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Database: PDB
Entry: 6CQW
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HEADER    HYDROLASE                               16-MAR-18   6CQW              
TITLE     CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE IN COMPLEX
TITLE    2 WITH VX(-) AND HI-6                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ACHE;                                                       
COMPND   5 EC: 3.1.1.7;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACHE;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.M.BESTER,M.A.GUELTA,S.D.PEGAN,J.J.HEIGHT                            
REVDAT   2   27-MAR-19 6CQW    1       JRNL                                     
REVDAT   1   05-DEC-18 6CQW    0                                                
JRNL        AUTH   S.M.BESTER,M.A.GUELTA,J.CHEUNG,M.D.WINEMILLER,S.Y.BAE,       
JRNL        AUTH 2 J.MYSLINSKI,S.D.PEGAN,J.J.HEIGHT                             
JRNL        TITL   STRUCTURAL INSIGHTS OF STEREOSPECIFIC INHIBITION OF HUMAN    
JRNL        TITL 2 ACETYLCHOLINESTERASE BY VX AND SUBSEQUENT REACTIVATION BY    
JRNL        TITL 3 HI-6.                                                        
JRNL        REF    CHEM. RES. TOXICOL.           V.  31  1405 2018              
JRNL        REFN                   ISSN 1520-5010                               
JRNL        PMID   30462502                                                     
JRNL        DOI    10.1021/ACS.CHEMRESTOX.8B00294                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.28 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.67                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 95442                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4748                            
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 39.6799 -  7.0643    0.99     3291   173  0.1737 0.1859        
REMARK   3     2  7.0643 -  5.6122    1.00     3182   156  0.1771 0.2053        
REMARK   3     3  5.6122 -  4.9042    1.00     3120   146  0.1512 0.1664        
REMARK   3     4  4.9042 -  4.4565    0.99     3097   145  0.1254 0.1541        
REMARK   3     5  4.4565 -  4.1374    1.00     3070   163  0.1331 0.1520        
REMARK   3     6  4.1374 -  3.8937    1.00     3017   179  0.1363 0.1555        
REMARK   3     7  3.8937 -  3.6989    1.00     3061   172  0.1460 0.1676        
REMARK   3     8  3.6989 -  3.5380    1.00     3055   140  0.1673 0.1912        
REMARK   3     9  3.5380 -  3.4018    1.00     3023   189  0.1708 0.1949        
REMARK   3    10  3.4018 -  3.2845    1.00     3016   162  0.1750 0.2015        
REMARK   3    11  3.2845 -  3.1819    1.00     3013   159  0.1827 0.2074        
REMARK   3    12  3.1819 -  3.0909    1.00     3043   166  0.1835 0.2312        
REMARK   3    13  3.0909 -  3.0096    1.00     2993   183  0.1815 0.2057        
REMARK   3    14  3.0096 -  2.9362    1.00     3029   153  0.1860 0.2505        
REMARK   3    15  2.9362 -  2.8695    1.00     2981   205  0.1970 0.2308        
REMARK   3    16  2.8695 -  2.8084    1.00     3003   179  0.2024 0.2239        
REMARK   3    17  2.8084 -  2.7522    1.00     2997   142  0.1971 0.2548        
REMARK   3    18  2.7522 -  2.7003    1.00     3034   153  0.1998 0.2550        
REMARK   3    19  2.7003 -  2.6521    1.00     3025   163  0.1951 0.2319        
REMARK   3    20  2.6521 -  2.6072    1.00     3013   148  0.2028 0.2427        
REMARK   3    21  2.6072 -  2.5651    1.00     2980   152  0.1995 0.2405        
REMARK   3    22  2.5651 -  2.5257    1.00     3014   158  0.2057 0.2412        
REMARK   3    23  2.5257 -  2.4885    1.00     3032   141  0.2035 0.2409        
REMARK   3    24  2.4885 -  2.4535    1.00     3020   139  0.2106 0.2274        
REMARK   3    25  2.4535 -  2.4203    1.00     2975   181  0.2137 0.2641        
REMARK   3    26  2.4203 -  2.3889    1.00     2980   146  0.2244 0.2611        
REMARK   3    27  2.3889 -  2.3590    1.00     3045   142  0.2320 0.3068        
REMARK   3    28  2.3590 -  2.3306    1.00     2945   154  0.2410 0.2708        
REMARK   3    29  2.3306 -  2.3035    0.97     2991   130  0.2496 0.2877        
REMARK   3    30  2.3035 -  2.2776    0.89     2649   129  0.2775 0.3747        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.980           
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           8839                                  
REMARK   3   ANGLE     :  0.721          12108                                  
REMARK   3   CHIRALITY :  0.046           1302                                  
REMARK   3   PLANARITY :  0.006           1592                                  
REMARK   3   DIHEDRAL  : 14.381           5177                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 3:32)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  71.9801  40.4330  45.5772              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6348 T22:   0.5669                                     
