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LongText Report for: 3WWC-pdb

Name Class
3WWC-pdb
HEADER    HYDROLASE                               17-JUN-14   3WWC              
TITLE     THE COMPLEX OF POPH_S172A OF PNPB                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OXIDIZED POLYVINYL ALCOHOL HYDROLASE;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 30-379;                                       
COMPND   5 SYNONYM: OPH, OXIDIZED PVA HYDROLASE, BETA-DIKETONE HYDROLASE;       
COMPND   6 EC: 3.7.1.7;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SP. VM15C;                          
SOURCE   3 ORGANISM_TAXID: 237605;                                              
SOURCE   4 GENE: PVAB;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET32A                                    
KEYWDS    TRYPTOPHAN, DISULFIDE BRIDGE, P-NITROPHENYL ESTERS, HYDROLASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.YANG,T.P.KO,J.H.LI,L.LIU,C.H.HUANG,J.CHEN,R.T.GUO,G.C.DU            
REVDAT   1   29-APR-15 3WWC    0                                                
JRNL        AUTH   Y.YANG,T.P.KO,L.LIU,J.LI,C.H.HUANG,J.CHEN,R.T.GUO,G.DU       
JRNL        TITL   ROLES OF TRYPTOPHAN RESIDUE AND DISULFIDE BOND IN THE        
JRNL        TITL 2 VARIABLE LID REGION OF OXIDIZED POLYVINYL ALCOHOL HYDROLASE  
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 452   509 2014              
JRNL        REFN                   ISSN 0006-291X                               
JRNL        PMID   25173935                                                     
JRNL        DOI    10.1016/J.BBRC.2014.08.106                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.49 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.21                                             
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) : 1.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 50987                          
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) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.173                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2546                            
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) : 1.49                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320                       
REMARK   3   BIN FREE R VALUE                    : 0.2590                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 203                          
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            : 2570                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 556                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.62700                                              
REMARK   3    B22 (A**2) : 1.57700                                              
REMARK   3    B33 (A**2) : -3.20400                                             
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.14                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.10                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.13                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.017                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.790                           
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) : 1.156 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.766 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.031 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.924 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 42.39                                                
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  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : BUTYL_ACID.PARAM                               
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  4  : CITRATE_ACID.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 3WWC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUL-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB096874.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-SEP-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
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                                  
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   : 52709                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.490                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 24.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.000                              
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: PDB ENTRY 3WL6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE, PH 5.6, 30%     
REMARK 280  W/V POLYETHYLENE GLYCOL 4000, 0.3% W/V N-OCTYL-BETA-D-GLUCOSIDE,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       29.16300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.16700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.61800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.16700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.16300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.61800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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     ALA A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     ALA A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     ASP A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     ASN A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     THR A    15                                                      
