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Database: PDB
Entry: 3T5O
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Original site: 3T5O 
HEADER    IMMUNE SYSTEM                           27-JUL-11   3T5O              
TITLE     CRYSTAL STRUCTURE OF HUMAN COMPLEMENT COMPONENT C6                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COMPLEMENT COMPONENT C6;                                   
COMPND   3 CHAIN: A                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    MACPF, MAC, MEMBRANE ATTACK COMPLEX, COMPLEMENT, INNATE IMMUNE        
KEYWDS   2 SYSTEM, BLOOD, MEMBRANE, C7, C8, C9, CYTOLYSIN, IMMUNE SYSTEM        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.E.ALESHIN,B.STEC,L.A.BANKSTON,R.G.DISCIPIO,R.C.LIDDINGTON           
REVDAT   3   11-APR-12 3T5O    1       JRNL                                     
REVDAT   2   08-FEB-12 3T5O    1       JRNL                                     
REVDAT   1   01-FEB-12 3T5O    0                                                
JRNL        AUTH   A.E.ALESHIN,I.U.SCHRAUFSTATTER,B.STEC,L.A.BANKSTON,          
JRNL        AUTH 2 R.C.LIDDINGTON,R.G.DISCIPIO                                  
JRNL        TITL   STRUCTURE OF COMPLEMENT C6 SUGGESTS A MECHANISM FOR          
JRNL        TITL 2 INITIATION AND UNIDIRECTIONAL, SEQUENTIAL ASSEMBLY OF        
JRNL        TITL 3 MEMBRANE ATTACK COMPLEX (MAC).                               
JRNL        REF    J.BIOL.CHEM.                  V. 287 10210 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22267737                                                     
JRNL        DOI    10.1074/JBC.M111.327809                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.87 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.06                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 35743                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2179                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 43.0618 -  6.1756    0.99     3732   233  0.2403 0.2840        
REMARK   3     2  6.1756 -  4.9040    1.00     3614   221  0.2021 0.2576        
REMARK   3     3  4.9040 -  4.2848    1.00     3524   254  0.1694 0.2378        
REMARK   3     4  4.2848 -  3.8933    1.00     3533   223  0.2036 0.2543        
REMARK   3     5  3.8933 -  3.6144    1.00     3528   205  0.2357 0.2679        
REMARK   3     6  3.6144 -  3.4014    1.00     3533   200  0.2411 0.3382        
REMARK   3     7  3.4014 -  3.2311    1.00     3460   249  0.2448 0.2974        
REMARK   3     8  3.2311 -  3.0905    1.00     3496   234  0.2552 0.3236        
REMARK   3     9  3.0905 -  2.9715    0.95     3279   229  0.2681 0.3159        
REMARK   3    10  2.9715 -  2.8690    0.54     1865   131  0.3180 0.3797        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 69.70                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.340           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.64170                                             
REMARK   3    B22 (A**2) : 1.52510                                              
REMARK   3    B33 (A**2) : 1.11670                                              
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           7123                                  
REMARK   3   ANGLE     :  1.408           9572                                  
REMARK   3   CHIRALITY :  0.087           1037                                  
REMARK   3   PLANARITY :  0.006           1246                                  
REMARK   3   DIHEDRAL  : 17.342           2689                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 1:57 OR RESID 1005:1008)            
REMARK   3    ORIGIN FOR THE GROUP (A):  13.4431   1.4421  23.0140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2412 T22:   0.2917                                     
REMARK   3      T33:   0.1882 T12:   0.0472                                     
REMARK   3      T13:  -0.0825 T23:   0.0397                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4048 L22:   3.8599                                     
REMARK   3      L33:   1.2824 L12:  -0.8374                                     
REMARK   3      L13:  -0.0206 L23:  -1.0789                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3157 S12:   0.1241 S13:   0.2598                       
REMARK   3      S21:  -0.4629 S22:  -0.1834 S23:  -0.8039                       
REMARK   3      S31:   0.5236 S32:   0.2378 S33:   0.0121                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 58:118                               
REMARK   3    ORIGIN FOR THE GROUP (A): -30.1121  21.4998  -7.8984              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0501 T22:   0.6259                                     
REMARK   3      T33:   0.7771 T12:  -0.1274                                     
REMARK   3      T13:  -0.0086 T23:   0.3764                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0758 L22:   0.4540                                     
REMARK   3      L33:   0.3185 L12:  -0.1393                                     
REMARK   3      L13:   0.0568 L23:   0.3356                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3141 S12:  -0.0380 S13:  -0.6864                       
REMARK   3      S21:   0.4006 S22:   0.2010 S23:   0.9423                       
REMARK   3      S31:   0.0286 S32:  -0.1227 S33:  -0.2482                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 119:536 OR RESID 1001:1003 OR       
REMARK   3               RESID 601:608)                                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5118  39.9569 -18.2742              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1946 T22:   0.2224                                     
