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LongText Report for: 4DNO-pdb

Name Class
4DNO-pdb
HEADER    HYDROLASE                               08-FEB-12   4DNO              
TITLE     CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF WITH THE E153Q    
TITLE    2 MUTATION ADDUCTED WITH THE 1,2-EPOXYHEXANE HYDROLYSIS INTERMEDIATE   
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 COVALENTLY ADDUCTED WITH THE  
KEYWDS   2 1,2-EPOXYHEXANE HYDROLYSIS INTERMEDIATE, SECRETED, HYDROLASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.D.BAHL,Y.R.PATANKAR,D.R.MADDEN                                      
REVDAT   1   07-AUG-13 4DNO    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.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.01                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 88434                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4411                            
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 46.0207 -  6.0547    0.99     2819   221  0.2335 0.2648        
REMARK   3     2  6.0547 -  4.8074    1.00     3001     0  0.1631 10000000.0000 
REMARK   3     3  4.8074 -  4.2002    1.00     2746   220  0.1375 0.1743        
REMARK   3     4  4.2002 -  3.8164    1.00     2730   221  0.1506 0.1893        
REMARK   3     5  3.8164 -  3.5429    1.00     3001     0  0.1666 10000000.0000 
REMARK   3     6  3.5429 -  3.3341    1.00     2727   221  0.1730 0.2145        
REMARK   3     7  3.3341 -  3.1672    1.00     2744   221  0.1750 0.2087        
REMARK   3     8  3.1672 -  3.0293    1.00     2920     0  0.1779 10000000.0000 
REMARK   3     9  3.0293 -  2.9127    1.00     2757   221  0.1803 0.2303        
REMARK   3    10  2.9127 -  2.8122    1.00     2728   221  0.1745 0.2425        
REMARK   3    11  2.8122 -  2.7243    1.00     2946     0  0.1708 10000000.0000 
REMARK   3    12  2.7243 -  2.6465    1.00     2742   221  0.1682 0.2215        
REMARK   3    13  2.6465 -  2.5768    1.00     2717   221  0.1735 0.2624        
REMARK   3    14  2.5768 -  2.5139    1.00     2961     0  0.1716 10000000.0000 
REMARK   3    15  2.5139 -  2.4568    1.00     2710   221  0.1730 0.2225        
REMARK   3    16  2.4568 -  2.4045    1.00     2686   221  0.1707 0.2344        
REMARK   3    17  2.4045 -  2.3564    1.00     2972     0  0.1741 10000000.0000 
REMARK   3    18  2.3564 -  2.3119    1.00     2733   221  0.1605 0.2218        
REMARK   3    19  2.3119 -  2.2707    1.00     2720   221  0.1704 0.2583        
REMARK   3    20  2.2707 -  2.2322    1.00     2898     0  0.1716 10000000.0000 
REMARK   3    21  2.2322 -  2.1962    1.00     2744   221  0.1608 0.2081        
REMARK   3    22  2.1962 -  2.1624    1.00     2754   220  0.1626 0.2146        
REMARK   3    23  2.1624 -  2.1306    1.00     2886     0  0.1672 10000000.0000 
REMARK   3    24  2.1306 -  2.1006    1.00     2748   221  0.1734 0.2365        
REMARK   3    25  2.1006 -  2.0722    1.00     2706   219  0.1837 0.2441        
REMARK   3    26  2.0722 -  2.0453    1.00     2907     0  0.1935 10000000.0000 
REMARK   3    27  2.0453 -  2.0197    1.00     2763   220  0.1893 0.2762        
REMARK   3    28  2.0197 -  1.9954    1.00     2678   221  0.2015 0.2664        
REMARK   3    29  1.9954 -  1.9722    0.99     2919     0  0.2099 10000000.0000 
REMARK   3    30  1.9722 -  1.9500    0.98     2660   217  0.2171 0.3001        
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              : 0.39                                          
REMARK   3   B_SOL              : 47.37                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.240           
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) : -5.92250                                             
REMARK   3    B22 (A**2) : -2.92370                                             
REMARK   3    B33 (A**2) : 8.84620                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.20550                                              
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           9819                                  
REMARK   3   ANGLE     :  1.006          13314                                  
REMARK   3   CHIRALITY :  0.073           1364                                  
REMARK   3   PLANARITY :  0.005           1752                                  
REMARK   3   DIHEDRAL  : 14.148           3568                                  
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 25:321)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0382  12.4459 -27.3134              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0562 T22:   0.0577                                     
REMARK   3      T33:   0.0563 T12:  -0.0036                                     
REMARK   3      T13:   0.0004 T23:  -0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2441 L22:   0.2767                                     
REMARK   3      L33:   0.2581 L12:   0.0265                                     
REMARK   3      L13:   0.0491 L23:  -0.0047                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0002 S12:   0.0132 S13:  -0.0502                       
REMARK   3      S21:   0.0048 S22:  -0.0084 S23:  -0.0526                       
REMARK   3      S31:   0.0519 S32:   0.0056 S33:   0.0048                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (chain B and resid 25:317)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  30.8479  51.4147 -15.6035              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0605 T22:   0.0564                                     
REMARK   3      T33:   0.1136 T12:  -0.0257                                     
