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Database: PDB
Entry: 3CDK
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Original site: 3CDK 
HEADER    TRANSFERASE                             27-FEB-08   3CDK              
TITLE     CRYSTAL STRUCTURE OF THE CO-EXPRESSED SUCCINYL-COA                    
TITLE    2 TRANSFERASE A AND B COMPLEX FROM BACILLUS SUBTILIS                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUCCINYL-COA:3-KETOACID-COENZYME A TRANSFERASE             
COMPND   3 SUBUNIT A;                                                           
COMPND   4 CHAIN: A, C;                                                         
COMPND   5 SYNONYM: SUCCINYL COA:3-OXOACID COA-TRANSFERASE, OXCT A;             
COMPND   6 EC: 2.8.3.5;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SUCCINYL-COA:3-KETOACID-COENZYME A TRANSFERASE             
COMPND  10 SUBUNIT B;                                                           
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 SYNONYM: SUCCINYL COA:3-OXOACID COA-TRANSFERASE, OXCT B;             
COMPND  13 EC: 2.8.3.5;                                                         
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: SCOA, YXJD, BSU38990, N15K;                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG17;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  13 ORGANISM_TAXID: 1423;                                                
SOURCE  14 STRAIN: 168;                                                         
SOURCE  15 GENE: SCOB, YXJE, BSU38980, N15L;                                    
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PMCSG21                                   
KEYWDS    CO-EXPRESSED COMPLEX, HETERO-TETRAMER, STRUCTURAL GENOMICS,           
KEYWDS   2 PSI-2, PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR              
KEYWDS   3 STRUCTURAL GENOMICS, MCSG, TRANSFERASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KIM,M.ZHOU,L.STOLS,W.ESCHENFELDT,M.DONNELLY,A.JOACHIMIAK,           
AUTHOR   2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)                        
REVDAT   2   24-FEB-09 3CDK    1       VERSN                                    
REVDAT   1   18-MAR-08 3CDK    0                                                
JRNL        AUTH   Y.KIM,M.ZHOU,L.STOLS,W.ESCHENFELDT,M.DONNELLY,               
JRNL        AUTH 2 A.JOACHIMIAK                                                 
JRNL        TITL   CRYSTAL STRUCTURE OF THE CO-EXPRESSED SUCCINYL-COA           
JRNL        TITL 2 TRANSFERASE A AND B COMPLEX FROM BACILLUS SUBTILIS.          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.59 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                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 28069                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1417                            
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) : 2.59                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1827                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.21                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 108                          
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6605                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 115                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 47.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.74                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.03000                                             
REMARK   3    B22 (A**2) : 2.07000                                              
REMARK   3    B33 (A**2) : 0.66000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.53000                                             