REMARK   3      T33:   0.4408 T12:  -0.0925                                     
REMARK   3      T13:  -0.1278 T23:  -0.0401                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6656 L22:   4.4463                                     
REMARK   3      L33:   7.0157 L12:  -1.3039                                     
REMARK   3      L13:  -3.8883 L23:   2.4520                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0415 S12:  -0.5229 S13:   0.3504                       
REMARK   3      S21:   0.5124 S22:   0.0943 S23:  -0.5908                       
REMARK   3      S31:  -0.4982 S32:   0.7845 S33:  -0.1042                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 33:490)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  54.1776  29.0222  26.0515              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3093 T22:   0.3357                                     
REMARK   3      T33:   0.3043 T12:   0.0235                                     
REMARK   3      T13:  -0.0323 T23:   0.0188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3319 L22:   1.0002                                     
REMARK   3      L33:   2.7973 L12:   0.1108                                     
REMARK   3      L13:   0.7997 L23:   0.2653                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0555 S12:  -0.1017 S13:  -0.0648                       
REMARK   3      S21:   0.0018 S22:   0.0313 S23:   0.0070                       
REMARK   3      S31:  -0.2281 S32:  -0.1195 S33:   0.0201                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 491:542)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  55.2456  36.7949   6.3767              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5802 T22:   0.4293                                     
REMARK   3      T33:   0.2923 T12:  -0.0475                                     
REMARK   3      T13:  -0.0643 T23:   0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8590 L22:   2.4300                                     
REMARK   3      L33:   2.8775 L12:  -0.6181                                     
REMARK   3      L13:  -0.1607 L23:   0.1293                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0495 S12:   0.3325 S13:   0.2893                       
REMARK   3      S21:  -0.0600 S22:  -0.0621 S23:  -0.0302                       
REMARK   3      S31:  -0.6580 S32:   0.1317 S33:   0.1121                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 4:257)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 108.0105  32.8187  40.0778              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2860 T22:   0.3490                                     
REMARK   3      T33:   0.3240 T12:  -0.1090                                     
REMARK   3      T13:  -0.0083 T23:   0.0358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3462 L22:   1.3520                                     
REMARK   3      L33:   2.2052 L12:  -0.3658                                     
REMARK   3      L13:  -0.1019 L23:  -0.2156                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0794 S12:  -0.1170 S13:  -0.0605                       
REMARK   3      S21:   0.1976 S22:  -0.0839 S23:  -0.0214                       
REMARK   3      S31:   0.0357 S32:   0.2195 S33:  -0.0018                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 258:542)                            
REMARK   3    ORIGIN FOR THE GROUP (A): 107.7185  45.9915  23.0955              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3325 T22:   0.4087                                     
REMARK   3      T33:   0.3360 T12:  -0.0815                                     
REMARK   3      T13:  -0.0111 T23:   0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8841 L22:   0.9465                                     
REMARK   3      L33:   2.1161 L12:   0.0177                                     
REMARK   3      L13:  -0.0053 L23:  -0.2645                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0361 S12:   0.1629 S13:   0.0524                       
REMARK   3      S21:  -0.0459 S22:  -0.1089 S23:  -0.0806                       
REMARK   3      S31:  -0.2420 S32:   0.2112 S33:   0.0666                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6CQW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000233252.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300-HS                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95513                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.278                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.10400                            
REMARK 200  R SYM                      (I) : 0.04600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: 4EY4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 TO 21% PEG 3350, 0.17 - 0.2M          
