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LongText Report for: 6arx-pdb

Name Class
6arx-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           23-AUG-17   6ARX              
TITLE     CRYSTAL STRUCTURE OF AN INSECTICIDE-RESISTANT ACETYLCHOLINESTERASE    
TITLE    2 MUTANT FROM THE MALARIA VECTOR ANOPHELES GAMBIAE IN THE LIGAND-FREE  
TITLE    3 STATE                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 162 TO 702;                                       
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ANOPHELES GAMBIAE;                              
SOURCE   3 ORGANISM_COMMON: AFRICAN MALARIA MOSQUITO;                           
SOURCE   4 ORGANISM_TAXID: 7165;                                                
SOURCE   5 GENE: ACE, ACE1, ACHE1, AGAP001356;                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACLOVIRUS;                           
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: MODIFIED PFASTBAC                         
KEYWDS    HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.CHEUNG,A.MAHMOOD,R.KALATHUR,L.LIXUAN,P.R.CARLIER                    
REVDAT   1   10-JAN-18 6ARX    0                                                
JRNL        AUTH   J.CHEUNG,A.MAHMOOD,R.KALATHUR,L.LIU,P.R.CARLIER              
JRNL        TITL   STRUCTURE OF THE G119S MUTANT ACETYLCHOLINESTERASE OF THE    
JRNL        TITL 2 MALARIA VECTOR ANOPHELES GAMBIAE REVEALS BASIS OF            
JRNL        TITL 3 INSECTICIDE RESISTANCE.                                      
JRNL        REF    STRUCTURE                     V.  26   130 2018              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   29276037                                                     
JRNL        DOI    10.1016/J.STR.2017.11.021                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.10                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 125762                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6259                            
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 49.1146 -  7.1461    0.99     4035   189  0.1498 0.1634        
REMARK   3     2  7.1461 -  5.6748    1.00     4043   190  0.1391 0.1615        
REMARK   3     3  5.6748 -  4.9582    1.00     3977   223  0.1279 0.1455        
REMARK   3     4  4.9582 -  4.5052    1.00     3997   225  0.1080 0.1243        
REMARK   3     5  4.5052 -  4.1825    1.00     3989   229  0.1120 0.1300        
REMARK   3     6  4.1825 -  3.9360    1.00     4004   212  0.1290 0.1542        
REMARK   3     7  3.9360 -  3.7390    1.00     4009   186  0.1408 0.1778        
REMARK   3     8  3.7390 -  3.5763    1.00     3991   221  0.1607 0.1691        
REMARK   3     9  3.5763 -  3.4386    1.00     3965   246  0.1720 0.2306        
REMARK   3    10  3.4386 -  3.3200    1.00     3994   192  0.1903 0.2302        
REMARK   3    11  3.3200 -  3.2162    1.00     3980   243  0.2100 0.2428        
REMARK   3    12  3.2162 -  3.1243    1.00     3940   213  0.2128 0.2411        
REMARK   3    13  3.1243 -  3.0421    1.00     3995   227  0.2081 0.2490        
REMARK   3    14  3.0421 -  2.9678    1.00     4027   220  0.2111 0.2408        
REMARK   3    15  2.9678 -  2.9004    1.00     3988   197  0.2255 0.2654        
REMARK   3    16  2.9004 -  2.8387    1.00     4015   173  0.2315 0.2709        
REMARK   3    17  2.8387 -  2.7819    1.00     3982   197  0.2341 0.2849        
REMARK   3    18  2.7819 -  2.7294    1.00     3945   229  0.2359 0.2602        
REMARK   3    19  2.7294 -  2.6807    1.00     3994   196  0.2472 0.2580        
REMARK   3    20  2.6807 -  2.6352    1.00     4027   182  0.2530 0.2838        
REMARK   3    21  2.6352 -  2.5927    1.00     4009   191  0.2611 0.2847        
REMARK   3    22  2.5927 -  2.5528    1.00     3999   216  0.2792 0.2993        
REMARK   3    23  2.5528 -  2.5153    1.00     3907   250  0.2724 0.3314        
REMARK   3    24  2.5153 -  2.4799    1.00     3995   223  0.2869 0.3207        
