GenomeNet

Database: PDB
Entry: 1T96
LinkDB: 1T96
Original site: 1T96 
HEADER    TRANSFERASE                             14-MAY-04   1T96              
TITLE     R106G KDO8PS WITH PEP                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE;                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PHOSPHO-2-DEHYDRO-3-DEOXYOCTONATE ALDOLASE, 3-DEOXY-D-MANNO-
COMPND   5 OCTULOSONIC ACID 8-PHOSPHATE SYNTHETASE, KDO-8-PHOSPHATE SYNTHETASE, 
COMPND   6 KDO 8-P SYNTHASE, KDOPS;                                             
COMPND   7 EC: 2.5.1.55;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;                               
SOURCE   3 ORGANISM_TAXID: 63363;                                               
SOURCE   4 GENE: KDSA, AQ_085;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLAMSID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    BETA-ALPHA-BARREL, KDO, KDO8PS, PEP, A5P, KDO8P, TRANSFERASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.L.GATTI                                                             
REVDAT   6   23-AUG-23 1T96    1       REMARK                                   
REVDAT   5   27-OCT-21 1T96    1       REMARK SEQADV LINK                       
REVDAT   4   16-NOV-11 1T96    1       HETATM                                   
REVDAT   3   13-JUL-11 1T96    1       VERSN                                    
REVDAT   2   24-FEB-09 1T96    1       VERSN                                    
REVDAT   1   14-JUN-05 1T96    0                                                
JRNL        AUTH   X.XU,J.WANG,F.KONA,P.DIVVELA,T.STEMMLER,D.L.GATTI            
JRNL        TITL   EFFECTS OF THE ARG106==>GLY MUTATION ON THE CATALYTIC AND    
JRNL        TITL 2 CONFORMATIONAL CYCLE OF AQUIFEX AEOLICUS KDO8P SYNTHASE.     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.T.BRUNGER,P.D.ADAMS,G.M.CLORE,W.L.DELANO,P.GROS,           
REMARK   1  AUTH 2 R.GROSSE-KUNSTLEVE,J.-S.JIANG,J.KUSZEWSKI,M.NILGES,          
REMARK   1  AUTH 3 N.S.PANNU,R.J.READ,L.M.RICE,T.SIMONSON,G.WARREN              
REMARK   1  TITL   CRYSTALLOGRAPHY & NMR SYSTEM: A NEW SOFTWARE SUITE FOR       
REMARK   1  TITL 2 MACROMOLECULAR STRUCTURE DETERMINATION.                      
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  54   905 1998              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   9757107                                                      
REMARK   1  DOI    10.1107/S0907444998003254                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.11                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 52248                          
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) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 5278                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.93                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 53.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3453                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5160                       
REMARK   3   BIN FREE R VALUE                    : 0.5270                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.40                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 402                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.026                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4021                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 483                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.29000                                              
REMARK   3    B22 (A**2) : 2.29000                                              
REMARK   3    B33 (A**2) : -4.58000                                             
REMARK   3    B12 (A**2) : 2.21000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
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) : 0.57                            
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) : 0.29                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.65                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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) : 3.340 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.160 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.080 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.410 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : CNS BULK SOLVENT MODEL USED                          
REMARK   3   KSOL        : 0.32                                                 
REMARK   3   BSOL        : 57.55                                                
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1T96 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAY-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000022468.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : CONFOCAL MIRRORS                   
REMARK 200  OPTICS                         : CONFOCAL MIRRORS                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)          
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55179                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.110                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY                : 3.730                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1FWN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4K, NA-ACETATE, PH 4.7, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       53.71700            
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      107.43400            
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      107.43400            
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       53.71700            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 15290 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -137.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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 A3591  LIES ON A SPECIAL POSITION.                          
