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LongText Report for: 4DMK-pdb

Name Class
4DMK-pdb
HEADER    HYDROLASE                               07-FEB-12   4DMK              
TITLE     CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF WITH THE Y239F    
TITLE    2 MUTATION                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE HYDROLASE;                                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: CIF (UNP RESIDUES 25-319);                                 
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 208963;                                              
SOURCE   4 STRAIN: UCBPP-PA14;                                                  
SOURCE   5 GENE: PA14_26090;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TOP10;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMQ70                                     
KEYWDS    ALPHA BETA HYDROLASE, EPOXIDE HYDROLASE, SECRETED, HYDROLASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.D.BAHL,D.R.MADDEN                                                   
REVDAT   1   07-AUG-13 4DMK    0                                                
JRNL        AUTH   C.D.BAHL,D.R.MADDEN                                          
JRNL        TITL   CIF EPOXIDE HYDROLASE ENZYME ACTIVITY IS REQUIRED FOR CFTR   
JRNL        TITL 2 INHIBITORY ACTIVITY                                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.1_357)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.19                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 190239                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.182                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9495                            
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 46.2074 -  4.6593    0.99     6144   480  0.1586 0.1395        
REMARK   3     2  4.6593 -  3.6987    0.99     6520     0  0.1335 10000000.0000 
REMARK   3     3  3.6987 -  3.2313    0.99     6001   489  0.1445 0.1595        
REMARK   3     4  3.2313 -  2.9359    0.99     5989   489  0.1627 0.1868        
REMARK   3     5  2.9359 -  2.7255    0.99     6478     0  0.1594 10000000.0000 
REMARK   3     6  2.7255 -  2.5648    0.98     5934   475  0.1618 0.1755        
REMARK   3     7  2.5648 -  2.4364    0.98     5942   483  0.1592 0.1779        
REMARK   3     8  2.4364 -  2.3304    0.98     6414     0  0.1559 10000000.0000 
REMARK   3     9  2.3304 -  2.2406    0.98     5877   476  0.1495 0.1694        
REMARK   3    10  2.2406 -  2.1633    0.98     5933   476  0.1520 0.1725        
REMARK   3    11  2.1633 -  2.0957    0.98     6358     0  0.1491 10000000.0000 
REMARK   3    12  2.0957 -  2.0358    0.98     5913   475  0.1541 0.1799        
REMARK   3    13  2.0358 -  1.9822    0.97     5880   477  0.1540 0.1808        
REMARK   3    14  1.9822 -  1.9338    0.97     6300     0  0.1546 10000000.0000 
REMARK   3    15  1.9338 -  1.8899    0.97     5852   476  0.1552 0.1767        
REMARK   3    16  1.8899 -  1.8496    0.97     5843   472  0.1564 0.1850        
REMARK   3    17  1.8496 -  1.8126    0.97     6341     0  0.1550 10000000.0000 
REMARK   3    18  1.8126 -  1.7784    0.97     5794   473  0.1526 0.1937        
REMARK   3    19  1.7784 -  1.7467    0.97     5798   479  0.1607 0.2020        
REMARK   3    20  1.7467 -  1.7171    0.97     6319     0  0.1586 10000000.0000 
REMARK   3    21  1.7171 -  1.6894    0.96     5819   470  0.1558 0.1804        
REMARK   3    22  1.6894 -  1.6634    0.96     5783   473  0.1502 0.1808        
REMARK   3    23  1.6634 -  1.6389    0.97     6285     0  0.1560 10000000.0000 
REMARK   3    24  1.6389 -  1.6158    0.97     5773   456  0.1591 0.1849        
REMARK   3    25  1.6158 -  1.5940    0.96     5758   467  0.1612 0.2011        
REMARK   3    26  1.5940 -  1.5733    0.96     6233     0  0.1650 10000000.0000 
REMARK   3    27  1.5733 -  1.5536    0.96     5786   466  0.1697 0.1975        
REMARK   3    28  1.5536 -  1.5349    0.96     5748   474  0.1766 0.2093        
REMARK   3    29  1.5349 -  1.5170    0.96     6197     0  0.1817 10000000.0000 
REMARK   3    30  1.5170 -  1.5000    0.96     5732   469  0.1894 0.2212        
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              : 0.35                                          
REMARK   3   B_SOL              : 33.64                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.280           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.05150                                             
REMARK   3    B22 (A**2) : -0.74060                                             
REMARK   3    B33 (A**2) : 1.79210                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.05110                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           9897                                  
REMARK   3   ANGLE     :  1.069          13436                                  
REMARK   3   CHIRALITY :  0.078           1378                                  
REMARK   3   PLANARITY :  0.005           1770                                  