REMARK 280  POTASSIUM NITRATE, PH 7.0, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 295K, TEMPERATURE 295.0K                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      108.20367            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      216.40733            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      216.40733            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      108.20367            
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: 6150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 38.0 KCAL/MOL                         
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 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000       52.51500            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000      -90.95865            
REMARK 350   BIOMT3   2  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     GLY A     2                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     THR A   262                                                      
REMARK 465     ARG A   493                                                      
REMARK 465     ASP A   494                                                      
REMARK 465     PRO A   495                                                      
REMARK 465     LYS A   496                                                      
REMARK 465     THR A   543                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     THR B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     ARG B   493                                                      
REMARK 465     ASP B   494                                                      
REMARK 465     PRO B   495                                                      
REMARK 465     LYS B   496                                                      
REMARK 465     THR B   543                                                      
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    GLY B   135     O    HOH B   701              2.02            
REMARK 500   O    ASN A   482     O    ASP A   488              2.03            
REMARK 500   OE1  GLU A   285     O    HOH A   701              2.06            
REMARK 500   CD   PRO A   492     O    HOH A   703              2.07            
REMARK 500   O    HOH B   851     O    HOH B   988              2.08            
REMARK 500   O4   NAG A   604     O    HOH A   702              2.11            
REMARK 500   O    HOH A   891     O    HOH A   990              2.11            
REMARK 500   O    HOH B   722     O    HOH B   953              2.11            
REMARK 500   O    HOH B   949     O    HOH B   953              2.12            
REMARK 500   N    VAL B   139     O    HOH B   701              2.13            
REMARK 500   OE1  GLU B    81     O    HOH B   702              2.14            
REMARK 500   O    HOH B  1006     O    HOH B  1038              2.15            
REMARK 500   O    HOH B   775     O    HOH B   988              2.16            
REMARK 500   O    HOH B   762     O    HOH B  1027              2.16            
REMARK 500   N    PRO A   492     O    HOH A   703              2.19            
REMARK 500   CA   SER A   110     O    HOH A   705              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    GLU A 468   CA  -  C   -  O   ANGL. DEV. =  13.4 DEGREES          
REMARK 500    GLU A 468   CA  -  C   -  O   ANGL. DEV. =  16.7 DEGREES          
REMARK 500    GLU A 468   CA  -  C   -  N   ANGL. DEV. = -15.2 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    PHE A  47       -8.57     74.23                                   
REMARK 500    ASN A 170       19.62     58.94                                   
REMARK 500    SER A 203     -121.29     56.56                                   
REMARK 500    ASP A 306      -78.22    -94.20                                   
REMARK 500    VAL A 407      -63.87   -122.87                                   
REMARK 500    ASN A 464       52.03    -95.10                                   
REMARK 500    PHE B  47       -6.83     73.80                                   
REMARK 500    ALA B  62       50.40   -113.03                                   
REMARK 500    SER B 203     -122.53     57.41                                   
REMARK 500    ASP B 306      -80.89    -99.24                                   
REMARK 500    VAL B 407      -60.97   -127.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue VX A 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HI6 A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HI6 B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 604 bound   
REMARK 800  to ASN A 265                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC A    
REMARK 800  601 through NAG A 603 bound to ASN A 350                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 605 bound   
REMARK 800  to ASN A 464                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B    
