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Database: PDB
Entry: 1D8T
LinkDB: 1D8T
Original site: 1D8T 
HEADER    HYDROLASE/ANTIBIOTIC                    25-OCT-99   1D8T              
TITLE     CRYSTAL STRUCTURE OF ELONGATION FACTOR, TU (EF-TU-MGGDP) COMPLEXED    
TITLE    2 WITH GE2270A, A THIAZOLYL PEPTIDE ANTIBIOTIC                         
CAVEAT     1D8T    BB8 D 8 HAS WRONG CHIRALITY AT ATOM CB, BB8 C 8 HAS WRONG    
CAVEAT   2 1D8T     CHIRALITY AT ATOM CB                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR TU;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: THIOCILLIN GE2270;                                         
COMPND   6 CHAIN: C, D;                                                         
COMPND   7 SYNONYM: GE2270A                                                     
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: PLANOBISPORA ROSEA;                             
SOURCE   6 ORGANISM_TAXID: 35762                                                
KEYWDS    HYDROLASE-ANTIBIOTIC COMPLEX, THIOPEPTIDE, ANTIBIOTIC, ANTIBACTERIAL, 
KEYWDS   2 THIAZOLE, OXAZOLE, HYDROLASE, GTPASE, TRANSLATION ELONGATION FACTOR, 
KEYWDS   3 PROTEIN SYNTHESIS, NUCLEOTIDE-BINDING, PHOSPHORYLATION               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.E.HEFFRON,F.JURNAK                                                  
REVDAT   6   18-APR-12 1D8T    1       COMPND                                   
REVDAT   5   27-JUL-11 1D8T    1       REMARK REVDAT                            
REVDAT   4   13-JUL-11 1D8T    1       VERSN                                    
REVDAT   3   24-FEB-09 1D8T    1       VERSN                                    
REVDAT   2   01-APR-03 1D8T    1       JRNL                                     
REVDAT   1   25-OCT-00 1D8T    0                                                
JRNL        AUTH   S.E.HEFFRON,F.JURNAK                                         
JRNL        TITL   STRUCTURE OF AN EF-TU COMPLEX WITH A THIAZOLYL PEPTIDE       
JRNL        TITL 2 ANTIBIOTIC DETERMINED AT 2.35 A RESOLUTION: ATOMIC BASIS FOR 
JRNL        TITL 3 GE2270A INHIBITION OF EF-TU.                                 
JRNL        REF    BIOCHEMISTRY                  V.  39    37 2000              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10625477                                                     
JRNL        DOI    10.1021/BI9913597                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 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) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.44                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1817617.550                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 31214                          
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) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2178                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.50                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 71.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3923                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE                    : 0.2880                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.40                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 314                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6156                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 178                                     
REMARK   3   SOLVENT ATOMS            : 379                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.75                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.79000                                             
REMARK   3    B22 (A**2) : 8.08000                                              
REMARK   3    B33 (A**2) : -3.29000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.54000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.20                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.31                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.29                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.91                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.420 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.250 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.320 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.390 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 56.13                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : GDP96_CNS.PARAM                                
REMARK   3  PARAMETER FILE  5  : PARAM_ED6.GE                                   
REMARK   3  PARAMETER FILE  6  : ACETATE.PARAM                                  
REMARK   3  PARAMETER FILE  7  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : GDP96_CNS.TOP                                  
REMARK   3  TOPOLOGY FILE  5   : TOPH_ED5.GE                                    
REMARK   3  TOPOLOGY FILE  6   : ACETATE.TOP                                    
REMARK   3  TOPOLOGY FILE  7   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: SOME NCS RESTRAINTS WERE APPLIED DURING   
REMARK   3  REFINEMENT.                                                         
REMARK   4                                                                      
REMARK   4 1D8T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB009897.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUN-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : MOSFLM, CCP4 (SCALA, TRUNCATE)     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31214                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.440                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -4.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.3                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : 0.03200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.10800                            
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: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL, MAGNESIUM CHLORIDE, GDP,       
REMARK 280  POLYETHYLENE GLYCOL 3350, AMMONIUM ACETATE, AMMONIUM CITRATE, PH    
REMARK 280  7.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       66.73500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.58500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       66.73500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.58500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA 1.18                                             
REMARK 350 TOTAL BURIED SURFACE AREA: 5710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA 1.18                                             
REMARK 350 TOTAL BURIED SURFACE AREA: 3740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2007  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A2003  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 GEA2270A IS A MEMBER OF A SULPHUR-RICH HETEROCYCLIC PEPTIDES         
REMARK 400 CLASS. ALL MEMBERS SHARE A MACROCYLIC CORE, CONSISTING OF A          
REMARK 400 NITROGEN CONTAINING, SIX-MEMBERED RING CENTRAL TO DEHYDROAMINO       
REMARK 400 ACIDS AND A SUBSET OF FIVE MEMBER RING STRUCTURES INCLUDING          
REMARK 400 THIAZOLES, THIAZOLINES AND OXAZOLES.                                 
