.23  
LINK        CA    CA E1418                 O   THR E 250     1555   1555  2.05  
LINK        CA    CA E1418                 OD1 ASP E 245     1555   1555  2.10  
LINK        CA    CA E1418                 OE2 GLU E 243     1555   1555  2.34  
LINK        CA    CA E1418                 OE2 GLU E 252     1555   1555  2.00  
LINK        CA    CA E1419                 OD1 ASN E 299     1555   1555  2.28  
LINK        CA    CA E1419                 OD2 ASP E 305     1555   1555  2.10  
LINK        CA    CA E1419                 OD1 ASP E 297     1555   1555  2.39  
LINK        CA    CA E1419                 OD1 ASP E 305     1555   1555  2.46  
LINK        CA    CA E1419                 OD2 ASP E 301     1555   1555  3.10  
LINK        CA    CA E1419                 O   ARG E 303     1555   1555  2.23  
LINK        CA    CA E1419                 OD1 ASP E 301     1555   1555  2.12  
LINK        CA    CA E1420                 OD2 ASP E 373     1555   1555  2.61  
LINK        CA    CA E1420                 OD1 ASP E 365     1555   1555  2.24  
LINK        CA    CA E1420                 O   TYR E 371     1555   1555  2.08  
LINK        CA    CA E1420                 OD1 ASP E 369     1555   1555  2.46  
LINK        CA    CA E1420                 OD1 ASP E 367     1555   1555  2.27  
LINK        CA    CA E1420                 OD1 ASP E 373     1555   1555  2.48  
LINK        CA    CA E1421                 OD1 ASP E 426     1555   1555  2.54  
LINK        CA    CA E1421                 OD1 ASP E 428     1555   1555  2.29  
LINK        CA    CA E1421                 OD1 ASN E 430     1555   1555  2.26  
LINK        CA    CA E1421                 O   TYR E 432     1555   1555  2.26  
LINK        CA    CA E1421                 OD1 ASP E 434     1555   1555  2.54  
LINK        CA    CA E1421                 OD2 ASP E 434     1555   1555  2.40  
LINK         O2  CAC F1303                MG    MG F1415     1555   1555  2.03  
LINK        MG    MG F1415                 O   HOH F1419     1555   1555  1.98  
LINK        MG    MG F1415                 OE1 GLU F 220     1555   1555  2.02  
LINK        MG    MG F1415                 OG  SER F 123     1555   1555  2.05  
LINK        MG    MG F1415                 OG  SER F 121     1555   1555  2.05  
LINK        MG    MG F1415                 O   HOH F1418     1555   1555  2.11  
LINK        CA    CA F1416                 OD1 ASP F 126     1555   1555  2.65  
LINK        CA    CA F1416                 O   SER F 123     1555   1555  2.23  
LINK        CA    CA F1416                 OD1 ASP F 127     1555   1555  2.31  
LINK        CA    CA F1416                 OD2 ASP F 251     1555   1555  2.61  
LINK        CA    CA F1416                 O   HOH F1420     1555   1555  2.51  
LINK        CA    CA F1417                 O   ASP F 217     1555   1555  2.28  
LINK        CA    CA F1417                 OD1 ASP F 217     1555   1555  2.44  
LINK        CA    CA F1417                 O   PRO F 219     1555   1555  1.99  
LINK        CA    CA F1417                 OD2 ASP F 158     1555   1555  2.13  
LINK        CA    CA F1417                 OE2 GLU F 220     1555   1555  2.49  
LINK        CA    CA F1417                 OD1 ASN F 215     1555   1555  2.00  
CISPEP   1 SER B  162    PRO B  163          0        -0.44                     
CISPEP   2 SER B  168    PRO B  169          0         0.18                     
CISPEP   3 SER D  162    PRO D  163          0         2.74                     
CISPEP   4 SER D  168    PRO D  169          0         0.56                     
CISPEP   5 SER F  162    PRO F  163          0         0.11                     
CISPEP   6 SER F  168    PRO F  169          0         0.31                     
SITE     1 AC1  2 ASN B  99  PHE B 100                                          
SITE     1 AC2  4 MET A 285  LEU B 317  ASN B 320  NAG B1003                    
SITE     1 AC3  3 ARG A 281  NAG B1002  MAN B1004                               
SITE     1 AC4  2 NAG B1003  BMA B1005                                          
SITE     1 AC5  1 MAN B1004                                                     
SITE     1 AC6  4 SER B 369  ASN B 371  SER B 398  GLU B 400                    
SITE     1 AC7  1 ASN D  99                                                     
SITE     1 AC8  5 MET C 285  ASN D 316  LEU D 317  ASN D 320                    
SITE     2 AC8  5 NAG D1009                                                     
SITE     1 AC9  3 ARG C 281  NAG D1008  MAN D1010                               
SITE     1 BC1  3 NAG D1009  BMA D1011  MAN D1012                               
SITE     1 BC2  1 MAN D1010                                                     
SITE     1 BC3  1 MAN D1010                                                     
SITE     1 BC4  3 ASN D 371  SER D 398  GLU D 400                               