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): 0.336         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.258         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.492        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6696 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9028 ; 1.599 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   874 ; 6.976 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   275 ;40.356 ;25.164       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1224 ;22.442 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    35 ;19.168 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1042 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4929 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3433 ; 0.246 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4433 ; 0.319 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   310 ; 0.166 ; 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):    57 ; 0.306 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.145 ; 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):  4298 ; 2.598 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6888 ; 4.414 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2398 ; 3.260 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2140 ; 5.569 ; 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  : 4                                          
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     4        A   232                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.7400  13.0520 -18.2270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0319 T22:   0.0521                                     
REMARK   3      T33:  -0.0207 T12:  -0.0052                                     
REMARK   3      T13:   0.0139 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0627 L22:   0.0002                                     
REMARK   3      L33:   0.0242 L12:  -0.0037                                     
REMARK   3      L13:  -0.0389 L23:   0.0023                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0167 S12:  -0.0103 S13:   0.0181                       
REMARK   3      S21:   0.0243 S22:   0.0099 S23:  -0.0049                       
REMARK   3      S31:  -0.0106 S32:  -0.0147 S33:   0.0068                       
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   213                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.6930 -14.9430 -19.1630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0227 T22:   0.0649                                     
REMARK   3      T33:  -0.0217 T12:   0.0017                                     
REMARK   3      T13:   0.0118 T23:   0.0000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0753 L22:   0.1037                                     
REMARK   3      L33:   0.0629 L12:   0.0523                                     
REMARK   3      L13:  -0.0083 L23:  -0.0704                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0017 S12:  -0.0151 S13:  -0.0195                       
REMARK   3      S21:  -0.0160 S22:   0.0034 S23:   0.0062                       
REMARK   3      S31:   0.0161 S32:  -0.0048 S33:  -0.0051                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     3        C   231                          
REMARK   3    ORIGIN FOR THE GROUP (A): -46.0900   6.6390 -31.6650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0356 T22:   0.0518                                     
REMARK   3      T33:  -0.0328 T12:  -0.0026                                     
REMARK   3      T13:   0.0130 T23:   0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1402 L22:   0.0086                                     
REMARK   3      L33:   0.0514 L12:   0.0158                                     
REMARK   3      L13:  -0.0120 L23:  -0.0199                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0161 S12:   0.0183 S13:  -0.0010                       
REMARK   3      S21:   0.0355 S22:   0.0040 S23:   0.0052                       
REMARK   3      S31:   0.0174 S32:   0.0037 S33:   0.0121                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D   210                          
REMARK   3    ORIGIN FOR THE GROUP (A): -46.1640  32.7550 -23.6240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0116 T22:   0.0729                                     
REMARK   3      T33:   0.0334 T12:   0.0016                                     
REMARK   3      T13:   0.0005 T23:   0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2882 L22:   0.0000                                     
REMARK   3      L33:   0.0802 L12:  -0.0021                                     