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: GEA2270A                                                     
REMARK 400   CHAIN: C, D                                                        
REMARK 400   COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 1 TO 15                
REMARK 400   DESCRIPTION: GEA2270A IS A THIOPEPTIDE CONSISTING OF ONE           
REMARK 400                PYRIDINE, ONE OXAZOLE AND FIVE THIAZOLE RINGS.        
REMARK 400                THE OBSERVED C-TERMINAL AMINO GROUP NH2(15) IS        
REMARK 400                LIKELY TO BE A POST-TRANSLATIONAL DECARBOXYLATED      
REMARK 400                REMNANT OF A SER C-TERMINAL RESIDUE.                  
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     SER B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     PHE B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     ARG B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER C   1    N    O    OG                                        
REMARK 470     MEN C   3    O                                                   
REMARK 470     VAL C   5    O                                                   
REMARK 470     BB9 C   9    O                                                   
REMARK 470     BB9 C  10    O                                                   
REMARK 470     MH6 C  11    O                                                   
REMARK 470     BB9 C  12    O                                                   
REMARK 470     SER D   1    N    O    OG                                        
REMARK 470     MEN D   3    O                                                   
REMARK 470     VAL D   5    O                                                   
REMARK 470     BB9 D   9    O                                                   
REMARK 470     BB9 D  10    O                                                   
REMARK 470     MH6 D  11    O                                                   
REMARK 470     BB9 D  12    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER C   1   CA    SER C   1   CB     -0.096                       
REMARK 500    SER D   1   CA    SER D   1   CB     -0.095                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A   4       86.72    -45.71                                   
REMARK 500    ILE A 247      -78.42     62.53                                   
REMARK 500    ARG A 262       -2.22     75.47                                   
REMARK 500    ARG A 333      -59.34     65.47                                   
REMARK 500    ALA B  57       88.59   -168.36                                   
REMARK 500    ARG B  58       -4.50     65.74                                   
REMARK 500    ILE B 247      -79.12     60.62                                   
REMARK 500    PHE B 261       61.97     22.15                                   
REMARK 500    ARG B 333      -62.03     64.75                                   
REMARK 500    LEU B 392      -77.91   -109.65                                   
REMARK 500    VAL C   5      -44.40   -145.65                                   
REMARK 500    SER C  13       78.17    121.80                                   
REMARK 500    VAL D   5      -42.68   -133.62                                   
REMARK 500    SER D  13       83.23    115.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS A   4        22.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2012        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH A2014        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH A2019        DISTANCE =  7.45 ANGSTROMS                       
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 A 998  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  25   OG1                                                    
REMARK 620 2 GDP A 999   O2B  91.8                                              
REMARK 620 3 HOH A2063   O    80.8  92.6                                        
REMARK 620 4 HOH A2064   O   164.4  96.6  85.6                                  
REMARK 620 5 HOH A2218   O    93.6  88.4 174.4  99.8                            
REMARK 620 6 HOH A2018   O    83.7 174.7  83.9  87.2  94.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 998  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2013   O                                                      
REMARK 620 2 HOH B2140   O    91.2                                              
REMARK 620 3 THR B  25   OG1  81.6  95.1                                        
REMARK 620 4 GDP B 999   O2B 172.8  86.7  91.7                                  
REMARK 620 5 HOH B2006   O    91.8 170.2  76.2  89.2                            
REMARK 620 6 HOH B2141   O   100.3 103.0 161.7  86.8  85.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AG" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "BG" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
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 998                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3016                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3019                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3020                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3025                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3026                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3028                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3030                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 998                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 3008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 3009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 3011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 3012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 3014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 3015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 3018                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 3024                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 3027                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 3029                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 C 15                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 D 15                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF THIOCILIN GE2270       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF THIOCILIN GE2270       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1E9W   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THIOPEPTIDE THIOSTREPTON                        
REMARK 900 RELATED ID: 1OLN   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF THIOPEPTIDE THIOSTREPTON BINDING TO            
REMARK 900 L11 SUBSTRATE FROM 50S RIBOSOMAL RNA                                 
REMARK 900 RELATED ID: 2C77   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ELONGATION FACTOR EF-TU-GNP                 
REMARK 900 COMPLEXED WITH THIOPEPTIDE GE2270A.                                  
