GenomeNet

Database: PDB
Entry: 4E0S
LinkDB: 4E0S
Original site: 4E0S 
HEADER    IMMUNE SYSTEM                           05-MAR-12   4E0S              
TITLE     CRYSTAL STRUCTURE OF C5B-6                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COMPLEMENT C5;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING     
COMPND   5 PROTEIN 4, COMPLEMENT C5 BETA CHAIN, COMPLEMENT C5 ALPHA CHAIN, C5A  
COMPND   6 ANAPHYLATOXIN, COMPLEMENT C5 ALPHA' CHAIN;                           
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: COMPLEMENT COMPONENT C6;                                   
COMPND   9 CHAIN: B                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606                                                 
KEYWDS    COMPLEMENT, MAC, IMMUNE SYSTEM                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.E.ALESHIN,B.STEC,R.DISCIPIO,R.C.LIDDINGTON                          
REVDAT   4   15-NOV-17 4E0S    1       REMARK                                   
REVDAT   3   20-JUN-12 4E0S    1       JRNL                                     
REVDAT   2   25-APR-12 4E0S    1       JRNL                                     
REVDAT   1   18-APR-12 4E0S    0                                                
JRNL        AUTH   A.E.ALESHIN,R.G.DISCIPIO,B.STEC,R.C.LIDDINGTON               
JRNL        TITL   CRYSTAL STRUCTURE OF C5B-6 SUGGESTS STRUCTURAL BASIS FOR     
JRNL        TITL 2 PRIMING ASSEMBLY OF THE MEMBRANE ATTACK COMPLEX.             
JRNL        REF    J.BIOL.CHEM.                  V. 287 19642 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22500023                                                     
JRNL        DOI    10.1074/JBC.M112.361121                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.21 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.21                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 81.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 28605                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1529                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 4.21                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 4.32                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1547                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 64.19                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3250                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 106                          
REMARK   3   BIN FREE R VALUE                    : 0.3730                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 19352                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 123                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 120.0                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 166.7                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.24000                                              
REMARK   3    B22 (A**2) : 2.80000                                              
REMARK   3    B33 (A**2) : -5.04000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 1.052         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.736         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 130.772       
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.877                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 19982 ; 0.010 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 27089 ; 1.649 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2443 ; 7.840 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   905 ;34.128 ;24.773       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3457 ;20.486 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    94 ;22.539 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3025 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14960 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    20        A   675                          
REMARK   3    RESIDUE RANGE :   A   768        A   823                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.4050  20.3150  18.0740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3141 T22:   0.2507                                     
REMARK   3      T33:   0.0964 T12:  -0.0556                                     
REMARK   3      T13:  -0.0346 T23:  -0.0910                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0577 L22:   0.5524                                     
REMARK   3      L33:   0.3834 L12:   0.5809                                     
REMARK   3      L13:   0.0305 L23:   0.2051                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0243 S12:   0.1441 S13:  -0.0485                       
REMARK   3      S21:  -0.0425 S22:   0.0380 S23:   0.0809                       
REMARK   3      S31:  -0.1066 S32:   0.2081 S33:  -0.0137                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1515        A  1676                          
REMARK   3    ORIGIN FOR THE GROUP (A): -52.4230 -19.5510  21.0140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3272 T22:   0.3070                                     
REMARK   3      T33:   0.2027 T12:  -0.0540                                     
REMARK   3      T13:  -0.0100 T23:   0.1888                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7456 L22:   4.0857                                     
REMARK   3      L33:   1.9237 L12:   1.5727                                     
REMARK   3      L13:   3.6500 L23:   1.5839                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1397 S12:  -0.2604 S13:  -0.3763                       
REMARK   3      S21:  -0.0794 S22:   0.4744 S23:  -0.1528                       
REMARK   3      S31:  -0.0502 S32:  -0.0364 S33:  -0.3346                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   824        A   932                          
REMARK   3    RESIDUE RANGE :   A  1369        A  1514                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.3910   7.3730  21.9370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3350 T22:   0.1467                                     
REMARK   3      T33:   0.2574 T12:   0.0097                                     
REMARK   3      T13:  -0.0665 T23:  -0.0691                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7017 L22:   1.5263                                     
REMARK   3      L33:   1.7286 L12:  -0.6127                                     
REMARK   3      L13:  -0.2499 L23:   1.0877                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0713 S12:  -0.0157 S13:  -0.1913                       
REMARK   3      S21:  -0.0350 S22:   0.0386 S23:   0.2972                       
REMARK   3      S31:  -0.1612 S32:  -0.0124 S33:  -0.1098                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   933        A  1368                          
REMARK   3    RESIDUE RANGE :   B   591        B   745                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.6960  21.4300  70.8960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4070 T22:   0.0888                                     
REMARK   3      T33:   0.1993 T12:  -0.1609                                     
REMARK   3      T13:   0.0046 T23:  -0.0579                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5642 L22:   0.2601                                     
REMARK   3      L33:   1.2388 L12:   0.2845                                     
REMARK   3      L13:   0.2861 L23:   0.3880                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1076 S12:  -0.0935 S13:   0.0149                       
REMARK   3      S21:   0.0858 S22:  -0.0640 S23:   0.0953                       
REMARK   3      S31:  -0.0982 S32:   0.0964 S33:  -0.0436                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   590                          
REMARK   3    RESIDUE RANGE :   B   750        B   913                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.6870  58.3540  75.9990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4868 T22:   0.0478                                     
REMARK   3      T33:   0.2327 T12:  -0.0999                                     
REMARK   3      T13:  -0.1758 T23:   0.0110                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2514 L22:   0.1233                                     
REMARK   3      L33:   0.0372 L12:  -0.0663                                     
