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Database: PDB
Entry: 2QJ3
LinkDB: 2QJ3
Original site: 2QJ3 
HEADER    TRANSFERASE                             06-JUL-07   2QJ3              
TITLE     MYCOBACTERIUM TUBERCULOSIS FABD                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE;             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: MCT;                                                        
COMPND   5 EC: 2.3.1.39;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 83332;                                               
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 GENE: FABD;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C41(DE3);                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    MALONYL-COA, FATTY ACID SYNTHASE, MYCOLIC ACIDS, TRANSFERASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.GHADBANE,A.K.BROWN,L.KREMER,G.S.BESRA,K.FUTTERER                    
REVDAT   4   13-JUL-11 2QJ3    1       VERSN                                    
REVDAT   3   24-FEB-09 2QJ3    1       VERSN                                    
REVDAT   2   06-NOV-07 2QJ3    1       JRNL                                     
REVDAT   1   04-SEP-07 2QJ3    0                                                
JRNL        AUTH   H.GHADBANE,A.K.BROWN,L.KREMER,G.S.BESRA,K.FUTTERER           
JRNL        TITL   STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS MTFABD, A            
JRNL        TITL 2 MALONYL-COA:ACYL CARRIER PROTEIN TRANSACYLASE (MCAT).        
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  63   831 2007              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        PMID   17909282                                                     
JRNL        DOI    10.1107/S1744309107042455                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 17832                          
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) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 965                             
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1266                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.26                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.3130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4548                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 43                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.45000                                              
REMARK   3    B22 (A**2) : 0.45000                                              
REMARK   3    B33 (A**2) : -0.67000                                             
REMARK   3    B12 (A**2) : 0.22000                                              
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): 0.414         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.304         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.315        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.916                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.893                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4622 ; 0.008 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6313 ; 1.206 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   631 ; 5.503 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   166 ;34.708 ;24.096       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   699 ;20.189 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;16.928 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   773 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3462 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2119 ; 0.215 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3160 ; 0.296 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   147 ; 0.146 ; 0.200       
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):    69 ; 0.328 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.111 ; 0.200       
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):  3203 ; 0.304 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5003 ; 0.546 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1525 ; 0.817 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1310 ; 1.454 ; 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 : NULL                              
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     1        A   302                          
REMARK   3    ORIGIN FOR THE GROUP (A):  78.3676  22.4721  29.7489              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2253 T22:  -0.1667                                     
REMARK   3      T33:  -0.2607 T12:   0.0233                                     
REMARK   3      T13:   0.0546 T23:  -0.0774                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4078 L22:   1.7694                                     
REMARK   3      L33:   2.0606 L12:   0.5395                                     
REMARK   3      L13:   0.5840 L23:   0.2675                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1046 S12:  -0.5782 S13:   0.1488                       
REMARK   3      S21:   0.2440 S22:  -0.0141 S23:   0.0827                       