REMARK   3   DIHEDRAL  : 12.756           3632                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (chain A and resid 25:320)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   5.7138  29.9198  26.9823              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0344 T22:   0.0302                                     
REMARK   3      T33:   0.0441 T12:   0.0050                                     
REMARK   3      T13:  -0.0022 T23:  -0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3200 L22:   0.4569                                     
REMARK   3      L33:   0.3883 L12:   0.0156                                     
REMARK   3      L13:   0.0379 L23:   0.0130                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0053 S12:  -0.0221 S13:   0.0533                       
REMARK   3      S21:   0.0334 S22:  -0.0088 S23:  -0.0560                       
REMARK   3      S31:  -0.0499 S32:   0.0057 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (chain B and resid 25:321)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  14.7027  -9.7387  15.6766              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0370 T22:   0.0410                                     
REMARK   3      T33:   0.0246 T12:   0.0169                                     
REMARK   3      T13:   0.0049 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5841 L22:   0.4971                                     
REMARK   3      L33:   0.2522 L12:  -0.1250                                     
REMARK   3      L13:   0.0194 L23:   0.1265                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0193 S12:   0.0151 S13:  -0.0295                       
REMARK   3      S21:  -0.0098 S22:  -0.0022 S23:  -0.0633                       
REMARK   3      S31:   0.0258 S32:   0.0102 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (chain C and resid 25:321)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -21.9860  -2.9665  27.2378              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0361 T22:   0.0375                                     
REMARK   3      T33:   0.0176 T12:   0.0034                                     
REMARK   3      T13:   0.0101 T23:   0.0119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3954 L22:   0.3607                                     
REMARK   3      L33:   0.3863 L12:  -0.0021                                     
REMARK   3      L13:   0.0452 L23:   0.0885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0041 S12:  -0.0535 S13:  -0.0380                       
REMARK   3      S21:   0.0425 S22:  -0.0102 S23:   0.0367                       
REMARK   3      S31:   0.0572 S32:  -0.0176 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (chain D and resid 25:320)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -31.0606  36.6377  15.7294              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0316 T22:   0.0254                                     
REMARK   3      T33:   0.0494 T12:   0.0124                                     
REMARK   3      T13:  -0.0158 T23:  -0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5987 L22:   0.5250                                     
REMARK   3      L33:   0.2289 L12:  -0.1914                                     
REMARK   3      L13:  -0.0340 L23:  -0.0891                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0095 S12:   0.0095 S13:   0.1003                       
REMARK   3      S21:  -0.0285 S22:   0.0029 S23:   0.0056                       
REMARK   3      S31:  -0.0326 S32:  -0.0083 S33:   0.0000                       
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 4DMK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070517.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9770                             
REMARK 200  MONOCHROMATOR                  : SI(111) CHANNEL CUT MONOCHROMATOR  
REMARK 200  OPTICS                         : TOROIDAL FOCUSING MIRROR           
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS-PACKAGE                        
REMARK 200  DATA SCALING SOFTWARE          : XDS-PACKAGE                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 190252                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.186                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05800                            
REMARK 200   FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.30200                            
REMARK 200   FOR SHELL         : 4.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: CHAIN A OF PDB ENTRY 3KD2                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15.5% PEG 8000, 0.125M CALCIUM           
REMARK 280  CHLORIDE, 0.1M SODIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       84.33900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.01600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       84.33900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       42.01600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 3330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 3350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 698  LIES ON A SPECIAL POSITION.                          
