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LongText Report for: 2QXU-pdb

Name Class
2QXU-pdb
HEADER    HYDROLASE                               13-AUG-07   2QXU              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS SUBTILIS LIPASE            
TITLE    2 CRYSTALLIZED AT PH 5.0                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE;                                                    
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: TRIACYLGLYCEROL LIPASE;                                     
COMPND   5 EC: 3.1.1.3;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 GENE: LIPA;                                                          
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET-21B                                   
KEYWDS    ALPHA/BETA HYDROLASE FOLD, LIPID DEGRADATION, SECRETED                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.RAJAKUMARA,R.SANKARANARAYANAN                                       
REVDAT   1   18-DEC-07 2QXU    0                                                
JRNL        AUTH   E.RAJAKUMARA,P.ACHARYA,S.AHMAD,R.SANKARANARYANAN,            
JRNL        AUTH 2 N.M.RAO                                                      
JRNL        TITL   STRUCTURAL BASIS FOR THE REMARKABLE STABILITY OF             
JRNL        TITL 2 BACILLUS SUBTILIS LIPASE (LIP A) AT LOW PH                   
JRNL        REF    BIOCHIM.BIOPHYS.ACTA                       2007              
JRNL        REFN   ASTM BBACAQ  NE ISSN 0006-3002                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.90 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 238428.730                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 96547                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4872                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.97                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9342                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300                       
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 488                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.013                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10808                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 840                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.88000                                              
REMARK   3    B22 (A**2) : -2.47000                                             
REMARK   3    B33 (A**2) : 1.59000                                              
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.08                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.27                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.15                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.67                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.180 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.620 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.060 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.870 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 39.85                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2QXU COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.                               
REMARK 100 THE RCSB ID CODE IS RCSB044180.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-OCT-2003                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC MIRROR SYSTEM                
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 96606                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09500                            
REMARK 200   FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.23000                            
REMARK 200   FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1I6W                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 6000, 100MM SODIUM ACETATE       
REMARK 280  PH 5.0, 15MM AMMONIUM SULFATE, VAPOR DIFFUSION, TEMPERATURE         
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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   1/2-X,1/2+Y,-Z                                          
REMARK 290       4555   1/2+X,1/2-Y,-Z                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   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      109.30400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.46700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      109.30400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.46700            
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, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13               
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: MONOMER                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
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: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
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: 8                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H                                     
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: 9                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER                      
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 AVERAGE BURIED SURFACE AREA: 960 ANGSTROM**2                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000     -109.30400            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      -55.46700            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       51.98800            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 10                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER                      