REMARK 800  601 through NAG B 603 bound to ASN B 350                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound   
REMARK 800  to ASN B 464                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide VX B 605 and SER B     
REMARK 800  203                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6CQX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6CQY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6CQZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6CQT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6CQU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6CQV   RELATED DB: PDB                                   
DBREF  6CQW A    2   543  UNP    P22303   ACES_HUMAN      33    574             
DBREF  6CQW B    2   543  UNP    P22303   ACES_HUMAN      33    574             
SEQRES   1 A  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY          
SEQRES   2 A  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY          
SEQRES   3 A  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO          
SEQRES   4 A  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS          
SEQRES   5 A  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN          
SEQRES   6 A  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY          
SEQRES   7 A  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU          
SEQRES   8 A  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR          
SEQRES   9 A  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE          
SEQRES  10 A  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP          
SEQRES  11 A  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR          
SEQRES  12 A  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY          
SEQRES  13 A  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN          
SEQRES  14 A  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL          
SEQRES  15 A  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER          
SEQRES  16 A  542  VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL          
SEQRES  17 A  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE          
SEQRES  18 A  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO          
SEQRES  19 A  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA          
SEQRES  20 A  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY          
SEQRES  21 A  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG          
SEQRES  22 A  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS          
SEQRES  23 A  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL          
SEQRES  24 A  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU          
SEQRES  25 A  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL          
SEQRES  26 A  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU          
SEQRES  27 A  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER          
SEQRES  28 A  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL          
SEQRES  29 A  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL          
SEQRES  30 A  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO          
SEQRES  31 A  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP          
SEQRES  32 A  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG          
SEQRES  33 A  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE          
SEQRES  34 A  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET          
SEQRES  35 A  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY          
SEQRES  36 A  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU          
SEQRES  37 A  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN          
SEQRES  38 A  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO          
SEQRES  39 A  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN          
SEQRES  40 A  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG          
SEQRES  41 A  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG          
SEQRES  42 A  542  PHE LEU PRO LYS LEU LEU SER ALA THR                          
SEQRES   1 B  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY          
SEQRES   2 B  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY          
SEQRES   3 B  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO          
SEQRES   4 B  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS          
SEQRES   5 B  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN          
SEQRES   6 B  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY          
SEQRES   7 B  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU          
SEQRES   8 B  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR          
SEQRES   9 B  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE          
SEQRES  10 B  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP          
