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LongText Report for: 3KOO-pdb

Name Class
3KOO-pdb
HEADER    HYDROLASE                               13-NOV-09   3KOO              
TITLE     CRYSTAL STRUCTURE OF SOLUBLE EPOXIDE HYDROLASE                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPOXIDE HYDROLASE 2;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SOLUBLE EPOXIDE HYDROLASE, SEH, EPOXIDE HYDRATASE, CYTOSOLIC
COMPND   5 EPOXIDE HYDROLASE, CEH;                                              
COMPND   6 EC: 3.3.2.10;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EPHX2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.A.FARROW                                                            
REVDAT   1   28-APR-10 3KOO    0                                                
JRNL        AUTH   A.B.ELDRUP,F.SOLEYMANZADEH,N.A.FARROW,A.KUKULKA,             
JRNL        AUTH 2 S.DE LOMBAERT                                                
JRNL        TITL   OPTIMIZATION OF PIPERIDYL-UREAS AS INHIBITORS OF SOLUBLE     
JRNL        TITL 2 EPOXIDE HYDROLASE.                                           
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  20   571 2010              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   19969453                                                     
JRNL        DOI    10.1016/J.BMCL.2009.11.091                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.5_2)                        
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.20                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.100                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 14809                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.307                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 736                             
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 48.2100 -  4.7710    0.97     3117   175  0.1910 0.2550        
REMARK   3     2  4.7710 -  3.7870    0.88     2644   146  0.2230 0.3480        
REMARK   3     3  3.7870 -  3.3090    0.97     2858   147  0.2130 0.3290        
REMARK   3     4  3.3090 -  3.0060    0.95     2804   140  0.2350 0.3540        
REMARK   3     5  3.0060 -  2.7910    0.91     2650   128  0.2620 0.3640        
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              : 0.33                                          
REMARK   3   B_SOL              : 58.36                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.500            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 77.03                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.53800                                              
REMARK   3    B22 (A**2) : 1.53800                                              
REMARK   3    B33 (A**2) : -3.07600                                             
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  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           4449                                  
REMARK   3   ANGLE     :  1.326           6028                                  
REMARK   3   CHIRALITY :  0.079            657                                  
REMARK   3   PLANARITY :  0.006            775                                  
REMARK   3   DIHEDRAL  : 21.613           1657                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3KOO COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB056254.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-04                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15463                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE, 36% PEG 2250,     
REMARK 280  0.1M TRIS PH 8.4, 0.6 UM B-HEXADECYL MALTOSIDE, VAPOR DIFFUSION     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      161.67733            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       80.83867            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      121.25800            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       40.41933            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      202.09667            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      161.67733            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       80.83867            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       40.41933            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      121.25800            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      202.09667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       91.76500            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      121.25800            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     PRO A   549                                                      
