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LongText Report for: 7bo4-pdb

Name Class
7bo4-pdb
HEADER    HYDROLASE                               23-JAN-21   7BO4              
TITLE     HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH 3-(2-(BUTYL(2-            
TITLE    2 CYCLOHEPTYLETHYL)AMINO)ETHYL)-1H-INDOL-6-OL                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLINESTERASE;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE   
COMPND   5 ESTERASE II,PSEUDOCHOLINESTERASE;                                    
COMPND   6 EC: 3.1.1.8;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BCHE, CHE1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    BUTYRYLCHOLINESTERASE, COMPLEX, INHIBITOR, HYDROLASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.BRAZZOLOTTO,A.MEDEN,D.KNEZ,F.NACHON,S.GOBEC                         
REVDAT   1   02-MAR-22 7BO4    0                                                
JRNL        AUTH   X.BRAZZOLOTTO,A.MEDEN,A.KNEZ,F.NACHON,S.GOBEC                
JRNL        TITL   HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH                  
JRNL        TITL 2 3-(2-(BUTYL(2-CYCLOHEPTYLETHYL)AMINO)ETHYL)-1H-INDOL-6-OL    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.19_4092                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.40                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 30662                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1534                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.1100 -  5.3400    1.00     2825   149  0.1838 0.2159        
REMARK   3     2  5.3400 -  4.2400    1.00     2696   142  0.1469 0.1788        
REMARK   3     3  4.2400 -  3.7000    1.00     2685   141  0.1534 0.1668        
REMARK   3     4  3.7000 -  3.3600    1.00     2641   139  0.1734 0.2223        
REMARK   3     5  3.3600 -  3.1200    1.00     2647   140  0.2016 0.2210        
REMARK   3     6  3.1200 -  2.9400    1.00     2645   139  0.2132 0.2524        
REMARK   3     7  2.9400 -  2.7900    1.00     2633   138  0.2180 0.2633        
REMARK   3     8  2.7900 -  2.6700    1.00     2618   138  0.2347 0.2993        
REMARK   3     9  2.6700 -  2.5700    1.00     2628   139  0.2609 0.3462        
REMARK   3    10  2.5700 -  2.4800    1.00     2612   137  0.2683 0.3302        
REMARK   3    11  2.4800 -  2.4010    0.96     2498   132  0.2687 0.3542        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.305            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.987           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 57.14                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           4651                                  
REMARK   3   ANGLE     :  0.941           6327                                  
REMARK   3   CHIRALITY :  0.056            709                                  
REMARK   3   PLANARITY :  0.008            784                                  
REMARK   3   DIHEDRAL  : 12.476            699                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 209 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  20.2758  28.9230  26.0899              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5411 T22:   0.4430                                     
REMARK   3      T33:   0.4139 T12:  -0.0573                                     
REMARK   3      T13:   0.0455 T23:   0.0432                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6149 L22:   2.2191                                     
REMARK   3      L33:   1.6893 L12:  -0.0327                                     
REMARK   3      L13:  -0.2279 L23:  -0.0256                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0753 S12:   0.2665 S13:   0.0234                       
REMARK   3      S21:  -0.4997 S22:   0.0856 S23:  -0.0704                       
REMARK   3      S31:   0.0547 S32:   0.1007 S33:  -0.0435                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 210 THROUGH 316 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.3390  38.3503  33.1931              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4840 T22:   0.5126                                     
REMARK   3      T33:   0.5432 T12:   0.0114                                     
REMARK   3      T13:  -0.0253 T23:   0.0708                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5030 L22:   2.7049                                     
REMARK   3      L33:   3.2907 L12:  -0.2968                                     
REMARK   3      L13:   0.1232 L23:  -1.5740                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1266 S12:   0.1646 S13:   0.4895                       
REMARK   3      S21:  -0.0847 S22:   0.2349 S23:   0.2433                       
REMARK   3      S31:  -0.5272 S32:  -0.4281 S33:  -0.1216                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 317 THROUGH 397 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.8654  44.8679  57.5900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5337 T22:   0.4972                                     
REMARK   3      T33:   0.4626 T12:  -0.0331                                     
REMARK   3      T13:   0.0820 T23:  -0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3067 L22:   4.0446                                     
REMARK   3      L33:   2.5523 L12:   0.7567                                     
REMARK   3      L13:  -1.2909 L23:   1.0553                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2274 S12:  -0.6275 S13:   0.4029                       
REMARK   3      S21:   0.3491 S22:   0.1088 S23:   0.0391                       
REMARK   3      S31:  -0.4330 S32:   0.1732 S33:  -0.3302                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 398 THROUGH 529 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.4242  24.9280  50.4615              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3777 T22:   0.4171                                     
REMARK   3      T33:   0.2994 T12:   0.0133                                     
REMARK   3      T13:  -0.0266 T23:   0.0653                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0229 L22:   3.6351                                     
REMARK   3      L33:   2.4283 L12:   0.1807                                     
REMARK   3      L13:  -0.8116 L23:   0.4693                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0191 S12:  -0.3782 S13:  -0.0429                       
REMARK   3      S21:   0.2215 S22:   0.0346 S23:  -0.0817                       
REMARK   3      S31:   0.0842 S32:   0.2569 S33:  -0.0226                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7BO4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-JAN-21.                  
