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LongText Report for: 3WZL-pdb

Name Class
3WZL-pdb
HEADER    HYDROLASE                               01-OCT-14   3WZL              
TITLE     ZEN LACTONASE                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ZEARALENONE HYDROLASE;                                     
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLONOSTACHYS ROSEA;                             
SOURCE   3 ORGANISM_TAXID: 29856;                                               
SOURCE   4 GENE: ZHD101;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-46 EK/LIC                             
KEYWDS    ALPHA/BETA-HYDROLASE, LACTONASE, ZEARALENONE, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.P.KO,C.H.HUANG,J.R.LIU,R.T.GUO                                      
REVDAT   1   26-NOV-14 3WZL    0                                                
JRNL        AUTH   W.PENG,T.P.KO,Y.YANG,Y.ZHENG,C.C.CHEN,Z.ZHU,C.H.HUANG,       
JRNL        AUTH 2 Y.F.ZENG,J.W.HUANG,A.H.-J.WAND,J.R.LIU,R.T.GUO               
JRNL        TITL   CRYSTAL STRUCTURE AND SUBSTRATE-BINDING MODE OF THE          
JRNL        TITL 2 MYCOESTROGEN-DETOXIFYING LACTONASE ZHD FROM CLONOSTACHYS     
JRNL        TITL 3 ROSEA                                                        
JRNL        REF    RSC ADV                       V.   4 62321 2014              
JRNL        REFN                   ESSN 2046-2069                               
JRNL        DOI    10.1039/C4RA12111B                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 31238                          
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) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1635                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3907                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2810                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 186                          
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6066                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 235                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 74.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.05000                                              
REMARK   3    B22 (A**2) : 4.05000                                              
REMARK   3    B33 (A**2) : -6.07000                                             
REMARK   3    B12 (A**2) : 2.02000                                              
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): 0.567         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.316         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.229         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.924        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6219 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8496 ; 1.677 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   789 ; 6.660 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   249 ;37.783 ;24.096       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   978 ;17.559 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;14.409 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   972 ; 0.110 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4719 ; 0.007 ; 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):  3957 ; 0.860 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6423 ; 1.640 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2262 ; 2.347 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2073 ; 3.904 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : C A B                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C      1       C     264      5                      
REMARK   3           1     A      1       A     264      5                      
REMARK   3           1     B      1       B     264      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1056 ; 0.390 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1056 ; 0.230 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1056 ; 0.240 ; 0.500           
REMARK   3   LOOSE POSITIONAL   1    C    (A):    966 ; 0.690 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    966 ; 0.460 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    B    (A):    966 ; 0.530 ; 5.000           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1056 ;32.400 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1056 ;16.790 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1056 ;16.360 ; 2.000           
REMARK   3   LOOSE THERMAL      1    C (A**2):    966 ;31.510 ;10.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):    966 ;16.340 ;10.000           
REMARK   3   LOOSE THERMAL      1    B (A**2):    966 ;16.050 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   264                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.7091  18.1579  11.3335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5409 T22:   0.2679                                     
REMARK   3      T33:   0.2894 T12:   0.0727                                     
REMARK   3      T13:   0.0336 T23:  -0.0223                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6505 L22:   0.1260                                     
REMARK   3      L33:   1.8377 L12:  -0.0109                                     
REMARK   3      L13:  -0.1785 L23:  -0.0097                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1611 S12:   0.1100 S13:  -0.0209                       
REMARK   3      S21:   0.1356 S22:   0.1847 S23:   0.0033                       
REMARK   3      S31:  -0.0553 S32:   0.0357 S33:  -0.0235                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   264                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.9615  26.1668 -27.5081              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4443 T22:   0.3221                                     
REMARK   3      T33:   0.3051 T12:  -0.2347                                     
REMARK   3      T13:   0.0458 T23:  -0.0201                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3172 L22:   0.3318                                     
REMARK   3      L33:   1.8870 L12:   0.2870                                     
REMARK   3      L13:  -0.4779 L23:  -0.1908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0191 S12:   0.0852 S13:  -0.0502                       
REMARK   3      S21:   0.0360 S22:   0.1162 S23:  -0.0384                       
REMARK   3      S31:  -0.1346 S32:  -0.0468 S33:  -0.1353                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   264                          
REMARK   3    ORIGIN FOR THE GROUP (A): -49.1470   3.5492 -19.8835              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1065 T22:   0.4426                                     
REMARK   3      T33:   1.2370 T12:  -0.1850                                     
REMARK   3      T13:  -0.2009 T23:   0.4156                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3652 L22:   1.1768                                     
REMARK   3      L33:   4.8260 L12:  -1.2193                                     
REMARK   3      L13:  -0.9869 L23:   0.4614                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0607 S12:   0.0251 S13:  -0.4938                       
REMARK   3      S21:  -0.1371 S22:   0.1288 S23:   0.4718                       
REMARK   3      S31:   0.1113 S32:  -0.9287 S33:  -0.1895                       
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 3WZL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-OCT-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB096991.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSRRC                              
REMARK 200  BEAMLINE                       : BL13B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33747                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 9.100                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 37.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 2000 MME, 0.1M BIS-TRIS PH       
REMARK 280  6.5, VAPOR DIFFUSION, SITTING DROP                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      158.00533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      316.01067            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      237.00800            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      395.01333            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       79.00267            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      158.00533            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      316.01067            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      395.01333            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      237.00800            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       79.00267            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 1240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20480 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 1240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 387  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 316  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 309  LIES ON A SPECIAL POSITION.                          