REMARK 900 RELATED ID: 2JQ7   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF THE COMPLEX OF THIOPEPTIDE                     
REMARK 900 THIOSTREPTON AND RIBOSOMAL L11-RNA                                   
REMARK 900 RELATED ID: 2ZJP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF NOSIHEPTIDE COMPLEXED WITH THE LARGE            
REMARK 900 RIBOSOMAL SUBUNIT OF DEINOCOCCUS RADIODURANS                         
REMARK 900 RELATED ID: 3CF5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RIBOSOMAL L11-RNA COMPLEXED WITH THE            
REMARK 900 THIOPEPTIDE THIOSTREPTON                                             
DBREF  1D8T A    1   393  UNP    P0A6N1   EFTU_ECOLI       1    393             
DBREF  1D8T B    1   393  UNP    P0A6N1   EFTU_ECOLI       1    393             
DBREF  1D8T C    1    14  UNP    Q7M0J8   THCL_PLARO       1     14             
DBREF  1D8T D    1    14  UNP    Q7M0J8   THCL_PLARO       1     14             
SEQADV 1D8T GLY A  393  UNP  P0A6N1    SER   393 CONFLICT                       
SEQADV 1D8T GLY B  393  UNP  P0A6N1    SER   393 CONFLICT                       
SEQRES   1 A  393  SER LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN          
SEQRES   2 A  393  VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR          
SEQRES   3 A  393  LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR          
SEQRES   4 A  393  GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA          
SEQRES   5 A  393  PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER          
SEQRES   6 A  393  HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS          
SEQRES   7 A  393  VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET          
SEQRES   8 A  393  ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL          
SEQRES   9 A  393  VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU          
SEQRES  10 A  393  HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE          
SEQRES  11 A  393  ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU          
SEQRES  12 A  393  GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU          
SEQRES  13 A  393  LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE          
SEQRES  14 A  393  VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA          
SEQRES  15 A  393  GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU          
SEQRES  16 A  393  ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS          
SEQRES  17 A  393  PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER          
SEQRES  18 A  393  GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY          
SEQRES  19 A  393  ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE          
SEQRES  20 A  393  LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET          
SEQRES  21 A  393  PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN          
SEQRES  22 A  393  VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE          
SEQRES  23 A  393  GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS          
SEQRES  24 A  393  PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER          
SEQRES  25 A  393  LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY          
SEQRES  26 A  393  TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR          
SEQRES  27 A  393  GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET          
SEQRES  28 A  393  PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS          
SEQRES  29 A  393  PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG          
SEQRES  30 A  393  GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS          
SEQRES  31 A  393  VAL LEU GLY                                                  
SEQRES   1 B  393  SER LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN          
SEQRES   2 B  393  VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR          
SEQRES   3 B  393  LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR          
SEQRES   4 B  393  GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA          
SEQRES   5 B  393  PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER          
SEQRES   6 B  393  HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS          
SEQRES   7 B  393  VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET          
SEQRES   8 B  393  ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL          
SEQRES   9 B  393  VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU          
SEQRES  10 B  393  HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE          
SEQRES  11 B  393  ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU          
SEQRES  12 B  393  GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU          
SEQRES  13 B  393  LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE          
SEQRES  14 B  393  VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA          
SEQRES  15 B  393  GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU          
SEQRES  16 B  393  ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS          
SEQRES  17 B  393  PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER          
SEQRES  18 B  393  GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY          
