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Database: PDB
Entry: 5HK7
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Original site: 5HK7 
HEADER    TRANSPORT PROTEIN                       14-JAN-16   5HK7              
TITLE     BACTERIAL SODIUM CHANNEL PORE, 2.95 ANGSTROM RESOLUTION               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ION TRANSPORT PROTEIN;                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 143-288;                                      
COMPND   5 SYNONYM: SODIUM CHANNEL;                                             
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ALKALILIMNICOLA EHRLICHII;                      
SOURCE   3 ORGANISM_TAXID: 351052;                                              
SOURCE   4 GENE: MLG_0322;                                                      
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BACTERIAL SODIUM CHANNEL PORE, TRANSPORT PROTEIN                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.SHAYA,F.FINDEISEN,A.ROHAIM,D.L.MINOR                                
REVDAT   1   09-MAR-16 5HK7    0                                                
JRNL        AUTH   C.ARRIGONI,A.ROHAIM,D.SHAYA,F.FINDEISEN,R.A.STEIN,S.R.NURVA, 
JRNL        AUTH 2 S.MISHRA,H.S.MCHAOURAB,D.L.MINOR                             
JRNL        TITL   UNFOLDING OF A TEMPERATURE-SENSITIVE DOMAIN CONTROLS         
JRNL        TITL 2 VOLTAGE-GATED CHANNEL ACTIVATION.                            
JRNL        REF    CELL                          V. 164   922 2016              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   26919429                                                     
JRNL        DOI    10.1016/J.CELL.2016.02.001                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0069                                      
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) : 2.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 40458                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2185                            
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) : 2.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.02                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2833                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.54                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3860                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 153                          
REMARK   3   BIN FREE R VALUE                    : 0.4250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4494                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 155                                     
REMARK   3   SOLVENT ATOMS            : 4                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 91.41                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.02000                                              
REMARK   3    B22 (A**2) : -0.28000                                             
REMARK   3    B33 (A**2) : -3.74000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.286         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.243         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.259         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.808        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4776 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6444 ; 2.173 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   702 ; 0.120 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3470 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2212 ; 8.584 ; 8.687       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2759 ;12.448 ;13.057       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2564 ;11.890 ; 9.415       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 20661 ;19.411 ;88.800       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 5HK7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217180.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-MAR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.999                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42643                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.260                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 8.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.20100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 2.96000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4LTO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 83.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEG300, 100 MM SODIUM ACETATE, PH    
REMARK 280  5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
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  1.000000  0.000000  0.000000       76.75500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       80.26000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       83.18500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       76.75500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       80.26000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       83.18500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       76.75500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       80.26000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       83.18500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       76.75500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       80.26000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       83.18500            
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: 15690 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -134.0 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     GLY A   137                                                      
REMARK 465     PRO A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     SER A   140                                                      
REMARK 465     PRO A   141                                                      
REMARK 465     SER A   142                                                      
REMARK 465     LEU A   143                                                      
