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LongText Report for: 3HJU-pdb

Name Class
3HJU-pdb
HEADER    HYDROLASE                               22-MAY-09   3HJU              
TITLE     CRYSTAL STRUCTURE OF HUMAN MONOGLYCERIDE LIPASE                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MONOGLYCERIDE LIPASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MONOACYLGLYCEROL LIPASE, MAGL, MGL,                         
COMPND   5 LYSOPHOSPHOLIPASE HOMOLOG, LYSOPHOSPHOLIPASE-LIKE, HU-K5;            
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;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PASK43                                    
KEYWDS    ALPHA/BETA HYDROLASE, HYDROLASE, SERINE ESTERASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.LABAR,C.BAUVOIS,F.BOREL,J.-L.FERRER,J.WOUTERS,D.M.LAMBERT           
REVDAT   1   08-DEC-09 3HJU    0                                                
JRNL        AUTH   G.LABAR,C.BAUVOIS,F.BOREL,J.-L.FERRER,J.WOUTERS,             
JRNL        AUTH 2 D.M.LAMBERT                                                  
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN MONOACYLGLYCEROL              
JRNL        TITL 2 LIPASE, A KEY ACTOR IN ENDOCANNABINOID SIGNALING             
JRNL        REF    CHEMBIOCHEM                                2009              
JRNL        REFN                   ESSN 1439-7633                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 35779                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1896                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2558                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.50                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 142                          
REMARK   3   BIN FREE R VALUE                    : 0.2630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4516                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 177                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.87000                                              
REMARK   3    B22 (A**2) : -1.35000                                             
REMARK   3    B33 (A**2) : 0.48000                                              
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): 0.228         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.187         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4622 ; 0.021 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6277 ; 1.839 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   580 ; 6.066 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   192 ;28.037 ;23.438       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   776 ;15.030 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;13.805 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   718 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3462 ; 0.013 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  2900 ; 1.065 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4677 ; 1.930 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1722 ; 3.179 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1600 ; 4.774 ; 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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3HJU COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAY-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053221.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4-6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976180                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37674                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.020                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11900                            
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.40000                            
REMARK 200   FOR SHELL         : 3.860                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: A PARTIAL/INCOMPLETE MODEL OF PDB ENTRIES            
REMARK 200  OBTAINED BY OTHER METHODS                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% V/V MPD, 70MM SODIUM                 
REMARK 280  CACODYLATE, PH 4-6, UNDER OIL, 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       42.93000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       63.61500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       68.57000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       42.93000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       63.61500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       68.57000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       42.93000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       63.61500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       68.57000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       42.93000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       63.61500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       68.57000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 APPLY THE FOLLOWING TO CHAINS: A, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 395  LIES ON A SPECIAL POSITION.                          
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 A   -17                                                      
REMARK 465     ARG A   -16                                                      
REMARK 465     GLY A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     ALA A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     PRO A    -1                                                      
REMARK 465     GLU A     0                                                      