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  1001                                                      
REMARK 465     GLY A  1192                                                      
REMARK 465     LEU A  1193                                                      
REMARK 465     GLY A  1194                                                      
REMARK 465     ASP A  1195                                                      
REMARK 465     LYS A  1196                                                      
REMARK 465     SER A  1197                                                      
REMARK 465     GLY A  1198                                                      
REMARK 465     PRO A  1265                                                      
REMARK 465     VAL A  1266                                                      
REMARK 465     LYS A  1267                                                      
REMARK 465     MET B  2001                                                      
REMARK 465     GLU B  2002                                                      
REMARK 465     GLY B  2192                                                      
REMARK 465     LEU B  2193                                                      
REMARK 465     GLY B  2194                                                      
REMARK 465     ASP B  2195                                                      
REMARK 465     LYS B  2196                                                      
REMARK 465     SER B  2197                                                      
REMARK 465     GLY B  2198                                                      
REMARK 465     PRO B  2265                                                      
REMARK 465     VAL B  2266                                                      
REMARK 465     LYS B  2267                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A1072   CD    GLU A1072   OE2     0.080                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A1042      138.03   -170.10                                   
REMARK 500    SER B2015      148.79    176.47                                   
REMARK 500    PHE B2033       71.19   -111.27                                   
REMARK 500    SER B2042      143.32   -173.55                                   
REMARK 500    ARG B2154       29.26   -141.66                                   
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                              CD A1270  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1011   SG                                                     
REMARK 620 2 HIS A1185   NE2 169.2                                              
REMARK 620 3 GLU A1222   OE2  89.9  88.3                                        
REMARK 620 4 GLU A1222   OE1  88.7  99.1  56.5                                  
REMARK 620 5 ASP A1233   OD2  92.8  95.2 141.3  85.0                            
REMARK 620 6 HOH A3419   O    92.4  80.6 129.7 173.7  88.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD B2270  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B2011   SG                                                     
REMARK 620 2 HIS B2185   NE2 166.5                                              
REMARK 620 3 GLU B2222   OE1  90.1 103.1                                        
REMARK 620 4 GLU B2222   OE2  90.6  95.1  53.7                                  
REMARK 620 5 ASP B2233   OD2  92.2  91.4  85.8 139.5                            
REMARK 620 6 HOH B3046   O    89.4  77.4 178.4 127.8  92.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1269                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 2269                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1270                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 2270                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP A 1268                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEP B 2268                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FWN   RELATED DB: PDB                                   