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 AVERAGE BURIED SURFACE AREA: 1080 ANGSTROM**2                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000     -109.30400            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       55.46700            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       51.98800            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 11                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER                      
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 AVERAGE BURIED SURFACE AREA: 960 ANGSTROM**2                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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 APPLY THE FOLLOWING TO CHAINS: F                                     
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      327.91200            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -55.46700            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      103.97600            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 12                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER                      
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 AVERAGE BURIED SURFACE AREA: 1060 ANGSTROM**2                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
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   BIOMT1   2 -1.000000  0.000000  0.000000      437.21600            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      110.93400            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 13                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER                      
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 AVERAGE BURIED SURFACE AREA: 1110 ANGSTROM**2                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H                                     
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   BIOMT1   2 -1.000000  0.000000  0.000000      437.21600            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      221.86800            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
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    SER A  77     -121.91     48.40                                   
REMARK 500    LEU A  90     -145.03   -110.03                                   
REMARK 500    ALA A 105       47.80    -90.44                                   
REMARK 500    ARG A 107        1.96    -68.52                                   
REMARK 500    THR A 109      -51.20   -120.92                                   
REMARK 500    GLN A 121      108.59   -169.71                                   
REMARK 500    ASN A 179       99.87   -161.51                                   
REMARK 500    SER B  77     -123.43     49.85                                   
REMARK 500    LEU B  90     -141.94   -109.02                                   
REMARK 500    ALA B  97      -67.03   -108.80                                   
REMARK 500    ALA B 105       52.38    -91.45                                   
REMARK 500    GLN B 121      116.70   -166.44                                   
REMARK 500    TYR B 161       50.69   -140.39                                   
REMARK 500    SER C  77     -118.24     49.57                                   
REMARK 500    LEU C  90     -149.54   -103.20                                   
REMARK 500    ALA C  97      -71.08   -103.63                                   
REMARK 500    ARG C 107        7.08    -64.71                                   
REMARK 500    ASN C 179      104.88   -174.46                                   
REMARK 500    SER D  77     -131.47     52.99                                   
REMARK 500    LEU D  90     -143.89   -100.38                                   
REMARK 500    ALA D  97      -62.29   -100.71                                   
REMARK 500    ASN D 179       99.12   -162.60                                   
REMARK 500    SER E  77     -124.93     50.48                                   
REMARK 500    LEU E  90     -134.55   -104.32                                   
REMARK 500    ALA E  97      -67.64   -103.30                                   
REMARK 500    SER F  77     -125.26     47.89                                   
REMARK 500    LEU F  90     -145.29   -101.67                                   
REMARK 500    ALA F  97      -70.53   -105.99                                   
REMARK 500    ARG F 107        1.86    -68.35                                   
REMARK 500    ASN F 179      107.48   -169.57                                   
REMARK 500    SER G  77     -123.48     48.30                                   
REMARK 500    LEU G  90     -144.59   -105.33                                   
REMARK 500    ALA G  97      -68.02   -102.67                                   
REMARK 500    ALA G 105       52.59    -92.47                                   
REMARK 500    GLN G 121      111.00   -167.80                                   
REMARK 500    ASN G 179       99.45   -165.59                                   
REMARK 500    SER H  77     -121.89     41.84                                   
REMARK 500    LEU H  90     -137.65   -103.76                                   
REMARK 500    ALA H  97      -72.21   -107.55                                   