REMARK 465     GLU A    16                                                      
REMARK 465     PRO A    17                                                      
REMARK 465     SER A   353                                                      
REMARK 465     HIS A   354                                                      
REMARK 465     PRO A   355                                                      
REMARK 465     GLN A   356                                                      
REMARK 465     PHE A   357                                                      
REMARK 465     GLU A   358                                                      
REMARK 465     LYS A   359                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   693     O    HOH A   964              1.97            
REMARK 500   C1   BUA A   402     C2   BUA A   403              1.97            
REMARK 500   O    HOH A   738     O    HOH A   882              2.00            
REMARK 500   O    HOH A   712     O    HOH A  1028              2.01            
REMARK 500   C2   BUA A   402     C1   BUA A   403              2.05            
REMARK 500   O    HOH A   558     O    HOH A   983              2.06            
REMARK 500   O    HOH A   519     O    HOH A  1006              2.07            
REMARK 500   O    HOH A   564     O    HOH A  1023              2.08            
REMARK 500   O    HOH A   587     O    HOH A   712              2.10            
REMARK 500   O    HOH A   932     O    HOH A  1024              2.15            
REMARK 500   O    HOH A   882     O    HOH A  1004              2.17            
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  81       58.29     36.77                                   
REMARK 500    ARG A 107     -102.46   -102.12                                   
REMARK 500    ASN A 139       32.46   -142.36                                   
REMARK 500    ALA A 172     -120.73     63.15                                   
REMARK 500    HIS A 298       79.03   -113.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 337         0.07    SIDE CHAIN                              
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 841        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH A 872        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH A 886        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH A 920        DISTANCE =  6.58 ANGSTROMS                       
REMARK 525    HOH A 939        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH A 959        DISTANCE = 10.61 ANGSTROMS                       
REMARK 525    HOH A 961        DISTANCE =  8.21 ANGSTROMS                       
REMARK 525    HOH A 971        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH A 973        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH A 986        DISTANCE =  5.64 ANGSTROMS                       
REMARK 525    HOH A1002        DISTANCE =  7.99 ANGSTROMS                       
REMARK 525    HOH A1027        DISTANCE =  8.10 ANGSTROMS                       
REMARK 525    HOH A1054        DISTANCE =  7.55 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BUA A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BUA A 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3WWC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3WWE   RELATED DB: PDB                                   
DBREF  3WWC A   -1   348  UNP    Q9LCQ7   OPH_PSESP       30    379             
SEQADV 3WWC ALA A   -4  UNP  Q9LCQ7              EXPRESSION TAG                 
SEQADV 3WWC GLY A   -3  UNP  Q9LCQ7              EXPRESSION TAG                 
SEQADV 3WWC ALA A   -2  UNP  Q9LCQ7              EXPRESSION TAG                 
SEQADV 3WWC ALA A  172  UNP  Q9LCQ7    SER   203 ENGINEERED MUTATION            
SEQADV 3WWC ALA A  349  UNP  Q9LCQ7              EXPRESSION TAG                 
SEQADV 3WWC SER A  350  UNP  Q9LCQ7              EXPRESSION TAG                 
SEQADV 3WWC ALA A  351  UNP  Q9LCQ7              EXPRESSION TAG                 
SEQADV 3WWC TRP A  352  UNP  Q9LCQ7              EXPRESSION TAG                 
SEQADV 3WWC SER A  353  UNP  Q9LCQ7              EXPRESSION TAG                 
SEQADV 3WWC HIS A  354  UNP  Q9LCQ7              EXPRESSION TAG                 
SEQADV 3WWC PRO A  355  UNP  Q9LCQ7              EXPRESSION TAG                 
SEQADV 3WWC GLN A  356  UNP  Q9LCQ7              EXPRESSION TAG                 
SEQADV 3WWC PHE A  357  UNP  Q9LCQ7              EXPRESSION TAG                 
SEQADV 3WWC GLU A  358  UNP  Q9LCQ7              EXPRESSION TAG                 
SEQADV 3WWC LYS A  359  UNP  Q9LCQ7              EXPRESSION TAG                 
SEQRES   1 A  364  ALA GLY ALA GLY ALA ASP ARG THR ALA ALA THR PRO ALA          
SEQRES   2 A  364  ALA ALA ASN PRO ALA ALA THR GLU PRO VAL LYS TRP GLU          
SEQRES   3 A  364  CYS PRO ALA GLY TYR GLU VAL LYS GLU GLY LEU ASN VAL          
SEQRES   4 A  364  ASP PHE PRO HIS LYS GLY MET LYS ARG ALA PHE ILE VAL          
SEQRES   5 A  364  TYR PRO ALA LYS ASN VAL SER GLY PRO ALA PRO VAL TRP          
SEQRES   6 A  364  VAL PRO MET THR GLY SER VAL GLU SER THR ASN ASP ASN          
SEQRES   7 A  364  LEU THR VAL ALA ARG SER GLY ALA ASN SER ILE LEU ALA          
SEQRES   8 A  364  ASP HIS GLY TYR THR VAL ILE ALA PRO VAL ARG ALA CYS          
SEQRES   9 A  364  ALA ASN GLN ASP PRO ASN ILE ARG GLY GLU ARG CYS ASN          
