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LongText Report for: 3AJA-pdb

Name Class
3AJA-pdb
HEADER    HYDROLASE                               27-MAY-10   3AJA              
TITLE     CRYSTAL STRUCTURE OF MSMEG_6394                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 36-337;                                           
COMPND   5 SYNONYM: MSMEG_6394 PROTEIN;                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;                        
SOURCE   3 ORGANISM_TAXID: 246196;                                              
SOURCE   4 STRAIN: STRAIN ATCC 700084 / MC(2)155;                               
SOURCE   5 GENE: MSMEG_6394;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-28B                                   
KEYWDS    ALPHA-BETA HYDROLASE, SERINE ESTERASE, CUTINASE, LIPASE, HYDROLASE    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.VIVIAN,J.SCOBLE,T.BEDDOE,J.ROSSJOHN                               
REVDAT   1   11-AUG-10 3AJA    0                                                
JRNL        AUTH   P.K.CRELLIN,J.P.VIVIAN,J.SCOBLE,F.M.CHOW,N.P.WEST,           
JRNL        AUTH 2 R.BRAMMANANTH,N.I.PROELLOCKS,A.SHAHINE,J.LE NOURS,           
JRNL        AUTH 3 M.C.J.WILCE,W.J.BRITTON,R.L.COPPEL,J.ROSSJOHN,T.BEDDOE       
JRNL        TITL   FUNCTIONAL CHARACTERISATION OF A LIPASE ESSENTIAL FOR        
JRNL        TITL 2 MYCOBACTERIAL VIABILITY                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.17                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 17098                          
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) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 932                             
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 560                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3670                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 34                           
REMARK   3   BIN FREE R VALUE                    : 0.3590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3924                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 32                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 114.00                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 103.11                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.18000                                             
REMARK   3    B22 (A**2) : -0.18000                                             
REMARK   3    B33 (A**2) : 0.36000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.355         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.299         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.613        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4025 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5503 ; 1.508 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   521 ; 5.817 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   178 ;35.605 ;25.169       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   589 ;20.035 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;18.852 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   607 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3160 ; 0.008 ; 0.022       
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):  2612 ; 0.462 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4213 ; 0.849 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1413 ; 1.547 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1290 ; 2.401 ; 4.500       
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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1645 ;  0.10 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1645 ;  0.16 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    250 ;  0.15 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    250 ;  0.96 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
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    71        A   334                          
REMARK   3    ORIGIN FOR THE GROUP (A):  71.1600  31.3820   9.4650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7813 T22:   0.1106                                     
REMARK   3      T33:   0.2797 T12:   0.2494                                     
REMARK   3      T13:   0.0260 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6263 L22:   4.3375                                     
REMARK   3      L33:   3.8462 L12:   1.4158                                     
REMARK   3      L13:   0.5366 L23:   1.3839                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3537 S12:   0.4090 S13:  -0.1802                       
REMARK   3      S21:   0.0312 S22:  -0.0145 S23:  -0.1241                       
REMARK   3      S31:   0.3975 S32:   0.1190 S33:  -0.3392                       
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    71        B   334                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.8390  13.5030  33.5920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5756 T22:   0.2042                                     