REMARK 500    GLN H 121      107.43   -172.93                                   
REMARK 500    ASN H 179      102.64   -162.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M=MODEL NUMBER;                               
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 251        DISTANCE =  5.77 ANGSTROMS                       
REMARK 525    HOH G 257        DISTANCE =  5.00 ANGSTROMS                       
REMARK 525    HOH C 265        DISTANCE =  6.92 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2QXT   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN CRYSTALLIZED AT PH 4.5                              
DBREF  2QXU A    3   181  UNP    P37957   LIP_BACSU       34    212             
DBREF  2QXU B    3   181  UNP    P37957   LIP_BACSU       34    212             
DBREF  2QXU C    3   181  UNP    P37957   LIP_BACSU       34    212             
DBREF  2QXU D    3   181  UNP    P37957   LIP_BACSU       34    212             
DBREF  2QXU E    3   181  UNP    P37957   LIP_BACSU       34    212             
DBREF  2QXU F    3   181  UNP    P37957   LIP_BACSU       34    212             
DBREF  2QXU G    3   181  UNP    P37957   LIP_BACSU       34    212             
DBREF  2QXU H    3   181  UNP    P37957   LIP_BACSU       34    212             
SEQRES   1 A  179  HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA          
SEQRES   2 A  179  SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER          
SEQRES   3 A  179  GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE          
SEQRES   4 A  179  TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL          
SEQRES   5 A  179  LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY          
SEQRES   6 A  179  ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY          
SEQRES   7 A  179  ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY          
SEQRES   8 A  179  ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN          
SEQRES   9 A  179  ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO          
SEQRES  10 A  179  ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA          
SEQRES  11 A  179  ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY          
SEQRES  12 A  179  ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY          
SEQRES  13 A  179  LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU          
SEQRES  14 A  179  GLY LEU ASN GLY GLY GLY GLN ASN THR ASN                      
SEQRES   1 B  179  HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA          
SEQRES   2 B  179  SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER          
SEQRES   3 B  179  GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE          
SEQRES   4 B  179  TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL          
SEQRES   5 B  179  LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY          
SEQRES   6 B  179  ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY          
SEQRES   7 B  179  ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY          
SEQRES   8 B  179  ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN          
SEQRES   9 B  179  ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO          
SEQRES  10 B  179  ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA          
SEQRES  11 B  179  ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY          
SEQRES  12 B  179  ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY          
SEQRES  13 B  179  LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU          
SEQRES  14 B  179  GLY LEU ASN GLY GLY GLY GLN ASN THR ASN                      
SEQRES   1 C  179  HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA          
SEQRES   2 C  179  SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER          
SEQRES   3 C  179  GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE          
SEQRES   4 C  179  TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL          
SEQRES   5 C  179  LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY          
SEQRES   6 C  179  ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY          
SEQRES   7 C  179  ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY          
SEQRES   8 C  179  ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN          
SEQRES   9 C  179  ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO          
SEQRES  10 C  179  ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA          
SEQRES  11 C  179  ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY          
SEQRES  12 C  179  ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY          
SEQRES  13 C  179  LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU          
SEQRES  14 C  179  GLY LEU ASN GLY GLY GLY GLN ASN THR ASN                      
SEQRES   1 D  179  HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA          
SEQRES   2 D  179  SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER          
SEQRES   3 D  179  GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE          
SEQRES   4 D  179  TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL          
SEQRES   5 D  179  LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY          
SEQRES   6 D  179  ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY          
SEQRES   7 D  179  ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY          
SEQRES   8 D  179  ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN          
SEQRES   9 D  179  ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO          
