Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 3AFI-pdb

Name Class
3AFI-pdb
HEADER    HYDROLASE                               02-MAR-10   3AFI              
TITLE     CRYSTAL STRUCTURE OF DBJA (HIS-DBJA)                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HALOALKANE DEHALOGENASE;                                   
COMPND   3 CHAIN: E, A, B, F;                                                   
COMPND   4 EC: 3.8.1.5;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BRADYRHIZOBIUM JAPONICUM;                       
SOURCE   3 ORGANISM_TAXID: 224911;                                              
SOURCE   4 STRAIN: USDA 110;                                                    
SOURCE   5 GENE: DBJA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PYBJA2                                    
KEYWDS    A/B-HYDROLASE, HYDROLASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.SATO,T.SENDA                                                        
REVDAT   1   19-JAN-11 3AFI    0                                                
JRNL        AUTH   Z.PROKOP,Y.SATO,J.BREZOVSKY,T.MOZGA,R.CHALOUPKOVA,           
JRNL        AUTH 2 T.KOUDELAKOVA,P.JERABEK,V.STEPANKOVA,R.NATSUME,              
JRNL        AUTH 3 J.G.VAN LEEUWEN,D.B.JANSSEN,J.FLORIAN,Y.NAGATA,T.SENDA,      
JRNL        AUTH 4 J.DAMBORSKY                                                  
JRNL        TITL   ENANTIOSELECTIVITY OF HALOALKANE DEHALOGENASES AND ITS       
JRNL        TITL 2 MODULATION BY SURFACE LOOP ENGINEERING                       
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  49  6111 2010              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   20645368                                                     
JRNL        DOI    10.1002/ANIE.201001753                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 127902                         
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 + TEST SET) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6770                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.80                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8607                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.86                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 450                          
REMARK   3   BIN FREE R VALUE                    : 0.2450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9401                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 1120                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.87                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.13000                                             
REMARK   3    B22 (A**2) : 0.07000                                              
REMARK   3    B33 (A**2) : 0.07000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.106         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.099         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.059         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.819         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9701 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13209 ; 1.275 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1196 ; 5.184 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   464 ;31.605 ;21.875       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1424 ;12.553 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   100 ;19.028 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1405 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7690 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4700 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6684 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   963 ; 0.113 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    35 ; 0.272 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    24 ; 0.087 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6028 ; 0.654 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9656 ; 1.233 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3673 ; 2.000 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3553 ; 3.366 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3AFI COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029188.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JAN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 134673                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.04100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17500                            
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: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1BN6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, PH 7.9, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