REMARK 100 THE DEPOSITION ID IS D_1292113648.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-SEP-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97856                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30671                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.401                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 26.90                              
REMARK 200  R MERGE                    (I) : 0.15480                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.5100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.17900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.840                              
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: 1P0I                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       77.65000            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       77.65000            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       64.03000            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       77.65000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       77.65000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       64.03000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       77.65000            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       77.65000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       64.03000            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       77.65000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       77.65000            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       64.03000            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       77.65000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       77.65000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       64.03000            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       77.65000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       77.65000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       64.03000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       77.65000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       77.65000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       64.03000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       77.65000            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       77.65000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       64.03000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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 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     GLU A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ASP A     3                                                      
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     GLN A 486    CG   CD   OE1  NE2                                  
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   NH2  ARG A   509     O    HOH A   701              2.09            
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  43      -13.04     80.78                                   
REMARK 500    ASP A  54     -168.70    -75.88                                   
REMARK 500    ALA A  58       69.37   -104.70                                   
REMARK 500    LYS A 103      125.20    -38.75                                   
REMARK 500    ASN A 106       51.76   -156.91                                   
REMARK 500    PHE A 118        9.01     59.54                                   
REMARK 500    PHE A 153       13.27   -144.68                                   
REMARK 500    ALA A 162       70.31   -164.50                                   
REMARK 500    SER A 198     -126.44     61.31                                   
REMARK 500    ASP A 297      -77.45   -129.53                                   
REMARK 500    SER A 338      140.89   -170.72                                   
REMARK 500    ASP A 378      112.31   -161.82                                   
REMARK 500    PHE A 398      -56.99   -134.05                                   
REMARK 500    ASN A 485       46.44   -101.23                                   
REMARK 500    GLU A 506      -90.62    -75.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7BO4 A    1   529  UNP    P06276   CHLE_HUMAN      29    557             
SEQADV 7BO4 GLN A   17  UNP  P06276    ASN    45 ENGINEERED MUTATION            
SEQADV 7BO4 GLN A  455  UNP  P06276    ASN   483 ENGINEERED MUTATION            
SEQADV 7BO4 GLN A  481  UNP  P06276    ASN   509 ENGINEERED MUTATION            
SEQADV 7BO4 GLN A  486  UNP  P06276    ASN   514 ENGINEERED MUTATION            
SEQRES   1 A  529  GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL          
SEQRES   2 A  529  ARG GLY MET GLN LEU THR VAL PHE GLY GLY THR VAL THR          
SEQRES   3 A  529  ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY          
SEQRES   4 A  529  ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP          
SEQRES   5 A  529  SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS          
SEQRES   6 A  529  CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY          
SEQRES   7 A  529  SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP          
SEQRES   8 A  529  CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO          