REMARK   3      S31:   0.0868 S32:   0.1393 S33:  -0.0904                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   302                          
REMARK   3    ORIGIN FOR THE GROUP (A): 114.7952  22.6711  12.4821              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1690 T22:  -0.3231                                     
REMARK   3      T33:  -0.2661 T12:  -0.0302                                     
REMARK   3      T13:  -0.0601 T23:   0.0309                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6979 L22:   2.5897                                     
REMARK   3      L33:   1.4519 L12:   0.1854                                     
REMARK   3      L13:   0.0376 L23:   0.2617                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0910 S12:  -0.1850 S13:  -0.0245                       
REMARK   3      S21:   0.4271 S22:  -0.0288 S23:  -0.2226                       
REMARK   3      S31:  -0.0380 S32:   0.0054 S33:  -0.0622                       
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 ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2QJ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043661.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
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) : 0.992,1.486                        
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : CYLINDRICAL MIRROR                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18818                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 13.000                             
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.34000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.34000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-12% PEG MME 2000, 0.1 M TRIS-HCL PH   
REMARK 280  8.0-8.5, 5-10 MM NICL2. , VAPOR DIFFUSION                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+2/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+1/3                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.99333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       31.99667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       63.99333            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       31.99667            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       63.99333            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       31.99667            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       63.99333            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       31.99667            
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   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
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     LEU B  80    CG   CD1  CD2                                       
REMARK 470     ARG B 183    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  11       15.42   -153.55                                   
REMARK 500    LEU A  44       -0.42    -59.77                                   
REMARK 500    THR A  46      -86.53    -97.40                                   
REMARK 500    ASP A  55      103.29   -161.89                                   
REMARK 500    SER A  91     -104.76     53.40                                   
REMARK 500    PRO A 128       98.42    -60.08                                   
REMARK 500    PRO A 153       84.30    -68.27                                   
REMARK 500    ALA A 186       91.66    -65.03                                   
REMARK 500    PHE A 197        5.36    -64.09                                   
REMARK 500    ASN A 211       24.76    -75.51                                   
REMARK 500    ASP A 226       -2.27   -143.90                                   
REMARK 500    GLU A 298       47.75    -76.77                                   
REMARK 500    GLU B  14      -57.72    -14.44                                   
REMARK 500    THR B  46      -92.34    -92.73                                   
REMARK 500    THR B  54       35.74    -81.58                                   
REMARK 500    SER B  91     -118.86     59.15                                   
REMARK 500    ALA B 186       98.64    -61.09                                   
REMARK 500    ASN B 211       48.79    -89.44                                   
REMARK 500    ARG B 249       67.69   -112.87                                   
REMARK 500    GLU B 298       -3.69    -57.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A  135     GLY A  136                 -147.51                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 801  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B -17   OG                                                     
REMARK 620 2 HIS A -14   NE2 115.8                                              
REMARK 620 3 HIS A -11   NE2 154.3  87.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 804  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B -15   NE2                                                    
REMARK 620 2 HIS B -13   NE2  92.5                                              
