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LongText Report for: 7pcw-pdb

Name Class
7pcw-pdb
HEADER    HYDROLASE                               04-AUG-21   7PCW              
TITLE     X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HALOTAG7-M175W LABELED 
TITLE    2 WITH A CHLOROALKANE-TETRAMETHYLRHODAMINE FLUOROPHORE SUBSTRATE       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HALOALKANE DEHALOGENASE;                                   
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 3.8.1.5;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;                                
SOURCE   3 ORGANISM_TAXID: 1831;                                                
SOURCE   4 GENE: DHAA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    HALOALKANE DEHALOGENASE, HALO, TAG, HALOTAG7, SELF-LABELING PROTEIN,  
KEYWDS   2 FLUOROPHORE, TETRAMETHYLRHODAMINE, HYDROLASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.TARNAWSKI,M.FREI,J.HIBLOT,K.JOHNSSON                                
REVDAT   1   15-DEC-21 7PCW    0                                                
JRNL        AUTH   M.TARNAWSKI,M.FREI,J.HIBLOT,K.JOHNSSON                       
JRNL        TITL   X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE               
JRNL        TITL 2 HALOTAG7-M175W LABELED WITH A                                
JRNL        TITL 3 CHLOROALKANE-TETRAMETHYLRHODAMINE FLUOROPHORE SUBSTRATE      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.19.2_4158                                   
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.36                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.980                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 43471                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2174                            
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 40.3600 -  5.7900    0.95     2559   135  0.1533 0.1718        
REMARK   3     2  5.7900 -  4.6000    0.94     2550   135  0.1694 0.1837        
REMARK   3     3  4.6000 -  4.0200    0.95     2544   134  0.1535 0.1861        
REMARK   3     4  4.0200 -  3.6500    0.96     2593   136  0.1690 0.2098        
REMARK   3     5  3.6500 -  3.3900    0.97     2608   137  0.1764 0.2437        
REMARK   3     6  3.3900 -  3.1900    0.95     2531   134  0.2013 0.2662        
REMARK   3     7  3.1900 -  3.0300    0.95     2612   137  0.2147 0.2751        
REMARK   3     8  3.0300 -  2.9000    0.96     2569   135  0.2067 0.2853        
REMARK   3     9  2.9000 -  2.7900    0.96     2552   134  0.2213 0.3070        
REMARK   3    10  2.7900 -  2.6900    0.96     2610   138  0.2256 0.2987        
REMARK   3    11  2.6900 -  2.6100    0.97     2577   136  0.2337 0.3398        
REMARK   3    12  2.6100 -  2.5300    0.95     2612   137  0.2292 0.3266        
REMARK   3    13  2.5300 -  2.4600    0.97     2580   136  0.2341 0.2730        
REMARK   3    14  2.4600 -  2.4000    0.95     2624   138  0.2313 0.3034        
REMARK   3    15  2.4000 -  2.3500    0.97     2562   135  0.2247 0.2800        
REMARK   3    16  2.3500 -  2.3000    0.96     2614   137  0.2218 0.2751        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.277            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.379           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.14                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.57                          
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      :  0.002           9918                                  
REMARK   3   ANGLE     :  0.576          13570                                  
REMARK   3   CHIRALITY :  0.045           1408                                  
REMARK   3   PLANARITY :  0.005           1904                                  
REMARK   3   DIHEDRAL  : 13.496           3700                                  
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 : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7PCW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-AUG-21.                  
