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LongText Report for: 1N5R-pdb

Name Class
1N5R-pdb
HEADER    HYDROLASE                               07-NOV-02   1N5R              
TITLE     CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                  
TITLE    2 PROPIDIUM COMPLEX                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND   5 EC: 3.1.1.7;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   5 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   6 EXPRESSION_SYSTEM_VARIANT: LAMBDA-ZAP, LAMBDA-FIX CDNA,              
SOURCE   7 GENOMIC DNA;                                                         
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293;                                
SOURCE   9 EXPRESSION_SYSTEM_CELL: HUMAN EMBRYONIC KIDNEY CELLS (HEK)           
KEYWDS    HYDROLASE, SERINE ESTERASE, ACETYLCHOLINESTERASE, HOMODIMER,          
KEYWDS   2 HYDROLASE FOLD, GLYCOSYLATED PROTEIN                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.BOURNE,P.TAYLOR,Z.RADIC,P.MARCHOT                                   
REVDAT   1   04-FEB-03 1N5R    0                                                
JRNL        AUTH   Y.BOURNE,P.TAYLOR,Z.RADIC,P.MARCHOT                          
JRNL        TITL   STRUCTURAL INSIGHTS INTO LIGAND INTERACTIONS AT              
JRNL        TITL 2 THE ACETYLCHOLINESTERASE PERIPHERAL ANIONIC SITE             
JRNL        REF    EMBO J.                       V.  22     1 2003              
JRNL        REFN   ASTM EMJODG  UK ISSN 0261-4189                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.25 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 95908                          
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 SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1907                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.39                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 15466                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE                    : 0.3220                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 1.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 302                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8349                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 113                                     
REMARK   3   SOLVENT ATOMS            : 428                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.58000                                              
REMARK   3    B22 (A**2) : 15.14000                                             
REMARK   3    B33 (A**2) : -24.72000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.34                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.33                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.38                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.21                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.340 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.210 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.140 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.190 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 43.86                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : LIG.PARAM                                      
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : LIG.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1N5R COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-DEC-2002.                
REMARK 100 THE RCSB ID CODE IS RCSB017552.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-EH2                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95908                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.790                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04100                            
REMARK 200   FOR THE DATA SET  : 13.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.4                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 600, DODIUM ACETATE, PH 6.5-         
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 253K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   1/2-X,-Y,1/2+Z                                          
REMARK 290       3555   -X,1/2+Y,1/2-Z                                          
REMARK 290       4555   1/2+X,1/2-Y,-Z                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       39.77600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.41700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.83250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.41700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.77600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.83250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 APPLY THE FOLLOWING TO CHAINS: A, B, D                               
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     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     THR A   543                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     PRO B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     GLY B   264                                                      
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 496    CG    CD    CE    NZ                                
REMARK 470     ARG B 493    CG    CD    NE    CZ    NH1   NH2                   
REMARK 470     SER B 495    OG                                                  
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),F6.3)                  
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET A  48   CE    MET A  48   SD     0.077                        
REMARK 500    MET A 211   SD    MET A 211   CG    -0.095                        
REMARK 500    PRO A 258   CG    PRO A 258   CB     0.121                        
REMARK 500    PRO A 258   CD    PRO A 258   CG     0.072                        
REMARK 500    PRO A 446   CG    PRO A 446   CB     0.093                        
REMARK 500    PRO B  41   CG    PRO B  41   CB     0.075                        
REMARK 500    MET B  48   CE    MET B  48   SD     0.098                        
REMARK 500    MET B 149   CE    MET B 149   SD     0.078                        
REMARK 500    MET B 477   CE    MET B 477   SD    -0.102                        
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: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL A 145   N   -  CA  -  C   ANGL. DEV. = -9.9 DEGREES           
REMARK 500    PHE A 158   N   -  CA  -  C   ANGL. DEV. = 10.1 DEGREES           
REMARK 500    LEU A 161   CA  -  CB  -  CG  ANGL. DEV. =-14.2 DEGREES           
REMARK 500    LEU A 161   N   -  CA  -  C   ANGL. DEV. =-12.8 DEGREES           
REMARK 500    PRO A 235   N   -  CA  -  C   ANGL. DEV. = 10.5 DEGREES           
REMARK 500    GLU A 292   N   -  CA  -  C   ANGL. DEV. =-10.2 DEGREES           
REMARK 500    GLY A 422   N   -  CA  -  C   ANGL. DEV. = 11.0 DEGREES           
REMARK 500    ILE A 429   N   -  CA  -  C   ANGL. DEV. =-10.2 DEGREES           
REMARK 500    VAL A 445   N   -  CA  -  C   ANGL. DEV. =-10.0 DEGREES           
REMARK 500    LEU B 161   N   -  CA  -  C   ANGL. DEV. =-13.1 DEGREES           
REMARK 500    PRO B 235   N   -  CA  -  C   ANGL. DEV. = 10.9 DEGREES           
REMARK 500    GLU B 292   N   -  CA  -  C   ANGL. DEV. =-11.1 DEGREES           
REMARK 500    SER B 298   N   -  CA  -  C   ANGL. DEV. = 10.3 DEGREES           
REMARK 500    GLY B 422   N   -  CA  -  C   ANGL. DEV. = 10.4 DEGREES           
REMARK 500    VAL B 445   N   -  CA  -  C   ANGL. DEV. =-10.8 DEGREES           
REMARK 500    SER B 497   N   -  CA  -  C   ANGL. DEV. =  9.9 DEGREES           
REMARK 500    PRO B 498   C   -  N   -  CA  ANGL. DEV. = 14.8 DEGREES           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 203     -119.93     58.83                                   
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED            
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE                 
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL                 
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH   504        DISTANCE =  5.57 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1MAA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1MAH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1N5M   RELATED DB: PDB                                   
REMARK 900 GALLAMINE COMPLEX                                                    
REMARK 900 RELATED ID: 1J06   RELATED DB: PDB                                   
REMARK 900 APO FORM                                                             
REMARK 900 RELATED ID: 1J07   RELATED DB: PDB                                   
REMARK 900 DECIDIUM COMPLEX                                                     
DBREF  1N5R A    1   543  SWS    P21836   ACES_MOUSE      32    574             
DBREF  1N5R B    1   543  SWS    P21836   ACES_MOUSE      32    574             
SEQRES   1 A  543  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 A  543  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 A  543  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 A  543  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 A  543  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 A  543  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 A  543  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 A  543  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 A  543  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 A  543  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 A  543  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 A  543  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 A  543  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 A  543  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 A  543  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 A  543  SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER          
SEQRES  17 A  543  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 A  543  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 A  543  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 A  543  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 A  543  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 A  543  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 A  543  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 A  543  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 A  543  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 A  543  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 A  543  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 A  543  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 A  543  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 A  543  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 A  543  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 A  543  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 A  543  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 A  543  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 A  543  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 A  543  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 A  543  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 A  543  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 A  543  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 A  543  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 A  543  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 A  543  ARG PHE LEU PRO LYS LEU LEU SER ALA THR                      
SEQRES   1 B  543  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 B  543  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 B  543  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 B  543  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 B  543  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 B  543  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 B  543  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 B  543  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 B  543  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 B  543  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 B  543  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 B  543  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 B  543  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 B  543  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 B  543  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 B  543  SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER          
SEQRES  17 B  543  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 B  543  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 B  543  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 B  543  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 B  543  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 B  543  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 B  543  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 B  543  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 B  543  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 B  543  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 B  543  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 B  543  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 B  543  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 B  543  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 B  543  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 B  543  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 B  543  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 B  543  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 B  543  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 B  543  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 B  543  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 B  543  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 B  543  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 B  543  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 B  543  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 B  543  ARG PHE LEU PRO LYS LEU LEU SER ALA THR                      
MODRES 1N5R ASN A  350  ASN  GLYCOSYLATION SITE                                 
MODRES 1N5R ASN A  464  ASN  GLYCOSYLATION SITE                                 
MODRES 1N5R ASN B  350  ASN  GLYCOSYLATION SITE                                 
HET    NAG  D 501      14                                                       
HET    FUC  D 502      10                                                       
HET    NAG  B 601      14                                                       
HET    NAG  A 701      14                                                       
HET    P6G    901      19                                                       
HET    PG4    902      11                                                       
HET    PRM    951      31                                                       
HET    ACY    904       4                                                       
HET    ACY    905       4                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC FUCOSE                                                           
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     PRM 3,8-DIAMINO-5[3-(DIETHYLMETHYLAMMONIO)PROPYL]-6-                 
HETNAM   2 PRM  PHENYLPHENANTHRIDINIUM                                          
HETNAM     ACY ACETIC ACID                                                      
HETSYN     NAG NAG                                                              
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
HETSYN     PG4 POLYETHYLENE GLYCOL PEG400                                       
HETSYN     PRM PROPIDIUM                                                        
FORMUL   3  NAG    3(C8 H15 N1 O6)                                              
FORMUL   3  FUC    C6 H12 O5                                                    
FORMUL   6  P6G    C12 H26 O7                                                   
FORMUL   7  PG4    C8 H18 O5                                                    
FORMUL   8  PRM    C27 H34 N4 2+                                                
FORMUL   9  ACY    2(C2 H4 O2)                                                  
FORMUL  11  HOH   *420(H2 O1)                                                   
HELIX    1   1 ASP A    5  GLN A    7  5                                   3    
HELIX    2   2 VAL A   42  ARG A   46  5                                   5    
HELIX    3   3 PHE A   80  MET A   85  1                                   6    
HELIX    4   4 LEU A  130  ASP A  134  5                                   5    
HELIX    5   5 GLY A  135  GLY A  143  1                                   9    
HELIX    6   6 VAL A  153  LEU A  159  1                                   7    
HELIX    7   7 ASN A  170  ILE A  187  1                                  18    
HELIX    8   8 ALA A  188  PHE A  190  5                                   3    
HELIX    9   9 SER A  203  LEU A  214  1                                  12    
HELIX   10  10 SER A  215  SER A  220  1                                   6    
HELIX   11  11 SER A  240  VAL A  255  1                                  16    
HELIX   12  12 ASN A  265  THR A  275  1                                  11    
HELIX   13  13 PRO A  277  GLU A  285  1                                   9    
HELIX   14  14 TRP A  286  LEU A  289  5                                   4    
HELIX   15  15 THR A  311  GLY A  319  1                                   9    
HELIX   16  16 GLY A  335  VAL A  340  1                                   6    
HELIX   17  17 SER A  355  VAL A  367  1                                  13    
HELIX   18  18 SER A  371  THR A  383  1                                  13    
HELIX   19  19 ASP A  390  VAL A  407  1                                  18    
HELIX   20  20 VAL A  407  GLN A  421  1                                  15    
HELIX   21  21 PRO A  440  GLY A  444  5                                   5    
HELIX   22  22 GLU A  450  PHE A  455  1                                   6    
HELIX   23  23 GLY A  456  ASN A  464  5                                   9    
HELIX   24  24 THR A  466  GLY A  487  1                                  22    
HELIX   25  25 ARG A  525  ARG A  534  1                                  10    
HELIX   26  26 ARG A  534  SER A  541  1                                   8    
HELIX   27  27 VAL B   42  ARG B   46  5                                   5    
HELIX   28  28 PHE B   80  MET B   85  1                                   6    
HELIX   29  29 LEU B  130  ASP B  134  5                                   5    
HELIX   30  30 GLY B  135  GLY B  143  1                                   9    
HELIX   31  31 VAL B  153  LEU B  159  1                                   7    
HELIX   32  32 ASN B  170  ILE B  187  1                                  18    
HELIX   33  33 ALA B  188  PHE B  190  5                                   3    
HELIX   34  34 SER B  203  LEU B  214  1                                  12    
HELIX   35  35 SER B  215  SER B  220  1                                   6    
HELIX   36  36 SER B  240  VAL B  255  1                                  16    
HELIX   37  37 ASN B  265  THR B  275  1                                  11    
HELIX   38  38 PRO B  277  GLU B  285  1                                   9    
HELIX   39  39 TRP B  286  LEU B  289  5                                   4    
HELIX   40  40 THR B  311  GLY B  319  1                                   9    
HELIX   41  41 GLY B  335  VAL B  340  1                                   6    
HELIX   42  42 SER B  355  VAL B  367  1                                  13    
HELIX   43  43 SER B  371  THR B  383  1                                  13    
HELIX   44  44 ASP B  390  VAL B  407  1                                  18    
HELIX   45  45 VAL B  407  GLN B  421  1                                  15    
HELIX   46  46 PRO B  440  GLY B  444  5                                   5    
HELIX   47  47 GLU B  450  PHE B  455  1                                   6    
HELIX   48  48 GLY B  456  ASN B  464  5                                   9    
HELIX   49  49 THR B  466  GLY B  487  1                                  22    
HELIX   50  50 ARG B  525  ARG B  534  1                                  10    
HELIX   51  51 ARG B  534  SER B  541  1                                   8    
SHEET    1   A 3 LEU A   9  VAL A  12  0                                        
SHEET    2   A 3 GLY A  15  ARG A  18 -1  O  LEU A  17   N  VAL A  10           
SHEET    3   A 3 VAL A  59  ASP A  61  1  O  LEU A  60   N  GLN A  16           
SHEET    1   B11 ILE A  20  ALA A  24  0                                        
SHEET    2   B11 GLY A  27  PRO A  36 -1  O  VAL A  29   N  LEU A  22           
SHEET    3   B11 TYR A  98  PRO A 104 -1  O  VAL A 101   N  PHE A  32           
SHEET    4   B11 VAL A 145  MET A 149 -1  O  SER A 148   N  ASN A 100           
SHEET    5   B11 THR A 112  ILE A 118  1  N  TRP A 117   O  VAL A 147           
SHEET    6   B11 GLY A 192  GLU A 202  1  O  SER A 196   N  VAL A 114           
SHEET    7   B11 ARG A 224  GLN A 228  1  O  GLN A 228   N  GLY A 201           
SHEET    8   B11 GLN A 325  VAL A 331  1  O  LEU A 327   N  LEU A 227           
SHEET    9   B11 ARG A 424  PHE A 430  1  O  ARG A 424   N  VAL A 326           
SHEET   10   B11 GLN A 509  LEU A 513  1  O  LEU A 513   N  ILE A 429           
SHEET   11   B11 GLU A 519  ARG A 522 -1  O  ARG A 521   N  TYR A 510           
SHEET    1   C 2 VAL A  68  CYS A  69  0                                        
SHEET    2   C 2 LEU A  92  SER A  93  1  O  SER A  93   N  VAL A  68           
SHEET    1   D 3 LEU B   9  VAL B  12  0                                        
SHEET    2   D 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3   D 3 VAL B  59  ASP B  61  1  O  LEU B  60   N  GLN B  16           
SHEET    1   E11 ILE B  20  ALA B  24  0                                        
SHEET    2   E11 GLY B  27  PRO B  36 -1  O  VAL B  29   N  LEU B  22           
SHEET    3   E11 TYR B  98  PRO B 104 -1  O  VAL B 101   N  PHE B  32           
SHEET    4   E11 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100           
SHEET    5   E11 THR B 112  ILE B 118  1  N  TRP B 117   O  VAL B 147           
SHEET    6   E11 GLY B 192  GLU B 202  1  O  THR B 198   N  ILE B 116           
SHEET    7   E11 ARG B 224  GLN B 228  1  O  GLN B 228   N  GLY B 201           
SHEET    8   E11 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227           
SHEET    9   E11 ARG B 424  PHE B 430  1  O  ARG B 424   N  VAL B 326           
SHEET   10   E11 GLN B 509  LEU B 513  1  O  LEU B 513   N  ILE B 429           
SHEET   11   E11 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1   F 2 VAL B  68  CYS B  69  0                                        
SHEET    2   F 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68           
SSBOND   1 CYS A   69    CYS A   96                                             
SSBOND   2 CYS A  257    CYS A  272                                             
SSBOND   3 CYS A  409    CYS A  529                                             
SSBOND   4 CYS B   69    CYS B   96                                             
SSBOND   5 CYS B  257    CYS B  272                                             
SSBOND   6 CYS B  409    CYS B  529                                             
LINK         ND2 ASN A 350                 C1  NAG D 501                        
LINK         ND2 ASN A 464                 C1  NAG A 701                        
LINK         ND2 ASN B 350                 C1  NAG B 601                        
LINK         O6  NAG D 501                 C1  FUC D 502                        
CISPEP   1 TYR A  105    PRO A  106          0        -0.24                     
CISPEP   2 TYR B  105    PRO B  106          0         0.14                     
CISPEP   3 CYS B  257    PRO B  258          0        -0.18                     
CISPEP   4 SER B  497    PRO B  498          0         0.28                     
CRYST1   79.552  111.665  226.834  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012570  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008955  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004409        0.00000                         
TER    4185      ALA A 542                                                      
TER    8351      THR B 543                                                      
MASTER      337    0    9   51   32    0    0    6 8890    2  136   84          
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
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