REMARK   3      T13:  -0.0145 T23:  -0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0829 L22:   0.0589                                     
REMARK   3      L33:   0.0479 L12:   0.0239                                     
REMARK   3      L13:   0.0139 L23:   0.0138                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0320 S12:  -0.0133 S13:   0.0848                       
REMARK   3      S21:   0.0205 S22:   0.0350 S23:  -0.0546                       
REMARK   3      S31:  -0.0380 S32:   0.0009 S33:   0.0110                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (chain C and resid 25:321)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.7191  44.5884 -27.2337              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0657 T22:   0.0666                                     
REMARK   3      T33:   0.1018 T12:  -0.0017                                     
REMARK   3      T13:   0.0110 T23:  -0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1594 L22:   0.1460                                     
REMARK   3      L33:   0.2432 L12:   0.0370                                     
REMARK   3      L13:  -0.0402 L23:   0.0284                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0227 S12:  -0.0118 S13:   0.1009                       
REMARK   3      S21:   0.0005 S22:  -0.0262 S23:   0.0522                       
REMARK   3      S31:  -0.0558 S32:  -0.0162 S33:   0.0012                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (chain D and resid 25:318)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -14.5599   5.5379 -15.7611              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0705 T22:   0.0689                                     
REMARK   3      T33:   0.0625 T12:  -0.0252                                     
REMARK   3      T13:   0.0101 T23:   0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1937 L22:   0.2458                                     
REMARK   3      L33:   0.1609 L12:   0.0754                                     
REMARK   3      L13:  -0.0278 L23:  -0.0785                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0108 S12:  -0.0257 S13:  -0.0022                       
REMARK   3      S21:   0.0225 S22:   0.0098 S23:   0.0725                       
REMARK   3      S31:   0.0279 S32:   0.0232 S33:  -0.0037                       
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 4DNO 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 RCSB070555.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-11                          
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) : 1.2006                             
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   : 88446                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.010                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09900                            
REMARK 200   FOR THE DATA SET  : 11.6800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.39400                            
REMARK 200   FOR SHELL         : 3.530                              
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   (%): 45.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 8000, 0.125M CALCIUM CHLORIDE,   
REMARK 280  0.1M SODIUM ACETATE, 0.01M 1,2-EPOXYHEXANE, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, 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       84.04000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.83150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       84.04000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.83150            
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: 3520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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: 3500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 D 637  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 617  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 734  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 700  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 704  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   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     HIS A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     GLY B   318                                                      
REMARK 465     ARG B   319                                                      
REMARK 465     HIS B   320                                                      
REMARK 465     HIS B   321                                                      
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     ARG D   319                                                      
REMARK 465     HIS D   320                                                      
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 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     -128.85     60.06                                   
REMARK 500    ALA A 154      147.83    175.84                                   
REMARK 500    CYS A 303       54.24   -142.77                                   
REMARK 500    THR B  99      -63.61    -91.20                                   
REMARK 500    ASP B 129     -131.00     60.19                                   
REMARK 500    ALA B 154      146.14    171.99                                   
REMARK 500    CYS B 303       54.64   -143.58                                   
REMARK 500    THR C  99      -70.72    -80.38                                   
REMARK 500    ASP C 129     -127.25     58.48                                   
REMARK 500    ALA C 154      148.64    176.18                                   
REMARK 500    THR D  99      -61.41    -92.05                                   
