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LongText Report for: 2PSE-pdb

Name Class
2PSE-pdb
HEADER    OXIDOREDUCTASE                          06-MAY-07   2PSE              
TITLE     CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN FLUORESCENT            
TITLE    2 PROTEIN FROM RENILLA RENIFORMIS                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RENILLA-LUCIFERIN 2-MONOOXYGENASE;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: RENILLA-TYPE LUCIFERASE;                                    
COMPND   5 EC: 1.13.12.5;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RENILLA RENIFORMIS;                             
SOURCE   3 ORGANISM_COMMON: SEA PANSY;                                          
SOURCE   4 GENE: RLUC;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BACTERIA;                                  
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: LMG194;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PBAD                                      
KEYWDS    ALPHA/BETA-HYDROLASE, LUCIFERASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.LOENING,T.D.FENN,S.S.GAMBHIR                                      
REVDAT   1   22-MAY-07 2PSE    0                                                
JRNL        AUTH   A.M.LOENING,T.D.FENN,S.S.GAMBHIR                             
JRNL        TITL   CRYSTAL STRUCTURES OF THE LUCIFERASE AND GREEN               
JRNL        TITL 2 FLUORESCENT PROTEIN FROM RENILLA RENIFORMIS                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.50 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.56                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 11477                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 604                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 727                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.57                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 34                           
REMARK   3   BIN FREE R VALUE                    : 0.4090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 2583                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.53000                                              
REMARK   3    B22 (A**2) : 0.53000                                              
REMARK   3    B33 (A**2) : -0.79000                                             
REMARK   3    B12 (A**2) : 0.26000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.760         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.291         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.202         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.232         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2580 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1804 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3492 ; 1.588 ; 1.954       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4383 ; 0.957 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   304 ; 6.744 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   125 ;35.875 ;24.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   451 ;16.591 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;17.540 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   363 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2837 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   539 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   627 ; 0.228 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1944 ; 0.205 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1258 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1272 ; 0.093 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   110 ; 0.190 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     5 ; 0.147 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    24 ; 0.339 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.135 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1953 ; 0.836 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   608 ; 0.139 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2474 ; 1.061 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1267 ; 1.662 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1018 ; 2.425 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 0                                 
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 0                                          
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2PSE COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006                         
REMARK   4                                                                      
REMARK   4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY.                    
REMARK   4 REMEDIATED DATA FILE REVISION 3.100 (2007-05-18)                     
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB .                              
REMARK 100 THE RCSB ID CODE IS RCSB042731.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAY-2005                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.40                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
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   : 11477                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
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   (%): 53.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 KSCN, 15% W/V PEG 6000, 0.1 M       
REMARK 280  TRIS-HCL, PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE        
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,1/3+Z                                            
REMARK 290       3555   -X+Y,-X,2/3+Z                                           
REMARK 290       4555   -X,-Y,1/2+Z                                             
REMARK 290       5555   Y,-X+Y,5/6+Z                                            
REMARK 290       6555   X-Y,X,1/6+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 -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       16.01600            
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       32.03200            
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       24.02400            
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       40.04000            
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        8.00800            
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 1 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                                     
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     ALA A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ASN A   309                                                      
REMARK 465     GLU A   310                                                      
REMARK 465     GLN A   311                                                      
REMARK 465     VAL A   312                                                      
REMARK 465     ASP A   313                                                      
REMARK 465     HIS A   314                                                      
REMARK 465     HIS A   315                                                      
REMARK 465     HIS A   316                                                      
REMARK 465     HIS A   317                                                      
REMARK 465     HIS A   318                                                      
REMARK 465     HIS A   319                                                      
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                             
