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Database: PDB
Entry: 4PC7
LinkDB: 4PC7
Original site: 4PC7 
HEADER    TRANSLATION                             14-APR-14   4PC7              
TITLE     ELONGATION FACTOR TU:TS COMPLEX IN A NEAR GTP CONFORMATION.           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR TU 1;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: EF-TU 1,P-43;                                               
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ELONGATION FACTOR TS;                                      
COMPND   8 CHAIN: C;                                                            
COMPND   9 SYNONYM: EF-TS;                                                      
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: TUFA, B3339, JW3301;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  10 ORGANISM_TAXID: 83333;                                               
SOURCE  11 STRAIN: K12;                                                         
SOURCE  12 GENE: TSF, B0170, JW0165;                                            
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    G:GEF:NUCLEOTIDE COMPLEX, ELONGATION FACTOR, TRANSLATION, PROTEIN     
KEYWDS   2 SYNTHESIS                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.S.THIRUP                                                            
REVDAT   4   07-MAR-18 4PC7    1       SOURCE JRNL   REMARK                     
REVDAT   3   15-JUL-15 4PC7    1       JRNL                                     
REVDAT   2   01-JUL-15 4PC7    1       JRNL                                     
REVDAT   1   06-MAY-15 4PC7    0                                                
JRNL        AUTH   S.S.THIRUP,L.B.VAN,T.K.NIELSEN,C.R.KNUDSEN                   
JRNL        TITL   STRUCTURAL OUTLINE OF THE DETAILED MECHANISM FOR ELONGATION  
JRNL        TITL 2 FACTOR TS-MEDIATED GUANINE NUCLEOTIDE EXCHANGE ON ELONGATION 
JRNL        TITL 3 FACTOR TU.                                                   
JRNL        REF    J.STRUCT.BIOL.                V. 191    10 2015              
JRNL        REFN                   ESSN 1095-8657                               
JRNL        PMID   26073967                                                     
JRNL        DOI    10.1016/J.JSB.2015.06.011                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1702)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 17857                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.257                           
REMARK   3   R VALUE            (WORKING SET) : 0.255                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 890                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.5014 -  6.5224    0.97     2896   149  0.1783 0.2168        
REMARK   3     2  6.5224 -  5.1862    1.00     2838   148  0.2716 0.3049        
REMARK   3     3  5.1862 -  4.5333    1.00     2833   149  0.2533 0.2559        
REMARK   3     4  4.5333 -  4.1200    1.00     2818   147  0.2890 0.3107        
REMARK   3     5  4.1200 -  3.8254    1.00     2805   151  0.3341 0.3358        
REMARK   3     6  3.8254 -  3.6003    1.00     2777   146  0.4065 0.4520        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.720            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.400           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           4961                                  
REMARK   3   ANGLE     :  0.573           6701                                  
REMARK   3   CHIRALITY :  0.026            776                                  
REMARK   3   PLANARITY :  0.002            869                                  
REMARK   3   DIHEDRAL  : 12.701           1852                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 8 THROUGH 210 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -21.6824  71.2413  58.0941              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6082 T22:   0.6170                                     
REMARK   3      T33:   1.0791 T12:  -0.0635                                     
REMARK   3      T13:   0.0803 T23:   0.1140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1288 L22:   4.0675                                     
REMARK   3      L33:   4.8933 L12:   1.4006                                     
REMARK   3      L13:   0.9957 L23:   1.9059                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1482 S12:  -0.0985 S13:   0.2015                       
REMARK   3      S21:   0.0083 S22:   0.2043 S23:  -0.1073                       
REMARK   3      S31:  -0.7466 S32:   0.2499 S33:  -0.1261                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 211 THROUGH 393 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.4385  95.7973  48.5810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8706 T22:   0.9989                                     
REMARK   3      T33:   1.5742 T12:  -0.3197                                     
REMARK   3      T13:  -0.2752 T23:   0.3280                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4501 L22:   1.3850                                     
REMARK   3      L33:   3.4063 L12:  -0.1384                                     
REMARK   3      L13:   1.9157 L23:   0.7404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5417 S12:   0.9374 S13:   1.0962                       
REMARK   3      S21:  -0.1930 S22:   0.0446 S23:   0.1218                       
REMARK   3      S31:  -1.9004 S32:   0.8342 S33:   0.5327                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 52 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   1.8614  66.3537  74.7292              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8327 T22:   1.1189                                     