REMARK 100 THE DEPOSITION ID IS D_1292117490.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-21                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER2 X 16M               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43477                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 2.670                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.4400                             
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) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.58                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.800                              
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: 6Y7A                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.0, 1.0 M LITHIUM          
REMARK 280  CHLORIDE, 22% (M/V) PEG 6000, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ILE A   295                                                      
REMARK 465     ILE D   295                                                      
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    PRO A  42       41.68   -105.34                                   
REMARK 500    THR A  43     -158.86    -97.28                                   
REMARK 500    ASP A 106     -122.74     53.43                                   
REMARK 500    ARG A 153       37.19    -81.47                                   
REMARK 500    ASP A 156      -67.18    -92.32                                   
REMARK 500    PRO A 210       90.61    -68.71                                   
REMARK 500    VAL A 245      -67.81   -124.90                                   
REMARK 500    LEU A 271      -96.34   -119.22                                   
REMARK 500    ASN A 278       67.61   -157.98                                   
REMARK 500    PRO B  42       42.71   -105.05                                   
REMARK 500    ASP B 106     -120.20     52.47                                   
REMARK 500    GLU B 130       59.20     39.33                                   
REMARK 500    ARG B 153       44.42    -84.60                                   
REMARK 500    ASP B 156      -63.34    -93.19                                   
REMARK 500    VAL B 245      -61.72   -128.57                                   
REMARK 500    LEU B 271      -95.82   -117.62                                   
REMARK 500    ASN B 278       66.42   -160.21                                   
REMARK 500    GLU B 294       79.69   -101.05                                   
REMARK 500    PRO C  42       44.92   -103.54                                   
REMARK 500    GLU C  98      -83.86    -95.54                                   
REMARK 500    ASP C 106     -124.17     52.94                                   
REMARK 500    ARG C 153       46.89    -88.53                                   
REMARK 500    ASP C 156      -69.45    -99.71                                   
REMARK 500    VAL C 245      -65.33   -130.72                                   
REMARK 500    LEU C 271      -90.61   -123.33                                   
REMARK 500    ASN C 278       66.78   -153.20                                   
REMARK 500    PRO D  42       51.30   -104.03                                   
REMARK 500    THR D  43     -165.36   -107.35                                   
REMARK 500    SER D  44     -159.38   -150.54                                   
REMARK 500    GLU D  98      -85.67   -100.30                                   
REMARK 500    ASP D 106     -122.88     56.71                                   
REMARK 500    ARG D 153       48.90    -88.49                                   
REMARK 500    ASP D 156      -67.04    -97.01                                   
REMARK 500    VAL D 245      -65.25   -129.67                                   
REMARK 500    LEU D 271      -99.24   -114.43                                   
REMARK 500    ASN D 278       69.26   -158.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6ZVU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6ZVV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6ZVW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6ZVX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6ZVY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 7PCX   RELATED DB: PDB                                   
DBREF  7PCW A    4   293  UNP    P0A3G3   DHAA_RHOSO       4    293             
DBREF  7PCW B    4   293  UNP    P0A3G3   DHAA_RHOSO       4    293             