SEQRES   9 A  529  LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY          
SEQRES  10 A  529  PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY          
SEQRES  11 A  529  LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER          
SEQRES  12 A  529  MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU          
SEQRES  13 A  529  PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE          
SEQRES  14 A  529  ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE          
SEQRES  15 A  529  ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE          
SEQRES  16 A  529  GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU          
SEQRES  17 A  529  LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE          
SEQRES  18 A  529  LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR          
SEQRES  19 A  529  SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA          
SEQRES  20 A  529  LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE          
SEQRES  21 A  529  ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU          
SEQRES  22 A  529  LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU          
SEQRES  23 A  529  SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU          
SEQRES  24 A  529  THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE          
SEQRES  25 A  529  LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU          
SEQRES  26 A  529  GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER          
SEQRES  27 A  529  LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN          
SEQRES  28 A  529  GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE          
SEQRES  29 A  529  GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL          
SEQRES  30 A  529  ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY          
SEQRES  31 A  529  ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU          
SEQRES  32 A  529  GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA          
SEQRES  33 A  529  PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO          
SEQRES  34 A  529  TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE          
SEQRES  35 A  529  GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP GLN          
SEQRES  36 A  529  TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL          
SEQRES  37 A  529  LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO GLN          
SEQRES  38 A  529  GLU THR GLN ASN GLN SER THR SER TRP PRO VAL PHE LYS          
SEQRES  39 A  529  SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER          
SEQRES  40 A  529  THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG          
SEQRES  41 A  529  PHE TRP THR SER PHE PHE PRO LYS VAL                          
HET    NAG  B   1      14                                                       
HET    FUC  B   2      10                                                       
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    FUC  C   3      10                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    FUC  D   3      10                                                       
HET    NAG  E   1      14                                                       
HET    FUC  E   2      10                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    FUC  F   3      10                                                       
HET    NAG  A 601      14                                                       
HET    MES  A 602      12                                                       
HET    MOH  A 603       2                                                       
HET    A87  A 604      52                                                       
HET    SIA  A 605      21                                                       
HET    SO4  A 606       5                                                       
HET    SO4  A 607       5                                                       
HET    SO4  A 608       5                                                       
HET    SO4  A 609       5                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     MOH METHANOL                                                         
HETNAM     A87 3-[2-[BUTYL(2-CYCLOHEPTYLETHYL)AMINO]ETHYL]-1~{H}-               
HETNAM   2 A87  INDOL-6-OL                                                      
HETNAM     SIA N-ACETYL-ALPHA-NEURAMINIC ACID                                   
HETNAM     SO4 SULFATE ION                                                      
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-              
HETSYN   2 FUC  FUCOSE; FUCOSE                                                  
HETSYN     SIA N-ACETYLNEURAMINIC ACID; SIALIC ACID; ALPHA-SIALIC               
HETSYN   2 SIA  ACID; O-SIALIC ACID                                             
FORMUL   2  NAG    9(C8 H15 N O6)                                               
FORMUL   2  FUC    5(C6 H12 O5)                                                 
FORMUL   8  MES    C6 H13 N O4 S                                                
FORMUL   9  MOH    C H4 O                                                       
FORMUL  10  A87    C23 H36 N2 O                                                 
