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LongText Report for: 3KDA-pdb

Name Class
3KDA-pdb
HEADER    HYDROLASE                               22-OCT-09   3KDA              
TITLE     CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF WITH THE          
TITLE    2 H269A MUTATION                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CFTR INHIBITORY FACTOR (CIF);                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA UCBPP-PA14;              
SOURCE   3 ORGANISM_TAXID: 208963;                                              
SOURCE   4 STRAIN: 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: PDMP77                                    
KEYWDS    ALPHA/BETA HYDROLASE, HYDROLASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.D.BAHL,D.R.MADDEN                                                   
REVDAT   1   26-JAN-10 3KDA    0                                                
JRNL        AUTH   C.D.BAHL,C.MORISSEAU,J.M.BOMBERGER,B.A.STANTON,              
JRNL        AUTH 2 B.D.HAMMOCK,G.A.O'TOOLE,D.R.MADDEN                           
JRNL        TITL   CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF          
JRNL        TITL 2 REVEALS NOVEL ACTIVE-SITE FEATURES OF AN EPOXIDE             
JRNL        TITL 3 HYDROLASE VIRULENCE FACTOR                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 30.72                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 192673                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.183                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9636                            
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 30.7281 -  4.6556    0.99     6212   308  0.1707 0.1530        
REMARK   3     2  4.6556 -  3.6973    1.00     6149   334  0.1417 0.1461        
REMARK   3     3  3.6973 -  3.2305    1.00     6156   311  0.1520 0.1580        
REMARK   3     4  3.2305 -  2.9354    1.00     6155   320  0.1720 0.1928        
REMARK   3     5  2.9354 -  2.7252    1.00     6111   335  0.1716 0.1914        
REMARK   3     6  2.7252 -  2.5646    1.00     6132   313  0.1685 0.1704        
REMARK   3     7  2.5646 -  2.4362    1.00     6121   299  0.1675 0.1686        
REMARK   3     8  2.4362 -  2.3302    1.00     6137   292  0.1671 0.1723        
REMARK   3     9  2.3302 -  2.2405    1.00     6117   311  0.1604 0.1657        
REMARK   3    10  2.2405 -  2.1632    1.00     6125   293  0.1602 0.1851        
REMARK   3    11  2.1632 -  2.0956    1.00     6075   323  0.1592 0.1855        
REMARK   3    12  2.0956 -  2.0357    1.00     6080   327  0.1595 0.1766        
REMARK   3    13  2.0357 -  1.9821    1.00     6157   324  0.1610 0.1671        
REMARK   3    14  1.9821 -  1.9338    1.00     6038   324  0.1677 0.1981        
REMARK   3    15  1.9338 -  1.8898    1.00     6071   350  0.1657 0.1845        
REMARK   3    16  1.8898 -  1.8496    1.00     6050   330  0.1661 0.1963        
REMARK   3    17  1.8496 -  1.8126    1.00     6111   333  0.1628 0.1847        
REMARK   3    18  1.8126 -  1.7784    1.00     6059   352  0.1611 0.1832        
REMARK   3    19  1.7784 -  1.7466    1.00     6138   281  0.1650 0.1918        
REMARK   3    20  1.7466 -  1.7170    1.00     6078   335  0.1673 0.1901        
REMARK   3    21  1.7170 -  1.6893    1.00     6077   355  0.1656 0.1860        
REMARK   3    22  1.6893 -  1.6634    1.00     6069   322  0.1722 0.1932        
REMARK   3    23  1.6634 -  1.6389    1.00     6033   355  0.1677 0.1978        
REMARK   3    24  1.6389 -  1.6158    1.00     6115   309  0.1735 0.1971        
REMARK   3    25  1.6158 -  1.5940    1.00     6086   306  0.1750 0.1863        
REMARK   3    26  1.5940 -  1.5733    1.00     6082   344  0.1733 0.1994        
REMARK   3    27  1.5733 -  1.5536    1.00     6065   309  0.1778 0.1952        
REMARK   3    28  1.5536 -  1.5349    1.00     6080   302  0.1877 0.1954        
REMARK   3    29  1.5349 -  1.5170    1.00     6085   331  0.1962 0.2391        
REMARK   3    30  1.5170 -  1.5000    1.00     6073   308  0.1996 0.2192        
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              : 0.40                                          
REMARK   3   B_SOL              : 40.59                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.380           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
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      :  0.005           9866                                  
REMARK   3   ANGLE     :  1.066          13397                                  
REMARK   3   CHIRALITY :  0.076           1376                                  
REMARK   3   PLANARITY :  0.006           1766                                  
REMARK   3   DIHEDRAL  : 17.094           3541                                  
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 25:319)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6798  -5.8001  15.6305              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0173 T22:   0.0368                                     
REMARK   3      T33:   0.0507 T12:   0.0237                                     
REMARK   3      T13:   0.0067 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4822 L22:   0.2073                                     
REMARK   3      L33:   0.1786 L12:  -0.1588                                     
REMARK   3      L13:  -0.0916 L23:   0.1079                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0210 S12:   0.0319 S13:  -0.0406                       
REMARK   3      S21:   0.0103 S22:   0.0091 S23:  -0.0218                       
REMARK   3      S31:   0.0153 S32:  -0.0031 S33:   0.0103                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 25:319)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9844  33.8714  27.0672              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0272 T22:   0.0343                                     
REMARK   3      T33:   0.0768 T12:   0.0065                                     
REMARK   3      T13:  -0.0055 T23:  -0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0891 L22:   0.3528                                     
REMARK   3      L33:   0.3155 L12:   0.0196                                     
REMARK   3      L13:   0.0045 L23:  -0.0625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0151 S12:   0.0022 S13:   0.0157                       
REMARK   3      S21:   0.0321 S22:  -0.0268 S23:  -0.0467                       