REMARK   3      L13:   0.0871 L23:   0.0028                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0632 S12:   0.0425 S13:   0.0654                       
REMARK   3      S21:   0.0431 S22:   0.0457 S23:  -0.0937                       
REMARK   3      S31:  -0.0057 S32:   0.0230 S33:   0.0175                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4E0S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000071024.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-JAN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 10                                 
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28605                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.0                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.16000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 3IDH, 3PRX, 3T5O                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.08M LITHIUM CHLORIDE, 0.01M            
REMARK 280  IMIDAZOLE-HCL, PH 7.6, SMALL TUBES, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y+1/2,Z                                             
REMARK 290       7555   -X+1/2,Y,-Z                                             
REMARK 290       8555   X,-Y,-Z+1/2                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       79.47450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      139.07850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      113.76450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      139.07850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       79.47450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      113.76450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       79.47450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      113.76450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      139.07850            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      113.76450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       79.47450            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      139.07850            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 120070 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     CYS A     8                                                      
REMARK 465     PHE A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     ILE A    11                                                      
REMARK 465     PHE A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     LYS A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     TRP A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     ARG A   677                                                      
REMARK 465     THR A   678                                                      
REMARK 465     LEU A   679                                                      
REMARK 465     GLN A   680                                                      
REMARK 465     LYS A   681                                                      
REMARK 465     LYS A   682                                                      
REMARK 465     ILE A   683                                                      
REMARK 465     GLU A   684                                                      
REMARK 465     GLU A   685                                                      
REMARK 465     ILE A   686                                                      
REMARK 465     ALA A   687                                                      
REMARK 465     ALA A   688                                                      
REMARK 465     LYS A   689                                                      
REMARK 465     TYR A   690                                                      
REMARK 465     LYS A   691                                                      
REMARK 465     HIS A   692                                                      
REMARK 465     SER A   693                                                      
REMARK 465     VAL A   694                                                      
REMARK 465     VAL A   695                                                      
REMARK 465     LYS A   696                                                      
REMARK 465     LYS A   697                                                      
REMARK 465     CYS A   698                                                      
REMARK 465     CYS A   699                                                      
REMARK 465     TYR A   700                                                      
REMARK 465     ASP A   701                                                      
REMARK 465     GLY A   702                                                      
REMARK 465     ALA A   703                                                      
REMARK 465     CYS A   704                                                      
REMARK 465     VAL A   705                                                      
REMARK 465     ASN A   706                                                      
REMARK 465     ASN A   707                                                      
REMARK 465     ASP A   708                                                      
REMARK 465     GLU A   709                                                      
REMARK 465     THR A   710                                                      
REMARK 465     CYS A   711                                                      
REMARK 465     GLU A   712                                                      
REMARK 465     GLN A   713                                                      
REMARK 465     ARG A   714                                                      
REMARK 465     ALA A   715                                                      
REMARK 465     ALA A   716                                                      
REMARK 465     ARG A   717                                                      
REMARK 465     ILE A   718                                                      
REMARK 465     SER A   719                                                      
REMARK 465     LEU A   720                                                      
REMARK 465     GLY A   721                                                      
REMARK 465     PRO A   722                                                      
REMARK 465     ARG A   723                                                      
REMARK 465     CYS A   724                                                      
REMARK 465     ILE A   725                                                      
REMARK 465     LYS A   726                                                      
REMARK 465     ALA A   727                                                      
REMARK 465     PHE A   728                                                      
REMARK 465     THR A   729                                                      
REMARK 465     GLU A   730                                                      
REMARK 465     CYS A   731                                                      
REMARK 465     CYS A   732                                                      
REMARK 465     VAL A   733                                                      
REMARK 465     VAL A   734                                                      
REMARK 465     ALA A   735                                                      
REMARK 465     SER A   736                                                      
REMARK 465     GLN A   737                                                      
REMARK 465     LEU A   738                                                      
REMARK 465     ARG A   739                                                      
REMARK 465     ALA A   740                                                      
REMARK 465     ASN A   741                                                      
REMARK 465     ILE A   742                                                      
REMARK 465     SER A   743                                                      
REMARK 465     HIS A   744                                                      
REMARK 465     LYS A   745                                                      
REMARK 465     ASP A   746                                                      
REMARK 465     MET A   747                                                      
REMARK 465     GLN A   748                                                      
REMARK 465     LEU A   749                                                      
REMARK 465     GLY A   750                                                      