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   -13                                                      
REMARK 465     ALA A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     LYS A     0                                                      
REMARK 465     MET B   -13                                                      
REMARK 465     ALA B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     ASP B    -4                                                      
REMARK 465     ASP B    -3                                                      
REMARK 465     ASP B    -2                                                      
REMARK 465     ASP B    -1                                                      
REMARK 465     LYS B     0                                                      
REMARK 465     MET C   -13                                                      
REMARK 465     ALA C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     HIS C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     ASP C    -4                                                      
REMARK 465     ASP C    -3                                                      
REMARK 465     ASP C    -2                                                      
REMARK 465     ASP C    -1                                                      
REMARK 465     LYS C     0                                                      
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   N    MET A     1     O    HOH A   333              2.13            
REMARK 500   O    HOH B   354     O    HOH B   368              2.18            
REMARK 500   OD2  ASP A    25     O    HOH A   343              2.18            
REMARK 500   O    HOH B   348     O    HOH B   399              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    CYS B 124   CB    CYS B 124   SG     -0.099                       
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    ARG A   2   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    PRO C  24   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  48       14.22    -62.36                                   
REMARK 500    PHE A  56      142.41   -171.50                                   
REMARK 500    SER A  62     -132.42     36.71                                   
REMARK 500    GLU A  74       52.63     36.01                                   
REMARK 500    SER A 102     -138.11     63.09                                   
REMARK 500    ALA A 167        0.28    -69.95                                   
REMARK 500    PRO A 196       34.36    -79.55                                   
REMARK 500    MET A 241     -118.00   -143.73                                   
REMARK 500    ASP B  31     -169.84    -76.06                                   
REMARK 500    SER B  62     -124.12     39.78                                   
REMARK 500    SER B 102     -120.50     61.12                                   
REMARK 500    MET B 241     -112.73   -132.83                                   
REMARK 500    ARG C   4       77.23   -112.43                                   
REMARK 500    ASP C  31     -158.73    -72.86                                   
REMARK 500    LEU C  33       -6.10    -54.33                                   
REMARK 500    ALA C  48        3.24    -67.76                                   
REMARK 500    SER C  62     -116.92     43.29                                   
REMARK 500    TYR C  72       10.17   -150.39                                   
REMARK 500    ALA C  81      -35.67    -38.90                                   
REMARK 500    ASP C  92       46.08     39.17                                   
REMARK 500    SER C 102     -103.30     35.65                                   
REMARK 500    GLU C 126       65.62     71.81                                   
REMARK 500    LEU C 131       92.87    -68.97                                   
REMARK 500    ASN C 137       36.37    -67.51                                   
REMARK 500    THR C 138      -45.38   -130.69                                   
REMARK 500    SER C 147       35.83    -83.13                                   
REMARK 500    LYS C 148      -36.87   -145.65                                   
REMARK 500    SER C 159      -91.94    -78.68                                   
REMARK 500    PRO C 196       19.35    -63.37                                   
REMARK 500    VAL C 197       57.51   -117.02                                   
REMARK 500    ARG C 204      107.53    -59.59                                   
REMARK 500    PRO C 207       84.68    -63.75                                   
REMARK 500    ALA C 214      -73.47    -18.33                                   
REMARK 500    PHE C 221       44.47   -141.08                                   
REMARK 500    THR C 227      -40.93   -136.38                                   
REMARK 500    ALA C 228      -72.05    -46.15                                   
REMARK 500    MET C 241     -105.51   -123.83                                   
REMARK 500    VAL C 246      -42.93   -136.88                                   
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 316        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH A 328        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH A 371        DISTANCE =  6.60 ANGSTROMS                       
REMARK 525    HOH A 372        DISTANCE =  7.87 ANGSTROMS                       
REMARK 525    HOH A 378        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH A 381        DISTANCE =  5.66 ANGSTROMS                       