REMARK   3      L13:  -0.0973 L23:   0.0005                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0113 S12:   0.0180 S13:   0.1416                       
REMARK   3      S21:   0.0151 S22:   0.0128 S23:  -0.0284                       
REMARK   3      S31:  -0.0547 S32:   0.0142 S33:  -0.0014                       
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: NATIVE DATA SET HAS BEEN USED FOR         
REMARK   3  STRUCTURE DETERMINATION.                                            
REMARK   4                                                                      
REMARK   4 3CDK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-FEB-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB046644.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : SI(111) CHANNEL                    
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28084                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.590                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.14700                            
REMARK 200  R SYM                      (I) : 0.14700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.54300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP, COOT                                          
REMARK 200 STARTING MODEL: PDB ENTRY 1M3E                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE DIHYDRATE        
REMARK 280  PH 5.6, 20% ISOPROPANOL, 20% PEG 4000, VAPOR DIFFUSION,             
REMARK 280  SITTING DROP, TEMPERATURE 289K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12510 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     SER A     0                                                      
REMARK 465     ASN A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     MET A     3                                                      
REMARK 465     ALA A   233                                                      
REMARK 465     SER A   234                                                      
REMARK 465     GLY A   235                                                      
REMARK 465     LYS A   236                                                      
REMARK 465     GLY A   237                                                      
REMARK 465     GLU A   238                                                      
REMARK 465     ALA A   239                                                      
REMARK 465     LYS A   240                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MET B   122                                                      
REMARK 465     LEU B   214                                                      
REMARK 465     ASN B   215                                                      
REMARK 465     SER B   216                                                      
REMARK 465     SER C     0                                                      
REMARK 465     ASN C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     GLN C   232                                                      
REMARK 465     ALA C   233                                                      
REMARK 465     SER C   234                                                      
REMARK 465     GLY C   235                                                      
REMARK 465     LYS C   236                                                      
REMARK 465     GLY C   237                                                      
REMARK 465     GLU C   238                                                      
REMARK 465     ALA C   239                                                      
REMARK 465     LYS C   240                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     ASN D    -1                                                      
REMARK 465     ALA D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     LYS D   121                                                      
REMARK 465     LYS D   148                                                      
REMARK 465     HIS D   149                                                      
REMARK 465     GLY D   150                                                      
REMARK 465     GLU D   151                                                      
