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LongText Report for: 5A7F-pdb

Name Class
5A7F-pdb
HEADER    HYDROLASE                               03-JUL-15   5A7F              
TITLE     COMPARISON OF THE STRUCTURE AND ACTIVITY OF GLYCOSYLATED              
TITLE    2 AND AGLYCOSYLATED HUMAN CARBOXYLESTERASE 1                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIVER CARBOXYLESTERASE 1;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 21-553;                                       
COMPND   5 SYNONYM: ACYL-COENZYME A- CHOLESTEROL ACYLTRANSFERASE, ACAT, BRAIN   
COMPND   6  CARBOXYLESTERASE HBR1, CARBOXYLESTERASE 1, CE-1, HCE-1, COCAINE     
COMPND   7  CARBOXYLESTERASE, EGASYN, HMSE, METHYLUMBELLIFERYL-ACETATE          
COMPND   8  DEACETYLASE 1, MONOCYTE/MACROPHAGE SERINE ESTERASE, RETINYL ESTER   
COMPND   9  HYDROLASE, REH, SERINE ESTERASE 1, TRIACYLGLYCEROL HYDROLASE, TGH,  
COMPND  10  CARBOXYLESTERASE 1;                                                 
COMPND  11 EC: 3.1.1.1, 3.1.1.1, 3.1.1.56;                                      
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: HEK 323;                                                  
SOURCE   6 ATCC: CRL-1573;                                                      
SOURCE   7 ORGAN: LIVER;                                                        
SOURCE   8 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   9 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  11 EXPRESSION_SYSTEM_CELL_LINE: HEK 323;                                
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: POPINTTG                                  
KEYWDS    HYDROLASE, ESTERASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.ARENA DE SOUZA,D.J.SCOTT,M.CHARLTON,M.A.WALSH,R.J.OWEN              
REVDAT   1   13-JAN-16 5A7F    0                                                
JRNL        AUTH   V.ARENA DE SOUZA,D.J.SCOTT,J.E.NETTLESHIP,N.RAHMAN,          
JRNL        AUTH 2 M.H.CHARLTON,M.A.WALSH,R.J.OWENS                             
JRNL        TITL   COMPARISON OF THE STRUCTURE AND ACTIVITY OF GLYCOSYLATED     
JRNL        TITL 2 AND AGLYCOSYLATED HUMAN CARBOXYLESTERASE 1.                  
JRNL        REF    PLOS ONE                      V.  10 43919 2015              
JRNL        REFN                   ISSN 1932-6203                               
JRNL        PMID   26657071                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0143919                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.86 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.94                          
REMARK   3   NUMBER OF REFLECTIONS             : 44506                          
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) : 0.15979                         
REMARK   3   R VALUE            (WORKING SET) : 0.15832                         
REMARK   3   FREE R VALUE                     : 0.18762                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2367                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.863                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.911                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2584                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 76.15                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.257                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 146                          
REMARK   3   BIN FREE R VALUE                    : 0.288                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4135                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 270                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.377                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.12                                                
REMARK   3    B22 (A**2) : -0.12                                                
REMARK   3    B33 (A**2) : 0.39                                                 
REMARK   3    B12 (A**2) : -0.12                                                
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.123         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.113         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.079         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.486         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4267 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4092 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5801 ; 1.630 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9453 ; 0.814 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   533 ; 5.797 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   173 ;33.464 ;24.740       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   717 ;13.297 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;20.170 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   644 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4771 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   926 ; 0.001 ; 0.020       
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):  2129 ; 1.227 ; 1.634       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2128 ; 1.226 ; 1.633       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2660 ; 1.984 ; 2.444       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2138 ; 1.988 ; 1.894       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3140 ; 2.953 ; 2.735       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    21        A   302                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.3340 -14.6230  32.3310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1431 T22:   0.1583                                     
REMARK   3      T33:   0.0084 T12:   0.0306                                     
REMARK   3      T13:   0.0133 T23:   0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7951 L22:   0.7387                                     
REMARK   3      L33:   0.2672 L12:  -0.3937                                     
REMARK   3      L13:  -0.0907 L23:   0.1362                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0213 S12:  -0.0474 S13:   0.0410                       
REMARK   3      S21:  -0.0112 S22:   0.0155 S23:  -0.0536                       
REMARK   3      S31:  -0.0091 S32:  -0.0276 S33:  -0.0367                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   303        A   552                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3800 -12.4690  28.4360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1482 T22:   0.1764                                     
REMARK   3      T33:   0.0180 T12:   0.0250                                     
REMARK   3      T13:   0.0223 T23:   0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4352 L22:   1.0009                                     
REMARK   3      L33:   0.4545 L12:   0.1620                                     
REMARK   3      L13:   0.0048 L23:  -0.0381                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0586 S12:   0.0822 S13:  -0.0468                       
REMARK   3      S21:  -0.1223 S22:   0.0547 S23:   0.0874                       
REMARK   3      S31:   0.0211 S32:  -0.1182 S33:   0.0039                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 5A7F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JUL-15.                  