REMARK   3      T33:   0.2440 T12:  -0.0701                                     
REMARK   3      T13:   0.1115 T23:   0.0164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5250 L22:   4.2590                                     
REMARK   3      L33:   4.4564 L12:   0.3102                                     
REMARK   3      L13:  -0.6713 L23:  -0.1466                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0480 S12:   0.2430 S13:  -0.0098                       
REMARK   3      S21:   0.1795 S22:  -0.0093 S23:   0.4574                       
REMARK   3      S31:  -0.3667 S32:  -0.6912 S33:  -0.0387                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 3AJA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029320.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97941, 0.97930, 0.96411          
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20363                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
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   (%): 64.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1M SODIUM FORMATE, 0.1M BISTRIS-       
REMARK 280  PROPANE, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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       65.21700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       65.21700            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      104.76650            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       65.21700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       52.38325            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       65.21700            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      157.14975            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       65.21700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      157.14975            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.21700            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       52.38325            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       65.21700            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       65.21700            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      104.76650            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       65.21700            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       65.21700            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      104.76650            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       65.21700            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      157.14975            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       65.21700            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       52.38325            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       65.21700            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       52.38325            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       65.21700            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      157.14975            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       65.21700            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       65.21700            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      104.76650            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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    36                                                      
REMARK 465     ARG A    37                                                      
REMARK 465     ARG A    38                                                      
REMARK 465     PRO A    39                                                      
REMARK 465     ASP A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     THR A    44                                                      
REMARK 465     PRO A    45                                                      
REMARK 465     PRO A    46                                                      
REMARK 465     PRO A    47                                                      
REMARK 465     SER A    48                                                      
REMARK 465     ALA A    49                                                      
REMARK 465     GLU A    50                                                      
REMARK 465     PRO A    51                                                      
REMARK 465     PRO A    52                                                      
REMARK 465     GLY A    53                                                      
REMARK 465     GLY A    54                                                      
REMARK 465     VAL A    55                                                      
REMARK 465     VAL A    56                                                      
REMARK 465     VAL A    57                                                      
REMARK 465     PRO A    58                                                      
REMARK 465     PRO A    59                                                      
REMARK 465     GLY A    60                                                      
REMARK 465     THR A    61                                                      
REMARK 465     ARG A    62                                                      
REMARK 465     LYS A    63                                                      
REMARK 465     PRO A    64                                                      
REMARK 465     ARG A    65                                                      
REMARK 465     PRO A    66                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     PHE A    68                                                      
REMARK 465     GLN A    69                                                      
REMARK 465     SER A    70                                                      
REMARK 465     SER A   294                                                      
REMARK 465     ALA A   295                                                      
REMARK 465     ALA A   296                                                      
REMARK 465     GLY A   297                                                      
REMARK 465     LYS A   335                                                      
REMARK 465     HIS A   336                                                      
REMARK 465     GLY A   337                                                      
REMARK 465     MET B    36                                                      
REMARK 465     ARG B    37                                                      
REMARK 465     ARG B    38                                                      
REMARK 465     PRO B    39                                                      
REMARK 465     ASP B    40                                                      
REMARK 465     THR B    41                                                      
REMARK 465     PRO B    42                                                      
REMARK 465     ALA B    43                                                      
REMARK 465     THR B    44                                                      
REMARK 465     PRO B    45                                                      
REMARK 465     PRO B    46                                                      
REMARK 465     PRO B    47                                                      
REMARK 465     SER B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     GLU B    50                                                      
REMARK 465     PRO B    51                                                      
REMARK 465     PRO B    52                                                      
REMARK 465     GLY B    53                                                      
REMARK 465     GLY B    54                                                      
REMARK 465     VAL B    55                                                      
REMARK 465     VAL B    56                                                      
REMARK 465     VAL B    57                                                      
REMARK 465     PRO B    58                                                      
REMARK 465     PRO B    59                                                      
REMARK 465     GLY B    60                                                      
REMARK 465     THR B    61                                                      
REMARK 465     ARG B    62                                                      
REMARK 465     LYS B    63                                                      
REMARK 465     PRO B    64                                                      
REMARK 465     ARG B    65                                                      
REMARK 465     PRO B    66                                                      
REMARK 465     GLU B    67                                                      
REMARK 465     PHE B    68                                                      
REMARK 465     GLN B    69                                                      
REMARK 465     SER B    70                                                      
REMARK 465     LYS B   335                                                      
REMARK 465     HIS B   336                                                      
REMARK 465     GLY B   337                                                      
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    ASP B    72     O    HOH B    25              2.00            
REMARK 500   CB   CYS B    73     SG   CYS B   165              2.08            
REMARK 500   OD2  ASP A   209     NH2  ARG A   250              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    PRO A  74   C   -  N   -  CD  ANGL. DEV. = -18.1 DEGREES          
REMARK 500    LEU B 244   CA  -  CB  -  CG  ANGL. DEV. =  13.8 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    ASP A  72      -65.40    149.98                                   
REMARK 500    ASP A  75      -73.53    -53.50                                   
REMARK 500    THR A  97      -26.95   -140.71                                   
REMARK 500    PHE A  99       75.92   -119.31                                   
REMARK 500    PHE A 131       88.34   -156.33                                   
REMARK 500    SER A 176     -111.94     29.82                                   
REMARK 500    PRO A 222       46.41    -81.71                                   
REMARK 500    SER A 267      105.32    -51.78                                   
REMARK 500    ASN A 283       58.59   -143.26                                   
REMARK 500    LEU A 302       72.71   -104.85                                   
REMARK 500    ASP B  72      -76.24    130.39                                   
REMARK 500    THR B  97      -24.19   -142.82                                   
REMARK 500    LYS B 139       30.22    -91.82                                   
REMARK 500    SER B 176     -112.55     31.42                                   
REMARK 500    PRO B 222       44.12    -83.86                                   
REMARK 500    VAL B 236      107.15    -57.62                                   
REMARK 500    SER B 267      109.25    -54.64                                   
REMARK 500    LEU B 302       25.44    -75.77                                   
REMARK 500    PRO B 306       31.09    -94.99                                   
REMARK 500    ASN B 312       46.57     32.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3AJA A   36   337  UNP    A0R619   A0R619_MYCS2    36    337             
DBREF  3AJA B   36   337  UNP    A0R619   A0R619_MYCS2    36    337             
SEQRES   1 A  302  MET ARG ARG PRO ASP THR PRO ALA THR PRO PRO PRO SER          
SEQRES   2 A  302  ALA GLU PRO PRO GLY GLY VAL VAL VAL PRO PRO GLY THR          
SEQRES   3 A  302  ARG LYS PRO ARG PRO GLU PHE GLN SER ALA ASP CYS PRO          
SEQRES   4 A  302  ASP VAL MET MET VAL SER ILE PRO GLY THR TRP GLU SER          
SEQRES   5 A  302  SER PRO THR ASP ASP PRO PHE ASN PRO THR GLN PHE PRO          
SEQRES   6 A  302  LEU SER LEU MET SER ASN ILE SER LYS PRO LEU ALA GLU          
SEQRES   7 A  302  GLN PHE GLY PRO ASP ARG LEU GLN VAL TYR THR THR PRO          
SEQRES   8 A  302  TYR THR ALA GLN PHE HIS ASN PRO PHE ALA ALA ASP LYS          
SEQRES   9 A  302  GLN MET SER TYR ASN ASP SER ARG ALA GLU GLY MET ARG          
SEQRES  10 A  302  THR THR VAL LYS ALA MET THR ASP MET ASN ASP ARG CYS          
SEQRES  11 A  302  PRO LEU THR SER TYR VAL ILE ALA GLY PHE SER GLN GLY          
SEQRES  12 A  302  ALA VAL ILE ALA GLY ASP ILE ALA SER ASP ILE GLY ASN          
SEQRES  13 A  302  GLY ARG GLY PRO VAL ASP GLU ASP LEU VAL LEU GLY VAL          
SEQRES  14 A  302  THR LEU ILE ALA ASP GLY ARG ARG GLN MET GLY VAL GLY          
SEQRES  15 A  302  GLN ASP VAL GLY PRO ASN PRO ALA GLY GLN GLY ALA GLU          
SEQRES  16 A  302  ILE THR LEU HIS GLU VAL PRO ALA LEU SER ALA LEU GLY          
SEQRES  17 A  302  LEU THR MET THR GLY PRO ARG PRO GLY GLY PHE GLY ALA          
SEQRES  18 A  302  LEU ASP ASN ARG THR ASN GLN ILE CYS GLY SER GLY ASP          
SEQRES  19 A  302  LEU ILE CYS SER ALA PRO GLU GLN ALA PHE SER VAL PHE          
SEQRES  20 A  302  ASN LEU PRO LYS THR LEU GLU THR LEU SER GLY SER ALA          
SEQRES  21 A  302  ALA GLY PRO VAL HIS ALA LEU TYR ASN THR PRO GLN PHE          
SEQRES  22 A  302  TRP VAL GLU ASN GLY GLN THR ALA THR GLN TRP THR LEU          
SEQRES  23 A  302  GLU TRP ALA ARG ASN LEU VAL GLU ASN ALA PRO HIS PRO          
SEQRES  24 A  302  LYS HIS GLY                                                  
SEQRES   1 B  302  MET ARG ARG PRO ASP THR PRO ALA THR PRO PRO PRO SER          
SEQRES   2 B  302  ALA GLU PRO PRO GLY GLY VAL VAL VAL PRO PRO GLY THR          
SEQRES   3 B  302  ARG LYS PRO ARG PRO GLU PHE GLN SER ALA ASP CYS PRO          
SEQRES   4 B  302  ASP VAL MET MET VAL SER ILE PRO GLY THR TRP GLU SER          
SEQRES   5 B  302  SER PRO THR ASP ASP PRO PHE ASN PRO THR GLN PHE PRO          
SEQRES   6 B  302  LEU SER LEU MET SER ASN ILE SER LYS PRO LEU ALA GLU          
SEQRES   7 B  302  GLN PHE GLY PRO ASP ARG LEU GLN VAL TYR THR THR PRO          
SEQRES   8 B  302  TYR THR ALA GLN PHE HIS ASN PRO PHE ALA ALA ASP LYS          
SEQRES   9 B  302  GLN MET SER TYR ASN ASP SER ARG ALA GLU GLY MET ARG          
SEQRES  10 B  302  THR THR VAL LYS ALA MET THR ASP MET ASN ASP ARG CYS          
SEQRES  11 B  302  PRO LEU THR SER TYR VAL ILE ALA GLY PHE SER GLN GLY          
SEQRES  12 B  302  ALA VAL ILE ALA GLY ASP ILE ALA SER ASP ILE GLY ASN          
SEQRES  13 B  302  GLY ARG GLY PRO VAL ASP GLU ASP LEU VAL LEU GLY VAL          
SEQRES  14 B  302  THR LEU ILE ALA ASP GLY ARG ARG GLN MET GLY VAL GLY          
SEQRES  15 B  302  GLN ASP VAL GLY PRO ASN PRO ALA GLY GLN GLY ALA GLU          
SEQRES  16 B  302  ILE THR LEU HIS GLU VAL PRO ALA LEU SER ALA LEU GLY          
SEQRES  17 B  302  LEU THR MET THR GLY PRO ARG PRO GLY GLY PHE GLY ALA          
SEQRES  18 B  302  LEU ASP ASN ARG THR ASN GLN ILE CYS GLY SER GLY ASP          
SEQRES  19 B  302  LEU ILE CYS SER ALA PRO GLU GLN ALA PHE SER VAL PHE          
SEQRES  20 B  302  ASN LEU PRO LYS THR LEU GLU THR LEU SER GLY SER ALA          
SEQRES  21 B  302  ALA GLY PRO VAL HIS ALA LEU TYR ASN THR PRO GLN PHE          
SEQRES  22 B  302  TRP VAL GLU ASN GLY GLN THR ALA THR GLN TRP THR LEU          
SEQRES  23 B  302  GLU TRP ALA ARG ASN LEU VAL GLU ASN ALA PRO HIS PRO          
SEQRES  24 B  302  LYS HIS GLY                                                  
FORMUL   3  HOH   *32(H2 O)                                                     
HELIX    1   1 MET A  104  PHE A  115  1                                  12    
HELIX    2   2 SER A  142  CYS A  165  1                                  24    
HELIX    3   3 SER A  176  ASN A  191  1                                  16    
HELIX    4   4 ASP A  197  ASP A  199  5                                   3    
HELIX    5   5 GLY A  228  LEU A  233  1                                   6    
HELIX    6   6 VAL A  236  LEU A  242  1                                   7    
HELIX    7   7 PHE A  254  ASP A  258  5                                   5    
HELIX    8   8 PRO A  275  PHE A  279  5                                   5    
HELIX    9   9 ASN A  283  GLY A  293  1                                  11    
HELIX   10  10 ALA A  316  ALA A  331  1                                  16    
HELIX   11  11 MET B  104  PHE B  115  1                                  12    
HELIX   12  12 SER B  142  CYS B  165  1                                  24    
HELIX   13  13 SER B  176  ASN B  191  1                                  16    
HELIX   14  14 ASP B  197  ASP B  199  5                                   3    
HELIX   15  15 GLY B  228  LEU B  233  1                                   6    
HELIX   16  16 VAL B  236  LEU B  242  1                                   7    
HELIX   17  17 PHE B  254  ASP B  258  5                                   5    
HELIX   18  18 PRO B  275  PHE B  279  5                                   5    
HELIX   19  19 ASN B  283  GLY B  293  1                                  11    
HELIX   20  20 GLY B  297  LEU B  302  1                                   6    
HELIX   21  21 TYR B  303  THR B  305  5                                   3    
HELIX   22  22 ALA B  316  ALA B  331  1                                  16    
SHEET    1   A 6 LEU A 120  THR A 124  0                                        
SHEET    2   A 6 VAL A  76  ILE A  81  1  N  MET A  78   O  GLN A 121           
SHEET    3   A 6 SER A 169  PHE A 175  1  O  SER A 169   N  MET A  77           
SHEET    4   A 6 VAL A 201  ILE A 207  1  O  ILE A 207   N  GLY A 174           
SHEET    5   A 6 THR A 261  ILE A 264  1  O  ASN A 262   N  VAL A 204           
SHEET    6   A 6 GLN A 218  ASP A 219  1  N  GLN A 218   O  THR A 261           
SHEET    1   B 2 VAL A 310  GLU A 311  0                                        
SHEET    2   B 2 GLN A 314  THR A 315 -1  O  GLN A 314   N  GLU A 311           
SHEET    1   C 6 LEU B 120  THR B 124  0                                        
SHEET    2   C 6 VAL B  76  ILE B  81  1  N  MET B  78   O  TYR B 123           
SHEET    3   C 6 SER B 169  PHE B 175  1  O  SER B 169   N  MET B  77           
SHEET    4   C 6 VAL B 201  ILE B 207  1  O  LEU B 202   N  TYR B 170           
SHEET    5   C 6 THR B 261  ILE B 264  1  O  ASN B 262   N  VAL B 204           
SHEET    6   C 6 GLN B 218  ASP B 219  1  N  GLN B 218   O  THR B 261           
SHEET    1   D 2 VAL B 310  GLU B 311  0                                        
SHEET    2   D 2 GLN B 314  THR B 315 -1  O  GLN B 314   N  GLU B 311           
SSBOND   1 CYS A   73    CYS A  165                          1555   1555  1.60  
SSBOND   2 CYS A  265    CYS A  272                          1555   1555  2.05  
SSBOND   3 CYS B   73    CYS B  165                          1555   1555  2.11  
SSBOND   4 CYS B  265    CYS B  272                          1555   1555  2.11  
CISPEP   1 GLY A  194    PRO A  195          0         1.27                     
CISPEP   2 GLY B  194    PRO B  195          0         1.43                     
CRYST1  130.434  130.434  209.533  90.00  90.00  90.00 I 41 2 2     32          
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      0.007667  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007667  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004773        0.00000                         
TER    1953      PRO A 334                                                      
TER    3926      PRO B 334                                                      
MASTER      490    0    0   22   16    0    0    6 3956    2    8   48          
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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