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LongText Report for: 3D2B-pdb

Name Class
3D2B-pdb
HEADER    HYDROLASE                               08-MAY-08   3D2B              
TITLE     STRUCTURE OF 2D9, A THERMOSTABLE MUTANT OF BACILLUS                   
TITLE    2 SUBTILIS LIPASE OBTAINED THROUGH DIRECTED EVOLUTION                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE;                                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: TRIACYLGLYCEROL LIPASE;                                     
COMPND   5 EC: 3.1.1.3;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 GENE: LIPA, LIP, BSU02700;                                           
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: PET21B                                    
KEYWDS    LIPASE, ALPHA/BETA HYDROLASE, STABILITY, DIRECTED EVOLUTION,          
KEYWDS   2 HYDROLASE, LIPID DEGRADATION, SECRETED                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.SANKARANARAYANAN,M.Z.KAMAL                                          
REVDAT   1   03-JUN-08 3D2B    0                                                
JRNL        AUTH   S.AHMAD,M.Z.KAMAL,R.SANKARANARAYANAN,N.M.RAO                 
JRNL        TITL   THERMOSTABLE BACILLUS SUBTILIS LIPASES: IN VITRO             
JRNL        TITL 2 EVOLUTION AND STRUCTURAL INSIGHT                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.95 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 36163                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1801                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2712                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 313                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.92800                                              
REMARK   3    B22 (A**2) : 2.65200                                              
REMARK   3    B33 (A**2) : -6.58000                                             
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.005 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.170 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 41.54                                                
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   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3D2B COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.                               
REMARK 100 THE RCSB ID CODE IS RCSB047502.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 9.50                               
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          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36223                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM ETHANOLAMINE BUFFE, 10MM           
REMARK 280  SODIUM SULFATE, PH 9.5, VAPOUR DIFFUSION, SITTING DROP,             
REMARK 280  TEMPERATURE 277K, VAPOR DIFFUSION, SITTING DROP                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   1/2+X,1/2+Y,1/2+Z                                       
REMARK 290       6555   1/2-X,1/2-Y,1/2+Z                                       
REMARK 290       7555   1/2-X,1/2+Y,1/2-Z                                       
REMARK 290       8555   1/2+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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       37.60150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       58.69950            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       58.77750            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       37.60150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       58.69950            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       58.77750            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       37.60150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       58.69950            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       58.77750            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       37.60150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       58.69950            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       58.77750            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                 
REMARK 465                                                                      
REMARK 465   M RES C  SSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLU B     2                                                      
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     -123.72     52.61                                   
REMARK 500    LEU A  90     -143.99   -107.00                                   
REMARK 500    ARG A 107        2.13    -69.99                                   
REMARK 500    ASN A 179       98.93   -167.72                                   
REMARK 500    SER B  77     -123.89     49.63                                   
REMARK 500    LEU B  90     -145.91   -104.56                                   
REMARK 500    ASN B 179       70.18   -164.40                                   
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 B 430        DISTANCE =  5.07 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1T2N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1T4M   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3D2A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3D2C   RELATED DB: PDB                                   
DBREF  3D2B A    1   181  UNP    P37957   LIP_BACSU       32    212             
DBREF  3D2B B    1   181  UNP    P37957   LIP_BACSU       32    212             
SEQADV 3D2B SER A   17  UNP  P37957    PHE    48 ENGINEERED                     
SEQADV 3D2B TYR A   89  UNP  P37957    ASN   120 ENGINEERED                     
SEQADV 3D2B PRO A  114  UNP  P37957    LEU   145 ENGINEERED                     
SEQADV 3D2B ASP A  132  UNP  P37957    ALA   163 ENGINEERED                     
SEQADV 3D2B MET A  157  UNP  P37957    ILE   188 ENGINEERED                     
SEQADV 3D2B TYR A  166  UNP  P37957    ASN   197 ENGINEERED                     
SEQADV 3D2B SER B   17  UNP  P37957    PHE    48 ENGINEERED                     
SEQADV 3D2B TYR B   89  UNP  P37957    ASN   120 ENGINEERED                     
SEQADV 3D2B PRO B  114  UNP  P37957    LEU   145 ENGINEERED                     
SEQADV 3D2B ASP B  132  UNP  P37957    ALA   163 ENGINEERED                     
SEQADV 3D2B MET B  157  UNP  P37957    ILE   188 ENGINEERED                     
SEQADV 3D2B TYR B  166  UNP  P37957    ASN   197 ENGINEERED                     
SEQRES   1 A  181  ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY          
SEQRES   2 A  181  GLY ALA SER SER ASN PHE ALA GLY ILE LYS SER TYR LEU          
SEQRES   3 A  181  VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL          
SEQRES   4 A  181  ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY          
SEQRES   5 A  181  PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU          
SEQRES   6 A  181  THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET          
SEQRES   7 A  181  GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP          
SEQRES   8 A  181  GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY          
SEQRES   9 A  181  ALA ASN ARG LEU THR THR GLY LYS ALA PRO PRO GLY THR          
SEQRES  10 A  181  ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER          
SEQRES  11 A  181  SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU          
SEQRES  12 A  181  ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS          
SEQRES  13 A  181  MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE          
SEQRES  14 A  181  LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN              
SEQRES   1 B  181  ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY          
SEQRES   2 B  181  GLY ALA SER SER ASN PHE ALA GLY ILE LYS SER TYR LEU          
SEQRES   3 B  181  VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL          
SEQRES   4 B  181  ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY          
SEQRES   5 B  181  PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU          
SEQRES   6 B  181  THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET          
SEQRES   7 B  181  GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP          
SEQRES   8 B  181  GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY          
SEQRES   9 B  181  ALA ASN ARG LEU THR THR GLY LYS ALA PRO PRO GLY THR          
SEQRES  10 B  181  ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER          
SEQRES  11 B  181  SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU          
SEQRES  12 B  181  ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS          
SEQRES  13 B  181  MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE          
SEQRES  14 B  181  LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN              
FORMUL   3  HOH   *313(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  TYR B   89  1                                  12    
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    
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  ASN A  98   N  ILE A  73           
SHEET    5   A 6 LEU A 124  SER A 130  1  O  ILE A 128   N  THR A 101           
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  VAL B 100   N  ALA B  75           
SHEET    5   B 6 LEU B 124  SER B 130  1  O  ILE B 128   N  THR B 101           
SHEET    6   B 6 ARG B 147  ILE B 151  1  O  VAL B 149   N  SER B 127           
CRYST1   75.203  117.399  117.555  90.00  90.00  90.00 I 2 2 2      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      0.013297  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008518  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008507        0.00000                         
TER    1357      ASN A 181                                                      
TER    2714      ASN B 181                                                      
MASTER      295    0    0   20   12    0    0    6 3025    2    0   28          
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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