REMARK 500   O    LYS A   167     O    HOH      65              2.02            
REMARK 500   NZ   LYS A   193     O    HOH      70              2.14            
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    GLU A  40      -55.43     66.37                                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2PSD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PSF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PSH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PSJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PSL   RELATED DB: PDB                                   
DBREF  2PSE A    3   311  UNP    P27652   LUCI_RENRE       3    311             
SEQADV 2PSE ALA A    2  UNP  P27652              CLONING ARTIFACT               
SEQADV 2PSE THR A   55  UNP  P27652    ALA    55 ENGINEERED                     
SEQADV 2PSE ALA A  124  UNP  P27652    CYS   124 ENGINEERED                     
SEQADV 2PSE ALA A  130  UNP  P27652    SER   130 ENGINEERED                     
SEQADV 2PSE ARG A  136  UNP  P27652    LYS   136 ENGINEERED                     
SEQADV 2PSE MET A  143  UNP  P27652    ALA   143 ENGINEERED                     
SEQADV 2PSE VAL A  185  UNP  P27652    MET   185 ENGINEERED                     
SEQADV 2PSE LEU A  253  UNP  P27652    MET   253 ENGINEERED                     
SEQADV 2PSE LEU A  287  UNP  P27652    SER   287 ENGINEERED                     
SEQADV 2PSE VAL A  312  UNP  P27652              CLONING ARTIFACT               
SEQADV 2PSE ASP A  313  UNP  P27652              CLONING ARTIFACT               
SEQADV 2PSE HIS A  314  UNP  P27652              HIS TAG                        
SEQADV 2PSE HIS A  315  UNP  P27652              HIS TAG                        
SEQADV 2PSE HIS A  316  UNP  P27652              HIS TAG                        
SEQADV 2PSE HIS A  317  UNP  P27652              HIS TAG                        
SEQADV 2PSE HIS A  318  UNP  P27652              HIS TAG                        
SEQADV 2PSE HIS A  319  UNP  P27652              HIS TAG                        
SEQRES   1 A  318  ALA SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG MET          
SEQRES   2 A  318  ILE THR GLY PRO GLN TRP TRP ALA ARG CYS LYS GLN MET          
SEQRES   3 A  318  ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER GLU          
SEQRES   4 A  318  LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY ASN          
SEQRES   5 A  318  ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO HIS          
SEQRES   6 A  318  ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU ILE          
SEQRES   7 A  318  GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER TYR          
SEQRES   8 A  318  ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP PHE          
SEQRES   9 A  318  GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL GLY          
SEQRES  10 A  318  HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA TYR          
SEQRES  11 A  318  GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET GLU          
SEQRES  12 A  318  SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP PRO          
SEQRES  13 A  318  ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU GLU          
SEQRES  14 A  318  GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL GLU          
SEQRES  15 A  318  THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU PRO          
SEQRES  16 A  318  GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU LYS          
SEQRES  17 A  318  GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG GLU          
SEQRES  18 A  318  ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL GLN          
SEQRES  19 A  318  ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER ASP          
SEQRES  20 A  318  ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY PHE          
SEQRES  21 A  318  PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE PRO          
SEQRES  22 A  318  ASN THR GLU PHE VAL LYS VAL LYS GLY LEU HIS PHE LEU          
SEQRES  23 A  318  GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE LYS          
SEQRES  24 A  318  SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN VAL ASP          
SEQRES  25 A  318  HIS HIS HIS HIS HIS HIS                                      
HET    IMD    101       5                                                       
HETNAM     IMD IMIDAZOLE                                                        
FORMUL   2  IMD    C3 H5 N2 1+                                                  
FORMUL   3  HOH   *76(H2 O)                                                     
HELIX    1   1 GLU A    9  MET A   14  1                                   6    
HELIX    2   2 THR A   16  ARG A   23  1                                   8    
HELIX    3   3 SER A   56  ARG A   61  5                                   6    
HELIX    4   4 VAL A   63  GLU A   68  1                                   6    
HELIX    5   5 PRO A   69  ALA A   71  5                                   3    
HELIX    6   6 ARG A   93  GLU A  106  1                                  14    
HELIX    7   7 ASP A  120  GLU A  132  1                                  13    
HELIX    8   8 ILE A  159  SER A  168  1                                  10    
HELIX    9   9 GLU A  170  LEU A  176  1                                   7    
HELIX   10  10 ASN A  179  THR A  184  1                                   6    
HELIX   11  11 THR A  184  LYS A  189  1                                   6    
HELIX   12  12 GLU A  195  GLU A  204  1                                  10    
HELIX   13  13 PRO A  205  LYS A  207  5                                   3    
HELIX   14  14 GLY A  210  VAL A  212  5                                   3    
HELIX   15  15 ARG A  213  GLU A  222  1                                  10    
HELIX   16  16 LYS A  230  ALA A  246  1                                  17    
HELIX   17  17 PHE A  262  LYS A  272  1                                  11    
HELIX   18  18 PHE A  286  ASP A  290  5                                   5    
HELIX   19  19 ALA A  291  LYS A  308  1                                  18    
SHEET    1   A 2 ASN A  28  VAL A  29  0                                        
SHEET    2   A 2 SER A  32  PHE A  33 -1  O  SER A  32   N  VAL A  29           
SHEET    1   B 7 TYR A  36  ASP A  38  0                                        
SHEET    2   B 7 ARG A  72  PRO A  76 -1  O  ILE A  75   N  TYR A  37           
SHEET    3   B 7 ALA A  46  LEU A  50  1  N  VAL A  47   O  ARG A  72           
SHEET    4   B 7 ILE A 114  HIS A 119  1  O  VAL A 117   N  LEU A  50           
SHEET    5   B 7 ILE A 137  MET A 143  1  O  LYS A 138   N  ILE A 114           
SHEET    6   B 7 LYS A 252  PRO A 259  1  O  LEU A 253   N  HIS A 142           
SHEET    7   B 7 THR A 276  GLY A 283  1  O  VAL A 279   N  GLU A 256           
CISPEP   1 ASP A  258    PRO A  259          0         7.10                     
CRYST1  119.443  119.443   48.048  90.00  90.00 120.00 P 61          6          
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      0.008372  0.004834  0.000000        0.00000                         
SCALE2      0.000000  0.009667  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020813        0.00000                         
TER    2503      LYS A 308                                                      
MASTER      285    0    1   19    9    0    0    6 2583    1    5   25          
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.
For technical information about these pages see:
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