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     HIS A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     HIS A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     HIS B   322                                                      
REMARK 465     HIS B   323                                                      
REMARK 465     HIS B   324                                                      
REMARK 465     HIS B   325                                                      
REMARK 465     HIS C   322                                                      
REMARK 465     HIS C   323                                                      
REMARK 465     HIS C   324                                                      
REMARK 465     HIS C   325                                                      
REMARK 465     HIS D   321                                                      
REMARK 465     HIS D   322                                                      
REMARK 465     HIS D   323                                                      
REMARK 465     HIS D   324                                                      
REMARK 465     HIS D   325                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A  319   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     ARG B  319   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     ARG C  319   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     ARG D  319   CB   CG   CD   NE   CZ   NH1  NH2                   
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    ASP A 129     -131.10     61.35                                   
REMARK 500    ALA A 154      148.16    178.03                                   
REMARK 500    CYS A 303       55.45   -141.34                                   
REMARK 500    THR B  99      -67.26    -90.49                                   
REMARK 500    ASP B 129     -137.49     60.86                                   
REMARK 500    ALA B 154      145.07   -179.12                                   
REMARK 500    ASP B 185       18.84     58.90                                   
REMARK 500    CYS B 303       54.65   -142.36                                   
REMARK 500    ASP C 129     -129.88     61.67                                   
REMARK 500    ALA C 154      148.55    175.10                                   
REMARK 500    CYS C 303       55.83   -142.19                                   
REMARK 500    THR D  99      -69.04    -91.16                                   
REMARK 500    ASP D 129     -134.82     58.38                                   
REMARK 500    ALA D 154      144.98   -179.96                                   
REMARK 500    ASP D 185       18.89     59.64                                   
REMARK 500    CYS D 303       54.60   -140.32                                   
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 GOL A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KD2   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN, BUT WITH THE WILD TYPE SEQUENCE                        
REMARK 900 RELATED ID: 3KDA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PI6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DLN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DM7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DMC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DMF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DMH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DNF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DNO   RELATED DB: PDB                                   
DBREF  4DMK A   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
DBREF  4DMK B   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
DBREF  4DMK C   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
DBREF  4DMK D   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
SEQADV 4DMK PHE A  239  UNP  Q02P97    TYR   239 ENGINEERED MUTATION            
SEQADV 4DMK HIS A  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS A  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS A  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS A  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS A  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS A  325  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK PHE B  239  UNP  Q02P97    TYR   239 ENGINEERED MUTATION            
SEQADV 4DMK HIS B  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS B  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS B  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS B  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS B  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS B  325  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK PHE C  239  UNP  Q02P97    TYR   239 ENGINEERED MUTATION            
SEQADV 4DMK HIS C  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS C  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS C  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS C  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS C  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS C  325  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK PHE D  239  UNP  Q02P97    TYR   239 ENGINEERED MUTATION            
SEQADV 4DMK HIS D  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS D  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS D  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS D  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS D  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DMK HIS D  325  UNP  Q02P97              EXPRESSION TAG                 
