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LongText Report for: 5ikx-pdb

Name Class
5ikx-pdb
HEADER    HYDROLASE                               04-MAR-16   5IKX              
TITLE     CRYSTAL STRUCTURE OF THE ALPHA-ESTERASE-7 CARBOXYL ESTERASE (DIMER),  
TITLE    2 E3, FROM LUCILIA CUPRINA                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.-;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LUCILIA CUPRINA;                                
SOURCE   3 ORGANISM_COMMON: GREEN BOTTLE FLY;                                   
SOURCE   4 ORGANISM_TAXID: 7375;                                                
SOURCE   5 GENE: LCAE7;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ORGANOPHOSPHATE, CARBOXYLESTERASE, OLIGERMERIZATION, HYDROLASE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.JACKSON,N.FRASER                                                    
REVDAT   1   22-JUN-16 5IKX    0                                                
SPRSDE     22-JUN-16 5IKX      4FG5                                             
JRNL        AUTH   N.J.FRASER,J.W.LIU,P.D.MABBITT,G.J.CORREY,C.W.COPPIN,        
JRNL        AUTH 2 M.LETHIER,M.A.PERUGINI,J.M.MURPHY,J.G.OAKESHOTT,M.WEIK,      
JRNL        AUTH 3 C.J.JACKSON                                                  
JRNL        TITL   EVOLUTION OF PROTEIN QUATERNARY STRUCTURE IN RESPONSE TO     
JRNL        TITL 2 SELECTIVE PRESSURE FOR INCREASED THERMOSTABILITY.            
JRNL        REF    J.MOL.BIOL.                   V. 428  2359 2016              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   27016206                                                     
JRNL        DOI    10.1016/J.JMB.2016.03.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.06                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 58544                          
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) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3276                            
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) : 2.19                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3419                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2370                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 172                          
REMARK   3   BIN FREE R VALUE                    : 0.2830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9140                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 376                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.72000                                             
REMARK   3    B22 (A**2) : 14.12000                                             
REMARK   3    B33 (A**2) : -25.84000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -15.41000                                            
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.055         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.040         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.142         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.304        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9372 ; 0.007 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12685 ; 1.155 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1136 ; 5.887 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   444 ;37.563 ;24.324       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1634 ;17.695 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    49 ;15.816 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1353 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7153 ; 0.005 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  : 6                                          
