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LongText Report for: 3WYD-pdb

Name Class
3WYD-pdb
HEADER    HYDROLASE                               26-AUG-14   3WYD              
TITLE     C-TERMINAL ESTERASE DOMAIN OF LC-EST1                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LC-EST1C;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UNCULTURED ORGANISM;                            
SOURCE   3 ORGANISM_TAXID: 155900;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    LEAF-BRANCH COMPOST; METAGENOME, ALPHA/BETA HYDROLASE FOLD, ESTERASE, 
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.OKANO,X.HONG,C.ANGKAWIDJAJA,S.KANAYA                                
REVDAT   1   12-NOV-14 3WYD    0                                                
JRNL        AUTH   H.OKANO,X.HONG,E.KANAYA,C.ANGKAWIDJAJA,S.KANAYA              
JRNL        TITL   STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF A             
JRNL        TITL 2 METAGENOME-DERIVED ESTERASE WITH A LONG N-TERMINAL EXTENSION 
JRNL        REF    PROTEIN SCI.                               2014              
JRNL        REFN                   ESSN 1469-896X                               
JRNL        PMID   25348365                                                     
JRNL        DOI    10.1002/PRO.2591                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.53 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.53                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 56727                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3030                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.53                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4164                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 233                          
REMARK   3   BIN FREE R VALUE                    : 0.2940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2992                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 451                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : -0.03000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.085         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.087         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.048         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.281         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3073 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4162 ; 1.439 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   380 ; 6.535 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   143 ;31.669 ;22.867       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   479 ;13.999 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;20.109 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   432 ; 0.116 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2393 ; 0.017 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1901 ; 1.649 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3053 ; 2.563 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1172 ; 3.798 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1109 ; 5.707 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3WYD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-AUG-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB096947.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAY-14; 18-JUL-14               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SPRING-8; SPRING-8                 
REMARK 200  BEAMLINE                       : BL44XU; BL44XU                     
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9; 0.978769, 0.979101, 0.994813  
REMARK 200  MONOCHROMATOR                  : ROTATED-INCLINED DOUBLE CRYSTAL;   
REMARK 200                                   ROTATED-INCLINED DOUBLE CRYSTAL    
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE; RAYONIX MX225HE   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60179                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.530                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 78.140                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.18100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CHLORIDE, 0.1M BIS-TRIS,     
REMARK 280  25% PEG3,350, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  293K                                                                
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       22.93050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       78.13750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.72300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       78.13750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.93050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       27.72300            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   283                                                      
REMARK 465     GLY A   284                                                      
REMARK 465     SER A   285                                                      
REMARK 465     SER A   286                                                      
REMARK 465     HIS A   287                                                      
REMARK 465     HIS A   288                                                      
REMARK 465     HIS A   289                                                      
REMARK 465     HIS A   290                                                      
REMARK 465     HIS A   291                                                      
REMARK 465     HIS A   292                                                      
REMARK 465     SER A   293                                                      
REMARK 465     SER A   294                                                      
REMARK 465     GLY A   295                                                      