REMARK   3    25  2.4799 -  2.4463    1.00     3962   224  0.2894 0.3183        
REMARK   3    26  2.4463 -  2.4146    1.00     3975   183  0.2962 0.2779        
REMARK   3    27  2.4146 -  2.3844    1.00     4014   185  0.2944 0.3214        
REMARK   3    28  2.3844 -  2.3557    1.00     3971   200  0.3050 0.3198        
REMARK   3    29  2.3557 -  2.3283    1.00     3989   226  0.3186 0.3409        
REMARK   3    30  2.3283 -  2.3021    0.94     3785   171  0.3437 0.3738        
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)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.210           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.63                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.22                          
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      :  0.012           8935                                  
REMARK   3   ANGLE     :  1.165          12214                                  
REMARK   3   CHIRALITY :  0.063           1297                                  
REMARK   3   PLANARITY :  0.008           1616                                  
REMARK   3   DIHEDRAL  : 11.879           5268                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND (RESID 163 THROUGH 337 OR      
REMARK   3                          RESID 339 THROUGH 351 OR RESID 353          
REMARK   3                          THROUGH 569 OR RESID 571 THROUGH 659 OR     
REMARK   3                          RESID 661 THROUGH 699))                     
REMARK   3     SELECTION          : (CHAIN B AND (RESID 163 THROUGH 337 OR      
REMARK   3                          RESID 339 THROUGH 351 OR RESID 353          
REMARK   3                          THROUGH 569 OR RESID 571 THROUGH 659 OR     
REMARK   3                          RESID 661 THROUGH 699))                     
REMARK   3     ATOM PAIRS NUMBER  : 5176                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6ARX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229275.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 125913                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 200.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.200                              
REMARK 200  R MERGE                    (I) : 0.21000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 3.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.63400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER (1.11.1_2575: ???)                             
REMARK 200 STARTING MODEL: 4EY4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 79.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9 - 1.0M TRI-AMMONIUM CITRATE PH       
REMARK 280  6.5, 1 - 3% ISOPROPANOL, VAPOR DIFFUSION, SITTING DROP,             
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
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   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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       75.28567            
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      150.57133            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      112.92850            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      188.21417            
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       37.64283            
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: 3400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 41450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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      -74.79950            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      129.55653            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000       75.28567            
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   161                                                      
REMARK 465     ASP A   162                                                      
REMARK 465     LEU A   700                                                      
REMARK 465     PRO A   701                                                      