REMARK 500    ASP D 129     -128.03     62.16                                   
REMARK 500    ALA D 154      145.62    171.51                                   
REMARK 500    CYS D 303       50.04   -141.56                                   
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 HE2 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HE2 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HE2 C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HE2 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                                   
DBREF  4DNO A   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
DBREF  4DNO B   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
DBREF  4DNO C   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
DBREF  4DNO D   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
SEQADV 4DNO GLN A  153  UNP  Q02P97    GLU   153 ENGINEERED MUTATION            
SEQADV 4DNO HIS A  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS A  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS A  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS A  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS A  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS A  325  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO GLN B  153  UNP  Q02P97    GLU   153 ENGINEERED MUTATION            
SEQADV 4DNO HIS B  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS B  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS B  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS B  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS B  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS B  325  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO GLN C  153  UNP  Q02P97    GLU   153 ENGINEERED MUTATION            
SEQADV 4DNO HIS C  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS C  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS C  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS C  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS C  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS C  325  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO GLN D  153  UNP  Q02P97    GLU   153 ENGINEERED MUTATION            
SEQADV 4DNO HIS D  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS D  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS D  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS D  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO HIS D  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 4DNO 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 GLN 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 TYR 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 GLN 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 TYR 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 GLN 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 TYR 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 GLN 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 TYR 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    HE2  A 401       7                                                       
HET    HE2  B 401       7                                                       
HET    HE2  C 401       7                                                       
HET    HE2  D 401       7                                                       
HETNAM     HE2 HEXAN-1-OL                                                       
FORMUL   5  HE2    4(C6 H14 O)                                                  
FORMUL   9  HOH   *995(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  LYS A  281  1                                   8    
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 SER B  215  LYS B  228  1                                  14    
HELIX   27  27 LYS B  228  ALA B  241  1                                  14    
HELIX   28  28 ALA B  241  ALA B  253  1                                  13    
HELIX   29  29 THR B  274  ALA B  284  1                                  11    
HELIX   30  30 TRP B  298  CYS B  303  1                                   6    
HELIX   31  31 CYS B  303  SER B  316  1                                  14    
HELIX   32  32 THR C   66  HIS C   71  5                                   6    
HELIX   33  33 LEU C   73  ALA C   78  1                                   6    
HELIX   34  34 SER C  102  SER C  118  1                                  17    
HELIX   35  35 ASP C  129  ASN C  134  1                                   6    
HELIX   36  36 THR C  135  ASN C  142  1                                   8    
HELIX   37  37 ASP C  158  PHE C  164  5                                   7    
HELIX   38  38 TRP C  176  ALA C  183  1                                   8    
HELIX   39  39 ARG C  186  ALA C  193  1                                   8    
HELIX   40  40 LYS C  195  HIS C  207  1                                  13    
HELIX   41  41 ASN C  210  PHE C  214  5                                   5    
HELIX   42  42 SER C  215  ALA C  227  1                                  13    
HELIX   43  43 LYS C  228  ALA C  241  1                                  14    
HELIX   44  44 ALA C  241  ALA C  253  1                                  13    
HELIX   45  45 THR C  274  LYS C  281  1                                   8    
HELIX   46  46 TRP C  298  CYS C  303  1                                   6    
HELIX   47  47 CYS C  303  SER C  316  1                                  14    
HELIX   48  48 THR D   66  HIS D   71  5                                   6    
HELIX   49  49 GLN D   72  ALA D   78  1                                   7    
HELIX   50  50 SER D  102  SER D  118  1                                  17    