REMARK 465     PRO A   550                                                      
REMARK 465     VAL A   551                                                      
REMARK 465     VAL A   552                                                      
REMARK 465     SER A   553                                                      
REMARK 465     LYS A   554                                                      
REMARK 465     MET A   555                                                      
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   OD2  ASP A   205     OG1  THR A   208              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  17   C   -  N   -  CA  ANGL. DEV. = -10.0 DEGREES          
REMARK 500    PRO A 302   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  10      -82.57    -74.59                                   
REMARK 500    ARG A  34      130.03    -28.19                                   
REMARK 500    PRO A  83      155.03    -41.14                                   
REMARK 500    ASN A  85       36.47    -95.50                                   
REMARK 500    ARG A 130      170.22    -55.72                                   
REMARK 500    LYS A 144      -55.95    -13.78                                   
REMARK 500    PRO A 161       50.44   -105.46                                   
REMARK 500    GLN A 204      -88.08   -139.59                                   
REMARK 500    ALA A 226      100.71    -57.86                                   
REMARK 500    SER A 231     -158.74    -97.35                                   
REMARK 500    PRO A 234      -37.71    -33.04                                   
REMARK 500    ASP A 236        8.81    -66.69                                   
REMARK 500    GLU A 269     -141.63   -127.56                                   
REMARK 500    SER A 273        0.40    -65.41                                   
REMARK 500    ALA A 284      -17.28    -48.60                                   
REMARK 500    LYS A 294      127.93    -37.14                                   
REMARK 500    GLU A 311      -62.03    -18.00                                   
REMARK 500    ASP A 335     -135.84     57.53                                   
REMARK 500    TYR A 348       45.89   -141.86                                   
REMARK 500    ASN A 359      -55.66     75.45                                   
REMARK 500    SER A 374       10.41    -65.83                                   
REMARK 500    ASN A 378       78.67     59.49                                   
REMARK 500    VAL A 380        3.99    -62.10                                   
REMARK 500    GLN A 388      -52.90    -11.30                                   
REMARK 500    ALA A 411      172.30    -59.73                                   
REMARK 500    SER A 415      148.35    -38.24                                   
REMARK 500    VAL A 416       20.18   -142.71                                   
REMARK 500    MET A 419       20.67    -70.15                                   
REMARK 500    PRO A 433     -164.89    -64.45                                   
REMARK 500    PRO A 436      136.76    -37.53                                   
REMARK 500    LYS A 456      -75.50    -73.18                                   
REMARK 500    MET A 469      -58.01   -168.20                                   
REMARK 500    LYS A 495       46.72    -96.48                                   
REMARK 500    GLN A 505      -35.99    -36.52                                   
REMARK 500    HIS A 513       51.19   -102.50                                   
REMARK 500    LYS A 530       52.05   -148.46                                   
REMARK 500    ALA A 546     -101.30    -81.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 MET A  291     ASP A  292                  147.63                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU A  16        25.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 578        DISTANCE =  8.46 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 24D A 556                 
DBREF  3KOO A    1   555  UNP    P34913   HYES_HUMAN       1    555             