REMARK 465     GLN D   191                                                      
REMARK 465     ASP D   192                                                      
REMARK 465     GLY D   193                                                      
REMARK 465     VAL D   194                                                      
REMARK 465     GLN D   211                                                      
REMARK 465     SER D   212                                                      
REMARK 465     VAL D   213                                                      
REMARK 465     LEU D   214                                                      
REMARK 465     ASN D   215                                                      
REMARK 465     SER D   216                                                      
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   OE2  GLU D    15     NH1  ARG D   170              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU C 222   CD    GLU C 222   OE2     0.067                       
REMARK 500    LEU D 190   C     LEU D 190   O       0.150                       
REMARK 500    GLU D 198   CD    GLU D 198   OE2     0.260                       
REMARK 500    GLU D 201   CG    GLU D 201   CD      0.121                       
REMARK 500    GLU D 201   CD    GLU D 201   OE1     0.078                       
REMARK 500    GLU D 201   CD    GLU D 201   OE2     0.080                       
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    LYS A  70       33.33     71.13                                   
REMARK 500    LYS A 171     -132.62     48.61                                   
REMARK 500    ASN A 175     -112.54     35.57                                   
REMARK 500    ILE A 205      124.27    -38.48                                   
REMARK 500    GLN B  14       -7.90    -57.04                                   
REMARK 500    GLU B  35       32.67    -93.36                                   
REMARK 500    ASN B 115       21.00   -147.17                                   
REMARK 500    SER C  53      147.72   -170.03                                   
REMARK 500    LYS C  70       35.02     73.96                                   
REMARK 500    LYS C 171     -132.51     50.22                                   
REMARK 500    ASN C 175     -110.08     31.66                                   
REMARK 500    LYS D  71        3.76     80.62                                   
REMARK 500    ASN D 115       13.82   -142.90                                   
REMARK 500    LEU D 175      -70.96    -79.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC152   RELATED DB: TARGETDB                            
DBREF  3CDK A    3   240  UNP    P42315   SCOA_BACSU       1    238             
DBREF  3CDK B    1   216  UNP    P42316   SCOB_BACSU       1    216             
DBREF  3CDK C    3   240  UNP    P42315   SCOA_BACSU       1    238             
DBREF  3CDK D    1   216  UNP    P42316   SCOB_BACSU       1    216             
SEQADV 3CDK SER A    0  UNP  P42315              EXPRESSION TAG                 
SEQADV 3CDK ASN A    1  UNP  P42315              EXPRESSION TAG                 
SEQADV 3CDK ALA A    2  UNP  P42315              EXPRESSION TAG                 
SEQADV 3CDK SER B   -2  UNP  P42316              EXPRESSION TAG                 
SEQADV 3CDK ASN B   -1  UNP  P42316              EXPRESSION TAG                 
SEQADV 3CDK ALA B    0  UNP  P42316              EXPRESSION TAG                 
SEQADV 3CDK SER C    0  UNP  P42315              EXPRESSION TAG                 
SEQADV 3CDK ASN C    1  UNP  P42315              EXPRESSION TAG                 
SEQADV 3CDK ALA C    2  UNP  P42315              EXPRESSION TAG                 
SEQADV 3CDK SER D   -2  UNP  P42316              EXPRESSION TAG                 
SEQADV 3CDK ASN D   -1  UNP  P42316              EXPRESSION TAG                 
SEQADV 3CDK ALA D    0  UNP  P42316              EXPRESSION TAG                 
SEQRES   1 A  241  SER ASN ALA MET GLY LYS VAL LEU SER SER SER LYS GLU          
SEQRES   2 A  241  ALA ALA LYS LEU ILE HIS ASP GLY ASP THR LEU ILE ALA          
SEQRES   3 A  241  GLY GLY PHE GLY LEU CYS GLY ILE PRO GLU GLN LEU ILE          
SEQRES   4 A  241  LEU SER ILE ARG ASP GLN GLY VAL LYS ASP LEU THR VAL          