REMARK   3      S31:  -0.0367 S32:   0.0203 S33:   0.0128                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID 25:319)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0941   0.6033  27.1173              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0209 T22:   0.0383                                     
REMARK   3      T33:   0.0460 T12:   0.0029                                     
REMARK   3      T13:   0.0145 T23:   0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0971 L22:   0.3368                                     
REMARK   3      L33:   0.3206 L12:   0.0678                                     
REMARK   3      L13:   0.0295 L23:   0.1127                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0031 S12:  -0.0131 S13:   0.0246                       
REMARK   3      S21:   0.0383 S22:  -0.0280 S23:   0.0371                       
REMARK   3      S31:   0.0382 S32:  -0.0215 S33:   0.0223                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN D AND RESID 25:319)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -30.9706  40.2725  15.4238              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0241 T22:   0.0285                                     
REMARK   3      T33:   0.0981 T12:   0.0186                                     
REMARK   3      T13:  -0.0161 T23:  -0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4851 L22:   0.2401                                     
REMARK   3      L33:   0.2540 L12:  -0.4255                                     
REMARK   3      L13:   0.1105 L23:  -0.0599                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0381 S12:  -0.0166 S13:   0.0570                       
REMARK   3      S21:  -0.0120 S22:   0.0270 S23:  -0.0073                       
REMARK   3      S31:  -0.0364 S32:  -0.0212 S33:   0.0130                       
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 3KDA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055847.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-SEP-07                          
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) : 0.9464                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : TOROIDAL 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   : 192680                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.980                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06300                            
REMARK 200   FOR THE DATA SET  : 22.5900                            
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) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.31400                            
REMARK 200   FOR SHELL         : 5.250                              
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: INITIAL MODEL OBTAINED FROM SAD WITH                 
REMARK 200  SELENOMETHIONINE LABELED CIF                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 0.55M CALCIUM              
REMARK 280  CHLORIDE, 0.1M SODIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       83.98000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.82000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       83.98000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.82000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21110 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21160 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 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   323                                                      
REMARK 465     HIS A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     HIS B   323                                                      
REMARK 465     HIS B   324                                                      
REMARK 465     HIS B   325                                                      
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 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    THR A  99      -61.06    -93.70                                   
REMARK 500    ASP A 129     -135.00     59.71                                   
REMARK 500    ALA A 154      148.97    179.21                                   
REMARK 500    ASP A 185       19.14     58.97                                   
REMARK 500    ASP B 129     -131.53     60.88                                   
REMARK 500    ALA B 154      149.37    178.19                                   
REMARK 500    CYS B 303       53.30   -143.48                                   
REMARK 500    ASP C 129     -131.73     60.38                                   
REMARK 500    ALA C 154      150.39    178.16                                   
REMARK 500    CYS C 303       55.09   -140.47                                   
REMARK 500    THR D  99      -66.13    -95.63                                   
REMARK 500    ASP D 129     -135.39     59.03                                   
REMARK 500    ALA D 154      146.50   -176.72                                   
REMARK 500    ASP D 185       18.47     58.01                                   
REMARK 500    CYS D 303       54.85   -142.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KD2   RELATED DB: PDB                                   
REMARK 900 CFTR INHIBITORY FACTOR (CIF)                                         
DBREF  3KDA A   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
DBREF  3KDA B   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
DBREF  3KDA C   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
DBREF  3KDA D   25   319  UNP    Q02P97   Q02P97_PSEAB    25    319             
SEQADV 3KDA ALA A  269  UNP  Q02P97    HIS   269 ENGINEERED                     
SEQADV 3KDA HIS A  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS A  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS A  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS A  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS A  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS A  325  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA ALA B  269  UNP  Q02P97    HIS   269 ENGINEERED                     
SEQADV 3KDA HIS B  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS B  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS B  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS B  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS B  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS B  325  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA ALA C  269  UNP  Q02P97    HIS   269 ENGINEERED                     