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   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000      106.42750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.92150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      106.42750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.92150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET E     1                                                      
REMARK 465     SER E     2                                                      
REMARK 465     LYS E     3                                                      
REMARK 465     PRO E     4                                                      
REMARK 465     ILE E     5                                                      
REMARK 465     GLU E     6                                                      
REMARK 465     ILE E     7                                                      
REMARK 465     GLU E     8                                                      
REMARK 465     ILE E     9                                                      
REMARK 465     LEU E   308                                                      
REMARK 465     ALA E   309                                                      
REMARK 465     ALA E   310                                                      
REMARK 465     HIS E   311                                                      
REMARK 465     HIS E   312                                                      
REMARK 465     HIS E   313                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     ILE A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     ILE A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     GLN A   307                                                      
REMARK 465     LEU A   308                                                      
REMARK 465     ALA A   309                                                      
REMARK 465     ALA A   310                                                      
REMARK 465     HIS A   311                                                      
REMARK 465     HIS A   312                                                      
REMARK 465     HIS A   313                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     ILE B     5                                                      
REMARK 465     ARG B   305                                                      
REMARK 465     PRO B   306                                                      
REMARK 465     GLN B   307                                                      
REMARK 465     LEU B   308                                                      
REMARK 465     ALA B   309                                                      
REMARK 465     ALA B   310                                                      
REMARK 465     HIS B   311                                                      
REMARK 465     HIS B   312                                                      
REMARK 465     HIS B   313                                                      
REMARK 465     MET F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     LYS F     3                                                      
REMARK 465     PRO F     4                                                      
REMARK 465     ILE F     5                                                      
REMARK 465     GLU F     6                                                      
REMARK 465     ILE F     7                                                      
REMARK 465     GLU F     8                                                      
REMARK 465     ILE F     9                                                      
REMARK 465     GLN F   307                                                      
REMARK 465     LEU F   308                                                      
REMARK 465     ALA F   309                                                      
REMARK 465     ALA F   310                                                      
REMARK 465     HIS F   311                                                      
REMARK 465     HIS F   312                                                      
REMARK 465     HIS F   313                                                      
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 PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG E  83   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG B  83   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG B  83   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 E  17     -152.69   -124.55                                   
REMARK 500    PRO E  39       52.81   -102.62                                   
REMARK 500    THR E  40     -159.22   -101.77                                   
