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LongText Report for: 3WJ2-pdb

Name Class
3WJ2-pdb
HEADER    HYDROLASE                               03-OCT-13   3WJ2              
TITLE     CRYSTAL STRUCTURE OF ESTFA (FE-LACKING APO FORM)                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXYLESTERASE;                                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 3.1.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: FERROPLASMA ACIDIPHILUM;                        
SOURCE   3 ORGANISM_TAXID: 74969;                                               
SOURCE   4 GENE: EST;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    ALPHA/BETA-HYDRORASE FOLD, CARBOXYLESTERASE, HYDROLASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.OHARA,H.UNNO,Y.OSHIMA,K.FURUKAWA,N.FUJINO,K.HIROOKA,H.HEMMI,        
AUTHOR   2 S.TAKAHASHI,T.NISHINO,M.KUSUNOKI,T.NAKAYAMA                          
REVDAT   1   30-JUL-14 3WJ2    0                                                
JRNL        AUTH   K.OHARA,H.UNNO,Y.OSHIMA,M.HOSOYA,N.FUJINO,K.HIROOKA,         
JRNL        AUTH 2 S.TAKAHASHI,S.YAMASHITA,M.KUSUNOKI,T.NAKAYAMA                
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE LOW-PH ADAPTATION OF A UNIQUE   
JRNL        TITL 2 CARBOXYLESTERASE FROM FERROPLASMA: ALTERING THE PH OPTIMA OF 
JRNL        TITL 3 TWO CARBOXYLESTERASES                                        
JRNL        REF    J.BIOL.CHEM.                               2014              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        DOI    10.1074/JBC.M113.521856                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.61 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) : 1.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 158320                         
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8382                            
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) : 1.61                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.65                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10768                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.13                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2990                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 546                          
REMARK   3   BIN FREE R VALUE                    : 0.3510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9444                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 983                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.14000                                              
REMARK   3    B22 (A**2) : 0.03000                                              
REMARK   3    B33 (A**2) : -0.17000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.02000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.095         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.062         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.751         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9648 ; 0.029 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13013 ; 2.395 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1191 ; 6.378 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   455 ;31.951 ;23.846       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1659 ;15.117 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    64 ;17.974 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1383 ; 0.171 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7400 ; 0.014 ; 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):  5959 ; 1.532 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9564 ; 2.418 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3689 ; 3.551 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3449 ; 5.332 ; 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 3WJ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-OCT-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB096397.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200                                   MONOCHROMATOR                      
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   : 166739                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.610                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 3350, 100MM SODIUM ACETATE, PH   