REMARK   3      T33:   0.2946 T12:  -0.0068                                     
REMARK   3      T13:  -0.0043 T23:   0.1983                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2258 L22:   1.1197                                     
REMARK   3      L33:   1.3988 L12:  -0.9197                                     
REMARK   3      L13:   0.7589 L23:  -0.8599                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0293 S12:  -0.1152 S13:   0.3896                       
REMARK   3      S21:   0.2693 S22:   0.1830 S23:  -0.0304                       
REMARK   3      S31:  -0.2712 S32:  -0.1991 S33:  -0.0636                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 537:591 OR RESID 1009:1010)         
REMARK   3    ORIGIN FOR THE GROUP (A): -11.8476  34.3441  12.1780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1256 T22:   1.5472                                     
REMARK   3      T33:   1.0328 T12:   0.1483                                     
REMARK   3      T13:   0.0887 T23:  -0.3649                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1003 L22:   1.5299                                     
REMARK   3      L33:   0.1981 L12:  -0.9746                                     
REMARK   3      L13:  -0.5842 L23:  -0.1725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1034 S12:   0.5319 S13:   0.7547                       
REMARK   3      S21:   1.1216 S22:  -0.2714 S23:   0.3385                       
REMARK   3      S31:  -0.8302 S32:  -0.0821 S33:   0.3283                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 620:681                              
REMARK   3    ORIGIN FOR THE GROUP (A): -62.8182  76.1868 -27.7196              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4184 T22:   0.2653                                     
REMARK   3      T33:   0.3701 T12:   0.0990                                     
REMARK   3      T13:   0.0730 T23:   0.1417                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7590 L22:   0.3791                                     
REMARK   3      L33:   0.2874 L12:  -0.2583                                     
REMARK   3      L13:  -0.0218 L23:   0.1540                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2100 S12:  -0.2159 S13:   0.1306                       
REMARK   3      S21:  -0.4696 S22:  -0.1962 S23:  -0.2904                       
REMARK   3      S31:  -0.0122 S32:   0.0589 S33:   0.1417                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 682:744                              
REMARK   3    ORIGIN FOR THE GROUP (A): -86.3530  93.2670 -50.4192              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3083 T22:   0.4940                                     
REMARK   3      T33:   0.2644 T12:   0.2036                                     
REMARK   3      T13:  -0.4004 T23:  -0.0513                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3251 L22:   0.7507                                     
REMARK   3      L33:   1.5754 L12:   0.0954                                     
REMARK   3      L13:  -0.0648 L23:  -1.0514                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0722 S12:   0.3230 S13:   0.0398                       
REMARK   3      S21:  -1.3948 S22:  -0.7285 S23:   0.0752                       
REMARK   3      S31:  -0.3921 S32:   0.8743 S33:  -0.0569                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 750:832                              
REMARK   3    ORIGIN FOR THE GROUP (A):-106.5545  85.8402 -80.4326              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5872 T22:   0.6685                                     
REMARK   3      T33:   1.4047 T12:  -0.2277                                     
REMARK   3      T13:   0.1490 T23:  -0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4876 L22:   0.0855                                     
REMARK   3      L33:   0.3890 L12:  -0.0863                                     
REMARK   3      L13:  -0.2674 L23:   0.2042                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0245 S12:  -0.5782 S13:  -0.2931                       
REMARK   3      S21:   0.3663 S22:   0.4233 S23:   0.2658                       
REMARK   3      S31:   0.4020 S32:  -0.4735 S33:   0.2786                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 833:913                              
REMARK   3    ORIGIN FOR THE GROUP (A):-120.1517  68.5702 -74.1476              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2988 T22:   1.0751                                     
REMARK   3      T33:   1.9244 T12:  -0.1707                                     
REMARK   3      T13:   0.0772 T23:  -0.0289                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6369 L22:   0.3082                                     
REMARK   3      L33:   1.4331 L12:  -0.0761                                     
REMARK   3      L13:   0.8550 L23:   0.2340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8534 S12:   0.5652 S13:  -0.4158                       
REMARK   3      S21:  -0.0968 S22:  -0.0536 S23:  -0.1551                       
REMARK   3      S31:   0.0520 S32:   0.5814 S33:  -0.8808                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE LAST DOMAIN (RESIDUES 834-913) WAS    
REMARK   3  BUILT BY THREADING THE AMINO ACID SEQUENCE ON THE NMR STRUCTURE     
REMARK   3  OF SAME DOMAIN FROM C7 (PDB ENTRY 2WCY). SINCE THE ELECTRON         
REMARK   3  DENSITY WAS WEAK, THE SEQUENCE ANNOTATION IS NOT RELIABLE.          