SEQRES  10 D  179  ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA          
SEQRES  11 D  179  ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY          
SEQRES  12 D  179  ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY          
SEQRES  13 D  179  LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU          
SEQRES  14 D  179  GLY LEU ASN GLY GLY GLY GLN ASN THR ASN                      
SEQRES   1 E  179  HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA          
SEQRES   2 E  179  SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER          
SEQRES   3 E  179  GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE          
SEQRES   4 E  179  TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL          
SEQRES   5 E  179  LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY          
SEQRES   6 E  179  ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY          
SEQRES   7 E  179  ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY          
SEQRES   8 E  179  ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN          
SEQRES   9 E  179  ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO          
SEQRES  10 E  179  ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA          
SEQRES  11 E  179  ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY          
SEQRES  12 E  179  ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY          
SEQRES  13 E  179  LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU          
SEQRES  14 E  179  GLY LEU ASN GLY GLY GLY GLN ASN THR ASN                      
SEQRES   1 F  179  HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA          
SEQRES   2 F  179  SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER          
SEQRES   3 F  179  GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE          
SEQRES   4 F  179  TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL          
SEQRES   5 F  179  LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY          
SEQRES   6 F  179  ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY          
SEQRES   7 F  179  ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY          
SEQRES   8 F  179  ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN          
SEQRES   9 F  179  ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO          
SEQRES  10 F  179  ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA          
SEQRES  11 F  179  ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY          
SEQRES  12 F  179  ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY          
SEQRES  13 F  179  LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU          
SEQRES  14 F  179  GLY LEU ASN GLY GLY GLY GLN ASN THR ASN                      
SEQRES   1 G  179  HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA          
SEQRES   2 G  179  SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER          
SEQRES   3 G  179  GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE          
SEQRES   4 G  179  TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL          
SEQRES   5 G  179  LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY          
SEQRES   6 G  179  ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY          
SEQRES   7 G  179  ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY          
SEQRES   8 G  179  ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN          
SEQRES   9 G  179  ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO          
SEQRES  10 G  179  ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA          
SEQRES  11 G  179  ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY          
SEQRES  12 G  179  ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY          
SEQRES  13 G  179  LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU          
SEQRES  14 G  179  GLY LEU ASN GLY GLY GLY GLN ASN THR ASN                      
SEQRES   1 H  179  HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA          
SEQRES   2 H  179  SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER          
SEQRES   3 H  179  GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE          
SEQRES   4 H  179  TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL          
SEQRES   5 H  179  LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY          
SEQRES   6 H  179  ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY          
SEQRES   7 H  179  ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY          
SEQRES   8 H  179  ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN          
SEQRES   9 H  179  ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO          
SEQRES  10 H  179  ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA          
SEQRES  11 H  179  ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY          
SEQRES  12 H  179  ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY          
SEQRES  13 H  179  LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU          
SEQRES  14 H  179  GLY LEU ASN GLY GLY GLY GLN ASN THR ASN                      
FORMUL   9  HOH   *840(H2 O)                                                    
HELIX    1   1 ALA A   15  ASN A   18  5                                   4    
HELIX    2   2 PHE A   19  GLN A   29  1                                  11    
HELIX    3   3 SER A   32  ASP A   34  5                                   3    
HELIX    4   4 THR A   47  GLY A   67  1                                  21    
