Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 4AB1-pdb

Name Class
4AB1-pdb
HEADER    HYDROLASE                               06-DEC-11   4AB1              
TITLE     RECOMBINANT HUMAN CARBOXYLESTERASE 1 FROM WHOLE CABBAGE               
TITLE    2 LOOPERS                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIVER CARBOXYLESTERASE 1;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 21-553;                                           
COMPND   5 SYNONYM: ACYL-COENZYME A\:CHOLESTEROL ACYLTRANSFERASE, ACAT, BRAIN   
COMPND   6  CARBOXYLESTERASE HBR1, COCAINE CARBOXYLESTERASE, EGASYN, HMSE,      
COMPND   7  METHYLUMBELLIFERYL-ACETATE DEACETYLASE 1, MONOCYTE/MACROPHAGE       
COMPND   8  SERINE ESTERASE, RETINYL ESTER HYDROLASE, REH, SERINE ESTERASE 1,   
COMPND   9  TRIACYLGLYCEROL HYDROLASE, TGH;                                     
COMPND  10 EC: 3.1.1.1, 3.1.1.56;                                               
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: LIVER;                                                        
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    HYDROLASE, WHOLE INSECT EXPRESSION SYSTEMS                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.M.GREENBLATT,T.OTTO,D.M.CERASOLI,J.L.SUSSMAN                        
REVDAT   1   07-MAR-12 4AB1    0                                                
JRNL        AUTH   H.M.GREENBLATT,T.OTTO,M.G.KIRKPATRICK,E.KOVALEVA,S.BROWN,    
JRNL        AUTH 2 G.BUCHMAN,D.M.CERASOLI,J.L.SUSSMAN                           
JRNL        TITL   STRUCTURE OF RECOMBINANT HUMAN CARBOXYLESTERASE 1 ISOLATED   
JRNL        TITL 2 FROM WHOLE CABBAGE LOOPER LARVAE                             
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V. F68   269 2012              
JRNL        REFN                   ISSN 1744-3091                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 47.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.80                          
REMARK   3   NUMBER OF REFLECTIONS             : 33751                          
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) : 0.18141                         
REMARK   3   R VALUE            (WORKING SET) : 0.17846                         
REMARK   3   FREE R VALUE                     : 0.23578                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.2                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1846                            
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) : 2.201                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.258                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2163                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.195                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 122                          
REMARK   3   BIN FREE R VALUE                    : 0.289                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3989                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 241                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.008                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.85                                                 
REMARK   3    B22 (A**2) : 0.85                                                 
REMARK   3    B33 (A**2) : -1.28                                                
REMARK   3    B12 (A**2) : 0.43                                                 
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): 0.202         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.188         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.118         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.573         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4115 ; 0.020 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5603 ; 1.979 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   522 ; 6.327 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   160 ;33.273 ;24.500       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   643 ;15.832 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;19.841 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   632 ; 0.142 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3107 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2178 ; 0.247 ;   0.2       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2817 ; 0.316 ;   0.2       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   148 ;  0.15 ;  0.20       
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):    61 ; 0.258 ;   0.2       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.201 ;   0.2       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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   : 1.20                                          
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 RIDING   
REMARK   3  POSITIONS. U VALUES REFINED INDIVIDUALLY.                           
REMARK   4                                                                      
REMARK   4 4AB1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-DEC-11.                  