REMARK 525    HOH A 382        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH A 383        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH A 388        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH A 399        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH A 403        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH B 339        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH B 362        DISTANCE =  5.74 ANGSTROMS                       
REMARK 525    HOH B 376        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH B 377        DISTANCE =  7.94 ANGSTROMS                       
REMARK 525    HOH B 379        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH B 389        DISTANCE =  7.58 ANGSTROMS                       
REMARK 525    HOH B 396        DISTANCE =  7.69 ANGSTROMS                       
REMARK 525    HOH C 303        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH C 316        DISTANCE =  8.74 ANGSTROMS                       
REMARK 525    HOH C 317        DISTANCE =  8.86 ANGSTROMS                       
REMARK 525    HOH C 319        DISTANCE =  7.72 ANGSTROMS                       
REMARK 525    HOH C 320        DISTANCE =  6.51 ANGSTROMS                       
REMARK 525    HOH C 321        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH C 325        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH C 326        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH C 327        DISTANCE =  6.79 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3WZM   RELATED DB: PDB                                   
DBREF  3WZL A    1   264  UNP    Q8NKB0   Q8NKB0_BIOOC     1    264             
DBREF  3WZL B    1   264  UNP    Q8NKB0   Q8NKB0_BIOOC     1    264             
DBREF  3WZL C    1   264  UNP    Q8NKB0   Q8NKB0_BIOOC     1    264             
SEQADV 3WZL MET A  -13  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ALA A  -12  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS A  -11  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS A  -10  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS A   -9  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS A   -8  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS A   -7  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS A   -6  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL VAL A   -5  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ASP A   -4  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ASP A   -3  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ASP A   -2  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ASP A   -1  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL LYS A    0  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL MET B  -13  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ALA B  -12  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS B  -11  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS B  -10  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS B   -9  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS B   -8  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS B   -7  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS B   -6  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL VAL B   -5  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ASP B   -4  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ASP B   -3  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ASP B   -2  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ASP B   -1  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL LYS B    0  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL MET C  -13  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ALA C  -12  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS C  -11  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS C  -10  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS C   -9  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS C   -8  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS C   -7  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL HIS C   -6  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL VAL C   -5  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ASP C   -4  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ASP C   -3  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ASP C   -2  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL ASP C   -1  UNP  Q8NKB0              EXPRESSION TAG                 
SEQADV 3WZL LYS C    0  UNP  Q8NKB0              EXPRESSION TAG                 
SEQRES   1 A  278  MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP          
SEQRES   2 A  278  LYS MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY          
SEQRES   3 A  278  ILE THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP          
SEQRES   4 A  278  VAL VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET          
SEQRES   5 A  278  PHE ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE          
SEQRES   6 A  278  ARG VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER          
SEQRES   7 A  278  ALA LYS ALA PRO PRO GLU THR TYR THR GLU VAL THR ALA          
SEQRES   8 A  278  GLN LYS LEU ALA SER TYR VAL ILE SER VAL LEU ASP ALA          
SEQRES   9 A  278  LEU ASP ILE LYS HIS ALA THR VAL TRP GLY CYS SER SER          
SEQRES  10 A  278  GLY ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO          
SEQRES  11 A  278  ASP ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR          