HELIX    5   5 MET A   78  LEU A   90  1                                  13    
HELIX    6   6 ASP A   91  ASN A   94  5                                   4    
HELIX    7   7 ALA A  105  THR A  109  5                                   5    
HELIX    8   8 MET A  137  ARG A  142  1                                   6    
HELIX    9   9 HIS A  156  TYR A  161  5                                   6    
HELIX   10  10 SER A  162  ASN A  174  1                                  13    
HELIX   11  11 ALA B   15  ASN B   18  5                                   4    
HELIX   12  12 PHE B   19  GLN B   29  1                                  11    
HELIX   13  13 SER B   32  ASP B   34  5                                   3    
HELIX   14  14 THR B   47  GLY B   67  1                                  21    
HELIX   15  15 MET B   78  LEU B   90  1                                  13    
HELIX   16  16 ASP B   91  ASN B   94  5                                   4    
HELIX   17  17 ALA B  105  THR B  109  5                                   5    
HELIX   18  18 MET B  137  ARG B  142  1                                   6    
HELIX   19  19 HIS B  156  TYR B  161  5                                   6    
HELIX   20  20 SER B  162  ASN B  174  1                                  13    
HELIX   21  21 ALA C   15  ASN C   18  5                                   4    
HELIX   22  22 PHE C   19  GLN C   29  1                                  11    
HELIX   23  23 SER C   32  ASP C   34  5                                   3    
HELIX   24  24 THR C   47  GLY C   67  1                                  21    
HELIX   25  25 MET C   78  LEU C   90  1                                  13    
HELIX   26  26 ASP C   91  ASN C   94  5                                   4    
HELIX   27  27 ALA C  105  THR C  109  5                                   5    
HELIX   28  28 MET C  137  ARG C  142  1                                   6    
HELIX   29  29 ILE C  157  TYR C  161  5                                   5    
HELIX   30  30 SER C  162  ASN C  174  1                                  13    
HELIX   31  31 ALA D   15  ASN D   18  5                                   4    
HELIX   32  32 PHE D   19  GLN D   29  1                                  11    
HELIX   33  33 SER D   32  ASP D   34  5                                   3    
HELIX   34  34 THR D   47  GLY D   67  1                                  21    
HELIX   35  35 MET D   78  ASN D   89  1                                  12    
HELIX   36  36 ASP D   91  ASN D   94  5                                   4    
HELIX   37  37 ALA D  105  THR D  109  5                                   5    
HELIX   38  38 MET D  137  SER D  141  5                                   5    
HELIX   39  39 ILE D  157  TYR D  161  5                                   5    
HELIX   40  40 SER D  162  ASN D  174  1                                  13    
HELIX   41  41 ALA E   15  ASN E   18  5                                   4    
HELIX   42  42 PHE E   19  GLN E   29  1                                  11    
HELIX   43  43 SER E   32  ASP E   34  5                                   3    
HELIX   44  44 THR E   47  GLY E   67  1                                  21    
HELIX   45  45 MET E   78  LEU E   90  1                                  13    
HELIX   46  46 ASP E   91  ASN E   94  5                                   4    
HELIX   47  47 ALA E  105  THR E  109  5                                   5    
HELIX   48  48 MET E  137  ARG E  142  1                                   6    
HELIX   49  49 ILE E  157  TYR E  161  5                                   5    
HELIX   50  50 SER E  162  ASN E  174  1                                  13    
HELIX   51  51 ALA F   15  ASN F   18  5                                   4    
HELIX   52  52 PHE F   19  GLN F   29  1                                  11    
HELIX   53  53 SER F   32  ASP F   34  5                                   3    
HELIX   54  54 THR F   47  GLY F   67  1                                  21    
HELIX   55  55 MET F   78  LEU F   90  1                                  13    
HELIX   56  56 ASP F   91  ASN F   94  5                                   4    
HELIX   57  57 ALA F  105  THR F  109  5                                   5    
HELIX   58  58 MET F  137  SER F  141  5                                   5    
HELIX   59  59 ILE F  157  TYR F  161  5                                   5    
HELIX   60  60 SER F  162  ASN F  174  1                                  13    
HELIX   61  61 ALA G   15  ASN G   18  5                                   4    
HELIX   62  62 PHE G   19  GLN G   29  1                                  11    
HELIX   63  63 SER G   32  ASP G   34  5                                   3    
HELIX   64  64 THR G   47  GLY G   67  1                                  21    
HELIX   65  65 MET G   78  LEU G   90  1                                  13    
HELIX   66  66 ASP G   91  ASN G   94  5                                   4    
HELIX   67  67 ALA G  105  THR G  109  5                                   5    
HELIX   68  68 MET G  137  ARG G  142  1                                   6    
HELIX   69  69 HIS G  156  TYR G  161  5                                   6    
HELIX   70  70 SER G  162  ASN G  174  1                                  13    
HELIX   71  71 ALA H   15  ASN H   18  5                                   4    
HELIX   72  72 PHE H   19  GLN H   29  1                                  11    
HELIX   73  73 SER H   32  ASP H   34  5                                   3    