SEQRES  19 B  393  ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE          
SEQRES  20 B  393  LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET          
SEQRES  21 B  393  PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN          
SEQRES  22 B  393  VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE          
SEQRES  23 B  393  GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS          
SEQRES  24 B  393  PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER          
SEQRES  25 B  393  LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY          
SEQRES  26 B  393  TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR          
SEQRES  27 B  393  GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET          
SEQRES  28 B  393  PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS          
SEQRES  29 B  393  PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG          
SEQRES  30 B  393  GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS          
SEQRES  31 B  393  VAL LEU GLY                                                  
SEQRES   1 C   15  SER BB9 MEN BB6 VAL BB7 GLY BB8 BB9 BB9 MH6 BB9 SER          
SEQRES   2 C   15  PRO NH2                                                      
SEQRES   1 D   15  SER BB9 MEN BB6 VAL BB7 GLY BB8 BB9 BB9 MH6 BB9 SER          
SEQRES   2 D   15  PRO NH2                                                      
MODRES 1D8T BB9 C    2  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T MEN C    3  ASN  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T BB6 C    4  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T BB7 C    6  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T BB8 C    8  PHE  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T BB9 C    9  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T BB9 C   10  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T MH6 C   11  SER  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T BB9 C   12  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T BB9 D    2  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T MEN D    3  ASN  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T BB6 D    4  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T BB7 D    6  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T BB8 D    8  PHE  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T BB9 D    9  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T BB9 D   10  CYS  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T MH6 D   11  SER  POST-TRANSLATIONAL MODIFICATION                    
MODRES 1D8T BB9 D   12  CYS  POST-TRANSLATIONAL MODIFICATION                    
HET    BB9  C   2       6                                                       
HET    MEN  C   3       8                                                       
HET    BB6  C   4       7                                                       
HET    BB7  C   6       9                                                       
HET    BB8  C   8      11                                                       
HET    BB9  C   9       5                                                       
HET    BB9  C  10       5                                                       
HET    MH6  C  11       4                                                       
HET    BB9  C  12       5                                                       
HET    NH2  C  15       1                                                       
HET    BB9  D   2       6                                                       
HET    MEN  D   3       8                                                       
HET    BB6  D   4       7                                                       
HET    BB7  D   6       9                                                       
HET    BB8  D   8      11                                                       
HET    BB9  D   9       5                                                       
HET    BB9  D  10       5                                                       
HET    MH6  D  11       4                                                       
HET    BB9  D  12       5                                                       
HET    NH2  D  15       1                                                       
HET     MG  A 998       1                                                       
HET    GDP  A 999      28                                                       
HET    ACT  A3002       4                                                       
HET    ACT  A3003       4                                                       
HET    ACT  A3004       4                                                       
HET    ACT  A3005       4                                                       
HET    ACT  A3006       4                                                       
HET    ACT  A3007       4                                                       
HET    ACT  A3010       4                                                       
HET    ACT  A3013       4                                                       
HET    ACT  A3016       4                                                       
HET    ACT  A3017       4                                                       
HET    ACT  A3019       4                                                       
HET    ACT  A3020       4                                                       
HET    ACT  A3021       4                                                       
HET    ACT  A3022       4                                                       
HET    ACT  A3023       4                                                       
HET    ACT  A3025       4                                                       
HET    ACT  A3026       4                                                       
HET    ACT  A3028       4                                                       
HET    ACT  A3030       4                                                       
HET     MG  B 998       1                                                       
HET    GDP  B 999      28                                                       
HET    ACT  B3001       4                                                       
HET    ACT  B3008       4                                                       
HET    ACT  B3009       4                                                       
HET    ACT  B3011       4                                                       
HET    ACT  B3012       4                                                       
HET    ACT  B3014       4                                                       
HET    ACT  B3015       4                                                       
HET    ACT  B3018       4                                                       
HET    ACT  B3024       4                                                       
HET    ACT  B3027       4                                                       
HET    ACT  B3029       4                                                       
HETNAM     BB9 (2Z)-2-AMINO-3-SULFANYLPROP-2-ENOIC ACID                         
HETNAM     MEN N-METHYL ASPARAGINE                                              
HETNAM     BB6 (2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC ACID                          
HETNAM     BB7 (2Z)-2-AMINO-4-METHOXY-3-SULFANYLBUT-2-ENOIC ACID                
HETNAM     BB8 (2S,3S)-BETA-HYDROXY-PHENYLALANINE                               
HETNAM     MH6 3-HYDROXY-2-IMINOPROPANOIC ACID                                  
HETNAM     NH2 AMINO GROUP                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     ACT ACETATE ION                                                      
HETSYN     BB8 BETA-HYDROXY-PHENYLALANINE, THREO-BETA-HYDROXY-L-                
HETSYN   2 BB8  PHENYLALANINE, (BETAS)-BETA-HYDROXY-L-PHENYLALANINE,            
HETSYN   3 BB8  L-THREO-3-PHENYLSERINE, L-THREO-BETA-PHENYLSERINE, 3-           
HETSYN   4 BB8  HYDROXY-L-PHENYLALANINE                                         
FORMUL   3  BB9    8(C3 H5 N O2 S)                                              
FORMUL   3  MEN    2(C5 H10 N2 O3)                                              
FORMUL   3  BB6    2(C4 H7 N O2 S)                                              
FORMUL   3  BB7    2(C5 H9 N O3 S)                                              
FORMUL   3  BB8    2(C9 H11 N O3)                                               
FORMUL   3  MH6    2(C3 H5 N O3)                                                
FORMUL   3  NH2    2(H2 N)                                                      
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   6  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL   7  ACT    30(C2 H3 O2 1-)                                              
FORMUL  39  HOH   *379(H2 O)                                                    
HELIX    1   1 GLY A   23  GLY A   40  1                                  18    
HELIX    2   2 ALA A   45  ASN A   51  1                                   7    
HELIX    3   3 GLY A   83  GLY A   94  1                                  12    
HELIX    4   4 MET A  112  GLY A  126  1                                  15    
HELIX    5   5 LYS A  136  VAL A  140  5                                   5    
HELIX    6   6 ASP A  142  TYR A  160  1                                  19    
HELIX    7   7 PRO A  163  THR A  167  5                                   5    
HELIX    8   8 SER A  173  GLU A  179  1                                   7    
HELIX    9   9 ASP A  181  ILE A  199  1                                  19    
HELIX   10  10 ARG A  204  LYS A  208  5                                   5    
HELIX   11  11 LYS A  282  ILE A  286  5                                   5    
HELIX   12  12 GLY B   23  GLY B   40  1                                  18    
HELIX   13  13 ALA B   45  ASN B   51  1                                   7    
HELIX   14  14 GLY B   83  GLY B   94  1                                  12    
HELIX   15  15 MET B  112  GLY B  126  1                                  15    
HELIX   16  16 LYS B  136  VAL B  140  5                                   5    
HELIX   17  17 ASP B  142  GLN B  159  1                                  18    
HELIX   18  18 PRO B  163  THR B  167  5                                   5    
HELIX   19  19 SER B  173  GLU B  179  1                                   7    
HELIX   20  20 ASP B  181  ILE B  199  1                                  19    
HELIX   21  21 ARG B  204  LYS B  208  5                                   5    
HELIX   22  22 LYS B  282  ILE B  286  5                                   5    