SEQRES   1 A  555  MET THR LEU ARG ALA ALA VAL PHE ASP LEU ASP GLY VAL          
SEQRES   2 A  555  LEU ALA LEU PRO ALA VAL PHE GLY VAL LEU GLY ARG THR          
SEQRES   3 A  555  GLU GLU ALA LEU ALA LEU PRO ARG GLY LEU LEU ASN ASP          
SEQRES   4 A  555  ALA PHE GLN LYS GLY GLY PRO GLU GLY ALA THR THR ARG          
SEQRES   5 A  555  LEU MET LYS GLY GLU ILE THR LEU SER GLN TRP ILE PRO          
SEQRES   6 A  555  LEU MET GLU GLU ASN CYS ARG LYS CYS SER GLU THR ALA          
SEQRES   7 A  555  LYS VAL CYS LEU PRO LYS ASN PHE SER ILE LYS GLU ILE          
SEQRES   8 A  555  PHE ASP LYS ALA ILE SER ALA ARG LYS ILE ASN ARG PRO          
SEQRES   9 A  555  MET LEU GLN ALA ALA LEU MET LEU ARG LYS LYS GLY PHE          
SEQRES  10 A  555  THR THR ALA ILE LEU THR ASN THR TRP LEU ASP ASP ARG          
SEQRES  11 A  555  ALA GLU ARG ASP GLY LEU ALA GLN LEU MET CYS GLU LEU          
SEQRES  12 A  555  LYS MET HIS PHE ASP PHE LEU ILE GLU SER CYS GLN VAL          
SEQRES  13 A  555  GLY MET VAL LYS PRO GLU PRO GLN ILE TYR LYS PHE LEU          
SEQRES  14 A  555  LEU ASP THR LEU LYS ALA SER PRO SER GLU VAL VAL PHE          
SEQRES  15 A  555  LEU ASP ASP ILE GLY ALA ASN LEU LYS PRO ALA ARG ASP          
SEQRES  16 A  555  LEU GLY MET VAL THR ILE LEU VAL GLN ASP THR ASP THR          
SEQRES  17 A  555  ALA LEU LYS GLU LEU GLU LYS VAL THR GLY ILE GLN LEU          
SEQRES  18 A  555  LEU ASN THR PRO ALA PRO LEU PRO THR SER CYS ASN PRO          
SEQRES  19 A  555  SER ASP MET SER HIS GLY TYR VAL THR VAL LYS PRO ARG          
SEQRES  20 A  555  VAL ARG LEU HIS PHE VAL GLU LEU GLY SER GLY PRO ALA          
SEQRES  21 A  555  VAL CYS LEU CYS HIS GLY PHE PRO GLU SER TRP TYR SER          
SEQRES  22 A  555  TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR          
SEQRES  23 A  555  ARG VAL LEU ALA MET ASP MET LYS GLY TYR GLY GLU SER          
SEQRES  24 A  555  SER ALA PRO PRO GLU ILE GLU GLU TYR CYS MET GLU VAL          
SEQRES  25 A  555  LEU CYS LYS GLU MET VAL THR PHE LEU ASP LYS LEU GLY          
SEQRES  26 A  555  LEU SER GLN ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY          
SEQRES  27 A  555  MET LEU VAL TRP TYR MET ALA LEU PHE TYR PRO GLU ARG          
SEQRES  28 A  555  VAL ARG ALA VAL ALA SER LEU ASN THR PRO PHE ILE PRO          
SEQRES  29 A  555  ALA ASN PRO ASN MET SER PRO LEU GLU SER ILE LYS ALA          
SEQRES  30 A  555  ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO          
SEQRES  31 A  555  GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN LEU SER ARG          
SEQRES  32 A  555  THR PHE LYS SER LEU PHE ARG ALA SER ASP GLU SER VAL          
SEQRES  33 A  555  LEU SER MET HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE          
SEQRES  34 A  555  VAL ASN SER PRO GLU GLU PRO SER LEU SER ARG MET VAL          
SEQRES  35 A  555  THR GLU GLU GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS          
SEQRES  36 A  555  LYS SER GLY PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN          
SEQRES  37 A  555  MET GLU ARG ASN TRP LYS TRP ALA CYS LYS SER LEU GLY          
SEQRES  38 A  555  ARG LYS ILE LEU ILE PRO ALA LEU MET VAL THR ALA GLU          
SEQRES  39 A  555  LYS ASP PHE VAL LEU VAL PRO GLN MET SER GLN HIS MET          
SEQRES  40 A  555  GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU          
SEQRES  41 A  555  ASP CYS GLY HIS TRP THR GLN MET ASP LYS PRO THR GLU          
SEQRES  42 A  555  VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP SER ASP ALA          
SEQRES  43 A  555  ARG ASN PRO PRO VAL VAL SER LYS MET                          
HET    24D  A 556      25                                                       
HETNAM     24D N-(2,4-DICHLOROBENZYL)-4-(PYRIMIDIN-2-YLOXY)PIPERIDINE-          
HETNAM   2 24D  1-CARBOXAMIDE                                                   
HETSYN     24D 4-(PYRIMIDIN-2-YLOXY)-PIPERIDINE-1-CARBOXYLIC ACID 2,4-          
HETSYN   2 24D  DICHLORO-BENZYLAMIDE                                            
FORMUL   2  24D    C17 H18 CL2 N4 O2                                            
FORMUL   3  HOH   *28(H2 O)                                                     
HELIX    1   1 ALA A   18  LEU A   30  1                                  13    
HELIX    2   2 GLY A   35  GLN A   42  1                                   8    
HELIX    3   3 LYS A   43  GLU A   47  5                                   5    
HELIX    4   4 GLY A   48  LYS A   55  1                                   8    
