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LongText Report for: 3PI6-pdb

Name Class
3PI6-pdb
HEADER    HYDROLASE                               05-NOV-10   3PI6              
TITLE     CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF WITH THE H177Y    
TITLE    2 MUTATION                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYDROLASE;                                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: CFTR INHIBITORY FACTOR CIF;                                 
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: CIF, 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                               
KEYWDS    ALPHA/BETA HYDROLASE, EPOXIDE HYDROLASE, SECRETED, HYDROLASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.D.BAHL,D.R.MADDEN                                                   
REVDAT   1   21-SEP-11 3PI6    0                                                
JRNL        AUTH   C.D.BAHL,D.R.MADDEN                                          
JRNL        TITL   PSEUDOMONAS AERUGINOSA CIF DEFINES A DISTINCT CLASS OF       
JRNL        TITL 2 ALPHA/BETA EPOXIDE HYDROLASES UTILIZING A HIS/TYR            
JRNL        TITL 3 RING-OPENING PAIR.                                           
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: 1.6.4_486)                    
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) : 43.93                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 195114                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.181                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9754                            
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 43.9490 -  3.2313    1.00    18808   975  0.1544 0.1527        
REMARK   3     2  3.2313 -  2.5649    1.00    18665   976  0.1633 0.1865        
REMARK   3     3  2.5649 -  2.2407    1.00    18528   975  0.1596 0.1780        
REMARK   3     4  2.2407 -  2.0358    1.00    18615   976  0.1622 0.1811        
REMARK   3     5  2.0358 -  1.8899    1.00    18508   975  0.1586 0.1830        
REMARK   3     6  1.8899 -  1.7785    1.00    18487   976  0.1544 0.1802        
REMARK   3     7  1.7785 -  1.6894    1.00    18536   975  0.1665 0.1959        
REMARK   3     8  1.6894 -  1.6158    1.00    18475   976  0.1764 0.2022        
REMARK   3     9  1.6158 -  1.5536    1.00    18502   975  0.1932 0.2314        
REMARK   3    10  1.5536 -  1.5000    0.99    18236   975  0.2259 0.2517        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.37                                          
REMARK   3   B_SOL              : 36.56                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.090           
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) : -1.24580                                             
REMARK   3    B22 (A**2) : -0.90270                                             
REMARK   3    B33 (A**2) : 2.14850                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.01460                                              
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           9952                                  
REMARK   3   ANGLE     :  1.082          13540                                  
REMARK   3   CHIRALITY :  0.078           1393                                  
REMARK   3   PLANARITY :  0.006           1779                                  
REMARK   3   DIHEDRAL  : 12.591           3658                                  
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): -21.9650  12.0372  27.2588              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0432 T22:   0.0440                                     
REMARK   3      T33:   0.0257 T12:  -0.0007                                     
REMARK   3      T13:   0.0095 T23:   0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3853 L22:   0.3700                                     
REMARK   3      L33:   0.3588 L12:   0.0002                                     
REMARK   3      L13:   0.0545 L23:   0.0760                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0022 S12:  -0.0567 S13:  -0.0398                       
REMARK   3      S21:   0.0420 S22:  -0.0128 S23:   0.0376                       
REMARK   3      S31:   0.0601 S32:  -0.0269 S33:   0.0083                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (chain B and resid 25:320)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -31.0061  51.4620  15.7505              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0437 T22:   0.0375                                     
REMARK   3      T33:   0.0711 T12:   0.0115                                     
REMARK   3      T13:  -0.0172 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6816 L22:   0.5161                                     
REMARK   3      L33:   0.3118 L12:  -0.2805                                     
REMARK   3      L13:  -0.0402 L23:  -0.0866                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0090 S12:   0.0052 S13:   0.1013                       
REMARK   3      S21:  -0.0338 S22:   0.0102 S23:   0.0160                       
REMARK   3      S31:  -0.0496 S32:  -0.0065 S33:   0.0019                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (chain C and resid 25:320)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   5.7940  44.7757  27.0021              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0445 T22:   0.0401                                     
REMARK   3      T33:   0.0533 T12:   0.0026                                     
REMARK   3      T13:  -0.0015 T23:  -0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3278 L22:   0.4273                                     
REMARK   3      L33:   0.4279 L12:   0.0014                                     
REMARK   3      L13:   0.0731 L23:   0.0242                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0044 S12:  -0.0181 S13:   0.0616                       
REMARK   3      S21:   0.0314 S22:  -0.0084 S23:  -0.0526                       
REMARK   3      S31:  -0.0527 S32:   0.0221 S33:   0.0111                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (chain D and resid 25:322)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  14.7918   5.0892  15.6684              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0397 T22:   0.0464                                     
REMARK   3      T33:   0.0287 T12:   0.0167                                     
REMARK   3      T13:   0.0054 T23:  -0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5995 L22:   0.5057                                     
REMARK   3      L33:   0.2455 L12:  -0.1386                                     
REMARK   3      L13:   0.0209 L23:   0.1068                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0113 S12:   0.0085 S13:  -0.0334                       
REMARK   3      S21:  -0.0140 S22:   0.0076 S23:  -0.0704                       
REMARK   3      S31:   0.0263 S32:   0.0058 S33:  -0.0150                       
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 3PI6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062400.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-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                         : OXFORD DANFYSIK TOROIDAL           
REMARK 200                                   FOCUSING MIRROR.                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 195124                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.150                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05100                            
REMARK 200   FOR THE DATA SET  : 25.7000                            
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) : 1.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.34100                            