REMARK   3      T33:   1.4775 T12:   0.2456                                     
REMARK   3      T13:  -0.1264 T23:  -0.0432                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2618 L22:   7.0932                                     
REMARK   3      L33:   9.3383 L12:   2.6957                                     
REMARK   3      L13:   1.2066 L23:   2.4340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2583 S12:  -1.0393 S13:  -2.2377                       
REMARK   3      S21:   0.2813 S22:   0.2520 S23:  -1.1480                       
REMARK   3      S31:   0.2666 S32:  -0.5322 S33:  -0.4315                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 53 THROUGH 163 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.5055  94.3023  90.0731              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4139 T22:   0.7186                                     
REMARK   3      T33:   1.3617 T12:  -0.1859                                     
REMARK   3      T13:  -0.2770 T23:  -0.1157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1555 L22:   2.4555                                     
REMARK   3      L33:   7.7116 L12:  -3.0258                                     
REMARK   3      L13:  -1.4195 L23:   0.1240                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7778 S12:  -0.0864 S13:   0.7655                       
REMARK   3      S21:  -0.4107 S22:   0.5179 S23:   0.3355                       
REMARK   3      S31:  -0.7733 S32:   0.1892 S33:   0.2366                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 164 THROUGH 266 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0410  84.3038  72.4258              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2629 T22:   1.8424                                     
REMARK   3      T33:   1.3395 T12:  -0.1192                                     
REMARK   3      T13:  -0.0331 T23:   0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1893 L22:   6.1034                                     
REMARK   3      L33:   2.2463 L12:   0.2230                                     
REMARK   3      L13:  -0.2230 L23:   1.7457                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2563 S12:   1.1603 S13:  -0.2013                       
REMARK   3      S21:  -0.6917 S22:  -0.2204 S23:  -0.5651                       
REMARK   3      S31:  -0.5448 S32:   1.4075 S33:   0.0137                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4PC7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000201136.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-APR-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17862                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.11600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS, 1.8M (NH4)2SO4, 0.5MM        
REMARK 280  GDPNP, 0.15MM PULVOMYCIN, 10MM MGCL2, PH 7.5, VAPOR DIFFUSION,      
REMARK 280  SITTING DROP, TEMPERATURE 292K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      115.55333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       57.77667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       57.77667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      115.55333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     PHE A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     ALA A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     ARG A    44                                                      
REMARK 465     ALA A    45                                                      
REMARK 465     PHE A    46                                                      
REMARK 465     ASP A    47                                                      
REMARK 465     GLN A    48                                                      
REMARK 465     ILE A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     ASN A    51                                                      
REMARK 465     ALA A    52                                                      
REMARK 465     PRO A    53                                                      
REMARK 465     GLU A    54                                                      
REMARK 465     GLU A    55                                                      
REMARK 465     LYS A    56                                                      
REMARK 465     ALA A    57                                                      
REMARK 465     ARG A    58                                                      
REMARK 465     GLY A    59                                                      
REMARK 465     ILE A    60                                                      
REMARK 465     MET C   202                                                      
REMARK 465     GLN C   203                                                      
REMARK 465     SER C   204                                                      
REMARK 465     GLY C   205                                                      
REMARK 465     LYS C   206                                                      
REMARK 465     VAL C   267                                                      
REMARK 465     GLU C   268                                                      
REMARK 465     THR C   269                                                      
REMARK 465     ASP C   270                                                      
REMARK 465     PHE C   271                                                      
REMARK 465     ALA C   272                                                      
REMARK 465     ALA C   273                                                      
REMARK 465     GLU C   274                                                      