REMARK 280  8.0, VAPOR DIFFUSION, TEMPERATURE 293K                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       68.68000            
REMARK 290   SMTRY3   2  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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10010 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, B, C                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     MET A   221                                                      
REMARK 465     GLN A   222                                                      
REMARK 465     ASP A   223                                                      
REMARK 465     LEU A   224                                                      
REMARK 465     MET B     1                                                      
REMARK 465     HIS B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     MET B   221                                                      
REMARK 465     GLN B   222                                                      
REMARK 465     ASP B   223                                                      
REMARK 465     LEU B   224                                                      
REMARK 465     MET C     1                                                      
REMARK 465     HIS C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     MET C     4                                                      
REMARK 465     MET C   221                                                      
REMARK 465     GLN C   222                                                      
REMARK 465     ASP C   223                                                      
REMARK 465     LEU C   224                                                      
REMARK 465     MET D     1                                                      
REMARK 465     HIS D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     MET D     4                                                      
REMARK 465     MET D   221                                                      
REMARK 465     GLN D   222                                                      
REMARK 465     ASP D   223                                                      
REMARK 465     LEU D   224                                                      
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   CG   MET B    69     O    HOH B   449              1.80            
REMARK 500   O    HOH B   554     O    HOH B   673              1.86            
REMARK 500   O    HOH B   456     O    HOH B   517              1.86            
REMARK 500   NH1  ARG C   116     OD1  ASP C   129              1.87            
REMARK 500   O    HOH C   476     O    HOH C   617              1.88            
REMARK 500   O    HOH B   574     O    HOH B   629              1.90            
REMARK 500   O    HOH D   512     O    HOH D   557              1.92            
REMARK 500   CD   ARG A   116     OD2  ASP A   129              1.92            
REMARK 500   O    HOH C   429     O    HOH C   474              1.92            
REMARK 500   O    HOH A   614     O    HOH A   653              1.96            
REMARK 500   NH2  ARG A   170     O    ASP A   236              1.97            
REMARK 500   N    ASN B     5     O    HOH B   661              1.99            
REMARK 500   O    ASP B   201     N    TYR B   203              2.01            
REMARK 500   NH1  ARG A   265     O    HOH A   448              2.01            
REMARK 500   O    HOH A   504     O    HOH C   607              2.02            
REMARK 500   ND2  ASN D   128     O    HOH D   577              2.02            
REMARK 500   O    HOH C   579     O    HOH C   603              2.05            
REMARK 500   O    HOH C   417     O    HOH C   601              2.05            
REMARK 500   N    ASN D     5     O    HOH D   448              2.07            
REMARK 500   O    HOH B   543     O    HOH B   579              2.07            
REMARK 500   O    HOH A   560     O    HOH A   640              2.08            
REMARK 500   O    HOH A   460     O    HOH A   612              2.09            
REMARK 500   OH   TYR A   217     O    HOH A   652              2.09            
REMARK 500   O    HOH A   544     O    HOH A   645              2.09            
REMARK 500   O    HOH D   456     O    HOH D   570              2.10            
REMARK 500   C    ASN B   220     O    HOH B   451              2.11            
REMARK 500   O    HOH B   586     O    HOH C   612              2.12            
REMARK 500   O    HOH A   505     O    HOH A   522              2.13            
REMARK 500   OG   SER B   200     O    HOH B   545              2.14            
REMARK 500   O    HOH A   476     O    HOH B   519              2.14            
REMARK 500   O    HOH A   591     O    HOH A   675              2.14            
REMARK 500   NZ   LYS D   142     O    HOH D   573              2.15            
REMARK 500   O    HOH D   444     O    HOH D   580              2.17            
REMARK 500   O    HOH A   515     O    HOH A   658              2.18            
REMARK 500   OH   TYR C   217     O    HOH C   583              2.19            
REMARK 500   O    ASN B   202     O    HOH B   663              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLU A 257   CD    GLU A 257   OE2     0.072                       
REMARK 500    VAL A 261   CB    VAL A 261   CG1    -0.164                       
REMARK 500    VAL A 261   CB    VAL A 261   CG2    -0.160                       
REMARK 500    TYR B  95   CD1   TYR B  95   CE1     0.094                       
REMARK 500    PHE B 123   CE1   PHE B 123   CZ      0.118                       
REMARK 500    MET B 176   CB    MET B 176   CG      0.259                       
REMARK 500    VAL B 261   CB    VAL B 261   CG2    -0.158                       
REMARK 500    TYR C  70   CE1   TYR C  70   CZ      0.081                       
REMARK 500    TYR C 228   CE1   TYR C 228   CZ      0.091                       
REMARK 500    VAL C 261   CB    VAL C 261   CG1    -0.176                       
REMARK 500    GLU C 288   CD    GLU C 288   OE2    -0.068                       
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    TYR A  98   CB  -  CG  -  CD2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG A 116   CG  -  CD  -  NE  ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ARG A 116   CD  -  NE  -  CZ  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    ARG A 116   NE  -  CZ  -  NH1 ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ARG A 116   NE  -  CZ  -  NH2 ANGL. DEV. = -10.1 DEGREES          
REMARK 500    ASP A 132   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG A 170   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG A 170   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG A 254   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 265   CD  -  NE  -  CZ  ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ARG A 265   NE  -  CZ  -  NH1 ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ARG A 265   NE  -  CZ  -  NH2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG A 270   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 294   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    MET B  69   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    LEU B  88   CB  -  CG  -  CD2 ANGL. DEV. = -11.0 DEGREES          
REMARK 500    TYR B  98   CB  -  CG  -  CD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    TYR B  98   CD1 -  CE1 -  CZ  ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG B 100   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B 116   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    MET B 176   CB  -  CG  -  SD  ANGL. DEV. = -23.7 DEGREES          
REMARK 500    MET B 176   CG  -  SD  -  CE  ANGL. DEV. = -11.8 DEGREES          
REMARK 500    ASP B 251   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ASP B 251   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    TYR B 260   CB  -  CG  -  CD1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG B 275   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    MET B 299   CG  -  SD  -  CE  ANGL. DEV. = -21.3 DEGREES          
REMARK 500    ASP C   8   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG C  63   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG C  68   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ASP C  96   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    MET C 216   CG  -  SD  -  CE  ANGL. DEV. = -12.4 DEGREES          