REMARK 465     LEU A   296                                                      
REMARK 465     VAL A   297                                                      
REMARK 465     PRO A   298                                                      
REMARK 465     ARG A   299                                                      
REMARK 465     GLY A   300                                                      
REMARK 465     SER A   301                                                      
REMARK 465     HIS A   302                                                      
REMARK 465     MET A   303                                                      
REMARK 465     ARG A   361                                                      
REMARK 465     GLN A   362                                                      
REMARK 465     PRO A   363                                                      
REMARK 465     ALA A   364                                                      
REMARK 465     SER A   365                                                      
REMARK 465     MET A   366                                                      
REMARK 465     ALA A   503                                                      
REMARK 465     ALA A   504                                                      
REMARK 465     LYS A   505                                                      
REMARK 465     ALA A   506                                                      
REMARK 465     ALA A   507                                                      
REMARK 465     THR A   508                                                      
REMARK 465     ASN A   509                                                      
REMARK 465     LYS A   510                                                      
REMARK 465     MET B   283                                                      
REMARK 465     GLY B   284                                                      
REMARK 465     SER B   285                                                      
REMARK 465     SER B   286                                                      
REMARK 465     HIS B   287                                                      
REMARK 465     HIS B   288                                                      
REMARK 465     HIS B   289                                                      
REMARK 465     HIS B   290                                                      
REMARK 465     HIS B   291                                                      
REMARK 465     HIS B   292                                                      
REMARK 465     SER B   293                                                      
REMARK 465     SER B   294                                                      
REMARK 465     GLY B   295                                                      
REMARK 465     LEU B   296                                                      
REMARK 465     VAL B   297                                                      
REMARK 465     PRO B   298                                                      
REMARK 465     ARG B   299                                                      
REMARK 465     GLY B   300                                                      
REMARK 465     SER B   301                                                      
REMARK 465     HIS B   302                                                      
REMARK 465     MET B   303                                                      
REMARK 465     ARG B   361                                                      
REMARK 465     GLN B   362                                                      
REMARK 465     PRO B   363                                                      
REMARK 465     ALA B   364                                                      
REMARK 465     SER B   365                                                      
REMARK 465     MET B   366                                                      
REMARK 465     ARG B   501                                                      
REMARK 465     PRO B   502                                                      
REMARK 465     ALA B   503                                                      
REMARK 465     ALA B   504                                                      
REMARK 465     LYS B   505                                                      
REMARK 465     ALA B   506                                                      
REMARK 465     ALA B   507                                                      
REMARK 465     THR B   508                                                      
REMARK 465     ASN B   509                                                      
REMARK 465     LYS B   510                                                      
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    SER A 338     -157.88   -113.19                                   
REMARK 500    TYR A 339       71.34     51.64                                   
REMARK 500    SER A 399     -118.17     68.14                                   
REMARK 500    SER B 338     -167.12   -116.92                                   
REMARK 500    SER B 399     -114.83     67.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE OF THIS PROTEIN WAS NOT AVAILABLE AT THE UNIPROT        
REMARK 999 KNOWLEDGEBASE DATABASE (UNIPROTKB) AT THE TIME OF DEPOSITION.        
REMARK 999 AUTHORS STATE THAT THE GENEBANK ACCESSION NUMBER IS KM406409 FOR     
REMARK 999 THE SEQUENCE.                                                        
DBREF  3WYD A  283   510  PDB    3WYD     3WYD           283    510             
DBREF  3WYD B  283   510  PDB    3WYD     3WYD           283    510             
SEQRES   1 A  228  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  228  LEU VAL PRO ARG GLY SER HIS MET PRO TYR ARG LEU TYR          
