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LongText Report for: 1F6W-pdb

Name Class
1F6W-pdb
HEADER    HYDROLASE                               23-JUN-00   1F6W              
TITLE     STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT                  
TITLE    2 ACTIVATED LIPASE                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BILE SALT ACTIVATED LIPASE;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND   5 EC: 3.1.1.3;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 TISSUE: PANCREAS;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BACTERIA;                                  
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    BILE SALT ACTIVATED LIPASE, ESTERASE, CATALYTIC DOMAIN                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.TERZYAN,X.ZHANG                                                     
REVDAT   1   18-OCT-00 1F6W    0                                                
JRNL        AUTH   S.TERZYAN,C.-S.WANG,D.DOWNS,B.HUNTER,X.ZHANG                 
JRNL        TITL   CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN           
JRNL        TITL 2 BILE SALT ACTIVATED LIPASE                                   
JRNL        REF    PROTEIN SCI.                  V.   9  1783 2000              
JRNL        REFN   ASTM PRCIEI  US ISSN 0961-8368                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.30 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 23474                          
REMARK   3                                                                      
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) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1171                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3232                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3600                       
REMARK   3   BIN FREE R VALUE                    : 0.4100                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 160                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.032                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4151                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 163                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.57000                                             
REMARK   3    B22 (A**2) : -17.67000                                            
REMARK   3    B33 (A**2) : 20.24000                                             
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) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.420                           
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) : 0.40                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.49                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.02                            
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) : 1.89  ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.12  ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.45  ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.51  ; 2.500                
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.28                                                 
REMARK   3   BSOL        : 31.29                                                
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  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1F6W COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-2000.                
REMARK 100 THE RCSB ID CODE IS RCSB011317.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-OCT-1999                        
REMARK 200  TEMPERATURE           (KELVIN) : 93.0                               
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRANDEIS Q4                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25287                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 19.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR                    
REMARK 200  REPLACEMENT                                                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1AKN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.0                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, NACL, N-(2-                    