DBREF  7PCW C    4   293  UNP    P0A3G3   DHAA_RHOSO       4    293             
DBREF  7PCW D    4   293  UNP    P0A3G3   DHAA_RHOSO       4    293             
SEQADV 7PCW GLY A    3  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 7PCW VAL A   47  UNP  P0A3G3    LEU    47 ENGINEERED MUTATION            
SEQADV 7PCW THR A   58  UNP  P0A3G3    SER    58 ENGINEERED MUTATION            
SEQADV 7PCW GLY A   78  UNP  P0A3G3    ASP    78 ENGINEERED MUTATION            
SEQADV 7PCW PHE A   87  UNP  P0A3G3    TYR    87 ENGINEERED MUTATION            
SEQADV 7PCW MET A   88  UNP  P0A3G3    LEU    88 ENGINEERED MUTATION            
SEQADV 7PCW PHE A  128  UNP  P0A3G3    CYS   128 ENGINEERED MUTATION            
SEQADV 7PCW THR A  155  UNP  P0A3G3    ALA   155 ENGINEERED MUTATION            
SEQADV 7PCW LYS A  160  UNP  P0A3G3    GLU   160 ENGINEERED MUTATION            
SEQADV 7PCW VAL A  167  UNP  P0A3G3    ALA   167 ENGINEERED MUTATION            
SEQADV 7PCW THR A  172  UNP  P0A3G3    ALA   172 ENGINEERED MUTATION            
SEQADV 7PCW TRP A  175  UNP  P0A3G3    LYS   175 ENGINEERED MUTATION            
SEQADV 7PCW GLY A  176  UNP  P0A3G3    CYS   176 ENGINEERED MUTATION            
SEQADV 7PCW ASN A  195  UNP  P0A3G3    LYS   195 ENGINEERED MUTATION            
SEQADV 7PCW GLU A  224  UNP  P0A3G3    ALA   224 ENGINEERED MUTATION            
SEQADV 7PCW ASP A  227  UNP  P0A3G3    ASN   227 ENGINEERED MUTATION            
SEQADV 7PCW LYS A  257  UNP  P0A3G3    GLU   257 ENGINEERED MUTATION            
SEQADV 7PCW ALA A  264  UNP  P0A3G3    THR   264 ENGINEERED MUTATION            
SEQADV 7PCW ASN A  272  UNP  P0A3G3    HIS   272 ENGINEERED MUTATION            
SEQADV 7PCW LEU A  273  UNP  P0A3G3    TYR   273 ENGINEERED MUTATION            
SEQADV 7PCW SER A  291  UNP  P0A3G3    PRO   291 ENGINEERED MUTATION            
SEQADV 7PCW THR A  292  UNP  P0A3G3    ALA   292 ENGINEERED MUTATION            
SEQADV 7PCW GLU A  294  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 7PCW ILE A  295  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 7PCW GLY B    3  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 7PCW VAL B   47  UNP  P0A3G3    LEU    47 ENGINEERED MUTATION            
SEQADV 7PCW THR B   58  UNP  P0A3G3    SER    58 ENGINEERED MUTATION            
SEQADV 7PCW GLY B   78  UNP  P0A3G3    ASP    78 ENGINEERED MUTATION            
SEQADV 7PCW PHE B   87  UNP  P0A3G3    TYR    87 ENGINEERED MUTATION            
SEQADV 7PCW MET B   88  UNP  P0A3G3    LEU    88 ENGINEERED MUTATION            
SEQADV 7PCW PHE B  128  UNP  P0A3G3    CYS   128 ENGINEERED MUTATION            
SEQADV 7PCW THR B  155  UNP  P0A3G3    ALA   155 ENGINEERED MUTATION            
SEQADV 7PCW LYS B  160  UNP  P0A3G3    GLU   160 ENGINEERED MUTATION            
SEQADV 7PCW VAL B  167  UNP  P0A3G3    ALA   167 ENGINEERED MUTATION            
SEQADV 7PCW THR B  172  UNP  P0A3G3    ALA   172 ENGINEERED MUTATION            
SEQADV 7PCW TRP B  175  UNP  P0A3G3    LYS   175 ENGINEERED MUTATION            
SEQADV 7PCW GLY B  176  UNP  P0A3G3    CYS   176 ENGINEERED MUTATION            
SEQADV 7PCW ASN B  195  UNP  P0A3G3    LYS   195 ENGINEERED MUTATION            
SEQADV 7PCW GLU B  224  UNP  P0A3G3    ALA   224 ENGINEERED MUTATION            
SEQADV 7PCW ASP B  227  UNP  P0A3G3    ASN   227 ENGINEERED MUTATION            
SEQADV 7PCW LYS B  257  UNP  P0A3G3    GLU   257 ENGINEERED MUTATION            
SEQADV 7PCW ALA B  264  UNP  P0A3G3    THR   264 ENGINEERED MUTATION            
SEQADV 7PCW ASN B  272  UNP  P0A3G3    HIS   272 ENGINEERED MUTATION            
SEQADV 7PCW LEU B  273  UNP  P0A3G3    TYR   273 ENGINEERED MUTATION            
SEQADV 7PCW SER B  291  UNP  P0A3G3    PRO   291 ENGINEERED MUTATION            
SEQADV 7PCW THR B  292  UNP  P0A3G3    ALA   292 ENGINEERED MUTATION            
SEQADV 7PCW GLU B  294  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 7PCW ILE B  295  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 7PCW GLY C    3  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 7PCW VAL C   47  UNP  P0A3G3    LEU    47 ENGINEERED MUTATION            
SEQADV 7PCW THR C   58  UNP  P0A3G3    SER    58 ENGINEERED MUTATION            
SEQADV 7PCW GLY C   78  UNP  P0A3G3    ASP    78 ENGINEERED MUTATION            
SEQADV 7PCW PHE C   87  UNP  P0A3G3    TYR    87 ENGINEERED MUTATION            
SEQADV 7PCW MET C   88  UNP  P0A3G3    LEU    88 ENGINEERED MUTATION            