REMARK   4                                                                      
REMARK   4 3T5O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB067068.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 180                                
REMARK 200  PH                             : 5.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.991                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35745                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.860                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 8.300                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.86                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.04                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.50000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MM MES, 89 MM SODIUM CHLORIDE, 0.01    
REMARK 280  MM CADMIUM CHLORIDE, PH 5.8, EVAPORATION, TEMPERATURE 284K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       73.40500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       90.07500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       73.40500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       90.07500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     ASN A   243                                                      
REMARK 465     GLU A   244                                                      
REMARK 465     ASN A   245                                                      
REMARK 465     GLN A   246                                                      
REMARK 465     GLN A   247                                                      
REMARK 465     GLY A   248                                                      
REMARK 465     SER A   249                                                      
REMARK 465     PHE A   250                                                      
REMARK 465     SER A   251                                                      
REMARK 465     SER A   252                                                      
REMARK 465     GLN A   253                                                      
REMARK 465     GLY A   254                                                      
REMARK 465     GLY A   255                                                      
REMARK 465     SER A   256                                                      
REMARK 465     SER A   257                                                      
REMARK 465     PHE A   258                                                      
REMARK 465     SER A   259                                                      
REMARK 465     PHE A   592                                                      
REMARK 465     SER A   593                                                      
REMARK 465     ILE A   594                                                      
REMARK 465     MET A   595                                                      
REMARK 465     GLU A   596                                                      
REMARK 465     ASN A   597                                                      
REMARK 465     ASN A   598                                                      
REMARK 465     GLY A   599                                                      
REMARK 465     GLN A   600                                                      
REMARK 465     MET A   609                                                      
REMARK 465     LYS A   610                                                      
REMARK 465     GLU A   611                                                      
REMARK 465     VAL A   612                                                      
REMARK 465     ASP A   613                                                      
REMARK 465     LEU A   614                                                      
REMARK 465     PRO A   615                                                      
REMARK 465     GLU A   616                                                      
REMARK 465     ILE A   617                                                      
REMARK 465     GLU A   618                                                      
REMARK 465     ALA A   619                                                      
REMARK 465     LEU A   745                                                      
REMARK 465     THR A   746                                                      
REMARK 465     LYS A   747                                                      
REMARK 465     LEU A   748                                                      
REMARK 465     LYS A   749                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 851    CD   CE   NZ                                        
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    GLU A   567     OD1  ASN A   569              1.84            
REMARK 500   CB   CYS A   711     SG   CYS A   740              1.95            
REMARK 500   ND2  ASN A   303     C2   NAG A  1002              2.18            
REMARK 500   OD1  ASP A   126     NH2  ARG A   150              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  58   C   -  N   -  CA  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    PRO A 499   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    LEU A 652   CA  -  CB  -  CG  ANGL. DEV. = -15.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  20       92.19     80.55                                   
REMARK 500    ASN A  53       59.80     31.87                                   
REMARK 500    ASP A  65      158.31    -49.06                                   
REMARK 500    ASP A  73       29.72   -144.20                                   
REMARK 500    LEU A  86      -70.11    -66.13                                   
REMARK 500    PHE A  91       41.39     40.00                                   
REMARK 500    THR A  97      -22.72   -145.60                                   
REMARK 500    ASP A 118      -54.75   -144.27                                   
REMARK 500    LYS A 120     -100.24    -88.11                                   
REMARK 500    CYS A 137       58.58     30.55                                   
REMARK 500    ASN A 141       89.33    -59.25                                   
REMARK 500    ASN A 146       15.54     55.32                                   
REMARK 500    ASP A 148        8.85    -65.75                                   
REMARK 500    GLU A 149       -1.57   -140.94                                   
REMARK 500    ARG A 150      -86.67    -37.54                                   
REMARK 500    ARG A 184     -134.65   -113.78                                   
REMARK 500    CYS A 197       74.58   -108.40                                   
REMARK 500    THR A 205       57.93   -143.84                                   
REMARK 500    SER A 206     -128.50     56.06                                   
REMARK 500    ASP A 227      -39.02    -30.71                                   
REMARK 500    ASN A 275      -35.86    -30.98                                   
REMARK 500    LYS A 288      157.90    174.07                                   
REMARK 500    LYS A 297      114.12   -166.77                                   
REMARK 500    PHE A 304      140.52   -178.65                                   
REMARK 500    LEU A 313      172.81    -57.23                                   
REMARK 500    ASP A 315      -70.56    -53.25                                   
REMARK 500    HIS A 323       11.17    -59.80                                   
REMARK 500    THR A 342      -30.84   -138.75                                   
REMARK 500    HIS A 408       39.37   -154.93                                   
REMARK 500    GLN A 414        2.12    -65.37                                   
REMARK 500    LYS A 438      131.53    -25.85                                   
REMARK 500    GLU A 453      -72.44    -47.65                                   
REMARK 500    ASN A 458       64.43   -152.40                                   
REMARK 500    ASP A 471        1.16    -68.23                                   
REMARK 500    ILE A 476     -163.26   -102.61                                   
REMARK 500    CYS A 478       79.66   -110.62                                   
REMARK 500    PRO A 506      -46.90    -24.11                                   
REMARK 500    ASN A 508       19.76     57.67                                   
REMARK 500    TYR A 527     -156.28   -144.13                                   
REMARK 500    SER A 540      154.80    -32.38                                   
REMARK 500    ASN A 541       26.38   -143.79                                   
REMARK 500    ASN A 569     -127.83   -101.35                                   
REMARK 500    ASN A 570     -122.56     57.82                                   
REMARK 500    LEU A 652      170.90    -54.24                                   
REMARK 500    ASP A 668      -34.44    -32.30                                   
REMARK 500    ASP A 675       62.64    -69.65                                   
REMARK 500    PRO A 686      162.21    -49.10                                   
REMARK 500    VAL A 687      101.01    -53.13                                   
REMARK 500    PRO A 712     -179.52    -43.47                                   
REMARK 500    ASN A 728       19.87     58.45                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      76 RAMACHANDRAN OUTLIERS.                        
