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LongText Report for: 3JW8-pdb

Name Class
3JW8-pdb
HEADER    HYDROLASE                               18-SEP-09   3JW8              
TITLE     CRYSTAL STRUCTURE OF HUMAN MONO-GLYCERIDE LIPASE                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MGLL PROTEIN;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MONOGLYCERIDE LIPASE, ISOFORM CRA_B, CDNA,                  
COMPND   5 FLJ96595, HOMO SAPIENS MONOGLYCERIDE LIPASE (MGLL), MRNA;            
COMPND   6 EC: 3.1.1.23;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MGLL, HCG_40840;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    ALPHA-BETA HYDROLASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.BERTRAND,F.AUGE,J.HOUTMANN,A.RAK,F.VALLEE,V.MIKOL,                  
AUTHOR   2 P.F.BERNE,N.MICHOT,D.CHEURET,C.HOORNAERT,M.MATHIEU                   
REVDAT   1   26-JAN-10 3JW8    0                                                
JRNL        AUTH   T.BERTRAND,F.AUGE,J.HOUTMANN,A.RAK,F.VALLEE,                 
JRNL        AUTH 2 V.MIKOL,P.F.BERNE,N.MICHOT,D.CHEURET,C.HOORNAERT,            
JRNL        AUTH 3 M.MATHIEU                                                    
JRNL        TITL   STRUCTURAL BASIS FOR HUMAN MONOGLYCERIDE LIPASE              
JRNL        TITL 2 INHIBITION.                                                  
JRNL        REF    J.MOL.BIOL.                                2009              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   19962385                                                     
JRNL        DOI    10.1016/J.JMB.2009.11.060                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.3                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 17.21                          
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)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 44314                          
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) : 0.157                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2230                            
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           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.04                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3037                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1522                       
REMARK   3   BIN FREE R VALUE                    : 0.2088                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.39                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 173                          
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            : 4404                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 532                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.56                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.24510                                             
REMARK   3    B22 (A**2) : 0.79650                                              
REMARK   3    B33 (A**2) : -0.55140                                             
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) : 0.17                            
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) : 0.020                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.32                            
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3JW8 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055237.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JAN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9797, 0.9799, 1.000              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44315                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05600                            
REMARK 200   FOR THE DATA SET  : 18.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.14900                            
REMARK 200   FOR SHELL         : 6.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES, 40% MPD, PH 6.0, VAPOR         
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
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   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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       43.29400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       63.15550            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       70.28350            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.29400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       63.15550            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       70.28350            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.29400            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       63.15550            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       70.28350            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.29400            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       63.15550            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       70.28350            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 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 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 45020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -280.0 KCAL/MOL                       
