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LongText Report for: 2PSH-pdb

Name Class
2PSH-pdb
HEADER    OXIDOREDUCTASE                          06-MAY-07   2PSH              
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, B;                                                         
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   05-JUN-07 2PSH    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. 1.79 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) : 1.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 86.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 58344                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3119                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 1.79                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 1.84                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3552                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.69                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2980                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 201                          
REMARK   3   BIN FREE R VALUE                    : 0.3530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 5336                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.95000                                              
REMARK   3    B22 (A**2) : 0.13000                                              
REMARK   3    B33 (A**2) : -1.10000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.04000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.136         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.127         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.091         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.928         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4994 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3487 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6755 ; 1.212 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8473 ; 0.878 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   593 ; 5.642 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   238 ;34.843 ;23.824       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   872 ;12.784 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;16.897 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   710 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5483 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1040 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1072 ; 0.212 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3548 ; 0.193 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2446 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2337 ; 0.082 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   379 ; 0.125 ; 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):     2 ; 0.139 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    23 ; 0.169 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    28 ; 0.116 ; 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):  3864 ; 0.776 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1192 ; 0.122 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4821 ; 0.858 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2434 ; 1.395 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1934 ; 1.994 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      3       A     310      4                      
REMARK   3           1     B      3       B     310      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   4149 ;  0.42 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   4149 ;  0.42 ;  2.00           
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 2PSH 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 (2007-06-01)                     
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB .                              
REMARK 100 THE RCSB ID CODE IS RCSB042733.                                      
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                             : 7.50                               
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   : 58344                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
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   (%): 46.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1~M HEPES, 10% V/V ISOPROPANOL         
REMARK 280  WITH 6MG/ML BENZYL-COELENTERAZINE, 15% W/V PEG 3350, PH 7.5,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       37.82600            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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                                     
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 BIOMOLECULE: 2                                                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASP A   154                                                      
REMARK 465     GLU A   155                                                      
REMARK 465     TRP A   156                                                      
REMARK 465     PRO A   157                                                      
REMARK 465     ASP A   158                                                      