REMARK 620 3 HIS A -15   NE2  99.5  98.6                                        
REMARK 620 4 HIS A -13   NE2  93.5 174.0  80.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 805  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B -14   NE2                                                    
REMARK 620 2 HIS B -11   NE2  83.2                                              
REMARK 620 3 SER A -17   OG  127.9 148.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 802  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B -12   NE2                                                    
REMARK 620 2 HIS B -10   NE2  89.6                                              
REMARK 620 3 HIS B   0   NE2  98.5  89.5                                        
REMARK 620 4 ASP B  84   OD1  82.0 171.2  89.3                                  
REMARK 620 5 ASP A 216   OD2  78.8  95.5 174.2  85.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 803  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 216   OD2                                                    
REMARK 620 2 HIS A -12   NE2  82.1                                              
REMARK 620 3 HIS A   0   NE2 167.9  88.6                                        
REMARK 620 4 ASP A  84   OD1  86.6  80.0  84.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 804                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 805                  
DBREF  2QJ3 A    1   302  UNP    P63458   FABD_MYCTU       1    302             
DBREF  2QJ3 B    1   302  UNP    P63458   FABD_MYCTU       1    302             
SEQADV 2QJ3 MET A  -19  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 GLY A  -18  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 SER A  -17  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 SER A  -16  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 HIS A  -15  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 HIS A  -14  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 HIS A  -13  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 HIS A  -12  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 HIS A  -11  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 HIS A  -10  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 SER A   -9  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 SER A   -8  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 GLY A   -7  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 LEU A   -6  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 VAL A   -5  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 PRO A   -4  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 ARG A   -3  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 GLY A   -2  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 SER A   -1  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 HIS A    0  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 MET B  -19  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 GLY B  -18  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 SER B  -17  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 SER B  -16  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 HIS B  -15  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 HIS B  -14  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 HIS B  -13  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 HIS B  -12  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 HIS B  -11  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 HIS B  -10  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 SER B   -9  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 SER B   -8  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 GLY B   -7  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 LEU B   -6  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 VAL B   -5  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 PRO B   -4  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 ARG B   -3  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 GLY B   -2  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 SER B   -1  UNP  P63458              EXPRESSION TAG                 
SEQADV 2QJ3 HIS B    0  UNP  P63458              EXPRESSION TAG                 
SEQRES   1 A  322  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  322  LEU VAL PRO ARG GLY SER HIS MET ILE ALA LEU LEU ALA          
SEQRES   3 A  322  PRO GLY GLN GLY SER GLN THR GLU GLY MET LEU SER PRO          
SEQRES   4 A  322  TRP LEU GLN LEU PRO GLY ALA ALA ASP GLN ILE ALA ALA          
SEQRES   5 A  322  TRP SER LYS ALA ALA ASP LEU ASP LEU ALA ARG LEU GLY          
SEQRES   6 A  322  THR THR ALA SER THR GLU GLU ILE THR ASP THR ALA VAL          
SEQRES   7 A  322  ALA GLN PRO LEU ILE VAL ALA ALA THR LEU LEU ALA HIS          
SEQRES   8 A  322  GLN GLU LEU ALA ARG ARG CYS VAL LEU ALA GLY LYS ASP          
SEQRES   9 A  322  VAL ILE VAL ALA GLY HIS SER VAL GLY GLU ILE ALA ALA          
SEQRES  10 A  322  TYR ALA ILE ALA GLY VAL ILE ALA ALA ASP ASP ALA VAL          
SEQRES  11 A  322  ALA LEU ALA ALA THR ARG GLY ALA GLU MET ALA LYS ALA          
SEQRES  12 A  322  CYS ALA THR GLU PRO THR GLY MET SER ALA VAL LEU GLY          