REMARK 100 THE PDBE ID CODE IS EBI-64251.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 315)                  
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46879                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.86                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 2.8                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.40                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.43                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.80                               
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: PDB ENTRY 2H7C                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.8                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN AT 20C IN            
REMARK 280  0.1 M MES/IMIDAZOLE, PH 6.5 CONTAINING 0.03 M EACH OF               
REMARK 280  DIETHYLENE GLYCOL, TRIETHYLENE GLYCOL, TETRAETHYLENE                
REMARK 280  GLYCOL, PENTAETHYLENE GLYCOL, 10 % (W/V) POLYETHYLENE               
REMARK 280  GLYCOL 4000, 20% (W/V) GLYCEROL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  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       57.35750            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       33.11537            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       39.26000            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       57.35750            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       33.11537            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       39.26000            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       57.35750            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       33.11537            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       39.26000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.23074            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       78.52000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       66.23074            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       78.52000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       66.23074            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       78.52000            
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: TRIMERIC                          
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 58900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.5 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000       57.35750            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      -99.34610            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000      114.71500            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES 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  64   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 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    PHE A  76     -153.16     62.60                                   
REMARK 500    ALA A  80       62.79   -101.09                                   
REMARK 500    SER A 185       82.72   -159.49                                   
REMARK 500    SER A 221     -119.81     59.36                                   
REMARK 500    MET A 326      -62.10   -120.51                                   
REMARK 500    THR A 343       45.26    -90.51                                   
REMARK 500    TRP A 357      -53.49   -154.35                                   
REMARK 500    PHE A 425      -54.31   -123.61                                   
REMARK 500    ASN A 520     -156.13   -108.49                                   
REMARK 500    ALA A 551       40.56    -78.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 N-ACETYL-D-GLUCOSAMINE (NAG): GLYCOSYLATION SITE N79                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1554                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1555                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800  NAG A1553  BOUND TO ASN A  79                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5A7G   RELATED DB: PDB                                   
REMARK 900  COMPARISON OF THE STRUCTURE AND ACTIVITY OF GLYCOSYLATED            
REMARK 900   AND AGLYCOSYLATED HUMAN CARBOXYLESTERASE 1                         
REMARK 900 RELATED ID: 5A7H   RELATED DB: PDB                                   
REMARK 900  COMPARISON OF THE STRUCTURE AND ACTIVITY OF GLYCOSYLATED            
REMARK 900   AND AGLYCOSYLATED HUMAN CARBOXYLESTERASE 1                         
DBREF  5A7F A   21   552  UNP    P23141-3 EST1_HUMAN      21    552             
SEQRES   1 A  532  SER SER PRO PRO VAL VAL ASP THR VAL HIS GLY LYS VAL          
SEQRES   2 A  532  LEU GLY LYS PHE VAL SER LEU GLU GLY PHE ALA GLN PRO          
SEQRES   3 A  532  VAL ALA ILE PHE LEU GLY ILE PRO PHE ALA LYS PRO PRO          
SEQRES   4 A  532  LEU GLY PRO LEU ARG PHE THR PRO PRO GLN PRO ALA GLU          
SEQRES   5 A  532  PRO TRP SER PHE VAL LYS ASN ALA THR SER TYR PRO PRO          
SEQRES   6 A  532  MET CYS THR GLN ASP PRO LYS ALA GLY GLN LEU LEU SER          
SEQRES   7 A  532  GLU LEU PHE THR ASN ARG LYS GLU ASN ILE PRO LEU LYS          
SEQRES   8 A  532  LEU SER GLU ASP CYS LEU TYR LEU ASN ILE TYR THR PRO          
SEQRES   9 A  532  ALA ASP LEU THR LYS LYS ASN ARG LEU PRO VAL MET VAL          
SEQRES  10 A  532  TRP ILE HIS GLY GLY GLY LEU MET VAL GLY ALA ALA SER          
SEQRES  11 A  532  THR TYR ASP GLY LEU ALA LEU ALA ALA HIS GLU ASN VAL          
SEQRES  12 A  532  VAL VAL VAL THR ILE GLN TYR ARG LEU GLY ILE TRP GLY          
SEQRES  13 A  532  PHE PHE SER THR GLY ASP GLU HIS SER ARG GLY ASN TRP          
SEQRES  14 A  532  GLY HIS LEU ASP GLN VAL ALA ALA LEU ARG TRP VAL GLN          
SEQRES  15 A  532  ASP ASN ILE ALA SER PHE GLY GLY ASN PRO GLY SER VAL          
SEQRES  16 A  532  THR ILE PHE GLY GLU SER ALA GLY GLY GLU SER VAL SER          
SEQRES  17 A  532  VAL LEU VAL LEU SER PRO LEU ALA LYS ASN LEU PHE HIS          
SEQRES  18 A  532  ARG ALA ILE SER GLU SER GLY VAL ALA LEU THR SER VAL          
SEQRES  19 A  532  LEU VAL LYS LYS GLY ASP VAL LYS PRO LEU ALA GLU GLN          
SEQRES  20 A  532  ILE ALA ILE THR ALA GLY CYS LYS THR THR THR SER ALA          
SEQRES  21 A  532  VAL MET VAL HIS CYS LEU ARG GLN LYS THR GLU GLU GLU          
SEQRES  22 A  532  LEU LEU GLU THR THR LEU LYS MET LYS PHE LEU SER LEU          
SEQRES  23 A  532  ASP LEU GLN GLY ASP PRO ARG GLU SER GLN PRO LEU LEU          
SEQRES  24 A  532  GLY THR VAL ILE ASP GLY MET LEU LEU LEU LYS THR PRO          
SEQRES  25 A  532  GLU GLU LEU GLN ALA GLU ARG ASN PHE HIS THR VAL PRO          
SEQRES  26 A  532  TYR MET VAL GLY ILE ASN LYS GLN GLU PHE GLY TRP LEU          
SEQRES  27 A  532  ILE PRO MET LEU MET SER TYR PRO LEU SER GLU GLY GLN          
SEQRES  28 A  532  LEU ASP GLN LYS THR ALA MET SER LEU LEU TRP LYS SER          
SEQRES  29 A  532  TYR PRO LEU VAL CYS ILE ALA LYS GLU LEU ILE PRO GLU          
SEQRES  30 A  532  ALA THR GLU LYS TYR LEU GLY GLY THR ASP ASP THR VAL          
SEQRES  31 A  532  LYS LYS LYS ASP LEU PHE LEU ASP LEU ILE ALA ASP VAL          
SEQRES  32 A  532  MET PHE GLY VAL PRO SER VAL ILE VAL ALA ARG ASN HIS          
SEQRES  33 A  532  ARG ASP ALA GLY ALA PRO THR TYR MET TYR GLU PHE GLN          
SEQRES  34 A  532  TYR ARG PRO SER PHE SER SER ASP MET LYS PRO LYS THR          
SEQRES  35 A  532  VAL ILE GLY ASP HIS GLY ASP GLU LEU PHE SER VAL PHE          
SEQRES  36 A  532  GLY ALA PRO PHE LEU LYS GLU GLY ALA SER GLU GLU GLU          
SEQRES  37 A  532  ILE ARG LEU SER LYS MET VAL MET LYS PHE TRP ALA ASN          
SEQRES  38 A  532  PHE ALA ARG ASN GLY ASN PRO ASN GLY GLU GLY LEU PRO          
SEQRES  39 A  532  HIS TRP PRO GLU TYR ASN GLN LYS GLU GLY TYR LEU GLN          
SEQRES  40 A  532  ILE GLY ALA ASN THR GLN ALA ALA GLN LYS LEU LYS ASP          
SEQRES  41 A  532  LYS GLU VAL ALA PHE TRP THR ASN LEU PHE ALA LYS              
MODRES 5A7F ASN A   79  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1553      14                                                       
HET    PO4  A1554       5                                                       
HET    PO4  A1555       5                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   3  PO4    2(O4 P 3-)                                                   
FORMUL   5  HOH   *270(H2 O)                                                    
HELIX    1   1 LEU A   60  ARG A   64  5                                   5    
HELIX    2   2 ASP A   90  THR A  102  1                                  13    
HELIX    3   3 GLY A  154  ASN A  162  1                                   9    
HELIX    4   4 LEU A  172  PHE A  178  1                                   7    