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     2        A    66                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.8150  -4.7350  -5.6640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1335 T22:   0.1499                                     
REMARK   3      T33:   0.2252 T12:   0.0533                                     
REMARK   3      T13:   0.1183 T23:  -0.0302                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2579 L22:   0.1936                                     
REMARK   3      L33:   1.2130 L12:  -0.1835                                     
REMARK   3      L13:  -0.2810 L23:   0.3400                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0256 S12:   0.0639 S13:   0.0284                       
REMARK   3      S21:   0.0397 S22:  -0.0666 S23:   0.0204                       
REMARK   3      S31:   0.2067 S32:   0.0574 S33:   0.0410                       
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 :   A    67        A   347                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0060   2.9250  11.0190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1211 T22:   0.1521                                     
REMARK   3      T33:   0.2303 T12:   0.0198                                     
REMARK   3      T13:   0.0958 T23:   0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3809 L22:   0.2588                                     
REMARK   3      L33:   0.4881 L12:   0.1415                                     
REMARK   3      L13:  -0.2266 L23:   0.1802                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0472 S12:   0.0114 S13:  -0.0216                       
REMARK   3      S21:   0.0229 S22:   0.0483 S23:   0.0104                       
REMARK   3      S31:   0.0482 S32:   0.0223 S33:  -0.0010                       
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 :   A   348        A   570                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.9000  22.8480  -0.5770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1725 T22:   0.1025                                     
REMARK   3      T33:   0.1909 T12:   0.0302                                     
REMARK   3      T13:   0.1150 T23:   0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8219 L22:   0.2843                                     
REMARK   3      L33:   0.8247 L12:  -0.1377                                     
REMARK   3      L13:  -0.5586 L23:   0.4247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1167 S12:   0.1049 S13:   0.0369                       
REMARK   3      S21:  -0.0914 S22:  -0.0557 S23:  -0.0182                       
REMARK   3      S31:  -0.2097 S32:  -0.0875 S33:  -0.0610                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B    66                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.0400   3.5520 -51.9860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1974 T22:   0.1561                                     
REMARK   3      T33:   0.2070 T12:   0.0611                                     
REMARK   3      T13:   0.0738 T23:   0.0293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1943 L22:   0.9427                                     
REMARK   3      L33:   0.9989 L12:  -0.3038                                     
REMARK   3      L13:  -0.3944 L23:   0.7009                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0560 S12:  -0.0298 S13:   0.0077                       
REMARK   3      S21:  -0.0718 S22:   0.0382 S23:   0.0008                       
REMARK   3      S31:  -0.0618 S32:   0.0217 S33:   0.0179                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    67        B   347                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.4350  -3.9740 -34.9470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0843 T22:   0.1580                                     