REMARK 500    ASP E 103     -137.07     57.82                                   
REMARK 500    ARG E 179      -56.18   -127.02                                   
REMARK 500    ALA E 253      -67.45   -147.54                                   
REMARK 500    LEU E 279     -135.44   -120.26                                   
REMARK 500    SER A  17     -147.88   -119.36                                   
REMARK 500    PRO A  39       51.58   -102.04                                   
REMARK 500    THR A  40     -158.02   -103.76                                   
REMARK 500    ASP A 103     -140.27     58.22                                   
REMARK 500    ARG A 179      -53.04   -123.64                                   
REMARK 500    ALA A 253      -72.12   -146.54                                   
REMARK 500    LEU A 279     -135.66   -123.84                                   
REMARK 500    SER B  17     -155.96   -122.30                                   
REMARK 500    PRO B  39       56.09   -102.89                                   
REMARK 500    THR B  40     -161.89   -105.11                                   
REMARK 500    ASP B 103     -133.71     57.33                                   
REMARK 500    ARG B 179      -54.89   -123.63                                   
REMARK 500    ALA B 253      -65.49   -147.92                                   
REMARK 500    LEU B 279     -134.67   -125.31                                   
REMARK 500    SER F  17     -149.46   -122.07                                   
REMARK 500    GLN F  27      -23.97    101.63                                   
REMARK 500    PRO F  39       54.46   -105.01                                   
REMARK 500    THR F  40     -160.44   -106.13                                   
REMARK 500    ASP F 103     -137.54     58.24                                   
REMARK 500    ARG F 179      -54.18   -127.36                                   
REMARK 500    ALA F 253      -72.20   -147.86                                   
REMARK 500    LEU F 279     -136.64   -122.19                                   
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 E1444        DISTANCE =  5.73 ANGSTROMS                       
REMARK 525    HOH A1337        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH A1466        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH B1525        DISTANCE =  5.73 ANGSTROMS                       
REMARK 525    HOH A1557        DISTANCE =  6.16 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 404                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3A2M   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF DBJA (WILD TYPE TYPE I)                         
REMARK 900 RELATED ID: 3A2N   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF DBJA (WILD TYPE TYPE II)                        
REMARK 900 RELATED ID: 3A2L   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF DBJA (MUTANT DBJA DELTA)                        
DBREF  3AFI E    1   310  UNP    P59337   DHAA_BRAJA       1    310             
DBREF  3AFI A    1   310  UNP    P59337   DHAA_BRAJA       1    310             
DBREF  3AFI B    1   310  UNP    P59337   DHAA_BRAJA       1    310             
DBREF  3AFI F    1   310  UNP    P59337   DHAA_BRAJA       1    310             
SEQADV 3AFI HIS E  311  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS E  312  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS E  313  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS E  314  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS E  315  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS E  316  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS A  311  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS A  312  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS A  313  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS A  314  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS A  315  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS A  316  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS B  311  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS B  312  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS B  313  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS B  314  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS B  315  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS B  316  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS F  311  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS F  312  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS F  313  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS F  314  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS F  315  UNP  P59337              EXPRESSION TAG                 