SEQRES   5 A  241  VAL SER ASN ASN CYS GLY VAL ASP ASP TRP GLY LEU GLY          
SEQRES   6 A  241  LEU LEU LEU ALA ASN LYS GLN ILE LYS LYS MET ILE ALA          
SEQRES   7 A  241  SER TYR VAL GLY GLU ASN LYS ILE PHE GLU ARG GLN PHE          
SEQRES   8 A  241  LEU SER GLY GLU LEU GLU VAL GLU LEU VAL PRO GLN GLY          
SEQRES   9 A  241  THR LEU ALA GLU ARG ILE ARG ALA GLY GLY ALA GLY ILE          
SEQRES  10 A  241  PRO GLY PHE TYR THR ALA THR GLY VAL GLY THR SER ILE          
SEQRES  11 A  241  ALA GLU GLY LYS GLU HIS LYS THR PHE GLY GLY ARG THR          
SEQRES  12 A  241  TYR VAL LEU GLU ARG GLY ILE THR GLY ASP VAL ALA ILE          
SEQRES  13 A  241  VAL LYS ALA TRP LYS ALA ASP THR MET GLY ASN LEU ILE          
SEQRES  14 A  241  PHE ARG LYS THR ALA ARG ASN PHE ASN PRO ILE ALA ALA          
SEQRES  15 A  241  MET ALA GLY LYS ILE THR ILE ALA GLU ALA GLU GLU ILE          
SEQRES  16 A  241  VAL GLU ALA GLY GLU LEU ASP PRO ASP HIS ILE HIS THR          
SEQRES  17 A  241  PRO GLY ILE TYR VAL GLN HIS VAL VAL LEU GLY ALA SER          
SEQRES  18 A  241  GLN GLU LYS ARG ILE GLU LYS ARG THR VAL GLN GLN ALA          
SEQRES  19 A  241  SER GLY LYS GLY GLU ALA LYS                                  
SEQRES   1 B  219  SER ASN ALA MET LYS GLU ALA ARG LYS ARG MET VAL LYS          
SEQRES   2 B  219  ARG ALA VAL GLN GLU ILE LYS ASP GLY MET ASN VAL ASN          
SEQRES   3 B  219  LEU GLY ILE GLY MET PRO THR LEU VAL ALA ASN GLU ILE          
SEQRES   4 B  219  PRO ASP GLY VAL HIS VAL MET LEU GLN SER GLU ASN GLY          
SEQRES   5 B  219  LEU LEU GLY ILE GLY PRO TYR PRO LEU GLU GLY THR GLU          
SEQRES   6 B  219  ASP ALA ASP LEU ILE ASN ALA GLY LYS GLU THR ILE THR          
SEQRES   7 B  219  GLU VAL THR GLY ALA SER TYR PHE ASP SER ALA GLU SER          
SEQRES   8 B  219  PHE ALA MET ILE ARG GLY GLY HIS ILE ASP LEU ALA ILE          
SEQRES   9 B  219  LEU GLY GLY MET GLU VAL SER GLU GLN GLY ASP LEU ALA          
SEQRES  10 B  219  ASN TRP MET ILE PRO GLY LYS MET VAL LYS GLY MET GLY          
SEQRES  11 B  219  GLY ALA MET ASP LEU VAL ASN GLY ALA LYS ARG ILE VAL          
SEQRES  12 B  219  VAL ILE MET GLU HIS VAL ASN LYS HIS GLY GLU SER LYS          
SEQRES  13 B  219  VAL LYS LYS THR CYS SER LEU PRO LEU THR GLY GLN LYS          
SEQRES  14 B  219  VAL VAL HIS ARG LEU ILE THR ASP LEU ALA VAL PHE ASP          
SEQRES  15 B  219  PHE VAL ASN GLY ARG MET THR LEU THR GLU LEU GLN ASP          
SEQRES  16 B  219  GLY VAL THR ILE GLU GLU VAL TYR GLU LYS THR GLU ALA          
SEQRES  17 B  219  ASP PHE ALA VAL SER GLN SER VAL LEU ASN SER                  
SEQRES   1 C  241  SER ASN ALA MET GLY LYS VAL LEU SER SER SER LYS GLU          
SEQRES   2 C  241  ALA ALA LYS LEU ILE HIS ASP GLY ASP THR LEU ILE ALA          
SEQRES   3 C  241  GLY GLY PHE GLY LEU CYS GLY ILE PRO GLU GLN LEU ILE          
SEQRES   4 C  241  LEU SER ILE ARG ASP GLN GLY VAL LYS ASP LEU THR VAL          
SEQRES   5 C  241  VAL SER ASN ASN CYS GLY VAL ASP ASP TRP GLY LEU GLY          
SEQRES   6 C  241  LEU LEU LEU ALA ASN LYS GLN ILE LYS LYS MET ILE ALA          
SEQRES   7 C  241  SER TYR VAL GLY GLU ASN LYS ILE PHE GLU ARG GLN PHE          
SEQRES   8 C  241  LEU SER GLY GLU LEU GLU VAL GLU LEU VAL PRO GLN GLY          
SEQRES   9 C  241  THR LEU ALA GLU ARG ILE ARG ALA GLY GLY ALA GLY ILE          
SEQRES  10 C  241  PRO GLY PHE TYR THR ALA THR GLY VAL GLY THR SER ILE          
SEQRES  11 C  241  ALA GLU GLY LYS GLU HIS LYS THR PHE GLY GLY ARG THR          
SEQRES  12 C  241  TYR VAL LEU GLU ARG GLY ILE THR GLY ASP VAL ALA ILE          
SEQRES  13 C  241  VAL LYS ALA TRP LYS ALA ASP THR MET GLY ASN LEU ILE          
SEQRES  14 C  241  PHE ARG LYS THR ALA ARG ASN PHE ASN PRO ILE ALA ALA          
SEQRES  15 C  241  MET ALA GLY LYS ILE THR ILE ALA GLU ALA GLU GLU ILE          
SEQRES  16 C  241  VAL GLU ALA GLY GLU LEU ASP PRO ASP HIS ILE HIS THR          
SEQRES  17 C  241  PRO GLY ILE TYR VAL GLN HIS VAL VAL LEU GLY ALA SER          
SEQRES  18 C  241  GLN GLU LYS ARG ILE GLU LYS ARG THR VAL GLN GLN ALA          
SEQRES  19 C  241  SER GLY LYS GLY GLU ALA LYS                                  
SEQRES   1 D  219  SER ASN ALA MET LYS GLU ALA ARG LYS ARG MET VAL LYS          