SEQRES   1 A  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 A  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 A  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 A  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 A  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 A  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 A  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 A  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 A  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 A  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA          
SEQRES  11 A  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 A  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 A  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 A  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 A  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 A  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 A  301  ASN ALA SER PHE GLU TYR PHE ARG ALA LEU ASN GLU SER          
SEQRES  18 A  301  VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN          
SEQRES  19 A  301  MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY          
SEQRES  20 A  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 A  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 A  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 A  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 A  301  HIS HIS                                                      
SEQRES   1 B  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 B  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 B  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 B  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 B  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 B  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 B  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 B  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 B  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 B  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA          
SEQRES  11 B  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 B  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 B  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 B  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 B  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 B  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 B  301  ASN ALA SER PHE GLU TYR PHE ARG ALA LEU ASN GLU SER          
SEQRES  18 B  301  VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN          
SEQRES  19 B  301  MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY          
SEQRES  20 B  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 B  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 B  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 B  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 B  301  HIS HIS                                                      
SEQRES   1 C  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 C  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 C  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 C  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 C  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 C  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 C  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 C  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 C  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 C  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA          
SEQRES  11 C  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 C  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 C  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 C  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 C  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 C  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 C  301  ASN ALA SER PHE GLU TYR PHE ARG ALA LEU ASN GLU SER          
SEQRES  18 C  301  VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN          
SEQRES  19 C  301  MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY          
SEQRES  20 C  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 C  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 C  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 C  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 C  301  HIS HIS                                                      
SEQRES   1 D  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 D  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 D  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 D  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 D  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 D  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 D  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 D  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 D  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 D  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA          
SEQRES  11 D  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 D  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 D  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 D  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 D  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 D  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 D  301  ASN ALA SER PHE GLU TYR PHE ARG ALA LEU ASN GLU SER          
SEQRES  18 D  301  VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN          
SEQRES  19 D  301  MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY          
SEQRES  20 D  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 D  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 D  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 D  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 D  301  HIS HIS                                                      
HET    GOL  A 401       6                                                       
HET    GOL  B 401       6                                                       
HET    GOL  C 401       6                                                       
HET    GOL  D 401       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  GOL    4(C3 H8 O3)                                                  
FORMUL   9  HOH   *1250(H2 O)                                                   
HELIX    1   1 THR A   66  HIS A   71  5                                   6    
HELIX    2   2 GLN A   72  ALA A   78  1                                   7    
HELIX    3   3 SER A  102  SER A  118  1                                  17    
HELIX    4   4 ASP A  129  ASN A  134  1                                   6    
HELIX    5   5 THR A  135  ASN A  142  1                                   8    
HELIX    6   6 ASP A  158  PHE A  164  5                                   7    
HELIX    7   7 TRP A  176  ALA A  183  1                                   8    
HELIX    8   8 ARG A  186  ALA A  193  1                                   8    
HELIX    9   9 LYS A  195  HIS A  207  1                                  13    
HELIX   10  10 ASN A  210  PHE A  214  5                                   5    
HELIX   11  11 SER A  215  ALA A  227  1                                  13    
HELIX   12  12 LYS A  228  ALA A  241  1                                  14    
HELIX   13  13 ALA A  241  ALA A  253  1                                  13    
HELIX   14  14 THR A  274  ALA A  284  1                                  11    
HELIX   15  15 TRP A  298  CYS A  303  1                                   6    
HELIX   16  16 CYS A  303  SER A  316  1                                  14    
HELIX   17  17 THR B   66  HIS B   71  5                                   6    
HELIX   18  18 GLN B   72  ALA B   78  1                                   7    
HELIX   19  19 SER B  102  SER B  118  1                                  17    
HELIX   20  20 ASP B  129  ASN B  134  1                                   6    
HELIX   21  21 THR B  135  ASN B  142  1                                   8    
HELIX   22  22 ASP B  158  PHE B  164  5                                   7    
HELIX   23  23 TRP B  176  ALA B  183  1                                   8    
HELIX   24  24 ARG B  186  ALA B  193  1                                   8    
HELIX   25  25 LYS B  195  HIS B  207  1                                  13    
HELIX   26  26 ASN B  210  PHE B  214  5                                   5    
HELIX   27  27 SER B  215  ALA B  227  1                                  13    
HELIX   28  28 LYS B  228  ALA B  241  1                                  14    
HELIX   29  29 ALA B  241  ALA B  253  1                                  13    
HELIX   30  30 THR B  274  ALA B  284  1                                  11    
HELIX   31  31 TRP B  298  CYS B  303  1                                   6    
HELIX   32  32 CYS B  303  ARG B  317  1                                  15    
HELIX   33  33 THR C   66  HIS C   71  5                                   6    
HELIX   34  34 LEU C   73  ALA C   78  1                                   6    
HELIX   35  35 SER C  102  SER C  118  1                                  17    
HELIX   36  36 ASP C  129  ASN C  134  1                                   6    
HELIX   37  37 THR C  135  ASN C  142  1                                   8    
HELIX   38  38 ASP C  158  PHE C  164  5                                   7    
HELIX   39  39 TRP C  176  ALA C  183  1                                   8    
HELIX   40  40 ARG C  186  ALA C  193  1                                   8    
HELIX   41  41 LYS C  195  HIS C  207  1                                  13    
HELIX   42  42 ASN C  210  PHE C  214  5                                   5    
HELIX   43  43 SER C  215  ALA C  227  1                                  13    
HELIX   44  44 LYS C  228  ALA C  241  1                                  14    
HELIX   45  45 ALA C  241  ALA C  253  1                                  13    
HELIX   46  46 THR C  274  ALA C  284  1                                  11    
HELIX   47  47 TRP C  298  CYS C  303  1                                   6    
HELIX   48  48 CYS C  303  SER C  316  1                                  14    
HELIX   49  49 THR D   66  HIS D   71  5                                   6    
HELIX   50  50 GLN D   72  ALA D   78  1                                   7    
HELIX   51  51 SER D  102  SER D  118  1                                  17    
HELIX   52  52 ASP D  129  ASN D  134  1                                   6    
HELIX   53  53 THR D  135  ASN D  142  1                                   8    
HELIX   54  54 ASP D  158  PHE D  164  5                                   7    
HELIX   55  55 TRP D  176  ALA D  183  1                                   8    
HELIX   56  56 ARG D  186  ALA D  193  1                                   8    
HELIX   57  57 LYS D  195  HIS D  207  1                                  13    
HELIX   58  58 ASN D  210  PHE D  214  5                                   5    
HELIX   59  59 SER D  215  LYS D  228  1                                  14    
HELIX   60  60 LYS D  228  ALA D  241  1                                  14    
HELIX   61  61 ALA D  241  ALA D  253  1                                  13    
HELIX   62  62 THR D  274  ALA D  284  1                                  11    
HELIX   63  63 TRP D  298  CYS D  303  1                                   6    
HELIX   64  64 CYS D  303  SER D  316  1                                  14    
SHEET    1   A 8 GLU A  35  VAL A  41  0                                        
SHEET    2   A 8 VAL A  44  GLY A  52 -1  O  LEU A  46   N  ARG A  39           
SHEET    3   A 8 THR A  82  PRO A  86 -1  O  VAL A  83   N  GLY A  51           
SHEET    4   A 8 LEU A  56  VAL A  60  1  N  LEU A  59   O  ILE A  84           
SHEET    5   A 8 PHE A 123  HIS A 128  1  O  ASP A 124   N  LEU A  56           
SHEET    6   A 8 ILE A 146  MET A 152  1  O  VAL A 150   N  LEU A 125           
SHEET    7   A 8 THR A 261  GLY A 266  1  O  MET A 262   N  TYR A 151           
SHEET    8   A 8 VAL A 287  LEU A 292  1  O  LEU A 292   N  ALA A 265           
SHEET    1   B 2 PHE A 167  THR A 168  0                                        
SHEET    2   B 2 GLY A 171  GLU A 172 -1  O  GLY A 171   N  THR A 168           
SHEET    1   C 8 GLU B  35  VAL B  41  0                                        
SHEET    2   C 8 VAL B  44  GLY B  52 -1  O  LEU B  46   N  ARG B  39           
SHEET    3   C 8 THR B  82  PRO B  86 -1  O  VAL B  83   N  GLY B  51           
SHEET    4   C 8 LEU B  56  VAL B  60  1  N  VAL B  57   O  THR B  82           
SHEET    5   C 8 PHE B 123  HIS B 128  1  O  VAL B 126   N  VAL B  60           
SHEET    6   C 8 ILE B 146  MET B 152  1  O  VAL B 150   N  LEU B 125           
SHEET    7   C 8 THR B 261  GLY B 266  1  O  MET B 262   N  LEU B 149           
SHEET    8   C 8 VAL B 287  LEU B 292  1  O  LEU B 292   N  ALA B 265           
SHEET    1   D 2 PHE B 167  THR B 168  0                                        
SHEET    2   D 2 GLY B 171  GLU B 172 -1  O  GLY B 171   N  THR B 168           
SHEET    1   E 8 GLU C  35  VAL C  41  0                                        
SHEET    2   E 8 VAL C  44  GLY C  52 -1  O  LYS C  50   N  GLU C  35           
SHEET    3   E 8 THR C  82  PRO C  86 -1  O  VAL C  83   N  GLY C  51           
SHEET    4   E 8 LEU C  56  VAL C  60  1  N  VAL C  57   O  THR C  82           
SHEET    5   E 8 PHE C 123  HIS C 128  1  O  ASP C 124   N  LEU C  56           
SHEET    6   E 8 ILE C 146  MET C 152  1  O  VAL C 150   N  LEU C 125           
SHEET    7   E 8 THR C 261  GLY C 266  1  O  MET C 262   N  TYR C 151           
SHEET    8   E 8 VAL C 287  LEU C 292  1  O  LEU C 292   N  ALA C 265           
SHEET    1   F 2 PHE C 167  THR C 168  0                                        
SHEET    2   F 2 GLY C 171  GLU C 172 -1  O  GLY C 171   N  THR C 168           
SHEET    1   G 8 GLU D  35  VAL D  41  0                                        
SHEET    2   G 8 VAL D  44  GLY D  52 -1  O  LEU D  46   N  ARG D  39           
SHEET    3   G 8 THR D  82  PRO D  86 -1  O  VAL D  83   N  GLY D  51           
SHEET    4   G 8 LEU D  56  VAL D  60  1  N  VAL D  57   O  THR D  82           
SHEET    5   G 8 PHE D 123  HIS D 128  1  O  ASP D 124   N  LEU D  56           
SHEET    6   G 8 ILE D 146  MET D 152  1  O  VAL D 150   N  LEU D 125           
SHEET    7   G 8 THR D 261  GLY D 266  1  O  MET D 262   N  LEU D 149           
SHEET    8   G 8 VAL D 287  LEU D 292  1  O  LEU D 292   N  ALA D 265           
SHEET    1   H 2 PHE D 167  THR D 168  0                                        
SHEET    2   H 2 GLY D 171  GLU D 172 -1  O  GLY D 171   N  THR D 168           
SSBOND   1 CYS A  295    CYS A  303                          1555   1555  2.01  
SSBOND   2 CYS B  295    CYS B  303                          1555   1555  2.01  
SSBOND   3 CYS C  295    CYS C  303                          1555   1555  2.01  
SSBOND   4 CYS D  295    CYS D  303                          1555   1555  2.01  
SITE     1 AC1 11 ASP A 129  GLU A 153  ALA A 154  PRO A 155                    
SITE     2 AC1 11 VAL A 175  PHE A 178  HIS A 207  HIS A 297                    
SITE     3 AC1 11 HOH A 529  HOH A 653  HOH A 682                               
SITE     1 AC2 10 ASP B 129  GLU B 153  ALA B 154  HIS B 177                    
SITE     2 AC2 10 PHE B 178  PHE B 239  HIS B 297  HOH B 608                    
SITE     3 AC2 10 HOH B 792  HOH B 795                                          
SITE     1 AC3 10 ASP C 129  GLU C 153  ALA C 154  PRO C 155                    
SITE     2 AC3 10 VAL C 175  HIS C 207  HIS C 297  HOH C 531                    
SITE     3 AC3 10 HOH C 646  HOH C 677                                          
SITE     1 AC4  8 ASP D 129  GLU D 153  PRO D 155  HIS D 207                    
SITE     2 AC4  8 HIS D 297  HOH D 567  HOH D 664  HOH D 783                    
CRYST1  168.678   84.032   89.278  90.00 100.50  90.00 C 1 2 1      16          
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      0.005928  0.000000  0.001099        0.00000                         
SCALE2      0.000000  0.011900  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011392        0.00000                         
TER    2408      HIS A 320                                                      
TER    4787      HIS B 321                                                      
TER    7195      HIS C 321                                                      
TER    9570      HIS D 320                                                      
MASTER      402    0    4   64   40    0   11    610742    4   32   96          
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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