REMARK 465     ILE A   159                                                      
REMARK 465     GLU A   160                                                      
REMARK 465     GLU A   161                                                      
REMARK 465     ASP A   162                                                      
REMARK 465     ILE A   163                                                      
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 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     TRP B   153                                                      
REMARK 465     ASP B   154                                                      
REMARK 465     GLU B   155                                                      
REMARK 465     TRP B   156                                                      
REMARK 465     PRO B   157                                                      
REMARK 465     ASP B   158                                                      
REMARK 465     ILE B   159                                                      
REMARK 465     GLU B   160                                                      
REMARK 465     GLU B   161                                                      
REMARK 465     GLN B   311                                                      
REMARK 465     VAL B   312                                                      
REMARK 465     ASP B   313                                                      
REMARK 465     HIS B   314                                                      
REMARK 465     HIS B   315                                                      
REMARK 465     HIS B   316                                                      
REMARK 465     HIS B   317                                                      
REMARK 465     HIS B   318                                                      
REMARK 465     HIS B   319                                                      
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    LYS A 272   CE    LYS A 272   NZ     0.056                        
REMARK 500    ASN B 179   CB    ASN B 179   CG    -0.058                        
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    PRO A  65   C   -  N   -  CA  ANGL. DEV. = -7.6 DEGREES           
REMARK 500    PRO A  65   C   -  N   -  CD  ANGL. DEV. =  8.7 DEGREES           
REMARK 500    LEU A 287   CA  -  CB  -  CG  ANGL. DEV. =  8.8 DEGREES           
REMARK 500    TYR B 240   CA  -  CB  -  CG  ANGL. DEV. =  8.1 DEGREES           
REMARK 500    LEU B 287   CA  -  CB  -  CG  ANGL. DEV. =  9.4 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    GLU A  40      -50.80     69.14                                   
REMARK 500    GLU B  40      -56.04     72.28                                   
REMARK 500    ASN B 179       68.19      3.57                                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2PSD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PSE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PSF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PSJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PSL   RELATED DB: PDB                                   
DBREF  2PSH A    1   311  UNP    P27652   LUCI_RENRE       1    311             
DBREF  2PSH B    1   311  UNP    P27652   LUCI_RENRE       1    311             
SEQADV 2PSH ALA A    2  UNP  P27652    THR     2 ENGINEERED                     
SEQADV 2PSH ALA A   25  UNP  P27652    LYS    25 ENGINEERED                     
SEQADV 2PSH THR A   55  UNP  P27652    ALA    55 ENGINEERED                     
SEQADV 2PSH ALA A  124  UNP  P27652    CYS   124 ENGINEERED                     
SEQADV 2PSH ALA A  130  UNP  P27652    SER   130 ENGINEERED                     
SEQADV 2PSH ARG A  136  UNP  P27652    LYS   136 ENGINEERED                     
SEQADV 2PSH MET A  143  UNP  P27652    ALA   143 ENGINEERED                     
SEQADV 2PSH VAL A  185  UNP  P27652    MET   185 ENGINEERED                     
SEQADV 2PSH LEU A  253  UNP  P27652    MET   253 ENGINEERED                     
SEQADV 2PSH ALA A  277  UNP  P27652    GLU   277 ENGINEERED                     
SEQADV 2PSH LEU A  287  UNP  P27652    SER   287 ENGINEERED                     
SEQADV 2PSH VAL A  312  UNP  P27652              CLONING ARTIFACT               
SEQADV 2PSH ASP A  313  UNP  P27652              CLONING ARTIFACT               
SEQADV 2PSH HIS A  314  UNP  P27652              HIS TAG                        
SEQADV 2PSH HIS A  315  UNP  P27652              HIS TAG                        
SEQADV 2PSH HIS A  316  UNP  P27652              HIS TAG                        
SEQADV 2PSH HIS A  317  UNP  P27652              HIS TAG                        
SEQADV 2PSH HIS A  318  UNP  P27652              HIS TAG                        
SEQADV 2PSH HIS A  319  UNP  P27652              HIS TAG                        
SEQADV 2PSH ALA B    2  UNP  P27652    THR     2 ENGINEERED                     
SEQADV 2PSH ALA B   25  UNP  P27652    LYS    25 ENGINEERED                     
SEQADV 2PSH THR B   55  UNP  P27652    ALA    55 ENGINEERED                     
SEQADV 2PSH ALA B  124  UNP  P27652    CYS   124 ENGINEERED                     