FORMUL  11  SIA    C11 H19 N O9                                                 
FORMUL  12  SO4    4(O4 S 2-)                                                   
FORMUL  16  HOH   *95(H2 O)                                                     
HELIX    1 AA1 LEU A   38  ARG A   42  5                                   5    
HELIX    2 AA2 PHE A   76  MET A   81  1                                   6    
HELIX    3 AA3 LEU A  125  ASP A  129  5                                   5    
HELIX    4 AA4 GLY A  130  ARG A  138  1                                   9    
HELIX    5 AA5 GLY A  149  LEU A  154  1                                   6    
HELIX    6 AA6 ASN A  165  ILE A  182  1                                  18    
HELIX    7 AA7 ALA A  183  PHE A  185  5                                   3    
HELIX    8 AA8 SER A  198  LEU A  208  1                                  11    
HELIX    9 AA9 SER A  210  PHE A  217  5                                   8    
HELIX   10 AB1 SER A  235  THR A  250  1                                  16    
HELIX   11 AB2 ASN A  256  ARG A  265  1                                  10    
HELIX   12 AB3 ASP A  268  ALA A  277  1                                  10    
HELIX   13 AB4 PHE A  278  VAL A  280  5                                   3    
HELIX   14 AB5 MET A  302  LEU A  309  1                                   8    
HELIX   15 AB6 GLY A  326  GLY A  333  5                                   8    
HELIX   16 AB7 THR A  346  PHE A  358  1                                  13    
HELIX   17 AB8 SER A  362  THR A  374  1                                  13    
HELIX   18 AB9 GLU A  383  PHE A  398  1                                  16    
HELIX   19 AC1 PHE A  398  GLU A  411  1                                  14    
HELIX   20 AC2 PRO A  431  GLY A  435  5                                   5    
HELIX   21 AC3 GLU A  441  PHE A  446  1                                   6    
HELIX   22 AC4 GLY A  447  GLU A  451  5                                   5    
HELIX   23 AC5 THR A  457  GLY A  478  1                                  22    
HELIX   24 AC6 ARG A  515  PHE A  525  1                                  11    
HELIX   25 AC7 PHE A  526  VAL A  529  5                                   4    
SHEET    1 AA1 3 ILE A   5  THR A   8  0                                        
SHEET    2 AA1 3 GLY A  11  ARG A  14 -1  O  GLY A  11   N  THR A   8           
SHEET    3 AA1 3 ILE A  55  ASN A  57  1  O  TRP A  56   N  ARG A  14           
SHEET    1 AA211 MET A  16  VAL A  20  0                                        
SHEET    2 AA211 GLY A  23  PRO A  32 -1  O  VAL A  25   N  LEU A  18           
SHEET    3 AA211 TYR A  94  PRO A 100 -1  O  VAL A  97   N  PHE A  28           
SHEET    4 AA211 ILE A 140  MET A 144 -1  O  SER A 143   N  ASN A  96           
SHEET    5 AA211 ALA A 107  ILE A 113  1  N  LEU A 110   O  ILE A 140           
SHEET    6 AA211 GLY A 187  GLU A 197  1  O  SER A 191   N  VAL A 109           
SHEET    7 AA211 ARG A 219  GLN A 223  1  O  GLN A 223   N  GLY A 196           
SHEET    8 AA211 ILE A 317  ASN A 322  1  O  LEU A 318   N  LEU A 222           
SHEET    9 AA211 ALA A 416  PHE A 421  1  O  PHE A 417   N  VAL A 319           
SHEET   10 AA211 LYS A 499  LEU A 503  1  O  LEU A 501   N  PHE A 418           
SHEET   11 AA211 ILE A 510  THR A 512 -1  O  MET A 511   N  TYR A 500           
SSBOND   1 CYS A   65    CYS A   92                          1555   1555  2.04  
SSBOND   2 CYS A  252    CYS A  263                          1555   1555  2.04  
SSBOND   3 CYS A  400    CYS A  519                          1555   1555  2.04  
LINK         ND2 ASN A  57                 C1  NAG B   1     1555   1555  1.45  
LINK         ND2 ASN A 106                 C1  NAG D   1     1555   1555  1.45  
LINK         ND2 ASN A 241                 C1  NAG C   1     1555   1555  1.46  
LINK         ND2 ASN A 256                 C1  NAG A 601     1555   1555  1.46  
LINK         ND2 ASN A 341                 C1  NAG F   1     1555   1555  1.46  
LINK         ND2 ASN A 485                 C1  NAG E   1     1555   1555  1.46  
LINK         O6  NAG B   1                 C1  FUC B   2     1555   1555  1.45  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.45  
LINK         O6  NAG C   1                 C1  FUC C   3     1555   1555  1.45  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.44  
LINK         O6  NAG D   1                 C1  FUC D   3     1555   1555  1.47  
LINK         O6  NAG E   1                 C1  FUC E   2     1555   1555  1.44  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.44  
LINK         O6  NAG F   1                 C1  FUC F   3     1555   1555  1.45  
CISPEP   1 ALA A  101    PRO A  102          0        -3.55                     
CRYST1  155.300  155.300  128.060  90.00  90.00  90.00 I 4 2 2      16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006439  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006439  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007809        0.00000                         
TER    4242      VAL A 529                                                      
MASTER      364    0   22   25   14    0    0    6 4543    1  295   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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