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                              CD A1001  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 140   O                                                      
REMARK 620 2 ASN A 138   OD1  92.3                                              
REMARK 620 3 LEU A 135   O   151.7  99.6                                        
REMARK 620 4 ASP A 142   OD2  75.0  86.8  80.1                                  
REMARK 620 5 GLU A 149   OE1  80.0  93.5 124.3 155.0                            
REMARK 620 6 ASP A 148   OD1  87.8 175.8  78.6  89.2  90.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUL A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1010                
DBREF  3T5O A    1   913  UNP    P13671   CO6_HUMAN       22    934             
SEQRES   1 A  913  CYS PHE CYS ASP HIS TYR ALA TRP THR GLN TRP THR SER          
SEQRES   2 A  913  CYS SER LYS THR CYS ASN SER GLY THR GLN SER ARG HIS          
SEQRES   3 A  913  ARG GLN ILE VAL VAL ASP LYS TYR TYR GLN GLU ASN PHE          
SEQRES   4 A  913  CYS GLU GLN ILE CYS SER LYS GLN GLU THR ARG GLU CYS          
SEQRES   5 A  913  ASN TRP GLN ARG CYS PRO ILE ASN CYS LEU LEU GLY ASP          
SEQRES   6 A  913  PHE GLY PRO TRP SER ASP CYS ASP PRO CYS ILE GLU LYS          
SEQRES   7 A  913  GLN SER LYS VAL ARG SER VAL LEU ARG PRO SER GLN PHE          
SEQRES   8 A  913  GLY GLY GLN PRO CYS THR ALA PRO LEU VAL ALA PHE GLN          
SEQRES   9 A  913  PRO CYS ILE PRO SER LYS LEU CYS LYS ILE GLU GLU ALA          
SEQRES  10 A  913  ASP CYS LYS ASN LYS PHE ARG CYS ASP SER GLY ARG CYS          
SEQRES  11 A  913  ILE ALA ARG LYS LEU GLU CYS ASN GLY GLU ASN ASP CYS          
SEQRES  12 A  913  GLY ASP ASN SER ASP GLU ARG ASP CYS GLY ARG THR LYS          
SEQRES  13 A  913  ALA VAL CYS THR ARG LYS TYR ASN PRO ILE PRO SER VAL          
SEQRES  14 A  913  GLN LEU MET GLY ASN GLY PHE HIS PHE LEU ALA GLY GLU          
SEQRES  15 A  913  PRO ARG GLY GLU VAL LEU ASP ASN SER PHE THR GLY GLY          
SEQRES  16 A  913  ILE CYS LYS THR VAL LYS SER SER ARG THR SER ASN PRO          
SEQRES  17 A  913  TYR ARG VAL PRO ALA ASN LEU GLU ASN VAL GLY PHE GLU          
SEQRES  18 A  913  VAL GLN THR ALA GLU ASP ASP LEU LYS THR ASP PHE TYR          
SEQRES  19 A  913  LYS ASP LEU THR SER LEU GLY HIS ASN GLU ASN GLN GLN          
SEQRES  20 A  913  GLY SER PHE SER SER GLN GLY GLY SER SER PHE SER VAL          
SEQRES  21 A  913  PRO ILE PHE TYR SER SER LYS ARG SER GLU ASN ILE ASN          
SEQRES  22 A  913  HIS ASN SER ALA PHE LYS GLN ALA ILE GLN ALA SER HIS          
SEQRES  23 A  913  LYS LYS ASP SER SER PHE ILE ARG ILE HIS LYS VAL MET          
SEQRES  24 A  913  LYS VAL LEU ASN PHE THR THR LYS ALA LYS ASP LEU HIS          
SEQRES  25 A  913  LEU SER ASP VAL PHE LEU LYS ALA LEU ASN HIS LEU PRO          
SEQRES  26 A  913  LEU GLU TYR ASN SER ALA LEU TYR SER ARG ILE PHE ASP          
SEQRES  27 A  913  ASP PHE GLY THR HIS TYR PHE THR SER GLY SER LEU GLY          
SEQRES  28 A  913  GLY VAL TYR ASP LEU LEU TYR GLN PHE SER SER GLU GLU          
SEQRES  29 A  913  LEU LYS ASN SER GLY LEU THR GLU GLU GLU ALA LYS HIS          
SEQRES  30 A  913  CYS VAL ARG ILE GLU THR LYS LYS ARG VAL LEU PHE ALA          
SEQRES  31 A  913  LYS LYS THR LYS VAL GLU HIS ARG CYS THR THR ASN LYS          
SEQRES  32 A  913  LEU SER GLU LYS HIS GLU GLY SER PHE ILE GLN GLY ALA          
SEQRES  33 A  913  GLU LYS SER ILE SER LEU ILE ARG GLY GLY ARG SER GLU          
SEQRES  34 A  913  TYR GLY ALA ALA LEU ALA TRP GLU LYS GLY SER SER GLY          
SEQRES  35 A  913  LEU GLU GLU LYS THR PHE SER GLU TRP LEU GLU SER VAL          
SEQRES  36 A  913  LYS GLU ASN PRO ALA VAL ILE ASP PHE GLU LEU ALA PRO          
SEQRES  37 A  913  ILE VAL ASP LEU VAL ARG ASN ILE PRO CYS ALA VAL THR          
SEQRES  38 A  913  LYS ARG ASN ASN LEU ARG LYS ALA LEU GLN GLU TYR ALA          