SEQRES  11 B  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR          
SEQRES  12 B  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY          
SEQRES  13 B  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN          
SEQRES  14 B  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL          
SEQRES  15 B  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER          
SEQRES  16 B  542  VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL          
SEQRES  17 B  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE          
SEQRES  18 B  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO          
SEQRES  19 B  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA          
SEQRES  20 B  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY          
SEQRES  21 B  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG          
SEQRES  22 B  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS          
SEQRES  23 B  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL          
SEQRES  24 B  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU          
SEQRES  25 B  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL          
SEQRES  26 B  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU          
SEQRES  27 B  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER          
SEQRES  28 B  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL          
SEQRES  29 B  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL          
SEQRES  30 B  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO          
SEQRES  31 B  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP          
SEQRES  32 B  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG          
SEQRES  33 B  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE          
SEQRES  34 B  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET          
SEQRES  35 B  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY          
SEQRES  36 B  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU          
SEQRES  37 B  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN          
SEQRES  38 B  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO          
SEQRES  39 B  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN          
SEQRES  40 B  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG          
SEQRES  41 B  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG          
SEQRES  42 B  542  PHE LEU PRO LYS LEU LEU SER ALA THR                          
HET    FUC  A 601      10                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    NAG  A 604      14                                                       
HET    NAG  A 605      14                                                       
HET     VX  A 606       6                                                       
HET    HI6  A 607      21                                                       
HET    FUC  B 601      10                                                       
HET    NAG  B 602      14                                                       
HET    NAG  B 603      14                                                       
HET    NAG  B 604      14                                                       
HET     VX  B 605       6                                                       
HET    HI6  B 606      21                                                       
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      VX O-ETHYLMETHYLPHOSPHONIC ACID ESTER GROUP                         
HETNAM     HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)                     
HETNAM   2 HI6  METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM                
HETSYN     HI6 1-(2-HYDROXY-IMINOMETHYLPYRIDINIUM)-1-(4-CARBOXYAMINO)-          
HETSYN   2 HI6  PYRIDINIUM DIMETHYLETHER                                        
FORMUL   3  FUC    2(C6 H12 O5)                                                 
FORMUL   3  NAG    7(C8 H15 N O6)                                               
FORMUL   6   VX    2(C3 H9 O3 P)                                                
FORMUL   7  HI6    2(C14 H16 N4 O3 2+)                                          
FORMUL  12  HOH   *665(H2 O)                                                    
HELIX    1 AA1 ASP A    5  GLU A    7  5                                   3    
HELIX    2 AA2 MET A   42  ARG A   46  5                                   5    
HELIX    3 AA3 PHE A   80  MET A   85  1                                   6    
HELIX    4 AA4 LEU A  130  ASP A  134  5                                   5    
HELIX    5 AA5 GLY A  135  ARG A  143  1                                   9    
HELIX    6 AA6 VAL A  153  LEU A  159  1                                   7    
HELIX    7 AA7 ASN A  170  VAL A  187  1                                  18    
HELIX    8 AA8 ALA A  188  PHE A  190  5                                   3    