SEQADV 3AFI HIS F  316  UNP  P59337              EXPRESSION TAG                 
SEQRES   1 E  316  MET SER LYS PRO ILE GLU ILE GLU ILE ARG ARG ALA PRO          
SEQRES   2 E  316  VAL LEU GLY SER SER MET ALA TYR ARG GLU THR GLY ALA          
SEQRES   3 E  316  GLN ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO          
SEQRES   4 E  316  THR SER SER HIS ILE TRP ARG ASN ILE LEU PRO LEU VAL          
SEQRES   5 E  316  SER PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY          
SEQRES   6 E  316  PHE GLY GLN SER GLY LYS PRO ASP ILE ALA TYR ARG PHE          
SEQRES   7 E  316  PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU GLN          
SEQRES   8 E  316  ARG GLY VAL THR SER ALA TYR LEU VAL ALA GLN ASP TRP          
SEQRES   9 E  316  GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO          
SEQRES  10 E  316  ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG          
SEQRES  11 E  316  PRO MET PRO THR TRP GLN ASP PHE HIS HIS THR GLU VAL          
SEQRES  12 E  316  ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA ARG ALA VAL          
SEQRES  13 E  316  PHE ARG LYS PHE ARG THR PRO GLY GLU GLY GLU ALA MET          
SEQRES  14 E  316  ILE LEU GLU ALA ASN ALA PHE VAL GLU ARG VAL LEU PRO          
SEQRES  15 E  316  GLY GLY ILE VAL ARG LYS LEU GLY ASP GLU GLU MET ALA          
SEQRES  16 E  316  PRO TYR ARG THR PRO PHE PRO THR PRO GLU SER ARG ARG          
SEQRES  17 E  316  PRO VAL LEU ALA PHE PRO ARG GLU LEU PRO ILE ALA GLY          
SEQRES  18 E  316  GLU PRO ALA ASP VAL TYR GLU ALA LEU GLN SER ALA HIS          
SEQRES  19 E  316  ALA ALA LEU ALA ALA SER SER TYR PRO LYS LEU LEU PHE          
SEQRES  20 E  316  THR GLY GLU PRO GLY ALA LEU VAL SER PRO GLU PHE ALA          
SEQRES  21 E  316  GLU ARG PHE ALA ALA SER LEU THR ARG CYS ALA LEU ILE          
SEQRES  22 E  316  ARG LEU GLY ALA GLY LEU HIS TYR LEU GLN GLU ASP HIS          
SEQRES  23 E  316  ALA ASP ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA          
SEQRES  24 E  316  GLY ILE GLU ALA VAL ARG PRO GLN LEU ALA ALA HIS HIS          
SEQRES  25 E  316  HIS HIS HIS HIS                                              
SEQRES   1 A  316  MET SER LYS PRO ILE GLU ILE GLU ILE ARG ARG ALA PRO          
SEQRES   2 A  316  VAL LEU GLY SER SER MET ALA TYR ARG GLU THR GLY ALA          
SEQRES   3 A  316  GLN ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO          
SEQRES   4 A  316  THR SER SER HIS ILE TRP ARG ASN ILE LEU PRO LEU VAL          
SEQRES   5 A  316  SER PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY          
SEQRES   6 A  316  PHE GLY GLN SER GLY LYS PRO ASP ILE ALA TYR ARG PHE          
SEQRES   7 A  316  PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU GLN          
SEQRES   8 A  316  ARG GLY VAL THR SER ALA TYR LEU VAL ALA GLN ASP TRP          
SEQRES   9 A  316  GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO          
SEQRES  10 A  316  ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG          
SEQRES  11 A  316  PRO MET PRO THR TRP GLN ASP PHE HIS HIS THR GLU VAL          
SEQRES  12 A  316  ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA ARG ALA VAL          
SEQRES  13 A  316  PHE ARG LYS PHE ARG THR PRO GLY GLU GLY GLU ALA MET          
SEQRES  14 A  316  ILE LEU GLU ALA ASN ALA PHE VAL GLU ARG VAL LEU PRO          
SEQRES  15 A  316  GLY GLY ILE VAL ARG LYS LEU GLY ASP GLU GLU MET ALA          
SEQRES  16 A  316  PRO TYR ARG THR PRO PHE PRO THR PRO GLU SER ARG ARG          
SEQRES  17 A  316  PRO VAL LEU ALA PHE PRO ARG GLU LEU PRO ILE ALA GLY          
SEQRES  18 A  316  GLU PRO ALA ASP VAL TYR GLU ALA LEU GLN SER ALA HIS          
SEQRES  19 A  316  ALA ALA LEU ALA ALA SER SER TYR PRO LYS LEU LEU PHE          
SEQRES  20 A  316  THR GLY GLU PRO GLY ALA LEU VAL SER PRO GLU PHE ALA          
SEQRES  21 A  316  GLU ARG PHE ALA ALA SER LEU THR ARG CYS ALA LEU ILE          
SEQRES  22 A  316  ARG LEU GLY ALA GLY LEU HIS TYR LEU GLN GLU ASP HIS          
SEQRES  23 A  316  ALA ASP ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA          
SEQRES  24 A  316  GLY ILE GLU ALA VAL ARG PRO GLN LEU ALA ALA HIS HIS          
SEQRES  25 A  316  HIS HIS HIS HIS                                              
SEQRES   1 B  316  MET SER LYS PRO ILE GLU ILE GLU ILE ARG ARG ALA PRO          
SEQRES   2 B  316  VAL LEU GLY SER SER MET ALA TYR ARG GLU THR GLY ALA          
SEQRES   3 B  316  GLN ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO          
SEQRES   4 B  316  THR SER SER HIS ILE TRP ARG ASN ILE LEU PRO LEU VAL          
SEQRES   5 B  316  SER PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY          
SEQRES   6 B  316  PHE GLY GLN SER GLY LYS PRO ASP ILE ALA TYR ARG PHE          
SEQRES   7 B  316  PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU GLN          