SEQADV 7PCW PHE C  128  UNP  P0A3G3    CYS   128 ENGINEERED MUTATION            
SEQADV 7PCW THR C  155  UNP  P0A3G3    ALA   155 ENGINEERED MUTATION            
SEQADV 7PCW LYS C  160  UNP  P0A3G3    GLU   160 ENGINEERED MUTATION            
SEQADV 7PCW VAL C  167  UNP  P0A3G3    ALA   167 ENGINEERED MUTATION            
SEQADV 7PCW THR C  172  UNP  P0A3G3    ALA   172 ENGINEERED MUTATION            
SEQADV 7PCW TRP C  175  UNP  P0A3G3    LYS   175 ENGINEERED MUTATION            
SEQADV 7PCW GLY C  176  UNP  P0A3G3    CYS   176 ENGINEERED MUTATION            
SEQADV 7PCW ASN C  195  UNP  P0A3G3    LYS   195 ENGINEERED MUTATION            
SEQADV 7PCW GLU C  224  UNP  P0A3G3    ALA   224 ENGINEERED MUTATION            
SEQADV 7PCW ASP C  227  UNP  P0A3G3    ASN   227 ENGINEERED MUTATION            
SEQADV 7PCW LYS C  257  UNP  P0A3G3    GLU   257 ENGINEERED MUTATION            
SEQADV 7PCW ALA C  264  UNP  P0A3G3    THR   264 ENGINEERED MUTATION            
SEQADV 7PCW ASN C  272  UNP  P0A3G3    HIS   272 ENGINEERED MUTATION            
SEQADV 7PCW LEU C  273  UNP  P0A3G3    TYR   273 ENGINEERED MUTATION            
SEQADV 7PCW SER C  291  UNP  P0A3G3    PRO   291 ENGINEERED MUTATION            
SEQADV 7PCW THR C  292  UNP  P0A3G3    ALA   292 ENGINEERED MUTATION            
SEQADV 7PCW GLU C  294  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 7PCW ILE C  295  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 7PCW GLY D    3  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 7PCW VAL D   47  UNP  P0A3G3    LEU    47 ENGINEERED MUTATION            
SEQADV 7PCW THR D   58  UNP  P0A3G3    SER    58 ENGINEERED MUTATION            
SEQADV 7PCW GLY D   78  UNP  P0A3G3    ASP    78 ENGINEERED MUTATION            
SEQADV 7PCW PHE D   87  UNP  P0A3G3    TYR    87 ENGINEERED MUTATION            
SEQADV 7PCW MET D   88  UNP  P0A3G3    LEU    88 ENGINEERED MUTATION            
SEQADV 7PCW PHE D  128  UNP  P0A3G3    CYS   128 ENGINEERED MUTATION            
SEQADV 7PCW THR D  155  UNP  P0A3G3    ALA   155 ENGINEERED MUTATION            
SEQADV 7PCW LYS D  160  UNP  P0A3G3    GLU   160 ENGINEERED MUTATION            
SEQADV 7PCW VAL D  167  UNP  P0A3G3    ALA   167 ENGINEERED MUTATION            
SEQADV 7PCW THR D  172  UNP  P0A3G3    ALA   172 ENGINEERED MUTATION            
SEQADV 7PCW TRP D  175  UNP  P0A3G3    LYS   175 ENGINEERED MUTATION            
SEQADV 7PCW GLY D  176  UNP  P0A3G3    CYS   176 ENGINEERED MUTATION            
SEQADV 7PCW ASN D  195  UNP  P0A3G3    LYS   195 ENGINEERED MUTATION            
SEQADV 7PCW GLU D  224  UNP  P0A3G3    ALA   224 ENGINEERED MUTATION            
SEQADV 7PCW ASP D  227  UNP  P0A3G3    ASN   227 ENGINEERED MUTATION            
SEQADV 7PCW LYS D  257  UNP  P0A3G3    GLU   257 ENGINEERED MUTATION            
SEQADV 7PCW ALA D  264  UNP  P0A3G3    THR   264 ENGINEERED MUTATION            
SEQADV 7PCW ASN D  272  UNP  P0A3G3    HIS   272 ENGINEERED MUTATION            
SEQADV 7PCW LEU D  273  UNP  P0A3G3    TYR   273 ENGINEERED MUTATION            
SEQADV 7PCW SER D  291  UNP  P0A3G3    PRO   291 ENGINEERED MUTATION            
SEQADV 7PCW THR D  292  UNP  P0A3G3    ALA   292 ENGINEERED MUTATION            
SEQADV 7PCW GLU D  294  UNP  P0A3G3              EXPRESSION TAG                 
SEQADV 7PCW ILE D  295  UNP  P0A3G3              EXPRESSION TAG                 
SEQRES   1 A  293  GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL          
SEQRES   2 A  293  GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY          
SEQRES   3 A  293  PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN          
SEQRES   4 A  293  PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS          
SEQRES   5 A  293  VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE          
SEQRES   6 A  293  GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE          
SEQRES   7 A  293  PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU          
SEQRES   8 A  293  ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP          
SEQRES   9 A  293  TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN          
SEQRES  10 A  293  PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE          
SEQRES  11 A  293  ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA          
SEQRES  12 A  293  ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY          
SEQRES  13 A  293  ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY          
SEQRES  14 A  293  THR LEU PRO TRP GLY VAL VAL ARG PRO LEU THR GLU VAL          