HELIX    9 AA9 SER A  203  SER A  215  1                                  13    
HELIX   10 AB1 SER A  215  GLY A  220  1                                   6    
HELIX   11 AB2 MET A  241  VAL A  255  1                                  15    
HELIX   12 AB3 ASN A  265  THR A  275  1                                  11    
HELIX   13 AB4 PRO A  277  GLU A  285  1                                   9    
HELIX   14 AB5 TRP A  286  LEU A  289  5                                   4    
HELIX   15 AB6 THR A  311  GLY A  319  1                                   9    
HELIX   16 AB7 GLY A  335  VAL A  340  1                                   6    
HELIX   17 AB8 SER A  355  VAL A  367  1                                  13    
HELIX   18 AB9 SER A  371  THR A  383  1                                  13    
HELIX   19 AC1 ASP A  390  VAL A  407  1                                  18    
HELIX   20 AC2 VAL A  407  GLN A  421  1                                  15    
HELIX   21 AC3 PRO A  440  GLY A  444  5                                   5    
HELIX   22 AC4 GLU A  450  PHE A  455  1                                   6    
HELIX   23 AC5 GLY A  456  ASP A  460  5                                   5    
HELIX   24 AC6 THR A  466  ARG A  485  1                                  20    
HELIX   25 AC7 ARG A  525  ARG A  534  1                                  10    
HELIX   26 AC8 ARG A  534  ALA A  542  1                                   9    
HELIX   27 AC9 ASP B    5  GLU B    7  5                                   3    
HELIX   28 AD1 MET B   42  ARG B   46  5                                   5    
HELIX   29 AD2 PHE B   80  MET B   85  1                                   6    
HELIX   30 AD3 LEU B  130  ASP B  134  5                                   5    
HELIX   31 AD4 GLY B  135  ARG B  143  1                                   9    
HELIX   32 AD5 VAL B  153  LEU B  159  1                                   7    
HELIX   33 AD6 ASN B  170  VAL B  187  1                                  18    
HELIX   34 AD7 ALA B  188  PHE B  190  5                                   3    
HELIX   35 AD8 SER B  203  LEU B  214  1                                  12    
HELIX   36 AD9 SER B  215  GLY B  220  1                                   6    
HELIX   37 AE1 GLY B  240  VAL B  255  1                                  16    
HELIX   38 AE2 ASN B  265  THR B  275  1                                  11    
HELIX   39 AE3 PRO B  277  GLU B  285  1                                   9    
HELIX   40 AE4 TRP B  286  LEU B  289  5                                   4    
HELIX   41 AE5 THR B  311  GLY B  319  1                                   9    
HELIX   42 AE6 GLY B  335  VAL B  340  1                                   6    
HELIX   43 AE7 SER B  355  VAL B  367  1                                  13    
HELIX   44 AE8 SER B  371  TYR B  382  1                                  12    
HELIX   45 AE9 ASP B  390  VAL B  407  1                                  18    
HELIX   46 AF1 VAL B  407  GLN B  421  1                                  15    
HELIX   47 AF2 PRO B  440  GLY B  444  5                                   5    
HELIX   48 AF3 GLU B  450  PHE B  455  1                                   6    
HELIX   49 AF4 GLY B  456  ASP B  460  5                                   5    
HELIX   50 AF5 THR B  466  GLY B  487  1                                  22    
HELIX   51 AF6 ARG B  525  ARG B  534  1                                  10    
HELIX   52 AF7 PHE B  535  SER B  541  1                                   7    
SHEET    1 AA1 3 LEU A   9  VAL A  12  0                                        
SHEET    2 AA1 3 GLY A  15  ARG A  18 -1  O  LEU A  17   N  VAL A  10           
SHEET    3 AA1 3 VAL A  59  ASP A  61  1  O  VAL A  60   N  ARG A  16           
SHEET    1 AA211 ILE A  20  THR A  24  0                                        
SHEET    2 AA211 GLY A  27  PRO A  36 -1  O  VAL A  29   N  LEU A  22           
SHEET    3 AA211 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
SHEET    4 AA211 VAL A 145  MET A 149 -1  O  SER A 148   N  ASN A 100           
SHEET    5 AA211 THR A 112  ILE A 118  1  N  LEU A 115   O  VAL A 147           
SHEET    6 AA211 GLY A 192  GLU A 202  1  O  THR A 198   N  VAL A 114           
SHEET    7 AA211 ARG A 224  GLN A 228  1  O  GLN A 228   N  GLY A 201           
SHEET    8 AA211 GLN A 325  VAL A 331  1  O  LEU A 327   N  LEU A 227           
SHEET    9 AA211 ARG A 424  PHE A 430  1  O  PHE A 430   N  VAL A 330           
SHEET   10 AA211 GLN A 509  LEU A 513  1  O  LEU A 513   N  VAL A 429           
SHEET   11 AA211 GLU A 519  ARG A 522 -1  O  ARG A 521   N  TYR A 510           
SHEET    1 AA3 2 VAL A  68  CYS A  69  0                                        
SHEET    2 AA3 2 LEU A  92  SER A  93  1  O  SER A  93   N  VAL A  68           
SHEET    1 AA4 2 VAL A 239  GLY A 240  0                                        