SEQRES  39 A  913  ALA LYS PHE ASP PRO CYS GLN CYS ALA PRO CYS PRO ASN          
SEQRES  40 A  913  ASN GLY ARG PRO THR LEU SER GLY THR GLU CYS LEU CYS          
SEQRES  41 A  913  VAL CYS GLN SER GLY THR TYR GLY GLU ASN CYS GLU LYS          
SEQRES  42 A  913  GLN SER PRO ASP TYR LYS SER ASN ALA VAL ASP GLY GLN          
SEQRES  43 A  913  TRP GLY CYS TRP SER SER TRP SER THR CYS ASP ALA THR          
SEQRES  44 A  913  TYR LYS ARG SER ARG THR ARG GLU CYS ASN ASN PRO ALA          
SEQRES  45 A  913  PRO GLN ARG GLY GLY LYS ARG CYS GLU GLY GLU LYS ARG          
SEQRES  46 A  913  GLN GLU GLU ASP CYS THR PHE SER ILE MET GLU ASN ASN          
SEQRES  47 A  913  GLY GLN PRO CYS ILE ASN ASP ASP GLU GLU MET LYS GLU          
SEQRES  48 A  913  VAL ASP LEU PRO GLU ILE GLU ALA ASP SER GLY CYS PRO          
SEQRES  49 A  913  GLN PRO VAL PRO PRO GLU ASN GLY PHE ILE ARG ASN GLU          
SEQRES  50 A  913  LYS GLN LEU TYR LEU VAL GLY GLU ASP VAL GLU ILE SER          
SEQRES  51 A  913  CYS LEU THR GLY PHE GLU THR VAL GLY TYR GLN TYR PHE          
SEQRES  52 A  913  ARG CYS LEU PRO ASP GLY THR TRP ARG GLN GLY ASP VAL          
SEQRES  53 A  913  GLU CYS GLN ARG THR GLU CYS ILE LYS PRO VAL VAL GLN          
SEQRES  54 A  913  GLU VAL LEU THR ILE THR PRO PHE GLN ARG LEU TYR ARG          
SEQRES  55 A  913  ILE GLY GLU SER ILE GLU LEU THR CYS PRO LYS GLY PHE          
SEQRES  56 A  913  VAL VAL ALA GLY PRO SER ARG TYR THR CYS GLN GLY ASN          
SEQRES  57 A  913  SER TRP THR PRO PRO ILE SER ASN SER LEU THR CYS GLU          
SEQRES  58 A  913  LYS ASP THR LEU THR LYS LEU LYS GLY HIS CYS GLN LEU          
SEQRES  59 A  913  GLY GLN LYS GLN SER GLY SER GLU CYS ILE CYS MET SER          
SEQRES  60 A  913  PRO GLU GLU ASP CYS SER HIS HIS SER GLU ASP LEU CYS          
SEQRES  61 A  913  VAL PHE ASP THR ASP SER ASN ASP TYR PHE THR SER PRO          
SEQRES  62 A  913  ALA CYS LYS PHE LEU ALA GLU LYS CYS LEU ASN ASN GLN          
SEQRES  63 A  913  GLN LEU HIS PHE LEU HIS ILE GLY SER CYS GLN ASP GLY          
SEQRES  64 A  913  ARG GLN LEU GLU TRP GLY LEU GLU ARG THR ARG LEU SER          
SEQRES  65 A  913  SER ASN SER THR LYS LYS GLU SER CYS GLY TYR ASP THR          
SEQRES  66 A  913  CYS TYR ASP TRP GLU LYS CYS SER ALA SER THR SER LYS          
SEQRES  67 A  913  CYS VAL CYS LEU LEU PRO PRO GLN CYS PHE LYS GLY GLY          
SEQRES  68 A  913  ASN GLN LEU TYR CYS VAL LYS MET GLY SER SER THR SER          
SEQRES  69 A  913  GLU LYS THR LEU ASN ILE CYS GLU VAL GLY THR ILE ARG          
SEQRES  70 A  913  CYS ALA ASN ARG LYS MET GLU ILE LEU HIS PRO GLY LYS          
SEQRES  71 A  913  CYS LEU ALA                                                  
MODRES 3T5O ASN A  303  ASN  GLYCOSYLATION SITE                                 
MODRES 3T5O THR A   17  THR  GLYCOSYLATION SITE                                 
MODRES 3T5O THR A  371  THR  GLYCOSYLATION SITE                                 
HET     CD  A1001       1                                                       
HET    NAG  A1002      14                                                       
HET    NAG  A1003      14                                                       
HET    FUL  A1004      10                                                       
HET    FUC  A1005      10                                                       
HET    BGC  A1006      11                                                       
HET    MAN  A1007      11                                                       
HET    MAN  A1008      11                                                       
HET    MAN  A1009      11                                                       
HET    MAN  A1010      11                                                       
HETNAM      CD CADMIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUL BETA-L-FUCOSE                                                    
