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LongText Report for: 4L3W-pdb

Name Class
4L3W-pdb
HEADER    HYDROLASE                               07-JUN-13   4L3W              
TITLE     CRYSTAL STRUCTURE OF LIPASE FROM RHIZOPUS MICROSPORUS VAR. CHINENSIS  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 94-389;                     
COMPND   5 EC: 3.1.1.3;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHIZOPUS MICROSPORUS VAR. CHINENSIS;            
SOURCE   3 ORGANISM_COMMON: BREAD MOLD;                                         
SOURCE   4 ORGANISM_TAXID: 4843;                                                
SOURCE   5 STRAIN: CCTCC M201021;                                               
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: GS115;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPIC9K                                    
KEYWDS    ESTERASES FAMILY 3, LIPASE, HYDROLASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.ZHANG,X.W.YU,Y.XU,C.H.HUANG,R.T.GUO                                 
REVDAT   1   10-DEC-14 4L3W    0                                                
JRNL        AUTH   M.ZHANG,X.W.YU,Y.XU,C.H.HUANG,R.T.GUO                        
JRNL        TITL   CRYSTAL STRUCTURE OF LIPASE FROM RHIZOPUS MICROSPORUS VAR.   
JRNL        TITL 2 CHINENSIS                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 27593                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1346                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3110                       
REMARK   3   BIN FREE R VALUE                    : 0.3480                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 116                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2062                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 61                                      
REMARK   3   SOLVENT ATOMS            : 323                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -11.67700                                            
REMARK   3    B22 (A**2) : -11.67700                                            
REMARK   3    B33 (A**2) : 23.35400                                             
REMARK   3    B12 (A**2) : -5.44500                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.187 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.733 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.177 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.992 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 54.27                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : PEG2.PARAM                                     
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4L3W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB080148.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSRRC                              
REMARK 200  BEAMLINE                       : BL13B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30238                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10.300                             
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 25.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM TRIS PH 8.0, 150MM NACL, 0.25M      
REMARK 280  (NH4)2SO4, 25% PEG 4000 , VAPOR DIFFUSION, SITTING DROP             
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       33.71700            
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       67.43400            
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       67.43400            
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       33.71700            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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     ASP A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     MET A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     ASP A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     PRO A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     ASN A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     PRO A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     ILE A    19                                                      
REMARK 465     PRO A    20                                                      
REMARK 465     ALA A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     THR A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     ASP A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     GLY A    31                                                      
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    ILE A 252   C     ILE A 252   O      -0.163                       
REMARK 500    LYS A 253   C     LYS A 253   O      -0.224                       
REMARK 500    GLU A 254   CD    GLU A 254   OE1    -0.159                       