REMARK 100 THE PDBE ID CODE IS EBI-50592.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8726                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (MAR225)                       
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35646                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.20                               
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 16.8                               
REMARK 200  R MERGE                    (I) : 0.12                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.60                               
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) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.1                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2HRQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: DROP WAS 45% PROTEIN SOLUTION            
REMARK 280  (11MG/ML) OF 50 MM TRIS, PH7.6, 150 MM NACL, MIXED WITH 45%         
REMARK 280  2 M AMMONIUM SULFATE, 0.1 M BIS-TRIS, PH 5.5, AND 10% 2 M           
REMARK 280  NASCN.                                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
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,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-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 -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        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       88.55000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       88.55000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       88.55000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       88.55000            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       88.55000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       88.55000            
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 21520 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 105320 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -133.5 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 -1.000000  0.000000  0.000000      114.84300            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       88.55000            
REMARK 350   BIOMT1   3  0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000       88.55000            
REMARK 350   BIOMT1   4 -0.500000 -0.866025  0.000000      114.84300            
REMARK 350   BIOMT2   4  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5 -0.500000  0.866025  0.000000       57.42150            
REMARK 350   BIOMT2   5 -0.866025 -0.500000  0.000000       99.45696            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   6  0.500000 -0.866025  0.000000       57.42150            
REMARK 350   BIOMT2   6 -0.866025 -0.500000  0.000000       99.45696            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000       88.55000            
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 A2167  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A2241  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     SER A    21                                                      
REMARK 465     GLU A   338                                                      
REMARK 465     ARG A   339                                                      
REMARK 465     ASN A   340                                                      
REMARK 465     PHE A   341                                                      
REMARK 465     HIS A   342                                                      
REMARK 465     SER A   369                                                      
REMARK 465     LYS A   553                                                      
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     LYS A  36    CD   CE   NZ                                        
REMARK 470     GLU A  41    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  92    CG   CD   CE   NZ                                   
REMARK 470     LYS A 105    CG   CD   CE   NZ                                   
REMARK 470     GLU A 106    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 111    CD   CE   NZ                                        
REMARK 470     LYS A 129    CD   CE   NZ                                        
REMARK 470     LYS A 237    CD   CE   NZ                                        
REMARK 470     LYS A 257    CE   NZ                                             
REMARK 470     LYS A 258    CG   CD   CE   NZ                                   
REMARK 470     GLN A 267    CD   OE1  NE2                                       
REMARK 470     LYS A 275    CE   NZ                                             
REMARK 470     LEU A 304    CD1  CD2                                            
REMARK 470     LEU A 308    CD1  CD2                                            
REMARK 470     GLU A 314    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 330    CD   CE   NZ                                        
REMARK 470     GLU A 333    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 336    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 376    CD   CE   NZ                                        
REMARK 470     GLU A 394    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 411    CG1  CG2                                            
REMARK 470     LYS A 414    CE   NZ                                             
REMARK 470     LYS A 462    CD   CE   NZ                                        
REMARK 470     GLU A 483    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 512    CG   CD   OE1  OE2                                  
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   NE   ARG A   452     O    HOH A  2193              2.13            
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    TRP A 175   CD2   TRP A 175   CE2     0.076                       
REMARK 500    MET A 361   C     LEU A 363   N       0.219                       
REMARK 500    TRP A 383   CD2   TRP A 383   CE2     0.075                       
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 104   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG A 186   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    LEU A 251   CA  -  CB  -  CG  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    MET A 361   CA  -  C   -  N   ANGL. DEV. =  14.4 DEGREES          
REMARK 500    MET A 361   O   -  C   -  N   ANGL. DEV. = -20.2 DEGREES          