REMARK 465     PHE A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     GLY A   298                                                      
REMARK 465     THR A   299                                                      
REMARK 465     ALA A   300                                                      
REMARK 465     SER A   301                                                      
REMARK 465     PRO A   302                                                      
REMARK 465     PRO A   303                                                      
REMARK 465     LEU A   304                                                      
REMARK 465     GLU A   305                                                      
REMARK 465     VAL A   306                                                      
REMARK 465     ASP A   307                                                      
REMARK 465     LEU A   308                                                      
REMARK 465     GLN A   309                                                      
REMARK 465     GLY A   310                                                      
REMARK 465     ASP A   311                                                      
REMARK 465     HIS A   312                                                      
REMARK 465     GLY A   313                                                      
REMARK 465     LEU A   314                                                      
REMARK 465     SER A   315                                                      
REMARK 465     ALA A   316                                                      
REMARK 465     TRP A   317                                                      
REMARK 465     SER A   318                                                      
REMARK 465     HIS A   319                                                      
REMARK 465     PRO A   320                                                      
REMARK 465     GLN A   321                                                      
REMARK 465     PHE A   322                                                      
REMARK 465     GLU A   323                                                      
REMARK 465     LYS A   324                                                      
REMARK 465     MET B   -17                                                      
REMARK 465     ARG B   -16                                                      
REMARK 465     GLY B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     ALA B    -6                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     ASP B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     PRO B    -1                                                      
REMARK 465     GLU B     0                                                      
REMARK 465     PHE B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     ALA B   297                                                      
REMARK 465     GLY B   298                                                      
REMARK 465     THR B   299                                                      
REMARK 465     ALA B   300                                                      
REMARK 465     SER B   301                                                      
REMARK 465     PRO B   302                                                      
REMARK 465     PRO B   303                                                      
REMARK 465     LEU B   304                                                      
REMARK 465     GLU B   305                                                      
REMARK 465     VAL B   306                                                      
REMARK 465     ASP B   307                                                      
REMARK 465     LEU B   308                                                      
REMARK 465     GLN B   309                                                      
REMARK 465     GLY B   310                                                      
REMARK 465     ASP B   311                                                      
REMARK 465     HIS B   312                                                      
REMARK 465     GLY B   313                                                      
REMARK 465     LEU B   314                                                      
REMARK 465     SER B   315                                                      
REMARK 465     ALA B   316                                                      
REMARK 465     TRP B   317                                                      
REMARK 465     SER B   318                                                      
REMARK 465     HIS B   319                                                      
REMARK 465     PRO B   320                                                      
REMARK 465     GLN B   321                                                      
REMARK 465     PHE B   322                                                      
REMARK 465     GLU B   323                                                      
REMARK 465     LYS B   324                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER B   6    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASN B   168     O    PRO B   172              1.46            
REMARK 500   OE1  GLU A    60     O    HOH A   390              1.56            
REMARK 500   OD1  ASN B   168     C    PRO B   172              1.85            
REMARK 500   O    THR B   158     CG1  VAL B   161              1.87            
REMARK 500   O    LEU B   167     N    LEU B   171              1.94            
REMARK 500   OD1  ASN B   168     CA   PRO B   172              1.96            
REMARK 500   CA   LEU B   167     CG1  VAL B   170              2.13            
REMARK 500   OH   TYR A    16     O    HOH A   386              2.14            