SEQRES   8 B  316  ARG GLY VAL THR SER ALA TYR LEU VAL ALA GLN ASP TRP          
SEQRES   9 B  316  GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO          
SEQRES  10 B  316  ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG          
SEQRES  11 B  316  PRO MET PRO THR TRP GLN ASP PHE HIS HIS THR GLU VAL          
SEQRES  12 B  316  ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA ARG ALA VAL          
SEQRES  13 B  316  PHE ARG LYS PHE ARG THR PRO GLY GLU GLY GLU ALA MET          
SEQRES  14 B  316  ILE LEU GLU ALA ASN ALA PHE VAL GLU ARG VAL LEU PRO          
SEQRES  15 B  316  GLY GLY ILE VAL ARG LYS LEU GLY ASP GLU GLU MET ALA          
SEQRES  16 B  316  PRO TYR ARG THR PRO PHE PRO THR PRO GLU SER ARG ARG          
SEQRES  17 B  316  PRO VAL LEU ALA PHE PRO ARG GLU LEU PRO ILE ALA GLY          
SEQRES  18 B  316  GLU PRO ALA ASP VAL TYR GLU ALA LEU GLN SER ALA HIS          
SEQRES  19 B  316  ALA ALA LEU ALA ALA SER SER TYR PRO LYS LEU LEU PHE          
SEQRES  20 B  316  THR GLY GLU PRO GLY ALA LEU VAL SER PRO GLU PHE ALA          
SEQRES  21 B  316  GLU ARG PHE ALA ALA SER LEU THR ARG CYS ALA LEU ILE          
SEQRES  22 B  316  ARG LEU GLY ALA GLY LEU HIS TYR LEU GLN GLU ASP HIS          
SEQRES  23 B  316  ALA ASP ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA          
SEQRES  24 B  316  GLY ILE GLU ALA VAL ARG PRO GLN LEU ALA ALA HIS HIS          
SEQRES  25 B  316  HIS HIS HIS HIS                                              
SEQRES   1 F  316  MET SER LYS PRO ILE GLU ILE GLU ILE ARG ARG ALA PRO          
SEQRES   2 F  316  VAL LEU GLY SER SER MET ALA TYR ARG GLU THR GLY ALA          
SEQRES   3 F  316  GLN ASP ALA PRO VAL VAL LEU PHE LEU HIS GLY ASN PRO          
SEQRES   4 F  316  THR SER SER HIS ILE TRP ARG ASN ILE LEU PRO LEU VAL          
SEQRES   5 F  316  SER PRO VAL ALA HIS CYS ILE ALA PRO ASP LEU ILE GLY          
SEQRES   6 F  316  PHE GLY GLN SER GLY LYS PRO ASP ILE ALA TYR ARG PHE          
SEQRES   7 F  316  PHE ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU GLN          
SEQRES   8 F  316  ARG GLY VAL THR SER ALA TYR LEU VAL ALA GLN ASP TRP          
SEQRES   9 F  316  GLY THR ALA LEU ALA PHE HIS LEU ALA ALA ARG ARG PRO          
SEQRES  10 F  316  ASP PHE VAL ARG GLY LEU ALA PHE MET GLU PHE ILE ARG          
SEQRES  11 F  316  PRO MET PRO THR TRP GLN ASP PHE HIS HIS THR GLU VAL          
SEQRES  12 F  316  ALA GLU GLU GLN ASP HIS ALA GLU ALA ALA ARG ALA VAL          
SEQRES  13 F  316  PHE ARG LYS PHE ARG THR PRO GLY GLU GLY GLU ALA MET          
SEQRES  14 F  316  ILE LEU GLU ALA ASN ALA PHE VAL GLU ARG VAL LEU PRO          
SEQRES  15 F  316  GLY GLY ILE VAL ARG LYS LEU GLY ASP GLU GLU MET ALA          
SEQRES  16 F  316  PRO TYR ARG THR PRO PHE PRO THR PRO GLU SER ARG ARG          
SEQRES  17 F  316  PRO VAL LEU ALA PHE PRO ARG GLU LEU PRO ILE ALA GLY          
SEQRES  18 F  316  GLU PRO ALA ASP VAL TYR GLU ALA LEU GLN SER ALA HIS          
SEQRES  19 F  316  ALA ALA LEU ALA ALA SER SER TYR PRO LYS LEU LEU PHE          
SEQRES  20 F  316  THR GLY GLU PRO GLY ALA LEU VAL SER PRO GLU PHE ALA          
SEQRES  21 F  316  GLU ARG PHE ALA ALA SER LEU THR ARG CYS ALA LEU ILE          
SEQRES  22 F  316  ARG LEU GLY ALA GLY LEU HIS TYR LEU GLN GLU ASP HIS          
SEQRES  23 F  316  ALA ASP ALA ILE GLY ARG SER VAL ALA GLY TRP ILE ALA          
SEQRES  24 F  316  GLY ILE GLU ALA VAL ARG PRO GLN LEU ALA ALA HIS HIS          
SEQRES  25 F  316  HIS HIS HIS HIS                                              
HET     CL  E 401       1                                                       
HET     CL  A 402       1                                                       
HET     CL  B 403       1                                                       
HET     CL  F 404       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   5   CL    4(CL 1-)                                                     
FORMUL   9  HOH   *1120(H2 O)                                                   
HELIX    1   1 SER E   41  ARG E   46  5                                   6    
HELIX    2   2 ILE E   48  SER E   53  1                                   6    
HELIX    3   3 ARG E   77  ARG E   92  1                                  16    
HELIX    4   4 ASP E  103  ARG E  116  1                                  14    
HELIX    5   5 THR E  134  PHE E  138  5                                   5    
HELIX    6   6 VAL E  143  GLU E  145  5                                   3    
HELIX    7   7 GLU E  146  ARG E  161  1                                  16    
HELIX    8   8 GLY E  164  LEU E  171  1                                   8    
HELIX    9   9 ASN E  174  ARG E  179  1                                   6    
HELIX   10  10 LEU E  181  ILE E  185  5                                   5    