REMARK 500    GLU A 254   CD    GLU A 254   OE2    -0.173                       
REMARK 500    ASP A 255   CA    ASP A 255   CB     -0.133                       
REMARK 500    ASP A 255   CG    ASP A 255   OD2    -0.164                       
REMARK 500    ASP A 255   C     ASP A 255   O      -0.145                       
REMARK 500    ALA A 257   C     ALA A 257   O      -0.148                       
REMARK 500    ASP A 258   CG    ASP A 258   OD1    -0.180                       
REMARK 500    ASP A 258   CG    ASP A 258   OD2    -0.168                       
REMARK 500    ASP A 258   C     ASP A 258   O      -0.169                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 256   C   -  N   -  CD  ANGL. DEV. =  17.3 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    TRP A  65       75.81   -114.40                                   
REMARK 500    ASP A  66       19.25   -143.18                                   
REMARK 500    SER A 172     -138.03     52.49                                   
REMARK 500    LYS A 229     -110.27     39.40                                   
REMARK 500    PRO A 234        0.86    -68.00                                   
REMARK 500    CYS A 271     -132.34   -100.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 494        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH A 531        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH A 557        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH A 563        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A 567        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH A 573        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH A 582        DISTANCE =  8.31 ANGSTROMS                       
REMARK 525    HOH A 584        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH A 585        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH A 587        DISTANCE =  8.04 ANGSTROMS                       
REMARK 525    HOH A 601        DISTANCE =  7.80 ANGSTROMS                       
REMARK 525    HOH A 602        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH A 608        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH A 609        DISTANCE =  8.44 ANGSTROMS                       
REMARK 525    HOH A 612        DISTANCE =  7.52 ANGSTROMS                       
REMARK 525    HOH A 613        DISTANCE =  7.64 ANGSTROMS                       
REMARK 525    HOH A 614        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH A 626        DISTANCE =  7.96 ANGSTROMS                       
REMARK 525    HOH A 627        DISTANCE =  7.93 ANGSTROMS                       
REMARK 525    HOH A 628        DISTANCE =  8.12 ANGSTROMS                       
REMARK 525    HOH A 631        DISTANCE =  7.15 ANGSTROMS                       
REMARK 525    HOH A 635        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH A 637        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH A 638        DISTANCE = 10.04 ANGSTROMS                       
REMARK 525    HOH A 643        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH A 656        DISTANCE =  7.13 ANGSTROMS                       
REMARK 525    HOH A 657        DISTANCE =  8.58 ANGSTROMS                       
REMARK 525    HOH A 666        DISTANCE =  9.93 ANGSTROMS                       
REMARK 525    HOH A 671        DISTANCE =  8.53 ANGSTROMS                       
REMARK 525    HOH A 672        DISTANCE =  9.02 ANGSTROMS                       
REMARK 525    HOH A 676        DISTANCE =  8.34 ANGSTROMS                       
REMARK 525    HOH A 679        DISTANCE =  6.98 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 312                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 313                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 314                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 315                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 316                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 317                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 318                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 319                 
DBREF  4L3W A    1   296  UNP    A3FM73   A3FM73_RHICH    94    389             
SEQRES   1 A  296  ASP THR GLU THR VAL GLY GLY MET THR LEU ASP LEU PRO          
SEQRES   2 A  296  GLU ASN PRO PRO PRO ILE PRO ALA THR SER THR ALA PRO          
SEQRES   3 A  296  SER SER ASP SER GLY GLU VAL VAL THR ALA THR ALA ALA          
SEQRES   4 A  296  GLN ILE LYS GLU LEU THR ASN TYR ALA GLY VAL ALA ALA          
SEQRES   5 A  296  THR ALA TYR CYS ARG SER VAL VAL PRO GLY THR LYS TRP          
SEQRES   6 A  296  ASP CYS LYS GLN CYS LEU LYS TYR VAL PRO ASP GLY LYS          