REMARK 465     ARG A   751                                                      
REMARK 465     LEU A   752                                                      
REMARK 465     HIS A   753                                                      
REMARK 465     MET A   754                                                      
REMARK 465     LYS A   755                                                      
REMARK 465     THR A   756                                                      
REMARK 465     LEU A   757                                                      
REMARK 465     LEU A   758                                                      
REMARK 465     PRO A   759                                                      
REMARK 465     VAL A   760                                                      
REMARK 465     PRO A   871                                                      
REMARK 465     VAL A   872                                                      
REMARK 465     ILE A   873                                                      
REMARK 465     ASP A   874                                                      
REMARK 465     HIS A   875                                                      
REMARK 465     GLN A   876                                                      
REMARK 465     GLY A   877                                                      
REMARK 465     THR A   878                                                      
REMARK 465     LYS A   879                                                      
REMARK 465     SER A   880                                                      
REMARK 465     SER A   881                                                      
REMARK 465     ALA A  1388                                                      
REMARK 465     SER A  1389                                                      
REMARK 465     HIS A  1390                                                      
REMARK 465     TYR A  1391                                                      
REMARK 465     ARG A  1392                                                      
REMARK 465     GLY A  1393                                                      
REMARK 465     TYR A  1394                                                      
REMARK 465     GLY A  1395                                                      
REMARK 465     ASN A  1396                                                      
REMARK 465     SER A  1397                                                      
REMARK 465     SER B   249                                                      
REMARK 465     PHE B   250                                                      
REMARK 465     SER B   251                                                      
REMARK 465     SER B   252                                                      
REMARK 465     GLN B   253                                                      
REMARK 465     GLY B   254                                                      
REMARK 465     GLY B   255                                                      
REMARK 465     SER B   256                                                      
REMARK 465     SER B   257                                                      
REMARK 465     PHE B   258                                                      
REMARK 465     SER B   259                                                      
REMARK 465     THR B   746                                                      
REMARK 465     LYS B   747                                                      
REMARK 465     LEU B   748                                                      
REMARK 465     LYS B   749                                                      
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   O    ALA A  1245     N    MET A  1247              1.96            
REMARK 500   N    ASN B   138     OE2  GLU B   149              2.05            
REMARK 500   NH2  ARG A  1548     OE1  GLU A  1646              2.09            
REMARK 500   NZ   LYS A   842     O    GLY A  1486              2.10            
REMARK 500   OE2  GLU A  1011     OH   TYR A  1059              2.14            
REMARK 500   O    PHE A   912     N    LEU A   923              2.14            
REMARK 500   OD2  ASP B   498     O2   MAN B  1008              2.16            
REMARK 500   ND2  ASN B   303     O5   NAG B  1002              2.18            
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    HIS A 908   CG    HIS A 908   CD2     0.054                       
REMARK 500    HIS B 286   CG    HIS B 286   CD2     0.055                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 191   C   -  N   -  CA  ANGL. DEV. =  12.7 DEGREES          
REMARK 500    PRO A 619   C   -  N   -  CA  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    PRO A 931   C   -  N   -  CA  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    PRO A1410   C   -  N   -  CD  ANGL. DEV. = -15.0 DEGREES          
REMARK 500    PRO B  74   C   -  N   -  CA  ANGL. DEV. = -10.5 DEGREES          
REMARK 500    PRO B 571   C   -  N   -  CA  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    PRO B 571   C   -  N   -  CD  ANGL. DEV. = -26.7 DEGREES          
REMARK 500    PRO B 573   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    CYS B 580   CA  -  CB  -  SG  ANGL. DEV. =   7.0 DEGREES          
REMARK 500    PRO B 732   C   -  N   -  CD  ANGL. DEV. = -15.6 DEGREES          
REMARK 500    CYS B 861   CA  -  CB  -  SG  ANGL. DEV. =   7.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  44       51.15   -118.71                                   
REMARK 500    GLU A  48       98.07    -22.98                                   
REMARK 500    PRO A  60       46.64     17.20                                   
REMARK 500    ASP A  61      115.16    168.03                                   
REMARK 500    LYS A  62       39.35    -83.53                                   
REMARK 500    LYS A  63      -72.11    -66.44                                   
REMARK 500    SER A  74     -175.96    178.66                                   
REMARK 500    ASN A  77       42.88   -107.40                                   
REMARK 500    LYS A  78       40.84     37.46                                   
REMARK 500    PRO A  89       71.38    -37.86                                   
REMARK 500    GLN A  96      122.23    -36.02                                   
REMARK 500    ALA A 155       75.00     65.16                                   
REMARK 500    VAL A 171      -56.70   -140.05                                   
REMARK 500    PRO A 191      177.93    -33.70                                   
REMARK 500    GLU A 207     -175.49    -59.72                                   
REMARK 500    LEU A 224      129.34    -37.63                                   
REMARK 500    ASN A 242       60.31   -110.35                                   
REMARK 500    THR A 261      -75.35    -69.98                                   
REMARK 500    GLN A 284     -179.86    -61.44                                   
REMARK 500    MET A 287      112.13    -38.55                                   
REMARK 500    ASN A 289       10.57     85.89                                   
REMARK 500    TYR A 313      -31.02   -145.13                                   
REMARK 500    PHE A 336      119.11   -168.44                                   
REMARK 500    LEU A 349      -71.55    -49.89                                   
REMARK 500    ASN A 355      116.17   -174.64                                   
REMARK 500    ASP A 415      -61.84    -97.30                                   
REMARK 500    THR A 429      -52.22   -126.82                                   
REMARK 500    TYR A 457      106.85    -56.64                                   
REMARK 500    LYS A 474        2.28     81.84                                   
REMARK 500    GLU A 480      178.38    -53.60                                   
REMARK 500    PRO A 488       46.56    -96.42                                   
REMARK 500    SER A 490      -49.10    112.07                                   
REMARK 500    PRO A 491      126.52    -31.51                                   
REMARK 500    LYS A 495       27.43    -72.02                                   
REMARK 500    SER A 522      -59.27     63.05                                   
REMARK 500    GLU A 549       21.25     46.09                                   
REMARK 500    GLN A 550      -22.74   -154.60                                   