HELIX   11  11 GLY E  190  THR E  199  1                                  10    
HELIX   12  12 PRO E  204  SER E  206  5                                   3    
HELIX   13  13 ARG E  207  PHE E  213  1                                   7    
HELIX   14  14 PRO E  214  LEU E  217  5                                   4    
HELIX   15  15 PRO E  223  SER E  240  1                                  18    
HELIX   16  16 SER E  256  LEU E  267  1                                  12    
HELIX   17  17 TYR E  281  VAL E  304  1                                  24    
HELIX   18  18 SER A   41  ARG A   46  5                                   6    
HELIX   19  19 ILE A   48  SER A   53  1                                   6    
HELIX   20  20 ARG A   77  ARG A   92  1                                  16    
HELIX   21  21 ASP A  103  ARG A  116  1                                  14    
HELIX   22  22 THR A  134  PHE A  138  5                                   5    
HELIX   23  23 VAL A  143  GLU A  145  5                                   3    
HELIX   24  24 GLU A  146  ARG A  161  1                                  16    
HELIX   25  25 GLY A  164  LEU A  171  1                                   8    
HELIX   26  26 ASN A  174  ARG A  179  1                                   6    
HELIX   27  27 LEU A  181  ILE A  185  5                                   5    
HELIX   28  28 GLY A  190  THR A  199  1                                  10    
HELIX   29  29 PRO A  204  SER A  206  5                                   3    
HELIX   30  30 ARG A  207  LEU A  217  1                                  11    
HELIX   31  31 PRO A  223  SER A  240  1                                  18    
HELIX   32  32 SER A  256  LEU A  267  1                                  12    
HELIX   33  33 TYR A  281  HIS A  286  1                                   6    
HELIX   34  34 HIS A  286  ARG A  305  1                                  20    
HELIX   35  35 SER B   41  ARG B   46  5                                   6    
HELIX   36  36 ILE B   48  SER B   53  1                                   6    
HELIX   37  37 ARG B   77  ARG B   92  1                                  16    
HELIX   38  38 ASP B  103  ARG B  116  1                                  14    
HELIX   39  39 THR B  134  PHE B  138  5                                   5    
HELIX   40  40 VAL B  143  GLU B  145  5                                   3    
HELIX   41  41 GLU B  146  ARG B  161  1                                  16    
HELIX   42  42 GLU B  165  LEU B  171  1                                   7    
HELIX   43  43 ASN B  174  ARG B  179  1                                   6    
HELIX   44  44 LEU B  181  ILE B  185  5                                   5    
HELIX   45  45 GLY B  190  THR B  199  1                                  10    
HELIX   46  46 PRO B  204  SER B  206  5                                   3    
HELIX   47  47 ARG B  207  PHE B  213  1                                   7    
HELIX   48  48 PRO B  214  LEU B  217  5                                   4    
HELIX   49  49 PRO B  223  SER B  240  1                                  18    
HELIX   50  50 SER B  256  LEU B  267  1                                  12    
HELIX   51  51 TYR B  281  VAL B  304  1                                  24    
HELIX   52  52 SER F   41  ARG F   46  5                                   6    
HELIX   53  53 ILE F   48  SER F   53  1                                   6    
HELIX   54  54 ARG F   77  ARG F   92  1                                  16    
HELIX   55  55 ASP F  103  ARG F  116  1                                  14    
HELIX   56  56 THR F  134  PHE F  138  5                                   5    
HELIX   57  57 VAL F  143  GLU F  145  5                                   3    
HELIX   58  58 GLU F  146  ARG F  161  1                                  16    
HELIX   59  59 GLY F  164  LEU F  171  1                                   8    
HELIX   60  60 ASN F  174  ARG F  179  1                                   6    
HELIX   61  61 ARG F  179  GLY F  184  1                                   6    
HELIX   62  62 GLY F  190  THR F  199  1                                  10    
HELIX   63  63 PRO F  204  SER F  206  5                                   3    
HELIX   64  64 ARG F  207  LEU F  217  1                                  11    
HELIX   65  65 PRO F  223  SER F  240  1                                  18    
HELIX   66  66 SER F  256  SER F  266  1                                  11    
HELIX   67  67 TYR F  281  VAL F  304  1                                  24    
SHEET    1   A 8 ARG E  11  VAL E  14  0                                        
SHEET    2   A 8 SER E  17  THR E  24 -1  O  SER E  17   N  VAL E  14           