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -221.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      126.31100            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      126.31100            
REMARK 350   BIOMT3   4  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     MSE A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     MSE A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     THR A   306                                                      
REMARK 465     ALA A   307                                                      
REMARK 465     GLY A   308                                                      
REMARK 465     THR A   309                                                      
REMARK 465     ALA A   310                                                      
REMARK 465     SER A   311                                                      
REMARK 465     PRO A   312                                                      
REMARK 465     PRO A   313                                                      
REMARK 465     MSE B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     MSE B    11                                                      
REMARK 465     PRO B    12                                                      
REMARK 465     GLU B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     SER B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     PRO B    17                                                      
REMARK 465     ARG B    18                                                      
REMARK 465     ARG B    19                                                      
REMARK 465     THR B    20                                                      
REMARK 465     PRO B    21                                                      
REMARK 465     GLN B    22                                                      
REMARK 465     SER B    23                                                      
REMARK 465     ILE B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     TYR B    26                                                      
REMARK 465     GLN B    27                                                      
REMARK 465     THR B   306                                                      
REMARK 465     ALA B   307                                                      
REMARK 465     GLY B   308                                                      
REMARK 465     THR B   309                                                      
REMARK 465     ALA B   310                                                      
REMARK 465     SER B   311                                                      
REMARK 465     PRO B   312                                                      
REMARK 465     PRO B   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 B  97   CD  -  NE  -  CZ  ANGL. DEV. =   8.4 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    GLU A  63     -153.88   -103.94                                   
REMARK 500    SER A 132     -129.83     62.56                                   
REMARK 500    SER A 156       62.94     38.62                                   
REMARK 500    VAL A 159      -33.58   -132.07                                   
REMARK 500    TYR A 278     -152.83    -89.36                                   
REMARK 500    GLU A 284     -164.31   -102.72                                   
REMARK 500    GLU B  63     -154.16   -106.27                                   
REMARK 500    SER B 132     -128.56     60.29                                   
REMARK 500    SER B 156       65.56     29.20                                   
REMARK 500    TYR B 278     -153.91    -88.97                                   
REMARK 500    GLU B 284     -166.15   -100.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU B 160        23.7      L          L   OUTSIDE RANGE           
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 A 549        DISTANCE =  7.15 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 707                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 831                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 866                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 886                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 812                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 830                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 865                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3JWE   RELATED DB: PDB                                   
DBREF  3JW8 A    1   313  UNP    Q6IBG9   Q6IBG9_HUMAN     1    313             
DBREF  3JW8 B    1   313  UNP    Q6IBG9   Q6IBG9_HUMAN     1    313             
SEQADV 3JW8 MSE A   -6  UNP  Q6IBG9              EXPRESSION TAG                 
SEQADV 3JW8 HIS A   -5  UNP  Q6IBG9              EXPRESSION TAG                 
SEQADV 3JW8 HIS A   -4  UNP  Q6IBG9              EXPRESSION TAG                 
SEQADV 3JW8 HIS A   -3  UNP  Q6IBG9              EXPRESSION TAG                 