SEQRES   2 D  219  ARG ALA VAL GLN GLU ILE LYS ASP GLY MET ASN VAL ASN          
SEQRES   3 D  219  LEU GLY ILE GLY MET PRO THR LEU VAL ALA ASN GLU ILE          
SEQRES   4 D  219  PRO ASP GLY VAL HIS VAL MET LEU GLN SER GLU ASN GLY          
SEQRES   5 D  219  LEU LEU GLY ILE GLY PRO TYR PRO LEU GLU GLY THR GLU          
SEQRES   6 D  219  ASP ALA ASP LEU ILE ASN ALA GLY LYS GLU THR ILE THR          
SEQRES   7 D  219  GLU VAL THR GLY ALA SER TYR PHE ASP SER ALA GLU SER          
SEQRES   8 D  219  PHE ALA MET ILE ARG GLY GLY HIS ILE ASP LEU ALA ILE          
SEQRES   9 D  219  LEU GLY GLY MET GLU VAL SER GLU GLN GLY ASP LEU ALA          
SEQRES  10 D  219  ASN TRP MET ILE PRO GLY LYS MET VAL LYS GLY MET GLY          
SEQRES  11 D  219  GLY ALA MET ASP LEU VAL ASN GLY ALA LYS ARG ILE VAL          
SEQRES  12 D  219  VAL ILE MET GLU HIS VAL ASN LYS HIS GLY GLU SER LYS          
SEQRES  13 D  219  VAL LYS LYS THR CYS SER LEU PRO LEU THR GLY GLN LYS          
SEQRES  14 D  219  VAL VAL HIS ARG LEU ILE THR ASP LEU ALA VAL PHE ASP          
SEQRES  15 D  219  PHE VAL ASN GLY ARG MET THR LEU THR GLU LEU GLN ASP          
SEQRES  16 D  219  GLY VAL THR ILE GLU GLU VAL TYR GLU LYS THR GLU ALA          
SEQRES  17 D  219  ASP PHE ALA VAL SER GLN SER VAL LEU ASN SER                  
FORMUL   5  HOH   *115(H2 O)                                                    
HELIX    1   1 SER A    9  LYS A   15  1                                   7    
HELIX    2   2 PRO A   34  GLY A   45  1                                  12    
HELIX    3   3 LEU A   63  ASN A   69  1                                   7    
HELIX    4   4 ASN A   83  LEU A   91  1                                   9    
HELIX    5   5 PRO A  101  GLY A  115  1                                  15    
HELIX    6   6 THR A  127  GLU A  131  5                                   5    
HELIX    7   7 ARG A  170  ARG A  174  5                                   5    
HELIX    8   8 PHE A  176  ALA A  183  1                                   8    
HELIX    9   9 PRO A  208  VAL A  212  5                                   5    
HELIX   10  10 MET B    1  GLN B   14  1                                  14    
HELIX   11  11 GLY B   27  ASN B   34  5                                   8    
HELIX   12  12 ASP B   84  GLY B   94  1                                  11    
HELIX   13  13 GLY B  128  ALA B  136  1                                   9    
HELIX   14  14 THR B  195  LYS B  202  1                                   8    
HELIX   15  15 SER C    9  LYS C   15  1                                   7    
HELIX   16  16 PRO C   34  GLY C   45  1                                  12    
HELIX   17  17 LEU C   63  ASN C   69  1                                   7    
HELIX   18  18 ASN C   83  SER C   92  1                                  10    
HELIX   19  19 PRO C  101  GLY C  115  1                                  15    
HELIX   20  20 THR C  127  GLU C  131  5                                   5    
HELIX   21  21 ARG C  170  ARG C  174  5                                   5    
HELIX   22  22 PHE C  176  ALA C  183  1                                   8    
HELIX   23  23 PRO C  208  VAL C  212  5                                   5    
HELIX   24  24 LYS D    2  GLN D   14  1                                  13    
HELIX   25  25 GLY D   27  ILE D   36  5                                  10    
HELIX   26  26 ASP D   84  GLY D   94  1                                  11    
HELIX   27  27 GLY D  128  ALA D  136  1                                   9    
HELIX   28  28 GLU D  197  THR D  203  1                                   7    
SHEET    1   A 6 GLU A  96  LEU A  99  0                                        
SHEET    2   A 6 ILE A  72  ALA A  77  1  N  MET A  75   O  GLU A  98           
SHEET    3   A 6 LEU A  49  SER A  53  1  N  VAL A  51   O  ILE A  76           
SHEET    4   A 6 THR A  22  ALA A  25  1  N  LEU A  23   O  VAL A  52           
SHEET    5   A 6 GLY A 151  ASP A 162  1  O  ILE A 155   N  ILE A  24           
SHEET    6   A 6 LEU A 167  ILE A 168 -1  O  ILE A 168   N  LYS A 160           
SHEET    1   B 7 GLU A  96  LEU A  99  0                                        
SHEET    2   B 7 ILE A  72  ALA A  77  1  N  MET A  75   O  GLU A  98           