SEQADV 3KDA HIS C  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS C  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS C  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS C  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS C  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS C  325  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA ALA D  269  UNP  Q02P97    HIS   269 ENGINEERED                     
SEQADV 3KDA HIS D  320  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS D  321  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS D  322  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS D  323  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS D  324  UNP  Q02P97              EXPRESSION TAG                 
SEQADV 3KDA HIS D  325  UNP  Q02P97              EXPRESSION TAG                 
SEQRES   1 A  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 A  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 A  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 A  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 A  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 A  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 A  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 A  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 A  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 A  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA          
SEQRES  11 A  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 A  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 A  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 A  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 A  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 A  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 A  301  ASN ALA SER PHE GLU TYR 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 ALA GLY GLY          
SEQRES  20 A  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 A  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 A  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 A  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 A  301  HIS HIS                                                      
SEQRES   1 B  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 B  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 B  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 B  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 B  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 B  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 B  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 B  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 B  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 B  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA          
SEQRES  11 B  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 B  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 B  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 B  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 B  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 B  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 B  301  ASN ALA SER PHE GLU TYR 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 ALA GLY GLY          
SEQRES  20 B  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 B  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 B  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 B  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 B  301  HIS HIS                                                      
SEQRES   1 C  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 C  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 C  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 C  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 C  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 C  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 C  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 C  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 C  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 C  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA          
SEQRES  11 C  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 C  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 C  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 C  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 C  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 C  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 C  301  ASN ALA SER PHE GLU TYR 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 ALA GLY GLY          
SEQRES  20 C  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 C  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 C  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 C  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 C  301  HIS HIS                                                      
SEQRES   1 D  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 D  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 D  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 D  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 D  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 D  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 D  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 D  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 D  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 D  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA          
SEQRES  11 D  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 D  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 D  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 D  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 D  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 D  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 D  301  ASN ALA SER PHE GLU TYR 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 ALA 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   *1111(H2 O)                                                   
HELIX    1   1 THR A   66  HIS A   71  5                                   6    
HELIX    2   2 GLN A   72  ALA A   78  1                                   7    
HELIX    3   3 SER A  102  SER A  118  1                                  17    
HELIX    4   4 ASP A  129  ASN A  134  1                                   6    
HELIX    5   5 THR A  135  ASN A  142  1                                   8    