REMARK 465     GLY A   702                                                      
REMARK 465     GLY B   161                                                      
REMARK 465     ASP B   162                                                      
REMARK 465     LEU B   700                                                      
REMARK 465     PRO B   701                                                      
REMARK 465     GLY B   702                                                      
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   NH2  ARG A   517     OG1  FLC A  1004              2.15            
REMARK 500   NH2  ARG B   676     OB2  FLC B  1002              2.17            
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    ARG A 376   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    GLY A 617   C   -  N   -  CA  ANGL. DEV. = -13.3 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 206       -7.28     74.43                                   
REMARK 500    THR A 221       79.13   -115.13                                   
REMARK 500    ALA A 312     -159.87     61.28                                   
REMARK 500    PHE A 316       12.89   -144.03                                   
REMARK 500    SER A 360     -119.50     59.81                                   
REMARK 500    HIS A 416       41.87   -153.17                                   
REMARK 500    LYS A 420       70.59   -117.93                                   
REMARK 500    GLU A 485       73.44   -119.51                                   
REMARK 500    LEU A 495       72.93   -106.68                                   
REMARK 500    LEU A 499       72.75   -102.62                                   
REMARK 500    GLU A 540       73.95   -155.30                                   
REMARK 500    PHE A 560      -77.11   -129.39                                   
REMARK 500    ASN A 670       69.42   -108.74                                   
REMARK 500    PHE B 206       -6.84     74.86                                   
REMARK 500    THR B 221       77.90   -112.81                                   
REMARK 500    ASP B 238       30.99    -91.53                                   
REMARK 500    ALA B 312     -156.22     59.15                                   
REMARK 500    PHE B 316       13.71   -142.29                                   
REMARK 500    SER B 360     -119.41     61.23                                   
REMARK 500    HIS B 416       40.98   -151.27                                   
REMARK 500    LEU B 495       70.84   -106.13                                   
REMARK 500    LEU B 499       73.85   -105.71                                   
REMARK 500    GLU B 540       75.80   -155.21                                   
REMARK 500    PHE B 560      -75.34   -129.52                                   
REMARK 500    ASN B 670       72.65   -111.44                                   
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 FLC A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC B 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1001        
REMARK 800  bound to ASN A 220                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1002        
REMARK 800  bound to ASN A 670                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 1001        
REMARK 800  bound to ASN B 220                                                  
DBREF  6ARX A  162   702  UNP    Q869C3   ACES_ANOGA     162    702             
DBREF  6ARX B  162   702  UNP    Q869C3   ACES_ANOGA     162    702             
SEQADV 6ARX GLY A  161  UNP  Q869C3              EXPRESSION TAG                 
SEQADV 6ARX SER A  280  UNP  Q869C3    GLY   280 ENGINEERED MUTATION            
SEQADV 6ARX GLY B  161  UNP  Q869C3              EXPRESSION TAG                 
SEQADV 6ARX SER B  280  UNP  Q869C3    GLY   280 ENGINEERED MUTATION            
SEQRES   1 A  542  GLY ASP ASN ASP PRO LEU VAL VAL ASN THR ASP LYS GLY          
