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LongText Report for: 7prm-pdb

Name Class
7prm-pdb
HEADER    HYDROLASE                               22-SEP-21   7PRM              
TITLE     CRYSTAL STRUCTURE OF HUMAN MONOGLYCERIDE LIPASE WITH COMPOUND 13      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MONOGLYCERIDE LIPASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MGL,HU-K5,LYSOPHOSPHOLIPASE HOMOLOG,LYSOPHOSPHOLIPASE-LIKE, 
COMPND   5 MONOACYLGLYCEROL LIPASE,MAGL;                                        
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                                         
KEYWDS    ALPHA/BETA HYDROLASE, HYDROLASE, SERINE ESTERASE;                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.GRETHER,L.GOBBI,B.KUHN,L.COLLIN,L.LEIBROCK,D.HEER,M.WITTWER,J.BENZ  
REVDAT   1   16-FEB-22 7PRM    0                                                
JRNL        AUTH   Y.HE,M.SCHILD,U.GRETHER,J.BENZ,L.LEIBROCK,D.HEER,A.TOPP,     
JRNL        AUTH 2 L.COLLIN,B.KUHN,M.WITTWER,C.KELLER,L.C.GOBBI,R.SCHIBLI,L.MU  
JRNL        TITL   DEVELOPMENT OF HIGH BRAIN-PENETRANT AND REVERSIBLE           
JRNL        TITL 2 MONOACYLGLYCEROL LIPASE PET TRACERS FOR NEUROIMAGING.        
JRNL        REF    J.MED.CHEM.                                2022              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   35089028                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.1C01706                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.8                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 43732                          
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)  : 0.208                          
REMARK   3   R VALUE            (WORKING SET)  : 0.206                          
REMARK   3   FREE R VALUE                      : 0.238                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : NULL                           
REMARK   3   FREE R VALUE TEST SET COUNT       : 2134                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : NULL                     
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.65                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.66                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.54                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : NULL                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL                     
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : NULL                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.4915                   
REMARK   3   BIN FREE R VALUE                        : 0.5022                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : NULL                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 45                       
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            : 2283                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 312                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.48                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.21060                                             
REMARK   3    B22 (A**2) : 3.98390                                              
REMARK   3    B33 (A**2) : 0.22680                                              
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) : 0.290               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.104               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.101               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.097               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.097               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.963                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2439   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3329   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 855    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 422    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2439   ; 10.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 309    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 2431   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.93                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.24                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 15.55                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   118.159   21.1037    0.0476           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.3247 T22:   -0.1471                                    
REMARK   3     T33:   -0.1383 T12:   -0.0156                                    
REMARK   3     T13:   -0.0053 T23:   -0.0056                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3245 L22:    3.4212                                    
REMARK   3     L33:    0.9209 L12:   -0.7734                                    
REMARK   3     L13:   -0.0124 L23:    0.1922                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0266 S12:    0.0836 S13:   -0.0995                     
REMARK   3     S21:    0.0836 S22:      0.04 S23:    0.0759                     
REMARK   3     S31:   -0.0995 S32:    0.0759 S33:   -0.0134                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7PRM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-SEP-21.                  
REMARK 100 THE DEPOSITION ID IS D_1292118256.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-FEB-21                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.999883                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SADABS                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43782                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.770                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08500                            
REMARK 200   FOR THE DATA SET  : 8.4700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.88                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.99000                            
REMARK 200   FOR SHELL         : 0.620                              
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: IN HOUSE MAGL STRUCTURE                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES 6.5 PH 6 %W/V PEG MME 5000     
REMARK 280  12 %V/V ISO-PROPANOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
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                                         
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       31.51650            
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       31.51650            
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       44.98350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       63.72400            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       44.98350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       63.72400            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       31.51650            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       44.98350            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       63.72400            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       31.51650            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       44.98350            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       63.72400            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 450 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 12660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 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 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 A 783  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   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     ASN A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     TYR A    -3                                                      
