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LongText Report for: 4FTW-pdb

Name Class
4FTW-pdb
HEADER    HYDROLASE                               28-JUN-12   4FTW              
TITLE     CRYSTAL STRUCTURE OF A CARBOXYL ESTERASE N110C/L145H AT 2.3 ANGSTROM  
TITLE    2 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOLIPASE/CARBOXYLESTERASE;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.1.1;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES;                        
SOURCE   3 ORGANISM_TAXID: 272943;                                              
SOURCE   4 STRAIN: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158;                    
SOURCE   5 GENE: CGMCC1.1737, RHOS4_13150, RSP_2728;                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-30A                                   
KEYWDS    ALPHA/BETA HYDROLASE SUPERFAMILY, ESTERASE, HYDROLASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.WU,J.MA,J.ZHOU,H.YU                                                 
REVDAT   1   03-OCT-12 4FTW    0                                                
JRNL        AUTH   J.MA,L.WU,F.GUO,J.GU,X.TANG,L.JIANG,J.LIU,J.ZHOU,H.YU        
JRNL        TITL   ENHANCED ENANTIOSELECTIVITY OF A CARBOXYL ESTERASE FROM      
JRNL        TITL 2 RHODOBACTER SPHAEROIDES BY DIRECTED EVOLUTION.               
JRNL        REF    APPL.MICROBIOL.BIOTECHNOL.                 2012              
JRNL        REFN                   ESSN 1432-0614                               
JRNL        PMID   22987200                                                     
JRNL        DOI    10.1007/S00253-012-4396-2                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.66                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 15208                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.299                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 757                             
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 48.6737 -  3.9312    0.89     2746   121  0.2367 0.2784        
REMARK   3     2  3.9312 -  3.1205    0.98     2930   146  0.2211 0.3225        
REMARK   3     3  3.1205 -  2.7261    1.00     2936   173  0.2506 0.2926        
REMARK   3     4  2.7261 -  2.4768    1.00     2947   151  0.2666 0.3259        
REMARK   3     5  2.4768 -  2.3000    1.00     2892   166  0.2851 0.3260        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.49                                          
REMARK   3   K_SOL              : 0.39                                          
REMARK   3   B_SOL              : 72.14                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.990           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.89100                                             
REMARK   3    B22 (A**2) : -7.89100                                             
REMARK   3    B33 (A**2) : 15.78210                                             
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      :  0.007           1699                                  
REMARK   3   ANGLE     :  1.219           2314                                  
REMARK   3   CHIRALITY :  0.077            255                                  
REMARK   3   PLANARITY :  0.004            302                                  
REMARK   3   DIHEDRAL  : 18.158            672                                  
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 4FTW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073350.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 2012                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15208                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 9.800                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200   FOR THE DATA SET  : 20.5380                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.30                              
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: PHASER MR                                             
REMARK 200 STARTING MODEL: PDB ENTRY 4FHZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3M NA-TARTRATE, 34.5MM CYMAL-3, 0.1M   
REMARK 280  PIPES , PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       15.85633            
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       31.71267            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       31.71267            
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       15.85633            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     HIS A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     VAL A    12                                                      
REMARK 465     PRO A    13                                                      
REMARK 465     ARG A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     MET A    18                                                      
REMARK 465     LYS A    19                                                      
REMARK 465     GLU A    20                                                      
REMARK 465     THR A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     ALA A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     LYS A    25                                                      
REMARK 465     PHE A    26                                                      
REMARK 465     GLU A    27                                                      
REMARK 465     ARG A    28                                                      
REMARK 465     GLN A    29                                                      
REMARK 465     HIS A    30                                                      
REMARK 465     MET A    31                                                      
REMARK 465     ASP A    32                                                      
REMARK 465     SER A    33                                                      
REMARK 465     PRO A    34                                                      
REMARK 465     ASP A    35                                                      
REMARK 465     LEU A    36                                                      
REMARK 465     GLY A    37                                                      
REMARK 465     THR A    38                                                      
REMARK 465     ASP A    39                                                      
REMARK 465     ASP A    40                                                      
REMARK 465     ASP A    41                                                      