SHEET    3   B 7 LEU A  49  SER A  53  1  N  VAL A  51   O  ILE A  76           
SHEET    4   B 7 THR A  22  ALA A  25  1  N  LEU A  23   O  VAL A  52           
SHEET    5   B 7 GLY A 151  ASP A 162  1  O  ILE A 155   N  ILE A  24           
SHEET    6   B 7 GLY A 184  VAL A 195  1  O  GLU A 190   N  ALA A 158           
SHEET    7   B 7 HIS A 214  LEU A 217  1  O  VAL A 216   N  ALA A 189           
SHEET    1   C 3 GLY A 118  THR A 121  0                                        
SHEET    2   C 3 ARG A 141  ARG A 147 -1  O  VAL A 144   N  THR A 121           
SHEET    3   C 3 HIS A 135  PHE A 138 -1  N  LYS A 136   O  TYR A 143           
SHEET    1   D10 THR B  75  TYR B  82  0                                        
SHEET    2   D10 LEU B  50  GLY B  54 -1  N  GLY B  54   O  THR B  75           
SHEET    3   D10 MET B  43  SER B  46 -1  N  SER B  46   O  LEU B  50           
SHEET    4   D10 ASN B  21  LEU B  24  1  N  VAL B  22   O  GLN B  45           
SHEET    5   D10 LEU B  99  LEU B 102  1  O  LEU B  99   N  ASN B  23           
SHEET    6   D10 ARG B 138  ILE B 142  1  O  VAL B 140   N  LEU B 102           
SHEET    7   D10 ARG B 170  ILE B 172  1  O  ILE B 172   N  VAL B 141           
SHEET    8   D10 ALA B 176  VAL B 181 -1  O  PHE B 178   N  LEU B 171           
SHEET    9   D10 ARG B 184  LEU B 190 -1  O  THR B 188   N  VAL B 177           
SHEET   10   D10 ALA B 208  VAL B 209  1  O  ALA B 208   N  LEU B 187           
SHEET    1   E 3 LEU B 113  ALA B 114  0                                        
SHEET    2   E 3 GLU B 106  SER B 108 -1  N  GLU B 106   O  ALA B 114           
SHEET    3   E 3 VAL B 154  LYS B 155  1  O  LYS B 155   N  VAL B 107           
SHEET    1   F 6 GLU C  96  LEU C  99  0                                        
SHEET    2   F 6 ILE C  72  ALA C  77  1  N  MET C  75   O  GLU C  98           
SHEET    3   F 6 LEU C  49  VAL C  52  1  N  VAL C  51   O  ILE C  76           
SHEET    4   F 6 THR C  22  ALA C  25  1  N  LEU C  23   O  VAL C  52           
SHEET    5   F 6 GLY C 151  ASP C 162  1  O  VAL C 153   N  ILE C  24           
SHEET    6   F 6 LEU C 167  ILE C 168 -1  O  ILE C 168   N  LYS C 160           
SHEET    1   G 7 GLU C  96  LEU C  99  0                                        
SHEET    2   G 7 ILE C  72  ALA C  77  1  N  MET C  75   O  GLU C  98           
SHEET    3   G 7 LEU C  49  VAL C  52  1  N  VAL C  51   O  ILE C  76           
SHEET    4   G 7 THR C  22  ALA C  25  1  N  LEU C  23   O  VAL C  52           
SHEET    5   G 7 GLY C 151  ASP C 162  1  O  VAL C 153   N  ILE C  24           
SHEET    6   G 7 GLY C 184  VAL C 195  1  O  GLU C 190   N  ALA C 158           
SHEET    7   G 7 HIS C 214  LEU C 217  1  O  VAL C 216   N  ALA C 191           
SHEET    1   H 3 GLY C 118  THR C 121  0                                        
SHEET    2   H 3 ARG C 141  ARG C 147 -1  O  GLU C 146   N  PHE C 119           
SHEET    3   H 3 HIS C 135  PHE C 138 -1  N  LYS C 136   O  TYR C 143           
SHEET    1   I 9 THR D  75  TYR D  82  0                                        
SHEET    2   I 9 LEU D  50  GLY D  54 -1  N  GLY D  54   O  THR D  75           
SHEET    3   I 9 MET D  43  SER D  46 -1  N  SER D  46   O  LEU D  50           
SHEET    4   I 9 ASN D  21  LEU D  24  1  N  VAL D  22   O  GLN D  45           
SHEET    5   I 9 LEU D  99  LEU D 102  1  O  LEU D  99   N  ASN D  23           
SHEET    6   I 9 ILE D 139  ILE D 142  1  O  VAL D 140   N  ALA D 100           
SHEET    7   I 9 ARG D 170  ILE D 172  1  O  ILE D 172   N  VAL D 141           
SHEET    8   I 9 VAL D 177  VAL D 181 -1  O  PHE D 178   N  LEU D 171           
SHEET    9   I 9 ARG D 184  GLU D 189 -1  O  THR D 186   N  ASP D 179           
SHEET    1   J 2 GLU D 106  VAL D 107  0                                        
SHEET    2   J 2 LEU D 113  ALA D 114 -1  O  ALA D 114   N  GLU D 106           
CRYST1   69.337   70.404   97.996  90.00 106.31  90.00 P 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014422  0.000000  0.004220        0.00000                         
SCALE2      0.000000  0.014204  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010632        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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