REMARK 280  ACETAMIDO) IMINODIACETIC ACID                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   1/2-X,-Y,1/2+Z                                          
REMARK 290       3555   -X,1/2+Y,1/2-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       32.35000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.15000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.48500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.15000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.35000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.48500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    THR A 140   N   -  CA  -  C   ANGL. DEV. =-10.8 DEGREES           
REMARK 500    LEU A 277   N   -  CA  -  C   ANGL. DEV. = 10.6 DEGREES           
REMARK 500    TYR A 284   N   -  CA  -  C   ANGL. DEV. =  9.7 DEGREES           
REMARK 500    ILE A 296   N   -  CA  -  C   ANGL. DEV. =-11.3 DEGREES           
REMARK 500    LYS A 409   N   -  CA  -  C   ANGL. DEV. =-13.8 DEGREES           
REMARK 500    LEU A 417   N   -  CA  -  C   ANGL. DEV. =-10.0 DEGREES           
REMARK 500    ASN A 470   N   -  CA  -  C   ANGL. DEV. = -9.9 DEGREES           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 194       56.19   -115.84                                   
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED            
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE                 
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL                 
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525  0 HOH    74        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525  0 HOH   136        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525  0 HOH   165        DISTANCE =  7.21 ANGSTROMS                       
REMARK 525  0 HOH   168        DISTANCE =  6.16 ANGSTROMS                       
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AKN   RELATED DB: PDB                                   
REMARK 900 1AKN CONTAINS THE STRUCTURE OF BOVINE BILE SALT ACTIVATED            
REMARK 900 LIPASE                                                               
DBREF  1F6W A    1   533  SWS    P19835   BAL_HUMAN       21    553             
SEQADV 1F6W ASP A  186  SWS  P19835    ASN   206 ENGINEERED                     
SEQADV 1F6W ASP A  298  SWS  P19835    ALA   318 ENGINEERED                     
SEQRES   1 A  533  ALA LYS LEU GLY ALA VAL TYR THR GLU GLY GLY PHE VAL          
SEQRES   2 A  533  GLU GLY VAL ASN LYS LYS LEU GLY LEU LEU GLY ASP SER          
SEQRES   3 A  533  VAL ASP ILE PHE LYS GLY ILE PRO PHE ALA ALA PRO THR          
SEQRES   4 A  533  LYS ALA LEU GLU ASN PRO GLN PRO HIS PRO GLY TRP GLN          
SEQRES   5 A  533  GLY THR LEU LYS ALA LYS ASN PHE LYS LYS ARG CYS LEU          
SEQRES   6 A  533  GLN ALA THR ILE THR GLN ASP SER THR TYR GLY ASP GLU          
SEQRES   7 A  533  ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO GLN GLY ARG          
SEQRES   8 A  533  LYS GLN VAL SER ARG ASP LEU PRO VAL MET ILE TRP ILE          
SEQRES   9 A  533  TYR GLY GLY ALA PHE LEU MET GLY SER GLY HIS GLY ALA          
SEQRES  10 A  533  ASN PHE LEU ASN ASN TYR LEU TYR ASP GLY GLU GLU ILE          
SEQRES  11 A  533  ALA THR ARG GLY ASN VAL ILE VAL VAL THR PHE ASN TYR          
SEQRES  12 A  533  ARG VAL GLY PRO LEU GLY PHE LEU SER THR GLY ASP ALA          
SEQRES  13 A  533  ASN LEU PRO GLY ASN TYR GLY LEU ARG ASP GLN HIS MET          
SEQRES  14 A  533  ALA ILE ALA TRP VAL LYS ARG ASN ILE ALA ALA PHE GLY          
SEQRES  15 A  533  GLY ASP PRO ASP ASN ILE THR LEU PHE GLY GLU SER ALA          
SEQRES  16 A  533  GLY GLY ALA SER VAL SER LEU GLN THR LEU SER PRO TYR          
SEQRES  17 A  533  ASN LYS GLY LEU ILE ARG ARG ALA ILE SER GLN SER GLY          
SEQRES  18 A  533  VAL ALA LEU SER PRO TRP VAL ILE GLN LYS ASN PRO LEU          
SEQRES  19 A  533  PHE TRP ALA LYS LYS VAL ALA GLU LYS VAL GLY CYS PRO          
SEQRES  20 A  533  VAL GLY ASP ALA ALA ARG MET ALA GLN CYS LEU LYS VAL          
SEQRES  21 A  533  THR ASP PRO ARG ALA LEU THR LEU ALA TYR LYS VAL PRO          
SEQRES  22 A  533  LEU ALA GLY LEU GLU TYR PRO MET LEU HIS TYR VAL GLY          
SEQRES  23 A  533  PHE VAL PRO VAL ILE ASP GLY ASP PHE ILE PRO ASP ASP          