REMARK 465     LEU A   144                                                      
REMARK 465     ARG A   145                                                      
REMARK 465     ALA A   146                                                      
REMARK 465     ILE A   147                                                      
REMARK 465     LYS A   287                                                      
REMARK 465     ARG A   288                                                      
REMARK 465     GLY B   137                                                      
REMARK 465     PRO B   138                                                      
REMARK 465     SER B   139                                                      
REMARK 465     SER B   140                                                      
REMARK 465     PRO B   141                                                      
REMARK 465     SER B   142                                                      
REMARK 465     LEU B   143                                                      
REMARK 465     LEU B   144                                                      
REMARK 465     ARG B   145                                                      
REMARK 465     ALA B   146                                                      
REMARK 465     ILE B   147                                                      
REMARK 465     GLY B   286                                                      
REMARK 465     LYS B   287                                                      
REMARK 465     ARG B   288                                                      
REMARK 465     GLY C   137                                                      
REMARK 465     PRO C   138                                                      
REMARK 465     SER C   139                                                      
REMARK 465     SER C   140                                                      
REMARK 465     PRO C   141                                                      
REMARK 465     SER C   142                                                      
REMARK 465     LEU C   143                                                      
REMARK 465     LEU C   144                                                      
REMARK 465     ARG C   145                                                      
REMARK 465     ALA C   146                                                      
REMARK 465     ILE C   147                                                      
REMARK 465     GLY C   286                                                      
REMARK 465     LYS C   287                                                      
REMARK 465     ARG C   288                                                      
REMARK 465     GLY D   137                                                      
REMARK 465     PRO D   138                                                      
REMARK 465     SER D   139                                                      
REMARK 465     SER D   140                                                      
REMARK 465     PRO D   141                                                      
REMARK 465     SER D   142                                                      
REMARK 465     LEU D   143                                                      
REMARK 465     LEU D   144                                                      
REMARK 465     ARG D   145                                                      
REMARK 465     ALA D   146                                                      
REMARK 465     ILE D   147                                                      
REMARK 465     GLY D   286                                                      
REMARK 465     LYS D   287                                                      
REMARK 465     ARG D   288                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 170    CG   CD   CE   NZ                                   
REMARK 470     GLU A 239    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 252    CG   CD   CE   NZ                                   
REMARK 470     GLU B 247    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 252    CG   CD   CE   NZ                                   
REMARK 470     GLN B 269    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 252    CG   CD   CE   NZ                                   
REMARK 470     ARG C 284    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 170    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ILE C   222     OG   SER C   226              1.79            
REMARK 500   O    VAL A   229     CD2  PHE A   233              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 171   CB  -  CG  -  CD2 ANGL. DEV. = -10.9 DEGREES          
REMARK 500    LEU A 270   CB  -  CG  -  CD1 ANGL. DEV. = -12.4 DEGREES          
REMARK 500    LEU A 270   CB  -  CG  -  CD2 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    MET C 167   CG  -  SD  -  CE  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    LEU D 171   CB  -  CG  -  CD1 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ARG D 205   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A 245      -67.27   -146.72                                   
REMARK 500    ILE B 238      -70.00    -46.27                                   
REMARK 500    HIS B 245      -65.81   -136.37                                   
REMARK 500    ILE C 203      -70.64   -110.63                                   
REMARK 500    HIS C 245      -54.20   -137.17                                   
REMARK 500    ALA D 151       -4.63    -54.13                                   
REMARK 500    HIS D 245      -63.09   -130.15                                   
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 ALA A  244     HIS A  245                 -145.06                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     VVA A  302                                                       
REMARK 610     VVA A  303                                                       
REMARK 610     VVA B  301                                                       
REMARK 610     VVA B  302                                                       
REMARK 610     VVA B  303                                                       
REMARK 610     VVA C  301                                                       
REMARK 610     VVA C  302                                                       
REMARK 610     VVA C  303                                                       
REMARK 610     VVA C  304                                                       
REMARK 610     VVA D  301                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue VVA A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue VVA A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue VVA B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue VVA B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue VVA B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue VVA C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue VVA C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 305                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5HJ8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HK6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HKD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HKT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HKU   RELATED DB: PDB                                   
DBREF  5HK7 A  143   288  UNP    Q0ABW0   Q0ABW0_ALKEH   143    288             
DBREF  5HK7 B  143   288  UNP    Q0ABW0   Q0ABW0_ALKEH   143    288             
DBREF  5HK7 C  143   288  UNP    Q0ABW0   Q0ABW0_ALKEH   143    288             
DBREF  5HK7 D  143   288  UNP    Q0ABW0   Q0ABW0_ALKEH   143    288             
SEQADV 5HK7 GLY A  137  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 PRO A  138  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 SER A  139  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 SER A  140  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 PRO A  141  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 SER A  142  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 GLY B  137  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 PRO B  138  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 SER B  139  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 SER B  140  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 PRO B  141  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 SER B  142  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 GLY C  137  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 PRO C  138  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 SER C  139  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 SER C  140  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 PRO C  141  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 SER C  142  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 GLY D  137  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 PRO D  138  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 SER D  139  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 SER D  140  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 PRO D  141  UNP  Q0ABW0              EXPRESSION TAG                 
SEQADV 5HK7 SER D  142  UNP  Q0ABW0              EXPRESSION TAG                 
SEQRES   1 A  152  GLY PRO SER SER PRO SER LEU LEU ARG ALA ILE PRO GLY          
SEQRES   2 A  152  ILE ALA TRP ILE ALA LEU LEU LEU LEU VAL ILE PHE TYR          
SEQRES   3 A  152  VAL PHE ALA VAL MET GLY THR LYS LEU PHE ALA GLN SER          
SEQRES   4 A  152  PHE PRO GLU TRP PHE GLY THR LEU GLY ALA SER MET TYR          
SEQRES   5 A  152  THR LEU PHE GLN VAL MET THR LEU GLU SER TRP SER MET          
SEQRES   6 A  152  GLY ILE ALA ARG PRO VAL ILE GLU ALA TYR PRO TRP ALA          
SEQRES   7 A  152  TRP ILE TYR PHE VAL SER PHE ILE LEU VAL SER SER PHE          
SEQRES   8 A  152  THR VAL LEU ASN LEU PHE ILE GLY ILE ILE ILE GLU SER          
SEQRES   9 A  152  MET GLN SER ALA HIS TRP GLU ALA GLU ASP ALA LYS ARG          
SEQRES  10 A  152  ILE GLU GLN GLU GLN ARG ALA HIS ASP GLU ARG LEU GLU          
SEQRES  11 A  152  MET LEU GLN LEU ILE ARG ASP LEU SER SER LYS VAL ASP          
SEQRES  12 A  152  ARG LEU GLU ARG ARG SER GLY LYS ARG                          
SEQRES   1 B  152  GLY PRO SER SER PRO SER LEU LEU ARG ALA ILE PRO GLY          
SEQRES   2 B  152  ILE ALA TRP ILE ALA LEU LEU LEU LEU VAL ILE PHE TYR          
SEQRES   3 B  152  VAL PHE ALA VAL MET GLY THR LYS LEU PHE ALA GLN SER          
SEQRES   4 B  152  PHE PRO GLU TRP PHE GLY THR LEU GLY ALA SER MET TYR          
SEQRES   5 B  152  THR LEU PHE GLN VAL MET THR LEU GLU SER TRP SER MET          
SEQRES   6 B  152  GLY ILE ALA ARG PRO VAL ILE GLU ALA TYR PRO TRP ALA          
SEQRES   7 B  152  TRP ILE TYR PHE VAL SER PHE ILE LEU VAL SER SER PHE          
SEQRES   8 B  152  THR VAL LEU ASN LEU PHE ILE GLY ILE ILE ILE GLU SER          
SEQRES   9 B  152  MET GLN SER ALA HIS TRP GLU ALA GLU ASP ALA LYS ARG          
SEQRES  10 B  152  ILE GLU GLN GLU GLN ARG ALA HIS ASP GLU ARG LEU GLU          
SEQRES  11 B  152  MET LEU GLN LEU ILE ARG ASP LEU SER SER LYS VAL ASP          
SEQRES  12 B  152  ARG LEU GLU ARG ARG SER GLY LYS ARG                          
SEQRES   1 C  152  GLY PRO SER SER PRO SER LEU LEU ARG ALA ILE PRO GLY          
SEQRES   2 C  152  ILE ALA TRP ILE ALA LEU LEU LEU LEU VAL ILE PHE TYR          
SEQRES   3 C  152  VAL PHE ALA VAL MET GLY THR LYS LEU PHE ALA GLN SER          
SEQRES   4 C  152  PHE PRO GLU TRP PHE GLY THR LEU GLY ALA SER MET TYR          
SEQRES   5 C  152  THR LEU PHE GLN VAL MET THR LEU GLU SER TRP SER MET          
SEQRES   6 C  152  GLY ILE ALA ARG PRO VAL ILE GLU ALA TYR PRO TRP ALA          
SEQRES   7 C  152  TRP ILE TYR PHE VAL SER PHE ILE LEU VAL SER SER PHE          
SEQRES   8 C  152  THR VAL LEU ASN LEU PHE ILE GLY ILE ILE ILE GLU SER          
SEQRES   9 C  152  MET GLN SER ALA HIS TRP GLU ALA GLU ASP ALA LYS ARG          
SEQRES  10 C  152  ILE GLU GLN GLU GLN ARG ALA HIS ASP GLU ARG LEU GLU          
SEQRES  11 C  152  MET LEU GLN LEU ILE ARG ASP LEU SER SER LYS VAL ASP          
SEQRES  12 C  152  ARG LEU GLU ARG ARG SER GLY LYS ARG                          
SEQRES   1 D  152  GLY PRO SER SER PRO SER LEU LEU ARG ALA ILE PRO GLY          