REMARK 500   O    LEU B   167     CG1  VAL B   170              2.15            
REMARK 500   OE1  GLN B   292     O    HOH B   337              2.15            
REMARK 500   CG   PRO A    15     OD2  ASP A    18              2.18            
REMARK 500   O    ALA B   164     N    ASN B   168              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS B   160     O    VAL B   166     2545     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 274   CD    GLU A 274   OE2    -0.077                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A  87   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP A  99   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 243   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG B  87   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    PRO B 153   C   -  N   -  CD  ANGL. DEV. = -18.3 DEGREES          
REMARK 500    PRO B 172   CA  -  N   -  CD  ANGL. DEV. = -12.6 DEGREES          
REMARK 500    PRO B 172   C   -  N   -  CD  ANGL. DEV. = -15.9 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    ARG A   8      169.48     81.19                                   
REMARK 500    SER A  13       -3.05     92.28                                   
REMARK 500    GLU A  53     -154.53   -109.60                                   
REMARK 500    SER A 122     -118.30     60.44                                   
REMARK 500    LEU A 176        7.11    -68.57                                   
REMARK 500    TYR A 268     -146.77    -90.79                                   
REMARK 500    GLU A 274     -164.16   -102.32                                   
REMARK 500    GLU B  53     -149.66   -102.81                                   
REMARK 500    SER B 122     -122.30     60.48                                   
REMARK 500    SER B 146       60.27     38.00                                   
REMARK 500    PRO B 153       53.11     13.05                                   
REMARK 500    SER B 155      164.91    -46.36                                   
REMARK 500    TYR B 268     -149.63    -83.29                                   
REMARK 500    GLU B 274     -160.66   -102.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A  154     SER A  155                 -143.86                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 382        DISTANCE =  6.40 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 417                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 410                 
DBREF  3HJU A    2   303  UNP    Q99685   MGLL_HUMAN       2    303             
DBREF  3HJU B    2   303  UNP    Q99685   MGLL_HUMAN       2    303             
SEQADV 3HJU MET A  -17  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU ARG A  -16  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLY A  -15  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU SER A  -14  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS A  -13  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS A  -12  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS A  -11  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS A  -10  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS A   -9  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS A   -8  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLY A   -7  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU ALA A   -6  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLY A   -5  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU ASP A   -4  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU ARG A   -3  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLY A   -2  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU PRO A   -1  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLU A    0  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU PHE A    1  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU LEU A  304  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLU A  305  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU VAL A  306  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU ASP A  307  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU LEU A  308  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLN A  309  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLY A  310  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU ASP A  311  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS A  312  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLY A  313  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU LEU A  314  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU SER A  315  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU ALA A  316  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU TRP A  317  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU SER A  318  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS A  319  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU PRO A  320  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLN A  321  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU PHE A  322  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLU A  323  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU LYS A  324  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU MET B  -17  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU ARG B  -16  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLY B  -15  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU SER B  -14  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS B  -13  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS B  -12  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS B  -11  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS B  -10  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS B   -9  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS B   -8  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLY B   -7  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU ALA B   -6  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLY B   -5  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU ASP B   -4  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU ARG B   -3  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLY B   -2  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU PRO B   -1  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLU B    0  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU PHE B    1  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU LEU B  304  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLU B  305  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU VAL B  306  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU ASP B  307  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU LEU B  308  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLN B  309  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLY B  310  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU ASP B  311  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS B  312  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLY B  313  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU LEU B  314  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU SER B  315  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU ALA B  316  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU TRP B  317  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU SER B  318  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU HIS B  319  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU PRO B  320  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLN B  321  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU PHE B  322  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU GLU B  323  UNP  Q99685              EXPRESSION TAG                 
SEQADV 3HJU LYS B  324  UNP  Q99685              EXPRESSION TAG                 
SEQRES   1 A  342  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY ALA GLY          
SEQRES   2 A  342  ASP ARG GLY PRO GLU PHE PRO GLU GLU SER SER PRO ARG          
SEQRES   3 A  342  ARG THR PRO GLN SER ILE PRO TYR GLN ASP LEU PRO HIS          
SEQRES   4 A  342  LEU VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS ARG TYR          
SEQRES   5 A  342  TRP LYS PRO THR GLY THR PRO LYS ALA LEU ILE PHE VAL          
SEQRES   6 A  342  SER HIS GLY ALA GLY GLU HIS SER GLY ARG TYR GLU GLU          
SEQRES   7 A  342  LEU ALA ARG MET LEU MET GLY LEU ASP LEU LEU VAL PHE          
SEQRES   8 A  342  ALA HIS ASP HIS VAL GLY HIS GLY GLN SER GLU GLY GLU          
SEQRES   9 A  342  ARG MET VAL VAL SER ASP PHE HIS VAL PHE VAL ARG ASP          
SEQRES  10 A  342  VAL LEU GLN HIS VAL ASP SER MET GLN LYS ASP TYR PRO          
SEQRES  11 A  342  GLY LEU PRO VAL PHE LEU LEU GLY HIS SER MET GLY GLY          
SEQRES  12 A  342  ALA ILE ALA ILE LEU THR ALA ALA GLU ARG PRO GLY HIS          
SEQRES  13 A  342  PHE ALA GLY MET VAL LEU ILE SER PRO LEU VAL LEU ALA          
SEQRES  14 A  342  ASN PRO GLU SER ALA THR THR PHE LYS VAL LEU ALA ALA          
SEQRES  15 A  342  LYS VAL LEU ASN LEU VAL LEU PRO ASN LEU SER LEU GLY          
SEQRES  16 A  342  PRO ILE ASP SER SER VAL LEU SER ARG ASN LYS THR GLU          
SEQRES  17 A  342  VAL ASP ILE TYR ASN SER ASP PRO LEU ILE CYS ARG ALA          
SEQRES  18 A  342  GLY LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU ASN ALA          
SEQRES  19 A  342  VAL SER ARG VAL GLU ARG ALA LEU PRO LYS LEU THR VAL          
SEQRES  20 A  342  PRO PHE LEU LEU LEU GLN GLY SER ALA ASP ARG LEU CYS          
SEQRES  21 A  342  ASP SER LYS GLY ALA TYR LEU LEU MET GLU LEU ALA LYS          
SEQRES  22 A  342  SER GLN ASP LYS THR LEU LYS ILE TYR GLU GLY ALA TYR          
SEQRES  23 A  342  HIS VAL LEU HIS LYS GLU LEU PRO GLU VAL THR ASN SER          
SEQRES  24 A  342  VAL PHE HIS GLU ILE ASN MET TRP VAL SER GLN ARG THR          
SEQRES  25 A  342  ALA THR ALA GLY THR ALA SER PRO PRO LEU GLU VAL ASP          
SEQRES  26 A  342  LEU GLN GLY ASP HIS GLY LEU SER ALA TRP SER HIS PRO          
SEQRES  27 A  342  GLN PHE GLU LYS                                              
SEQRES   1 B  342  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY ALA GLY          
SEQRES   2 B  342  ASP ARG GLY PRO GLU PHE PRO GLU GLU SER SER PRO ARG          
SEQRES   3 B  342  ARG THR PRO GLN SER ILE PRO TYR GLN ASP LEU PRO HIS          
SEQRES   4 B  342  LEU VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS ARG TYR          
SEQRES   5 B  342  TRP LYS PRO THR GLY THR PRO LYS ALA LEU ILE PHE VAL          
SEQRES   6 B  342  SER HIS GLY ALA GLY GLU HIS SER GLY ARG TYR GLU GLU          
SEQRES   7 B  342  LEU ALA ARG MET LEU MET GLY LEU ASP LEU LEU VAL PHE          
SEQRES   8 B  342  ALA HIS ASP HIS VAL GLY HIS GLY GLN SER GLU GLY GLU          
SEQRES   9 B  342  ARG MET VAL VAL SER ASP PHE HIS VAL PHE VAL ARG ASP          
SEQRES  10 B  342  VAL LEU GLN HIS VAL ASP SER MET GLN LYS ASP TYR PRO          
SEQRES  11 B  342  GLY LEU PRO VAL PHE LEU LEU GLY HIS SER MET GLY GLY          
SEQRES  12 B  342  ALA ILE ALA ILE LEU THR ALA ALA GLU ARG PRO GLY HIS          
SEQRES  13 B  342  PHE ALA GLY MET VAL LEU ILE SER PRO LEU VAL LEU ALA          
SEQRES  14 B  342  ASN PRO GLU SER ALA THR THR PHE LYS VAL LEU ALA ALA          
SEQRES  15 B  342  LYS VAL LEU ASN LEU VAL LEU PRO ASN LEU SER LEU GLY          
SEQRES  16 B  342  PRO ILE ASP SER SER VAL LEU SER ARG ASN LYS THR GLU          