REMARK   3      T33:   0.2303 T12:  -0.0093                                     
REMARK   3      T13:   0.1141 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3550 L22:   0.0373                                     
REMARK   3      L33:   0.7911 L12:  -0.0542                                     
REMARK   3      L13:   0.0859 L23:   0.0030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0659 S12:   0.0231 S13:  -0.0125                       
REMARK   3      S21:  -0.0071 S22:   0.0523 S23:  -0.0018                       
REMARK   3      S31:  -0.0277 S32:   0.0554 S33:   0.0136                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   348        B   570                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.3290 -24.1270 -46.1850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2388 T22:   0.1173                                     
REMARK   3      T33:   0.1952 T12:   0.0300                                     
REMARK   3      T13:   0.0926 T23:  -0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3100 L22:   0.3414                                     
REMARK   3      L33:   0.8386 L12:  -0.2460                                     
REMARK   3      L13:   0.1467 L23:  -0.0331                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0249 S12:   0.0239 S13:  -0.0021                       
REMARK   3      S21:  -0.0747 S22:   0.0232 S23:   0.0150                       
REMARK   3      S31:   0.2323 S32:   0.1215 S33:   0.0017                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3   THE INPUT                                                          
REMARK   4                                                                      
REMARK   4 5IKX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218989.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.82655                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62125                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43900                            
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: 4FNG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 20% PEG 2K MME, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 292K                           
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       54.47800            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     MET B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 306    CG   CD   CE   NZ                                   
REMARK 470     VAL A 366    CG1  CG2                                            
REMARK 470     LYS B  46    CG   CD   CE   NZ                                   
REMARK 470     MET B 308    CB   CG   SD   CE                                   
REMARK 470     ARG B 385    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 405    CG   CD   OE1  OE2                                  
REMARK 470     THR B 436    OG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    TRP B   337     OG   SER B   340              2.18            
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    LEU B 114   CA  -  CB  -  CG  ANGL. DEV. =  13.9 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    ILE A 101      -55.69   -121.59                                   
REMARK 500    ASN A 120      116.26   -162.63                                   
REMARK 500    GLU A 142     -175.38   -171.24                                   
REMARK 500    ILE A 154        1.09    -69.71                                   
REMARK 500    SER A 218     -110.68     66.59                                   
REMARK 500    LYS A 270      -78.43    139.60                                   
REMARK 500    ASP A 273       85.94    -66.97                                   
REMARK 500    ASN A 305        7.51    -69.44                                   