SEQRES  13 A  322  GLY ASP GLU THR GLU VAL LEU SER ARG LEU GLU GLN LEU          
SEQRES  14 A  322  ASP LEU VAL PRO ALA ASN ARG ASN ALA ALA GLY GLN ILE          
SEQRES  15 A  322  VAL ALA ALA GLY ARG LEU THR ALA LEU GLU LYS LEU ALA          
SEQRES  16 A  322  GLU ASP PRO PRO ALA LYS ALA ARG VAL ARG ALA LEU GLY          
SEQRES  17 A  322  VAL ALA GLY ALA PHE HIS THR GLU PHE MET ALA PRO ALA          
SEQRES  18 A  322  LEU ASP GLY PHE ALA ALA ALA ALA ALA ASN ILE ALA THR          
SEQRES  19 A  322  ALA ASP PRO THR ALA THR LEU LEU SER ASN ARG ASP GLY          
SEQRES  20 A  322  LYS PRO VAL THR SER ALA ALA ALA ALA MET ASP THR LEU          
SEQRES  21 A  322  VAL SER GLN LEU THR GLN PRO VAL ARG TRP ASP LEU CYS          
SEQRES  22 A  322  THR ALA THR LEU ARG GLU HIS THR VAL THR ALA ILE VAL          
SEQRES  23 A  322  GLU PHE PRO PRO ALA GLY THR LEU SER GLY ILE ALA LYS          
SEQRES  24 A  322  ARG GLU LEU ARG GLY VAL PRO ALA ARG ALA VAL LYS SER          
SEQRES  25 A  322  PRO ALA ASP LEU ASP GLU LEU ALA ASN LEU                      
SEQRES   1 B  322  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  322  LEU VAL PRO ARG GLY SER HIS MET ILE ALA LEU LEU ALA          
SEQRES   3 B  322  PRO GLY GLN GLY SER GLN THR GLU GLY MET LEU SER PRO          
SEQRES   4 B  322  TRP LEU GLN LEU PRO GLY ALA ALA ASP GLN ILE ALA ALA          
SEQRES   5 B  322  TRP SER LYS ALA ALA ASP LEU ASP LEU ALA ARG LEU GLY          
SEQRES   6 B  322  THR THR ALA SER THR GLU GLU ILE THR ASP THR ALA VAL          
SEQRES   7 B  322  ALA GLN PRO LEU ILE VAL ALA ALA THR LEU LEU ALA HIS          
SEQRES   8 B  322  GLN GLU LEU ALA ARG ARG CYS VAL LEU ALA GLY LYS ASP          
SEQRES   9 B  322  VAL ILE VAL ALA GLY HIS SER VAL GLY GLU ILE ALA ALA          
SEQRES  10 B  322  TYR ALA ILE ALA GLY VAL ILE ALA ALA ASP ASP ALA VAL          
SEQRES  11 B  322  ALA LEU ALA ALA THR ARG GLY ALA GLU MET ALA LYS ALA          
SEQRES  12 B  322  CYS ALA THR GLU PRO THR GLY MET SER ALA VAL LEU GLY          
SEQRES  13 B  322  GLY ASP GLU THR GLU VAL LEU SER ARG LEU GLU GLN LEU          
SEQRES  14 B  322  ASP LEU VAL PRO ALA ASN ARG ASN ALA ALA GLY GLN ILE          
SEQRES  15 B  322  VAL ALA ALA GLY ARG LEU THR ALA LEU GLU LYS LEU ALA          
SEQRES  16 B  322  GLU ASP PRO PRO ALA LYS ALA ARG VAL ARG ALA LEU GLY          
SEQRES  17 B  322  VAL ALA GLY ALA PHE HIS THR GLU PHE MET ALA PRO ALA          
SEQRES  18 B  322  LEU ASP GLY PHE ALA ALA ALA ALA ALA ASN ILE ALA THR          
SEQRES  19 B  322  ALA ASP PRO THR ALA THR LEU LEU SER ASN ARG ASP GLY          
SEQRES  20 B  322  LYS PRO VAL THR SER ALA ALA ALA ALA MET ASP THR LEU          
SEQRES  21 B  322  VAL SER GLN LEU THR GLN PRO VAL ARG TRP ASP LEU CYS          
SEQRES  22 B  322  THR ALA THR LEU ARG GLU HIS THR VAL THR ALA ILE VAL          
SEQRES  23 B  322  GLU PHE PRO PRO ALA GLY THR LEU SER GLY ILE ALA LYS          
SEQRES  24 B  322  ARG GLU LEU ARG GLY VAL PRO ALA ARG ALA VAL LYS SER          
SEQRES  25 B  322  PRO ALA ASP LEU ASP GLU LEU ALA ASN LEU                      
HET     NI  B 801       1                                                       
HET     NI  B 802       1                                                       
HET     NI  B 803       1                                                       
HET     NI  B 804       1                                                       
HET     NI  B 805       1                                                       
HETNAM      NI NICKEL (II) ION                                                  
FORMUL   3   NI    5(NI 2+)                                                     
FORMUL   8  HOH   *43(H2 O)                                                     
HELIX    1   1 LEU A   17  GLN A   22  1                                   6    
HELIX    2   2 GLY A   25  ASP A   38  1                                  14    
HELIX    3   3 ASP A   40  THR A   46  1                                   7    
HELIX    4   4 SER A   49  THR A   54  1                                   6    
HELIX    5   5 ASP A   55  ARG A   77  1                                  23    
HELIX    6   6 VAL A   92  ALA A  101  1                                  10    
HELIX    7   7 ALA A  105  ALA A  125  1                                  21    
HELIX    8   8 ASP A  138  LEU A  149  1                                  12    
HELIX    9   9 LEU A  168  ASP A  177  1                                  10    
HELIX   10  10 THR A  195  ALA A  199  5                                   5    
HELIX   11  11 PRO A  200  ASN A  211  1                                  12    
HELIX   12  12 SER A  232  GLN A  243  1                                  12    
HELIX   13  13 LEU A  244  GLN A  246  5                                   3    
HELIX   14  14 ARG A  249  GLU A  259  1                                  11    
HELIX   15  15 GLY A  272  LEU A  282  1                                  11    
HELIX   16  16 SER A  292  ASP A  297  5                                   6    
HELIX   17  17 LEU B   17  GLN B   22  1                                   6    
HELIX   18  18 GLY B   25  ASP B   38  1                                  14    
HELIX   19  19 ASP B   40  THR B   46  1                                   7    