SHEET    1  AA 6 SER A  65  ASP A  70  0                                        
SHEET    2  AA 6 HIS A  75  ASP A  80 -1  O  TYR A  76   N  TYR A  69           
SHEET    3  AA 6 HIS A  11  ILE A  17  1  O  VAL A  12   N  ALA A  77           
SHEET    4  AA 6 ALA A 101  ALA A 106  1  O  ILE A 102   N  ILE A  17           
SHEET    5  AA 6 ILE A 130  ASN A 135  1  O  ILE A 131   N  LEU A 103           
SHEET    6  AA 6 ILE A 169  ARG A 171  1  O  VAL A 170   N  LEU A 134           
SHEET    1  AB 2 GLU A  54  ALA A  57  0                                        
SHEET    2  AB 2 ILE A  60  ASN A  63 -1  O  ILE A  60   N  ALA A  57           
SHEET    1  AC 5 LEU A 211  PRO A 213  0                                        
SHEET    2  AC 5 VAL A 291  ALA A 293 -1  O  LEU A 292   N  LEU A 212           
SHEET    3  AC 5 GLU A 241  VAL A 245 -1  O  GLU A 243   N  ALA A 293           
SHEET    4  AC 5 GLN A 251  MET A 260 -1  O  GLN A 251   N  ILE A 244           
SHEET    5  AC 5 LYS A 263  LEU A 265 -1  O  LYS A 263   N  MET A 260           
SHEET    1  AD 7 LEU A 211  PRO A 213  0                                        
SHEET    2  AD 7 VAL A 291  ALA A 293 -1  O  LEU A 292   N  LEU A 212           
SHEET    3  AD 7 GLU A 241  VAL A 245 -1  O  GLU A 243   N  ALA A 293           
SHEET    4  AD 7 GLN A 251  MET A 260 -1  O  GLN A 251   N  ILE A 244           
SHEET    5  AD 7 ASN A 273  LEU A 278 -1  O  GLY A 275   N  GLU A 259           
SHEET    6  AD 7 GLY A 224  ARG A 230 -1  O  THR A 225   N  LEU A 278           
SHEET    7  AD 7 ASP A 216  ILE A 220 -1  O  ASP A 216   N  THR A 228           
SHEET    1  AE 2 LYS A 263  LEU A 265  0                                        
SHEET    2  AE 2 GLN A 251  MET A 260 -1  O  VAL A 258   N  LEU A 265           
SHEET    1  AF 2 ILE A 235  LYS A 237  0                                        
SHEET    2  AF 2 GLU A 267  ARG A 269 -1  O  GLY A 268   N  ILE A 236           
SHEET    1  AG 7 LYS A 299  ILE A 310  0                                        
SHEET    2  AG 7 ASN A 355  MET A 368 -1  O  ILE A 356   N  VAL A 308           
SHEET    3  AG 7 THR A 335  GLU A 342 -1  O  THR A 338   N  ILE A 363           
SHEET    4  AG 7 GLN A 329  PHE A 332 -1  O  PHE A 330   N  VAL A 337           
SHEET    5  AG 7 ARG A 373  GLU A 378 -1  O  ALA A 375   N  TYR A 331           
SHEET    6  AG 7 ARG A 381  GLY A 393 -1  O  ARG A 381   N  GLU A 378           
SHEET    7  AG 7 LYS A 299  ILE A 310 -1  N  THR A 302   O  GLY A 393           
SHEET    1  AH 2 PHE A 322  PHE A 323  0                                        
SHEET    2  AH 2 MET A 349  VAL A 350 -1  O  VAL A 350   N  PHE A 322           
SHEET    1  BA 6 SER B  65  ASP B  70  0                                        
SHEET    2  BA 6 HIS B  75  ASP B  80 -1  O  TYR B  76   N  TYR B  69           
SHEET    3  BA 6 HIS B  11  ILE B  17  1  O  VAL B  12   N  ALA B  77           
SHEET    4  BA 6 GLY B 100  ALA B 106  1  O  GLY B 100   N  GLY B  15           
SHEET    5  BA 6 ILE B 130  ASN B 135  1  O  ILE B 131   N  LEU B 103           
SHEET    6  BA 6 ILE B 169  ARG B 171  1  O  VAL B 170   N  LEU B 134           
SHEET    1  BB 2 GLU B  54  GLU B  55  0                                        
SHEET    2  BB 2 ILE B  62  ASN B  63 -1  O  ILE B  62   N  GLU B  55           
SHEET    1  BC 5 LEU B 211  PRO B 213  0                                        
SHEET    2  BC 5 VAL B 291  ALA B 293 -1  O  LEU B 292   N  LEU B 212           
SHEET    3  BC 5 GLU B 241  VAL B 245 -1  O  GLU B 243   N  ALA B 293           
SHEET    4  BC 5 GLN B 251  MET B 260 -1  O  GLN B 251   N  ILE B 244           
SHEET    5  BC 5 LYS B 263  LEU B 265 -1  O  LYS B 263   N  MET B 260           
SHEET    1  BD 7 LEU B 211  PRO B 213  0                                        
SHEET    2  BD 7 VAL B 291  ALA B 293 -1  O  LEU B 292   N  LEU B 212           
SHEET    3  BD 7 GLU B 241  VAL B 245 -1  O  GLU B 243   N  ALA B 293           
SHEET    4  BD 7 GLN B 251  MET B 260 -1  O  GLN B 251   N  ILE B 244           
SHEET    5  BD 7 ASN B 273  LEU B 278 -1  O  GLY B 275   N  GLU B 259           
SHEET    6  BD 7 GLY B 224  ARG B 230 -1  O  THR B 225   N  LEU B 278           
SHEET    7  BD 7 ASP B 216  ILE B 220 -1  O  ASP B 216   N  THR B 228           
SHEET    1  BE 2 LYS B 263  LEU B 265  0                                        
SHEET    2  BE 2 GLN B 251  MET B 260 -1  O  VAL B 258   N  LEU B 265           
SHEET    1  BF 2 ILE B 235  LYS B 237  0                                        
SHEET    2  BF 2 GLU B 267  ARG B 269 -1  O  GLY B 268   N  ILE B 236           
SHEET    1  BG 7 LYS B 299  ILE B 310  0                                        
SHEET    2  BG 7 ASN B 355  MET B 368 -1  O  ILE B 356   N  VAL B 308           
SHEET    3  BG 7 THR B 335  GLU B 342 -1  O  THR B 338   N  ILE B 363           
SHEET    4  BG 7 GLN B 329  PHE B 332 -1  O  PHE B 330   N  VAL B 337           
SHEET    5  BG 7 ARG B 373  GLU B 378 -1  O  ALA B 375   N  TYR B 331           
SHEET    6  BG 7 ARG B 381  GLY B 393 -1  O  ARG B 381   N  GLU B 378           
SHEET    7  BG 7 LYS B 299  ILE B 310 -1  N  THR B 302   O  GLY B 393           
SHEET    1  BH 2 PHE B 322  PHE B 323  0                                        
SHEET    2  BH 2 MET B 349  VAL B 350 -1  O  VAL B 350   N  PHE B 322           