HELIX    5   5 THR A   59  ALA A   78  1                                  20    
HELIX    6   6 SER A   87  ARG A   99  1                                  13    
HELIX    7   7 ASN A  102  LYS A  115  1                                  14    
HELIX    8   8 ARG A  130  GLU A  132  5                                   3    
HELIX    9   9 ARG A  133  MET A  145  1                                  13    
HELIX   10  10 SER A  153  GLY A  157  1                                   5    
HELIX   11  11 GLU A  162  LYS A  174  1                                  13    
HELIX   12  12 SER A  176  SER A  178  5                                   3    
HELIX   13  13 ILE A  186  ASP A  195  1                                  10    
HELIX   14  14 ASP A  205  GLY A  218  1                                  14    
HELIX   15  15 ASN A  233  MET A  237  5                                   5    
HELIX   16  16 SER A  270  ARG A  275  5                                   6    
HELIX   17  17 TYR A  276  GLY A  285  1                                  10    
HELIX   18  18 GLU A  304  TYR A  308  5                                   5    
HELIX   19  19 CYS A  309  LYS A  323  1                                  15    
HELIX   20  20 ASP A  335  TYR A  348  1                                  14    
HELIX   21  21 LEU A  372  ALA A  377  1                                   6    
HELIX   22  22 ASN A  378  VAL A  380  5                                   3    
HELIX   23  23 PHE A  381  GLN A  388  1                                   8    
HELIX   24  24 GLY A  391  ASN A  400  1                                  10    
HELIX   25  25 ASN A  400  PHE A  409  1                                  10    
HELIX   26  26 LYS A  421  GLY A  426  1                                   6    
HELIX   27  27 THR A  443  GLY A  458  1                                  16    
HELIX   28  28 PHE A  459  TRP A  465  1                                   7    
HELIX   29  29 TYR A  466  ASN A  468  5                                   3    
HELIX   30  30 MET A  469  SER A  479  1                                  11    
HELIX   31  31 LEU A  480  ARG A  482  5                                   3    
HELIX   32  32 VAL A  500  TRP A  510  5                                  11    
HELIX   33  33 TRP A  525  LYS A  530  1                                   6    
HELIX   34  34 LYS A  530  ALA A  546  1                                  17    
SHEET    1   A 5 PHE A 149  GLU A 152  0                                        
SHEET    2   A 5 THR A 118  THR A 123  1  N  ILE A 121   O  ILE A 151           
SHEET    3   A 5 ALA A   5  PHE A   8  1  N  PHE A   8   O  ALA A 120           
SHEET    4   A 5 VAL A 180  ASP A 184  1  O  VAL A 181   N  ALA A   5           
SHEET    5   A 5 VAL A 199  LEU A 202  1  O  ILE A 201   N  PHE A 182           
SHEET    1   B 8 HIS A 239  LYS A 245  0                                        
SHEET    2   B 8 VAL A 248  LEU A 255 -1  O  LEU A 250   N  VAL A 242           
SHEET    3   B 8 ARG A 287  ASP A 292 -1  O  VAL A 288   N  LEU A 255           
SHEET    4   B 8 ALA A 260  CYS A 264  1  N  VAL A 261   O  ARG A 287           
SHEET    5   B 8 ALA A 329  HIS A 334  1  O  VAL A 330   N  CYS A 262           
SHEET    6   B 8 VAL A 352  LEU A 358  1  O  ALA A 356   N  GLY A 333           
SHEET    7   B 8 ALA A 488  ALA A 493  1  O  LEU A 489   N  SER A 357           
SHEET    8   B 8 LEU A 514  ILE A 519  1  O  GLY A 517   N  MET A 490           
CISPEP   1 LYS A  160    PRO A  161          0         8.65                     
CISPEP   2 PHE A  267    PRO A  268          0        -8.37                     
SITE     1 AC1 11 PHE A 267  ASP A 335  MET A 339  TYR A 383                    
SITE     2 AC1 11 GLN A 384  TYR A 466  PHE A 497  VAL A 498                    
SITE     3 AC1 11 LEU A 499  MET A 503  HIS A 524                               
CRYST1   91.765   91.765  242.516  90.00  90.00 120.00 P 65 2 2     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010897  0.006292  0.000000        0.00000                         
SCALE2      0.000000  0.012583  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004123        0.00000                         
TER    4317      ASN A 548                                                      
MASTER      387    0    1   34   13    0    3    6 4369    1   25   43          
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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