REMARK 500    TYR A 350       62.04   -154.48                                   
REMARK 500    PRO A 377      125.72    -37.69                                   
REMARK 500    PHE A 421      -62.44   -125.64                                   
REMARK 500    SER A 437       41.42   -107.86                                   
REMARK 500    ASP A 447       30.70   -142.21                                   
REMARK 500    THR A 472      -22.64    109.00                                   
REMARK 500    SER A 542     -134.60   -129.20                                   
REMARK 500    SER B 218     -120.16     57.65                                   
REMARK 500    LYS B 270       50.31     91.92                                   
REMARK 500    CYS B 372       39.87    -95.47                                   
REMARK 500    PHE B 421      -67.98   -134.79                                   
REMARK 500    HIS B 435       -0.35   -147.03                                   
REMARK 500    PRO B 440      155.60    -48.09                                   
REMARK 500    THR B 472      -24.68     99.52                                   
REMARK 500    ASN B 523       20.93     81.14                                   
REMARK 500    SER B 542     -145.45   -117.35                                   
REMARK 500    HIS B 566       58.03   -119.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5IKX A    1   570  UNP    Q25252   Q25252_LUCCU     1    570             
DBREF  5IKX B    1   570  UNP    Q25252   Q25252_LUCCU     1    570             
SEQADV 5IKX MET A   -6  UNP  Q25252              INITIATING METHIONINE          
SEQADV 5IKX HIS A   -5  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5IKX HIS A   -4  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5IKX HIS A   -3  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5IKX HIS A   -2  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5IKX HIS A   -1  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5IKX HIS A    0  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5IKX ALA A   83  UNP  Q25252    ASP    83 CONFLICT                       
SEQADV 5IKX LEU A  364  UNP  Q25252    MET   364 CONFLICT                       
SEQADV 5IKX PHE A  419  UNP  Q25252    ILE   419 CONFLICT                       
SEQADV 5IKX THR A  472  UNP  Q25252    ALA   472 CONFLICT                       
SEQADV 5IKX THR A  505  UNP  Q25252    ILE   505 CONFLICT                       
SEQADV 5IKX GLU A  530  UNP  Q25252    LYS   530 CONFLICT                       
SEQADV 5IKX GLY A  554  UNP  Q25252    ASP   554 CONFLICT                       
SEQADV 5IKX MET B   -6  UNP  Q25252              INITIATING METHIONINE          
SEQADV 5IKX HIS B   -5  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5IKX HIS B   -4  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5IKX HIS B   -3  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5IKX HIS B   -2  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5IKX HIS B   -1  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5IKX HIS B    0  UNP  Q25252              EXPRESSION TAG                 
SEQADV 5IKX ALA B   83  UNP  Q25252    ASP    83 CONFLICT                       
SEQADV 5IKX LEU B  364  UNP  Q25252    MET   364 CONFLICT                       
SEQADV 5IKX PHE B  419  UNP  Q25252    ILE   419 CONFLICT                       
SEQADV 5IKX THR B  472  UNP  Q25252    ALA   472 CONFLICT                       
SEQADV 5IKX THR B  505  UNP  Q25252    ILE   505 CONFLICT                       
SEQADV 5IKX GLU B  530  UNP  Q25252    LYS   530 CONFLICT                       
SEQADV 5IKX GLY B  554  UNP  Q25252    ASP   554 CONFLICT                       
SEQRES   1 A  577  MET HIS HIS HIS HIS HIS HIS MET ASN PHE ASN VAL SER          
SEQRES   2 A  577  LEU MET GLU LYS LEU LYS TRP LYS ILE LYS CYS ILE GLU          