REMARK 500    ASN C 220   N   -  CA  -  C   ANGL. DEV. =  17.5 DEGREES          
REMARK 500    ASN C 220   C   -  N   -  CA  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    ARG C 270   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    LEU D  80   CB  -  CG  -  CD1 ANGL. DEV. =  11.4 DEGREES          
REMARK 500    ARG D 116   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG D 270   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG D 275   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.9 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    ASN A  73       24.76   -148.64                                   
REMARK 500    ASN A  74       55.40     37.90                                   
REMARK 500    SER A 156     -119.86     46.56                                   
REMARK 500    TYR A 184       63.22     36.56                                   
REMARK 500    PHE A 192      -10.42   -150.27                                   
REMARK 500    ASN A 202        0.83     82.29                                   
REMARK 500    VAL A 204      -65.19     69.67                                   
REMARK 500    TYR A 250       73.50   -109.96                                   
REMARK 500    ASN B  73       22.44   -150.13                                   
REMARK 500    ASN B  74       50.77     34.67                                   
REMARK 500    PHE B  87        0.08     80.03                                   
REMARK 500    SER B 156     -127.56     55.22                                   
REMARK 500    TYR B 184       64.59     37.46                                   
REMARK 500    PHE B 192      -13.21   -151.74                                   
REMARK 500    ASN B 202       43.44    -54.14                                   
REMARK 500    TYR B 203      -39.73     73.55                                   
REMARK 500    TYR B 250       69.57   -111.10                                   
REMARK 500    ASP C  61       98.94    -64.15                                   
REMARK 500    ASN C  73       26.89   -151.21                                   
REMARK 500    ASN C  74       48.84     38.62                                   
REMARK 500    SER C 156     -125.87     51.75                                   
REMARK 500    TYR C 184       61.09     39.95                                   
REMARK 500    PHE C 192       -7.56   -150.81                                   
REMARK 500    ASP C 201      -50.61   -121.64                                   
REMARK 500    VAL C 204      -59.60     69.17                                   
REMARK 500    TYR C 250       70.08   -106.24                                   
REMARK 500    MET D   6       50.80   -118.72                                   
REMARK 500    SER D  42      -94.03    -65.08                                   
REMARK 500    SER D  43       40.79    -74.51                                   
REMARK 500    ASP D  61       99.17    -47.35                                   
REMARK 500    ASN D  73       21.73   -150.80                                   
REMARK 500    ASN D  74       58.93     37.56                                   
REMARK 500    PHE D  89     -169.28   -124.82                                   
REMARK 500    LYS D 140       41.38   -101.94                                   
REMARK 500    SER D 156     -123.25     60.14                                   
REMARK 500    TYR D 184       66.15     35.21                                   
REMARK 500    PHE D 192       -4.64   -149.09                                   
REMARK 500    ASN D 202       -3.35     84.79                                   
REMARK 500    TYR D 203       43.44   -108.12                                   
REMARK 500    VAL D 204      -61.90     73.37                                   
REMARK 500    LYS D 219     -104.29    -88.48                                   
REMARK 500    TYR D 250       77.00   -106.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ILE A 303        23.9      L          L   OUTSIDE RANGE           
REMARK 500    TYR B 203        20.9      L          L   OUTSIDE RANGE           
REMARK 500    ASP C 201        22.3      L          L   OUTSIDE RANGE           
REMARK 500    ASN C 220        16.9      L          L   OUTSIDE RANGE           
REMARK 500    ILE C 225        24.9      L          L   OUTSIDE RANGE           