REMARK 465     VAL C   275                                                      
REMARK 465     ALA C   276                                                      
REMARK 465     ALA C   277                                                      
REMARK 465     MET C   278                                                      
REMARK 465     SER C   279                                                      
REMARK 465     LYS C   280                                                      
REMARK 465     GLN C   281                                                      
REMARK 465     SER C   282                                                      
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   9       93.30     59.26                                   
REMARK 500    ILE A  17      143.75   -170.27                                   
REMARK 500    ASP A  21       47.56     15.97                                   
REMARK 500    TYR A  39     -117.32   -125.96                                   
REMARK 500    SER A  65       99.63    -56.73                                   
REMARK 500    TYR A  87       41.80    -90.33                                   
REMARK 500    LYS A  89      -73.54    -69.90                                   
REMARK 500    VAL A 125       66.38   -104.33                                   
REMARK 500    VAL A 127       84.05     49.87                                   
REMARK 500    TYR A 160       42.80    -91.25                                   
REMARK 500    PRO A 163       71.38    -61.13                                   
REMARK 500    ASP A 181       87.77     57.76                                   
REMARK 500    PRO A 202       48.07    -83.33                                   
REMARK 500    ALA A 205      -50.23   -159.64                                   
REMARK 500    ILE A 206     -141.79    -78.26                                   
REMARK 500    GLU A 243       81.34   -159.92                                   
REMARK 500    ILE A 247      -62.23     21.83                                   
REMARK 500    LYS A 248     -119.98   -101.78                                   
REMARK 500    PHE A 261      -85.09     56.39                                   
REMARK 500    GLU A 267     -105.51   -114.84                                   
REMARK 500    VAL A 274     -161.74   -129.75                                   
REMARK 500    LYS A 282     -163.08   -101.95                                   
REMARK 500    PRO A 295       96.78    -50.81                                   
REMARK 500    THR A 297      -60.71   -129.09                                   
REMARK 500    VAL A 308      104.34     62.54                                   
REMARK 500    SER A 312     -166.71   -113.07                                   
REMARK 500    PHE A 323     -158.41   -131.65                                   
REMARK 500    LYS A 324       38.82    -85.05                                   
REMARK 500    PRO A 328     -151.16    -88.51                                   
REMARK 500    ARG A 333     -113.88     54.01                                   
REMARK 500    THR A 340     -159.61   -103.34                                   
REMARK 500    GLU A 342       91.45   -161.37                                   
REMARK 500    GLU A 345       99.47    -65.64                                   
REMARK 500    GLU A 348       -8.84   -140.94                                   
REMARK 500    PRO A 352       88.49    -51.68                                   
REMARK 500    ASN A 355       70.45   -164.49                                   
REMARK 500    PHE A 374     -166.53   -123.29                                   
REMARK 500    ARG A 381      104.30    -58.57                                   
REMARK 500    ALA A 389      -71.31    -72.68                                   
REMARK 500    LEU A 392      -93.51   -134.86                                   
REMARK 500    GLU C   2     -112.91   -134.47                                   
REMARK 500    ALA C  48      -97.14     50.43                                   
REMARK 500    ALA C  57     -161.92   -102.57                                   
REMARK 500    ASP C  66       80.76   -154.20                                   
REMARK 500    CYS C  77     -134.73   -110.44                                   
REMARK 500    GLN C  78      -99.95   -122.71                                   
REMARK 500    ALA C  86       -8.76     66.40                                   
REMARK 500    ASP C 161     -169.65    -75.15                                   
REMARK 500    ALA C 174      -88.55    -79.50                                   
REMARK 500    GLU C 178      -16.55   -163.68                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      59 RAMACHANDRAN OUTLIERS.                        
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 A 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  25   OG1                                                    
REMARK 620 2 ASP A  80   OD2  70.4                                              
REMARK 620 3 GNP A 401   O1G 107.0 147.8                                        
REMARK 620 4 GNP A 401   O2G 131.1 142.5  64.1                                  
REMARK 620 5 GNP A 401   O1B  58.2 122.9  75.3  73.6                            
REMARK 620 6 HOH A 501   O    54.5 112.2  53.1 104.6  55.2                      
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 GNP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PUL A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 403                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4PC1   RELATED DB: PDB                                   
REMARK 900 CONTAINS THE TU:TS COMPLEX IN THE GDP LIKE CONFORMATION.             