SEQRES   3 A  577  ASN LYS PHE LEU ASN TYR ARG LEU THR THR ASN GLU THR          
SEQRES   4 A  577  VAL VAL ALA GLU THR GLU TYR GLY LYS VAL LYS GLY VAL          
SEQRES   5 A  577  LYS ARG LEU THR VAL TYR ASP ASP SER TYR TYR SER PHE          
SEQRES   6 A  577  GLU GLY ILE PRO TYR ALA GLN PRO PRO VAL GLY GLU LEU          
SEQRES   7 A  577  ARG PHE LYS ALA PRO GLN ARG PRO THR PRO TRP ALA GLY          
SEQRES   8 A  577  VAL ARG ASP CYS CYS ASN HIS LYS ASP LYS SER VAL GLN          
SEQRES   9 A  577  VAL ASP PHE ILE THR GLY LYS VAL CYS GLY SER GLU ASP          
SEQRES  10 A  577  CYS LEU TYR LEU SER VAL TYR THR ASN ASN LEU ASN PRO          
SEQRES  11 A  577  GLU THR LYS ARG PRO VAL LEU VAL TYR ILE HIS GLY GLY          
SEQRES  12 A  577  GLY PHE ILE ILE GLY GLU ASN HIS ARG ASP MET TYR GLY          
SEQRES  13 A  577  PRO ASP TYR PHE ILE LYS LYS ASP VAL VAL LEU ILE ASN          
SEQRES  14 A  577  ILE GLN TYR ARG LEU GLY ALA LEU GLY PHE LEU SER LEU          
SEQRES  15 A  577  ASN SER GLU ASP LEU ASN VAL PRO GLY ASN ALA GLY LEU          
SEQRES  16 A  577  LYS ASP GLN VAL MET ALA LEU ARG TRP ILE LYS ASN ASN          
SEQRES  17 A  577  CYS ALA ASN PHE GLY GLY ASN PRO ASP ASN ILE THR VAL          
SEQRES  18 A  577  PHE GLY GLU SER ALA GLY ALA ALA SER THR HIS TYR MET          
SEQRES  19 A  577  MET LEU THR GLU GLN THR ARG GLY LEU PHE HIS ARG GLY          
SEQRES  20 A  577  ILE LEU MET SER GLY ASN ALA ILE CYS PRO TRP ALA ASN          
SEQRES  21 A  577  THR GLN CYS GLN HIS ARG ALA PHE THR LEU ALA LYS LEU          
SEQRES  22 A  577  ALA GLY TYR LYS GLY GLU ASP ASN ASP LYS ASP VAL LEU          
SEQRES  23 A  577  GLU PHE LEU MET LYS ALA LYS PRO GLN ASP LEU ILE LYS          
SEQRES  24 A  577  LEU GLU GLU LYS VAL LEU THR LEU GLU GLU ARG THR ASN          
SEQRES  25 A  577  LYS VAL MET PHE PRO PHE GLY PRO THR VAL GLU PRO TYR          
SEQRES  26 A  577  GLN THR ALA ASP CYS VAL LEU PRO LYS HIS PRO ARG GLU          
SEQRES  27 A  577  MET VAL LYS THR ALA TRP GLY ASN SER ILE PRO THR MET          
SEQRES  28 A  577  MET GLY ASN THR SER TYR GLU GLY LEU PHE PHE THR SER          
SEQRES  29 A  577  ILE LEU LYS GLN MET PRO LEU LEU VAL LYS GLU LEU GLU          
SEQRES  30 A  577  THR CYS VAL ASN PHE VAL PRO SER GLU LEU ALA ASP ALA          
SEQRES  31 A  577  GLU ARG THR ALA PRO GLU THR LEU GLU MET GLY ALA LYS          
SEQRES  32 A  577  ILE LYS LYS ALA HIS VAL THR GLY GLU THR PRO THR ALA          
SEQRES  33 A  577  ASP ASN PHE MET ASP LEU CYS SER HIS PHE TYR PHE TRP          
SEQRES  34 A  577  PHE PRO MET HIS ARG LEU LEU GLN LEU ARG PHE ASN HIS          
SEQRES  35 A  577  THR SER GLY THR PRO VAL TYR LEU TYR ARG PHE ASP PHE          
SEQRES  36 A  577  ASP SER GLU ASP LEU ILE ASN PRO TYR ARG ILE MET ARG          
SEQRES  37 A  577  SER GLY ARG GLY VAL LYS GLY VAL SER HIS THR ASP GLU          
SEQRES  38 A  577  LEU THR TYR PHE PHE TRP ASN GLN LEU ALA LYS ARG MET          
SEQRES  39 A  577  PRO LYS GLU SER ARG GLU TYR LYS THR ILE GLU ARG MET          
SEQRES  40 A  577  THR GLY ILE TRP THR GLN PHE ALA THR THR GLY ASN PRO          
SEQRES  41 A  577  TYR SER ASN GLU ILE GLU GLY MET GLU ASN VAL SER TRP          
SEQRES  42 A  577  ASP PRO ILE GLU LYS SER ASP GLU VAL TYR LYS CYS LEU          
SEQRES  43 A  577  ASN ILE SER ASP GLU LEU LYS MET ILE ASP VAL PRO GLU          
SEQRES  44 A  577  MET GLY LYS ILE LYS GLN TRP GLU SER MET PHE GLU LYS          
SEQRES  45 A  577  HIS ARG ASP LEU PHE                                          
SEQRES   1 B  577  MET HIS HIS HIS HIS HIS HIS MET ASN PHE ASN VAL SER          
SEQRES   2 B  577  LEU MET GLU LYS LEU LYS TRP LYS ILE LYS CYS ILE GLU          
SEQRES   3 B  577  ASN LYS PHE LEU ASN TYR ARG LEU THR THR ASN GLU THR          
SEQRES   4 B  577  VAL VAL ALA GLU THR GLU TYR GLY LYS VAL LYS GLY VAL          
SEQRES   5 B  577  LYS ARG LEU THR VAL TYR ASP ASP SER TYR TYR SER PHE          
SEQRES   6 B  577  GLU GLY ILE PRO TYR ALA GLN PRO PRO VAL GLY GLU LEU          
SEQRES   7 B  577  ARG PHE LYS ALA PRO GLN ARG PRO THR PRO TRP ALA GLY          
SEQRES   8 B  577  VAL ARG ASP CYS CYS ASN HIS LYS ASP LYS SER VAL GLN          
SEQRES   9 B  577  VAL ASP PHE ILE THR GLY LYS VAL CYS GLY SER GLU ASP          
SEQRES  10 B  577  CYS LEU TYR LEU SER VAL TYR THR ASN ASN LEU ASN PRO          
SEQRES  11 B  577  GLU THR LYS ARG PRO VAL LEU VAL TYR ILE HIS GLY GLY          
SEQRES  12 B  577  GLY PHE ILE ILE GLY GLU ASN HIS ARG ASP MET TYR GLY          
SEQRES  13 B  577  PRO ASP TYR PHE ILE LYS LYS ASP VAL VAL LEU ILE ASN          
SEQRES  14 B  577  ILE GLN TYR ARG LEU GLY ALA LEU GLY PHE LEU SER LEU          
SEQRES  15 B  577  ASN SER GLU ASP LEU ASN VAL PRO GLY ASN ALA GLY LEU          
SEQRES  16 B  577  LYS ASP GLN VAL MET ALA LEU ARG TRP ILE LYS ASN ASN          
SEQRES  17 B  577  CYS ALA ASN PHE GLY GLY ASN PRO ASP ASN ILE THR VAL          
SEQRES  18 B  577  PHE GLY GLU SER ALA GLY ALA ALA SER THR HIS TYR MET          
SEQRES  19 B  577  MET LEU THR GLU GLN THR ARG GLY LEU PHE HIS ARG GLY          
SEQRES  20 B  577  ILE LEU MET SER GLY ASN ALA ILE CYS PRO TRP ALA ASN          
SEQRES  21 B  577  THR GLN CYS GLN HIS ARG ALA PHE THR LEU ALA LYS LEU          
SEQRES  22 B  577  ALA GLY TYR LYS GLY GLU ASP ASN ASP LYS ASP VAL LEU          
SEQRES  23 B  577  GLU PHE LEU MET LYS ALA LYS PRO GLN ASP LEU ILE LYS          
SEQRES  24 B  577  LEU GLU GLU LYS VAL LEU THR LEU GLU GLU ARG THR ASN          
SEQRES  25 B  577  LYS VAL MET PHE PRO PHE GLY PRO THR VAL GLU PRO TYR          
SEQRES  26 B  577  GLN THR ALA ASP CYS VAL LEU PRO LYS HIS PRO ARG GLU          
SEQRES  27 B  577  MET VAL LYS THR ALA TRP GLY ASN SER ILE PRO THR MET          
SEQRES  28 B  577  MET GLY ASN THR SER TYR GLU GLY LEU PHE PHE THR SER          
SEQRES  29 B  577  ILE LEU LYS GLN MET PRO LEU LEU VAL LYS GLU LEU GLU          
SEQRES  30 B  577  THR CYS VAL ASN PHE VAL PRO SER GLU LEU ALA ASP ALA          
SEQRES  31 B  577  GLU ARG THR ALA PRO GLU THR LEU GLU MET GLY ALA LYS          
SEQRES  32 B  577  ILE LYS LYS ALA HIS VAL THR GLY GLU THR PRO THR ALA          
SEQRES  33 B  577  ASP ASN PHE MET ASP LEU CYS SER HIS PHE TYR PHE TRP          
SEQRES  34 B  577  PHE PRO MET HIS ARG LEU LEU GLN LEU ARG PHE ASN HIS          
SEQRES  35 B  577  THR SER GLY THR PRO VAL TYR LEU TYR ARG PHE ASP PHE          
SEQRES  36 B  577  ASP SER GLU ASP LEU ILE ASN PRO TYR ARG ILE MET ARG          
SEQRES  37 B  577  SER GLY ARG GLY VAL LYS GLY VAL SER HIS THR ASP GLU          
SEQRES  38 B  577  LEU THR TYR PHE PHE TRP ASN GLN LEU ALA LYS ARG MET          
SEQRES  39 B  577  PRO LYS GLU SER ARG GLU TYR LYS THR ILE GLU ARG MET          
SEQRES  40 B  577  THR GLY ILE TRP THR GLN PHE ALA THR THR GLY ASN PRO          
SEQRES  41 B  577  TYR SER ASN GLU ILE GLU GLY MET GLU ASN VAL SER TRP          
SEQRES  42 B  577  ASP PRO ILE GLU LYS SER ASP GLU VAL TYR LYS CYS LEU          
SEQRES  43 B  577  ASN ILE SER ASP GLU LEU LYS MET ILE ASP VAL PRO GLU          
SEQRES  44 B  577  MET GLY LYS ILE LYS GLN TRP GLU SER MET PHE GLU LYS          
SEQRES  45 B  577  HIS ARG ASP LEU PHE                                          
FORMUL   3  HOH   *376(H2 O)                                                    
HELIX    1 AA1 SER A    6  LEU A   27  1                                  22    
HELIX    2 AA2 VAL A   68  ARG A   72  5                                   5    
HELIX    3 AA3 TYR A  152  LYS A  156  5                                   5    
HELIX    4 AA4 LEU A  167  LEU A  173  1                                   7    
HELIX    5 AA5 ASN A  185  CYS A  202  1                                  18    