REMARK 500    SER D  42        24.1      L          L   OUTSIDE RANGE           
REMARK 500    ILE D 225        23.9      L          L   OUTSIDE RANGE           
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 651        DISTANCE =  5.47 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3WJ1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P9N   RELATED DB: PDB                                   
DBREF  3WJ2 A    1   308  UNP    Q2PCE5   Q2PCE5_9EURY     1    308             
DBREF  3WJ2 B    1   308  UNP    Q2PCE5   Q2PCE5_9EURY     1    308             
DBREF  3WJ2 C    1   308  UNP    Q2PCE5   Q2PCE5_9EURY     1    308             
DBREF  3WJ2 D    1   308  UNP    Q2PCE5   Q2PCE5_9EURY     1    308             
SEQRES   1 A  308  MET HIS LEU MET ASN MET VAL ASP PRO ASP PHE ASN SER          
SEQRES   2 A  308  LEU ILE GLU LEU SER LYS SER ALA GLY ASP MET THR LYS          
SEQRES   3 A  308  ILE GLU PRO ALA MET LEU ARG ASN PHE LEU ASP GLU SER          
SEQRES   4 A  308  SER LEU SER SER ARG GLY ALA PRO VAL GLU ILE LYS GLU          
SEQRES   5 A  308  ILE LYS ASP TYR LYS ILE LYS LEU ASP GLY ARG THR LEU          
SEQRES   6 A  308  ASN ALA ARG MET TYR ASP ASP ASN ASN ALA LYS SER ALA          
SEQRES   7 A  308  ILE LEU TYR TYR HIS GLY GLY GLY PHE LEU PHE GLY ASN          
SEQRES   8 A  308  ILE GLU THR TYR ASP ASN TYR CYS ARG PHE LEU ALA LYS          
SEQRES   9 A  308  GLU SER GLY VAL LYS ILE ILE SER ILE GLU TYR ARG LEU          
SEQRES  10 A  308  ALA PRO GLU HIS LYS PHE PRO ASP ALA PHE ASN ASP ALA          
SEQRES  11 A  308  TYR ASP SER PHE HIS TYR ILE ALA LYS LYS LYS LYS ASP          
SEQRES  12 A  308  PHE GLY ILE GLU GLY ARG ILE GLY VAL ALA GLY ASP SER          
SEQRES  13 A  308  ALA GLY ALA ASN LEU ALA ALA ALA LEU CYS LEU LYS CYS          
SEQRES  14 A  308  ARG ASP GLY LYS THR GLU MET PRO ALA VAL GLN VAL LEU          
SEQRES  15 A  308  PHE TYR PRO SER LEU ALA PRO ASP ASN PHE SER ARG SER          
SEQRES  16 A  308  PHE ILE GLU TYR SER ASP ASN TYR VAL LEU THR GLY LYS          
SEQRES  17 A  308  MET ILE ARG TYR PHE GLY ASN MET TYR SER LYS ASN MET          
SEQRES  18 A  308  GLN ASP LEU ILE ASN PRO TYR PHE SER PRO LEU VAL ALA          
SEQRES  19 A  308  ASP ASP PHE SER ASN LEU PRO PRO ALA ILE MET VAL THR          
SEQRES  20 A  308  ASN GLU TYR ASP PRO LEU ARG ASP PRO GLU GLU THR TYR          
SEQRES  21 A  308  VAL LYS LYS LEU ARG GLU ALA GLY VAL ARG ALA VAL GLY          
SEQRES  22 A  308  ILE ARG GLY ILE GLY MET ILE HIS GLY SER ALA THR ASP          
SEQRES  23 A  308  PHE GLU VAL SER ASP GLY ALA ARG ASN ILE VAL LYS MET          
SEQRES  24 A  308  VAL ALA ARG ILE ILE PRO ASP TYR LEU                          
SEQRES   1 B  308  MET HIS LEU MET ASN MET VAL ASP PRO ASP PHE ASN SER          
SEQRES   2 B  308  LEU ILE GLU LEU SER LYS SER ALA GLY ASP MET THR LYS          
SEQRES   3 B  308  ILE GLU PRO ALA MET LEU ARG ASN PHE LEU ASP GLU SER          
SEQRES   4 B  308  SER LEU SER SER ARG GLY ALA PRO VAL GLU ILE LYS GLU          
SEQRES   5 B  308  ILE LYS ASP TYR LYS ILE LYS LEU ASP GLY ARG THR LEU          
SEQRES   6 B  308  ASN ALA ARG MET TYR ASP ASP ASN ASN ALA LYS SER ALA          
SEQRES   7 B  308  ILE LEU TYR TYR HIS GLY GLY GLY PHE LEU PHE GLY ASN          
SEQRES   8 B  308  ILE GLU THR TYR ASP ASN TYR CYS ARG PHE LEU ALA LYS          
SEQRES   9 B  308  GLU SER GLY VAL LYS ILE ILE SER ILE GLU TYR ARG LEU          
SEQRES  10 B  308  ALA PRO GLU HIS LYS PHE PRO ASP ALA PHE ASN ASP ALA          
SEQRES  11 B  308  TYR ASP SER PHE HIS TYR ILE ALA LYS LYS LYS LYS ASP          
SEQRES  12 B  308  PHE GLY ILE GLU GLY ARG ILE GLY VAL ALA GLY ASP SER          
SEQRES  13 B  308  ALA GLY ALA ASN LEU ALA ALA ALA LEU CYS LEU LYS CYS          
SEQRES  14 B  308  ARG ASP GLY LYS THR GLU MET PRO ALA VAL GLN VAL LEU          
SEQRES  15 B  308  PHE TYR PRO SER LEU ALA PRO ASP ASN PHE SER ARG SER          
SEQRES  16 B  308  PHE ILE GLU TYR SER ASP ASN TYR VAL LEU THR GLY LYS          
SEQRES  17 B  308  MET ILE ARG TYR PHE GLY ASN MET TYR SER LYS ASN MET          
SEQRES  18 B  308  GLN ASP LEU ILE ASN PRO TYR PHE SER PRO LEU VAL ALA          
SEQRES  19 B  308  ASP ASP PHE SER ASN LEU PRO PRO ALA ILE MET VAL THR          
SEQRES  20 B  308  ASN GLU TYR ASP PRO LEU ARG ASP PRO GLU GLU THR TYR          