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BGC BETA-D-GLUCOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
FORMUL   2   CD    CD 2+                                                        
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4  FUL    C6 H12 O5                                                    
FORMUL   5  FUC    C6 H12 O5                                                    
FORMUL   5  BGC    C6 H12 O6                                                    
FORMUL   6  MAN    4(C6 H12 O6)                                                 
HELIX    1   1 PHE A    2  TYR A    6  5                                   5    
HELIX    2   2 ASP A   32  ASN A   38  1                                   7    
HELIX    3   3 PHE A   39  CYS A   44  1                                   6    
HELIX    4   4 ALA A  132  GLU A  136  5                                   5    
HELIX    5   5 ASN A  146  ARG A  150  5                                   5    
HELIX    6   6 SER A  168  MET A  172  5                                   5    
HELIX    7   7 ASP A  236  HIS A  242  5                                   7    
HELIX    8   8 SER A  276  LYS A  287  1                                  12    
HELIX    9   9 SER A  314  HIS A  323  1                                  10    
HELIX   10  10 ASN A  329  GLY A  341  1                                  13    
HELIX   11  11 SER A  362  GLY A  369  1                                   8    
HELIX   12  12 THR A  371  VAL A  387  1                                  17    
HELIX   13  13 GLU A  396  THR A  400  5                                   5    
HELIX   14  14 LEU A  404  GLU A  409  5                                   6    
HELIX   15  15 PHE A  412  ALA A  416  5                                   5    
HELIX   16  16 ARG A  427  ALA A  435  1                                   9    
HELIX   17  17 GLU A  444  ASN A  458  1                                  15    
HELIX   18  18 VAL A  470  VAL A  473  5                                   4    
HELIX   19  19 CYS A  478  LYS A  496  1                                  19    
HELIX   20  20 PHE A  497  CYS A  502  5                                   6    
HELIX   21  21 ASP A  785  ASN A  787  5                                   3    
HELIX   22  22 ALA A  794  CYS A  802  1                                   9    
HELIX   23  23 LEU A  803  GLN A  806  5                                   4    
HELIX   24  24 GLY A  819  SER A  832  1                                  14    
SHEET    1   A 2 GLY A  21  HIS A  26  0                                        
SHEET    2   A 2 GLN A  47  CYS A  52 -1  O  GLU A  48   N  ARG A  25           
SHEET    1   B 2 LEU A  62  LEU A  63  0                                        
SHEET    2   B 2 VAL A  85  ARG A  87 -1  O  ARG A  87   N  LEU A  62           
SHEET    1   C 2 LYS A  78  GLN A  79  0                                        
SHEET    2   C 2 GLN A 104  PRO A 105 -1  O  GLN A 104   N  GLN A  79           
SHEET    1   D 3 SER A  89  GLN A  90  0                                        
SHEET    2   D 3 GLU A 517  VAL A 521  1  O  CYS A 518   N  SER A  89           
SHEET    3   D 3 ARG A 510  SER A 514 -1  N  SER A 514   O  GLU A 517           
SHEET    1   E 2 PHE A 123  ARG A 124  0                                        
SHEET    2   E 2 CYS A 130  ILE A 131 -1  O  ILE A 131   N  PHE A 123           
SHEET    1   F 2 ASN A 164  PRO A 165  0                                        
SHEET    2   F 2 TYR A 209  ARG A 210  1  O  ARG A 210   N  ASN A 164           
SHEET    1   G 5 LEU A 215  GLY A 219  0                                        
SHEET    2   G 5 SER A 290  THR A 306 -1  O  THR A 305   N  ASN A 217           
SHEET    3   G 5 HIS A 343  SER A 361 -1  O  THR A 346   N  THR A 306           
SHEET    4   G 5 ASN A 174  HIS A 177 -1  N  PHE A 176   O  HIS A 343           
SHEET    5   G 5 GLU A 182  GLU A 186 -1  O  ARG A 184   N  GLY A 175           