SEQADV 3JW8 HIS A   -2  UNP  Q6IBG9              EXPRESSION TAG                 
SEQADV 3JW8 HIS A   -1  UNP  Q6IBG9              EXPRESSION TAG                 
SEQADV 3JW8 HIS A    0  UNP  Q6IBG9              EXPRESSION TAG                 
SEQADV 3JW8 MSE B   -6  UNP  Q6IBG9              EXPRESSION TAG                 
SEQADV 3JW8 HIS B   -5  UNP  Q6IBG9              EXPRESSION TAG                 
SEQADV 3JW8 HIS B   -4  UNP  Q6IBG9              EXPRESSION TAG                 
SEQADV 3JW8 HIS B   -3  UNP  Q6IBG9              EXPRESSION TAG                 
SEQADV 3JW8 HIS B   -2  UNP  Q6IBG9              EXPRESSION TAG                 
SEQADV 3JW8 HIS B   -1  UNP  Q6IBG9              EXPRESSION TAG                 
SEQADV 3JW8 HIS B    0  UNP  Q6IBG9              EXPRESSION TAG                 
SEQRES   1 A  320  MSE HIS HIS HIS HIS HIS HIS MSE GLU THR GLY PRO GLU          
SEQRES   2 A  320  ASP PRO SER SER MSE PRO GLU GLU SER SER PRO ARG ARG          
SEQRES   3 A  320  THR PRO GLN SER ILE PRO TYR GLN ASP LEU PRO HIS LEU          
SEQRES   4 A  320  VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS ARG TYR TRP          
SEQRES   5 A  320  LYS PRO THR GLY THR PRO LYS ALA LEU ILE PHE VAL SER          
SEQRES   6 A  320  HIS GLY ALA GLY GLU HIS SER GLY ARG TYR GLU GLU LEU          
SEQRES   7 A  320  ALA ARG MSE LEU MSE GLY LEU ASP LEU LEU VAL PHE ALA          
SEQRES   8 A  320  HIS ASP HIS VAL GLY HIS GLY GLN SER GLU GLY GLU ARG          
SEQRES   9 A  320  MSE VAL VAL SER ASP PHE HIS VAL PHE VAL ARG ASP VAL          
SEQRES  10 A  320  LEU GLN HIS VAL ASP SER MSE GLN LYS ASP TYR PRO GLY          
SEQRES  11 A  320  LEU PRO VAL PHE LEU LEU GLY HIS SER MSE GLY GLY ALA          
SEQRES  12 A  320  ILE ALA ILE LEU THR ALA ALA GLU ARG PRO GLY HIS PHE          
SEQRES  13 A  320  ALA GLY MSE VAL LEU ILE SER PRO LEU VAL LEU ALA ASN          
SEQRES  14 A  320  PRO GLU SER ALA THR THR PHE LYS VAL LEU ALA ALA LYS          
SEQRES  15 A  320  VAL LEU ASN LEU VAL LEU PRO ASN LEU SER LEU GLY PRO          
SEQRES  16 A  320  ILE ASP SER SER VAL LEU SER ARG ASN LYS THR GLU VAL          
SEQRES  17 A  320  ASP ILE TYR ASN SER ASP PRO LEU ILE CYS ARG ALA GLY          
SEQRES  18 A  320  LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU ASN ALA VAL          
SEQRES  19 A  320  SER ARG VAL GLU ARG ALA LEU PRO LYS LEU THR VAL PRO          
SEQRES  20 A  320  PHE LEU LEU LEU GLN GLY SER ALA ASP ARG LEU CYS ASP          
SEQRES  21 A  320  SER LYS GLY ALA TYR LEU LEU MSE GLU LEU ALA LYS SER          
SEQRES  22 A  320  GLN ASP LYS THR LEU LYS ILE TYR GLU GLY ALA TYR HIS          
SEQRES  23 A  320  VAL LEU HIS LYS GLU LEU PRO GLU VAL THR ASN SER VAL          
SEQRES  24 A  320  PHE HIS GLU ILE ASN MSE TRP VAL SER GLN ARG THR ALA          
SEQRES  25 A  320  THR ALA GLY THR ALA SER PRO PRO                              
SEQRES   1 B  320  MSE HIS HIS HIS HIS HIS HIS MSE GLU THR GLY PRO GLU          
SEQRES   2 B  320  ASP PRO SER SER MSE PRO GLU GLU SER SER PRO ARG ARG          
SEQRES   3 B  320  THR PRO GLN SER ILE PRO TYR GLN ASP LEU PRO HIS LEU          
SEQRES   4 B  320  VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS ARG TYR TRP          
SEQRES   5 B  320  LYS PRO THR GLY THR PRO LYS ALA LEU ILE PHE VAL SER          
SEQRES   6 B  320  HIS GLY ALA GLY GLU HIS SER GLY ARG TYR GLU GLU LEU          
SEQRES   7 B  320  ALA ARG MSE LEU MSE GLY LEU ASP LEU LEU VAL PHE ALA          
SEQRES   8 B  320  HIS ASP HIS VAL GLY HIS GLY GLN SER GLU GLY GLU ARG          
SEQRES   9 B  320  MSE VAL VAL SER ASP PHE HIS VAL PHE VAL ARG ASP VAL          
SEQRES  10 B  320  LEU GLN HIS VAL ASP SER MSE GLN LYS ASP TYR PRO GLY          
SEQRES  11 B  320  LEU PRO VAL PHE LEU LEU GLY HIS SER MSE GLY GLY ALA          
SEQRES  12 B  320  ILE ALA ILE LEU THR ALA ALA GLU ARG PRO GLY HIS PHE          
SEQRES  13 B  320  ALA GLY MSE VAL LEU ILE SER PRO LEU VAL LEU ALA ASN          
SEQRES  14 B  320  PRO GLU SER ALA THR THR PHE LYS VAL LEU ALA ALA LYS          
SEQRES  15 B  320  VAL LEU ASN LEU VAL LEU PRO ASN LEU SER LEU GLY PRO          
SEQRES  16 B  320  ILE ASP SER SER VAL LEU SER ARG ASN LYS THR GLU VAL          
SEQRES  17 B  320  ASP ILE TYR ASN SER ASP PRO LEU ILE CYS ARG ALA GLY          
SEQRES  18 B  320  LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU ASN ALA VAL          
SEQRES  19 B  320  SER ARG VAL GLU ARG ALA LEU PRO LYS LEU THR VAL PRO          
SEQRES  20 B  320  PHE LEU LEU LEU GLN GLY SER ALA ASP ARG LEU CYS ASP          
SEQRES  21 B  320  SER LYS GLY ALA TYR LEU LEU MSE GLU LEU ALA LYS SER          
SEQRES  22 B  320  GLN ASP LYS THR LEU LYS ILE TYR GLU GLY ALA TYR HIS          
SEQRES  23 B  320  VAL LEU HIS LYS GLU LEU PRO GLU VAL THR ASN SER VAL          
SEQRES  24 B  320  PHE HIS GLU ILE ASN MSE TRP VAL SER GLN ARG THR ALA          
SEQRES  25 B  320  THR ALA GLY THR ALA SER PRO PRO                              