HELIX   51  51 ASP D  129  ASN D  134  1                                   6    
HELIX   52  52 THR D  135  ASN D  142  1                                   8    
HELIX   53  53 ASP D  158  PHE D  164  5                                   7    
HELIX   54  54 TRP D  176  ALA D  183  1                                   8    
HELIX   55  55 ARG D  186  ALA D  193  1                                   8    
HELIX   56  56 LYS D  195  HIS D  207  1                                  13    
HELIX   57  57 ASN D  210  PHE D  214  5                                   5    
HELIX   58  58 SER D  215  ALA D  227  1                                  13    
HELIX   59  59 LYS D  228  ALA D  241  1                                  14    
HELIX   60  60 ALA D  241  ALA D  253  1                                  13    
HELIX   61  61 THR D  274  ALA D  282  1                                   9    
HELIX   62  62 TRP D  298  CYS D  303  1                                   6    
HELIX   63  63 CYS D  303  ARG D  317  1                                  15    
SHEET    1   A 8 GLU A  35  VAL A  41  0                                        
SHEET    2   A 8 VAL A  44  GLY A  52 -1  O  VAL A  44   N  VAL A  41           
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  VAL A  57   O  ILE A  84           
SHEET    5   A 8 PHE A 123  HIS A 128  1  O  VAL A 126   N  VAL A  60           
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 8 GLU B  35  VAL B  41  0                                        
SHEET    2   B 8 VAL B  44  GLY B  52 -1  O  VAL B  44   N  VAL B  41           
SHEET    3   B 8 THR B  82  PRO B  86 -1  O  VAL B  83   N  GLY B  51           
SHEET    4   B 8 LEU B  56  VAL B  60  1  N  VAL B  57   O  ILE B  84           
SHEET    5   B 8 PHE B 123  HIS B 128  1  O  VAL B 126   N  VAL B  60           
SHEET    6   B 8 ILE B 146  MET B 152  1  O  VAL B 150   N  LEU B 125           
SHEET    7   B 8 THR B 261  GLY B 266  1  O  MET B 262   N  LEU B 149           
SHEET    8   B 8 VAL B 287  LEU B 292  1  O  LEU B 292   N  ALA B 265           
SHEET    1   C 2 PHE B 167  THR B 168  0                                        
SHEET    2   C 2 GLY B 171  GLU B 172 -1  O  GLY B 171   N  THR B 168           
SHEET    1   D 8 GLU C  35  VAL C  41  0                                        
SHEET    2   D 8 VAL C  44  GLY C  52 -1  O  LEU C  46   N  ARG C  39           
SHEET    3   D 8 THR C  82  PRO C  86 -1  O  VAL C  83   N  GLY C  51           
SHEET    4   D 8 LEU C  56  VAL C  60  1  N  VAL C  57   O  ILE C  84           
SHEET    5   D 8 PHE C 123  HIS C 128  1  O  VAL C 126   N  VAL C  60           
SHEET    6   D 8 ILE C 146  MET C 152  1  O  VAL C 150   N  LEU C 125           
SHEET    7   D 8 THR C 261  GLY C 266  1  O  MET C 262   N  TYR C 151           
SHEET    8   D 8 VAL C 287  LEU C 292  1  O  LEU C 292   N  ALA C 265           
SHEET    1   E 8 GLU D  35  VAL D  41  0                                        
SHEET    2   E 8 VAL D  44  GLY D  52 -1  O  LEU D  46   N  ARG D  39           
SHEET    3   E 8 THR D  82  PRO D  86 -1  O  VAL D  83   N  GLY D  51           
SHEET    4   E 8 LEU D  56  VAL D  60  1  N  LEU D  59   O  ILE D  84           
SHEET    5   E 8 PHE D 123  HIS D 128  1  O  VAL D 126   N  VAL D  60           
SHEET    6   E 8 ILE D 146  MET D 152  1  O  VAL D 150   N  ALA D 127           
SHEET    7   E 8 THR D 261  GLY D 266  1  O  MET D 262   N  LEU D 149           
SHEET    8   E 8 VAL D 287  LEU D 292  1  O  LEU D 292   N  ALA D 265           
SHEET    1   F 2 PHE D 167  THR D 168  0                                        
SHEET    2   F 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  2.02  
SSBOND   2 CYS B  295    CYS B  303                          1555   1555  2.01  
SSBOND   3 CYS C  295    CYS C  303                          1555   1555  2.02  
SSBOND   4 CYS D  295    CYS D  303                          1555   1555  2.00  
LINK         OD2 ASP A 129                 CAF HE2 A 401     1555   1555  1.41  
LINK         OD2 ASP B 129                 CAF HE2 B 401     1555   1555  1.41  
LINK         OD2 ASP C 129                 CAF HE2 C 401     1555   1555  1.41  
LINK         OD2 ASP D 129                 CAF HE2 D 401     1555   1555  1.42  
SITE     1 AC1  6 ASP A 129  HIS A 177  PHE A 178  HIS A 207                    
SITE     2 AC1  6 TYR A 239  HIS A 297                                          
SITE     1 AC2  7 ASP B 129  LEU B 174  HIS B 177  PHE B 178                    
SITE     2 AC2  7 HIS B 207  TYR B 239  HIS B 297                               
SITE     1 AC3  7 ASP C 129  HIS C 177  PHE C 178  HIS C 207                    
SITE     2 AC3  7 TYR C 239  GLY C 270  HIS C 297                               
SITE     1 AC4  5 ASP D 129  HIS D 177  PHE D 178  TYR D 239                    
SITE     2 AC4  5 HIS D 297                                                     
CRYST1  168.080   83.663   89.248  90.00 100.52  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      0.005950  0.000000  0.001105        0.00000                         
SCALE2      0.000000  0.011953  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011396        0.00000                         
TER    2407      HIS A 321                                                      
TER    4750      ARG B 317                                                      
TER    7157      HIS C 321                                                      
TER    9500      GLY D 318                                                      
MASTER      397    0    4   63   36    0    8    610449    4   40   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.
For technical information about these pages see:
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