REMARK 500    LEU A 420   CA  -  CB  -  CG  ANGL. DEV. =  15.7 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    ALA A  80       58.79   -117.90                                   
REMARK 500    LYS A 129       49.72   -101.39                                   
REMARK 500    SER A 185       79.65   -153.19                                   
REMARK 500    SER A 214       80.54   -154.64                                   
REMARK 500    SER A 221     -120.87     66.67                                   
REMARK 500    THR A 252        0.42     58.08                                   
REMARK 500    TRP A 357      -61.69   -162.03                                   
REMARK 500    ASP A 409      105.77    -54.78                                   
REMARK 500    ASN A 521     -150.35   -108.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    MET A 361        -11.46                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR A 252        23.9      L          L   OUTSIDE RANGE           
REMARK 500    GLN A 375        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ARG A 505        20.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1553                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1554                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1555                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A1079 BOUND TO ASN A  79                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MX1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE                   
REMARK 900  INCOMPLEX WITH TACRINE                                              
REMARK 900 RELATED ID: 1MX5   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE                   
REMARK 900  INCOMPLEXED WITH HOMATROPINE, A COCAINE ANALOGUE                    
REMARK 900 RELATED ID: 1MX9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE                   
REMARK 900  INCOMPLEXED WITH NALOXONE METHIODIDE, A HEROIN ANALOGUE             
REMARK 900 RELATED ID: 1YA4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE 1                 
REMARK 900  INCOMPLEX WITH TAMOXIFEN                                            
REMARK 900 RELATED ID: 1YA8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE                   
REMARK 900  INCOMPLEX WITH CLEAVAGE PRODUCTS OF MEVASTATIN                      
REMARK 900 RELATED ID: 1YAH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE                   
REMARK 900  COMPLEXEDTO ETYL ACETATE; A FATTY ACID ETHYL ESTER                  
REMARK 900  ANALOGUE                                                            
REMARK 900 RELATED ID: 1YAJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN LIVER CARBOXYLESTERASE                   
REMARK 900  INCOMPLEX WITH BENZIL                                               
DBREF  4AB1 A   21   553  UNP    P23141   EST1_HUMAN      21    553             
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              
HET    NAG  A1079      14                                                       
HET    SCN  A1553       3                                                       
HET    SCN  A1554       3                                                       
HET    SCN  A1555       3                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     SCN THIOCYANATE ION                                                  
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   3  SCN    3(C N S 1-)                                                  
FORMUL   4  HOH   *241(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  SER A  233  1                                  13    
HELIX    8   8 PRO A  234  LYS A  237  5                                   4    
HELIX    9   9 VAL A  261  ALA A  272  1                                  12    
HELIX   10  10 THR A  278  LYS A  289  1                                  12    
HELIX   11  11 THR A  290  LYS A  302  1                                  13    
HELIX   12  12 THR A  331  ALA A  337  1                                   7    
HELIX   13  13 TRP A  357  MET A  364  1                                   7    
HELIX   14  14 ASP A  374  SER A  385  1                                  12    
HELIX   15  15 SER A  385  CYS A  390  1                                   6    
HELIX   16  16 LEU A  395  GLY A  405  1                                  11    
HELIX   17  17 VAL A  411  PHE A  426  1                                  16    
HELIX   18  18 PHE A  426  ALA A  440  1                                  15    
HELIX   19  19 GLU A  471  PHE A  476  1                                   6    
HELIX   20  20 GLY A  477  LEU A  481  5                                   5    
HELIX   21  21 SER A  486  GLY A  507  1                                  22    
HELIX   22  22 LYS A  540  ALA A  552  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 LYS A  78  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 444  GLN A 450  1  O  TYR A 445   N  VAL A 348           
SHEET   10  AB11 GLY A 525  GLY A 530  1  O  LEU A 527   N  GLU A 448           
SHEET   11  AB11 GLN A 534  GLN A 537 -1  O  GLN A 534   N  GLN A 528           
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  2.02  
SSBOND   2 CYS A  274    CYS A  285                          1555   1555  2.13  
LINK         ND2 ASN A  79                 C1  NAG A1079     1555   1555  1.43  
SITE     1 AC1  5 ALA A 250  THR A 252  THR A 331  PRO A 332                    
SITE     2 AC1  5 GLU A 333                                                     
SITE     1 AC2  3 GLY A  61  PRO A  62  GLN A 288                               
SITE     1 AC3  6 SER A  75  PHE A  76  ASP A 182  GLU A 183                    
SITE     2 AC3  6 ARG A 186  HOH A2153                                          
SITE     1 AC4  2 ASN A  79  THR A  81                                          
CRYST1  114.843  114.843  177.100  90.00  90.00 120.00 P 63 2 2     12          
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      0.008708  0.005027  0.000000        0.00000                         
SCALE2      0.000000  0.010055  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005647        0.00000                         
TER    3990      ALA A 552                                                      
MASTER      494    0    4   22   18    0    6    6 4253    1   28   41          
END                                                                             

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

Acknowledgements and disclaimer