MODRES 3JW8 MSE A   74  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE A   76  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE A   98  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE A  117  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE A  133  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE A  152  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE A  261  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE A  298  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE B   74  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE B   76  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE B   98  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE B  117  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE B  133  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE B  152  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE B  261  MET  SELENOMETHIONINE                                   
MODRES 3JW8 MSE B  298  MET  SELENOMETHIONINE                                   
HET    MSE  A  74       8                                                       
HET    MSE  A  76       8                                                       
HET    MSE  A  98       8                                                       
HET    MSE  A 117       8                                                       
HET    MSE  A 133       8                                                       
HET    MSE  A 152       8                                                       
HET    MSE  A 261       8                                                       
HET    MSE  A 298       8                                                       
HET    MSE  B  74       8                                                       
HET    MSE  B  76       8                                                       
HET    MSE  B  98       8                                                       
HET    MSE  B 117       8                                                       
HET    MSE  B 133       8                                                       
HET    MSE  B 152       8                                                       
HET    MSE  B 261       8                                                       
HET    MSE  B 298       8                                                       
HET    MPD  A 707       8                                                       
HET    MRD  A 831       8                                                       
HET    MRD  A 866       8                                                       
HET    MRD  A 886       8                                                       
HET    MPD  B 812       8                                                       
HET    MRD  B 830       8                                                       
HET    MRD  B 865       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETNAM     MRD (4R)-2-METHYLPENTANE-2,4-DIOL                                    
FORMUL   1  MSE    16(C5 H11 N O2 SE)                                           
FORMUL   3  MPD    2(C6 H14 O2)                                                 
FORMUL   4  MRD    5(C6 H14 O2)                                                 
FORMUL  10  HOH   *532(H2 O)                                                    
HELIX    1   1 PRO A   25  LEU A   29  5                                   5    
HELIX    2   2 HIS A   64  ARG A   67  5                                   4    
HELIX    3   3 TYR A   68  LEU A   78  1                                  11    
HELIX    4   4 PHE A  103  TYR A  121  1                                  19    
HELIX    5   5 MSE A  133  ARG A  145  1                                  13    
HELIX    6   6 THR A  167  LEU A  181  1                                  15    
HELIX    7   7 ASP A  190  LEU A  194  5                                   5    
HELIX    8   8 ASN A  197  ASP A  207  1                                  11    
HELIX    9   9 LYS A  216  LEU A  234  1                                  19    
HELIX   10  10 PRO A  235  LEU A  237  5                                   3    
HELIX   11  11 ASP A  253  ALA A  264  1                                  12    
HELIX   12  12 VAL A  280  GLU A  284  5                                   5    
HELIX   13  13 LEU A  285  ARG A  303  1                                  19    
HELIX   14  14 HIS B   64  ARG B   67  5                                   4    
HELIX   15  15 TYR B   68  GLY B   77  1                                  10    
HELIX   16  16 PHE B  103  TYR B  121  1                                  19    
HELIX   17  17 MSE B  133  ARG B  145  1                                  13    
HELIX   18  18 THR B  167  LEU B  181  1                                  15    
HELIX   19  19 ASP B  190  LEU B  194  5                                   5    
HELIX   20  20 ASN B  197  ASP B  207  1                                  11    
HELIX   21  21 LYS B  216  LEU B  234  1                                  19    
HELIX   22  22 PRO B  235  LEU B  237  5                                   3    
HELIX   23  23 ASP B  253  ALA B  264  1                                  12    
HELIX   24  24 VAL B  280  GLU B  284  5                                   5    
HELIX   25  25 LEU B  285  ARG B  303  1                                  19    
SHEET    1   A16 HIS A  31  VAL A  33  0                                        
SHEET    2   A16 TYR A  39  TRP A  45 -1  O  LEU A  40   N  LEU A  32           
SHEET    3   A16 LEU A  80  HIS A  85 -1  O  VAL A  82   N  TRP A  45           