SEQRES  15 A  293  GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL          
SEQRES  16 A  293  ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO          
SEQRES  17 A  293  ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU          
SEQRES  18 A  293  GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS          
SEQRES  19 A  293  LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO          
SEQRES  20 A  293  ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS          
SEQRES  21 A  293  LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN          
SEQRES  22 A  293  GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG          
SEQRES  23 A  293  TRP LEU SER THR LEU GLU ILE                                  
SEQRES   1 B  293  GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL          
SEQRES   2 B  293  GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY          
SEQRES   3 B  293  PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN          
SEQRES   4 B  293  PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS          
SEQRES   5 B  293  VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE          
SEQRES   6 B  293  GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE          
SEQRES   7 B  293  PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU          
SEQRES   8 B  293  ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP          
SEQRES   9 B  293  TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN          
SEQRES  10 B  293  PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE          
SEQRES  11 B  293  ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA          
SEQRES  12 B  293  ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY          
SEQRES  13 B  293  ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY          
SEQRES  14 B  293  THR LEU PRO TRP GLY VAL VAL ARG PRO LEU THR GLU VAL          
SEQRES  15 B  293  GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL          
SEQRES  16 B  293  ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO          
SEQRES  17 B  293  ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU          
SEQRES  18 B  293  GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS          
SEQRES  19 B  293  LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO          
SEQRES  20 B  293  ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS          
SEQRES  21 B  293  LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN          
SEQRES  22 B  293  GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG          
SEQRES  23 B  293  TRP LEU SER THR LEU GLU ILE                                  
SEQRES   1 C  293  GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL          
SEQRES   2 C  293  GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY          
SEQRES   3 C  293  PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN          
SEQRES   4 C  293  PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS          
SEQRES   5 C  293  VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE          
SEQRES   6 C  293  GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE          
SEQRES   7 C  293  PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU          
SEQRES   8 C  293  ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP          
SEQRES   9 C  293  TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN          
SEQRES  10 C  293  PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE          
SEQRES  11 C  293  ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA          
SEQRES  12 C  293  ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY          
SEQRES  13 C  293  ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY          
SEQRES  14 C  293  THR LEU PRO TRP GLY VAL VAL ARG PRO LEU THR GLU VAL          
SEQRES  15 C  293  GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL          
SEQRES  16 C  293  ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO          
SEQRES  17 C  293  ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU          
SEQRES  18 C  293  GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS          
SEQRES  19 C  293  LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO          
SEQRES  20 C  293  ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS          
SEQRES  21 C  293  LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN          