SEQRES  17 B  342  VAL ASP ILE TYR ASN SER ASP PRO LEU ILE CYS ARG ALA          
SEQRES  18 B  342  GLY LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU ASN ALA          
SEQRES  19 B  342  VAL SER ARG VAL GLU ARG ALA LEU PRO LYS LEU THR VAL          
SEQRES  20 B  342  PRO PHE LEU LEU LEU GLN GLY SER ALA ASP ARG LEU CYS          
SEQRES  21 B  342  ASP SER LYS GLY ALA TYR LEU LEU MET GLU LEU ALA LYS          
SEQRES  22 B  342  SER GLN ASP LYS THR LEU LYS ILE TYR GLU GLY ALA TYR          
SEQRES  23 B  342  HIS VAL LEU HIS LYS GLU LEU PRO GLU VAL THR ASN SER          
SEQRES  24 B  342  VAL PHE HIS GLU ILE ASN MET TRP VAL SER GLN ARG THR          
SEQRES  25 B  342  ALA THR ALA GLY THR ALA SER PRO PRO LEU GLU VAL ASP          
SEQRES  26 B  342  LEU GLN GLY ASP HIS GLY LEU SER ALA TRP SER HIS PRO          
SEQRES  27 B  342  GLN PHE GLU LYS                                              
HET    GOL  A 417       6                                                       
HET    GOL  B 410       6                                                       
HETNAM     GOL GLYCEROL                                                         
FORMUL   3  GOL    2(C3 H8 O3)                                                  
FORMUL   5  HOH   *177(H2 O)                                                    
HELIX    1   1 HIS A   54  ARG A   57  5                                   4    
HELIX    2   2 TYR A   58  GLY A   67  1                                  10    
HELIX    3   3 PHE A   93  TYR A  111  1                                  19    
HELIX    4   4 SER A  122  ARG A  135  1                                  14    
HELIX    5   5 THR A  157  LEU A  171  1                                  15    
HELIX    6   6 ASP A  180  LEU A  184  5                                   5    
HELIX    7   7 ASN A  187  SER A  196  1                                  10    
HELIX    8   8 LYS A  206  LEU A  224  1                                  19    
HELIX    9   9 PRO A  225  LEU A  227  5                                   3    
HELIX   10  10 ASP A  243  ALA A  254  1                                  12    
HELIX   11  11 VAL A  270  GLU A  274  5                                   5    
HELIX   12  12 LEU A  275  THR A  296  1                                  22    
HELIX   13  13 PRO B   15  LEU B   19  5                                   5    
HELIX   14  14 HIS B   54  ARG B   57  5                                   4    
HELIX   15  15 TYR B   58  LEU B   68  1                                  11    
HELIX   16  16 PHE B   93  TYR B  111  1                                  19    
HELIX   17  17 SER B  122  ARG B  135  1                                  14    
HELIX   18  18 SER B  155  LYS B  160  1                                   6    
HELIX   19  19 VAL B  161  VAL B  166  1                                   6    
HELIX   20  20 ASP B  180  LEU B  184  5                                   5    
HELIX   21  21 ASN B  187  ASP B  197  1                                  11    
HELIX   22  22 LYS B  206  LEU B  224  1                                  19    
HELIX   23  23 PRO B  225  LEU B  227  5                                   3    
HELIX   24  24 ASP B  243  ALA B  254  1                                  12    
HELIX   25  25 VAL B  270  GLU B  274  5                                   5    
HELIX   26  26 LEU B  275  ARG B  293  1                                  19    
SHEET    1   A16 HIS A  21  VAL A  23  0                                        
SHEET    2   A16 TYR A  29  TRP A  35 -1  O  LEU A  30   N  LEU A  22           
SHEET    3   A16 LEU A  70  HIS A  75 -1  O  VAL A  72   N  TRP A  35           
SHEET    4   A16 ALA A  43  SER A  48  1  N  ALA A  43   O  LEU A  71           
SHEET    5   A16 VAL A 116  HIS A 121  1  O  PHE A 117   N  LEU A  44           
SHEET    6   A16 GLY A 141  ILE A 145  1  O  ILE A 145   N  GLY A 120           
SHEET    7   A16 PHE A 231  GLY A 236  1  O  LEU A 232   N  LEU A 144           
SHEET    8   A16 LYS A 259  TYR A 264  1  O  TYR A 264   N  GLN A 235           
SHEET    9   A16 LYS B 259  TYR B 264 -1  O  LEU B 261   N  LEU A 261           
SHEET   10   A16 PHE B 231  GLY B 236  1  N  LEU B 233   O  LYS B 262           
SHEET   11   A16 GLY B 141  ILE B 145  1  N  LEU B 144   O  LEU B 232           
SHEET   12   A16 VAL B 116  HIS B 121  1  N  GLY B 120   O  ILE B 145           
SHEET   13   A16 ALA B  43  SER B  48  1  N  SER B  48   O  LEU B 119           
SHEET   14   A16 LEU B  70  HIS B  75  1  O  LEU B  71   N  ALA B  43           
SHEET   15   A16 TYR B  29  TRP B  35 -1  N  TRP B  35   O  VAL B  72           
SHEET   16   A16 HIS B  21  VAL B  23 -1  N  LEU B  22   O  LEU B  30           
SITE     1 AC1  6 ALA A  51  GLU A  53  ARG A  57  HIS A 121                    
SITE     2 AC1  6 TYR A 194  VAL A 270                                          
SITE     1 AC2  5 GLY B  50  ALA B  51  GLU B  53  HIS B 121                    
SITE     2 AC2  5 VAL B 270                                                     
CRYST1   85.860  127.230  137.140  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      0.011647  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007860  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007292        0.00000                         
TER    2259      ALA A 297                                                      
TER    4518      THR B 296                                                      
MASTER      518    0    2   26   16    0    4    6 4705    2   12   54          
END                                                                             

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Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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