SHEET    3   A 8 HIS E  57  PRO E  61 -1  O  ALA E  60   N  ARG E  22           
SHEET    4   A 8 VAL E  31  LEU E  35  1  N  VAL E  32   O  ILE E  59           
SHEET    5   A 8 ALA E  97  GLN E 102  1  O  TYR E  98   N  LEU E  33           
SHEET    6   A 8 VAL E 120  MET E 126  1  O  ALA E 124   N  LEU E  99           
SHEET    7   A 8 LYS E 244  PRO E 251  1  O  LEU E 245   N  PHE E 125           
SHEET    8   A 8 CYS E 270  GLY E 278  1  O  ALA E 271   N  LEU E 246           
SHEET    1   B 8 ARG A  10  VAL A  14  0                                        
SHEET    2   B 8 SER A  17  THR A  24 -1  O  TYR A  21   N  ARG A  10           
SHEET    3   B 8 HIS A  57  PRO A  61 -1  O  ALA A  60   N  ARG A  22           
SHEET    4   B 8 VAL A  31  LEU A  35  1  N  VAL A  32   O  ILE A  59           
SHEET    5   B 8 ALA A  97  GLN A 102  1  O  TYR A  98   N  LEU A  33           
SHEET    6   B 8 VAL A 120  MET A 126  1  O  ALA A 124   N  LEU A  99           
SHEET    7   B 8 LYS A 244  PRO A 251  1  O  LEU A 245   N  PHE A 125           
SHEET    8   B 8 CYS A 270  GLY A 278  1  O  ILE A 273   N  LEU A 246           
SHEET    1   C 8 ARG B  10  VAL B  14  0                                        
SHEET    2   C 8 SER B  17  THR B  24 -1  O  MET B  19   N  ALA B  12           
SHEET    3   C 8 HIS B  57  PRO B  61 -1  O  ALA B  60   N  ARG B  22           
SHEET    4   C 8 VAL B  31  LEU B  35  1  N  VAL B  32   O  ILE B  59           
SHEET    5   C 8 ALA B  97  GLN B 102  1  O  VAL B 100   N  LEU B  35           
SHEET    6   C 8 VAL B 120  MET B 126  1  O  ALA B 124   N  LEU B  99           
SHEET    7   C 8 LYS B 244  PRO B 251  1  O  LEU B 245   N  PHE B 125           
SHEET    8   C 8 CYS B 270  GLY B 278  1  O  ILE B 273   N  LEU B 246           
SHEET    1   D 8 ARG F  11  VAL F  14  0                                        
SHEET    2   D 8 SER F  17  THR F  24 -1  O  MET F  19   N  ALA F  12           
SHEET    3   D 8 HIS F  57  PRO F  61 -1  O  CYS F  58   N  THR F  24           
SHEET    4   D 8 VAL F  31  LEU F  35  1  N  VAL F  32   O  ILE F  59           
SHEET    5   D 8 ALA F  97  GLN F 102  1  O  VAL F 100   N  LEU F  35           
SHEET    6   D 8 VAL F 120  MET F 126  1  O  ALA F 124   N  LEU F  99           
SHEET    7   D 8 LYS F 244  PRO F 251  1  O  LEU F 245   N  PHE F 125           
SHEET    8   D 8 CYS F 270  GLY F 278  1  O  LEU F 275   N  THR F 248           
CISPEP   1 ASN E   38    PRO E   39          0       -13.51                     
CISPEP   2 GLU E  222    PRO E  223          0        -3.63                     
CISPEP   3 GLU E  250    PRO E  251          0         3.58                     
CISPEP   4 ASN A   38    PRO A   39          0       -15.44                     
CISPEP   5 GLU A  222    PRO A  223          0        -4.50                     
CISPEP   6 GLU A  250    PRO A  251          0         1.15                     
CISPEP   7 ASN B   38    PRO B   39          0       -14.36                     
CISPEP   8 GLU B  222    PRO B  223          0        -5.27                     
CISPEP   9 GLU B  250    PRO B  251          0         1.30                     
CISPEP  10 ASN F   38    PRO F   39          0       -10.50                     
CISPEP  11 GLU F  222    PRO F  223          0        -4.14                     
CISPEP  12 GLU F  250    PRO F  251          0         1.93                     
SITE     1 AC1  5 ASN E  38  TRP E 104  PHE E 213  PRO E 214                    
SITE     2 AC1  5 HOH E1162                                                     
SITE     1 AC2  5 ASN A  38  TRP A 104  PHE A 213  PRO A 214                    
SITE     2 AC2  5 HOH A 772                                                     
SITE     1 AC3  5 ASN B  38  TRP B 104  PHE B 213  PRO B 214                    
SITE     2 AC3  5 HOH B 567                                                     
SITE     1 AC4  5 ASN F  38  TRP F 104  PHE F 213  PRO F 214                    
SITE     2 AC4  5 HOH F 974                                                     
CRYST1  212.855  117.843   55.796  90.00  90.00  90.00 P 21 21 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      0.004698  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008486  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017922        0.00000                         
TER    2352      HIS E 316                                                      
TER    4703      HIS A 316                                                      
TER    7074      HIS B 316                                                      
TER    9425      HIS F 316                                                      
MASTER      421    0    4   67   32    0    8    610525    4    0  100          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer