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Database: PDB
Entry: 2HDN
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Original site: 2HDN 
HEADER    TRANSLATION                             20-JUN-06   2HDN              
TITLE     TRYPSIN-MODIFIED ELONGATION FACTOR TU IN COMPLEX WITH                 
TITLE    2 TETRACYCLINE AT 2.8 ANGSTROM RESOLUTION                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR EF-TU;                                   
COMPND   3 CHAIN: A, C, E, G, I, K;                                             
COMPND   4 FRAGMENT: EF-TU FRAGMENT, RESIDUES 8-44;                             
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: ELONGATION FACTOR EF-TU;                                   
COMPND   7 CHAIN: B, D, F, H, J, L;                                             
COMPND   8 FRAGMENT: EF-TU FRAGMENT, RESIDUES 59-393                            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 STRAIN: TUFA;                                                        
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   7 ORGANISM_TAXID: 562;                                                 
SOURCE   8 STRAIN: TUFA                                                         
KEYWDS    TRYPSIN-MODIFIED EF-TU, GTPASE CENTER, COMPLEX WITH                   
KEYWDS   2 TETRACYCLINE, TRANSLATION                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.MUI,S.E.HEFFRON,A.AORORA,K.ABEL,E.BERGMANN,F.JURNAK                 
REVDAT   2   24-FEB-09 2HDN    1       VERSN                                    
REVDAT   1   31-OCT-06 2HDN    0                                                
JRNL        AUTH   S.E.HEFFRON,S.MUI,A.AORORA,K.ABEL,E.BERGMANN,                
JRNL        AUTH 2 F.JURNAK                                                     
JRNL        TITL   MOLECULAR COMPLEMENTARITY BETWEEN TETRACYCLINE AND           
JRNL        TITL 2 THE GTPASE ACTIVE SITE OF ELONGATION FACTOR TU.              
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  62  1392 2006              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   17057344                                                     
JRNL        DOI    10.1107/S0907444906035426                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 64651                          
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 SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4601                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 16998                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 366                                     
REMARK   3   SOLVENT ATOMS            : 244                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.58500                                              
REMARK   3    B22 (A**2) : -1.46800                                             
REMARK   3    B33 (A**2) : -5.11700                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -7.17200                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.020                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.82                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.781 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.366 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 40.31                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : MYTOPPAR:GDP96_CNS.PARAM                       
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  4  : MYTOPPAR:TAC_CNS5.PARAM                        
REMARK   3  PARAMETER FILE  5  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: EACH MOLECULAR REPLACEMENT SOLUTION       
REMARK   3  WAS VERIFIED BY SUCCESSFULLY CROSS-PHASING THE MERCURY              
REMARK   3  DERIVATIVE SITES WITH THE GENERATED MODEL PHASES.                   
REMARK   4                                                                      
REMARK   4 2HDN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB038230.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 298.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 6                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SDMS                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73085                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
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) : NULL                               
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: MERLOT                                                
REMARK 200 STARTING MODEL: AN UNREFINED 2.7 ANGSTROM MODEL OF E. COLI           
REMARK 200  TRYPSIN-MODIFIED EF-TU-MGGDP, CONSISTING OF RESIDUES 9 TO 40,       
REMARK 200  50 TO 258 AND 260 TO 393, PLUS ONE MG ION AND GDP                   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MULTIPLE CRYSTALS WERE USED TO           
REMARK 280  COLLECT THE NATIVE AND EACH DERIVATIVE DATA SET. VAPOR              
REMARK 280  DIFFUSION, SITTING DROP                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       78.03000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9                               
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 7                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13550 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 30250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 8                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13720 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 29940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 9                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13700 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 30220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
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    41                                                      
REMARK 465     ALA A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     ARG A    44                                                      
REMARK 465     GLY C    41                                                      
REMARK 465     ALA C    42                                                      
REMARK 465     ALA C    43                                                      
REMARK 465     ARG C    44                                                      
REMARK 465     GLY E    41                                                      
REMARK 465     ALA E    42                                                      
REMARK 465     ALA E    43                                                      
REMARK 465     ARG E    44                                                      
REMARK 465     GLY G    41                                                      
REMARK 465     ALA G    42                                                      
REMARK 465     ALA G    43                                                      
REMARK 465     ARG G    44                                                      
REMARK 465     GLY I    41                                                      
REMARK 465     ALA I    42                                                      
REMARK 465     ALA I    43                                                      
REMARK 465     ARG I    44                                                      
REMARK 465     GLY K    41                                                      
REMARK 465     ALA K    42                                                      
REMARK 465     ALA K    43                                                      
REMARK 465     ARG K    44                                                      
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    ASP B 266   N   -  CA  -  CB  ANGL. DEV. = -11.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP B 141       25.38   -159.63                                   
REMARK 500    GLU B 143      -35.06    -39.33                                   
REMARK 500    PRO B 163       73.81    -63.59                                   
REMARK 500    ASP B 181      106.94    -55.38                                   
REMARK 500    ILE B 247      -79.51     64.88                                   
REMARK 500    LYS B 248     -156.50    -81.44                                   
REMARK 500    ARG B 262      -21.65     72.84                                   
REMARK 500    ARG B 333      -67.55     61.49                                   
REMARK 500    ASP D 141       30.97   -161.53                                   
REMARK 500    PRO D 163       69.45    -62.24                                   
REMARK 500    ASP D 181      105.94    -52.07                                   
REMARK 500    SER D 221      111.68    -30.32                                   
REMARK 500    ILE D 247      -78.29     64.07                                   
REMARK 500    LYS D 248     -156.13    -82.11                                   
REMARK 500    ARG D 262      -35.95     70.56                                   
REMARK 500    ARG D 333      -69.06     61.90                                   
REMARK 500    ASP F 141       26.81   -150.27                                   
REMARK 500    PRO F 163       71.07    -61.16                                   
REMARK 500    ASP F 181      105.43    -54.67                                   
REMARK 500    ILE F 247      -80.62     64.43                                   
REMARK 500    LYS F 248     -153.00    -82.03                                   
REMARK 500    ARG F 262      -34.98     67.36                                   
REMARK 500    ARG F 283      -15.28    -48.16                                   
REMARK 500    ARG F 333      -65.91     59.83                                   
REMARK 500    ASP H 141       39.40   -156.13                                   
REMARK 500    PRO H 163       71.04    -63.14                                   
REMARK 500    ASP H 181      105.55    -53.31                                   
REMARK 500    SER H 221      108.13    -29.98                                   
REMARK 500    ILE H 247      -79.98     64.48                                   
REMARK 500    LYS H 248     -157.58    -77.84                                   
REMARK 500    ARG H 262      -39.49     69.91                                   
REMARK 500    ILE H 281      113.08   -160.66                                   
REMARK 500    ARG H 283      -13.36    -46.27                                   
REMARK 500    ARG H 333      -67.71     61.72                                   
REMARK 500    ASP J 141       31.54   -152.53                                   
REMARK 500    PRO J 163       70.48    -61.88                                   
REMARK 500    ASP J 181      102.83    -51.74                                   
REMARK 500    ILE J 247      -77.77     62.05                                   
REMARK 500    LYS J 248     -159.73    -77.77                                   
REMARK 500    PHE J 261       71.63     41.95                                   
REMARK 500    ARG J 262      -42.42     67.25                                   
REMARK 500    ARG J 333      -66.89     62.78                                   
REMARK 500    ASP L 141       38.02   -159.22                                   
REMARK 500    PRO L 163       70.09    -61.99                                   
REMARK 500    ASP L 181      106.29    -55.28                                   
REMARK 500    ILE L 247      -78.37     62.78                                   
REMARK 500    LYS L 248     -156.83    -80.16                                   
REMARK 500    ARG L 262      -41.47     73.75                                   
REMARK 500    ARG L 333      -67.53     61.62                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR E  39         0.08    SIDE_CHAIN                              
REMARK 500    TYR I  39         0.08    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1998  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  25   OG1                                                    
REMARK 620 2 GDP B1999   O2B  75.1                                              
REMARK 620 3 TAC B1888   O12  73.7  87.5                                        
REMARK 620 4 HOH B1001   O    77.8 108.8 142.1                                  
REMARK 620 5 TAC B1888   O11  67.8 140.5  70.0  76.4                            
REMARK 620 6 HOH B1002   O   163.0  96.0  91.7 119.1 116.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C2998  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D2002   O                                                      
REMARK 620 2 GDP D2999   O2B  89.4                                              
REMARK 620 3 THR C  25   OG1 163.2  74.0                                        
REMARK 620 4 TAC D2888   O11 123.4 145.9  72.7                                  
REMARK 620 5 TAC D2888   O12 100.3  88.4  77.2  77.6                            
REMARK 620 6 HOH D2001   O   101.9 100.7  84.0  82.7 156.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E3998  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR E  25   OG1                                                    
REMARK 620 2 GDP F3999   O2B  70.7                                              
REMARK 620 3 TAC F3888   O12  71.6  82.1                                        
REMARK 620 4 TAC F3888   O11  67.3 135.9  72.7                                  
REMARK 620 5 HOH F3001   O    75.1 102.4 142.7  79.4                            
REMARK 620 6 HOH F3002   O   166.2  97.9  99.7 121.3 115.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G4998  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G  25   OG1                                                    
REMARK 620 2 TAC H4888   O11  68.0                                              
REMARK 620 3 HOH H4001   O    78.8  89.4                                        
REMARK 620 4 HOH H4002   O   157.4 124.5 117.3                                  
REMARK 620 5 GDP H4999   O2B  67.5 133.1  96.1  93.9                            
REMARK 620 6 TAC H4888   O12  67.3  70.9 145.1  97.6  78.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG I5998  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TAC J5888   O12                                                    
REMARK 620 2 HOH J5002   O    86.3                                              
REMARK 620 3 HOH J5001   O   160.5 109.0                                        
REMARK 620 4 TAC J5888   O11  77.3 113.0  85.4                                  
REMARK 620 5 GDP J5999   O2B  90.1  89.2 101.8 153.2                            
REMARK 620 6 THR I  25   OG1  82.7 165.3  83.9  73.9  81.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG K6998  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH L6002   O                                                      
REMARK 620 2 TAC L6888   O11 120.8                                              
REMARK 620 3 HOH L6001   O   106.3  85.3                                        
REMARK 620 4 TAC L6888   O12  97.4  76.4 155.3                                  
REMARK 620 5 GDP L6999   O2B  90.0 145.9 100.8  85.9                            
REMARK 620 6 THR K  25   OG1 161.2  74.5  84.7  74.6  72.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1998                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 2998                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 3998                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 4998                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 5998                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 6998                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 1999                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAC B 1888                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP D 2999                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAC D 2888                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP F 3999                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAC F 3888                
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP H 4999                
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAC H 4888                
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP J 5999                
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAC J 5888                
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP L 6999                
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAC L 6888                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2HCJ   RELATED DB: PDB                                   
REMARK 900 TM-EF-TU-MGGDP-TETRACYCLINE COMPLEX AT 2.1 ANGSTROM                  
REMARK 900 RESOLUTION, IN S.G. P43 21 2                                         
DBREF  2HDN A    8    44  UNP    P0A6N1   EFTU_ECOLI       8     44             
DBREF  2HDN C    8    44  UNP    P0A6N1   EFTU_ECOLI       8     44             
DBREF  2HDN E    8    44  UNP    P0A6N1   EFTU_ECOLI       8     44             
DBREF  2HDN G    8    44  UNP    P0A6N1   EFTU_ECOLI       8     44             
DBREF  2HDN I    8    44  UNP    P0A6N1   EFTU_ECOLI       8     44             
DBREF  2HDN K    8    44  UNP    P0A6N1   EFTU_ECOLI       8     44             
DBREF  2HDN B   59   393  UNP    P0A6N1   EFTU_ECOLI      59    393             
DBREF  2HDN D   59   393  UNP    P0A6N1   EFTU_ECOLI      59    393             
DBREF  2HDN F   59   393  UNP    P0A6N1   EFTU_ECOLI      59    393             
DBREF  2HDN H   59   393  UNP    P0A6N1   EFTU_ECOLI      59    393             
DBREF  2HDN J   59   393  UNP    P0A6N1   EFTU_ECOLI      59    393             
DBREF  2HDN L   59   393  UNP    P0A6N1   EFTU_ECOLI      59    393             
SEQADV 2HDN GLY B  393  UNP  P0A6N1    SER   393 VARIANT                        
SEQADV 2HDN GLY D  393  UNP  P0A6N1    SER   393 VARIANT                        
SEQADV 2HDN GLY F  393  UNP  P0A6N1    SER   393 VARIANT                        
SEQADV 2HDN GLY H  393  UNP  P0A6N1    SER   393 VARIANT                        
SEQADV 2HDN GLY J  393  UNP  P0A6N1    SER   393 VARIANT                        
SEQADV 2HDN GLY L  393  UNP  P0A6N1    SER   393 VARIANT                        
SEQRES   1 A   37  THR LYS PRO HIS VAL ASN VAL GLY THR ILE GLY HIS VAL          
SEQRES   2 A   37  ASP HIS GLY LYS THR THR LEU THR ALA ALA ILE THR THR          
SEQRES   3 A   37  VAL LEU ALA LYS THR TYR GLY GLY ALA ALA ARG                  
SEQRES   1 B  335  GLY ILE THR ILE ASN THR SER HIS VAL GLU TYR ASP THR          
SEQRES   2 B  335  PRO THR ARG HIS TYR ALA HIS VAL ASP CYS PRO GLY HIS          
SEQRES   3 B  335  ALA ASP TYR VAL LYS ASN MET ILE THR GLY ALA ALA GLN          
SEQRES   4 B  335  MET ASP GLY ALA ILE LEU VAL VAL ALA ALA THR ASP GLY          
SEQRES   5 B  335  PRO MET PRO GLN THR ARG GLU HIS ILE LEU LEU GLY ARG          
SEQRES   6 B  335  GLN VAL GLY VAL PRO TYR ILE ILE VAL PHE LEU ASN LYS          
SEQRES   7 B  335  CYS ASP MET VAL ASP ASP GLU GLU LEU LEU GLU LEU VAL          
SEQRES   8 B  335  GLU MET GLU VAL ARG GLU LEU LEU SER GLN TYR ASP PHE          
SEQRES   9 B  335  PRO GLY ASP ASP THR PRO ILE VAL ARG GLY SER ALA LEU          
SEQRES  10 B  335  LYS ALA LEU GLU GLY ASP ALA GLU TRP GLU ALA LYS ILE          
SEQRES  11 B  335  LEU GLU LEU ALA GLY PHE LEU ASP SER TYR ILE PRO GLU          
SEQRES  12 B  335  PRO GLU ARG ALA ILE ASP LYS PRO PHE LEU LEU PRO ILE          
SEQRES  13 B  335  GLU ASP VAL PHE SER ILE SER GLY ARG GLY THR VAL VAL          
SEQRES  14 B  335  THR GLY ARG VAL GLU ARG GLY ILE ILE LYS VAL GLY GLU          
SEQRES  15 B  335  GLU VAL GLU ILE VAL GLY ILE LYS GLU THR GLN LYS SER          
SEQRES  16 B  335  THR CYS THR GLY VAL GLU MET PHE ARG LYS LEU LEU ASP          
SEQRES  17 B  335  GLU GLY ARG ALA GLY GLU ASN VAL GLY VAL LEU LEU ARG          
SEQRES  18 B  335  GLY ILE LYS ARG GLU GLU ILE GLU ARG GLY GLN VAL LEU          
SEQRES  19 B  335  ALA LYS PRO GLY THR ILE LYS PRO HIS THR LYS PHE GLU          
SEQRES  20 B  335  SER GLU VAL TYR ILE LEU SER LYS ASP GLU GLY GLY ARG          
SEQRES  21 B  335  HIS THR PRO PHE PHE LYS GLY TYR ARG PRO GLN PHE TYR          
SEQRES  22 B  335  PHE ARG THR THR ASP VAL THR GLY THR ILE GLU LEU PRO          
SEQRES  23 B  335  GLU GLY VAL GLU MET VAL MET PRO GLY ASP ASN ILE LYS          
SEQRES  24 B  335  MET VAL VAL THR LEU ILE HIS PRO ILE ALA MET ASP ASP          
SEQRES  25 B  335  GLY LEU ARG PHE ALA ILE ARG GLU GLY GLY ARG THR VAL          
SEQRES  26 B  335  GLY ALA GLY VAL VAL ALA LYS VAL LEU GLY                      
SEQRES   1 C   37  THR LYS PRO HIS VAL ASN VAL GLY THR ILE GLY HIS VAL          
SEQRES   2 C   37  ASP HIS GLY LYS THR THR LEU THR ALA ALA ILE THR THR          
SEQRES   3 C   37  VAL LEU ALA LYS THR TYR GLY GLY ALA ALA ARG                  
SEQRES   1 D  335  GLY ILE THR ILE ASN THR SER HIS VAL GLU TYR ASP THR          
SEQRES   2 D  335  PRO THR ARG HIS TYR ALA HIS VAL ASP CYS PRO GLY HIS          
SEQRES   3 D  335  ALA ASP TYR VAL LYS ASN MET ILE THR GLY ALA ALA GLN          
SEQRES   4 D  335  MET ASP GLY ALA ILE LEU VAL VAL ALA ALA THR ASP GLY          
SEQRES   5 D  335  PRO MET PRO GLN THR ARG GLU HIS ILE LEU LEU GLY ARG          
SEQRES   6 D  335  GLN VAL GLY VAL PRO TYR ILE ILE VAL PHE LEU ASN LYS          
SEQRES   7 D  335  CYS ASP MET VAL ASP ASP GLU GLU LEU LEU GLU LEU VAL          
SEQRES   8 D  335  GLU MET GLU VAL ARG GLU LEU LEU SER GLN TYR ASP PHE          
SEQRES   9 D  335  PRO GLY ASP ASP THR PRO ILE VAL ARG GLY SER ALA LEU          
SEQRES  10 D  335  LYS ALA LEU GLU GLY ASP ALA GLU TRP GLU ALA LYS ILE          
SEQRES  11 D  335  LEU GLU LEU ALA GLY PHE LEU ASP SER TYR ILE PRO GLU          
SEQRES  12 D  335  PRO GLU ARG ALA ILE ASP LYS PRO PHE LEU LEU PRO ILE          
SEQRES  13 D  335  GLU ASP VAL PHE SER ILE SER GLY ARG GLY THR VAL VAL          
SEQRES  14 D  335  THR GLY ARG VAL GLU ARG GLY ILE ILE LYS VAL GLY GLU          
SEQRES  15 D  335  GLU VAL GLU ILE VAL GLY ILE LYS GLU THR GLN LYS SER          
SEQRES  16 D  335  THR CYS THR GLY VAL GLU MET PHE ARG LYS LEU LEU ASP          
SEQRES  17 D  335  GLU GLY ARG ALA GLY GLU ASN VAL GLY VAL LEU LEU ARG          
SEQRES  18 D  335  GLY ILE LYS ARG GLU GLU ILE GLU ARG GLY GLN VAL LEU          
SEQRES  19 D  335  ALA LYS PRO GLY THR ILE LYS PRO HIS THR LYS PHE GLU          
SEQRES  20 D  335  SER GLU VAL TYR ILE LEU SER LYS ASP GLU GLY GLY ARG          
SEQRES  21 D  335  HIS THR PRO PHE PHE LYS GLY TYR ARG PRO GLN PHE TYR          
SEQRES  22 D  335  PHE ARG THR THR ASP VAL THR GLY THR ILE GLU LEU PRO          
SEQRES  23 D  335  GLU GLY VAL GLU MET VAL MET PRO GLY ASP ASN ILE LYS          
SEQRES  24 D  335  MET VAL VAL THR LEU ILE HIS PRO ILE ALA MET ASP ASP          
SEQRES  25 D  335  GLY LEU ARG PHE ALA ILE ARG GLU GLY GLY ARG THR VAL          
SEQRES  26 D  335  GLY ALA GLY VAL VAL ALA LYS VAL LEU GLY                      
SEQRES   1 E   37  THR LYS PRO HIS VAL ASN VAL GLY THR ILE GLY HIS VAL          
SEQRES   2 E   37  ASP HIS GLY LYS THR THR LEU THR ALA ALA ILE THR THR          
SEQRES   3 E   37  VAL LEU ALA LYS THR TYR GLY GLY ALA ALA ARG                  
SEQRES   1 F  335  GLY ILE THR ILE ASN THR SER HIS VAL GLU TYR ASP THR          
SEQRES   2 F  335  PRO THR ARG HIS TYR ALA HIS VAL ASP CYS PRO GLY HIS          
SEQRES   3 F  335  ALA ASP TYR VAL LYS ASN MET ILE THR GLY ALA ALA GLN          
SEQRES   4 F  335  MET ASP GLY ALA ILE LEU VAL VAL ALA ALA THR ASP GLY          
SEQRES   5 F  335  PRO MET PRO GLN THR ARG GLU HIS ILE LEU LEU GLY ARG          
SEQRES   6 F  335  GLN VAL GLY VAL PRO TYR ILE ILE VAL PHE LEU ASN LYS          
SEQRES   7 F  335  CYS ASP MET VAL ASP ASP GLU GLU LEU LEU GLU LEU VAL          
SEQRES   8 F  335  GLU MET GLU VAL ARG GLU LEU LEU SER GLN TYR ASP PHE          
SEQRES   9 F  335  PRO GLY ASP ASP THR PRO ILE VAL ARG GLY SER ALA LEU          
SEQRES  10 F  335  LYS ALA LEU GLU GLY ASP ALA GLU TRP GLU ALA LYS ILE          
SEQRES  11 F  335  LEU GLU LEU ALA GLY PHE LEU ASP SER TYR ILE PRO GLU          
SEQRES  12 F  335  PRO GLU ARG ALA ILE ASP LYS PRO PHE LEU LEU PRO ILE          
SEQRES  13 F  335  GLU ASP VAL PHE SER ILE SER GLY ARG GLY THR VAL VAL          
SEQRES  14 F  335  THR GLY ARG VAL GLU ARG GLY ILE ILE LYS VAL GLY GLU          
SEQRES  15 F  335  GLU VAL GLU ILE VAL GLY ILE LYS GLU THR GLN LYS SER          
SEQRES  16 F  335  THR CYS THR GLY VAL GLU MET PHE ARG LYS LEU LEU ASP          
SEQRES  17 F  335  GLU GLY ARG ALA GLY GLU ASN VAL GLY VAL LEU LEU ARG          
SEQRES  18 F  335  GLY ILE LYS ARG GLU GLU ILE GLU ARG GLY GLN VAL LEU          
SEQRES  19 F  335  ALA LYS PRO GLY THR ILE LYS PRO HIS THR LYS PHE GLU          
SEQRES  20 F  335  SER GLU VAL TYR ILE LEU SER LYS ASP GLU GLY GLY ARG          
SEQRES  21 F  335  HIS THR PRO PHE PHE LYS GLY TYR ARG PRO GLN PHE TYR          
SEQRES  22 F  335  PHE ARG THR THR ASP VAL THR GLY THR ILE GLU LEU PRO          
SEQRES  23 F  335  GLU GLY VAL GLU MET VAL MET PRO GLY ASP ASN ILE LYS          
SEQRES  24 F  335  MET VAL VAL THR LEU ILE HIS PRO ILE ALA MET ASP ASP          
SEQRES  25 F  335  GLY LEU ARG PHE ALA ILE ARG GLU GLY GLY ARG THR VAL          
SEQRES  26 F  335  GLY ALA GLY VAL VAL ALA LYS VAL LEU GLY                      
SEQRES   1 G   37  THR LYS PRO HIS VAL ASN VAL GLY THR ILE GLY HIS VAL          
SEQRES   2 G   37  ASP HIS GLY LYS THR THR LEU THR ALA ALA ILE THR THR          
SEQRES   3 G   37  VAL LEU ALA LYS THR TYR GLY GLY ALA ALA ARG                  
SEQRES   1 H  335  GLY ILE THR ILE ASN THR SER HIS VAL GLU TYR ASP THR          
SEQRES   2 H  335  PRO THR ARG HIS TYR ALA HIS VAL ASP CYS PRO GLY HIS          
SEQRES   3 H  335  ALA ASP TYR VAL LYS ASN MET ILE THR GLY ALA ALA GLN          
SEQRES   4 H  335  MET ASP GLY ALA ILE LEU VAL VAL ALA ALA THR ASP GLY          
SEQRES   5 H  335  PRO MET PRO GLN THR ARG GLU HIS ILE LEU LEU GLY ARG          
SEQRES   6 H  335  GLN VAL GLY VAL PRO TYR ILE ILE VAL PHE LEU ASN LYS          
SEQRES   7 H  335  CYS ASP MET VAL ASP ASP GLU GLU LEU LEU GLU LEU VAL          
SEQRES   8 H  335  GLU MET GLU VAL ARG GLU LEU LEU SER GLN TYR ASP PHE          
SEQRES   9 H  335  PRO GLY ASP ASP THR PRO ILE VAL ARG GLY SER ALA LEU          
SEQRES  10 H  335  LYS ALA LEU GLU GLY ASP ALA GLU TRP GLU ALA LYS ILE          
SEQRES  11 H  335  LEU GLU LEU ALA GLY PHE LEU ASP SER TYR ILE PRO GLU          
SEQRES  12 H  335  PRO GLU ARG ALA ILE ASP LYS PRO PHE LEU LEU PRO ILE          
SEQRES  13 H  335  GLU ASP VAL PHE SER ILE SER GLY ARG GLY THR VAL VAL          
SEQRES  14 H  335  THR GLY ARG VAL GLU ARG GLY ILE ILE LYS VAL GLY GLU          
SEQRES  15 H  335  GLU VAL GLU ILE VAL GLY ILE LYS GLU THR GLN LYS SER          
SEQRES  16 H  335  THR CYS THR GLY VAL GLU MET PHE ARG LYS LEU LEU ASP          
SEQRES  17 H  335  GLU GLY ARG ALA GLY GLU ASN VAL GLY VAL LEU LEU ARG          
SEQRES  18 H  335  GLY ILE LYS ARG GLU GLU ILE GLU ARG GLY GLN VAL LEU          
SEQRES  19 H  335  ALA LYS PRO GLY THR ILE LYS PRO HIS THR LYS PHE GLU          
SEQRES  20 H  335  SER GLU VAL TYR ILE LEU SER LYS ASP GLU GLY GLY ARG          
SEQRES  21 H  335  HIS THR PRO PHE PHE LYS GLY TYR ARG PRO GLN PHE TYR          
SEQRES  22 H  335  PHE ARG THR THR ASP VAL THR GLY THR ILE GLU LEU PRO          
SEQRES  23 H  335  GLU GLY VAL GLU MET VAL MET PRO GLY ASP ASN ILE LYS          
SEQRES  24 H  335  MET VAL VAL THR LEU ILE HIS PRO ILE ALA MET ASP ASP          
SEQRES  25 H  335  GLY LEU ARG PHE ALA ILE ARG GLU GLY GLY ARG THR VAL          
SEQRES  26 H  335  GLY ALA GLY VAL VAL ALA LYS VAL LEU GLY                      
SEQRES   1 I   37  THR LYS PRO HIS VAL ASN VAL GLY THR ILE GLY HIS VAL          
SEQRES   2 I   37  ASP HIS GLY LYS THR THR LEU THR ALA ALA ILE THR THR          
SEQRES   3 I   37  VAL LEU ALA LYS THR TYR GLY GLY ALA ALA ARG                  
SEQRES   1 J  335  GLY ILE THR ILE ASN THR SER HIS VAL GLU TYR ASP THR          
SEQRES   2 J  335  PRO THR ARG HIS TYR ALA HIS VAL ASP CYS PRO GLY HIS          
SEQRES   3 J  335  ALA ASP TYR VAL LYS ASN MET ILE THR GLY ALA ALA GLN          
SEQRES   4 J  335  MET ASP GLY ALA ILE LEU VAL VAL ALA ALA THR ASP GLY          
SEQRES   5 J  335  PRO MET PRO GLN THR ARG GLU HIS ILE LEU LEU GLY ARG          
SEQRES   6 J  335  GLN VAL GLY VAL PRO TYR ILE ILE VAL PHE LEU ASN LYS          
SEQRES   7 J  335  CYS ASP MET VAL ASP ASP GLU GLU LEU LEU GLU LEU VAL          
SEQRES   8 J  335  GLU MET GLU VAL ARG GLU LEU LEU SER GLN TYR ASP PHE          
SEQRES   9 J  335  PRO GLY ASP ASP THR PRO ILE VAL ARG GLY SER ALA LEU          
SEQRES  10 J  335  LYS ALA LEU GLU GLY ASP ALA GLU TRP GLU ALA LYS ILE          
SEQRES  11 J  335  LEU GLU LEU ALA GLY PHE LEU ASP SER TYR ILE PRO GLU          
SEQRES  12 J  335  PRO GLU ARG ALA ILE ASP LYS PRO PHE LEU LEU PRO ILE          
SEQRES  13 J  335  GLU ASP VAL PHE SER ILE SER GLY ARG GLY THR VAL VAL          
SEQRES  14 J  335  THR GLY ARG VAL GLU ARG GLY ILE ILE LYS VAL GLY GLU          
SEQRES  15 J  335  GLU VAL GLU ILE VAL GLY ILE LYS GLU THR GLN LYS SER          
SEQRES  16 J  335  THR CYS THR GLY VAL GLU MET PHE ARG LYS LEU LEU ASP          
SEQRES  17 J  335  GLU GLY ARG ALA GLY GLU ASN VAL GLY VAL LEU LEU ARG          
SEQRES  18 J  335  GLY ILE LYS ARG GLU GLU ILE GLU ARG GLY GLN VAL LEU          
SEQRES  19 J  335  ALA LYS PRO GLY THR ILE LYS PRO HIS THR LYS PHE GLU          
SEQRES  20 J  335  SER GLU VAL TYR ILE LEU SER LYS ASP GLU GLY GLY ARG          
SEQRES  21 J  335  HIS THR PRO PHE PHE LYS GLY TYR ARG PRO GLN PHE TYR          
SEQRES  22 J  335  PHE ARG THR THR ASP VAL THR GLY THR ILE GLU LEU PRO          
SEQRES  23 J  335  GLU GLY VAL GLU MET VAL MET PRO GLY ASP ASN ILE LYS          
SEQRES  24 J  335  MET VAL VAL THR LEU ILE HIS PRO ILE ALA MET ASP ASP          
SEQRES  25 J  335  GLY LEU ARG PHE ALA ILE ARG GLU GLY GLY ARG THR VAL          
SEQRES  26 J  335  GLY ALA GLY VAL VAL ALA LYS VAL LEU GLY                      
SEQRES   1 K   37  THR LYS PRO HIS VAL ASN VAL GLY THR ILE GLY HIS VAL          
SEQRES   2 K   37  ASP HIS GLY LYS THR THR LEU THR ALA ALA ILE THR THR          
SEQRES   3 K   37  VAL LEU ALA LYS THR TYR GLY GLY ALA ALA ARG                  
SEQRES   1 L  335  GLY ILE THR ILE ASN THR SER HIS VAL GLU TYR ASP THR          
SEQRES   2 L  335  PRO THR ARG HIS TYR ALA HIS VAL ASP CYS PRO GLY HIS          
SEQRES   3 L  335  ALA ASP TYR VAL LYS ASN MET ILE THR GLY ALA ALA GLN          
SEQRES   4 L  335  MET ASP GLY ALA ILE LEU VAL VAL ALA ALA THR ASP GLY          
SEQRES   5 L  335  PRO MET PRO GLN THR ARG GLU HIS ILE LEU LEU GLY ARG          
SEQRES   6 L  335  GLN VAL GLY VAL PRO TYR ILE ILE VAL PHE LEU ASN LYS          
SEQRES   7 L  335  CYS ASP MET VAL ASP ASP GLU GLU LEU LEU GLU LEU VAL          
SEQRES   8 L  335  GLU MET GLU VAL ARG GLU LEU LEU SER GLN TYR ASP PHE          
SEQRES   9 L  335  PRO GLY ASP ASP THR PRO ILE VAL ARG GLY SER ALA LEU          
SEQRES  10 L  335  LYS ALA LEU GLU GLY ASP ALA GLU TRP GLU ALA LYS ILE          
SEQRES  11 L  335  LEU GLU LEU ALA GLY PHE LEU ASP SER TYR ILE PRO GLU          
SEQRES  12 L  335  PRO GLU ARG ALA ILE ASP LYS PRO PHE LEU LEU PRO ILE          
SEQRES  13 L  335  GLU ASP VAL PHE SER ILE SER GLY ARG GLY THR VAL VAL          
SEQRES  14 L  335  THR GLY ARG VAL GLU ARG GLY ILE ILE LYS VAL GLY GLU          
SEQRES  15 L  335  GLU VAL GLU ILE VAL GLY ILE LYS GLU THR GLN LYS SER          
SEQRES  16 L  335  THR CYS THR GLY VAL GLU MET PHE ARG LYS LEU LEU ASP          
SEQRES  17 L  335  GLU GLY ARG ALA GLY GLU ASN VAL GLY VAL LEU LEU ARG          
SEQRES  18 L  335  GLY ILE LYS ARG GLU GLU ILE GLU ARG GLY GLN VAL LEU          
SEQRES  19 L  335  ALA LYS PRO GLY THR ILE LYS PRO HIS THR LYS PHE GLU          
SEQRES  20 L  335  SER GLU VAL TYR ILE LEU SER LYS ASP GLU GLY GLY ARG          
SEQRES  21 L  335  HIS THR PRO PHE PHE LYS GLY TYR ARG PRO GLN PHE TYR          
SEQRES  22 L  335  PHE ARG THR THR ASP VAL THR GLY THR ILE GLU LEU PRO          
SEQRES  23 L  335  GLU GLY VAL GLU MET VAL MET PRO GLY ASP ASN ILE LYS          
SEQRES  24 L  335  MET VAL VAL THR LEU ILE HIS PRO ILE ALA MET ASP ASP          
SEQRES  25 L  335  GLY LEU ARG PHE ALA ILE ARG GLU GLY GLY ARG THR VAL          
SEQRES  26 L  335  GLY ALA GLY VAL VAL ALA LYS VAL LEU GLY                      
HET     MG  A1998       1                                                       
HET     MG  C2998       1                                                       
HET     MG  E3998       1                                                       
HET     MG  G4998       1                                                       
HET     MG  I5998       1                                                       
HET     MG  K6998       1                                                       
HET    GDP  B1999      28                                                       
HET    TAC  B1888      32                                                       
HET    GDP  D2999      28                                                       
HET    TAC  D2888      32                                                       
HET    GDP  F3999      28                                                       
HET    TAC  F3888      32                                                       
HET    GDP  H4999      28                                                       
HET    TAC  H4888      32                                                       
HET    GDP  J5999      28                                                       
HET    TAC  J5888      32                                                       
HET    GDP  L6999      28                                                       
HET    TAC  L6888      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     TAC TETRACYCLINE                                                     
FORMUL  13   MG    6(MG 2+)                                                     
FORMUL  19  GDP    6(C10 H15 N5 O11 P2)                                         
FORMUL  20  TAC    6(C22 H24 N2 O8)                                             
FORMUL  31  HOH   *244(H2 O)                                                    
HELIX    1   1 GLY A   23  GLY A   40  1                                  18    
HELIX    2   2 GLY B   83  GLY B   94  1                                  12    
HELIX    3   3 MET B  112  GLY B  126  1                                  15    
HELIX    4   4 ASP B  142  TYR B  160  1                                  19    
HELIX    5   5 SER B  173  GLY B  180  1                                   8    
HELIX    6   6 ASP B  181  ILE B  199  1                                  19    
HELIX    7   7 ARG B  204  LYS B  208  5                                   5    
HELIX    8   8 GLY C   23  GLY C   40  1                                  18    
HELIX    9   9 GLY D   83  THR D   93  1                                  11    
HELIX   10  10 MET D  112  GLY D  126  1                                  15    
HELIX   11  11 ASP D  142  TYR D  160  1                                  19    
HELIX   12  12 SER D  173  GLY D  180  1                                   8    
HELIX   13  13 ASP D  181  ILE D  199  1                                  19    
HELIX   14  14 ARG D  204  LYS D  208  5                                   5    
HELIX   15  15 GLY E   23  GLY E   40  1                                  18    
HELIX   16  16 GLY F   83  GLY F   94  1                                  12    
HELIX   17  17 MET F  112  GLY F  126  1                                  15    
HELIX   18  18 ASP F  142  TYR F  160  1                                  19    
HELIX   19  19 SER F  173  GLY F  180  1                                   8    
HELIX   20  20 ASP F  181  ILE F  199  1                                  19    
HELIX   21  21 ARG F  204  LYS F  208  5                                   5    
HELIX   22  22 GLY G   23  GLY G   40  1                                  18    
HELIX   23  23 GLY H   83  GLY H   94  1                                  12    
HELIX   24  24 MET H  112  GLY H  126  1                                  15    
HELIX   25  25 ASP H  142  TYR H  160  1                                  19    
HELIX   26  26 SER H  173  GLY H  180  1                                   8    
HELIX   27  27 ASP H  181  ILE H  199  1                                  19    
HELIX   28  28 ARG H  204  LYS H  208  5                                   5    
HELIX   29  29 GLY I   23  GLY I   40  1                                  18    
HELIX   30  30 GLY J   83  GLY J   94  1                                  12    
HELIX   31  31 MET J  112  GLY J  126  1                                  15    
HELIX   32  32 ASP J  142  TYR J  160  1                                  19    
HELIX   33  33 SER J  173  GLY J  180  1                                   8    
HELIX   34  34 ASP J  181  ILE J  199  1                                  19    
HELIX   35  35 ARG J  204  LYS J  208  5                                   5    
HELIX   36  36 GLY K   23  GLY K   40  1                                  18    
HELIX   37  37 GLY L   83  THR L   93  1                                  11    
HELIX   38  38 MET L  112  GLY L  126  1                                  15    
HELIX   39  39 ASP L  142  TYR L  160  1                                  19    
HELIX   40  40 SER L  173  GLY L  180  1                                   8    
HELIX   41  41 ASP L  181  ILE L  199  1                                  19    
HELIX   42  42 ARG L  204  LYS L  208  5                                   5    
SHEET    1   A12 ILE B 169  ARG B 171  0                                        
SHEET    2   A12 ILE B 130  ASN B 135  1  N  LEU B 134   O  VAL B 170           
SHEET    3   A12 ALA B 101  ALA B 106  1  N  LEU B 103   O  ILE B 131           
SHEET    4   A12 HIS A  11  ILE A  17  1  N  GLY A  15   O  ILE B 102           
SHEET    5   A12 HIS B  75  ASP B  80  1  O  ALA B  77   N  VAL A  14           
SHEET    6   A12 THR B  64  ASP B  70 -1  N  TYR B  69   O  TYR B  76           
SHEET    7   A12 THR D  64  ASP D  70 -1  O  HIS D  66   N  THR B  64           
SHEET    8   A12 HIS D  75  ASP D  80 -1  O  TYR D  76   N  TYR D  69           
SHEET    9   A12 HIS C  11  ILE C  17  1  N  VAL C  14   O  ALA D  77           
SHEET   10   A12 ALA D 101  ALA D 106  1  O  ILE D 102   N  GLY C  15           
SHEET   11   A12 ILE D 130  ASN D 135  1  O  ILE D 131   N  LEU D 103           
SHEET   12   A12 ILE D 169  ARG D 171  1  O  VAL D 170   N  LEU D 134           
SHEET    1   B 7 LEU B 211  PRO B 213  0                                        
SHEET    2   B 7 VAL B 291  ALA B 293 -1  O  LEU B 292   N  LEU B 212           
SHEET    3   B 7 GLU B 241  VAL B 245 -1  N  GLU B 243   O  ALA B 293           
SHEET    4   B 7 GLN B 251  MET B 260 -1  O  GLN B 251   N  ILE B 244           
SHEET    5   B 7 ASN B 273  LEU B 278 -1  O  LEU B 277   N  GLY B 257           
SHEET    6   B 7 GLY B 224  ARG B 230 -1  N  VAL B 227   O  VAL B 276           
SHEET    7   B 7 ASP B 216  ILE B 220 -1  N  PHE B 218   O  VAL B 226           
SHEET    1   C 5 LEU B 211  PRO B 213  0                                        
SHEET    2   C 5 VAL B 291  ALA B 293 -1  O  LEU B 292   N  LEU B 212           
SHEET    3   C 5 GLU B 241  VAL B 245 -1  N  GLU B 243   O  ALA B 293           
SHEET    4   C 5 GLN B 251  MET B 260 -1  O  GLN B 251   N  ILE B 244           
SHEET    5   C 5 LYS B 263  LEU B 265 -1  O  LEU B 265   N  VAL B 258           
SHEET    1   D 2 ILE B 235  LYS B 237  0                                        
SHEET    2   D 2 GLU B 267  ARG B 269 -1  O  GLY B 268   N  ILE B 236           
SHEET    1   E 7 PRO B 300  ILE B 310  0                                        
SHEET    2   E 7 ASN B 355  ALA B 367 -1  O  LEU B 362   N  THR B 302           
SHEET    3   E 7 THR B 335  GLU B 342 -1  N  THR B 340   O  THR B 361           
SHEET    4   E 7 GLN B 329  PHE B 332 -1  N  PHE B 330   O  VAL B 337           
SHEET    5   E 7 ARG B 373  GLU B 378 -1  O  ALA B 375   N  TYR B 331           
SHEET    6   E 7 ARG B 381  VAL B 391 -1  O  GLY B 384   N  ILE B 376           
SHEET    7   E 7 PRO B 300  ILE B 310 -1  N  TYR B 309   O  ALA B 385           
SHEET    1   F 2 PHE B 322  PHE B 323  0                                        
SHEET    2   F 2 MET B 349  VAL B 350 -1  O  VAL B 350   N  PHE B 322           
SHEET    1   G 7 LEU D 211  PRO D 213  0                                        
SHEET    2   G 7 VAL D 291  ALA D 293 -1  O  LEU D 292   N  LEU D 212           
SHEET    3   G 7 GLU D 241  VAL D 245 -1  N  GLU D 243   O  ALA D 293           
SHEET    4   G 7 GLN D 251  MET D 260 -1  O  GLN D 251   N  ILE D 244           
SHEET    5   G 7 ASN D 273  LEU D 278 -1  O  LEU D 277   N  GLY D 257           
SHEET    6   G 7 GLY D 224  ARG D 230 -1  N  VAL D 227   O  VAL D 276           
SHEET    7   G 7 ASP D 216  ILE D 220 -1  N  PHE D 218   O  VAL D 226           
SHEET    1   H 5 LEU D 211  PRO D 213  0                                        
SHEET    2   H 5 VAL D 291  ALA D 293 -1  O  LEU D 292   N  LEU D 212           
SHEET    3   H 5 GLU D 241  VAL D 245 -1  N  GLU D 243   O  ALA D 293           
SHEET    4   H 5 GLN D 251  MET D 260 -1  O  GLN D 251   N  ILE D 244           
SHEET    5   H 5 LYS D 263  LEU D 265 -1  O  LEU D 265   N  VAL D 258           
SHEET    1   I 2 ILE D 235  LYS D 237  0                                        
SHEET    2   I 2 GLU D 267  ARG D 269 -1  O  GLY D 268   N  ILE D 236           
SHEET    1   J 7 PRO D 300  ILE D 310  0                                        
SHEET    2   J 7 ASN D 355  ALA D 367 -1  O  LEU D 362   N  THR D 302           
SHEET    3   J 7 THR D 335  GLU D 342 -1  N  THR D 338   O  ILE D 363           
SHEET    4   J 7 GLN D 329  PHE D 332 -1  N  PHE D 332   O  THR D 335           
SHEET    5   J 7 ARG D 373  GLU D 378 -1  O  ALA D 375   N  TYR D 331           
SHEET    6   J 7 ARG D 381  VAL D 391 -1  O  GLY D 384   N  ILE D 376           
SHEET    7   J 7 PRO D 300  ILE D 310 -1  N  TYR D 309   O  ALA D 385           
SHEET    1   K 2 PHE D 322  PHE D 323  0                                        
SHEET    2   K 2 MET D 349  VAL D 350 -1  O  VAL D 350   N  PHE D 322           
SHEET    1   L12 ILE F 169  ARG F 171  0                                        
SHEET    2   L12 ILE F 130  ASN F 135  1  N  LEU F 134   O  VAL F 170           
SHEET    3   L12 ALA F 101  ALA F 106  1  N  ALA F 101   O  ILE F 131           
SHEET    4   L12 HIS E  11  ILE E  17  1  N  GLY E  15   O  ILE F 102           
SHEET    5   L12 HIS F  75  ASP F  80  1  O  ALA F  77   N  VAL E  14           
SHEET    6   L12 THR F  64  ASP F  70 -1  N  TYR F  69   O  TYR F  76           
SHEET    7   L12 THR H  64  ASP H  70 -1  O  THR H  64   N  HIS F  66           
SHEET    8   L12 HIS H  75  ASP H  80 -1  O  TYR H  76   N  TYR H  69           
SHEET    9   L12 HIS G  11  ILE G  17  1  N  VAL G  14   O  ALA H  77           
SHEET   10   L12 ALA H 101  ALA H 106  1  O  ILE H 102   N  GLY G  15           
SHEET   11   L12 ILE H 130  ASN H 135  1  O  PHE H 133   N  LEU H 103           
SHEET   12   L12 ILE H 169  ARG H 171  1  O  VAL H 170   N  LEU H 134           
SHEET    1   M 7 LEU F 211  PRO F 213  0                                        
SHEET    2   M 7 VAL F 291  ALA F 293 -1  O  LEU F 292   N  LEU F 212           
SHEET    3   M 7 GLU F 241  VAL F 245 -1  N  GLU F 243   O  ALA F 293           
SHEET    4   M 7 GLN F 251  MET F 260 -1  O  GLN F 251   N  ILE F 244           
SHEET    5   M 7 ASN F 273  LEU F 278 -1  O  LEU F 277   N  GLY F 257           
SHEET    6   M 7 GLY F 224  ARG F 230 -1  N  VAL F 227   O  VAL F 276           
SHEET    7   M 7 ASP F 216  ILE F 220 -1  N  PHE F 218   O  VAL F 226           
SHEET    1   N 5 LEU F 211  PRO F 213  0                                        
SHEET    2   N 5 VAL F 291  ALA F 293 -1  O  LEU F 292   N  LEU F 212           
SHEET    3   N 5 GLU F 241  VAL F 245 -1  N  GLU F 243   O  ALA F 293           
SHEET    4   N 5 GLN F 251  MET F 260 -1  O  GLN F 251   N  ILE F 244           
SHEET    5   N 5 LYS F 263  LEU F 265 -1  O  LEU F 265   N  VAL F 258           
SHEET    1   O 2 ILE F 235  LYS F 237  0                                        
SHEET    2   O 2 GLU F 267  ARG F 269 -1  O  GLY F 268   N  ILE F 236           
SHEET    1   P 7 PRO F 300  ILE F 310  0                                        
SHEET    2   P 7 ASN F 355  ALA F 367 -1  O  LEU F 362   N  THR F 302           
SHEET    3   P 7 THR F 335  GLU F 342 -1  N  GLU F 342   O  VAL F 359           
SHEET    4   P 7 GLN F 329  PHE F 332 -1  N  PHE F 330   O  VAL F 337           