SEQRES  10 A  364  GLY PRO GLY SER ASN GLY TRP ASN TRP ASN PRO TRP PHE          
SEQRES  11 A  364  GLU GLY ARG ALA ALA ASP PRO SER GLY GLU HIS TRP LYS          
SEQRES  12 A  364  ASN ASP GLU GLY PRO ASP SER SER PHE PHE VAL ALA MET          
SEQRES  13 A  364  VAL GLN CYS VAL GLY THR LYS TYR LYS LEU ASP ALA ARG          
SEQRES  14 A  364  ARG LEU PHE LEU GLY GLY ILE ALA SER GLY GLY THR MET          
SEQRES  15 A  364  THR ASN ARG ALA LEU LEU PHE ARG SER ASN PHE TRP ALA          
SEQRES  16 A  364  GLY GLY LEU PRO ILE SER GLY GLU TRP TYR VAL THR SER          
SEQRES  17 A  364  ASP ASP GLY THR PRO LEU SER PHE ASP ASP ALA ARG ALA          
SEQRES  18 A  364  ALA VAL ALA ALA ALA PRO THR LYS ILE HIS GLN GLY ARG          
SEQRES  19 A  364  VAL GLY PRO TYR PRO LEU PRO ALA LYS VAL GLY PRO LEU          
SEQRES  20 A  364  ILE VAL MET THR VAL TRP GLY GLY GLU LYS ASP LEU TRP          
SEQRES  21 A  364  ASN CYS THR ARG PRO ASP GLY SER ARG PHE LEU CYS ALA          
SEQRES  22 A  364  ASP TYR ARG PRO SER THR GLN ALA GLY SER ASN PHE PHE          
SEQRES  23 A  364  SER ALA GLN PRO ASP VAL VAL HIS VAL ALA CYS SER SER          
SEQRES  24 A  364  THR HIS GLY HIS MET TRP PRO GLN LEU ASN THR GLN GLU          
SEQRES  25 A  364  PHE ASN ARG TRP ALA LEU ASP THR LEU ALA SER HIS PRO          
SEQRES  26 A  364  LYS GLY SER ASP PRO ARG SER PHE LYS LEU THR GLN PRO          
SEQRES  27 A  364  PRO GLU GLY TYR THR CYS HIS VAL GLY PRO PHE THR GLY          
SEQRES  28 A  364  LEU TYR ALA SER ALA TRP SER HIS PRO GLN PHE GLU LYS          
HET    CIT  A 401      13                                                       
HET    BUA  A 402       6                                                       
HET    BUA  A 403       6                                                       
HETNAM     CIT CITRIC ACID                                                      
HETNAM     BUA BUTANOIC ACID                                                    
FORMUL   2  CIT    C6 H8 O7                                                     
FORMUL   3  BUA    2(C4 H8 O2)                                                  
FORMUL   5  HOH   *556(H2 O)                                                    
HELIX    1   1 SER A   69  VAL A   76  1                                   8    
HELIX    2   2 ALA A   77  GLY A   80  5                                   4    
HELIX    3   3 ALA A   81  GLY A   89  5                                   9    
HELIX    4   4 ARG A   97  ASN A  101  5                                   5    
HELIX    5   5 ASP A  131  ASN A  139  5                                   9    
HELIX    6   6 GLY A  142  GLY A  156  1                                  15    
HELIX    7   7 ALA A  172  ARG A  185  1                                  14    
HELIX    8   8 SER A  210  ALA A  221  1                                  12    
HELIX    9   9 TYR A  270  GLN A  284  1                                  15    
HELIX   10  10 ASN A  304  SER A  318  1                                  15    
HELIX   11  11 ASP A  324  PHE A  328  5                                   5    
SHEET    1   A 9 GLY A  31  HIS A  38  0                                        
SHEET    2   A 9 MET A  41  TYR A  48 -1  O  PHE A  45   N  ASN A  33           
SHEET    3   A 9 THR A  91  PRO A  95 -1  O  VAL A  92   N  TYR A  48           
SHEET    4   A 9 ALA A  57  MET A  63  1  N  PRO A  58   O  THR A  91           
SHEET    5   A 9 LEU A 161  ILE A 171  1  O  ASP A 162   N  ALA A  57           
SHEET    6   A 9 GLY A 191  ILE A 195  1  O  ILE A 195   N  GLY A 170           
SHEET    7   A 9 LEU A 242  TRP A 248  1  O  MET A 245   N  GLY A 192           
SHEET    8   A 9 VAL A 287  SER A 293  1  O  VAL A 290   N  VAL A 244           
SHEET    9   A 9 THR A 338  VAL A 341 -1  O  THR A 338   N  SER A 293           
SHEET    1   B 2 LEU A 254  THR A 258  0                                        
SHEET    2   B 2 ARG A 264  ASP A 269 -1  O  CYS A 267   N  TRP A 255           
SSBOND   1 CYS A   22    CYS A  154                          1555   1555  2.10  
SSBOND   2 CYS A   99    CYS A  111                          1555   1555  2.09  
SSBOND   3 CYS A  257    CYS A  267                          1555   1555  2.05  
SSBOND   4 CYS A  292    CYS A  339                          1555   1555  2.06  
CISPEP   1 TYR A  233    PRO A  234          0        -1.23                     
SITE     1 AC1 12 ARG A 110  ASN A 304  THR A 305  GLN A 306                    
SITE     2 AC1 12 GLU A 307  ARG A 310  HOH A 517  HOH A 678                    
SITE     3 AC1 12 HOH A 701  HOH A 783  HOH A 989  HOH A1021                    
SITE     1 AC2  9 SER A  66  TRP A 121  ALA A 172  SER A 173                    
SITE     2 AC2  9 TRP A 255  TYR A 270  HIS A 298  BUA A 403                    
SITE     3 AC2  9 HOH A 632                                                     
SITE     1 AC3  4 ASN A 120  CYS A 257  BUA A 402  HOH A 772                    
CRYST1   58.326   65.236   84.334  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017145  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015329  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011858        0.00000                         
TER    2571      TRP A 352                                                      
MASTER      355    0    3   11   11    0    7    6 3151    1   33   28          
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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