SEQRES   2 A  542  ARG ILE ARG GLY ILE THR VAL ASP ALA PRO SER GLY LYS          
SEQRES   3 A  542  LYS VAL ASP VAL TRP LEU GLY ILE PRO TYR ALA GLN PRO          
SEQRES   4 A  542  PRO VAL GLY PRO LEU ARG PHE ARG HIS PRO ARG PRO ALA          
SEQRES   5 A  542  GLU LYS TRP THR GLY VAL LEU ASN THR THR THR PRO PRO          
SEQRES   6 A  542  ASN SER CYS VAL GLN ILE VAL ASP THR VAL PHE GLY ASP          
SEQRES   7 A  542  PHE PRO GLY ALA THR MET TRP ASN PRO ASN THR PRO LEU          
SEQRES   8 A  542  SER GLU ASP CYS LEU TYR ILE ASN VAL VAL ALA PRO ARG          
SEQRES   9 A  542  PRO ARG PRO LYS ASN ALA ALA VAL MET LEU TRP ILE PHE          
SEQRES  10 A  542  GLY GLY SER PHE TYR SER GLY THR ALA THR LEU ASP VAL          
SEQRES  11 A  542  TYR ASP HIS ARG ALA LEU ALA SER GLU GLU ASN VAL ILE          
SEQRES  12 A  542  VAL VAL SER LEU GLN TYR ARG VAL ALA SER LEU GLY PHE          
SEQRES  13 A  542  LEU PHE LEU GLY THR PRO GLU ALA PRO GLY ASN ALA GLY          
SEQRES  14 A  542  LEU PHE ASP GLN ASN LEU ALA LEU ARG TRP VAL ARG ASP          
SEQRES  15 A  542  ASN ILE HIS ARG PHE GLY GLY ASP PRO SER ARG VAL THR          
SEQRES  16 A  542  LEU PHE GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU          
SEQRES  17 A  542  HIS LEU LEU SER ALA LEU SER ARG ASP LEU PHE GLN ARG          
SEQRES  18 A  542  ALA ILE LEU GLN SER GLY SER PRO THR ALA PRO TRP ALA          
SEQRES  19 A  542  LEU VAL SER ARG GLU GLU ALA THR LEU ARG ALA LEU ARG          
SEQRES  20 A  542  LEU ALA GLU ALA VAL GLY CYS PRO HIS GLU PRO SER LYS          
SEQRES  21 A  542  LEU SER ASP ALA VAL GLU CYS LEU ARG GLY LYS ASP PRO          
SEQRES  22 A  542  HIS VAL LEU VAL ASN ASN GLU TRP GLY THR LEU GLY ILE          
SEQRES  23 A  542  CYS GLU PHE PRO PHE VAL PRO VAL VAL ASP GLY ALA PHE          
SEQRES  24 A  542  LEU ASP GLU THR PRO GLN ARG SER LEU ALA SER GLY ARG          
SEQRES  25 A  542  PHE LYS LYS THR GLU ILE LEU THR GLY SER ASN THR GLU          
SEQRES  26 A  542  GLU GLY TYR TYR PHE ILE ILE TYR TYR LEU THR GLU LEU          
SEQRES  27 A  542  LEU ARG LYS GLU GLU GLY VAL THR VAL THR ARG GLU GLU          
SEQRES  28 A  542  PHE LEU GLN ALA VAL ARG GLU LEU ASN PRO TYR VAL ASN          
SEQRES  29 A  542  GLY ALA ALA ARG GLN ALA ILE VAL PHE GLU TYR THR ASP          
SEQRES  30 A  542  TRP THR GLU PRO ASP ASN PRO ASN SER ASN ARG ASP ALA          
SEQRES  31 A  542  LEU ASP LYS MET VAL GLY ASP TYR HIS PHE THR CYS ASN          
SEQRES  32 A  542  VAL ASN GLU PHE ALA GLN ARG TYR ALA GLU GLU GLY ASN          
SEQRES  33 A  542  ASN VAL TYR MET TYR LEU TYR THR HIS ARG SER LYS GLY          
SEQRES  34 A  542  ASN PRO TRP PRO ARG TRP THR GLY VAL MET HIS GLY ASP          
SEQRES  35 A  542  GLU ILE ASN TYR VAL PHE GLY GLU PRO LEU ASN PRO THR          
SEQRES  36 A  542  LEU GLY TYR THR GLU ASP GLU LYS ASP PHE SER ARG LYS          
SEQRES  37 A  542  ILE MET ARG TYR TRP SER ASN PHE ALA LYS THR GLY ASN          
SEQRES  38 A  542  PRO ASN PRO ASN THR ALA SER SER GLU PHE PRO GLU TRP          
SEQRES  39 A  542  PRO LYS HIS THR ALA HIS GLY ARG HIS TYR LEU GLU LEU          
SEQRES  40 A  542  GLY LEU ASN THR SER PHE VAL GLY ARG GLY PRO ARG LEU          
SEQRES  41 A  542  ARG GLN CYS ALA PHE TRP LYS LYS TYR LEU PRO GLN LEU          
SEQRES  42 A  542  VAL ALA ALA THR SER ASN LEU PRO GLY                          
SEQRES   1 B  542  GLY ASP ASN ASP PRO LEU VAL VAL ASN THR ASP LYS GLY          
SEQRES   2 B  542  ARG ILE ARG GLY ILE THR VAL ASP ALA PRO SER GLY LYS          
SEQRES   3 B  542  LYS VAL ASP VAL TRP LEU GLY ILE PRO TYR ALA GLN PRO          
SEQRES   4 B  542  PRO VAL GLY PRO LEU ARG PHE ARG HIS PRO ARG PRO ALA          
SEQRES   5 B  542  GLU LYS TRP THR GLY VAL LEU ASN THR THR THR PRO PRO          
SEQRES   6 B  542  ASN SER CYS VAL GLN ILE VAL ASP THR VAL PHE GLY ASP          
SEQRES   7 B  542  PHE PRO GLY ALA THR MET TRP ASN PRO ASN THR PRO LEU          
SEQRES   8 B  542  SER GLU ASP CYS LEU TYR ILE ASN VAL VAL ALA PRO ARG          
SEQRES   9 B  542  PRO ARG PRO LYS ASN ALA ALA VAL MET LEU TRP ILE PHE          
SEQRES  10 B  542  GLY GLY SER PHE TYR SER GLY THR ALA THR LEU ASP VAL          
SEQRES  11 B  542  TYR ASP HIS ARG ALA LEU ALA SER GLU GLU ASN VAL ILE          
SEQRES  12 B  542  VAL VAL SER LEU GLN TYR ARG VAL ALA SER LEU GLY PHE          
SEQRES  13 B  542  LEU PHE LEU GLY THR PRO GLU ALA PRO GLY ASN ALA GLY          
SEQRES  14 B  542  LEU PHE ASP GLN ASN LEU ALA LEU ARG TRP VAL ARG ASP          
SEQRES  15 B  542  ASN ILE HIS ARG PHE GLY GLY ASP PRO SER ARG VAL THR          
SEQRES  16 B  542  LEU PHE GLY GLU SER ALA GLY ALA VAL SER VAL SER LEU          
SEQRES  17 B  542  HIS LEU LEU SER ALA LEU SER ARG ASP LEU PHE GLN ARG          
SEQRES  18 B  542  ALA ILE LEU GLN SER GLY SER PRO THR ALA PRO TRP ALA          
SEQRES  19 B  542  LEU VAL SER ARG GLU GLU ALA THR LEU ARG ALA LEU ARG          
SEQRES  20 B  542  LEU ALA GLU ALA VAL GLY CYS PRO HIS GLU PRO SER LYS          
SEQRES  21 B  542  LEU SER ASP ALA VAL GLU CYS LEU ARG GLY LYS ASP PRO          
SEQRES  22 B  542  HIS VAL LEU VAL ASN ASN GLU TRP GLY THR LEU GLY ILE          
SEQRES  23 B  542  CYS GLU PHE PRO PHE VAL PRO VAL VAL ASP GLY ALA PHE          
SEQRES  24 B  542  LEU ASP GLU THR PRO GLN ARG SER LEU ALA SER GLY ARG          
SEQRES  25 B  542  PHE LYS LYS THR GLU ILE LEU THR GLY SER ASN THR GLU          
SEQRES  26 B  542  GLU GLY TYR TYR PHE ILE ILE TYR TYR LEU THR GLU LEU          
SEQRES  27 B  542  LEU ARG LYS GLU GLU GLY VAL THR VAL THR ARG GLU GLU          
SEQRES  28 B  542  PHE LEU GLN ALA VAL ARG GLU LEU ASN PRO TYR VAL ASN          
SEQRES  29 B  542  GLY ALA ALA ARG GLN ALA ILE VAL PHE GLU TYR THR ASP          
SEQRES  30 B  542  TRP THR GLU PRO ASP ASN PRO ASN SER ASN ARG ASP ALA          
SEQRES  31 B  542  LEU ASP LYS MET VAL GLY ASP TYR HIS PHE THR CYS ASN          
SEQRES  32 B  542  VAL ASN GLU PHE ALA GLN ARG TYR ALA GLU GLU GLY ASN          
SEQRES  33 B  542  ASN VAL TYR MET TYR LEU TYR THR HIS ARG SER LYS GLY          
SEQRES  34 B  542  ASN PRO TRP PRO ARG TRP THR GLY VAL MET HIS GLY ASP          
SEQRES  35 B  542  GLU ILE ASN TYR VAL PHE GLY GLU PRO LEU ASN PRO THR          
SEQRES  36 B  542  LEU GLY TYR THR GLU ASP GLU LYS ASP PHE SER ARG LYS          
SEQRES  37 B  542  ILE MET ARG TYR TRP SER ASN PHE ALA LYS THR GLY ASN          
SEQRES  38 B  542  PRO ASN PRO ASN THR ALA SER SER GLU PHE PRO GLU TRP          
SEQRES  39 B  542  PRO LYS HIS THR ALA HIS GLY ARG HIS TYR LEU GLU LEU          
SEQRES  40 B  542  GLY LEU ASN THR SER PHE VAL GLY ARG GLY PRO ARG LEU          
SEQRES  41 B  542  ARG GLN CYS ALA PHE TRP LYS LYS TYR LEU PRO GLN LEU          
SEQRES  42 B  542  VAL ALA ALA THR SER ASN LEU PRO GLY                          
HET    NAG  A1001      14                                                       
HET    NAG  A1002      14                                                       
HET    FLC  A1003      13                                                       
HET    FLC  A1004      13                                                       
HET     CL  A1005       1                                                       
HET    NAG  B1001      14                                                       
HET    FLC  B1002      13                                                       
HET    FLC  B1003      13                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FLC CITRATE ANION                                                    
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3  NAG    3(C8 H15 N O6)                                               
FORMUL   5  FLC    4(C6 H5 O7 3-)                                               
FORMUL   7   CL    CL 1-                                                        
FORMUL  11  HOH   *360(H2 O)                                                    
HELIX    1 AA1 VAL A  201  ARG A  205  5                                   5    
HELIX    2 AA2 PHE A  239  MET A  244  1                                   6    
HELIX    3 AA3 LEU A  288  ASP A  292  5                                   5    