HELIX    6 AA6 ALA A  203  PHE A  205  5                                   3    
HELIX    7 AA7 SER A  218  THR A  230  1                                  13    
HELIX    8 AA8 GLU A  231  ARG A  234  5                                   4    
HELIX    9 AA9 HIS A  258  ALA A  267  1                                  10    
HELIX   10 AB1 ASN A  274  ALA A  285  1                                  12    
HELIX   11 AB2 LYS A  286  GLU A  294  1                                   9    
HELIX   12 AB3 GLU A  295  VAL A  297  5                                   3    
HELIX   13 AB4 THR A  299  ASN A  305  1                                   7    
HELIX   14 AB5 HIS A  328  LYS A  334  1                                   7    
HELIX   15 AB6 ALA A  336  ILE A  341  5                                   6    
HELIX   16 AB7 TYR A  350  PHE A  354  5                                   5    
HELIX   17 AB8 PHE A  355  MET A  362  1                                   8    
HELIX   18 AB9 PRO A  363  THR A  371  5                                   9    
HELIX   19 AC1 CYS A  372  VAL A  376  5                                   5    
HELIX   20 AC2 ALA A  387  VAL A  402  1                                  16    
HELIX   21 AC3 THR A  408  PHE A  421  1                                  14    
HELIX   22 AC4 PHE A  421  HIS A  435  1                                  15    
HELIX   23 AC5 ASN A  455  ARG A  461  1                                   7    
HELIX   24 AC6 THR A  472  PHE A  478  5                                   7    
HELIX   25 AC7 SER A  491  GLY A  511  1                                  21    
HELIX   26 AC8 GLU A  552  SER A  561  1                                  10    
HELIX   27 AC9 MET A  562  GLU A  564  5                                   3    
HELIX   28 AD1 HIS A  566  PHE A  570  5                                   5    
HELIX   29 AD2 SER B    6  LEU B   27  1                                  22    
HELIX   30 AD3 VAL B   68  ARG B   72  5                                   5    
HELIX   31 AD4 TYR B  152  LYS B  156  5                                   5    
HELIX   32 AD5 LEU B  167  LEU B  173  1                                   7    
HELIX   33 AD6 SER B  177  ASN B  181  5                                   5    
HELIX   34 AD7 ASN B  185  CYS B  202  1                                  18    
HELIX   35 AD8 ALA B  203  PHE B  205  5                                   3    
HELIX   36 AD9 SER B  218  THR B  230  1                                  13    
HELIX   37 AE1 GLU B  231  ARG B  234  5                                   4    
HELIX   38 AE2 CYS B  249  ASN B  253  5                                   5    
HELIX   39 AE3 HIS B  258  ALA B  267  1                                  10    
HELIX   40 AE4 ASN B  274  MET B  283  1                                  10    
HELIX   41 AE5 LYS B  286  GLU B  294  1                                   9    
HELIX   42 AE6 GLU B  295  VAL B  297  5                                   3    
HELIX   43 AE7 THR B  299  ASN B  305  1                                   7    
HELIX   44 AE8 HIS B  328  LYS B  334  1                                   7    
HELIX   45 AE9 THR B  335  ILE B  341  5                                   7    
HELIX   46 AF1 TYR B  350  PHE B  354  5                                   5    
HELIX   47 AF2 PHE B  355  MET B  362  1                                   8    
HELIX   48 AF3 PRO B  363  GLU B  370  5                                   8    
HELIX   49 AF4 CYS B  372  VAL B  376  5                                   5    
HELIX   50 AF5 ALA B  387  VAL B  402  1                                  16    
HELIX   51 AF6 THR B  408  PHE B  421  1                                  14    
HELIX   52 AF7 PHE B  421  THR B  436  1                                  16    
HELIX   53 AF8 PRO B  456  ARG B  461  1                                   6    