SHEET    2 AA4 2 VAL A 302  VAL A 303  1  O  VAL A 303   N  VAL A 239           
SHEET    1 AA5 3 LEU B   9  VAL B  12  0                                        
SHEET    2 AA5 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3 AA5 3 VAL B  59  ASP B  61  1  O  VAL B  60   N  ARG B  16           
SHEET    1 AA611 ILE B  20  LEU B  22  0                                        
SHEET    2 AA611 VAL B  29  PRO B  36 -1  O  ALA B  31   N  ILE B  20           
SHEET    3 AA611 TYR B  98  PRO B 104 -1  O  THR B 103   N  SER B  30           
SHEET    4 AA611 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100           
SHEET    5 AA611 THR B 112  ILE B 118  1  N  LEU B 115   O  VAL B 147           
SHEET    6 AA611 GLY B 192  GLU B 202  1  O  ASP B 193   N  THR B 112           
SHEET    7 AA611 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8 AA611 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227           
SHEET    9 AA611 ARG B 424  PHE B 430  1  O  PHE B 430   N  VAL B 330           
SHEET   10 AA611 GLN B 509  LEU B 513  1  O  LEU B 513   N  VAL B 429           
SHEET   11 AA611 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1 AA7 2 VAL B  68  CYS B  69  0                                        
SHEET    2 AA7 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.03  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.04  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.03  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.04  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.04  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.03  
LINK         OG  SER A 203                 P1   VX A 606     1555   1555  1.40  
LINK         ND2 ASN A 265                 C1  NAG A 604     1555   1555  1.44  
LINK         ND2 ASN A 350                 C1  NAG A 602     1555   1555  1.37  
LINK         ND2 ASN A 464                 C1  NAG A 605     1555   1555  1.44  
LINK         OG  SER B 203                 P1   VX B 605     1555   1555  1.40  
LINK         ND2 ASN B 350                 C1  NAG B 602     1555   1555  1.57  
LINK         ND2 ASN B 464                 C1  NAG B 604     1555   1555  1.45  
LINK         C1  FUC A 601                 O6  NAG A 602     1555   1555  1.44  
LINK         O4  NAG A 602                 C1  NAG A 603     1555   1555  1.44  
LINK         C1  FUC B 601                 O6  NAG B 602     1555   1555  1.43  
LINK         O4  NAG B 602                 C1  NAG B 603     1555   1555  1.44  
CISPEP   1 TYR A  105    PRO A  106          0         3.65                     
CISPEP   2 CYS A  257    PRO A  258          0        -5.79                     
CISPEP   3 TYR B  105    PRO B  106          0        -1.53                     
CISPEP   4 PRO B  258    PRO B  259          0        12.00                     
CISPEP   5 ALA B  497    PRO B  498          0        -1.97                     
SITE     1 AC1  9 GLY A 121  GLY A 122  SER A 203  ALA A 204                    
SITE     2 AC1  9 PHE A 295  PHE A 297  PHE A 338  HIS A 447                    
SITE     3 AC1  9 HOH A 825                                                     
SITE     1 AC2 14 TYR A  72  ASP A  74  TYR A 124  VAL A 282                    
SITE     2 AC2 14 GLU A 285  TRP A 286  VAL A 294  PHE A 295                    
SITE     3 AC2 14 TYR A 337  TYR A 341  HOH A 717  HOH A 749                    
SITE     4 AC2 14 HOH A 781  HOH A 790                                          
SITE     1 AC3 12 TYR B  72  ASP B  74  TYR B 124  VAL B 282                    
SITE     2 AC3 12 GLU B 285  TRP B 286  VAL B 294  PHE B 295                    
SITE     3 AC3 12 TYR B 337  PHE B 338  TYR B 341  HOH B 850                    
SITE     1 AC4  5 ASN A 265  THR A 267  GLU A 268  HOH A 702                    
SITE     2 AC4  5 HOH A 885                                                     
SITE     1 AC5  7 ALA A 343  PRO A 344  GLY A 345  PHE A 346                    
SITE     2 AC5  7 SER A 347  ASN A 350  HOH A 836                               
SITE     1 AC6  2 SER A 462  ASN A 464                                          
SITE     1 AC7  3 PRO B 344  GLY B 345  ASN B 350                               
SITE     1 AC8  3 ASN B 464  HOH B 731  HOH B 849                               
SITE     1 AC9 13 GLY B 121  GLY B 122  GLU B 202  ALA B 204                    
SITE     2 AC9 13 GLY B 205  ALA B 206  ALA B 207  GLN B 228                    
SITE     3 AC9 13 SER B 229  PHE B 295  PHE B 297  PHE B 338                    
SITE     4 AC9 13 HIS B 447                                                     
CRYST1  105.030  105.030  324.611  90.00  90.00 120.00 P 31 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009521  0.005497  0.000000        0.00000                         
SCALE2      0.000000  0.010994  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003081        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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