REMARK 500    THR A 551      112.40   -176.72                                   
REMARK 500    SER A 576      -75.68    -60.07                                   
REMARK 500    PRO A 584       49.16    -66.64                                   
REMARK 500    LEU A 620      -66.72     83.70                                   
REMARK 500    CYS A 634      139.11    175.92                                   
REMARK 500    LEU A 640      -22.13   -142.40                                   
REMARK 500    ASN A 641     -163.85   -112.13                                   
REMARK 500    SER A 662      152.09    143.47                                   
REMARK 500    GLN A 663       58.18   -140.84                                   
REMARK 500    LYS A 762       21.04     88.33                                   
REMARK 500    SER A 767      -36.91   -145.83                                   
REMARK 500    PHE A 769       71.26   -114.45                                   
REMARK 500    PRO A 781       46.68    -74.13                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     179 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 LYS A   90     GLN A   91                 -146.70                    
REMARK 500 GLY A  985     GLU A  986                  148.17                    
REMARK 500 LYS B  391     LYS B  392                 -149.90                    
REMARK 500 GLY B  599     GLN B  600                 -141.72                    
REMARK 500 THR B  731     PRO B  732                  -34.94                    
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 B1001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 138   OD1                                                    
REMARK 620 2 ASP B 148   OD1 174.6                                              
REMARK 620 3 ASP B 142   OD2  90.5  94.5                                        
REMARK 620 4 GLU B 149   OE1  95.6  79.1 168.9                                  
REMARK 620 5 LEU B 135   O    99.3  82.4  91.1  97.0                            
REMARK 620 6 GLU B 140   O    92.4  86.8  79.5  90.9 165.1                      
REMARK 620 7 GLU B 149   OE2  52.2 122.5 140.8  43.5 105.1  89.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC B 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 1008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 1009                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 V802I IS A NATURAL VARIANT ACCORDING TO UNIPROT                      
DBREF  4E0S A    1  1676  UNP    P01031   CO5_HUMAN        1   1676             
DBREF  4E0S B    1   913  UNP    P13671   CO6_HUMAN       22    934             
SEQADV 4E0S ILE A  802  UNP  P01031    VAL   802 SEE REMARK 999                 
SEQRES   1 A 1676  MET GLY LEU LEU GLY ILE LEU CYS PHE LEU ILE PHE LEU          
SEQRES   2 A 1676  GLY LYS THR TRP GLY GLN GLU GLN THR TYR VAL ILE SER          
SEQRES   3 A 1676  ALA PRO LYS ILE PHE ARG VAL GLY ALA SER GLU ASN ILE          
SEQRES   4 A 1676  VAL ILE GLN VAL TYR GLY TYR THR GLU ALA PHE ASP ALA          
SEQRES   5 A 1676  THR ILE SER ILE LYS SER TYR PRO ASP LYS LYS PHE SER          
SEQRES   6 A 1676  TYR SER SER GLY HIS VAL HIS LEU SER SER GLU ASN LYS          
SEQRES   7 A 1676  PHE GLN ASN SER ALA ILE LEU THR ILE GLN PRO LYS GLN          
SEQRES   8 A 1676  LEU PRO GLY GLY GLN ASN PRO VAL SER TYR VAL TYR LEU          
SEQRES   9 A 1676  GLU VAL VAL SER LYS HIS PHE SER LYS SER LYS ARG MET          
SEQRES  10 A 1676  PRO ILE THR TYR ASP ASN GLY PHE LEU PHE ILE HIS THR          
SEQRES  11 A 1676  ASP LYS PRO VAL TYR THR PRO ASP GLN SER VAL LYS VAL          
SEQRES  12 A 1676  ARG VAL TYR SER LEU ASN ASP ASP LEU LYS PRO ALA LYS          
SEQRES  13 A 1676  ARG GLU THR VAL LEU THR PHE ILE ASP PRO GLU GLY SER          
SEQRES  14 A 1676  GLU VAL ASP MET VAL GLU GLU ILE ASP HIS ILE GLY ILE          
SEQRES  15 A 1676  ILE SER PHE PRO ASP PHE LYS ILE PRO SER ASN PRO ARG          
SEQRES  16 A 1676  TYR GLY MET TRP THR ILE LYS ALA LYS TYR LYS GLU ASP          
SEQRES  17 A 1676  PHE SER THR THR GLY THR ALA TYR PHE GLU VAL LYS GLU          
SEQRES  18 A 1676  TYR VAL LEU PRO HIS PHE SER VAL SER ILE GLU PRO GLU          
SEQRES  19 A 1676  TYR ASN PHE ILE GLY TYR LYS ASN PHE LYS ASN PHE GLU          
SEQRES  20 A 1676  ILE THR ILE LYS ALA ARG TYR PHE TYR ASN LYS VAL VAL          
SEQRES  21 A 1676  THR GLU ALA ASP VAL TYR ILE THR PHE GLY ILE ARG GLU          
SEQRES  22 A 1676  ASP LEU LYS ASP ASP GLN LYS GLU MET MET GLN THR ALA          
SEQRES  23 A 1676  MET GLN ASN THR MET LEU ILE ASN GLY ILE ALA GLN VAL          
SEQRES  24 A 1676  THR PHE ASP SER GLU THR ALA VAL LYS GLU LEU SER TYR          
SEQRES  25 A 1676  TYR SER LEU GLU ASP LEU ASN ASN LYS TYR LEU TYR ILE          
SEQRES  26 A 1676  ALA VAL THR VAL ILE GLU SER THR GLY GLY PHE SER GLU          
SEQRES  27 A 1676  GLU ALA GLU ILE PRO GLY ILE LYS TYR VAL LEU SER PRO          
SEQRES  28 A 1676  TYR LYS LEU ASN LEU VAL ALA THR PRO LEU PHE LEU LYS          
SEQRES  29 A 1676  PRO GLY ILE PRO TYR PRO ILE LYS VAL GLN VAL LYS ASP          
SEQRES  30 A 1676  SER LEU ASP GLN LEU VAL GLY GLY VAL PRO VAL THR LEU          
SEQRES  31 A 1676  ASN ALA GLN THR ILE ASP VAL ASN GLN GLU THR SER ASP          
SEQRES  32 A 1676  LEU ASP PRO SER LYS SER VAL THR ARG VAL ASP ASP GLY          
SEQRES  33 A 1676  VAL ALA SER PHE VAL LEU ASN LEU PRO SER GLY VAL THR          
SEQRES  34 A 1676  VAL LEU GLU PHE ASN VAL LYS THR ASP ALA PRO ASP LEU          
SEQRES  35 A 1676  PRO GLU GLU ASN GLN ALA ARG GLU GLY TYR ARG ALA ILE          
SEQRES  36 A 1676  ALA TYR SER SER LEU SER GLN SER TYR LEU TYR ILE ASP          
SEQRES  37 A 1676  TRP THR ASP ASN HIS LYS ALA LEU LEU VAL GLY GLU HIS          
SEQRES  38 A 1676  LEU ASN ILE ILE VAL THR PRO LYS SER PRO TYR ILE ASP          
SEQRES  39 A 1676  LYS ILE THR HIS TYR ASN TYR LEU ILE LEU SER LYS GLY          
SEQRES  40 A 1676  LYS ILE ILE HIS PHE GLY THR ARG GLU LYS PHE SER ASP          
SEQRES  41 A 1676  ALA SER TYR GLN SER ILE ASN ILE PRO VAL THR GLN ASN          
SEQRES  42 A 1676  MET VAL PRO SER SER ARG LEU LEU VAL TYR TYR ILE VAL          
SEQRES  43 A 1676  THR GLY GLU GLN THR ALA GLU LEU VAL SER ASP SER VAL          
SEQRES  44 A 1676  TRP LEU ASN ILE GLU GLU LYS CYS GLY ASN GLN LEU GLN          
SEQRES  45 A 1676  VAL HIS LEU SER PRO ASP ALA ASP ALA TYR SER PRO GLY          
SEQRES  46 A 1676  GLN THR VAL SER LEU ASN MET ALA THR GLY MET ASP SER          
SEQRES  47 A 1676  TRP VAL ALA LEU ALA ALA VAL ASP SER ALA VAL TYR GLY          
SEQRES  48 A 1676  VAL GLN ARG GLY ALA LYS LYS PRO LEU GLU ARG VAL PHE          
SEQRES  49 A 1676  GLN PHE LEU GLU LYS SER ASP LEU GLY CYS GLY ALA GLY          
SEQRES  50 A 1676  GLY GLY LEU ASN ASN ALA ASN VAL PHE HIS LEU ALA GLY          
SEQRES  51 A 1676  LEU THR PHE LEU THR ASN ALA ASN ALA ASP ASP SER GLN          
SEQRES  52 A 1676  GLU ASN ASP GLU PRO CYS LYS GLU ILE LEU ARG PRO ARG          
SEQRES  53 A 1676  ARG THR LEU GLN LYS LYS ILE GLU GLU ILE ALA ALA LYS          
SEQRES  54 A 1676  TYR LYS HIS SER VAL VAL LYS LYS CYS CYS TYR ASP GLY          
SEQRES  55 A 1676  ALA CYS VAL ASN ASN ASP GLU THR CYS GLU GLN ARG ALA          
SEQRES  56 A 1676  ALA ARG ILE SER LEU GLY PRO ARG CYS ILE LYS ALA PHE          
SEQRES  57 A 1676  THR GLU CYS CYS VAL VAL ALA SER GLN LEU ARG ALA ASN          
SEQRES  58 A 1676  ILE SER HIS LYS ASP MET GLN LEU GLY ARG LEU HIS MET          
SEQRES  59 A 1676  LYS THR LEU LEU PRO VAL SER LYS PRO GLU ILE ARG SER          
SEQRES  60 A 1676  TYR PHE PRO GLU SER TRP LEU TRP GLU VAL HIS LEU VAL          
SEQRES  61 A 1676  PRO ARG ARG LYS GLN LEU GLN PHE ALA LEU PRO ASP SER          
SEQRES  62 A 1676  LEU THR THR TRP GLU ILE GLN GLY ILE GLY ILE SER ASN          
SEQRES  63 A 1676  THR GLY ILE CYS VAL ALA ASP THR VAL LYS ALA LYS VAL          
SEQRES  64 A 1676  PHE LYS ASP VAL PHE LEU GLU MET ASN ILE PRO TYR SER          
SEQRES  65 A 1676  VAL VAL ARG GLY GLU GLN ILE GLN LEU LYS GLY THR VAL          
SEQRES  66 A 1676  TYR ASN TYR ARG THR SER GLY MET GLN PHE CYS VAL LYS          
SEQRES  67 A 1676  MET SER ALA VAL GLU GLY ILE CYS THR SER GLU SER PRO          
SEQRES  68 A 1676  VAL ILE ASP HIS GLN GLY THR LYS SER SER LYS CYS VAL          
SEQRES  69 A 1676  ARG GLN LYS VAL GLU GLY SER SER SER HIS LEU VAL THR          
SEQRES  70 A 1676  PHE THR VAL LEU PRO LEU GLU ILE GLY LEU HIS ASN ILE          
SEQRES  71 A 1676  ASN PHE SER LEU GLU THR TRP PHE GLY LYS GLU ILE LEU          
SEQRES  72 A 1676  VAL LYS THR LEU ARG VAL VAL PRO GLU GLY VAL LYS ARG          