HELIX    5   5 ASN A  188  ILE A  205  1                                  18    
HELIX    6   6 ALA A  206  PHE A  208  5                                   3    
HELIX    7   7 SER A  221  LEU A  232  1                                  12    
HELIX    8   8 SER A  233  LYS A  237  5                                   5    
HELIX    9   9 THR A  252  VAL A  254  5                                   3    
HELIX   10  10 VAL A  261  GLY A  273  1                                  13    
HELIX   11  11 THR A  278  LYS A  289  1                                  12    
HELIX   12  12 THR A  290  LYS A  302  1                                  13    
HELIX   13  13 ASP A  311  SER A  315  5                                   5    
HELIX   14  14 THR A  331  GLU A  338  1                                   8    
HELIX   15  15 TRP A  357  MET A  363  1                                   7    
HELIX   16  16 ASP A  373  SER A  384  1                                  12    
HELIX   17  17 SER A  384  CYS A  389  1                                   6    
HELIX   18  18 ALA A  391  GLU A  393  5                                   3    
HELIX   19  19 LEU A  394  GLY A  404  1                                  11    
HELIX   20  20 ASP A  408  PHE A  425  1                                  18    
HELIX   21  21 PHE A  425  ALA A  439  1                                  15    
HELIX   22  22 GLU A  470  PHE A  475  1                                   6    
HELIX   23  23 GLY A  476  LYS A  481  1                                   6    
HELIX   24  24 SER A  485  GLY A  506  1                                  22    
HELIX   25  25 LYS A  539  ALA A  551  1                                  13    
SHEET    1  AA 3 VAL A  25  THR A  28  0                                        
SHEET    2  AA 3 GLY A  31  LEU A  34 -1  O  GLY A  31   N  THR A  28           
SHEET    3  AA 3 VAL A  77  ASN A  79  1  O  LYS A  78   N  LEU A  34           
SHEET    1  AB11 LYS A  36  VAL A  38  0                                        
SHEET    2  AB11 VAL A  47  PRO A  54 -1  O  VAL A  47   N  VAL A  38           
SHEET    3  AB11 TYR A 118  THR A 123 -1  O  LEU A 119   N  ILE A  53           
SHEET    4  AB11 VAL A 164  ILE A 168 -1  O  VAL A 165   N  TYR A 122           
SHEET    5  AB11 LEU A 133  ILE A 139  1  O  PRO A 134   N  VAL A 164           
SHEET    6  AB11 GLY A 210  GLU A 220  1  N  ASN A 211   O  LEU A 133           
SHEET    7  AB11 ARG A 242  GLU A 246  1  O  ARG A 242   N  ILE A 217           
SHEET    8  AB11 TYR A 346  ASN A 351  1  O  MET A 347   N  SER A 245           
SHEET    9  AB11 THR A 443  GLN A 449  1  O  TYR A 444   N  VAL A 348           
SHEET   10  AB11 GLY A 524  GLY A 529  1  O  LEU A 526   N  GLU A 447           
SHEET   11  AB11 GLN A 533  GLN A 536 -1  O  GLN A 533   N  GLN A 527           
SHEET    1  AC 2 MET A  86  CYS A  87  0                                        
SHEET    2  AC 2 LEU A 112  SER A 113  1  N  SER A 113   O  MET A  86           
SHEET    1  AD 2 VAL A 256  LYS A 257  0                                        
SHEET    2  AD 2 THR A 321  VAL A 322  1  O  THR A 321   N  LYS A 257           
SSBOND   1 CYS A   87    CYS A  116                          1555   1555  1.95  
SSBOND   2 CYS A  274    CYS A  285                          1555   1555  2.11  
LINK         ND2 ASN A  79                 C1  NAG A1553     1555   1555  1.45  
SITE     1 AC1  7 ALA A 236  LYS A 237  ASN A 238  LEU A 239                    
SITE     2 AC1  7 PHE A 240  HIS A 342  VAL A 344                               
SITE     1 AC2  5 ARG A  64  HIS A 284  GLN A 288  LYS A 289                    
SITE     2 AC2  5 HOH A2037                                                     
SITE     1 AC3  3 ASN A  79  THR A  81  SER A  82                               
CRYST1  114.715  114.715  117.780  90.00  90.00 120.00 H 3           9          
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      0.008717  0.005033  0.000000        0.00000                         
SCALE2      0.000000  0.010066  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008490        0.00000                         
TER    4136      LYS A 552                                                      
MASTER      369    0    3   25   18    0    5    6 4429    1   29   41          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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