REMARK 900 RELATED ID: 4PC2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PC3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4PC6   RELATED DB: PDB                                   
DBREF  4PC7 A    0   393  UNP    P0CE47   EFTU1_ECOLI      1    394             
DBREF  4PC7 C    1   282  UNP    P0A6P1   EFTS_ECOLI       2    283             
SEQRES   1 A  394  MET SER LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL          
SEQRES   2 A  394  ASN VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR          
SEQRES   3 A  394  THR LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR          
SEQRES   4 A  394  TYR GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN          
SEQRES   5 A  394  ALA PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR          
SEQRES   6 A  394  SER HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA          
SEQRES   7 A  394  HIS VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN          
SEQRES   8 A  394  MET ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU          
SEQRES   9 A  394  VAL VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG          
SEQRES  10 A  394  GLU HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR          
SEQRES  11 A  394  ILE ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP          
SEQRES  12 A  394  GLU GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU          
SEQRES  13 A  394  LEU LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO          
SEQRES  14 A  394  ILE VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP          
SEQRES  15 A  394  ALA GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE          
SEQRES  16 A  394  LEU ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP          
SEQRES  17 A  394  LYS PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE          
SEQRES  18 A  394  SER GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG          
SEQRES  19 A  394  GLY ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY          
SEQRES  20 A  394  ILE LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU          
SEQRES  21 A  394  MET PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU          
SEQRES  22 A  394  ASN VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU          
SEQRES  23 A  394  ILE GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE          
SEQRES  24 A  394  LYS PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU          
SEQRES  25 A  394  SER LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS          
SEQRES  26 A  394  GLY TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL          
SEQRES  27 A  394  THR GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL          
SEQRES  28 A  394  MET PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE          
SEQRES  29 A  394  HIS PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE          
SEQRES  30 A  394  ARG GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA          
SEQRES  31 A  394  LYS VAL LEU GLY                                              
SEQRES   1 C  282  ALA GLU ILE THR ALA SER LEU VAL LYS GLU LEU ARG GLU          
SEQRES   2 C  282  ARG THR GLY ALA GLY MET MET ASP CYS LYS LYS ALA LEU          
SEQRES   3 C  282  THR GLU ALA ASN GLY ASP ILE GLU LEU ALA ILE GLU ASN          
SEQRES   4 C  282  MET ARG LYS SER GLY ALA ILE LYS ALA ALA LYS LYS ALA          
SEQRES   5 C  282  GLY ASN VAL ALA ALA ASP GLY VAL ILE LYS THR LYS ILE          
SEQRES   6 C  282  ASP GLY ASN TYR GLY ILE ILE LEU GLU VAL ASN CYS GLN          
SEQRES   7 C  282  THR ASP PHE VAL ALA LYS ASP ALA GLY PHE GLN ALA PHE          
SEQRES   8 C  282  ALA ASP LYS VAL LEU ASP ALA ALA VAL ALA GLY LYS ILE          
SEQRES   9 C  282  THR ASP VAL GLU VAL LEU LYS ALA GLN PHE GLU GLU GLU          
SEQRES  10 C  282  ARG VAL ALA LEU VAL ALA LYS ILE GLY GLU ASN ILE ASN          