SITE     1 BC5  1 ASN E  15                                                     
SITE     1 BC6  3 ASN F  99  PHE F 100  SER F 101                               
SITE     1 BC7  4 ASN F 316  LEU F 317  ASN F 320  NAG F1017                    
SITE     1 BC8  3 ARG E 281  NAG F1016  MAN F1018                               
SITE     1 BC9  2 NAG F1017  BMA F1019                                          
SITE     1 CC1  1 MAN F1018                                                     
SITE     1 CC2  3 ASN F 371  SER F 398  GLU F 400                               
SITE     1 CC3  8 SER B 121  TYR B 122  SER B 123  ARG B 214                    
SITE     2 CC3  8 ASN B 215  ASP B 217  GLU B 220   MG B1401                    
SITE     1 CC4  8 SER D 121  TYR D 122  SER D 123  ARG D 214                    
SITE     2 CC4  8 ASN D 215  ASP D 217  GLU D 220   MG D1408                    
SITE     1 CC5  8 SER F 121  TYR F 122  SER F 123  ARG F 214                    
SITE     2 CC5  8 ASN F 215  ASP F 217  GLU F 220   MG F1415                    
SITE     1 CC6  6 SER B 121  SER B 123  GLU B 220  CAC B1301                    
SITE     2 CC6  6 HOH B1404  HOH B1405                                          
SITE     1 CC7  5 SER B 123  ASP B 126  ASP B 127  ASP B 251                    
SITE     2 CC7  5 HOH B1406                                                     
SITE     1 CC8  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 CC8  5 GLU B 220                                                     
SITE     1 CC9  5 GLU A 243  ASP A 245  ASP A 247  THR A 250                    
SITE     2 CC9  5 GLU A 252                                                     
SITE     1 DC1  5 ASP A 297  ASN A 299  ASP A 301  ARG A 303                    
SITE     2 DC1  5 ASP A 305                                                     
SITE     1 DC2  5 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 DC2  5 ASP A 373                                                     
SITE     1 DC3  5 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 DC3  5 ASP A 434                                                     
SITE     1 DC4  6 SER D 121  SER D 123  GLU D 220  CAC D1302                    
SITE     2 DC4  6 HOH D1411  HOH D1412                                          
SITE     1 DC5  5 SER D 123  ASP D 126  ASP D 127  ASP D 251                    
SITE     2 DC5  5 HOH D1413                                                     
SITE     1 DC6  5 ASP D 158  ASN D 215  ASP D 217  PRO D 219                    
SITE     2 DC6  5 GLU D 220                                                     
SITE     1 DC7  5 GLU C 243  ASP C 245  ASP C 247  THR C 250                    
SITE     2 DC7  5 GLU C 252                                                     
SITE     1 DC8  5 ASP C 297  ASN C 299  ASP C 301  ARG C 303                    
SITE     2 DC8  5 ASP C 305                                                     
SITE     1 DC9  5 ASP C 365  ASP C 367  ASP C 369  TYR C 371                    
SITE     2 DC9  5 ASP C 373                                                     
SITE     1 EC1  5 ASP C 426  ASP C 428  ASN C 430  TYR C 432                    
SITE     2 EC1  5 ASP C 434                                                     
SITE     1 EC2  6 SER F 121  SER F 123  GLU F 220  CAC F1303                    
SITE     2 EC2  6 HOH F1418  HOH F1419                                          
SITE     1 EC3  5 SER F 123  ASP F 126  ASP F 127  ASP F 251                    
SITE     2 EC3  5 HOH F1420                                                     
SITE     1 EC4  5 ASP F 158  ASN F 215  ASP F 217  PRO F 219                    
SITE     2 EC4  5 GLU F 220                                                     
SITE     1 EC5  5 GLU E 243  ASP E 245  ASP E 247  THR E 250                    
SITE     2 EC5  5 GLU E 252                                                     
SITE     1 EC6  5 ASP E 297  ASN E 299  ASP E 301  ARG E 303                    
SITE     2 EC6  5 ASP E 305                                                     
SITE     1 EC7  5 ASP E 365  ASP E 367  ASP E 369  TYR E 371                    
SITE     2 EC7  5 ASP E 373                                                     
SITE     1 EC8  5 ASP E 426  ASP E 428  ASN E 430  TYR E 432                    
SITE     2 EC8  5 ASP E 434                                                     
CRYST1  332.093  332.093   88.288  90.00  90.00 120.00 P 62         18          
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      0.003011  0.001739  0.000000        0.00000                         
SCALE2      0.000000  0.003477  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011327        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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