HELIX   74  74 THR H   47  GLY H   67  1                                  21    
HELIX   75  75 MET H   78  LEU H   90  1                                  13    
HELIX   76  76 ASP H   91  ASN H   94  5                                   4    
HELIX   77  77 ALA H  105  THR H  109  5                                   5    
HELIX   78  78 MET H  137  ARG H  142  1                                   6    
HELIX   79  79 ILE H  157  TYR H  161  5                                   5    
HELIX   80  80 SER H  162  ASN H  174  1                                  13    
SHEET    1   A 6 LEU A  36  ALA A  38  0                                        
SHEET    2   A 6 VAL A   6  VAL A   9  1  N  VAL A   6   O  TYR A  37           
SHEET    3   A 6 VAL A  71  HIS A  76  1  O  ASP A  72   N  VAL A   7           
SHEET    4   A 6 VAL A  96  LEU A 102  1  O  LEU A 102   N  ALA A  75           
SHEET    5   A 6 LEU A 124  SER A 130  1  O  LEU A 124   N  VAL A  99           
SHEET    6   A 6 ARG A 147  ILE A 151  1  O  VAL A 149   N  SER A 127           
SHEET    1   B 6 LEU B  36  ALA B  38  0                                        
SHEET    2   B 6 VAL B   6  VAL B   9  1  N  VAL B   6   O  TYR B  37           
SHEET    3   B 6 VAL B  71  HIS B  76  1  O  ASP B  72   N  VAL B   7           
SHEET    4   B 6 VAL B  96  LEU B 102  1  O  LEU B 102   N  ALA B  75           
SHEET    5   B 6 LEU B 124  SER B 130  1  O  LEU B 124   N  VAL B  99           
SHEET    6   B 6 ARG B 147  ILE B 151  1  O  VAL B 149   N  SER B 127           
SHEET    1   C 6 LEU C  36  ALA C  38  0                                        
SHEET    2   C 6 VAL C   6  VAL C   9  1  N  VAL C   6   O  TYR C  37           
SHEET    3   C 6 VAL C  71  HIS C  76  1  O  ASP C  72   N  VAL C   7           
SHEET    4   C 6 VAL C  96  LEU C 102  1  O  LEU C 102   N  ALA C  75           
SHEET    5   C 6 LEU C 124  SER C 130  1  O  LEU C 124   N  VAL C  99           
SHEET    6   C 6 ARG C 147  ILE C 151  1  O  ARG C 147   N  SER C 127           
SHEET    1   D 6 LEU D  36  ALA D  38  0                                        
SHEET    2   D 6 VAL D   6  VAL D   9  1  N  VAL D   6   O  TYR D  37           
SHEET    3   D 6 VAL D  71  HIS D  76  1  O  HIS D  76   N  VAL D   9           
SHEET    4   D 6 VAL D  96  LEU D 102  1  O  LEU D 102   N  ALA D  75           
SHEET    5   D 6 LEU D 124  SER D 130  1  O  LEU D 124   N  VAL D  99           
SHEET    6   D 6 ARG D 147  ILE D 151  1  O  ILE D 151   N  TYR D 129           
SHEET    1   E 6 LEU E  36  ALA E  38  0                                        
SHEET    2   E 6 VAL E   6  VAL E   9  1  N  VAL E   6   O  TYR E  37           
SHEET    3   E 6 VAL E  71  HIS E  76  1  O  ASP E  72   N  VAL E   7           
SHEET    4   E 6 VAL E  96  LEU E 102  1  O  ASN E  98   N  ILE E  73           
SHEET    5   E 6 LEU E 124  SER E 130  1  O  ILE E 128   N  THR E 101           
SHEET    6   E 6 ARG E 147  ILE E 151  1  O  VAL E 149   N  SER E 127           
SHEET    1   F 6 LEU F  36  ALA F  38  0                                        
SHEET    2   F 6 VAL F   6  VAL F   9  1  N  VAL F   6   O  TYR F  37           
SHEET    3   F 6 VAL F  71  HIS F  76  1  O  HIS F  76   N  VAL F   9           
SHEET    4   F 6 VAL F  96  LEU F 102  1  O  LEU F 102   N  ALA F  75           
SHEET    5   F 6 LEU F 124  SER F 130  1  O  ILE F 128   N  THR F 101           
SHEET    6   F 6 ARG F 147  ILE F 151  1  O  VAL F 149   N  SER F 127           
SHEET    1   G 6 LEU G  36  ALA G  38  0                                        
SHEET    2   G 6 VAL G   6  VAL G   9  1  N  VAL G   6   O  TYR G  37           
SHEET    3   G 6 VAL G  71  HIS G  76  1  O  ASP G  72   N  VAL G   7           
SHEET    4   G 6 VAL G  96  LEU G 102  1  O  ASN G  98   N  ILE G  73           
SHEET    5   G 6 LEU G 124  SER G 130  1  O  ILE G 128   N  THR G 101           
SHEET    6   G 6 ARG G 147  ILE G 151  1  O  VAL G 149   N  SER G 127           
SHEET    1   H 6 LEU H  36  ALA H  38  0                                        
SHEET    2   H 6 VAL H   6  VAL H   9  1  N  VAL H   6   O  TYR H  37           
SHEET    3   H 6 VAL H  71  HIS H  76  1  O  ASP H  72   N  VAL H   7           
SHEET    4   H 6 VAL H  96  LEU H 102  1  O  LEU H 102   N  ALA H  75           
SHEET    5   H 6 LEU H 124  SER H 130  1  O  LEU H 124   N  VAL H  99           
SHEET    6   H 6 ARG H 147  ILE H 151  1  O  VAL H 149   N  SER H 127           
CRYST1  218.608  110.934   51.988  90.00  90.00  90.00 P 21 21 2    32          
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      0.004574  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009014  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019235        0.00000                         
TER    1352      ASN A 181                                                      
TER    2704      ASN B 181                                                      
TER    4056      ASN C 181                                                      
TER    5408      ASN D 181                                                      
TER    6760      ASN E 181                                                      
TER    8112      ASN F 181                                                      
TER    9464      ASN G 181                                                      
TER   10816      ASN H 181                                                      
MASTER      403    0    0   80   48    0    0    611648    8    0  112          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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