SHEET    5   P 7 ARG F 373  GLU F 378 -1  O  ALA F 375   N  TYR F 331           
SHEET    6   P 7 ARG F 381  VAL F 391 -1  O  GLY F 384   N  ILE F 376           
SHEET    7   P 7 PRO F 300  ILE F 310 -1  N  TYR F 309   O  ALA F 385           
SHEET    1   Q 2 PHE F 322  PHE F 323  0                                        
SHEET    2   Q 2 MET F 349  VAL F 350 -1  O  VAL F 350   N  PHE F 322           
SHEET    1   R 7 LEU H 211  PRO H 213  0                                        
SHEET    2   R 7 VAL H 291  ALA H 293 -1  O  LEU H 292   N  LEU H 212           
SHEET    3   R 7 GLU H 241  VAL H 245 -1  N  GLU H 243   O  ALA H 293           
SHEET    4   R 7 GLN H 251  MET H 260 -1  O  GLN H 251   N  ILE H 244           
SHEET    5   R 7 ASN H 273  LEU H 278 -1  O  LEU H 277   N  GLY H 257           
SHEET    6   R 7 GLY H 224  ARG H 230 -1  N  VAL H 227   O  VAL H 276           
SHEET    7   R 7 ASP H 216  ILE H 220 -1  N  PHE H 218   O  VAL H 226           
SHEET    1   S 5 LEU H 211  PRO H 213  0                                        
SHEET    2   S 5 VAL H 291  ALA H 293 -1  O  LEU H 292   N  LEU H 212           
SHEET    3   S 5 GLU H 241  VAL H 245 -1  N  GLU H 243   O  ALA H 293           
SHEET    4   S 5 GLN H 251  MET H 260 -1  O  GLN H 251   N  ILE H 244           
SHEET    5   S 5 LYS H 263  LEU H 265 -1  O  LEU H 265   N  VAL H 258           
SHEET    1   T 2 ILE H 235  LYS H 237  0                                        
SHEET    2   T 2 GLU H 267  ARG H 269 -1  O  GLY H 268   N  ILE H 236           
SHEET    1   U 7 PRO H 300  ILE H 310  0                                        
SHEET    2   U 7 ASN H 355  ALA H 367 -1  O  LEU H 362   N  THR H 302           
SHEET    3   U 7 THR H 335  GLU H 342 -1  N  GLU H 342   O  VAL H 359           
SHEET    4   U 7 GLN H 329  PHE H 332 -1  N  PHE H 330   O  VAL H 337           
SHEET    5   U 7 ARG H 373  GLU H 378 -1  O  ALA H 375   N  TYR H 331           
SHEET    6   U 7 ARG H 381  VAL H 391 -1  O  GLY H 384   N  ILE H 376           
SHEET    7   U 7 PRO H 300  ILE H 310 -1  N  TYR H 309   O  ALA H 385           
SHEET    1   V 2 PHE H 322  PHE H 323  0                                        
SHEET    2   V 2 MET H 349  VAL H 350 -1  O  VAL H 350   N  PHE H 322           
SHEET    1   W12 ILE J 169  ARG J 171  0                                        
SHEET    2   W12 ILE J 130  ASN J 135  1  N  LEU J 134   O  VAL J 170           
SHEET    3   W12 ALA J 101  ALA J 106  1  N  ALA J 101   O  ILE J 131           
SHEET    4   W12 HIS I  11  ILE I  17  1  N  GLY I  15   O  ILE J 102           
SHEET    5   W12 HIS J  75  ASP J  80  1  O  ALA J  77   N  VAL I  14           
SHEET    6   W12 THR J  64  ASP J  70 -1  N  TYR J  69   O  TYR J  76           
SHEET    7   W12 THR L  64  ASP L  70 -1  O  THR L  64   N  HIS J  66           
SHEET    8   W12 HIS L  75  ASP L  80 -1  O  TYR L  76   N  TYR L  69           
SHEET    9   W12 HIS K  11  ILE K  17  1  N  VAL K  14   O  ALA L  77           
SHEET   10   W12 ALA L 101  ALA L 106  1  O  ILE L 102   N  GLY K  15           
SHEET   11   W12 ILE L 130  ASN L 135  1  O  ILE L 131   N  LEU L 103           
SHEET   12   W12 ILE L 169  ARG L 171  1  O  VAL L 170   N  LEU L 134           
SHEET    1   X 7 LEU J 211  PRO J 213  0                                        
SHEET    2   X 7 VAL J 291  ALA J 293 -1  O  LEU J 292   N  LEU J 212           
SHEET    3   X 7 GLU J 241  VAL J 245 -1  N  GLU J 243   O  ALA J 293           
SHEET    4   X 7 GLN J 251  MET J 260 -1  O  GLN J 251   N  ILE J 244           
SHEET    5   X 7 ASN J 273  LEU J 278 -1  O  LEU J 277   N  GLY J 257           
SHEET    6   X 7 GLY J 224  ARG J 230 -1  N  VAL J 227   O  VAL J 276           
SHEET    7   X 7 ASP J 216  ILE J 220 -1  N  PHE J 218   O  VAL J 226           
SHEET    1   Y 5 LEU J 211  PRO J 213  0                                        
SHEET    2   Y 5 VAL J 291  ALA J 293 -1  O  LEU J 292   N  LEU J 212           
SHEET    3   Y 5 GLU J 241  VAL J 245 -1  N  GLU J 243   O  ALA J 293           
SHEET    4   Y 5 GLN J 251  MET J 260 -1  O  GLN J 251   N  ILE J 244           
SHEET    5   Y 5 LYS J 263  LEU J 265 -1  O  LEU J 265   N  VAL J 258           
SHEET    1   Z 2 ILE J 235  LYS J 237  0                                        
SHEET    2   Z 2 GLU J 267  ARG J 269 -1  O  GLY J 268   N  ILE J 236           
SHEET    1  AA 7 PRO J 300  ILE J 310  0                                        
SHEET    2  AA 7 ASN J 355  ALA J 367 -1  O  LEU J 362   N  THR J 302           
SHEET    3  AA 7 THR J 335  GLU J 342 -1  N  THR J 340   O  THR J 361           
SHEET    4  AA 7 GLN J 329  PHE J 332 -1  N  PHE J 330   O  VAL J 337           
SHEET    5  AA 7 ARG J 373  GLU J 378 -1  O  ARG J 377   N  GLN J 329           
SHEET    6  AA 7 ARG J 381  VAL J 391 -1  O  VAL J 383   N  ILE J 376           
SHEET    7  AA 7 PRO J 300  ILE J 310 -1  N  TYR J 309   O  ALA J 385           
SHEET    1  AB 2 PHE J 322  PHE J 323  0                                        
SHEET    2  AB 2 MET J 349  VAL J 350 -1  O  VAL J 350   N  PHE J 322           
SHEET    1  AC 7 LEU L 211  PRO L 213  0                                        
SHEET    2  AC 7 VAL L 291  ALA L 293 -1  O  LEU L 292   N  LEU L 212           
SHEET    3  AC 7 GLU L 241  VAL L 245 -1  N  GLU L 243   O  ALA L 293           
SHEET    4  AC 7 GLN L 251  MET L 260 -1  O  GLN L 251   N  ILE L 244           
SHEET    5  AC 7 ASN L 273  LEU L 278 -1  O  LEU L 277   N  GLY L 257           
SHEET    6  AC 7 GLY L 224  ARG L 230 -1  N  VAL L 227   O  VAL L 276           
SHEET    7  AC 7 ASP L 216  ILE L 220 -1  N  PHE L 218   O  VAL L 226           
SHEET    1  AD 5 LEU L 211  PRO L 213  0                                        
SHEET    2  AD 5 VAL L 291  ALA L 293 -1  O  LEU L 292   N  LEU L 212           
SHEET    3  AD 5 GLU L 241  VAL L 245 -1  N  GLU L 243   O  ALA L 293           
SHEET    4  AD 5 GLN L 251  MET L 260 -1  O  GLN L 251   N  ILE L 244           
SHEET    5  AD 5 LYS L 263  LEU L 265 -1  O  LEU L 265   N  VAL L 258           
SHEET    1  AE 2 ILE L 235  LYS L 237  0                                        
SHEET    2  AE 2 GLU L 267  ARG L 269 -1  O  GLY L 268   N  ILE L 236           
SHEET    1  AF 7 PRO L 300  ILE L 310  0                                        
SHEET    2  AF 7 ASN L 355  ALA L 367 -1  O  LEU L 362   N  THR L 302           
SHEET    3  AF 7 THR L 335  GLU L 342 -1  N  GLU L 342   O  VAL L 359           
SHEET    4  AF 7 GLN L 329  PHE L 332 -1  N  PHE L 332   O  THR L 335           
SHEET    5  AF 7 ARG L 373  GLU L 378 -1  O  ALA L 375   N  TYR L 331           
SHEET    6  AF 7 ARG L 381  VAL L 391 -1  O  GLY L 384   N  ILE L 376           
SHEET    7  AF 7 PRO L 300  ILE L 310 -1  N  TYR L 309   O  ALA L 385           
SHEET    1  AG 2 PHE L 322  PHE L 323  0                                        
SHEET    2  AG 2 MET L 349  VAL L 350 -1  O  VAL L 350   N  PHE L 322           
LINK        MG    MG A1998                 OG1 THR A  25     1555   1555  2.33  
LINK        MG    MG A1998                 O2B GDP B1999     1555   1555  2.07  
LINK        MG    MG A1998                 O12 TAC B1888     1555   1555  2.09  
LINK        MG    MG A1998                 O   HOH B1001     1555   1555  2.16  
LINK        MG    MG A1998                 O11 TAC B1888     1555   1555  2.37  
LINK        MG    MG A1998                 O   HOH B1002     1555   1555  2.05  