SEQADV 2PSH ALA B  130  UNP  P27652    SER   130 ENGINEERED                     
SEQADV 2PSH ARG B  136  UNP  P27652    LYS   136 ENGINEERED                     
SEQADV 2PSH MET B  143  UNP  P27652    ALA   143 ENGINEERED                     
SEQADV 2PSH VAL B  185  UNP  P27652    MET   185 ENGINEERED                     
SEQADV 2PSH LEU B  253  UNP  P27652    MET   253 ENGINEERED                     
SEQADV 2PSH ALA B  277  UNP  P27652    GLU   277 ENGINEERED                     
SEQADV 2PSH LEU B  287  UNP  P27652    SER   287 ENGINEERED                     
SEQADV 2PSH VAL B  312  UNP  P27652              CLONING ARTIFACT               
SEQADV 2PSH ASP B  313  UNP  P27652              CLONING ARTIFACT               
SEQADV 2PSH HIS B  314  UNP  P27652              HIS TAG                        
SEQADV 2PSH HIS B  315  UNP  P27652              HIS TAG                        
SEQADV 2PSH HIS B  316  UNP  P27652              HIS TAG                        
SEQADV 2PSH HIS B  317  UNP  P27652              HIS TAG                        
SEQADV 2PSH HIS B  318  UNP  P27652              HIS TAG                        
SEQADV 2PSH HIS B  319  UNP  P27652              HIS TAG                        
SEQRES   1 A  319  MET ALA SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG          
SEQRES   2 A  319  MET ILE THR GLY PRO GLN TRP TRP ALA ARG CYS ALA GLN          
SEQRES   3 A  319  MET ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER          
SEQRES   4 A  319  GLU LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY          
SEQRES   5 A  319  ASN ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO          
SEQRES   6 A  319  HIS ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU          
SEQRES   7 A  319  ILE GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER          
SEQRES   8 A  319  TYR ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP          
SEQRES   9 A  319  PHE GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL          
SEQRES  10 A  319  GLY HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA          
SEQRES  11 A  319  TYR GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET          
SEQRES  12 A  319  GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP          
SEQRES  13 A  319  PRO ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU          
SEQRES  14 A  319  GLU GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL          
SEQRES  15 A  319  GLU THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU          
SEQRES  16 A  319  PRO GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU          
SEQRES  17 A  319  LYS GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG          
SEQRES  18 A  319  GLU ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL          
SEQRES  19 A  319  GLN ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER          
SEQRES  20 A  319  ASP ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY          
SEQRES  21 A  319  PHE PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE          
SEQRES  22 A  319  PRO ASN THR ALA PHE VAL LYS VAL LYS GLY LEU HIS PHE          
SEQRES  23 A  319  LEU GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE          
SEQRES  24 A  319  LYS SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN VAL          
SEQRES  25 A  319  ASP HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B  319  MET ALA SER LYS VAL TYR ASP PRO GLU GLN ARG LYS ARG          
SEQRES   2 B  319  MET ILE THR GLY PRO GLN TRP TRP ALA ARG CYS ALA GLN          
SEQRES   3 B  319  MET ASN VAL LEU ASP SER PHE ILE ASN TYR TYR ASP SER          
SEQRES   4 B  319  GLU LYS HIS ALA GLU ASN ALA VAL ILE PHE LEU HIS GLY          
SEQRES   5 B  319  ASN ALA THR SER SER TYR LEU TRP ARG HIS VAL VAL PRO          
SEQRES   6 B  319  HIS ILE GLU PRO VAL ALA ARG CYS ILE ILE PRO ASP LEU          
SEQRES   7 B  319  ILE GLY MET GLY LYS SER GLY LYS SER GLY ASN GLY SER          
SEQRES   8 B  319  TYR ARG LEU LEU ASP HIS TYR LYS TYR LEU THR ALA TRP          
SEQRES   9 B  319  PHE GLU LEU LEU ASN LEU PRO LYS LYS ILE ILE PHE VAL          
SEQRES  10 B  319  GLY HIS ASP TRP GLY ALA ALA LEU ALA PHE HIS TYR ALA          
SEQRES  11 B  319  TYR GLU HIS GLN ASP ARG ILE LYS ALA ILE VAL HIS MET          
SEQRES  12 B  319  GLU SER VAL VAL ASP VAL ILE GLU SER TRP ASP GLU TRP          
SEQRES  13 B  319  PRO ASP ILE GLU GLU ASP ILE ALA LEU ILE LYS SER GLU          
SEQRES  14 B  319  GLU GLY GLU LYS MET VAL LEU GLU ASN ASN PHE PHE VAL          
SEQRES  15 B  319  GLU THR VAL LEU PRO SER LYS ILE MET ARG LYS LEU GLU          
SEQRES  16 B  319  PRO GLU GLU PHE ALA ALA TYR LEU GLU PRO PHE LYS GLU          
SEQRES  17 B  319  LYS GLY GLU VAL ARG ARG PRO THR LEU SER TRP PRO ARG          
SEQRES  18 B  319  GLU ILE PRO LEU VAL LYS GLY GLY LYS PRO ASP VAL VAL          
SEQRES  19 B  319  GLN ILE VAL ARG ASN TYR ASN ALA TYR LEU ARG ALA SER          
SEQRES  20 B  319  ASP ASP LEU PRO LYS LEU PHE ILE GLU SER ASP PRO GLY          
SEQRES  21 B  319  PHE PHE SER ASN ALA ILE VAL GLU GLY ALA LYS LYS PHE          
SEQRES  22 B  319  PRO ASN THR ALA PHE VAL LYS VAL LYS GLY LEU HIS PHE          
SEQRES  23 B  319  LEU GLN GLU ASP ALA PRO ASP GLU MET GLY LYS TYR ILE          