SEQRES   7 A  296  LEU ILE LYS THR PHE THR SER LEU LEU THR ASP THR ASN          
SEQRES   8 A  296  GLY PHE ILE LEU ARG SER ASP ALA GLN LYS THR ILE TYR          
SEQRES   9 A  296  VAL THR PHE ARG GLY THR ASN SER PHE ARG SER ALA ILE          
SEQRES  10 A  296  THR ASP MET VAL PHE THR PHE THR ASP TYR SER PRO VAL          
SEQRES  11 A  296  LYS GLY ALA LYS VAL HIS ALA GLY PHE LEU SER SER TYR          
SEQRES  12 A  296  ASN GLN VAL VAL LYS ASP TYR PHE PRO VAL VAL GLN ASP          
SEQRES  13 A  296  GLN LEU THR ALA TYR PRO ASP TYR LYS VAL ILE VAL THR          
SEQRES  14 A  296  GLY HIS SER LEU GLY GLY ALA GLN ALA LEU LEU ALA GLY          
SEQRES  15 A  296  MET ASP LEU TYR GLN ARG GLU LYS ARG LEU SER PRO LYS          
SEQRES  16 A  296  ASN LEU SER ILE TYR THR VAL GLY CYS PRO ARG VAL GLY          
SEQRES  17 A  296  ASN ASN ALA PHE ALA TYR TYR VAL ASP SER THR GLY ILE          
SEQRES  18 A  296  PRO PHE HIS ARG THR VAL HIS LYS ARG ASP ILE VAL PRO          
SEQRES  19 A  296  HIS VAL PRO PRO GLN ALA PHE GLY TYR LEU HIS PRO GLY          
SEQRES  20 A  296  VAL GLU SER TRP ILE LYS GLU ASP PRO ALA ASP VAL GLN          
SEQRES  21 A  296  ILE CYS THR SER ASN ILE GLU THR LYS GLN CYS SER ASN          
SEQRES  22 A  296  SER ILE VAL PRO PHE THR SER ILE ALA ASP HIS LEU THR          
SEQRES  23 A  296  TYR PHE GLY ILE ASN GLU GLY SER CYS LEU                      
HET    EDO  A 301       3                                                       
HET    EDO  A 302       3                                                       
HET    EDO  A 303       3                                                       
HET    EDO  A 304       3                                                       
HET    EDO  A 305       3                                                       
HET    EDO  A 306       3                                                       
HET    EDO  A 307       3                                                       
HET    EDO  A 308       3                                                       
HET    EDO  A 309       3                                                       
HET    EDO  A 310       3                                                       
HET    EDO  A 311       3                                                       
HET    EDO  A 312       3                                                       
HET    EDO  A 313       3                                                       
HET    EDO  A 314       3                                                       
HET    EDO  A 315       3                                                       
HET    EDO  A 316       3                                                       
HET    EDO  A 317       3                                                       
HET    SO4  A 318       5                                                       
HET    SO4  A 319       5                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     SO4 SULFATE ION                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  EDO    17(C2 H6 O2)                                                 
FORMUL  19  SO4    2(O4 S 2-)                                                   
FORMUL  21  HOH   *323(H2 O)                                                    
HELIX    1   1 THR A   37  THR A   53  1                                  17    
HELIX    2   2 ALA A   54  CYS A   56  5                                   3    
HELIX    3   3 CYS A   67  VAL A   74  1                                   8    
HELIX    4   4 LEU A   86  ASP A   89  5                                   4    
HELIX    5   5 SER A  112  ASP A  119  1                                   8    
HELIX    6   6 ALA A  137  TYR A  161  1                                  25    
HELIX    7   7 SER A  172  GLU A  189  1                                  18    
HELIX    8   8 ASN A  209  GLY A  220  1                                  12    
HELIX    9   9 ILE A  232  VAL A  236  5                                   5    
HELIX   10  10 PRO A  238  GLY A  242  5                                   5    
HELIX   11  11 CYS A  271  VAL A  276  5                                   6    
HELIX   12  12 ILE A  281  HIS A  284  5                                   4    
SHEET    1   A 9 VAL A  33  THR A  35  0                                        
SHEET    2   A 9 ASP A 258  CYS A 262 -1  O  ILE A 261   N  VAL A  34           
SHEET    3   A 9 VAL A 248  GLU A 254 -1  N  TRP A 251   O  GLN A 260           
SHEET    4   A 9 PHE A 223  HIS A 228  1  N  ARG A 225   O  VAL A 248           
SHEET    5   A 9 LEU A 197  VAL A 202  1  N  ILE A 199   O  HIS A 224           
SHEET    6   A 9 LYS A 165  HIS A 171  1  N  VAL A 168   O  TYR A 200           
SHEET    7   A 9 THR A 102  ARG A 108  1  N  VAL A 105   O  ILE A 167           