REMARK 465     PHE A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     THR A   296                                                      
REMARK 465     ALA A   297                                                      
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 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  53     -155.93   -110.58                                   
REMARK 500    ASP A  69       33.23     70.05                                   
REMARK 500    SER A 122     -123.60     60.42                                   
REMARK 500    GLU A 274     -160.17   -102.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7PRM A    1   303  UNP    Q99685   MGLL_HUMAN       1    303             
SEQADV 7PRM MET A  -19  UNP  Q99685              INITIATING METHIONINE          
SEQADV 7PRM GLY A  -18  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM SER A  -17  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM SER A  -16  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM HIS A  -15  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM HIS A  -14  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM HIS A  -13  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM HIS A  -12  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM HIS A  -11  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM HIS A  -10  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM SER A   -9  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM SER A   -8  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM GLY A   -7  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM GLU A   -6  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM ASN A   -5  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM LEU A   -4  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM TYR A   -3  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM PHE A   -2  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM GLN A   -1  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM GLY A    0  UNP  Q99685              EXPRESSION TAG                 
SEQADV 7PRM ALA A   36  UNP  Q99685    LYS    36 ENGINEERED MUTATION            
SEQADV 7PRM SER A  169  UNP  Q99685    LEU   169 ENGINEERED MUTATION            
SEQADV 7PRM SER A  176  UNP  Q99685    LEU   176 ENGINEERED MUTATION            
SEQRES   1 A  323  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  323  GLU ASN LEU TYR PHE GLN GLY MET PRO GLU GLU SER SER          
SEQRES   3 A  323  PRO ARG ARG THR PRO GLN SER ILE PRO TYR GLN ASP LEU          
SEQRES   4 A  323  PRO HIS LEU VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS          
SEQRES   5 A  323  ARG TYR TRP ALA PRO THR GLY THR PRO LYS ALA LEU ILE          
SEQRES   6 A  323  PHE VAL SER HIS GLY ALA GLY GLU HIS SER GLY ARG TYR          
SEQRES   7 A  323  GLU GLU LEU ALA ARG MET LEU MET GLY LEU ASP LEU LEU          
SEQRES   8 A  323  VAL PHE ALA HIS ASP HIS VAL GLY HIS GLY GLN SER GLU          
SEQRES   9 A  323  GLY GLU ARG MET VAL VAL SER ASP PHE HIS VAL PHE VAL          
SEQRES  10 A  323  ARG ASP VAL LEU GLN HIS VAL ASP SER MET GLN LYS ASP          
SEQRES  11 A  323  TYR PRO GLY LEU PRO VAL PHE LEU LEU GLY HIS SER MET          
SEQRES  12 A  323  GLY GLY ALA ILE ALA ILE LEU THR ALA ALA GLU ARG PRO          
SEQRES  13 A  323  GLY HIS PHE ALA GLY MET VAL LEU ILE SER PRO LEU VAL          
SEQRES  14 A  323  LEU ALA ASN PRO GLU SER ALA THR THR PHE LYS VAL LEU          
SEQRES  15 A  323  ALA ALA LYS VAL LEU ASN SER VAL LEU PRO ASN LEU SER          
SEQRES  16 A  323  SER GLY PRO ILE ASP SER SER VAL LEU SER ARG ASN LYS          
SEQRES  17 A  323  THR GLU VAL ASP ILE TYR ASN SER ASP PRO LEU ILE CYS          
SEQRES  18 A  323  ARG ALA GLY LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU          
SEQRES  19 A  323  ASN ALA VAL SER ARG VAL GLU ARG ALA LEU PRO LYS LEU          
SEQRES  20 A  323  THR VAL PRO PHE LEU LEU LEU GLN GLY SER ALA ASP ARG          
SEQRES  21 A  323  LEU CYS ASP SER LYS GLY ALA TYR LEU LEU MET GLU LEU          
SEQRES  22 A  323  ALA LYS SER GLN ASP LYS THR LEU LYS ILE TYR GLU GLY          
SEQRES  23 A  323  ALA TYR HIS VAL LEU HIS LYS GLU LEU PRO GLU VAL THR          
SEQRES  24 A  323  ASN SER VAL PHE HIS GLU ILE ASN MET TRP VAL SER GLN          
SEQRES  25 A  323  ARG THR ALA THR ALA GLY THR ALA SER PRO PRO                  
HET    81I  A 401      32                                                       
HET    EDO  A 402       4                                                       
HET    EDO  A 403       4                                                       
HETNAM     81I (4~{R})-1-[4-(4-FLUOROPHENYL)PHENYL]-4-[4-(FURAN-2-              
HETNAM   2 81I  YLCARBONYL)PIPERAZIN-1-YL]PYRROLIDIN-2-ONE                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  81I    C25 H24 F N3 O3                                              
FORMUL   3  EDO    2(C2 H6 O2)                                                  
FORMUL   5  HOH   *312(H2 O)                                                    
HELIX    1 AA1 PRO A   15  LEU A   19  5                                   5    
HELIX    2 AA2 HIS A   54  ARG A   57  5                                   4    
HELIX    3 AA3 TYR A   58  LEU A   68  1                                  11    
HELIX    4 AA4 PHE A   93  TYR A  111  1                                  19    
HELIX    5 AA5 MET A  123  ARG A  135  1                                  13    
HELIX    6 AA6 ASN A  152  SER A  169  1                                  18    
HELIX    7 AA7 ASP A  180  LEU A  184  5                                   5    
HELIX    8 AA8 ASN A  187  ASP A  197  1                                  11    
HELIX    9 AA9 LYS A  206  LEU A  224  1                                  19    
HELIX   10 AB1 PRO A  225  LEU A  227  5                                   3    
HELIX   11 AB2 ASP A  243  ALA A  254  1                                  12    
HELIX   12 AB3 VAL A  270  GLU A  274  5                                   5    
HELIX   13 AB4 LEU A  275  ARG A  293  1                                  19    
SHEET    1 AA1 8 HIS A  21  VAL A  23  0                                        
SHEET    2 AA1 8 TYR A  29  TRP A  35 -1  O  LEU A  30   N  LEU A  22           
SHEET    3 AA1 8 LEU A  71  HIS A  75 -1  O  VAL A  72   N  TRP A  35           
SHEET    4 AA1 8 LEU A  44  SER A  48  1  N  ILE A  45   O  PHE A  73           
SHEET    5 AA1 8 VAL A 116  SER A 122  1  O  LEU A 119   N  SER A  48           
SHEET    6 AA1 8 GLY A 141  PRO A 147  1  O  VAL A 143   N  LEU A 118           
SHEET    7 AA1 8 PHE A 231  GLY A 236  1  O  LEU A 234   N  SER A 146           
SHEET    8 AA1 8 LYS A 259  TYR A 264  1  O  THR A 260   N  LEU A 233           
CRYST1   89.967  127.448   63.033  90.00  90.00  90.00 C 2 2 21      8          
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      0.011115  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007846  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015865        0.00000                         
TER    2331      ALA A 295                                                      
MASTER      313    0    3   13    8    0    0    6 2635    1   40   25          
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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