HELIX    6   6 ASP A  158  PHE A  164  5                                   7    
HELIX    7   7 TRP A  176  ALA A  183  1                                   8    
HELIX    8   8 ARG A  186  ALA A  193  1                                   8    
HELIX    9   9 LYS A  195  HIS A  207  1                                  13    
HELIX   10  10 ASN A  210  PHE A  214  5                                   5    
HELIX   11  11 SER A  215  ALA A  227  1                                  13    
HELIX   12  12 LYS A  228  ALA A  241  1                                  14    
HELIX   13  13 ALA A  241  ALA A  253  1                                  13    
HELIX   14  14 THR A  274  ALA A  284  1                                  11    
HELIX   15  15 TRP A  298  CYS A  303  1                                   6    
HELIX   16  16 CYS A  303  SER A  316  1                                  14    
HELIX   17  17 THR B   66  HIS B   71  5                                   6    
HELIX   18  18 GLN B   72  ALA B   78  1                                   7    
HELIX   19  19 SER B  102  SER B  118  1                                  17    
HELIX   20  20 ASP B  129  ASN B  134  1                                   6    
HELIX   21  21 THR B  135  ASN B  142  1                                   8    
HELIX   22  22 ASP B  158  PHE B  164  5                                   7    
HELIX   23  23 TRP B  176  ALA B  183  1                                   8    
HELIX   24  24 ARG B  186  ALA B  193  1                                   8    
HELIX   25  25 LYS B  195  HIS B  207  1                                  13    
HELIX   26  26 ASN B  210  PHE B  214  5                                   5    
HELIX   27  27 SER B  215  ALA B  227  1                                  13    
HELIX   28  28 LYS B  228  ALA B  241  1                                  14    
HELIX   29  29 ALA B  241  ALA B  253  1                                  13    
HELIX   30  30 THR B  274  ALA B  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 LEU C   73  ALA C   78  1                                   6    
HELIX   35  35 SER C  102  SER C  118  1                                  17    
HELIX   36  36 ASP C  129  ASN C  134  1                                   6    
HELIX   37  37 THR C  135  ASN C  142  1                                   8    
HELIX   38  38 ASP C  158  PHE C  164  5                                   7    
HELIX   39  39 TRP C  176  ALA C  183  1                                   8    
HELIX   40  40 ARG C  186  ALA C  193  1                                   8    
HELIX   41  41 LYS C  195  HIS C  207  1                                  13    
HELIX   42  42 ASN C  210  PHE C  214  5                                   5    
HELIX   43  43 SER C  215  ALA C  227  1                                  13    
HELIX   44  44 LYS C  228  ALA C  241  1                                  14    
HELIX   45  45 ALA C  241  ALA C  253  1                                  13    
HELIX   46  46 THR C  274  ALA C  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 SER D  215  LYS D  228  1                                  14    
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  284  1                                  11    
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 PHE A  34  VAL A  41  0                                        
SHEET    2   A 8 VAL A  44  GLY A  52 -1  O  LEU A  46   N  ARG A  39           
SHEET    3   A 8 THR A  82  PRO A  86 -1  O  VAL A  83   N  GLY A  51           
SHEET    4   A 8 LEU A  56  VAL A  60  1  N  VAL A  57   O  THR A  82           
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  LEU A 149           
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  TYR B  48   N  ALA B  37           
SHEET    3   C 8 THR B  82  PRO B  86 -1  O  VAL B  83   N  GLY B  51           
SHEET    4   C 8 LEU B  56  VAL B  60  1  N  VAL B  57   O  THR B  82           
SHEET    5   C 8 PHE B 123  HIS B 128  1  O  ASP B 124   N  LEU B  56           
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  TYR B 151           
SHEET    8   C 8 VAL B 287  LEU B 292  1  O  LEU B 292   N  ALA B 265           
SHEET    1   D 2 PHE B 167  THR B 168  0                                        
SHEET    2   D 2 GLY B 171  GLU B 172 -1  O  GLY B 171   N  THR B 168           
SHEET    1   E 8 GLU C  35  VAL C  41  0                                        
SHEET    2   E 8 VAL C  44  GLY C  52 -1  O  LYS C  50   N  GLU C  35           
SHEET    3   E 8 THR C  82  PRO C  86 -1  O  VAL C  83   N  GLY C  51           
SHEET    4   E 8 LEU C  56  VAL C  60  1  N  VAL C  57   O  THR C  82           
SHEET    5   E 8 PHE C 123  HIS C 128  1  O  ASP C 124   N  LEU C  56           
SHEET    6   E 8 ILE C 146  MET C 152  1  O  VAL C 150   N  LEU C 125           
SHEET    7   E 8 THR C 261  GLY C 266  1  O  MET C 262   N  TYR C 151           
SHEET    8   E 8 VAL C 287  LEU C 292  1  O  LEU C 292   N  ALA C 265           
SHEET    1   F 2 PHE C 167  THR C 168  0                                        
SHEET    2   F 2 GLY C 171  GLU C 172 -1  O  GLY C 171   N  THR C 168           
SHEET    1   G 8 PHE D  34  VAL D  41  0                                        
SHEET    2   G 8 VAL D  44  GLY D  52 -1  O  LEU D  46   N  ARG D  39           
SHEET    3   G 8 THR D  82  PRO D  86 -1  O  VAL D  83   N  GLY D  51           
SHEET    4   G 8 LEU D  56  VAL D  60  1  N  VAL D  57   O  THR D  82           
SHEET    5   G 8 PHE D 123  HIS D 128  1  O  ASP D 124   N  LEU D  56           
SHEET    6   G 8 ILE D 146  MET D 152  1  O  VAL D 150   N  LEU D 125           
SHEET    7   G 8 THR D 261  GLY D 266  1  O  MET D 262   N  LEU D 149           
SHEET    8   G 8 VAL D 287  LEU D 292  1  O  LEU D 292   N  ALA D 265           
SHEET    1   H 2 PHE D 167  THR D 168  0                                        
SHEET    2   H 2 GLY D 171  GLU D 172 -1  O  GLY D 171   N  THR D 168           
SSBOND   1 CYS A  295    CYS A  303                          1555   1555  2.02  
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  1.99  
CRYST1  167.960   83.640   88.930  90.00 100.49  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      0.005954  0.000000  0.001102        0.00000                         
SCALE2      0.000000  0.011956  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011436        0.00000                         
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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