SEQRES  12 A  278  LYS LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU          
SEQRES  13 A  278  ASP GLU GLU ILE SER LYS ILE LEU ALA ASN VAL MET LEU          
SEQRES  14 A  278  ASN ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA MET          
SEQRES  15 A  278  GLY ASP GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO          
SEQRES  16 A  278  VAL TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER          
SEQRES  17 A  278  ALA PRO VAL LYS ASP LEU GLU ALA LEU ARG GLY LYS PRO          
SEQRES  18 A  278  LEU ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER          
SEQRES  19 A  278  PHE PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL          
SEQRES  20 A  278  ASN ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL          
SEQRES  21 A  278  SER HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR          
SEQRES  22 A  278  THR GLN LYS HIS LEU                                          
SEQRES   1 B  278  MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP          
SEQRES   2 B  278  LYS MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY          
SEQRES   3 B  278  ILE THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP          
SEQRES   4 B  278  VAL VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET          
SEQRES   5 B  278  PHE ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE          
SEQRES   6 B  278  ARG VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER          
SEQRES   7 B  278  ALA LYS ALA PRO PRO GLU THR TYR THR GLU VAL THR ALA          
SEQRES   8 B  278  GLN LYS LEU ALA SER TYR VAL ILE SER VAL LEU ASP ALA          
SEQRES   9 B  278  LEU ASP ILE LYS HIS ALA THR VAL TRP GLY CYS SER SER          
SEQRES  10 B  278  GLY ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO          
SEQRES  11 B  278  ASP ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR          
SEQRES  12 B  278  LYS LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU          
SEQRES  13 B  278  ASP GLU GLU ILE SER LYS ILE LEU ALA ASN VAL MET LEU          
SEQRES  14 B  278  ASN ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA MET          
SEQRES  15 B  278  GLY ASP GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO          
SEQRES  16 B  278  VAL TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER          
SEQRES  17 B  278  ALA PRO VAL LYS ASP LEU GLU ALA LEU ARG GLY LYS PRO          
SEQRES  18 B  278  LEU ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER          
SEQRES  19 B  278  PHE PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL          
SEQRES  20 B  278  ASN ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL          
SEQRES  21 B  278  SER HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR          
SEQRES  22 B  278  THR GLN LYS HIS LEU                                          
SEQRES   1 C  278  MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP          
SEQRES   2 C  278  LYS MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY          
SEQRES   3 C  278  ILE THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP          
SEQRES   4 C  278  VAL VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET          
SEQRES   5 C  278  PHE ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE          
SEQRES   6 C  278  ARG VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER          
SEQRES   7 C  278  ALA LYS ALA PRO PRO GLU THR TYR THR GLU VAL THR ALA          
SEQRES   8 C  278  GLN LYS LEU ALA SER TYR VAL ILE SER VAL LEU ASP ALA          
SEQRES   9 C  278  LEU ASP ILE LYS HIS ALA THR VAL TRP GLY CYS SER SER          
SEQRES  10 C  278  GLY ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO          
SEQRES  11 C  278  ASP ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR          
SEQRES  12 C  278  LYS LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU          
SEQRES  13 C  278  ASP GLU GLU ILE SER LYS ILE LEU ALA ASN VAL MET LEU          
SEQRES  14 C  278  ASN ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA MET          
SEQRES  15 C  278  GLY ASP GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO          
SEQRES  16 C  278  VAL TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER          
SEQRES  17 C  278  ALA PRO VAL LYS ASP LEU GLU ALA LEU ARG GLY LYS PRO          
SEQRES  18 C  278  LEU ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER          
SEQRES  19 C  278  PHE PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL          
SEQRES  20 C  278  ASN ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL          
SEQRES  21 C  278  SER HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR          
SEQRES  22 C  278  THR GLN LYS HIS LEU                                          
FORMUL   4  HOH   *235(H2 O)                                                    
HELIX    1   1 GLU A   35  MET A   38  5                                   4    
HELIX    2   2 PHE A   39  ALA A   48  1                                  10    
HELIX    3   3 MET A   61  ALA A   65  5                                   5    
HELIX    4   4 PRO A   68  TYR A   72  5                                   5    
HELIX    5   5 THR A   76  LEU A   91  1                                  16    
HELIX    6   6 SER A  102  TYR A  115  1                                  14    
HELIX    7   7 LEU A  132  ASN A  137  1                                   6    
HELIX    8   8 THR A  138  LEU A  141  5                                   4    
HELIX    9   9 GLU A  142  ASP A  157  1                                  16    