SEQRES  24 B  319  LYS SER PHE VAL GLU ARG VAL LEU LYS ASN GLU GLN VAL          
SEQRES  25 B  319  ASP HIS HIS HIS HIS HIS HIS                                  
FORMUL   3  HOH   *476(H2 O)                                                    
HELIX    1   1 GLN A   10  MET A   14  5                                   5    
HELIX    2   2 THR A   16  ALA A   22  1                                   7    
HELIX    3   3 SER A   56  ARG A   61  5                                   6    
HELIX    4   4 VAL A   63  ILE A   67  5                                   5    
HELIX    5   5 ARG A   93  GLU A  106  1                                  14    
HELIX    6   6 ASP A  120  HIS A  133  1                                  14    
HELIX    7   7 SER A  168  GLU A  177  1                                  10    
HELIX    8   8 ASN A  179  THR A  184  1                                   6    
HELIX    9   9 THR A  184  LYS A  189  1                                   6    
HELIX   10  10 GLU A  195  GLU A  204  1                                  10    
HELIX   11  11 PRO A  205  LYS A  207  5                                   3    
HELIX   12  12 GLY A  210  VAL A  212  5                                   3    
HELIX   13  13 ARG A  213  GLU A  222  1                                  10    
HELIX   14  14 LYS A  230  ALA A  246  1                                  17    
HELIX   15  15 SER A  263  LYS A  271  1                                   9    
HELIX   16  16 PHE A  286  ASP A  290  5                                   5    
HELIX   17  17 ALA A  291  GLU A  310  1                                  20    
HELIX   18  18 GLU B    9  ARG B   13  5                                   5    
HELIX   19  19 THR B   16  ALA B   22  1                                   7    
HELIX   20  20 SER B   56  ARG B   61  5                                   6    
HELIX   21  21 VAL B   63  ILE B   67  5                                   5    
HELIX   22  22 ARG B   93  GLU B  106  1                                  14    
HELIX   23  23 ASP B  120  HIS B  133  1                                  14    
HELIX   24  24 ASP B  162  SER B  168  1                                   7    
HELIX   25  25 SER B  168  GLU B  177  1                                  10    
HELIX   26  26 ASN B  179  THR B  184  1                                   6    
HELIX   27  27 THR B  184  LYS B  189  1                                   6    
HELIX   28  28 GLU B  195  GLU B  204  1                                  10    
HELIX   29  29 PRO B  205  LYS B  207  5                                   3    
HELIX   30  30 GLY B  210  VAL B  212  5                                   3    
HELIX   31  31 ARG B  213  GLU B  222  1                                  10    
HELIX   32  32 LYS B  230  ALA B  246  1                                  17    
HELIX   33  33 SER B  263  LYS B  271  1                                   9    
HELIX   34  34 PHE B  286  ASP B  290  5                                   5    
HELIX   35  35 ALA B  291  GLU B  310  1                                  20    
SHEET    1   A 8 ALA A  25  VAL A  29  0                                        
SHEET    2   A 8 SER A  32  ASP A  38 -1  O  TYR A  36   N  ALA A  25           
SHEET    3   A 8 ARG A  72  PRO A  76 -1  O  ILE A  75   N  TYR A  37           
SHEET    4   A 8 ALA A  46  LEU A  50  1  N  VAL A  47   O  ARG A  72           
SHEET    5   A 8 ILE A 114  HIS A 119  1  O  VAL A 117   N  LEU A  50           
SHEET    6   A 8 ILE A 137  MET A 143  1  O  VAL A 141   N  PHE A 116           
SHEET    7   A 8 LYS A 252  PRO A 259  1  O  LEU A 253   N  HIS A 142           
SHEET    8   A 8 THR A 276  GLY A 283  1  O  VAL A 279   N  GLU A 256           
SHEET    1   B 8 ALA B  25  VAL B  29  0                                        
SHEET    2   B 8 SER B  32  ASP B  38 -1  O  TYR B  36   N  ALA B  25           
SHEET    3   B 8 ARG B  72  PRO B  76 -1  O  ILE B  75   N  TYR B  37           
SHEET    4   B 8 ALA B  46  LEU B  50  1  N  VAL B  47   O  ARG B  72           
SHEET    5   B 8 ILE B 114  HIS B 119  1  O  VAL B 117   N  LEU B  50           
SHEET    6   B 8 ILE B 137  MET B 143  1  O  VAL B 141   N  PHE B 116           
SHEET    7   B 8 LYS B 252  PRO B 259  1  O  LEU B 253   N  HIS B 142           
SHEET    8   B 8 THR B 276  GLY B 283  1  O  VAL B 279   N  GLU B 256           
CISPEP   1 ASP A  258    PRO A  259          0         8.16                     
CISPEP   2 ASP B  258    PRO B  259          0         9.24                     
CRYST1   51.776   75.652   89.185  90.00  76.48  90.00 P 1 21 1      4          
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      0.019314  0.000000 -0.004645        0.00000                         
SCALE2      0.000000  0.013218  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011532        0.00000                         
TER    2430      GLU A 310                                                      
TER    4862      GLU B 310                                                      
MASTER      342    0    0   35   16    0    0    6 5336    2    0   50          
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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