SEQRES   2 D  152  ILE ALA TRP ILE ALA LEU LEU LEU LEU VAL ILE PHE TYR          
SEQRES   3 D  152  VAL PHE ALA VAL MET GLY THR LYS LEU PHE ALA GLN SER          
SEQRES   4 D  152  PHE PRO GLU TRP PHE GLY THR LEU GLY ALA SER MET TYR          
SEQRES   5 D  152  THR LEU PHE GLN VAL MET THR LEU GLU SER TRP SER MET          
SEQRES   6 D  152  GLY ILE ALA ARG PRO VAL ILE GLU ALA TYR PRO TRP ALA          
SEQRES   7 D  152  TRP ILE TYR PHE VAL SER PHE ILE LEU VAL SER SER PHE          
SEQRES   8 D  152  THR VAL LEU ASN LEU PHE ILE GLY ILE ILE ILE GLU SER          
SEQRES   9 D  152  MET GLN SER ALA HIS TRP GLU ALA GLU ASP ALA LYS ARG          
SEQRES  10 D  152  ILE GLU GLN GLU GLN ARG ALA HIS ASP GLU ARG LEU GLU          
SEQRES  11 D  152  MET LEU GLN LEU ILE ARG ASP LEU SER SER LYS VAL ASP          
SEQRES  12 D  152  ARG LEU GLU ARG ARG SER GLY LYS ARG                          
HET     CL  A 301       1                                                       
HET    VVA  A 302      21                                                       
HET    VVA  A 303      13                                                       
HET     CL  A 304       1                                                       
HET    VVA  B 301      21                                                       
HET    VVA  B 302      21                                                       
HET    VVA  B 303      17                                                       
HET     NA  B 304       1                                                       
HET    VVA  C 301      21                                                       
HET    VVA  C 302      10                                                       
HET    VVA  C 303       6                                                       
HET    VVA  C 304      11                                                       
HET     NA  C 305       1                                                       
HET    VVA  D 301      10                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     VVA 2-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}ETHYL             
HETNAM   2 VVA  HEPTADECANOATE                                                  
HETNAM      NA SODIUM ION                                                       
FORMUL   5   CL    2(CL 1-)                                                     
FORMUL   6  VVA    10(C21 H44 N O6 P)                                           
FORMUL  12   NA    2(NA 1+)                                                     
FORMUL  19  HOH   *4(H2 O)                                                      
HELIX    1 AA1 GLY A  149  ALA A  173  1                                  25    
HELIX    2 AA2 PHE A  176  GLY A  181  1                                   6    
HELIX    3 AA3 THR A  182  THR A  195  1                                  14    
HELIX    4 AA4 ILE A  203  TYR A  211  1                                   9    
HELIX    5 AA5 ALA A  214  HIS A  245  1                                  32    
HELIX    6 AA6 HIS A  245  SER A  285  1                                  41    
HELIX    7 AA7 ILE B  150  ALA B  173  1                                  24    
HELIX    8 AA8 PHE B  176  GLY B  181  1                                   6    
HELIX    9 AA9 THR B  182  THR B  195  1                                  14    
HELIX   10 AB1 PRO B  206  TYR B  211  1                                   6    
HELIX   11 AB2 ALA B  214  HIS B  245  1                                  32    
HELIX   12 AB3 HIS B  245  SER B  285  1                                  41    
HELIX   13 AB4 ILE C  150  ALA C  173  1                                  24    
HELIX   14 AB5 PHE C  176  GLY C  181  1                                   6    
HELIX   15 AB6 THR C  182  THR C  195  1                                  14    
HELIX   16 AB7 ILE C  203  TYR C  211  1                                   9    
HELIX   17 AB8 ALA C  214  HIS C  245  1                                  32    
HELIX   18 AB9 HIS C  245  SER C  285  1                                  41    
HELIX   19 AC1 ILE D  150  ALA D  173  1                                  24    
HELIX   20 AC2 PHE D  176  GLY D  181  1                                   6    
HELIX   21 AC3 THR D  182  THR D  195  1                                  14    
HELIX   22 AC4 ILE D  203  GLU D  209  1                                   7    
HELIX   23 AC5 TYR D  211  TRP D  213  5                                   3    
HELIX   24 AC6 ALA D  214  HIS D  245  1                                  32    
HELIX   25 AC7 HIS D  245  VAL D  278  1                                  34    
LINK        NA    NA B 304                 O   HOH D 401     1555   1555  2.52  
SITE     1 AC1  4 ARG A 264  ARG B 264  ARG C 264  ARG D 264                    
SITE     1 AC2  3 TRP A 215  HOH A 401  GLY D 184                               
SITE     1 AC3  2 MET A 194  SER A 226                                          
SITE     1 AC4  4 TRP A 246  TRP B 246  TRP C 246  TRP D 246                    
SITE     1 AC5  6 PHE A 161  GLU A 178  GLY A 184  TYR A 188                    
SITE     2 AC5  6 ILE B 208  TRP B 215                                          
SITE     1 AC6  7 GLU B 178  GLY B 184  MET B 187  TYR B 188                    
SITE     2 AC6  7 PHE B 191  PRO C 212  TRP C 215                               
SITE     1 AC7  1 MET B 194                                                     
SITE     1 AC8  3 GLU B 197  SER B 198  HOH D 401                               
SITE     1 AC9  8 PHE C 161  GLU C 178  GLY C 184  MET C 187                    
SITE     2 AC9  8 TYR C 188  VVA C 302  ILE D 208  TRP D 215                    
SITE     1 AD1  2 MET C 187  VVA C 301                                          
SITE     1 AD2  1 LEU C 196                                                     
CRYST1  153.510  160.520  166.370  90.00  90.00  90.00 I 2 2 2      32          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006514  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006230  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006011        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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