HELIX   10  10 GLY A  161  ALA A  167  1                                   7    
HELIX   11  11 GLY A  169  TYR A  187  1                                  19    
HELIX   12  12 ILE A  191  ALA A  195  5                                   5    
HELIX   13  13 ASP A  199  ARG A  204  1                                   6    
HELIX   14  14 PRO A  217  GLY A  232  1                                  16    
HELIX   15  15 PHE A  243  HIS A  248  1                                   6    
HELIX   16  16 HIS A  248  HIS A  263  1                                  16    
HELIX   17  17 GLU B   35  MET B   38  5                                   4    
HELIX   18  18 PHE B   39  GLN B   49  1                                  11    
HELIX   19  19 MET B   61  ALA B   65  5                                   5    
HELIX   20  20 PRO B   68  TYR B   72  5                                   5    
HELIX   21  21 THR B   76  LEU B   91  1                                  16    
HELIX   22  22 SER B  102  TYR B  115  1                                  14    
HELIX   23  23 LEU B  132  ASN B  137  1                                   6    
HELIX   24  24 THR B  138  LEU B  141  5                                   4    
HELIX   25  25 GLU B  142  VAL B  158  1                                  17    
HELIX   26  26 GLY B  161  ALA B  167  1                                   7    
HELIX   27  27 GLY B  169  TYR B  187  1                                  19    
HELIX   28  28 ILE B  191  ALA B  195  5                                   5    
HELIX   29  29 ASP B  199  ARG B  204  1                                   6    
HELIX   30  30 PRO B  217  ALA B  231  1                                  15    
HELIX   31  31 PHE B  243  HIS B  248  1                                   6    
HELIX   32  32 HIS B  248  LEU B  264  1                                  17    
HELIX   33  33 PHE C   39  ALA C   48  1                                  10    
HELIX   34  34 PRO C   68  TYR C   72  5                                   5    
HELIX   35  35 THR C   76  ALA C   90  1                                  15    
HELIX   36  36 SER C  102  TYR C  115  1                                  14    
HELIX   37  37 LEU C  132  ASN C  137  1                                   6    
HELIX   38  38 GLU C  145  ASP C  157  1                                  13    
HELIX   39  39 TRP C  165  MET C  168  5                                   4    
HELIX   40  40 GLY C  169  TYR C  187  1                                  19    
HELIX   41  41 ASP C  199  ARG C  204  1                                   6    
HELIX   42  42 PRO C  217  PHE C  222  1                                   6    
HELIX   43  43 ASN C  224  THR C  229  1                                   6    
HELIX   44  44 LYS C  230  GLY C  232  5                                   3    
HELIX   45  45 PHE C  243  HIS C  248  1                                   6    
HELIX   46  46 PRO C  249  LYS C  262  1                                  14    
SHEET    1   A 8 THR A   3  SER A   8  0                                        
SHEET    2   A 8 THR A  14  GLU A  20 -1  O  TYR A  17   N  SER A   5           
SHEET    3   A 8 ARG A  52  PHE A  56 -1  O  VAL A  53   N  GLU A  20           
SHEET    4   A 8 ASP A  25  VAL A  29  1  N  VAL A  26   O  ARG A  52           
SHEET    5   A 8 ALA A  96  CYS A 101  1  O  THR A  97   N  VAL A  27           
SHEET    6   A 8 ILE A 119  HIS A 125  1  O  MET A 123   N  VAL A  98           
SHEET    7   A 8 LEU A 208  GLY A 213  1  O  ASP A 209   N  CYS A 124           
SHEET    8   A 8 ASN A 234  LEU A 238  1  O  ASN A 234   N  TRP A 210           
SHEET    1   B 8 ARG B   2  SER B   8  0                                        
SHEET    2   B 8 THR B  14  GLU B  20 -1  O  GLN B  19   N  THR B   3           
SHEET    3   B 8 ARG B  52  PHE B  56 -1  O  VAL B  53   N  GLU B  20           
SHEET    4   B 8 ASP B  25  VAL B  29  1  N  VAL B  26   O  THR B  54           
SHEET    5   B 8 ALA B  96  CYS B 101  1  O  THR B  97   N  VAL B  27           
SHEET    6   B 8 ILE B 119  HIS B 125  1  O  MET B 123   N  VAL B  98           
SHEET    7   B 8 LEU B 208  GLY B 213  1  O  ASP B 209   N  ALA B 122           
SHEET    8   B 8 ASN B 234  LEU B 238  1  O  ASN B 234   N  TRP B 210           
SHEET    1   C 5 TYR C  17  GLU C  20  0                                        
SHEET    2   C 5 ARG C  52  PHE C  56 -1  O  THR C  55   N  GLU C  18           
SHEET    3   C 5 ASP C  25  VAL C  29  1  N  VAL C  26   O  THR C  54           
SHEET    4   C 5 ALA C  96  CYS C 101  1  O  TRP C  99   N  VAL C  29           
SHEET    5   C 5 CYS C 124  HIS C 125  1  O  HIS C 125   N  GLY C 100           
SHEET    1   D 2 ASP C 209  VAL C 212  0                                        
SHEET    2   D 2 ASN C 234  LEU C 237  1  O  ASN C 234   N  TRP C 210           
CRYST1   86.637   86.637  474.016  90.00  90.00 120.00 P 61 2 2     36          
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      0.011542  0.006664  0.000000        0.00000                         
SCALE2      0.000000  0.013328  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002110        0.00000                         
TER    2023      LEU A 264                                                      
TER    4046      LEU B 264                                                      
TER    6069      LEU C 264                                                      
MASTER      568    0    0   46   23    0    0    6 6301    3    0   66          
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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