LINK        MG    MG A 998                 OG1 THR A  25     1555   1555  2.05  
LINK        MG    MG A 998                 O2B GDP A 999     1555   1555  2.14  
LINK        MG    MG A 998                 O   HOH A2063     1555   1555  2.13  
LINK        MG    MG A 998                 O   HOH A2064     1555   1555  2.07  
LINK        MG    MG A 998                 O   HOH A2218     1555   1555  2.21  
LINK        MG    MG A 998                 O   HOH A2018     1555   1555  2.19  
LINK        MG    MG B 998                 O   HOH B2013     1555   1555  2.41  
LINK        MG    MG B 998                 O   HOH B2140     1555   1555  2.21  
LINK        MG    MG B 998                 OG1 THR B  25     1555   1555  2.05  
LINK        MG    MG B 998                 O2B GDP B 999     1555   1555  2.27  
LINK        MG    MG B 998                 O   HOH B2006     1555   1555  2.22  
LINK        MG    MG B 998                 O   HOH B2141     1555   1555  2.36  
LINK         CB  SER C   1                 CB  MH6 C  11     1555   1555  1.41  
LINK         C   SER C   1                 N   BB9 C   2     1555   1555  1.32  
LINK         C   SER C   1                 SG  BB9 C   2     1555   1555  1.72  
LINK         CA  SER C   1                 C   BB9 C  10     1555   1555  1.46  
LINK         C   BB9 C   2                 N   MEN C   3     1555   1555  1.36  
LINK         C   MEN C   3                 SG  BB6 C   4     1555   1555  1.72  
LINK         C   MEN C   3                 N   BB6 C   4     1555   1555  1.32  
LINK         C   BB6 C   4                 N   VAL C   5     1555   1555  1.36  
LINK         C   VAL C   5                 SG  BB7 C   6     1555   1555  1.71  
LINK         C   VAL C   5                 N   BB7 C   6     1555   1555  1.33  
LINK         C   BB7 C   6                 N   GLY C   7     1555   1555  1.36  
LINK         C   GLY C   7                 N   BB8 C   8     1555   1555  1.35  
LINK         C   BB8 C   8                 SG  BB9 C   9     1555   1555  1.72  
LINK         C   BB8 C   8                 N   BB9 C   9     1555   1555  1.32  
LINK         C   BB9 C   9                 N   BB9 C  10     1555   1555  1.33  
LINK         C   BB9 C   9                 SG  BB9 C  10     1555   1555  1.70  
LINK         C   BB9 C  10                 N   MH6 C  11     1555   1555  1.34  
LINK         C   MH6 C  11                 N   BB9 C  12     1555   1555  1.33  
LINK         C   MH6 C  11                 SG  BB9 C  12     1555   1555  1.72  
LINK         C   BB9 C  12                 OG  SER C  13     1555   1555  1.35  
LINK         C   BB9 C  12                 N   SER C  13     1555   1555  1.51  
LINK         C   PRO C  14                 N   NH2 C  15     1555   1555  1.35  
LINK         CA  SER D   1                 C   BB9 D  10     1555   1555  1.47  
LINK         C   SER D   1                 SG  BB9 D   2     1555   1555  1.72  
LINK         C   SER D   1                 N   BB9 D   2     1555   1555  1.33  
LINK         CB  SER D   1                 CB  MH6 D  11     1555   1555  1.42  
LINK         C   BB9 D   2                 N   MEN D   3     1555   1555  1.36  
LINK         C   MEN D   3                 SG  BB6 D   4     1555   1555  1.71  
LINK         C   MEN D   3                 N   BB6 D   4     1555   1555  1.31  
LINK         C   BB6 D   4                 N   VAL D   5     1555   1555  1.35  
LINK         C   VAL D   5                 SG  BB7 D   6     1555   1555  1.70  
LINK         C   VAL D   5                 N   BB7 D   6     1555   1555  1.34  
LINK         C   BB7 D   6                 N   GLY D   7     1555   1555  1.38  
LINK         C   GLY D   7                 N   BB8 D   8     1555   1555  1.37  
LINK         C   BB8 D   8                 N   BB9 D   9     1555   1555  1.29  
LINK         C   BB8 D   8                 SG  BB9 D   9     1555   1555  1.74  
LINK         C   BB9 D   9                 SG  BB9 D  10     1555   1555  1.71  
LINK         C   BB9 D   9                 N   BB9 D  10     1555   1555  1.31  
LINK         C   BB9 D  10                 N   MH6 D  11     1555   1555  1.34  
LINK         C   MH6 D  11                 SG  BB9 D  12     1555   1555  1.71  
LINK         C   MH6 D  11                 N   BB9 D  12     1555   1555  1.32  
LINK         C   BB9 D  12                 OG  SER D  13     1555   1555  1.35  
LINK         C   BB9 D  12                 N   SER D  13     1555   1555  1.52  
LINK         C   PRO D  14                 N   NH2 D  15     1555   1555  1.35  
SITE     1 AC1  6 THR A  25  GDP A 999  HOH A2018  HOH A2063                    
SITE     2 AC1  6 HOH A2064  HOH A2218                                          
SITE     1 AC2 21 ASP A  21  HIS A  22  GLY A  23  LYS A  24                    
SITE     2 AC2 21 THR A  25  THR A  26  PHE A  46  ASN A 135                    
SITE     3 AC2 21 LYS A 136  ASP A 138  MET A 139  SER A 173                    
SITE     4 AC2 21 ALA A 174  LEU A 175   MG A 998  HOH A2017                    
SITE     5 AC2 21 HOH A2063  HOH A2064  HOH A2217  HOH A2218                    
SITE     6 AC2 21 HOH A2219                                                     
SITE     1 AC3  5 THR A 167  PRO A 168  ILE A 169  HOH A2115                    