REMARK 465     ASP A    42                                                      
REMARK 465     LYS A    43                                                      
REMARK 465     ALA A    44                                                      
REMARK 465     MET A    45                                                      
REMARK 465     ALA A    46                                                      
REMARK 465     ASP A    47                                                      
REMARK 465     ASP A   268                                                      
REMARK 465     ALA A   269                                                      
REMARK 465     CYS A   270                                                      
REMARK 465     GLY A   271                                                      
REMARK 465     ARG A   272                                                      
REMARK 465     THR A   273                                                      
REMARK 465     ARG A   274                                                      
REMARK 465     ALA A   275                                                      
REMARK 465     PRO A   276                                                      
REMARK 465     PRO A   277                                                      
REMARK 465     PRO A   278                                                      
REMARK 465     PRO A   279                                                      
REMARK 465     PRO A   280                                                      
REMARK 465     LEU A   281                                                      
REMARK 465     ARG A   282                                                      
REMARK 465     SER A   283                                                      
REMARK 465     GLY A   284                                                      
REMARK 465     CYS A   285                                                      
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),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 107   CB    CYS A 107   SG     -0.097                       
REMARK 500    CYS A 110   CB    CYS A 110   SG     -0.151                       
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    SER A 165   C   -  N   -  CA  ANGL. DEV. =  16.0 DEGREES          
REMARK 500    SER A 189   N   -  CA  -  C   ANGL. DEV. =  16.3 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    ALA A  77     -156.55   -100.36                                   
REMARK 500    SER A 165      -98.26     80.48                                   
REMARK 500    SER A 189       54.58     39.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PIN A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3CM A 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FHZ   RELATED DB: PDB                                   
DBREF  4FTW A   49   268  UNP    Q3J2V1   Q3J2V1_RHOS4     1    220             
SEQADV 4FTW MET A    1  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW HIS A    2  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW HIS A    3  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW HIS A    4  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW HIS A    5  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW HIS A    6  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW HIS A    7  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW SER A    8  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW SER A    9  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW GLY A   10  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW LEU A   11  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW VAL A   12  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW PRO A   13  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ARG A   14  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW GLY A   15  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW SER A   16  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW GLY A   17  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW MET A   18  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW LYS A   19  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW GLU A   20  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW THR A   21  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ALA A   22  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ALA A   23  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ALA A   24  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW LYS A   25  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW PHE A   26  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW GLU A   27  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ARG A   28  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW GLN A   29  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW HIS A   30  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW MET A   31  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ASP A   32  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW SER A   33  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW PRO A   34  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ASP A   35  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW LEU A   36  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW GLY A   37  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW THR A   38  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ASP A   39  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ASP A   40  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ASP A   41  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ASP A   42  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW LYS A   43  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ALA A   44  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW MET A   45  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ALA A   46  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ASP A   47  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ILE A   48  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW CYS A  110  UNP  Q3J2V1    ASN    62 ENGINEERED MUTATION            
SEQADV 4FTW HIS A  145  UNP  Q3J2V1    LEU    97 ENGINEERED MUTATION            