SEQRES  22 C  293  GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG          
SEQRES  23 C  293  TRP LEU SER THR LEU GLU ILE                                  
SEQRES   1 D  293  GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL          
SEQRES   2 D  293  GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY          
SEQRES   3 D  293  PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN          
SEQRES   4 D  293  PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS          
SEQRES   5 D  293  VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE          
SEQRES   6 D  293  GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE          
SEQRES   7 D  293  PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU          
SEQRES   8 D  293  ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP          
SEQRES   9 D  293  TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN          
SEQRES  10 D  293  PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE          
SEQRES  11 D  293  ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA          
SEQRES  12 D  293  ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY          
SEQRES  13 D  293  ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY          
SEQRES  14 D  293  THR LEU PRO TRP GLY VAL VAL ARG PRO LEU THR GLU VAL          
SEQRES  15 D  293  GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL          
SEQRES  16 D  293  ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO          
SEQRES  17 D  293  ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU          
SEQRES  18 D  293  GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS          
SEQRES  19 D  293  LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO          
SEQRES  20 D  293  ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS          
SEQRES  21 D  293  LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN          
SEQRES  22 D  293  GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG          
SEQRES  23 D  293  TRP LEU SER THR LEU GLU ILE                                  
HET    OEH  A 301      44                                                       
HET     CL  A 302       1                                                       
HET    OEH  B 301      44                                                       
HET     CL  B 302       1                                                       
HET    OEH  C 301      44                                                       
HET     CL  C 302       1                                                       
HET    OEH  D 301      44                                                       
HET     CL  D 302       1                                                       
HETNAM     OEH [9-[2-CARBOXY-5-[2-[2-(6-CHLORANYLHEXOXY)                        
HETNAM   2 OEH  ETHOXY]ETHYLCARBAMOYL]PHENYL]-6-(DIMETHYLAMINO)                 
HETNAM   3 OEH  XANTHEN-3-YLIDENE]-DIMETHYL-AZANIUM                             
HETNAM      CL CHLORIDE ION                                                     
FORMUL   5  OEH    4(C35 H43 CL N3 O6 1+)                                       
FORMUL   6   CL    4(CL 1-)                                                     
FORMUL  13  HOH   *125(H2 O)                                                    
HELIX    1 AA1 SER A   44  ARG A   49  5                                   6    
HELIX    2 AA2 ILE A   51  ALA A   56  1                                   6    
HELIX    3 AA3 PHE A   80  LEU A   95  1                                  16    
HELIX    4 AA4 ASP A  106  ASN A  119  1                                  14    
HELIX    5 AA5 THR A  137  TRP A  141  5                                   5    
HELIX    6 AA6 PRO A  142  ARG A  153  1                                  12    
HELIX    7 AA7 ASP A  156  ILE A  163  1                                   8    
HELIX    8 AA8 ASN A  166  GLY A  171  1                                   6    
HELIX    9 AA9 LEU A  173  VAL A  177  5                                   5    
HELIX   10 AB1 THR A  182  GLU A  191  1                                  10    
HELIX   11 AB2 PRO A  192  LEU A  194  5                                   3    
HELIX   12 AB3 ASN A  195  ASP A  198  5                                   4    
HELIX   13 AB4 ARG A  199  GLU A  208  1                                  10    
HELIX   14 AB5 PRO A  215  SER A  232  1                                  18    
HELIX   15 AB6 PRO A  248  LEU A  259  1                                  12    