SEQRES  11 C  282  ILE ARG ARG VAL ALA ALA LEU GLU GLY ASP VAL LEU GLY          
SEQRES  12 C  282  SER TYR GLN HIS GLY ALA ARG ILE GLY VAL LEU VAL ALA          
SEQRES  13 C  282  ALA LYS GLY ALA ASP GLU GLU LEU VAL LYS HIS ILE ALA          
SEQRES  14 C  282  MET HIS VAL ALA ALA SER LYS PRO GLU PHE ILE LYS PRO          
SEQRES  15 C  282  GLU ASP VAL SER ALA GLU VAL VAL GLU LYS GLU TYR GLN          
SEQRES  16 C  282  VAL GLN LEU ASP ILE ALA MET GLN SER GLY LYS PRO LYS          
SEQRES  17 C  282  GLU ILE ALA GLU LYS MET VAL GLU GLY ARG MET LYS LYS          
SEQRES  18 C  282  PHE THR GLY GLU VAL SER LEU THR GLY GLN PRO PHE VAL          
SEQRES  19 C  282  MET GLU PRO SER LYS THR VAL GLY GLN LEU LEU LYS GLU          
SEQRES  20 C  282  HIS ASN ALA GLU VAL THR GLY PHE ILE ARG PHE GLU VAL          
SEQRES  21 C  282  GLY GLU GLY ILE GLU LYS VAL GLU THR ASP PHE ALA ALA          
SEQRES  22 C  282  GLU VAL ALA ALA MET SER LYS GLN SER                          
HET    GNP  A 401      32                                                       
HET    PUL  A 402      60                                                       
HET     MG  A 403       1                                                       
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
HETNAM     PUL (1S,2S,3E,5E,7E,10S,11S,12S)-12-[(2R,4E,6E,8Z,10R,12E,           
HETNAM   2 PUL  14E,16Z,18S,19Z)-10,18-DIHYDROXY-12,16,19-TRIMETHYL-            
HETNAM   3 PUL  11,22-DIOXOOXACYCLODOCOSA-4,6,8,12,14,16,19-HEPTAEN-2-          
HETNAM   4 PUL  YL]-2,11-DIHYDROXY-1,10-DIMETHYL-9-OXOTRIDECA-3,5,7-            
HETNAM   5 PUL  TRIEN-1-YL 6-DEOXY-2,4-DI-O-METHYL-BETA-L-                      
HETNAM   6 PUL  GALACTOPYRANOSIDE                                               
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     PUL PULVOMYCIN                                                       
FORMUL   3  GNP    C10 H17 N6 O13 P3                                            
FORMUL   4  PUL    C47 H66 O13                                                  
FORMUL   5   MG    MG 2+                                                        
FORMUL   6  HOH   *(H2 O)                                                       
HELIX    1 AA1 GLY A   23  LYS A   37  1                                  15    
HELIX    2 AA2 VAL A   88  MET A   98  1                                  11    
HELIX    3 AA3 MET A  112  VAL A  125  1                                  14    
HELIX    4 AA4 LYS A  136  VAL A  140  5                                   5    
HELIX    5 AA5 ASP A  142  TYR A  160  1                                  19    
HELIX    6 AA6 PRO A  163  THR A  167  5                                   5    
HELIX    7 AA7 ALA A  174  GLU A  179  1                                   6    
HELIX    8 AA8 ASP A  181  TYR A  198  1                                  18    
HELIX    9 AA9 THR C    4  ARG C   14  1                                  11    
HELIX   10 AB1 GLY C   18  ALA C   29  1                                  12    
HELIX   11 AB2 ASP C   32  SER C   43  1                                  12    
HELIX   12 AB3 PHE C   81  ASP C   85  5                                   5    
HELIX   13 AB4 GLY C   87  LYS C  103  1                                  17    
HELIX   14 AB5 ASP C  106  PHE C  114  1                                   9    
HELIX   15 AB6 PHE C  114  GLY C  126  1                                  13    
HELIX   16 AB7 GLU C  163  SER C  175  1                                  13    
HELIX   17 AB8 LYS C  181  VAL C  185  5                                   5    
HELIX   18 AB9 SER C  186  ASP C  199  1                                  14    
HELIX   19 AC1 ALA C  211  SER C  227  1                                  17    
SHEET    1 AA1 6 VAL A  67  ASP A  70  0                                        