HELIX   20  20 SER B   49  THR B   54  1                                   6    
HELIX   21  21 ASP B   55  ARG B   77  1                                  23    
HELIX   22  22 VAL B   92  ALA B  101  1                                  10    
HELIX   23  23 ALA B  105  ALA B  125  1                                  21    
HELIX   24  24 ASP B  138  LEU B  149  1                                  12    
HELIX   25  25 LEU B  168  ASP B  177  1                                  10    
HELIX   26  26 THR B  195  PRO B  200  5                                   6    
HELIX   27  27 ALA B  201  ASN B  211  1                                  11    
HELIX   28  28 SER B  232  GLN B  243  1                                  12    
HELIX   29  29 LEU B  244  GLN B  246  5                                   3    
HELIX   30  30 ARG B  249  HIS B  260  1                                  12    
HELIX   31  31 GLY B  272  LEU B  282  1                                  11    
HELIX   32  32 SER B  292  LEU B  302  5                                  11    
SHEET    1   A 5 THR A 220  LEU A 221  0                                        
SHEET    2   A 5 ASP A  84  GLY A  89  1  N  VAL A  87   O  THR A 220           
SHEET    3   A 5 MET A   1  ALA A   6  1  N  LEU A   4   O  ILE A  86           
SHEET    4   A 5 ALA A 264  GLU A 267  1  O  VAL A 266   N  LEU A   5           
SHEET    5   A 5 ALA A 287  ALA A 289  1  O  ARG A 288   N  GLU A 267           
SHEET    1   B 3 THR A 129  LEU A 135  0                                        
SHEET    2   B 3 GLN A 161  ARG A 167 -1  O  ILE A 162   N  VAL A 134           
SHEET    3   B 3 VAL A 152  ALA A 158 -1  N  ASN A 155   O  VAL A 163           
SHEET    1   C 5 THR B 220  LEU B 222  0                                        
SHEET    2   C 5 ASP B  84  GLY B  89  1  N  VAL B  87   O  THR B 220           
SHEET    3   C 5 MET B   1  ALA B   6  1  N  LEU B   4   O  ILE B  86           
SHEET    4   C 5 ALA B 264  GLU B 267  1  O  VAL B 266   N  LEU B   5           
SHEET    5   C 5 ALA B 287  ALA B 289  1  O  ARG B 288   N  GLU B 267           
SHEET    1   D 4 VAL B 152  ALA B 158  0                                        
SHEET    2   D 4 GLN B 161  ARG B 167 -1  O  GLN B 161   N  ALA B 158           
SHEET    3   D 4 THR B 129  VAL B 134 -1  N  VAL B 134   O  ILE B 162           
SHEET    4   D 4 VAL B 184  LEU B 187 -1  O  ARG B 185   N  ALA B 133           
SSBOND   1 CYS B   78    CYS B   78                          1555   8555  2.70  
LINK         OG  SER B -17                NI    NI B 801     1555   1555  2.39  
LINK         NE2 HIS B -15                NI    NI B 804     1555   1555  2.13  
LINK         NE2 HIS B -14                NI    NI B 805     1555   1555  2.27  
LINK         NE2 HIS B -13                NI    NI B 804     1555   1555  2.26  
LINK         NE2 HIS B -12                NI    NI B 802     1555   1555  2.32  
LINK         NE2 HIS B -11                NI    NI B 805     1555   1555  2.15  
LINK         NE2 HIS B -10                NI    NI B 802     1555   1555  2.14  
LINK         NE2 HIS B   0                NI    NI B 802     1555   1555  2.03  
LINK         OD1 ASP B  84                NI    NI B 802     1555   1555  2.20  
LINK         OD2 ASP B 216                NI    NI B 803     1555   1555  2.06  
LINK        NI    NI B 801                 NE2 HIS A -14     1555  11655  2.25  
LINK        NI    NI B 801                 NE2 HIS A -11     1555  11655  2.57  
LINK        NI    NI B 802                 OD2 ASP A 216     1555  11655  2.11  
LINK        NI    NI B 803                 NE2 HIS A -12     1555  11655  2.54  
LINK        NI    NI B 803                 NE2 HIS A   0     1555  11655  2.09  
LINK        NI    NI B 803                 OD1 ASP A  84     1555  11655  2.17  
LINK        NI    NI B 804                 NE2 HIS A -15     1555  11655  2.45  
LINK        NI    NI B 804                 NE2 HIS A -13     1555  11655  2.22  
LINK        NI    NI B 805                 OG  SER A -17     1555  11655  2.07  
CISPEP   1 PRO A  269    PRO A  270          0        -1.21                     
CISPEP   2 PRO B  269    PRO B  270          0        -6.66                     
SITE     1 AC1  3 HIS A -14  HIS A -11  SER B -17                               
SITE     1 AC2  5 ASP A 216  HIS B -10  HIS B -12  HIS B   0                    
SITE     2 AC2  5 ASP B  84                                                     
SITE     1 AC3  5 HIS A -12  HIS A -10  HIS A   0  ASP A  84                    
SITE     2 AC3  5 ASP B 216                                                     
SITE     1 AC4  4 HIS A -15  HIS A -13  HIS B -13  HIS B -15                    
SITE     1 AC5  3 SER A -17  HIS B -14  HIS B -11                               
CRYST1  180.240  180.240   95.990  90.00  90.00 120.00 P 62 2 2     24          
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      0.005548  0.003203  0.000000        0.00000                         
SCALE2      0.000000  0.006406  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010418        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system