SITE     2 AC3  5 ACT A3019                                                     
SITE     1 AC4  3 ARG A 123  ASP A 370  ALA A 389                               
SITE     1 AC5  4 ARG A 154  ASP A 165  SER A 221  ACT A3028                    
SITE     1 AC6  4 GLU A 152  GLU A 155  GLN A 159  HOH A2221                    
SITE     1 AC7  4 THR A 302  LEU A 362  ILE A 363  HOH A2172                    
SITE     1 AC8  2 VAL A 127  ARG A 373                                          
SITE     1 AC9  4 PRO A 113  HOH A2221  HOH A2222  ACT B3009                    
SITE     1 BC1  4 ARG A 171  TRP A 184  HOH A2223  ACT A3023                    
SITE     1 BC2  2 ILE A 247  GLU A 287                                          
SITE     1 BC3  2 VAL A 391  LEU A 392                                          
SITE     1 BC4  6 ILE A 169  VAL A 170  ARG A 171  LYS A 187                    
SITE     2 BC4  6 GLU A 190  ACT A3002                                          
SITE     1 BC5  3 GLU A   6  GLY A  94  ALA A  95                               
SITE     1 BC6  3 ASP A  50  PRO A  82  HOH A2017                               
SITE     1 BC7  2 SER A  65  HIS A  66                                          
SITE     1 BC8  7 VAL A 140  ASP A 141  ASP A 142  GLU A 143                    
SITE     2 BC8  7 LEU A 146  ACT A3013  BB9 C   2                               
SITE     1 BC9  4 TYR A 129  TYR A 198  HOH A2226  HOH A2227                    
SITE     1 CC1  2 HIS A  84  ASN A 355                                          
SITE     1 CC2  3 ILE A 220  SER A 221  ACT A3004                               
SITE     1 CC3  4 TYR A  39  LEU A 189  ALA A 192  ASP A 196                    
SITE     1 CC4  7 THR B  25  ASP B  50  GDP B 999  HOH B2006                    
SITE     2 CC4  7 HOH B2013  HOH B2140  HOH B2141                               
SITE     1 CC5 19 ASP B  21  HIS B  22  GLY B  23  LYS B  24                    
SITE     2 CC5 19 THR B  25  THR B  26  PHE B  46  ASN B 135                    
SITE     3 CC5 19 LYS B 136  ASP B 138  MET B 139  SER B 173                    
SITE     4 CC5 19 ALA B 174  LEU B 175   MG B 998  HOH B2004                    
SITE     5 CC5 19 HOH B2139  HOH B2140  HOH B2141                               
SITE     1 CC6  3 ARG B 154  ILE B 169  ACT B3008                               
SITE     1 CC7  5 VAL B 170  ARG B 171  LYS B 187  GLU B 190                    
SITE     2 CC7  5 ACT B3001                                                     
SITE     1 CC8  6 PRO A 111  ACT A3010  ARG B 318  HIS B 319                    
SITE     2 CC8  6 THR B 320  GLU B 378                                          
SITE     1 CC9  5 PHE A 323  GLU A 348  VAL B 140  ASP B 141                    
SITE     2 CC9  5 ASP B 142                                                     
SITE     1 DC1  5 GLU B 215  ARG B 288  TYR B 331  ARG B 333                    
SITE     2 DC1  5 HOH B2087                                                     
SITE     1 DC2  3 HIS B  84  GLY B 353  ASN B 355                               
SITE     1 DC3  5 GLY B  41  ALA B  42  GLU B  68  ASP B  70                    
SITE     2 DC3  5 HOH B2008                                                     
SITE     1 DC4  1 ASP B 166                                                     
SITE     1 DC5  2 GLU B 201  HOH B2144                                          
SITE     1 DC6  1 ASP B 336                                                     
SITE     1 DC7  5 TYR B  39  LEU B 189  ASP B 196  HOH B2145                    
SITE     2 DC7  5 HOH B2146                                                     
SITE     1 DC8  2 GLY A 222  PRO C  14                                          
SITE     1 DC9  3 GLY B 222  SER D  13  PRO D  14                               
SITE     1 EC1 27 THR A  73  GLU A 143  ALA A 182  GLU A 215                    
SITE     2 EC1 27 ASP A 216  GLY A 222  ARG A 223  VAL A 226                    
SITE     3 EC1 27 THR A 228  GLY A 229  ARG A 230  THR A 256                    
SITE     4 EC1 27 GLY A 257  VAL A 258  GLU A 259  PHE A 261                    
SITE     5 EC1 27 ARG A 262  ASN A 273  VAL A 274  GLY A 275                    
SITE     6 EC1 27 LEU A 277  HOH A2024  HOH A2161  ACT A3023                    
SITE     7 EC1 27 NH2 C  15  HOH C2002  HOH C2003                               
SITE     1 EC2 25 PRO B  72  THR B  73  GLU B 143  GLU B 215                    
SITE     2 EC2 25 ASP B 216  PHE B 218  ARG B 223  VAL B 226                    
SITE     3 EC2 25 THR B 228  ARG B 230  THR B 256  GLY B 257                    
SITE     4 EC2 25 VAL B 258  GLU B 259  PHE B 261  ARG B 262                    
SITE     5 EC2 25 LEU B 264  ASN B 273  VAL B 274  GLY B 275                    
SITE     6 EC2 25 LEU B 277  HOH B2097  HOH B2099  NH2 D  15                    
SITE     7 EC2 25 HOH D2001                                                     
CRYST1  133.470   45.170  144.000  90.00  94.64  90.00 C 1 2 1       8          
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      0.007492  0.000000  0.000608        0.00000                         
SCALE2      0.000000  0.022139  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006967        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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