HELIX   16 AB7 LEU A  273  ASN A  278  1                                   6    
HELIX   17 AB8 ASN A  278  THR A  292  1                                  15    
HELIX   18 AB9 SER B   44  ARG B   49  5                                   6    
HELIX   19 AC1 ILE B   51  ALA B   56  1                                   6    
HELIX   20 AC2 PHE B   80  LEU B   95  1                                  16    
HELIX   21 AC3 ASP B  106  ASN B  119  1                                  14    
HELIX   22 AC4 PRO B  142  PHE B  144  5                                   3    
HELIX   23 AC5 ALA B  145  ARG B  153  1                                   9    
HELIX   24 AC6 ASP B  156  ILE B  163  1                                   8    
HELIX   25 AC7 ASN B  166  GLY B  171  1                                   6    
HELIX   26 AC8 LEU B  173  VAL B  177  5                                   5    
HELIX   27 AC9 THR B  182  GLU B  191  1                                  10    
HELIX   28 AD1 PRO B  192  LEU B  194  5                                   3    
HELIX   29 AD2 ASN B  195  ASP B  198  5                                   4    
HELIX   30 AD3 ARG B  199  LEU B  209  1                                  11    
HELIX   31 AD4 PRO B  215  SER B  232  1                                  18    
HELIX   32 AD5 PRO B  248  LEU B  259  1                                  12    
HELIX   33 AD6 LEU B  273  ASN B  278  1                                   6    
HELIX   34 AD7 ASN B  278  SER B  291  1                                  14    
HELIX   35 AD8 SER C   44  ARG C   49  5                                   6    
HELIX   36 AD9 ILE C   51  ALA C   56  1                                   6    
HELIX   37 AE1 PHE C   80  LEU C   95  1                                  16    
HELIX   38 AE2 ASP C  106  ASN C  119  1                                  14    
HELIX   39 AE3 THR C  137  TRP C  141  5                                   5    
HELIX   40 AE4 PRO C  142  PHE C  144  5                                   3    
HELIX   41 AE5 ALA C  145  ARG C  153  1                                   9    
HELIX   42 AE6 ASP C  156  ILE C  163  1                                   8    
HELIX   43 AE7 ASN C  166  GLY C  171  1                                   6    
HELIX   44 AE8 LEU C  173  VAL C  177  5                                   5    
HELIX   45 AE9 THR C  182  GLU C  191  1                                  10    
HELIX   46 AF1 PRO C  192  LEU C  194  5                                   3    
HELIX   47 AF2 ASN C  195  ASP C  198  5                                   4    
HELIX   48 AF3 ARG C  199  LEU C  209  1                                  11    
HELIX   49 AF4 PRO C  215  SER C  232  1                                  18    
HELIX   50 AF5 PRO C  248  LEU C  259  1                                  12    
HELIX   51 AF6 LEU C  273  ASP C  277  5                                   5    
HELIX   52 AF7 ASN C  278  SER C  291  1                                  14    
HELIX   53 AF8 SER D   44  ARG D   49  5                                   6    
HELIX   54 AF9 ILE D   51  VAL D   55  5                                   5    
HELIX   55 AG1 PHE D   80  LEU D   95  1                                  16    
HELIX   56 AG2 ASP D  106  ASN D  119  1                                  14    
HELIX   57 AG3 PRO D  142  ARG D  153  1                                  12    
HELIX   58 AG4 ASP D  156  ILE D  163  1                                   8    
HELIX   59 AG5 ASN D  166  GLY D  171  1                                   6    
HELIX   60 AG6 LEU D  173  VAL D  177  5                                   5    
HELIX   61 AG7 THR D  182  GLU D  191  1                                  10    
HELIX   62 AG8 PRO D  192  LEU D  194  5                                   3    
HELIX   63 AG9 ASN D  195  ASP D  198  5                                   4    
HELIX   64 AH1 ARG D  199  GLU D  208  1                                  10    
HELIX   65 AH2 PRO D  215  SER D  232  1                                  18    
HELIX   66 AH3 PRO D  248  LEU D  259  1                                  12    
HELIX   67 AH4 LEU D  273  ASN D  278  1                                   6    
HELIX   68 AH5 ASN D  278  THR D  292  1                                  15    
SHEET    1 AA1 8 HIS A  13  VAL A  17  0                                        
SHEET    2 AA1 8 GLU A  20  VAL A  27 -1  O  GLU A  20   N  VAL A  17           
SHEET    3 AA1 8 CYS A  61  PRO A  64 -1  O  CYS A  61   N  VAL A  27           