SEQRES  24 A  533  PRO ILE ASN LEU TYR ALA ASN ALA ALA ASP ILE ASP TYR          
SEQRES  25 A  533  ILE ALA GLY THR ASN ASN MET ASP GLY HIS ILE PHE ALA          
SEQRES  26 A  533  SER ILE ASP MET PRO ALA ILE ASN LYS GLY ASN LYS LYS          
SEQRES  27 A  533  VAL THR GLU GLU ASP PHE TYR LYS LEU VAL SER GLU PHE          
SEQRES  28 A  533  THR ILE THR LYS GLY LEU ARG GLY ALA LYS THR THR PHE          
SEQRES  29 A  533  ASP VAL TYR THR GLU SER TRP ALA GLN ASP PRO SER GLN          
SEQRES  30 A  533  GLU ASN LYS LYS LYS THR VAL VAL ASP PHE GLU THR ASP          
SEQRES  31 A  533  VAL LEU PHE LEU VAL PRO THR GLU ILE ALA LEU ALA GLN          
SEQRES  32 A  533  HIS ARG ALA ASN ALA LYS SER ALA LYS THR TYR ALA TYR          
SEQRES  33 A  533  LEU PHE SER HIS PRO SER ARG MET PRO VAL TYR PRO LYS          
SEQRES  34 A  533  TRP VAL GLY ALA ASP HIS ALA ASP ASP ILE GLN TYR VAL          
SEQRES  35 A  533  PHE GLY LYS PRO PHE ALA THR PRO THR GLY TYR ARG PRO          
SEQRES  36 A  533  GLN ASP ARG THR VAL SER LYS ALA MET ILE ALA TYR TRP          
SEQRES  37 A  533  THR ASN PHE ALA LYS THR GLY ASP PRO ASN MET GLY ASP          
SEQRES  38 A  533  SER ALA VAL PRO THR HIS TRP GLU PRO TYR THR THR GLU          
SEQRES  39 A  533  ASN SER GLY TYR LEU GLU ILE THR LYS LYS MET GLY SER          
SEQRES  40 A  533  SER SER MET LYS ARG SER LEU ARG THR ASN PHE LEU ARG          
SEQRES  41 A  533  TYR TRP THR LEU THR TYR LEU ALA LEU PRO THR VAL THR          
FORMUL   2  HOH   *163(H2 O1)                                                   
HELIX    1   1 GLY A  127  ASN A  135  1                                   9    
HELIX    2   2 GLY A  146  LEU A  151  1                                   6    
HELIX    3   3 ASN A  161  ILE A  178  1                                  18    
HELIX    4   4 SER A  194  LEU A  205  1                                  12    
HELIX    5   5 PRO A  233  VAL A  244  1                                  12    
HELIX    6   6 ALA A  251  THR A  261  1                                  11    
HELIX    7   7 ASP A  262  ALA A  269  1                                   8    
HELIX    8   8 GLY A  321  MET A  329  1                                   9    
HELIX    9   9 THR A  340  THR A  352  1                                  13    
HELIX   10  10 GLY A  356  THR A  368  1                                  13    
HELIX   11  12 ASP A  438  GLY A  444  1                                   7    
HELIX   12  13 PRO A  455  GLY A  475  5                                  21    
HELIX   13  14 ARG A  515  LEU A  527  1                                  13    
SHEET    1   A 3 GLY A   4  THR A   8  0                                        
SHEET    2   A 3 GLY A  11  GLY A  15 -1  N  GLY A  11   O  THR A   8           
SHEET    3   A 3 THR A  54  LYS A  56  1  O  LEU A  55   N  GLU A  14           
SHEET    1   B11 VAL A  16  LEU A  20  0                                        
SHEET    2   B11 ASP A  25  PRO A  34 -1  O  VAL A  27   N  LYS A  18           
SHEET    3   B11 LEU A  81  GLY A  90 -1  N  LEU A  83   O  ILE A  33           
SHEET    4   B11 ILE A 137  ASN A 142 -1  N  VAL A 138   O  TRP A  86           
SHEET    5   B11 LEU A  98  ILE A 104  1  O  PRO A  99   N  ILE A 137           
SHEET    6   B11 GLY A 183  GLU A 193  1  N  ASP A 184   O  LEU A  98           
SHEET    7   B11 ARG A 215  SER A 220  1  O  ARG A 215   N  LEU A 190           
SHEET    8   B11 ASP A 311  ASN A 318  1  O  ASP A 311   N  ALA A 216           
SHEET    9   B11 LYS A 412  SER A 419  1  N  TYR A 414   O  TYR A 312           
SHEET   10   B11 TYR A 498  ILE A 501  1  O  LEU A 499   N  LEU A 417           
SHEET   11   B11 SER A 509  LYS A 511 -1  N  LYS A 511   O  TYR A 498           
SSBOND   1 CYS A   64    CYS A   80                                             
SSBOND   2 CYS A  246    CYS A  257                                             
CRYST1   64.700   88.970  104.300  90.00  90.00  90.00 P 21 21 21    4          
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      0.015458  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011240  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009587        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.
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