SHEET    1   H 4 LEU A 229  TYR A 234  0                                        
SHEET    2   H 4 SER A 290  THR A 306 -1  O  PHE A 292   N  TYR A 234           
SHEET    3   H 4 HIS A 343  SER A 361 -1  O  THR A 346   N  THR A 306           
SHEET    4   H 4 LYS A 418  SER A 421 -1  O  ILE A 420   N  LEU A 357           
SHEET    1   I 4 ALA A 460  PRO A 468  0                                        
SHEET    2   I 4 HIS A 343  SER A 361 -1  N  GLY A 351   O  ALA A 460           
SHEET    3   I 4 SER A 290  THR A 306 -1  N  THR A 306   O  THR A 346           
SHEET    4   I 4 LEU A 215  GLY A 219 -1  N  ASN A 217   O  THR A 305           
SHEET    1   J 2 ARG A 562  THR A 565  0                                        
SHEET    2   J 2 ARG A 585  GLU A 588 -1  O  GLN A 586   N  ARG A 564           
SHEET    1   K 4 GLY A 632  ILE A 634  0                                        
SHEET    2   K 4 ASP A 646  CYS A 651 -1  O  SER A 650   N  PHE A 633           
SHEET    3   K 4 TYR A 662  CYS A 665 -1  O  PHE A 663   N  VAL A 647           
SHEET    4   K 4 TRP A 671  ARG A 672 -1  O  ARG A 672   N  ARG A 664           
SHEET    1   L 2 PHE A 655  VAL A 658  0                                        
SHEET    2   L 2 GLU A 677  ARG A 680 -1  O  GLN A 679   N  GLU A 656           
SHEET    1   M 2 GLU A 682  ILE A 684  0                                        
SHEET    2   M 2 LEU A 700  ARG A 702 -1  O  TYR A 701   N  CYS A 683           
SHEET    1   N 2 SER A 706  GLU A 708  0                                        
SHEET    2   N 2 ARG A 722  THR A 724 -1  O  TYR A 723   N  ILE A 707           
SHEET    1   O 2 PHE A 715  VAL A 716  0                                        
SHEET    2   O 2 GLU A 741  LYS A 742 -1  O  GLU A 741   N  VAL A 716           
SHEET    1   P 2 GLN A 756  SER A 759  0                                        
SHEET    2   P 2 GLU A 762  CYS A 765 -1  O  ILE A 764   N  LYS A 757           
SHEET    1   Q 3 ASP A 788  PRO A 793  0                                        
SHEET    2   Q 3 ASP A 778  ASP A 783 -1  N  LEU A 779   O  SER A 792           
SHEET    3   Q 3 LEU A 808  ILE A 813 -1  O  HIS A 809   N  PHE A 782           
SSBOND   1 CYS A    1    CYS A   40                          1555   1555  2.04  
SSBOND   2 CYS A    3    CYS A   44                          1555   1555  2.02  
SSBOND   3 CYS A   14    CYS A   52                          1555   1555  2.03  
SSBOND   4 CYS A   18    CYS A   57                          1555   1555  2.02  
SSBOND   5 CYS A   61    CYS A   96                          1555   1555  2.03  
SSBOND   6 CYS A   72    CYS A  106                          1555   1555  2.03  
SSBOND   7 CYS A   75    CYS A  112                          1555   1555  2.04  
SSBOND   8 CYS A  119    CYS A  130                          1555   1555  2.03  
SSBOND   9 CYS A  125    CYS A  143                          1555   1555  2.04  
SSBOND  10 CYS A  137    CYS A  152                          1555   1555  2.03  
SSBOND  11 CYS A  159    CYS A  197                          1555   1555  2.04  
SSBOND  12 CYS A  378    CYS A  399                          1555   1555  2.07  
SSBOND  13 CYS A  478    CYS A  602                          1555   1555  2.02  
SSBOND  14 CYS A  500    CYS A  549                          1555   1555  2.05  
SSBOND  15 CYS A  502    CYS A  518                          1555   1555  2.03  
SSBOND  16 CYS A  505    CYS A  520                          1555   1555  2.05  
SSBOND  17 CYS A  522    CYS A  531                          1555   1555  2.06  
SSBOND  18 CYS A  556    CYS A  590                          1555   1555  2.04  
SSBOND  19 CYS A  568    CYS A  580                          1555   1555  2.03  
SSBOND  20 CYS A  623    CYS A  665                          1555   1555  2.03  
SSBOND  21 CYS A  651    CYS A  678                          1555   1555  2.08  