LINK        MG    MG C2998                 O   HOH D2002     1555   1555  2.14  
LINK        MG    MG C2998                 O2B GDP D2999     1555   1555  2.17  
LINK        MG    MG C2998                 OG1 THR C  25     1555   1555  2.23  
LINK        MG    MG C2998                 O11 TAC D2888     1555   1555  2.19  
LINK        MG    MG C2998                 O12 TAC D2888     1555   1555  1.94  
LINK        MG    MG C2998                 O   HOH D2001     1555   1555  2.20  
LINK        MG    MG E3998                 OG1 THR E  25     1555   1555  2.44  
LINK        MG    MG E3998                 O2B GDP F3999     1555   1555  2.24  
LINK        MG    MG E3998                 O12 TAC F3888     1555   1555  2.10  
LINK        MG    MG E3998                 O11 TAC F3888     1555   1555  2.33  
LINK        MG    MG E3998                 O   HOH F3001     1555   1555  2.08  
LINK        MG    MG E3998                 O   HOH F3002     1555   1555  2.05  
LINK        MG    MG G4998                 OG1 THR G  25     1555   1555  2.44  
LINK        MG    MG G4998                 O11 TAC H4888     1555   1555  2.25  
LINK        MG    MG G4998                 O   HOH H4001     1555   1555  2.10  
LINK        MG    MG G4998                 O   HOH H4002     1555   1555  2.01  
LINK        MG    MG G4998                 O2B GDP H4999     1555   1555  2.29  
LINK        MG    MG G4998                 O12 TAC H4888     1555   1555  2.15  
LINK        MG    MG I5998                 O12 TAC J5888     1555   1555  1.96  
LINK        MG    MG I5998                 O   HOH J5002     1555   1555  2.31  
LINK        MG    MG I5998                 O   HOH J5001     1555   1555  2.14  
LINK        MG    MG I5998                 O11 TAC J5888     1555   1555  2.20  
LINK        MG    MG I5998                 O2B GDP J5999     1555   1555  2.11  
LINK        MG    MG I5998                 OG1 THR I  25     1555   1555  2.12  
LINK        MG    MG K6998                 O   HOH L6002     1555   1555  2.19  
LINK        MG    MG K6998                 O11 TAC L6888     1555   1555  2.23  
LINK        MG    MG K6998                 O   HOH L6001     1555   1555  2.14  
LINK        MG    MG K6998                 O12 TAC L6888     1555   1555  1.97  
LINK        MG    MG K6998                 O2B GDP L6999     1555   1555  2.20  
LINK        MG    MG K6998                 OG1 THR K  25     1555   1555  2.22  
SITE     1 AC1  5 THR A  25  HOH B1001  HOH B1002  TAC B1888                    
SITE     2 AC1  5 GDP B1999                                                     
SITE     1 AC2  5 THR C  25  HOH D2001  HOH D2002  TAC D2888                    
SITE     2 AC2  5 GDP D2999                                                     
SITE     1 AC3  5 THR E  25  HOH F3001  HOH F3002  TAC F3888                    
SITE     2 AC3  5 GDP F3999                                                     
SITE     1 AC4  6 THR G  25  CYS H  81  HOH H4001  HOH H4002                    
SITE     2 AC4  6 TAC H4888  GDP H4999                                          
SITE     1 AC5  5 THR I  25  HOH J5001  HOH J5002  TAC J5888                    
SITE     2 AC5  5 GDP J5999                                                     
SITE     1 AC6  5 THR K  25  HOH L6001  HOH L6002  TAC L6888                    
SITE     2 AC6  5 GDP L6999                                                     
SITE     1 AC7 16 ASP A  21  HIS A  22  GLY A  23  LYS A  24                    
SITE     2 AC7 16 THR A  25  THR A  26   MG A1998  ASN B 135                    
SITE     3 AC7 16 LYS B 136  ASP B 138  MET B 139  SER B 173                    
SITE     4 AC7 16 ALA B 174  LEU B 175  HOH B1002  TAC B1888                    
SITE     1 AC8 12 THR A  25   MG A1998  THR B  64  SER B  65                    
SITE     2 AC8 12 ASP B  80  CYS B  81  PRO B  82  HOH B1001                    
SITE     3 AC8 12 HOH B1002  HOH B1003  GDP B1999  TAC D2888                    
SITE     1 AC9 16 ASP C  21  HIS C  22  GLY C  23  LYS C  24                    
SITE     2 AC9 16 THR C  25  THR C  26   MG C2998  ASN D 135                    
SITE     3 AC9 16 LYS D 136  ASP D 138  MET D 139  SER D 173                    
SITE     4 AC9 16 ALA D 174  LEU D 175  HOH D2002  TAC D2888                    
SITE     1 BC1 11 TAC B1888  THR C  25  HOH C2003   MG C2998                    
SITE     2 BC1 11 THR D  64  SER D  65  ASP D  80  CYS D  81                    
SITE     3 BC1 11 PRO D  82  HOH D2001  GDP D2999                               
SITE     1 BC2 17 ASP E  21  HIS E  22  GLY E  23  LYS E  24                    
SITE     2 BC2 17 THR E  25  THR E  26   MG E3998  ASN F 135                    
SITE     3 BC2 17 LYS F 136  ASP F 138  MET F 139  SER F 173                    
SITE     4 BC2 17 ALA F 174  LEU F 175  HOH F3002  HOH F3114                    
SITE     5 BC2 17 TAC F3888                                                     
SITE     1 BC3 12 THR E  25   MG E3998  THR F  64  SER F  65                    
SITE     2 BC3 12 ASP F  80  CYS F  81  PRO F  82  HOH F3001                    
SITE     3 BC3 12 HOH F3003  GDP F3999  VAL H  67  TAC H4888                    
SITE     1 BC4 17 ASP G  21  HIS G  22  GLY G  23  LYS G  24                    
SITE     2 BC4 17 THR G  25  THR G  26   MG G4998  ASN H 135                    
SITE     3 BC4 17 LYS H 136  ASP H 138  MET H 139  SER H 173                    
SITE     4 BC4 17 ALA H 174  LEU H 175  HOH H4002  HOH H4115                    
SITE     5 BC4 17 TAC H4888                                                     
SITE     1 BC5 14 VAL F  67  LEU F 178  TAC F3888  THR G  25                    
SITE     2 BC5 14  MG G4998  THR H  64  SER H  65  ASP H  80                    
SITE     3 BC5 14 CYS H  81  PRO H  82  HOH H4001  HOH H4003                    
SITE     4 BC5 14 HOH H4115  GDP H4999                                          
SITE     1 BC6 16 ASP I  21  HIS I  22  GLY I  23  LYS I  24                    
SITE     2 BC6 16 THR I  25  THR I  26   MG I5998  ASN J 135                    
SITE     3 BC6 16 LYS J 136  ASP J 138  MET J 139  SER J 173                    
SITE     4 BC6 16 ALA J 174  LEU J 175  HOH J5002  TAC J5888                    
SITE     1 BC7 12 THR I  25   MG I5998  THR J  64  SER J  65                    
SITE     2 BC7 12 ASP J  80  CYS J  81  PRO J  82  HOH J5001                    
SITE     3 BC7 12 HOH J5002  HOH J5003  GDP J5999  TAC L6888                    
SITE     1 BC8 16 ASP K  21  HIS K  22  GLY K  23  LYS K  24                    
SITE     2 BC8 16 THR K  25  THR K  26   MG K6998  ASN L 135                    
SITE     3 BC8 16 LYS L 136  ASP L 138  MET L 139  SER L 173                    
SITE     4 BC8 16 ALA L 174  LEU L 175  HOH L6002  TAC L6888                    
SITE     1 BC9 12 VAL J  67  TAC J5888  THR K  25   MG K6998                    
SITE     2 BC9 12 THR L  64  SER L  65  ASP L  80  CYS L  81                    
SITE     3 BC9 12 PRO L  82  HOH L6001  HOH L6003  GDP L6999                    
CRYST1   69.710  156.060  134.830  90.00  95.38  90.00 P 1 21 1     12          
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      0.014345  0.000000  0.001351        0.00000                         
SCALE2      0.000000  0.006408  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007450        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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