SEQADV 4FTW ALA A  269  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW CYS A  270  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW GLY A  271  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ARG A  272  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW THR A  273  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ARG A  274  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ALA A  275  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW PRO A  276  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW PRO A  277  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW PRO A  278  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW PRO A  279  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW PRO A  280  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW LEU A  281  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW ARG A  282  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW SER A  283  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW GLY A  284  UNP  Q3J2V1              EXPRESSION TAG                 
SEQADV 4FTW CYS A  285  UNP  Q3J2V1              EXPRESSION TAG                 
SEQRES   1 A  285  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 A  285  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 A  285  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 A  285  ASP ASP ASP LYS ALA MET ALA ASP ILE MET THR ARG LYS          
SEQRES   5 A  285  LEU THR PHE GLY ARG ARG GLY ALA ALA PRO GLY GLU ALA          
SEQRES   6 A  285  THR SER LEU VAL VAL PHE LEU HIS GLY TYR GLY ALA ASP          
SEQRES   7 A  285  GLY ALA ASP LEU LEU GLY LEU ALA GLU PRO LEU ALA PRO          
SEQRES   8 A  285  HIS LEU PRO GLY THR ALA PHE VAL ALA PRO ASP ALA PRO          
SEQRES   9 A  285  GLU PRO CYS ARG ALA CYS GLY PHE GLY PHE GLN TRP PHE          
SEQRES  10 A  285  PRO ILE PRO TRP LEU ASP GLY SER SER GLU THR ALA ALA          
SEQRES  11 A  285  ALA GLU GLY MET ALA ALA ALA ALA ARG ASP LEU ASP ALA          
SEQRES  12 A  285  PHE HIS ASP GLU ARG LEU ALA GLU GLU GLY LEU PRO PRO          
SEQRES  13 A  285  GLU ALA LEU ALA LEU VAL GLY PHE SER GLN GLY THR MET          
SEQRES  14 A  285  MET ALA LEU HIS VAL ALA PRO ARG ARG ALA GLU GLU ILE          
SEQRES  15 A  285  ALA GLY ILE VAL GLY PHE SER GLY ARG LEU LEU ALA PRO          
SEQRES  16 A  285  GLU ARG LEU ALA GLU GLU ALA ARG SER LYS PRO PRO VAL          
SEQRES  17 A  285  LEU LEU VAL HIS GLY ASP ALA ASP PRO VAL VAL PRO PHE          
SEQRES  18 A  285  ALA ASP MET SER LEU ALA GLY GLU ALA LEU ALA GLU ALA          
SEQRES  19 A  285  GLY PHE THR THR TYR GLY HIS VAL MET LYS GLY THR GLY          
SEQRES  20 A  285  HIS GLY ILE ALA PRO ASP GLY LEU SER VAL ALA LEU ALA          
SEQRES  21 A  285  PHE LEU LYS GLU ARG LEU PRO ASP ALA CYS GLY ARG THR          
SEQRES  22 A  285  ARG ALA PRO PRO PRO PRO PRO LEU ARG SER GLY CYS              
HET    PIN  A 301      18                                                       
HET    3CM  A 302      32                                                       
HET     NA  A 303       1                                                       
HET     CL  A 304       1                                                       
HETNAM     PIN PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID)                       
HETNAM     3CM 3-CYCLOHEXYLPROPYL 4-O-ALPHA-D-GLUCOPYRANOSYL-BETA-D-            
HETNAM   2 3CM  GLUCOPYRANOSIDE                                                 
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETSYN     PIN PIPES; 1,4-PIPERAZINEDIETHANESULFONIC ACID                       
HETSYN     3CM CYMAL-3                                                          
FORMUL   2  PIN    C8 H18 N2 O6 S2                                              
FORMUL   3  3CM    C21 H38 O11                                                  
FORMUL   4   NA    NA 1+                                                        
FORMUL   5   CL    CL 1-                                                        
FORMUL   6  HOH   *22(H2 O)                                                     
HELIX    1   1 ASP A   78  GLY A   84  1                                   7    
HELIX    2   2 LEU A   85  ALA A   90  1                                   6    
HELIX    3   3 PRO A   91  LEU A   93  5                                   3    
HELIX    4   4 ILE A  119  GLY A  124  1                                   6    
HELIX    5   5 SER A  126  GLU A  152  1                                  27    
HELIX    6   6 PRO A  155  GLU A  157  5                                   3    
HELIX    7   7 SER A  165  ALA A  175  1                                  11    
HELIX    8   8 PRO A  176  ARG A  178  5                                   3    
HELIX    9   9 ALA A  194  GLU A  196  5                                   3    
HELIX   10  10 ARG A  197  ALA A  202  1                                   6    
HELIX   11  11 PHE A  221  ALA A  234  1                                  14    
HELIX   12  12 ALA A  251  LEU A  266  1                                  16    
SHEET    1   A 7 PHE A  55  GLY A  59  0                                        
SHEET    2   A 7 THR A  96  PRO A 101 -1  O  PHE A  98   N  ARG A  58           
SHEET    3   A 7 SER A  67  LEU A  72  1  N  PHE A  71   O  VAL A  99           
SHEET    4   A 7 LEU A 159  PHE A 164  1  O  VAL A 162   N  VAL A  70           
SHEET    5   A 7 GLY A 184  PHE A 188  1  O  VAL A 186   N  LEU A 161           
SHEET    6   A 7 VAL A 208  GLY A 213  1  O  LEU A 209   N  ILE A 185           
SHEET    7   A 7 THR A 238  MET A 243  1  O  TYR A 239   N  VAL A 208           
SHEET    1   B 2 GLU A 105  PRO A 106  0                                        
SHEET    2   B 2 PHE A 114  GLN A 115 -1  O  GLN A 115   N  GLU A 105           
SSBOND   1 CYS A  107    CYS A  110                          1555   1555  2.28  
CISPEP   1 ARG A   58    GLY A   59          0       -14.72                     
CISPEP   2 SER A  189    GLY A  190          0        25.69                     
SITE     1 AC1  6 TYR A  75  GLY A  76  PHE A 112  LEU A 122                    
SITE     2 AC1  6 SER A 256  3CM A 302                                          
SITE     1 AC2  7 ASP A  81  LEU A 122  PHE A 164  VAL A 218                    
SITE     2 AC2  7 HIS A 248  GLY A 249  PIN A 301                               
CRYST1  112.382  112.382   47.569  90.00  90.00 120.00 P 31 2 1      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      0.008898  0.005137  0.000000        0.00000                         
SCALE2      0.000000  0.010275  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021022        0.00000                         
TER    1612      PRO A 267                                                      
MASTER      352    0    4   12    9    0    4    6 1685    1   52   22          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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