SEQRES  21 B  308  VAL LYS LYS LEU ARG GLU ALA GLY VAL ARG ALA VAL GLY          
SEQRES  22 B  308  ILE ARG GLY ILE GLY MET ILE HIS GLY SER ALA THR ASP          
SEQRES  23 B  308  PHE GLU VAL SER ASP GLY ALA ARG ASN ILE VAL LYS MET          
SEQRES  24 B  308  VAL ALA ARG ILE ILE PRO ASP TYR LEU                          
SEQRES   1 C  308  MET HIS LEU MET ASN MET VAL ASP PRO ASP PHE ASN SER          
SEQRES   2 C  308  LEU ILE GLU LEU SER LYS SER ALA GLY ASP MET THR LYS          
SEQRES   3 C  308  ILE GLU PRO ALA MET LEU ARG ASN PHE LEU ASP GLU SER          
SEQRES   4 C  308  SER LEU SER SER ARG GLY ALA PRO VAL GLU ILE LYS GLU          
SEQRES   5 C  308  ILE LYS ASP TYR LYS ILE LYS LEU ASP GLY ARG THR LEU          
SEQRES   6 C  308  ASN ALA ARG MET TYR ASP ASP ASN ASN ALA LYS SER ALA          
SEQRES   7 C  308  ILE LEU TYR TYR HIS GLY GLY GLY PHE LEU PHE GLY ASN          
SEQRES   8 C  308  ILE GLU THR TYR ASP ASN TYR CYS ARG PHE LEU ALA LYS          
SEQRES   9 C  308  GLU SER GLY VAL LYS ILE ILE SER ILE GLU TYR ARG LEU          
SEQRES  10 C  308  ALA PRO GLU HIS LYS PHE PRO ASP ALA PHE ASN ASP ALA          
SEQRES  11 C  308  TYR ASP SER PHE HIS TYR ILE ALA LYS LYS LYS LYS ASP          
SEQRES  12 C  308  PHE GLY ILE GLU GLY ARG ILE GLY VAL ALA GLY ASP SER          
SEQRES  13 C  308  ALA GLY ALA ASN LEU ALA ALA ALA LEU CYS LEU LYS CYS          
SEQRES  14 C  308  ARG ASP GLY LYS THR GLU MET PRO ALA VAL GLN VAL LEU          
SEQRES  15 C  308  PHE TYR PRO SER LEU ALA PRO ASP ASN PHE SER ARG SER          
SEQRES  16 C  308  PHE ILE GLU TYR SER ASP ASN TYR VAL LEU THR GLY LYS          
SEQRES  17 C  308  MET ILE ARG TYR PHE GLY ASN MET TYR SER LYS ASN MET          
SEQRES  18 C  308  GLN ASP LEU ILE ASN PRO TYR PHE SER PRO LEU VAL ALA          
SEQRES  19 C  308  ASP ASP PHE SER ASN LEU PRO PRO ALA ILE MET VAL THR          
SEQRES  20 C  308  ASN GLU TYR ASP PRO LEU ARG ASP PRO GLU GLU THR TYR          
SEQRES  21 C  308  VAL LYS LYS LEU ARG GLU ALA GLY VAL ARG ALA VAL GLY          
SEQRES  22 C  308  ILE ARG GLY ILE GLY MET ILE HIS GLY SER ALA THR ASP          
SEQRES  23 C  308  PHE GLU VAL SER ASP GLY ALA ARG ASN ILE VAL LYS MET          
SEQRES  24 C  308  VAL ALA ARG ILE ILE PRO ASP TYR LEU                          
SEQRES   1 D  308  MET HIS LEU MET ASN MET VAL ASP PRO ASP PHE ASN SER          
SEQRES   2 D  308  LEU ILE GLU LEU SER LYS SER ALA GLY ASP MET THR LYS          
SEQRES   3 D  308  ILE GLU PRO ALA MET LEU ARG ASN PHE LEU ASP GLU SER          
SEQRES   4 D  308  SER LEU SER SER ARG GLY ALA PRO VAL GLU ILE LYS GLU          
SEQRES   5 D  308  ILE LYS ASP TYR LYS ILE LYS LEU ASP GLY ARG THR LEU          
SEQRES   6 D  308  ASN ALA ARG MET TYR ASP ASP ASN ASN ALA LYS SER ALA          
SEQRES   7 D  308  ILE LEU TYR TYR HIS GLY GLY GLY PHE LEU PHE GLY ASN          
SEQRES   8 D  308  ILE GLU THR TYR ASP ASN TYR CYS ARG PHE LEU ALA LYS          
SEQRES   9 D  308  GLU SER GLY VAL LYS ILE ILE SER ILE GLU TYR ARG LEU          
SEQRES  10 D  308  ALA PRO GLU HIS LYS PHE PRO ASP ALA PHE ASN ASP ALA          
SEQRES  11 D  308  TYR ASP SER PHE HIS TYR ILE ALA LYS LYS LYS LYS ASP          
SEQRES  12 D  308  PHE GLY ILE GLU GLY ARG ILE GLY VAL ALA GLY ASP SER          
SEQRES  13 D  308  ALA GLY ALA ASN LEU ALA ALA ALA LEU CYS LEU LYS CYS          
SEQRES  14 D  308  ARG ASP GLY LYS THR GLU MET PRO ALA VAL GLN VAL LEU          
SEQRES  15 D  308  PHE TYR PRO SER LEU ALA PRO ASP ASN PHE SER ARG SER          
SEQRES  16 D  308  PHE ILE GLU TYR SER ASP ASN TYR VAL LEU THR GLY LYS          
SEQRES  17 D  308  MET ILE ARG TYR PHE GLY ASN MET TYR SER LYS ASN MET          
SEQRES  18 D  308  GLN ASP LEU ILE ASN PRO TYR PHE SER PRO LEU VAL ALA          
SEQRES  19 D  308  ASP ASP PHE SER ASN LEU PRO PRO ALA ILE MET VAL THR          
SEQRES  20 D  308  ASN GLU TYR ASP PRO LEU ARG ASP PRO GLU GLU THR TYR          
SEQRES  21 D  308  VAL LYS LYS LEU ARG GLU ALA GLY VAL ARG ALA VAL GLY          
SEQRES  22 D  308  ILE ARG GLY ILE GLY MET ILE HIS GLY SER ALA THR ASP          
SEQRES  23 D  308  PHE GLU VAL SER ASP GLY ALA ARG ASN ILE VAL LYS MET          
SEQRES  24 D  308  VAL ALA ARG ILE ILE PRO ASP TYR LEU                          
FORMUL   5  HOH   *983(H2 O)                                                    
HELIX    1   1 ASP A    8  ASP A   10  5                                   3    