SSBOND  22 CYS A  683    CYS A  725                          1555   1555  2.03  
SSBOND  23 CYS A  711    CYS A  740                          1555   1555  2.03  
SSBOND  24 CYS A  752    CYS A  763                          1555   1555  1.94  
SSBOND  25 CYS A  765    CYS A  802                          1555   1555  2.03  
SSBOND  26 CYS A  772    CYS A  795                          1555   1555  2.04  
SSBOND  27 CYS A  780    CYS A  816                          1555   1555  2.04  
SSBOND  28 CYS A  841    CYS A  852                          1555   1555  2.04  
SSBOND  29 CYS A  846    CYS A  859                          1555   1555  2.03  
SSBOND  30 CYS A  861    CYS A  898                          1555   1555  2.03  
SSBOND  31 CYS A  867    CYS A  891                          1555   1555  2.03  
SSBOND  32 CYS A  876    CYS A  911                          1555   1555  2.03  
LINK         ND2 ASN A 303                 C1  NAG A1002     1555   1555  1.43  
LINK         O3  FUC A1005                 C1  BGC A1006     1555   1555  1.43  
LINK         O4  NAG A1002                 C1  NAG A1003     1555   1555  1.45  
LINK         OG1 THR A  17                 C1  FUC A1005     1555   1555  1.44  
LINK         OG1 THR A 371                 C1  FUL A1004     1555   1555  1.46  
LINK         C1  MAN A1007                 CD1 TRP A  11     1555   1555  1.44  
LINK         C1  MAN A1008                 CD1 TRP A   8     1555   1555  1.44  
LINK         C1  MAN A1009                 CD1 TRP A 550     1555   1555  1.45  
LINK         C1  MAN A1010                 CD1 TRP A 547     1555   1555  1.46  
LINK         O   GLU A 140                CD    CD A1001     1555   1555  2.39  
LINK         OD1 ASN A 138                CD    CD A1001     1555   1555  2.40  
LINK         O   LEU A 135                CD    CD A1001     1555   1555  2.41  
LINK         OD2 ASP A 142                CD    CD A1001     1555   1555  2.41  
LINK         OE1 GLU A 149                CD    CD A1001     1555   1555  2.42  
LINK         OD1 ASP A 148                CD    CD A1001     1555   1555  2.42  
CISPEP   1 THR A  695    PRO A  696          0         2.85                     
CISPEP   2 THR A  731    PRO A  732          0       -16.81                     
CISPEP   3 TYR A  843    ASP A  844          0        -3.38                     
SITE     1 AC1  6 LEU A 135  ASN A 138  GLU A 140  ASP A 142                    
SITE     2 AC1  6 ASP A 148  GLU A 149                                          
SITE     1 AC2  6 GLY A 219  PHE A 220  GLU A 221  LYS A 267                    
SITE     2 AC2  6 ASN A 303  NAG A1003                                          
SITE     1 AC3  2 GLU A 221  NAG A1002                                          
SITE     1 AC4  3 THR A 371  GLU A 372  GLU A 373                               
SITE     1 AC5  3 THR A  17  CYS A  18  BGC A1006                               
SITE     1 AC6  2 LYS A  16  FUC A1005                                          
SITE     1 AC7  3 GLN A  10  TRP A  11  ARG A  50                               
SITE     1 AC8  6 ALA A   7  TRP A   8  ARG A  25  HIS A 775                    
SITE     2 AC8  6 ASP A 778  THR A 791                                          
SITE     1 AC9  4 ALA A 495  ASP A 498  TRP A 550  ARG A 564                    
SITE     1 BC1  5 GLY A 545  GLN A 546  TRP A 547  CYS A 580                    
SITE     2 BC1  5 GLU A 581                                                     
CRYST1  146.810  180.150   60.530  90.00  90.00  90.00 P 21 21 2     4          
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      0.006812  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005551  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016521        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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