HELIX    4 AA4 HIS A  293  ASN A  301  1                                   9    
HELIX    5 AA5 VAL A  311  LEU A  317  1                                   7    
HELIX    6 AA6 ASN A  327  ILE A  344  1                                  18    
HELIX    7 AA7 HIS A  345  PHE A  347  5                                   3    
HELIX    8 AA8 SER A  360  SER A  372  1                                  13    
HELIX    9 AA9 SER A  397  VAL A  412  1                                  16    
HELIX   10 AB1 LYS A  420  LYS A  431  1                                  12    
HELIX   11 AB2 ASP A  432  ASN A  438  1                                   7    
HELIX   12 AB3 THR A  463  GLY A  471  1                                   9    
HELIX   13 AB4 GLY A  487  LEU A  495  1                                   9    
HELIX   14 AB5 THR A  508  ASN A  520  1                                  13    
HELIX   15 AB6 ASN A  524  TYR A  535  1                                  12    
HELIX   16 AB7 ASN A  543  PHE A  560  1                                  18    
HELIX   17 AB8 PHE A  560  GLU A  574  1                                  15    
HELIX   18 AB9 PRO A  593  GLY A  597  5                                   5    
HELIX   19 AC1 GLU A  603  PHE A  608  1                                   6    
HELIX   20 AC2 GLY A  609  ASN A  613  5                                   5    
HELIX   21 AC3 THR A  619  GLY A  640  1                                  22    
HELIX   22 AC4 ARG A  679  LYS A  688  1                                  10    
HELIX   23 AC5 LYS A  688  THR A  697  1                                  10    
HELIX   24 AC6 VAL B  201  ARG B  205  5                                   5    
HELIX   25 AC7 PHE B  239  MET B  244  1                                   6    
HELIX   26 AC8 LEU B  288  ASP B  292  5                                   5    
HELIX   27 AC9 HIS B  293  ASN B  301  1                                   9    
HELIX   28 AD1 VAL B  311  LEU B  317  1                                   7    
HELIX   29 AD2 ASN B  327  ILE B  344  1                                  18    
HELIX   30 AD3 HIS B  345  PHE B  347  5                                   3    
HELIX   31 AD4 SER B  360  LEU B  370  1                                  11    
HELIX   32 AD5 SER B  397  VAL B  412  1                                  16    
HELIX   33 AD6 LYS B  420  LYS B  431  1                                  12    
HELIX   34 AD7 ASP B  432  ASN B  438  1                                   7    
HELIX   35 AD8 THR B  463  GLY B  471  1                                   9    
HELIX   36 AD9 GLY B  487  LEU B  495  1                                   9    
HELIX   37 AE1 THR B  508  ASN B  520  1                                  13    
HELIX   38 AE2 ASN B  524  TYR B  535  1                                  12    
HELIX   39 AE3 ASN B  543  PHE B  560  1                                  18    
HELIX   40 AE4 PHE B  560  GLU B  574  1                                  15    
HELIX   41 AE5 PRO B  593  GLY B  597  5                                   5    
HELIX   42 AE6 ASP B  602  PHE B  608  1                                   7    
HELIX   43 AE7 GLY B  609  ASN B  613  5                                   5    
HELIX   44 AE8 THR B  619  GLY B  640  1                                  22    
HELIX   45 AE9 ARG B  679  LYS B  688  1                                  10    
HELIX   46 AF1 LYS B  688  THR B  697  1                                  10    
SHEET    1 AA1 3 VAL A 167  THR A 170  0                                        
SHEET    2 AA1 3 GLY A 173  ARG A 176 -1  O  GLY A 173   N  THR A 170           
SHEET    3 AA1 3 VAL A 218  ASN A 220  1  O  LEU A 219   N  ARG A 176           
SHEET    1 AA211 ILE A 178  ASP A 181  0                                        
SHEET    2 AA211 LYS A 187  PRO A 195 -1  O  VAL A 188   N  VAL A 180           
SHEET    3 AA211 TYR A 257  PRO A 263 -1  O  VAL A 260   N  TRP A 191           
SHEET    4 AA211 ILE A 303  LEU A 307 -1  O  SER A 306   N  ASN A 259           