SEQRES   3 A  228  VAL PRO THR THR TYR ASP GLY THR LYS ALA PHE PRO LEU          
SEQRES   4 A  228  VAL ILE ALA LEU HIS GLY MET GLY GLY ASP GLU ASN SER          
SEQRES   5 A  228  TYR PHE ASP SER TYR GLN ARG GLY ALA PHE MET ILE GLU          
SEQRES   6 A  228  ALA GLU ASN ARG GLY TYR ILE VAL ALA CYS PRO LYS GLY          
SEQRES   7 A  228  ARG GLN PRO ALA SER MET TYR VAL GLY PRO ALA GLU ARG          
SEQRES   8 A  228  ASP VAL MET ASP VAL ILE ALA GLU VAL ARG ARG ASP TYR          
SEQRES   9 A  228  LYS ILE ASP PRO ASP ARG ILE TYR MET THR GLY HIS SER          
SEQRES  10 A  228  MET GLY GLY TYR GLY THR TRP SER ILE ALA MET ASN HIS          
SEQRES  11 A  228  PRO ASP VAL PHE ALA ALA LEU ALA PRO VAL ALA GLY GLY          
SEQRES  12 A  228  GLY ASN PRO LEU GLY MET ALA ASN ILE ALA HIS ILE PRO          
SEQRES  13 A  228  GLN LEU VAL VAL HIS GLY ASP ASN ASP LYS THR VAL PRO          
SEQRES  14 A  228  VAL GLU ARG SER ARG VAL MET VAL GLU ALA ALA LYS LYS          
SEQRES  15 A  228  HIS GLY THR GLU ILE LYS TYR ILE GLU ILE PRO GLY GLY          
SEQRES  16 A  228  ASP HIS VAL SER VAL ALA ALA ARG THR PHE LYS ASP VAL          
SEQRES  17 A  228  PHE ASP TRP PHE ASP SER HIS LYS ARG LYS ARG PRO ALA          
SEQRES  18 A  228  ALA LYS ALA ALA THR ASN LYS                                  
SEQRES   1 B  228  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  228  LEU VAL PRO ARG GLY SER HIS MET PRO TYR ARG LEU TYR          
SEQRES   3 B  228  VAL PRO THR THR TYR ASP GLY THR LYS ALA PHE PRO LEU          
SEQRES   4 B  228  VAL ILE ALA LEU HIS GLY MET GLY GLY ASP GLU ASN SER          
SEQRES   5 B  228  TYR PHE ASP SER TYR GLN ARG GLY ALA PHE MET ILE GLU          
SEQRES   6 B  228  ALA GLU ASN ARG GLY TYR ILE VAL ALA CYS PRO LYS GLY          
SEQRES   7 B  228  ARG GLN PRO ALA SER MET TYR VAL GLY PRO ALA GLU ARG          
SEQRES   8 B  228  ASP VAL MET ASP VAL ILE ALA GLU VAL ARG ARG ASP TYR          
SEQRES   9 B  228  LYS ILE ASP PRO ASP ARG ILE TYR MET THR GLY HIS SER          
SEQRES  10 B  228  MET GLY GLY TYR GLY THR TRP SER ILE ALA MET ASN HIS          
SEQRES  11 B  228  PRO ASP VAL PHE ALA ALA LEU ALA PRO VAL ALA GLY GLY          
SEQRES  12 B  228  GLY ASN PRO LEU GLY MET ALA ASN ILE ALA HIS ILE PRO          
SEQRES  13 B  228  GLN LEU VAL VAL HIS GLY ASP ASN ASP LYS THR VAL PRO          
SEQRES  14 B  228  VAL GLU ARG SER ARG VAL MET VAL GLU ALA ALA LYS LYS          
SEQRES  15 B  228  HIS GLY THR GLU ILE LYS TYR ILE GLU ILE PRO GLY GLY          
SEQRES  16 B  228  ASP HIS VAL SER VAL ALA ALA ARG THR PHE LYS ASP VAL          
SEQRES  17 B  228  PHE ASP TRP PHE ASP SER HIS LYS ARG LYS ARG PRO ALA          
SEQRES  18 B  228  ALA LYS ALA ALA THR ASN LYS                                  
FORMUL   3  HOH   *451(H2 O)                                                    
HELIX    1   1 ASN A  333  SER A  338  1                                   6    
HELIX    2   2 SER A  338  GLY A  352  1                                  15    
HELIX    3   3 GLY A  369  TYR A  386  1                                  18    
HELIX    4   4 SER A  399  HIS A  412  1                                  14    
HELIX    5   5 ASN A  427  ALA A  435  5                                   9    
HELIX    6   6 VAL A  452  LYS A  464  1                                  13    
HELIX    7   7 SER A  481  THR A  486  1                                   6    
HELIX    8   8 THR A  486  SER A  496  1                                  11    
HELIX    9   9 ASN B  333  SER B  338  1                                   6    
HELIX   10  10 SER B  338  GLY B  352  1                                  15    
HELIX   11  11 GLY B  369  TYR B  386  1                                  18    
HELIX   12  12 SER B  399  HIS B  412  1                                  14    
HELIX   13  13 ASN B  427  ALA B  435  5                                   9    
HELIX   14  14 VAL B  452  HIS B  465  1                                  14    
HELIX   15  15 SER B  481  THR B  486  1                                   6    
HELIX   16  16 THR B  486  SER B  496  1                                  11    
SHEET    1   A 5 TYR A 305  TYR A 308  0                                        
SHEET    2   A 5 ILE A 354  PRO A 358 -1  O  CYS A 357   N  ARG A 306           
SHEET    3   A 5 PHE A 319  LEU A 325  1  N  VAL A 322   O  ALA A 356           
SHEET    4   A 5 ILE A 388  HIS A 398  1  O  TYR A 394   N  LEU A 321           
SHEET    5   A 5 ALA A 418  VAL A 422  1  O  VAL A 422   N  GLY A 397           
SHEET    1   B 2 GLN A 439  GLY A 444  0                                        
SHEET    2   B 2 ILE A 469  ILE A 474  1  O  ILE A 472   N  VAL A 441           
SHEET    1   C 5 TYR B 305  TYR B 308  0                                        
SHEET    2   C 5 ILE B 354  PRO B 358 -1  O  CYS B 357   N  ARG B 306           
SHEET    3   C 5 PHE B 319  LEU B 325  1  N  VAL B 322   O  ALA B 356           
SHEET    4   C 5 ILE B 388  HIS B 398  1  O  TYR B 394   N  LEU B 321           
SHEET    5   C 5 ALA B 418  VAL B 422  1  O  VAL B 422   N  GLY B 397           
SHEET    1   D 2 GLN B 439  GLY B 444  0                                        
SHEET    2   D 2 ILE B 469  ILE B 474  1  O  ILE B 472   N  VAL B 441           
CRYST1   45.861   55.446  156.275  90.00  90.00  90.00 P 21 21 21    8          
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      0.021805  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018036  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006399        0.00000                         
TER    1506      PRO A 502                                                      
TER    2994      LYS B 500                                                      
MASTER      347    0    0   16   14    0    0    6 3443    2    0   36          
END                                                                             

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