SEQRES  73 A 1676  GLU SER TYR SER GLY VAL THR LEU ASP PRO ARG GLY ILE          
SEQRES  74 A 1676  TYR GLY THR ILE SER ARG ARG LYS GLU PHE PRO TYR ARG          
SEQRES  75 A 1676  ILE PRO LEU ASP LEU VAL PRO LYS THR GLU ILE LYS ARG          
SEQRES  76 A 1676  ILE LEU SER VAL LYS GLY LEU LEU VAL GLY GLU ILE LEU          
SEQRES  77 A 1676  SER ALA VAL LEU SER GLN GLU GLY ILE ASN ILE LEU THR          
SEQRES  78 A 1676  HIS LEU PRO LYS GLY SER ALA GLU ALA GLU LEU MET SER          
SEQRES  79 A 1676  VAL VAL PRO VAL PHE TYR VAL PHE HIS TYR LEU GLU THR          
SEQRES  80 A 1676  GLY ASN HIS TRP ASN ILE PHE HIS SER ASP PRO LEU ILE          
SEQRES  81 A 1676  GLU LYS GLN LYS LEU LYS LYS LYS LEU LYS GLU GLY MET          
SEQRES  82 A 1676  LEU SER ILE MET SER TYR ARG ASN ALA ASP TYR SER TYR          
SEQRES  83 A 1676  SER VAL TRP LYS GLY GLY SER ALA SER THR TRP LEU THR          
SEQRES  84 A 1676  ALA PHE ALA LEU ARG VAL LEU GLY GLN VAL ASN LYS TYR          
SEQRES  85 A 1676  VAL GLU GLN ASN GLN ASN SER ILE CYS ASN SER LEU LEU          
SEQRES  86 A 1676  TRP LEU VAL GLU ASN TYR GLN LEU ASP ASN GLY SER PHE          
SEQRES  87 A 1676  LYS GLU ASN SER GLN TYR GLN PRO ILE LYS LEU GLN GLY          
SEQRES  88 A 1676  THR LEU PRO VAL GLU ALA ARG GLU ASN SER LEU TYR LEU          
SEQRES  89 A 1676  THR ALA PHE THR VAL ILE GLY ILE ARG LYS ALA PHE ASP          
SEQRES  90 A 1676  ILE CYS PRO LEU VAL LYS ILE ASP THR ALA LEU ILE LYS          
SEQRES  91 A 1676  ALA ASP ASN PHE LEU LEU GLU ASN THR LEU PRO ALA GLN          
SEQRES  92 A 1676  SER THR PHE THR LEU ALA ILE SER ALA TYR ALA LEU SER          
SEQRES  93 A 1676  LEU GLY ASP LYS THR HIS PRO GLN PHE ARG SER ILE VAL          
SEQRES  94 A 1676  SER ALA LEU LYS ARG GLU ALA LEU VAL LYS GLY ASN PRO          
SEQRES  95 A 1676  PRO ILE TYR ARG PHE TRP LYS ASP ASN LEU GLN HIS LYS          
SEQRES  96 A 1676  ASP SER SER VAL PRO ASN THR GLY THR ALA ARG MET VAL          
SEQRES  97 A 1676  GLU THR THR ALA TYR ALA LEU LEU THR SER LEU ASN LEU          
SEQRES  98 A 1676  LYS ASP ILE ASN TYR VAL ASN PRO VAL ILE LYS TRP LEU          
SEQRES  99 A 1676  SER GLU GLU GLN ARG TYR GLY GLY GLY PHE TYR SER THR          
SEQRES 100 A 1676  GLN ASP THR ILE ASN ALA ILE GLU GLY LEU THR GLU TYR          
SEQRES 101 A 1676  SER LEU LEU VAL LYS GLN LEU ARG LEU SER MET ASP ILE          
SEQRES 102 A 1676  ASP VAL SER TYR LYS HIS LYS GLY ALA LEU HIS ASN TYR          
SEQRES 103 A 1676  LYS MET THR ASP LYS ASN PHE LEU GLY ARG PRO VAL GLU          
SEQRES 104 A 1676  VAL LEU LEU ASN ASP ASP LEU ILE VAL SER THR GLY PHE          
SEQRES 105 A 1676  GLY SER GLY LEU ALA THR VAL HIS VAL THR THR VAL VAL          
SEQRES 106 A 1676  HIS LYS THR SER THR SER GLU GLU VAL CYS SER PHE TYR          
SEQRES 107 A 1676  LEU LYS ILE ASP THR GLN ASP ILE GLU ALA SER HIS TYR          
SEQRES 108 A 1676  ARG GLY TYR GLY ASN SER ASP TYR LYS ARG ILE VAL ALA          
SEQRES 109 A 1676  CYS ALA SER TYR LYS PRO SER ARG GLU GLU SER SER SER          
SEQRES 110 A 1676  GLY SER SER HIS ALA VAL MET ASP ILE SER LEU PRO THR          
SEQRES 111 A 1676  GLY ILE SER ALA ASN GLU GLU ASP LEU LYS ALA LEU VAL          
SEQRES 112 A 1676  GLU GLY VAL ASP GLN LEU PHE THR ASP TYR GLN ILE LYS          
SEQRES 113 A 1676  ASP GLY HIS VAL ILE LEU GLN LEU ASN SER ILE PRO SER          
SEQRES 114 A 1676  SER ASP PHE LEU CYS VAL ARG PHE ARG ILE PHE GLU LEU          
SEQRES 115 A 1676  PHE GLU VAL GLY PHE LEU SER PRO ALA THR PHE THR VAL          
SEQRES 116 A 1676  TYR GLU TYR HIS ARG PRO ASP LYS GLN CYS THR MET PHE          
SEQRES 117 A 1676  TYR SER THR SER ASN ILE LYS ILE GLN LYS VAL CYS GLU          
SEQRES 118 A 1676  GLY ALA ALA CYS LYS CYS VAL GLU ALA ASP CYS GLY GLN          
SEQRES 119 A 1676  MET GLN GLU GLU LEU ASP LEU THR ILE SER ALA GLU THR          
SEQRES 120 A 1676  ARG LYS GLN THR ALA CYS LYS PRO GLU ILE ALA TYR ALA          
SEQRES 121 A 1676  TYR LYS VAL SER ILE THR SER ILE THR VAL GLU ASN VAL          
SEQRES 122 A 1676  PHE VAL LYS TYR LYS ALA THR LEU LEU ASP ILE TYR LYS          
SEQRES 123 A 1676  THR GLY GLU ALA VAL ALA GLU LYS ASP SER GLU ILE THR          
SEQRES 124 A 1676  PHE ILE LYS LYS VAL THR CYS THR ASN ALA GLU LEU VAL          
SEQRES 125 A 1676  LYS GLY ARG GLN TYR LEU ILE MET GLY LYS GLU ALA LEU          
SEQRES 126 A 1676  GLN ILE LYS TYR ASN PHE SER PHE ARG TYR ILE TYR PRO          
SEQRES 127 A 1676  LEU ASP SER LEU THR TRP ILE GLU TYR TRP PRO ARG ASP          
SEQRES 128 A 1676  THR THR CYS SER SER CYS GLN ALA PHE LEU ALA ASN LEU          
SEQRES 129 A 1676  ASP GLU PHE ALA GLU ASP ILE PHE LEU ASN GLY CYS              
SEQRES   1 B  913  CYS PHE CYS ASP HIS TYR ALA TRP THR GLN TRP THR SER          
SEQRES   2 B  913  CYS SER LYS THR CYS ASN SER GLY THR GLN SER ARG HIS          
SEQRES   3 B  913  ARG GLN ILE VAL VAL ASP LYS TYR TYR GLN GLU ASN PHE          
SEQRES   4 B  913  CYS GLU GLN ILE CYS SER LYS GLN GLU THR ARG GLU CYS          
SEQRES   5 B  913  ASN TRP GLN ARG CYS PRO ILE ASN CYS LEU LEU GLY ASP          
SEQRES   6 B  913  PHE GLY PRO TRP SER ASP CYS ASP PRO CYS ILE GLU LYS          
SEQRES   7 B  913  GLN SER LYS VAL ARG SER VAL LEU ARG PRO SER GLN PHE          
SEQRES   8 B  913  GLY GLY GLN PRO CYS THR ALA PRO LEU VAL ALA PHE GLN          
SEQRES   9 B  913  PRO CYS ILE PRO SER LYS LEU CYS LYS ILE GLU GLU ALA          
SEQRES  10 B  913  ASP CYS LYS ASN LYS PHE ARG CYS ASP SER GLY ARG CYS          
SEQRES  11 B  913  ILE ALA ARG LYS LEU GLU CYS ASN GLY GLU ASN ASP CYS          
SEQRES  12 B  913  GLY ASP ASN SER ASP GLU ARG ASP CYS GLY ARG THR LYS          
SEQRES  13 B  913  ALA VAL CYS THR ARG LYS TYR ASN PRO ILE PRO SER VAL          
SEQRES  14 B  913  GLN LEU MET GLY ASN GLY PHE HIS PHE LEU ALA GLY GLU          
SEQRES  15 B  913  PRO ARG GLY GLU VAL LEU ASP ASN SER PHE THR GLY GLY          
SEQRES  16 B  913  ILE CYS LYS THR VAL LYS SER SER ARG THR SER ASN PRO          
SEQRES  17 B  913  TYR ARG VAL PRO ALA ASN LEU GLU ASN VAL GLY PHE GLU          
SEQRES  18 B  913  VAL GLN THR ALA GLU ASP ASP LEU LYS THR ASP PHE TYR          
SEQRES  19 B  913  LYS ASP LEU THR SER LEU GLY HIS ASN GLU ASN GLN GLN          
SEQRES  20 B  913  GLY SER PHE SER SER GLN GLY GLY SER SER PHE SER VAL          
SEQRES  21 B  913  PRO ILE PHE TYR SER SER LYS ARG SER GLU ASN ILE ASN          
SEQRES  22 B  913  HIS ASN SER ALA PHE LYS GLN ALA ILE GLN ALA SER HIS          
SEQRES  23 B  913  LYS LYS ASP SER SER PHE ILE ARG ILE HIS LYS VAL MET          
SEQRES  24 B  913  LYS VAL LEU ASN PHE THR THR LYS ALA LYS ASP LEU HIS          
SEQRES  25 B  913  LEU SER ASP VAL PHE LEU LYS ALA LEU ASN HIS LEU PRO          
SEQRES  26 B  913  LEU GLU TYR ASN SER ALA LEU TYR SER ARG ILE PHE ASP          
SEQRES  27 B  913  ASP PHE GLY THR HIS TYR PHE THR SER GLY SER LEU GLY          
SEQRES  28 B  913  GLY VAL TYR ASP LEU LEU TYR GLN PHE SER SER GLU GLU          
SEQRES  29 B  913  LEU LYS ASN SER GLY LEU THR GLU GLU GLU ALA LYS HIS          
SEQRES  30 B  913  CYS VAL ARG ILE GLU THR LYS LYS ARG VAL LEU PHE ALA          
SEQRES  31 B  913  LYS LYS THR LYS VAL GLU HIS ARG CYS THR THR ASN LYS          
SEQRES  32 B  913  LEU SER GLU LYS HIS GLU GLY SER PHE ILE GLN GLY ALA          
SEQRES  33 B  913  GLU LYS SER ILE SER LEU ILE ARG GLY GLY ARG SER GLU          
SEQRES  34 B  913  TYR GLY ALA ALA LEU ALA TRP GLU LYS GLY SER SER GLY          
SEQRES  35 B  913  LEU GLU GLU LYS THR PHE SER GLU TRP LEU GLU SER VAL          
SEQRES  36 B  913  LYS GLU ASN PRO ALA VAL ILE ASP PHE GLU LEU ALA PRO          
SEQRES  37 B  913  ILE VAL ASP LEU VAL ARG ASN ILE PRO CYS ALA VAL THR          
SEQRES  38 B  913  LYS ARG ASN ASN LEU ARG LYS ALA LEU GLN GLU TYR ALA          
SEQRES  39 B  913  ALA LYS PHE ASP PRO CYS GLN CYS ALA PRO CYS PRO ASN          
SEQRES  40 B  913  ASN GLY ARG PRO THR LEU SER GLY THR GLU CYS LEU CYS          
SEQRES  41 B  913  VAL CYS GLN SER GLY THR TYR GLY GLU ASN CYS GLU LYS          
SEQRES  42 B  913  GLN SER PRO ASP TYR LYS SER ASN ALA VAL ASP GLY GLN          
SEQRES  43 B  913  TRP GLY CYS TRP SER SER TRP SER THR CYS ASP ALA THR          
SEQRES  44 B  913  TYR LYS ARG SER ARG THR ARG GLU CYS ASN ASN PRO ALA          
SEQRES  45 B  913  PRO GLN ARG GLY GLY LYS ARG CYS GLU GLY GLU LYS ARG          
SEQRES  46 B  913  GLN GLU GLU ASP CYS THR PHE SER ILE MET GLU ASN ASN          
SEQRES  47 B  913  GLY GLN PRO CYS ILE ASN ASP ASP GLU GLU MET LYS GLU          
SEQRES  48 B  913  VAL ASP LEU PRO GLU ILE GLU ALA ASP SER GLY CYS PRO          
SEQRES  49 B  913  GLN PRO VAL PRO PRO GLU ASN GLY PHE ILE ARG ASN GLU          