SHEET    4 AA1 8 VAL A  35  LEU A  38  1  N  PHE A  37   O  ILE A  62           
SHEET    5 AA1 8 VAL A 100  HIS A 105  1  O  VAL A 101   N  LEU A  36           
SHEET    6 AA1 8 VAL A 123  MET A 129  1  O  ALA A 127   N  LEU A 102           
SHEET    7 AA1 8 LYS A 236  PRO A 243  1  O  LEU A 237   N  PHE A 128           
SHEET    8 AA1 8 CYS A 262  GLY A 270  1  O  LYS A 263   N  LEU A 238           
SHEET    1 AA2 8 HIS B  13  VAL B  17  0                                        
SHEET    2 AA2 8 GLU B  20  VAL B  27 -1  O  GLU B  20   N  VAL B  17           
SHEET    3 AA2 8 CYS B  61  PRO B  64 -1  O  CYS B  61   N  VAL B  27           
SHEET    4 AA2 8 VAL B  35  LEU B  38  1  N  PHE B  37   O  ILE B  62           
SHEET    5 AA2 8 VAL B 100  HIS B 105  1  O  VAL B 101   N  LEU B  36           
SHEET    6 AA2 8 VAL B 123  MET B 129  1  O  ALA B 127   N  LEU B 102           
SHEET    7 AA2 8 LYS B 236  PRO B 243  1  O  LEU B 237   N  PHE B 128           
SHEET    8 AA2 8 CYS B 262  GLY B 270  1  O  LYS B 263   N  LEU B 238           
SHEET    1 AA3 8 HIS C  13  VAL C  17  0                                        
SHEET    2 AA3 8 GLU C  20  VAL C  27 -1  O  GLU C  20   N  VAL C  17           
SHEET    3 AA3 8 CYS C  61  PRO C  64 -1  O  CYS C  61   N  VAL C  27           
SHEET    4 AA3 8 VAL C  35  LEU C  38  1  N  VAL C  35   O  ILE C  62           
SHEET    5 AA3 8 VAL C 100  HIS C 105  1  O  VAL C 101   N  LEU C  36           
SHEET    6 AA3 8 VAL C 123  MET C 129  1  O  ALA C 127   N  LEU C 102           
SHEET    7 AA3 8 LYS C 236  PRO C 243  1  O  LEU C 237   N  PHE C 128           
SHEET    8 AA3 8 CYS C 262  GLY C 270  1  O  LYS C 263   N  LEU C 238           
SHEET    1 AA4 8 HIS D  13  VAL D  17  0                                        
SHEET    2 AA4 8 GLU D  20  VAL D  27 -1  O  GLU D  20   N  VAL D  17           
SHEET    3 AA4 8 CYS D  61  PRO D  64 -1  O  CYS D  61   N  VAL D  27           
SHEET    4 AA4 8 VAL D  35  LEU D  38  1  N  PHE D  37   O  ILE D  62           
SHEET    5 AA4 8 VAL D 100  HIS D 105  1  O  VAL D 101   N  LEU D  36           
SHEET    6 AA4 8 VAL D 123  MET D 129  1  O  ALA D 127   N  LEU D 102           
SHEET    7 AA4 8 LYS D 236  PRO D 243  1  O  LEU D 237   N  PHE D 128           
SHEET    8 AA4 8 CYS D 262  GLY D 270  1  O  LYS D 263   N  LEU D 238           
LINK         OD2 ASP A 106                 C20 OEH A 301     1555   1555  1.38  
LINK         OD2 ASP B 106                 C20 OEH B 301     1555   1555  1.38  
LINK         OD2 ASP C 106                 C20 OEH C 301     1555   1555  1.38  
LINK         OD2 ASP D 106                 C20 OEH D 301     1555   1555  1.38  
CISPEP   1 ASN A   41    PRO A   42          0        -0.88                     
CISPEP   2 GLU A  214    PRO A  215          0        -3.29                     
CISPEP   3 THR A  242    PRO A  243          0         3.49                     
CISPEP   4 ASN B   41    PRO B   42          0        -0.75                     
CISPEP   5 GLU B  214    PRO B  215          0        -6.81                     
CISPEP   6 THR B  242    PRO B  243          0         4.38                     
CISPEP   7 ASN C   41    PRO C   42          0        -1.78                     
CISPEP   8 GLU C  214    PRO C  215          0        -4.58                     
CISPEP   9 THR C  242    PRO C  243          0         2.32                     
CISPEP  10 ASN D   41    PRO D   42          0        -1.83                     
CISPEP  11 GLU D  214    PRO D  215          0        -2.83                     
CISPEP  12 THR D  242    PRO D  243          0         2.25                     
CRYST1   44.320   76.560   85.760  68.40  79.81  79.02 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022563 -0.004377 -0.002710        0.00000                         
SCALE2      0.000000  0.013305 -0.004909        0.00000                         
SCALE3      0.000000  0.000000  0.012628        0.00000                         
TER    2348      GLU A 294                                                      
TER    4705      ILE B 295                                                      
TER    7062      ILE C 295                                                      
TER    9410      GLU D 294                                                      
MASTER      282    0    8   68   32    0    0    6 9711    4  180   92          
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.
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