REMARK 200   FOR SHELL         : 5.900                              
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: PDB ENTRY 3KD2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 8000, 0.125M CALCIUM CHLORIDE,   
REMARK 280  0.1M SODIUM ACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  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       84.19700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.02800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       84.19700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       42.02800            
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: 2760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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: 2740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 809  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     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   321                                                      
REMARK 465     HIS C   322                                                      
REMARK 465     HIS C   323                                                      
REMARK 465     HIS C   324                                                      
REMARK 465     HIS C   325                                                      
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     -130.59     61.23                                   
REMARK 500    ALA A 154      150.45    176.31                                   
REMARK 500    CYS A 303       55.25   -141.46                                   
REMARK 500    THR B  99      -69.97    -92.78                                   
REMARK 500    ASP B 129     -133.89     58.76                                   
REMARK 500    ALA B 154      149.35   -179.26                                   
REMARK 500    CYS B 303       54.65   -142.94                                   
REMARK 500    ASP C 129     -130.57     59.92                                   
REMARK 500    ALA C 154      150.76    177.20                                   
REMARK 500    CYS C 303       55.76   -142.20                                   
REMARK 500    THR D  99      -67.65    -91.36                                   
REMARK 500    ASP D 129     -134.88     57.42                                   
REMARK 500    ALA D 154      147.46   -177.03                                   
REMARK 500    CYS D 303       54.25   -143.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KD2   RELATED DB: PDB                                   
REMARK 900 THE WT VERSION OF THIS PROTEIN.                                      
REMARK 900 RELATED ID: 3KDA   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH THE H269A MUTATION.                            
DBREF  3PI6 A   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
DBREF  3PI6 B   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
DBREF  3PI6 C   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
DBREF  3PI6 D   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
SEQADV 3PI6 TYR A  177  UNP  Q02P97    HIS   177 ENGINEERED MUTATION            
SEQADV 3PI6 HIS A  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS A  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS A  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS A  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS A  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS A  325  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 TYR B  177  UNP  Q02P97    HIS   177 ENGINEERED MUTATION            
SEQADV 3PI6 HIS B  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS B  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS B  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS B  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS B  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS B  325  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 TYR C  177  UNP  Q02P97    HIS   177 ENGINEERED MUTATION            
SEQADV 3PI6 HIS C  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS C  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS C  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS C  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS C  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS C  325  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 TYR D  177  UNP  Q02P97    HIS   177 ENGINEERED MUTATION            
SEQADV 3PI6 HIS D  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS D  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS D  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS D  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 HIS D  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3PI6 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 TYR 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 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 TYR 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 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 TYR 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 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 TYR 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                                                      
FORMUL   5  HOH   *1244(H2 O)                                                   
HELIX    1   1 THR A   66  HIS A   71  5                                   6    
HELIX    2   2 LEU A   73  ALA A   78  1                                   6    
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  282  1                                   9    
HELIX   31  31 TRP B  298  CYS B  303  1                                   6    
HELIX   32  32 CYS B  303  SER B  316  1                                  14    
HELIX   33  33 THR C   66  HIS C   71  5                                   6    
HELIX   34  34 GLN C   72  ALA C   78  1                                   7    
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 VAL C  175  ALA C  183  1                                   9    
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  282  1                                   9    
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  ALA D  227  1                                  13    
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  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  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 PHE B  34  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  LEU B  59   O  ILE B  84           
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  LEU C  46   N  ARG C  39           
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  VAL C 126   N  VAL C  60           
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  VAL D 126   N  VAL D  60           
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  2.00  
CRYST1  168.394   84.056   89.325  90.00 100.39  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      0.005938  0.000000  0.001089        0.00000                         
SCALE2      0.000000  0.011897  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011382        0.00000                         
TER    2425      HIS A 321                                                      
TER    4818      HIS B 320                                                      
TER    7227      HIS C 320                                                      
TER    9632      HIS D 322                                                      
MASTER      356    0    0   64   40    0    0    610734    4    8   96          
END                                                                             

Send your questions or comments to :
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:
ESTHER Home Page and ACEDB Home Page
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