SEQRES  50 B  913  LYS GLN LEU TYR LEU VAL GLY GLU ASP VAL GLU ILE SER          
SEQRES  51 B  913  CYS LEU THR GLY PHE GLU THR VAL GLY TYR GLN TYR PHE          
SEQRES  52 B  913  ARG CYS LEU PRO ASP GLY THR TRP ARG GLN GLY ASP VAL          
SEQRES  53 B  913  GLU CYS GLN ARG THR GLU CYS ILE LYS PRO VAL VAL GLN          
SEQRES  54 B  913  GLU VAL LEU THR ILE THR PRO PHE GLN ARG LEU TYR ARG          
SEQRES  55 B  913  ILE GLY GLU SER ILE GLU LEU THR CYS PRO LYS GLY PHE          
SEQRES  56 B  913  VAL VAL ALA GLY PRO SER ARG TYR THR CYS GLN GLY ASN          
SEQRES  57 B  913  SER TRP THR PRO PRO ILE SER ASN SER LEU THR CYS GLU          
SEQRES  58 B  913  LYS ASP THR LEU THR LYS LEU LYS GLY HIS CYS GLN LEU          
SEQRES  59 B  913  GLY GLN LYS GLN SER GLY SER GLU CYS ILE CYS MET SER          
SEQRES  60 B  913  PRO GLU GLU ASP CYS SER HIS HIS SER GLU ASP LEU CYS          
SEQRES  61 B  913  VAL PHE ASP THR ASP SER ASN ASP TYR PHE THR SER PRO          
SEQRES  62 B  913  ALA CYS LYS PHE LEU ALA GLU LYS CYS LEU ASN ASN GLN          
SEQRES  63 B  913  GLN LEU HIS PHE LEU HIS ILE GLY SER CYS GLN ASP GLY          
SEQRES  64 B  913  ARG GLN LEU GLU TRP GLY LEU GLU ARG THR ARG LEU SER          
SEQRES  65 B  913  SER ASN SER THR LYS LYS GLU SER CYS GLY TYR ASP THR          
SEQRES  66 B  913  CYS TYR ASP TRP GLU LYS CYS SER ALA SER THR SER LYS          
SEQRES  67 B  913  CYS VAL CYS LEU LEU PRO PRO GLN CYS PHE LYS GLY GLY          
SEQRES  68 B  913  ASN GLN LEU TYR CYS VAL LYS MET GLY SER SER THR SER          
SEQRES  69 B  913  GLU LYS THR LEU ASN ILE CYS GLU VAL GLY THR ILE ARG          
SEQRES  70 B  913  CYS ALA ASN ARG LYS MET GLU ILE LEU HIS PRO GLY LYS          
SEQRES  71 B  913  CYS LEU ALA                                                  
MODRES 4E0S ASN B  303  ASN  GLYCOSYLATION SITE                                 
MODRES 4E0S ASN A  911  ASN  GLYCOSYLATION SITE                                 
MODRES 4E0S THR B   17  THR  GLYCOSYLATION SITE                                 
HET    NAG  A2001      14                                                       
HET    NAG  A2002      14                                                       
HET     NA  A2003       1                                                       
HET     CA  B1001       1                                                       
HET    NAG  B1002      14                                                       
HET    NAG  B1003      14                                                       
HET    FUC  B1004      10                                                       
HET    BGC  B1005      11                                                       
HET    MAN  B1006      11                                                       
HET    MAN  B1007      11                                                       
HET    MAN  B1008      11                                                       
HET    MAN  B1009      11                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      NA SODIUM ION                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   4   NA    NA 1+                                                        
FORMUL   5   CA    CA 2+                                                        
FORMUL   7  FUC    C6 H12 O5                                                    
FORMUL   7  BGC    C6 H12 O6                                                    
FORMUL   8  MAN    4(C6 H12 O6)                                                 
HELIX    1   1 SER A   74  LYS A   78  5                                   5    
HELIX    2   2 ASP A  302  LYS A  308  1                                   7    
HELIX    3   3 THR A  531  VAL A  535  5                                   5    
HELIX    4   4 ALA A  608  VAL A  612  5                                   5    
HELIX    5   5 LEU A  620  GLU A  628  1                                   9    
HELIX    6   6 ASN A  641  ALA A  649  1                                   9    
HELIX    7   7 SER A  993  LEU A 1003  1                                  11    
HELIX    8   8 ALA A 1010  GLY A 1028  1                                  19    
HELIX    9   9 HIS A 1030  HIS A 1035  5                                   6    
HELIX   10  10 ASP A 1037  SER A 1058  1                                  22    
HELIX   11  11 SER A 1075  LYS A 1091  1                                  17    
HELIX   12  12 ASN A 1096  TYR A 1111  1                                  16    
HELIX   13  13 ARG A 1138  PHE A 1156  1                                  19    
HELIX   14  14 ASP A 1157  CYS A 1159  5                                   3    
HELIX   15  15 LEU A 1161  ASN A 1178  1                                  18    
HELIX   16  16 SER A 1184  SER A 1196  1                                  13    
HELIX   17  17 HIS A 1202  ALA A 1216  1                                  15    
HELIX   18  18 ALA A 1245  LYS A 1262  1                                  18    
HELIX   19  19 ASP A 1263  GLY A 1282  1                                  20    
HELIX   20  20 SER A 1286  LEU A 1302  1                                  17    
HELIX   21  21 LEU A 1302  ARG A 1308  1                                   7    
HELIX   22  22 ASN A 1435  GLU A 1444  1                                  10    
HELIX   23  23 SER A 1544  CYS A 1553  1                                  10    
HELIX   24  24 SER A 1656  ASN A 1674  1                                  19    
HELIX   25  25 PHE B    2  TYR B    6  5                                   5    
HELIX   26  26 ASP B   32  ASN B   38  1                                   7    
HELIX   27  27 PHE B   39  CYS B   44  1                                   6    
HELIX   28  28 ASP B  118  LYS B  122  5                                   5    
HELIX   29  29 ALA B  132  GLU B  136  5                                   5    
HELIX   30  30 ASN B  146  ARG B  150  5                                   5    
HELIX   31  31 SER B  168  MET B  172  5                                   5    
HELIX   32  32 ALA B  225  ASP B  227  5                                   3    
HELIX   33  33 THR B  238  ASN B  245  1                                   8    
HELIX   34  34 HIS B  274  HIS B  286  1                                  13    
HELIX   35  35 SER B  314  LEU B  321  1                                   8    
HELIX   36  36 ASN B  329  GLY B  341  1                                  13    
HELIX   37  37 SER B  362  GLY B  369  1                                   8    
HELIX   38  38 THR B  371  VAL B  387  1                                  17    
HELIX   39  39 LEU B  404  GLU B  409  5                                   6    
HELIX   40  40 PHE B  412  ALA B  416  5                                   5    
HELIX   41  41 ARG B  427  ALA B  435  1                                   9    
HELIX   42  42 GLU B  444  ASN B  458  1                                  15    
HELIX   43  43 PRO B  468  VAL B  473  5                                   6    
HELIX   44  44 CYS B  478  ASP B  498  1                                  21    
HELIX   45  45 LYS B  610  LEU B  614  5                                   5    
HELIX   46  46 SER B  767  CYS B  772  1                                   6    
HELIX   47  47 ALA B  794  ASN B  805  1                                  12    
HELIX   48  48 GLY B  819  THR B  829  1                                  11    
HELIX   49  49 LEU B  863  CYS B  867  5                                   5    
HELIX   50  50 ASN B  889  ALA B  899  1                                  11    
SHEET    1   A 4 GLN A  80  ASN A  81  0                                        
SHEET    2   A 4 VAL A  40  VAL A  43 -1  N  ILE A  41   O  ASN A  81           
SHEET    3   A 4 TYR A  23  PRO A  28 -1  N  SER A  26   O  VAL A  40           
SHEET    4   A 4 LEU A 651  THR A 655 -1  O  THR A 652   N  ALA A  27           
SHEET    1   B 5 PHE A  31  ARG A  32  0                                        
SHEET    2   B 5 SER A 112  THR A 120  1  O  THR A 120   N  PHE A  31           
SHEET    3   B 5 TYR A 101  SER A 108 -1  N  VAL A 102   O  MET A 117           
SHEET    4   B 5 PHE A  50  LYS A  57 -1  N  THR A  53   O  VAL A 107           
SHEET    5   B 5 SER A  65  LEU A  73 -1  O  GLY A  69   N  ILE A  54           
SHEET    1   C 2 SER A  36  ASN A  38  0                                        
SHEET    2   C 2 ILE A  84  THR A  86 -1  O  LEU A  85   N  GLU A  37           
SHEET    1   D 3 PHE A 125  THR A 130  0                                        