SHEET    5 AA211 ALA A 270  ILE A 276  1  N  TRP A 275   O  VAL A 305           
SHEET    6 AA211 GLY A 349  GLU A 359  1  O  ASP A 350   N  ALA A 270           
SHEET    7 AA211 ARG A 381  GLN A 385  1  O  GLN A 385   N  GLY A 358           
SHEET    8 AA211 ILE A 478  ASN A 483  1  O  LEU A 479   N  LEU A 384           
SHEET    9 AA211 VAL A 578  TYR A 583  1  O  TYR A 583   N  SER A 482           
SHEET   10 AA211 HIS A 663  LEU A 667  1  O  LEU A 667   N  LEU A 582           
SHEET   11 AA211 VAL A 674  ARG A 676 -1  O  GLY A 675   N  TYR A 664           
SHEET    1 AA3 3 VAL B 167  THR B 170  0                                        
SHEET    2 AA3 3 GLY B 173  ARG B 176 -1  O  ILE B 175   N  VAL B 168           
SHEET    3 AA3 3 VAL B 218  ASN B 220  1  O  LEU B 219   N  ARG B 176           
SHEET    1 AA411 ILE B 178  ASP B 181  0                                        
SHEET    2 AA411 LYS B 187  PRO B 195 -1  O  VAL B 188   N  VAL B 180           
SHEET    3 AA411 TYR B 257  PRO B 263 -1  O  VAL B 260   N  TRP B 191           
SHEET    4 AA411 ILE B 303  LEU B 307 -1  O  SER B 306   N  ASN B 259           
SHEET    5 AA411 ALA B 270  ILE B 276  1  N  TRP B 275   O  VAL B 305           
SHEET    6 AA411 GLY B 349  GLU B 359  1  O  ASP B 350   N  ALA B 270           
SHEET    7 AA411 ARG B 381  GLN B 385  1  O  GLN B 385   N  GLY B 358           
SHEET    8 AA411 ILE B 478  ASN B 483  1  O  LEU B 479   N  LEU B 384           
SHEET    9 AA411 VAL B 578  TYR B 583  1  O  TYR B 583   N  SER B 482           
SHEET   10 AA411 HIS B 663  LEU B 667  1  O  LEU B 667   N  LEU B 582           
SHEET   11 AA411 VAL B 674  ARG B 676 -1  O  GLY B 675   N  TYR B 664           
SSBOND   1 CYS A  228    CYS A  255                          1555   1555  2.06  
SSBOND   2 CYS A  414    CYS A  427                          1555   1555  2.10  
SSBOND   3 CYS A  562    CYS A  683                          1555   1555  2.05  
SSBOND   4 CYS B  228    CYS B  255                          1555   1555  2.05  
SSBOND   5 CYS B  414    CYS B  427                          1555   1555  2.12  
SSBOND   6 CYS B  562    CYS B  683                          1555   1555  2.06  
LINK         ND2 ASN A 220                 C1  NAG A1001     1555   1555  1.47  
LINK         ND2 ASN A 670                 C1  NAG A1002     1555   1555  1.45  
LINK         ND2 ASN B 220                 C1  NAG B1001     1555   1555  1.46  
CISPEP   1 ARG A  264    PRO A  265          0         0.98                     
CISPEP   2 GLY A  677    PRO A  678          0        10.43                     
CISPEP   3 ARG B  264    PRO B  265          0         1.06                     
CISPEP   4 GLY B  677    PRO B  678          0         9.78                     
SITE     1 AC1  4 THR A 658  HIS A 660  HIS A 663  ARG A 676                    
SITE     1 AC2  4 ARG A 517  ASN A 524  GLY A 525  ARG A 528                    
SITE     1 AC3  3 ARG A 376  ARG A 472  GLN B 198                               
SITE     1 AC4  4 THR B 658  HIS B 660  HIS B 663  ARG B 676                    
SITE     1 AC5  4 ARG B 517  ASN B 524  GLY B 525  ARG B 528                    
SITE     1 AC6  2 ARG A 176  ASN A 220                                          
SITE     1 AC7  1 ASN A 670                                                     
SITE     1 AC8  2 VAL B 218  ASN B 220                                          
CRYST1  149.599  149.599  225.857  90.00  90.00 120.00 P 61         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      0.006685  0.003859  0.000000        0.00000                         
SCALE2      0.000000  0.007719  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004428        0.00000                         
TER    4290      ASN A 699                                                      
TER    8580      ASN B 699                                                      
MASTER      372    0    8   46   28    0    8    6 8957    2  109   84          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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