SHEET    2 AA1 6 HIS A  75  HIS A  78 -1  O  HIS A  78   N  VAL A  67           
SHEET    3 AA1 6 HIS A  11  GLY A  18  1  N  VAL A  14   O  ALA A  77           
SHEET    4 AA1 6 GLY A 100  ALA A 106  1  O  VAL A 104   N  ILE A  17           
SHEET    5 AA1 6 TYR A 129  ASN A 135  1  O  PHE A 133   N  LEU A 103           
SHEET    6 AA1 6 ILE A 169  VAL A 170  1  O  VAL A 170   N  LEU A 134           
SHEET    1 AA2 2 LEU A 211  PRO A 213  0                                        
SHEET    2 AA2 2 VAL A 291  ALA A 293 -1  O  LEU A 292   N  LEU A 212           
SHEET    1 AA3 5 VAL A 217  ILE A 220  0                                        
SHEET    2 AA3 5 GLY A 224  ARG A 230 -1  O  VAL A 226   N  PHE A 218           
SHEET    3 AA3 5 ASN A 273  LEU A 278 -1  O  VAL A 276   N  VAL A 227           
SHEET    4 AA3 5 CYS A 255  MET A 260 -1  N  THR A 256   O  LEU A 277           
SHEET    5 AA3 5 LYS A 263  LEU A 265 -1  O  LYS A 263   N  MET A 260           
SHEET    1 AA4 3 MET A 358  MET A 368  0                                        
SHEET    2 AA4 3 LYS A 299  SER A 306 -1  N  THR A 302   O  LEU A 362           
SHEET    3 AA4 3 VAL A 388  VAL A 391 -1  O  ALA A 389   N  GLU A 305           
SHEET    1 AA5 3 THR A 335  VAL A 337  0                                        
SHEET    2 AA5 3 GLN A 329  PHE A 332 -1  N  PHE A 330   O  VAL A 337           
SHEET    3 AA5 3 ALA A 375  ARG A 377 -1  O  ALA A 375   N  TYR A 331           
SHEET    1 AA6 3 GLY C  59  LYS C  64  0                                        
SHEET    2 AA6 3 TYR C  69  ASN C  76 -1  O  VAL C  75   N  VAL C  60           
SHEET    3 AA6 3 ASN C 130  GLU C 138 -1  O  ASN C 130   N  ASN C  76           
SHEET    1 AA7 3 VAL C 141  HIS C 147  0                                        
SHEET    2 AA7 3 ILE C 151  ALA C 157 -1  O  ALA C 157   N  VAL C 141           
SHEET    3 AA7 3 VAL C 252  GLU C 259 -1  O  PHE C 258   N  GLY C 152           
LINK         OG1 THR A  25                MG    MG A 403     1555   1555  2.38  
LINK         OD2 ASP A  80                MG    MG A 403     1555   1555  2.96  
LINK         O1G GNP A 401                MG    MG A 403     1555   1555  2.13  
LINK         O2G GNP A 401                MG    MG A 403     1555   1555  2.62  
LINK         O1B GNP A 401                MG    MG A 403     1555   1555  2.86  
LINK        MG    MG A 403                 O   HOH A 501     1555   1555  2.78  
SITE     1 AC1 18 VAL A  20  ASP A  21  HIS A  22  GLY A  23                    
SITE     2 AC1 18 LYS A  24  THR A  25  THR A  26  PRO A  82                    
SITE     3 AC1 18 GLY A  83  ASN A 135  LYS A 136  ASP A 138                    
SITE     4 AC1 18 MET A 139  SER A 173  ALA A 174  LEU A 175                    
SITE     5 AC1 18  MG A 403  HOH A 501                                          
SITE     1 AC2 21 ILE A  92  THR A  93  GLN A  97  GLN A 124                    
SITE     2 AC2 21 VAL A 125  PRO A 213  GLU A 215  THR A 228                    
SITE     3 AC2 21 GLY A 229  ARG A 230  GLU A 259  PHE A 261                    
SITE     4 AC2 21 ARG A 262  ASN A 273  VAL A 274  TYR A 331                    
SITE     5 AC2 21 ARG A 333  THR A 334  ARG A 373  ALA A 375                    
SITE     6 AC2 21 ARG A 377                                                     
SITE     1 AC3  5 THR A  25  ASP A  80  CYS A  81  GNP A 401                    
SITE     2 AC3  5 HOH A 501                                                     
CRYST1  122.820  122.820  173.330  90.00  90.00 120.00 P 32 2 1      6          
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      0.008142  0.004701  0.000000        0.00000                         
SCALE2      0.000000  0.009402  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005769        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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