SHEET    2   D 3 SER A 140  LEU A 148 -1  O  ARG A 144   N  HIS A 129           
SHEET    3   D 3 ILE A 182  LYS A 189 -1  O  PHE A 188   N  VAL A 141           
SHEET    1   E 5 VAL A 134  TYR A 135  0                                        
SHEET    2   E 5 THR A 212  VAL A 219  1  O  GLU A 218   N  TYR A 135           
SHEET    3   E 5 GLY A 197  TYR A 205 -1  N  TRP A 199   O  PHE A 217           
SHEET    4   E 5 THR A 159  ILE A 164 -1  N  VAL A 160   O  LYS A 204           
SHEET    5   E 5 GLU A 170  GLU A 176 -1  O  VAL A 174   N  LEU A 161           
SHEET    1   F 3 PHE A 227  PRO A 233  0                                        
SHEET    2   F 3 GLU A 247  TYR A 254 -1  O  THR A 249   N  GLU A 232           
SHEET    3   F 3 ALA A 297  THR A 300 -1  O  VAL A 299   N  ILE A 248           
SHEET    1   G 5 PHE A 237  ILE A 238  0                                        
SHEET    2   G 5 SER A 337  TYR A 347  1  O  LYS A 346   N  ILE A 238           
SHEET    3   G 5 LYS A 321  GLU A 331 -1  N  LYS A 321   O  TYR A 347           
SHEET    4   G 5 GLU A 262  ARG A 272 -1  N  ASP A 264   O  ILE A 330           
SHEET    5   G 5 GLU A 281  MET A 283 -1  O  GLU A 281   N  ILE A 271           
SHEET    1   H 5 PHE A 237  ILE A 238  0                                        
SHEET    2   H 5 SER A 337  TYR A 347  1  O  LYS A 346   N  ILE A 238           
SHEET    3   H 5 LYS A 321  GLU A 331 -1  N  LYS A 321   O  TYR A 347           
SHEET    4   H 5 GLU A 262  ARG A 272 -1  N  ASP A 264   O  ILE A 330           
SHEET    5   H 5 GLN A 288  ILE A 293 -1  O  THR A 290   N  VAL A 265           
SHEET    1   I 3 LYS A 353  LEU A 354  0                                        
SHEET    2   I 3 PRO A 368  LYS A 376 -1  O  LYS A 376   N  LYS A 353           
SHEET    3   I 3 VAL A 417  ASN A 423 -1  O  LEU A 422   N  TYR A 369           
SHEET    1   J 5 PHE A 362  LEU A 363  0                                        
SHEET    2   J 5 ARG A 449  ALA A 456  1  O  ILE A 455   N  LEU A 363           
SHEET    3   J 5 VAL A 428  THR A 437 -1  N  LEU A 431   O  ALA A 454           
SHEET    4   J 5 PRO A 387  ASP A 396 -1  N  ASN A 391   O  ASN A 434           
SHEET    5   J 5 THR A 401  ASP A 403 -1  O  SER A 402   N  THR A 394           
SHEET    1   K 5 PHE A 362  LEU A 363  0                                        
SHEET    2   K 5 ARG A 449  ALA A 456  1  O  ILE A 455   N  LEU A 363           
SHEET    3   K 5 VAL A 428  THR A 437 -1  N  LEU A 431   O  ALA A 454           
SHEET    4   K 5 PRO A 387  ASP A 396 -1  N  ASN A 391   O  ASN A 434           
SHEET    5   K 5 SER A 407  VAL A 410 -1  O  SER A 409   N  VAL A 388           
SHEET    1   L 3 TYR A 466  ASP A 468  0                                        
SHEET    2   L 3 HIS A 481  THR A 487 -1  O  THR A 487   N  TYR A 466           
SHEET    3   L 3 GLN A 524  PRO A 529 -1  O  GLN A 524   N  VAL A 486           
SHEET    1   M 4 LYS A 508  GLU A 516  0                                        
SHEET    2   M 4 HIS A 498  SER A 505 -1  N  TYR A 499   O  ARG A 515           
SHEET    3   M 4 SER A 537  THR A 547 -1  O  TYR A 543   N  ASN A 500           
SHEET    4   M 4 ALA A 552  ASN A 562 -1  O  LEU A 561   N  SER A 538           
SHEET    1   N 3 HIS A 574  LEU A 575  0                                        
SHEET    2   N 3 THR A 587  ALA A 593 -1  O  ASN A 591   N  HIS A 574           
SHEET    3   N 3 ARG A 783  ALA A 789 -1  O  LYS A 784   N  MET A 592           
SHEET    1   O 4 VAL A 777  VAL A 780  0                                        
SHEET    2   O 4 SER A 598  ALA A 601 -1  N  SER A 598   O  VAL A 780           
SHEET    3   O 4 ILE A 802  SER A 805 -1  O  ILE A 802   N  ALA A 601           
SHEET    4   O 4 GLY A 808  VAL A 811 -1  O  CYS A 810   N  GLY A 803           
SHEET    1   P 4 SER A 772  TRP A 773  0                                        
SHEET    2   P 4 ALA A 604  ASP A 606 -1  N  ALA A 604   O  TRP A 773           
SHEET    3   P 4 THR A 795  ILE A 799 -1  O  GLU A 798   N  VAL A 605           
SHEET    4   P 4 VAL A 815  VAL A 819 -1  O  VAL A 815   N  ILE A 799           
SHEET    1   Q 5 ILE A 765  ARG A 766  0                                        
SHEET    2   Q 5 GLY A 919  LYS A 925  1  O  ILE A 922   N  ARG A 766           
SHEET    3   Q 5 ILE A 910  THR A 916 -1  N  PHE A 912   O  LEU A 923           
SHEET    4   Q 5 MET A 853  SER A 860 -1  N  SER A 860   O  ASN A 911           
SHEET    5   Q 5 GLN A 886  VAL A 888 -1  O  VAL A 888   N  MET A 853           
SHEET    1   R 3 VAL A 823  ASN A 828  0                                        
SHEET    2   R 3 ILE A 839  ASN A 847 -1  O  TYR A 846   N  PHE A 824           
SHEET    3   R 3 SER A 892  LEU A 895 -1  O  SER A 892   N  ASN A 847           
SHEET    1   S 3 VAL A 823  ASN A 828  0                                        
SHEET    2   S 3 ILE A 839  ASN A 847 -1  O  TYR A 846   N  PHE A 824           
SHEET    3   S 3 PHE A 898  VAL A 900 -1  O  PHE A 898   N  LEU A 841           
SHEET    1   T 2 VAL A 833  VAL A 834  0                                        
SHEET    2   T 2 VAL A 929  VAL A 930  1  O  VAL A 930   N  VAL A 833           
SHEET    1   U 4 GLU A 937  LEU A 944  0                                        
SHEET    2   U 4 ALA A1357  VAL A1364 -1  O  THR A1363   N  SER A 938           
SHEET    3   U 4 LYS A 974  GLY A 981 -1  N  SER A 978   O  HIS A1360           
SHEET    4   U 4 ARG A1336  GLU A1339 -1  O  VAL A1338   N  LEU A 977           
SHEET    1   V 3 ARG A 956  PHE A 959  0                                        
SHEET    2   V 3 LEU A1346  SER A1349 -1  O  LEU A1346   N  PHE A 959           
SHEET    3   V 3 VAL A1315  TYR A1317 -1  N  SER A1316   O  ILE A1347           
SHEET    1   W 2 LEU A1217  LYS A1219  0                                        
SHEET    2   W 2 TYR A1225  PHE A1227 -1  O  PHE A1227   N  LEU A1217           
SHEET    1   X 3 PHE A1377  ASP A1385  0                                        
SHEET    2   X 3 LYS A1400  TYR A1408 -1  O  SER A1407   N  TYR A1378           
SHEET    3   X 3 LEU A1473  ILE A1479 -1  O  PHE A1477   N  ILE A1402           
SHEET    1   Y 5 ILE A1455  LYS A1456  0                                        
SHEET    2   Y 5 HIS A1459  LEU A1464 -1  O  HIS A1459   N  LYS A1456           
SHEET    3   Y 5 ALA A1422  SER A1427 -1  N  ALA A1422   O  LEU A1464           
SHEET    4   Y 5 ALA A1491  GLU A1497 -1  O  THR A1492   N  SER A1427           
SHEET    5   Y 5 ARG A1500  TYR A1509 -1  O  MET A1507   N  PHE A1493           
SHEET    1   Z 2 GLN A1517  GLU A1521  0                                        
SHEET    2   Z 2 ALA A1524  VAL A1528 -1  O  ALA A1524   N  GLU A1521           
SHEET    1  AA 6 ILE A1636  PRO A1638  0                                        
SHEET    2  AA 6 GLU A1597  ILE A1601  1  N  ILE A1601   O  TYR A1637           
SHEET    3  AA 6 TYR A1577  LEU A1581 -1  N  TYR A1577   O  PHE A1600           
SHEET    4  AA 6 TYR A1559  ILE A1568 -1  N  SER A1564   O  THR A1580           
SHEET    5  AA 6 GLN A1616  GLY A1621 -1  O  TYR A1617   N  VAL A1563           
SHEET    6  AA 6 TRP A1644  GLU A1646 -1  O  GLU A1646   N  LEU A1618           
SHEET    1  AB 2 LYS A1628  TYR A1629  0                                        
SHEET    2  AB 2 SER A1632  PHE A1633 -1  O  SER A1632   N  TYR A1629           
SHEET    1  AC 2 SER B  24  ARG B  25  0                                        
SHEET    2  AC 2 GLU B  48  THR B  49 -1  O  GLU B  48   N  ARG B  25           
SHEET    1  AD 2 LYS B  78  GLN B  79  0                                        
SHEET    2  AD 2 GLN B 104  PRO B 105 -1  O  GLN B 104   N  GLN B  79           
SHEET    1  AE 3 SER B  89  GLN B  90  0                                        
SHEET    2  AE 3 GLU B 517  VAL B 521  1  O  CYS B 518   N  SER B  89           
SHEET    3  AE 3 ARG B 510  SER B 514 -1  N  THR B 512   O  LEU B 519           
SHEET    1  AF 3 ASN B 164  PRO B 165  0                                        
SHEET    2  AF 3 TYR B 209  ARG B 210  1  O  ARG B 210   N  ASN B 164           
SHEET    3  AF 3 THR B 199  VAL B 200 -1  N  VAL B 200   O  TYR B 209           
SHEET    1  AG 2 ASN B 174  HIS B 177  0                                        
SHEET    2  AG 2 GLU B 182  GLU B 186 -1  O  ARG B 184   N  GLY B 175           
SHEET    1  AH 4 LEU B 215  GLY B 219  0                                        
SHEET    2  AH 4 SER B 290  THR B 306 -1  O  ASN B 303   N  GLY B 219           
SHEET    3  AH 4 SER B 347  SER B 361 -1  O  TYR B 358   N  ILE B 293           