HELIX   54 AF9 THR B  472  PHE B  478  5                                   7    
HELIX   55 AG1 SER B  491  GLY B  511  1                                  21    
HELIX   56 AG2 GLU B  552  MET B  562  1                                  11    
SHEET    1 AA1 3 THR A  28  ALA A  35  0                                        
SHEET    2 AA1 3 LYS A  41  LEU A  48 -1  O  LYS A  46   N  GLU A  31           
SHEET    3 AA1 3 VAL A  85  ASP A  87  1  O  ARG A  86   N  LYS A  43           
SHEET    1 AA212 THR A  28  ALA A  35  0                                        
SHEET    2 AA212 LYS A  41  LEU A  48 -1  O  LYS A  46   N  GLU A  31           
SHEET    3 AA212 SER A  54  PRO A  62 -1  O  SER A  57   N  VAL A  45           
SHEET    4 AA212 TYR A 113  THR A 118 -1  O  THR A 118   N  TYR A  56           
SHEET    5 AA212 VAL A 159  ILE A 163 -1  O  LEU A 160   N  TYR A 117           
SHEET    6 AA212 ARG A 127  ILE A 133  1  N  LEU A 130   O  VAL A 159           
SHEET    7 AA212 GLY A 207  GLU A 217  1  O  THR A 213   N  VAL A 129           
SHEET    8 AA212 ARG A 239  MET A 243  1  O  ARG A 239   N  VAL A 214           
SHEET    9 AA212 THR A 343  THR A 348  1  O  MET A 344   N  LEU A 242           
SHEET   10 AA212 TYR A 442  PHE A 446  1  O  TYR A 442   N  MET A 345           
SHEET   11 AA212 LYS A 537  ILE A 541  1  O  ILE A 541   N  ARG A 445           
SHEET   12 AA212 LEU A 545  ASP A 549 -1  O  LYS A 546   N  ASN A 540           
SHEET    1 AA3 2 GLN A  97  VAL A  98  0                                        
SHEET    2 AA3 2 VAL A 105  CYS A 106 -1  O  CYS A 106   N  GLN A  97           
SHEET    1 AA4 3 THR B  28  ALA B  35  0                                        
SHEET    2 AA4 3 LYS B  41  LEU B  48 -1  O  GLY B  44   N  VAL B  33           
SHEET    3 AA4 3 VAL B  85  ASP B  87  1  O  ARG B  86   N  LYS B  41           
SHEET    1 AA512 THR B  28  ALA B  35  0                                        
SHEET    2 AA512 LYS B  41  LEU B  48 -1  O  GLY B  44   N  VAL B  33           
SHEET    3 AA512 SER B  54  PRO B  62 -1  O  TYR B  55   N  ARG B  47           
SHEET    4 AA512 TYR B 113  THR B 118 -1  O  THR B 118   N  TYR B  56           
SHEET    5 AA512 VAL B 159  ILE B 163 -1  O  LEU B 160   N  TYR B 117           
SHEET    6 AA512 ARG B 127  ILE B 133  1  N  LEU B 130   O  VAL B 159           
SHEET    7 AA512 GLY B 207  GLU B 217  1  O  THR B 213   N  VAL B 129           
SHEET    8 AA512 ARG B 239  MET B 243  1  O  ARG B 239   N  VAL B 214           
SHEET    9 AA512 THR B 343  THR B 348  1  O  MET B 344   N  LEU B 242           
SHEET   10 AA512 VAL B 441  PHE B 446  1  O  TYR B 442   N  MET B 345           
SHEET   11 AA512 LYS B 537  ILE B 541  1  O  ILE B 541   N  ARG B 445           
SHEET   12 AA512 LEU B 545  ASP B 549 -1  O  LYS B 546   N  ASN B 540           
SHEET    1 AA6 2 GLN B  97  VAL B  98  0                                        
SHEET    2 AA6 2 VAL B 105  CYS B 106 -1  O  CYS B 106   N  GLN B  97           
CISPEP   1 TYR A  269    LYS A  270          0        -8.36                     
CISPEP   2 TYR B  269    LYS B  270          0       -13.73                     
CRYST1   61.767  108.956   92.172  90.00  90.36  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016190  0.000000  0.000101        0.00000                         
SCALE2      0.000000  0.009178  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010849        0.00000                         
TER    4578      PHE A 570                                                      
TER    9142      PHE B 570                                                      
MASTER      445    0    0   56   34    0    0    6 9516    2    0   90          
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.
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