HELIX    2   2 PHE A   11  GLY A   22  1                                  12    
HELIX    3   3 GLU A   28  SER A   43  1                                  16    
HELIX    4   4 ASN A   91  GLY A  107  1                                  17    
HELIX    5   5 PRO A  124  LYS A  140  1                                  17    
HELIX    6   6 LYS A  141  GLY A  145  5                                   5    
HELIX    7   7 SER A  156  GLY A  172  1                                  17    
HELIX    8   8 SER A  193  TYR A  199  1                                   7    
HELIX    9   9 THR A  206  SER A  218  1                                  13    
HELIX   10  10 SER A  230  ALA A  234  5                                   5    
HELIX   11  11 LEU A  253  ALA A  267  1                                  15    
HELIX   12  12 SER A  283  PHE A  287  5                                   5    
HELIX   13  13 SER A  290  ILE A  304  1                                  15    
HELIX   14  14 PRO A  305  LEU A  308  5                                   4    
HELIX   15  15 ASP B    8  ASP B   10  5                                   3    
HELIX   16  16 PHE B   11  ALA B   21  1                                  11    
HELIX   17  17 GLU B   28  ARG B   44  1                                  17    
HELIX   18  18 TYR B   95  GLY B  107  1                                  13    
HELIX   19  19 PRO B  124  LYS B  140  1                                  17    
HELIX   20  20 LYS B  141  GLY B  145  5                                   5    
HELIX   21  21 SER B  156  LYS B  173  1                                  18    
HELIX   22  22 SER B  193  TYR B  199  1                                   7    
HELIX   23  23 THR B  206  SER B  218  1                                  13    
HELIX   24  24 SER B  230  ALA B  234  5                                   5    
HELIX   25  25 LEU B  253  ALA B  267  1                                  15    
HELIX   26  26 GLY B  282  PHE B  287  5                                   6    
HELIX   27  27 SER B  290  ILE B  304  1                                  15    
HELIX   28  28 PRO B  305  LEU B  308  5                                   4    
HELIX   29  29 ASP C    8  ASP C   10  5                                   3    
HELIX   30  30 PHE C   11  ALA C   21  1                                  11    
HELIX   31  31 ASP C   23  ILE C   27  5                                   5    
HELIX   32  32 GLU C   28  ARG C   44  1                                  17    
HELIX   33  33 ASN C   91  GLY C  107  1                                  17    
HELIX   34  34 PRO C  124  LYS C  140  1                                  17    
HELIX   35  35 LYS C  141  GLY C  145  5                                   5    
HELIX   36  36 SER C  156  LYS C  173  1                                  18    
HELIX   37  37 SER C  193  SER C  200  1                                   8    
HELIX   38  38 THR C  206  SER C  218  1                                  13    
HELIX   39  39 SER C  230  ALA C  234  5                                   5    
HELIX   40  40 LEU C  253  ALA C  267  1                                  15    
HELIX   41  41 SER C  283  PHE C  287  5                                   5    
HELIX   42  42 SER C  290  ILE C  304  1                                  15    
HELIX   43  43 PRO C  305  LEU C  308  5                                   4    
HELIX   44  44 ASP D    8  ASP D   10  5                                   3    
HELIX   45  45 PHE D   11  ALA D   21  1                                  11    
HELIX   46  46 GLU D   28  SER D   42  1                                  15    
HELIX   47  47 TYR D   95  GLY D  107  1                                  13    
HELIX   48  48 PRO D  124  LYS D  140  1                                  17    
HELIX   49  49 LYS D  141  GLY D  145  5                                   5    
HELIX   50  50 SER D  156  GLY D  172  1                                  17    
HELIX   51  51 SER D  193  TYR D  199  1                                   7    
HELIX   52  52 THR D  206  SER D  218  1                                  13    
HELIX   53  53 SER D  230  ALA D  234  5                                   5    
HELIX   54  54 LEU D  253  ALA D  267  1                                  15    