SHEET    4  AH 4 LYS B 418  SER B 421 -1  O  LYS B 418   N  GLN B 359           
SHEET    1  AI 4 LEU B 229  TYR B 234  0                                        
SHEET    2  AI 4 SER B 290  THR B 306 -1  O  PHE B 292   N  TYR B 234           
SHEET    3  AI 4 SER B 347  SER B 361 -1  O  TYR B 358   N  ILE B 293           
SHEET    4  AI 4 ALA B 460  GLU B 465 -1  O  GLU B 465   N  SER B 347           
SHEET    1  AJ 2 THR B 526  TYR B 527  0                                        
SHEET    2  AJ 2 LYS B 533  GLN B 534 -1  O  LYS B 533   N  TYR B 527           
SHEET    1  AK 2 LYS B 561  THR B 565  0                                        
SHEET    2  AK 2 ARG B 585  ASP B 589 -1  O  GLU B 588   N  ARG B 562           
SHEET    1  AL 2 CYS B 623  PRO B 624  0                                        
SHEET    2  AL 2 LEU B 640  TYR B 641 -1  O  TYR B 641   N  CYS B 623           
SHEET    1  AM 4 GLY B 632  ILE B 634  0                                        
SHEET    2  AM 4 ASP B 646  CYS B 651 -1  O  SER B 650   N  PHE B 633           
SHEET    3  AM 4 TYR B 662  CYS B 665 -1  O  PHE B 663   N  VAL B 647           
SHEET    4  AM 4 TRP B 671  GLN B 673 -1  O  ARG B 672   N  ARG B 664           
SHEET    1  AN 2 SER B 706  GLU B 708  0                                        
SHEET    2  AN 2 ARG B 722  THR B 724 -1  O  TYR B 723   N  ILE B 707           
SHEET    1  AO 2 GLN B 756  GLN B 758  0                                        
SHEET    2  AO 2 CYS B 763  CYS B 765 -1  O  ILE B 764   N  LYS B 757           
SHEET    1  AP 3 TYR B 789  PRO B 793  0                                        
SHEET    2  AP 3 ASP B 778  ASP B 783 -1  N  LEU B 779   O  SER B 792           
SHEET    3  AP 3 LEU B 808  ILE B 813 -1  O  HIS B 809   N  PHE B 782           
SHEET    1  AQ 3 LYS B 886  THR B 887  0                                        
SHEET    2  AQ 3 CYS B 876  VAL B 877 -1  N  VAL B 877   O  LYS B 886           
SHEET    3  AQ 3 ILE B 905  HIS B 907 -1  O  LEU B 906   N  CYS B 876           
SSBOND   1 CYS A  567    CYS A  810                          1555   1555  2.04  
SSBOND   2 CYS A  634    CYS A  669                          1555   1555  2.02  
SSBOND   3 CYS A  856    CYS A  883                          1555   1555  2.04  
SSBOND   4 CYS A  866    CYS A 1527                          1555   1555  2.01  
SSBOND   5 CYS A 1101    CYS A 1159                          1555   1555  2.03  
SSBOND   6 CYS A 1375    CYS A 1505                          1555   1555  2.04  
SSBOND   7 CYS A 1405    CYS A 1474                          1555   1555  2.02  
SSBOND   8 CYS A 1520    CYS A 1525                          1555   1555  2.03  
SSBOND   9 CYS A 1532    CYS A 1606                          1555   1555  2.05  
SSBOND  10 CYS A 1553    CYS A 1676                          1555   1555  2.03  
SSBOND  11 CYS A 1654    CYS A 1657                          1555   1555  2.03  
SSBOND  12 CYS B    1    CYS B   40                          1555   1555  2.03  
SSBOND  13 CYS B    3    CYS B   44                          1555   1555  2.01  
SSBOND  14 CYS B   14    CYS B   52                          1555   1555  2.02  
SSBOND  15 CYS B   18    CYS B   57                          1555   1555  2.03  
SSBOND  16 CYS B   61    CYS B   96                          1555   1555  2.02  
SSBOND  17 CYS B   72    CYS B  106                          1555   1555  2.01  
SSBOND  18 CYS B   75    CYS B  112                          1555   1555  2.01  
SSBOND  19 CYS B  119    CYS B  130                          1555   1555  2.03  
SSBOND  20 CYS B  125    CYS B  143                          1555   1555  2.03  
SSBOND  21 CYS B  137    CYS B  152                          1555   1555  2.03  
SSBOND  22 CYS B  159    CYS B  197                          1555   1555  2.04  
SSBOND  23 CYS B  378    CYS B  399                          1555   1555  2.04  
SSBOND  24 CYS B  478    CYS B  602                          1555   1555  2.00  
SSBOND  25 CYS B  500    CYS B  549                          1555   1555  2.04  
SSBOND  26 CYS B  502    CYS B  518                          1555   1555  2.03  
SSBOND  27 CYS B  505    CYS B  520                          1555   1555  2.03  
SSBOND  28 CYS B  522    CYS B  531                          1555   1555  2.03  
SSBOND  29 CYS B  556    CYS B  590                          1555   1555  2.04  
SSBOND  30 CYS B  568    CYS B  580                          1555   1555  2.02  
SSBOND  31 CYS B  623    CYS B  665                          1555   1555  2.06  
SSBOND  32 CYS B  651    CYS B  678                          1555   1555  2.04  
SSBOND  33 CYS B  683    CYS B  725                          1555   1555  2.03  
SSBOND  34 CYS B  711    CYS B  740                          1555   1555  2.03  
SSBOND  35 CYS B  752    CYS B  763                          1555   1555  2.03  
SSBOND  36 CYS B  765    CYS B  802                          1555   1555  2.01  
SSBOND  37 CYS B  772    CYS B  795                          1555   1555  2.04  
SSBOND  38 CYS B  780    CYS B  816                          1555   1555  2.02  
SSBOND  39 CYS B  841    CYS B  852                          1555   1555  2.03  
SSBOND  40 CYS B  846    CYS B  859                          1555   1555  2.02  
SSBOND  41 CYS B  861    CYS B  898                          1555   1555  2.02  
SSBOND  42 CYS B  867    CYS B  891                          1555   1555  2.03  
SSBOND  43 CYS B  876    CYS B  911                          1555   1555  2.04  
LINK         O3  FUC B1004                 C1  BGC B1005     1555   1555  1.42  
LINK         ND2 ASN B 303                 C1  NAG B1002     1555   1555  1.42  
LINK         ND2 ASN A 911                 C1  NAG A2001     1555   1555  1.43  
LINK         O4  NAG A2001                 C1  NAG A2002     1555   1555  1.43  
LINK         O4  NAG B1002                 C1  NAG B1003     1555   1555  1.44  
LINK         OG1 THR B  17                 C1  FUC B1004     1555   1555  1.44  
LINK         CD1 TRP B  11                 C1  MAN B1006     1555   1555  1.43  
LINK         CD1 TRP B   8                 C1  MAN B1007     1555   1555  1.44  
LINK         CD1 TRP B 547                 C1  MAN B1009     1555   1555  1.45  
LINK         CD1 TRP B 550                 C1  MAN B1008     1555   1555  1.45  
LINK         OD1 ASN B 138                CA    CA B1001     1555   1555  2.30  
LINK         OD1 ASP B 148                CA    CA B1001     1555   1555  2.31  
LINK         OD2 ASP B 142                CA    CA B1001     1555   1555  2.32  
LINK         OE1 GLU B 149                CA    CA B1001     1555   1555  2.32  
LINK         O   LEU B 135                CA    CA B1001     1555   1555  2.32  
LINK         O   GLU B 140                CA    CA B1001     1555   1555  2.33  
LINK         OD2 ASP A 468                NA    NA A2003     1555   1555  2.66  
LINK         OE2 GLU B 149                CA    CA B1001     1555   1555  3.15  
CISPEP   1 ASN A 1221    PRO A 1222          0         2.71                     
CISPEP   2 THR B  695    PRO B  696          0        -3.41                     
SITE     1 AC1  6 ILE A 765  SER A 860  VAL A 862  ASN A 909                    
SITE     2 AC1  6 ASN A 911  NAG A2002                                          
SITE     1 AC2  2 ILE A 765  NAG A2001                                          
SITE     1 AC3  2 ASP A 468  ALA A 521                                          
SITE     1 AC4  6 LEU B 135  ASN B 138  GLU B 140  ASP B 142                    
SITE     2 AC4  6 ASP B 148  GLU B 149                                          
SITE     1 AC5  4 GLU B 221  LYS B 300  ASN B 303  NAG B1003                    
SITE     1 AC6  1 NAG B1002                                                     
SITE     1 AC7  2 THR B  17  BGC B1005                                          
SITE     1 AC8  1 FUC B1004                                                     
SITE     1 AC9  3 TRP B  11  GLU B  51  ASN B 541                               
SITE     1 BC1  4 ASP B   4  TRP B   8  ARG B  25  ARG B 575                    
SITE     1 BC2  4 ALA B 495  ASP B 498  TRP B 550  ARG B 564                    
SITE     1 BC3  3 GLN B 546  TRP B 547  GLU B 581                               
CRYST1  158.949  227.529  278.157  90.00  90.00  90.00 I 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006291  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004395  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003595        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system