SHEET    4   A16 ALA A  53  SER A  58  1  N  VAL A  57   O  PHE A  83           
SHEET    5   A16 VAL A 126  HIS A 131  1  O  LEU A 129   N  SER A  58           
SHEET    6   A16 GLY A 151  ILE A 155  1  O  ILE A 155   N  GLY A 130           
SHEET    7   A16 PHE A 241  GLY A 246  1  O  LEU A 242   N  LEU A 154           
SHEET    8   A16 LYS A 269  TYR A 274  1  O  THR A 270   N  LEU A 243           
SHEET    9   A16 LYS B 269  TYR B 274 -1  O  LEU B 271   N  LEU A 271           
SHEET   10   A16 PHE B 241  GLY B 246  1  N  LEU B 243   O  THR B 270           
SHEET   11   A16 GLY B 151  ILE B 155  1  N  LEU B 154   O  LEU B 242           
SHEET   12   A16 VAL B 126  HIS B 131  1  N  GLY B 130   O  ILE B 155           
SHEET   13   A16 ALA B  53  SER B  58  1  N  SER B  58   O  LEU B 129           
SHEET   14   A16 LEU B  80  HIS B  85  1  O  LEU B  81   N  ALA B  53           
SHEET   15   A16 TYR B  39  TRP B  45 -1  N  TRP B  45   O  VAL B  82           
SHEET   16   A16 HIS B  31  VAL B  33 -1  N  LEU B  32   O  LEU B  40           
LINK         C   MSE A  74                 N   LEU A  75     1555   1555  1.33  
LINK         C   MSE A  76                 N   GLY A  77     1555   1555  1.35  
LINK         C   MSE A  98                 N   VAL A  99     1555   1555  1.32  
LINK         C   MSE A 117                 N   GLN A 118     1555   1555  1.33  
LINK         C   MSE A 133                 N   GLY A 134     1555   1555  1.32  
LINK         C   MSE A 152                 N   VAL A 153     1555   1555  1.35  
LINK         C   MSE A 261                 N   GLU A 262     1555   1555  1.32  
LINK         C   MSE A 298                 N   TRP A 299     1555   1555  1.35  
LINK         C   MSE B  74                 N   LEU B  75     1555   1555  1.34  
LINK         C   MSE B  76                 N   GLY B  77     1555   1555  1.34  
LINK         C   MSE B  98                 N   VAL B  99     1555   1555  1.33  
LINK         C   MSE B 117                 N   GLN B 118     1555   1555  1.36  
LINK         C   MSE B 133                 N   GLY B 134     1555   1555  1.34  
LINK         C   MSE B 152                 N   VAL B 153     1555   1555  1.33  
LINK         C   MSE B 261                 N   GLU B 262     1555   1555  1.32  
LINK         C   MSE B 298                 N   TRP B 299     1555   1555  1.35  
LINK         C   ARG A  73                 N   MSE A  74     1555   1555  1.36  
LINK         C   LEU A  75                 N   MSE A  76     1555   1555  1.35  
LINK         C   ARG A  97                 N   MSE A  98     1555   1555  1.36  
LINK         C   SER A 116                 N   MSE A 117     1555   1555  1.38  
LINK         C   SER A 132                 N   MSE A 133     1555   1555  1.35  
LINK         C   GLY A 151                 N   MSE A 152     1555   1555  1.33  
LINK         C   LEU A 260                 N   MSE A 261     1555   1555  1.34  
LINK         C   ASN A 297                 N   MSE A 298     1555   1555  1.33  
LINK         C   ARG B  73                 N   MSE B  74     1555   1555  1.38  
LINK         C   LEU B  75                 N   MSE B  76     1555   1555  1.32  
LINK         C   ARG B  97                 N   MSE B  98     1555   1555  1.34  
LINK         C   SER B 116                 N   MSE B 117     1555   1555  1.37  
LINK         C   SER B 132                 N   MSE B 133     1555   1555  1.32  
LINK         C   GLY B 151                 N   MSE B 152     1555   1555  1.35  
LINK         C   LEU B 260                 N   MSE B 261     1555   1555  1.35  
LINK         C   ASN B 297                 N   MSE B 298     1555   1555  1.34  
SITE     1 AC1  8 LEU A 158  ALA A 161  ASN A 162  SER A 165                    
SITE     2 AC1  8 ALA A 166  GLY A 220  MRD A 831  MRD A 886                    
SITE     1 AC2  4 SER A 132  HOH A 445  HOH A 513  MPD A 707                    
SITE     1 AC3  8 ALA A  61  HIS A 131  ILE A 189  LEU A 251                    
SITE     2 AC3  8 HIS A 279  VAL A 280  HOH A 445  HOH A 529                    
SITE     1 AC4  4 SER A 165  LYS A 170  LEU A 186  MPD A 707                    
SITE     1 AC5  7 ALA B 161  ASN B 162  SER B 165  LEU B 215                    
SITE     2 AC5  7 LEU B 223  HOH B 456  MRD B 830                               
SITE     1 AC6  4 SER B 132  HOH B 444  HOH B 516  MPD B 812                    
SITE     1 AC7 12 GLY B  60  ALA B  61  GLU B  63  HIS B 131                    
SITE     2 AC7 12 LEU B 194  TYR B 204  LEU B 251  HIS B 279                    
SITE     3 AC7 12 VAL B 280  HOH B 444  HOH B 447  HOH B 516                    
CRYST1   86.588  126.311  140.567  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      0.011549  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007917  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007114        0.00000                         
TER    2253      ALA A 305                                                      
TER    4406      ALA B 305                                                      
MASTER      445    0   23   25   16    0   12    6 4992    2  216   50          
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:
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