SHEET    8   A 9 THR A  90  SER A  97 -1  N  LEU A  95   O  TYR A 104           
SHEET    9   A 9 LYS A  78  SER A  85 -1  N  SER A  85   O  THR A  90           
SHEET    1   B 2 PHE A 124  ASP A 126  0                                        
SHEET    2   B 2 LYS A 134  HIS A 136 -1  O  VAL A 135   N  THR A 125           
SHEET    1   C 2 THR A 286  TYR A 287  0                                        
SHEET    2   C 2 ILE A 290  ASN A 291 -1  O  ILE A 290   N  TYR A 287           
SSBOND   1 CYS A   56    CYS A  295                          1555   1555  2.04  
SSBOND   2 CYS A   67    CYS A   70                          1555   1555  2.04  
SSBOND   3 CYS A  262    CYS A  271                          1555   1555  2.02  
LINK         C2  EDO A 301                 O1  EDO A 302     1555   1555  1.51  
LINK         C2  EDO A 302                 O1  EDO A 303     1555   1555  1.52  
LINK         C2  EDO A 303                 O1  EDO A 304     1555   1555  1.52  
LINK         C2  EDO A 304                 O1  EDO A 305     1555   1555  1.51  
LINK         C2  EDO A 305                 O1  EDO A 306     1555   1555  1.52  
LINK         C2  EDO A 306                 O1  EDO A 307     1555   1555  1.52  
LINK         C2  EDO A 307                 O1  EDO A 308     1555   1555  1.52  
LINK         C2  EDO A 308                 O1  EDO A 309     1555   1555  1.52  
LINK         C2  EDO A 309                 O1  EDO A 310     1555   1555  1.54  
LINK         C2  EDO A 310                 O1  EDO A 311     1555   1555  1.56  
LINK         C2  EDO A 311                 O1  EDO A 312     1555   1555  1.52  
LINK         C2  EDO A 312                 O1  EDO A 313     1555   1555  1.50  
LINK         C2  EDO A 313                 O1  EDO A 314     1555   1555  1.51  
LINK         C2  EDO A 314                 O1  EDO A 315     1555   1555  1.50  
LINK         C2  EDO A 315                 O1  EDO A 316     1555   1555  1.53  
LINK         C2  EDO A 316                 O1  EDO A 317     1555   1555  1.54  
CISPEP   1 VAL A   60    PRO A   61          0         0.64                     
CISPEP   2 VAL A  236    PRO A  237          0        -0.62                     
CISPEP   3 ASP A  255    PRO A  256          0         1.97                     
CISPEP   4 VAL A  276    PRO A  277          0         0.13                     
SITE     1 AC1  2 EDO A 302  HOH A 701                                          
SITE     1 AC2  5 ASP A 156  LYS A 253  EDO A 301  EDO A 303                    
SITE     2 AC2  5 HOH A 574                                                     
SITE     1 AC3  3 ASP A 156  EDO A 302  EDO A 304                               
SITE     1 AC4  3 EDO A 303  EDO A 305  HOH A 499                               
SITE     1 AC5  5 ARG A 230  EDO A 304  EDO A 306  HOH A 421                    
SITE     2 AC5  5 HOH A 499                                                     
SITE     1 AC6  4 EDO A 305  EDO A 307  HOH A 421  HOH A 498                    
SITE     1 AC7  3 EDO A 306  EDO A 308  HOH A 411                               
SITE     1 AC8  3 EDO A 307  EDO A 309  HOH A 411                               
SITE     1 AC9  3 EDO A 308  EDO A 310  HOH A 503                               
SITE     1 BC1  4 EDO A 309  EDO A 311  HOH A 503  HOH A 515                    
SITE     1 BC2  3 EDO A 310  EDO A 312  HOH A 449                               
SITE     1 BC3  4 THR A 279  EDO A 311  EDO A 313  HOH A 458                    
SITE     1 BC4  5 PRO A 277  THR A 279  EDO A 312  EDO A 314                    
SITE     2 BC4  5 HOH A 458                                                     
SITE     1 BC5  3 EDO A 313  EDO A 315  HOH A 470                               
SITE     1 BC6  3 EDO A 314  EDO A 316  HOH A 430                               
SITE     1 BC7  4 EDO A 315  EDO A 317  HOH A 430  HOH A 504                    
SITE     1 BC8  2 EDO A 316  HOH A 580                                          
SITE     1 BC9  3 GLN A  40  GLU A  43  HIS A 224                               
SITE     1 CC1  7 HIS A 228  LYS A 229  ASP A 255  THR A 286                    
SITE     2 CC1  7 PHE A 288  GLY A 289  HOH A 704                               
CRYST1   86.225   86.225  101.151  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      0.011598  0.006696  0.000000        0.00000                         
SCALE2      0.000000  0.013392  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009886        0.00000                         
TER    2063      LEU A 296                                                      
MASTER      456    0   19   12   13    0   23    6 2446    1   67   23          
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:
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