HELIX   55  55 SER D  290  ILE D  304  1                                  15    
HELIX   56  56 PRO D  305  LEU D  308  5                                   4    
SHEET    1   A16 GLU A  52  LEU A  60  0                                        
SHEET    2   A16 ARG A  63  ASP A  71 -1  O  MET A  69   N  LYS A  54           
SHEET    3   A16 LYS A 109  ILE A 113 -1  O  ILE A 110   N  TYR A  70           
SHEET    4   A16 ALA A  78  TYR A  82  1  N  ILE A  79   O  ILE A 111           
SHEET    5   A16 ILE A 150  ASP A 155  1  O  GLY A 151   N  LEU A  80           
SHEET    6   A16 GLN A 180  PHE A 183  1  O  PHE A 183   N  GLY A 154           
SHEET    7   A16 ALA A 243  TYR A 250  1  O  ILE A 244   N  LEU A 182           
SHEET    8   A16 ALA A 271  ILE A 280  1  O  GLY A 276   N  THR A 247           
SHEET    9   A16 ALA D 271  ILE D 280 -1  O  GLY D 273   N  ILE A 277           
SHEET   10   A16 ALA D 243  TYR D 250  1  N  TYR D 250   O  MET D 279           
SHEET   11   A16 GLN D 180  PHE D 183  1  N  LEU D 182   O  ILE D 244           
SHEET   12   A16 ILE D 150  ASP D 155  1  N  GLY D 154   O  PHE D 183           
SHEET   13   A16 ALA D  78  TYR D  82  1  N  TYR D  82   O  ALA D 153           
SHEET   14   A16 LYS D 109  ILE D 113  1  O  ILE D 111   N  ILE D  79           
SHEET   15   A16 ARG D  63  ASP D  71 -1  N  ARG D  68   O  SER D 112           
SHEET   16   A16 GLU D  52  LEU D  60 -1  N  LYS D  54   O  MET D  69           
SHEET    1   B16 GLU B  52  LEU B  60  0                                        
SHEET    2   B16 ARG B  63  ASP B  71 -1  O  MET B  69   N  LYS B  54           
SHEET    3   B16 LYS B 109  ILE B 113 -1  O  SER B 112   N  ARG B  68           
SHEET    4   B16 ALA B  78  TYR B  82  1  N  TYR B  81   O  ILE B 111           
SHEET    5   B16 ILE B 150  ASP B 155  1  O  GLY B 151   N  LEU B  80           
SHEET    6   B16 GLN B 180  PHE B 183  1  O  PHE B 183   N  GLY B 154           
SHEET    7   B16 ALA B 243  TYR B 250  1  O  ILE B 244   N  LEU B 182           
SHEET    8   B16 ALA B 271  ILE B 280  1  O  GLY B 276   N  THR B 247           
SHEET    9   B16 ALA C 271  ILE C 280 -1  O  GLY C 273   N  ILE B 277           
SHEET   10   B16 ALA C 243  TYR C 250  1  N  THR C 247   O  GLY C 276           
SHEET   11   B16 GLN C 180  PHE C 183  1  N  LEU C 182   O  ILE C 244           
SHEET   12   B16 ILE C 150  ASP C 155  1  N  GLY C 154   O  PHE C 183           
SHEET   13   B16 ALA C  78  TYR C  82  1  N  LEU C  80   O  GLY C 151           
SHEET   14   B16 LYS C 109  ILE C 113  1  O  ILE C 111   N  TYR C  81           
SHEET   15   B16 ARG C  63  ASP C  71 -1  N  ARG C  68   O  SER C 112           
SHEET   16   B16 GLU C  52  LEU C  60 -1  N  ILE C  58   O  LEU C  65           
CISPEP   1 ALA A  118    PRO A  119          0        -5.62                     
CISPEP   2 PHE A  123    PRO A  124          0         9.19                     
CISPEP   3 ALA B  118    PRO B  119          0         5.81                     
CISPEP   4 PHE B  123    PRO B  124          0        15.46                     
CISPEP   5 ALA C  118    PRO C  119          0         3.29                     
CISPEP   6 PHE C  123    PRO C  124          0         9.10                     
CISPEP   7 LYS C  219    ASN C  220          0       -18.17                     
CISPEP   8 ALA D  118    PRO D  119          0         3.01                     
CISPEP   9 PHE D  123    PRO D  124          0         2.69                     
CRYST1   62.804  137.360   76.878  90.00  91.47  90.00 P 1 21 1      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      0.015923  0.000000  0.000408        0.00000                         
SCALE2      0.000000  0.007280  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013012        0.00000                         
TER    2356      LEU A 308                                                      
TER    4720      LEU B 308                                                      
TER    7084      LEU C 308                                                      
TER    9448      LEU D 308                                                      
MASTER      502    0    0   56   32    0    0    610427    4    0   96          
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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