REMARK 900 WILD-TYPE KDO8PS WITH PEP                                            
REMARK 900 RELATED ID: 1T8X   RELATED DB: PDB                                   
REMARK 900 R106G KDO8PS WITH PEP AND A5P                                        
REMARK 900 RELATED ID: 1T99   RELATED DB: PDB                                   
REMARK 900 R106G KDO8PS WITHOUT SUBSTRATES                                      
DBREF  1T96 A 1001  1267  UNP    O66496   KDSA_AQUAE       1    267             
DBREF  1T96 B 2001  2267  UNP    O66496   KDSA_AQUAE       1    267             
SEQADV 1T96 GLY A 1106  UNP  O66496    ARG   106 ENGINEERED MUTATION            
SEQADV 1T96 GLY B 2106  UNP  O66496    ARG   106 ENGINEERED MUTATION            
SEQRES   1 A  267  MET GLU LYS PHE LEU VAL ILE ALA GLY PRO CYS ALA ILE          
SEQRES   2 A  267  GLU SER GLU GLU LEU LEU LEU LYS VAL GLY GLU GLU ILE          
SEQRES   3 A  267  LYS ARG LEU SER GLU LYS PHE LYS GLU VAL GLU PHE VAL          
SEQRES   4 A  267  PHE LYS SER SER PHE ASP LYS ALA ASN ARG SER SER ILE          
SEQRES   5 A  267  HIS SER PHE ARG GLY HIS GLY LEU GLU TYR GLY VAL LYS          
SEQRES   6 A  267  ALA LEU ARG LYS VAL LYS GLU GLU PHE GLY LEU LYS ILE          
SEQRES   7 A  267  THR THR ASP ILE HIS GLU SER TRP GLN ALA GLU PRO VAL          
SEQRES   8 A  267  ALA GLU VAL ALA ASP ILE ILE GLN ILE PRO ALA PHE LEU          
SEQRES   9 A  267  CYS GLY GLN THR ASP LEU LEU LEU ALA ALA ALA LYS THR          
SEQRES  10 A  267  GLY ARG ALA VAL ASN VAL LYS LYS GLY GLN PHE LEU ALA          
SEQRES  11 A  267  PRO TRP ASP THR LYS ASN VAL VAL GLU LYS LEU LYS PHE          
SEQRES  12 A  267  GLY GLY ALA LYS GLU ILE TYR LEU THR GLU ARG GLY THR          
SEQRES  13 A  267  THR PHE GLY TYR ASN ASN LEU VAL VAL ASP PHE ARG SER          
SEQRES  14 A  267  LEU PRO ILE MET LYS GLN TRP ALA LYS VAL ILE TYR ASP          
SEQRES  15 A  267  ALA THR HIS SER VAL GLN LEU PRO GLY GLY LEU GLY ASP          
SEQRES  16 A  267  LYS SER GLY GLY MET ARG GLU PHE ILE PHE PRO LEU ILE          
SEQRES  17 A  267  ARG ALA ALA VAL ALA VAL GLY CYS ASP GLY VAL PHE MET          
SEQRES  18 A  267  GLU THR HIS PRO GLU PRO GLU LYS ALA LEU SER ASP ALA          
SEQRES  19 A  267  SER THR GLN LEU PRO LEU SER GLN LEU GLU GLY ILE ILE          
SEQRES  20 A  267  GLU ALA ILE LEU GLU ILE ARG GLU VAL ALA SER LYS TYR          
SEQRES  21 A  267  TYR GLU THR ILE PRO VAL LYS                                  
SEQRES   1 B  267  MET GLU LYS PHE LEU VAL ILE ALA GLY PRO CYS ALA ILE          
SEQRES   2 B  267  GLU SER GLU GLU LEU LEU LEU LYS VAL GLY GLU GLU ILE          
SEQRES   3 B  267  LYS ARG LEU SER GLU LYS PHE LYS GLU VAL GLU PHE VAL          
SEQRES   4 B  267  PHE LYS SER SER PHE ASP LYS ALA ASN ARG SER SER ILE          
SEQRES   5 B  267  HIS SER PHE ARG GLY HIS GLY LEU GLU TYR GLY VAL LYS          
SEQRES   6 B  267  ALA LEU ARG LYS VAL LYS GLU GLU PHE GLY LEU LYS ILE          
SEQRES   7 B  267  THR THR ASP ILE HIS GLU SER TRP GLN ALA GLU PRO VAL          
SEQRES   8 B  267  ALA GLU VAL ALA ASP ILE ILE GLN ILE PRO ALA PHE LEU          
SEQRES   9 B  267  CYS GLY GLN THR ASP LEU LEU LEU ALA ALA ALA LYS THR          
SEQRES  10 B  267  GLY ARG ALA VAL ASN VAL LYS LYS GLY GLN PHE LEU ALA          
SEQRES  11 B  267  PRO TRP ASP THR LYS ASN VAL VAL GLU LYS LEU LYS PHE          
SEQRES  12 B  267  GLY GLY ALA LYS GLU ILE TYR LEU THR GLU ARG GLY THR          
SEQRES  13 B  267  THR PHE GLY TYR ASN ASN LEU VAL VAL ASP PHE ARG SER          
SEQRES  14 B  267  LEU PRO ILE MET LYS GLN TRP ALA LYS VAL ILE TYR ASP          
SEQRES  15 B  267  ALA THR HIS SER VAL GLN LEU PRO GLY GLY LEU GLY ASP          
SEQRES  16 B  267  LYS SER GLY GLY MET ARG GLU PHE ILE PHE PRO LEU ILE          
SEQRES  17 B  267  ARG ALA ALA VAL ALA VAL GLY CYS ASP GLY VAL PHE MET          
SEQRES  18 B  267  GLU THR HIS PRO GLU PRO GLU LYS ALA LEU SER ASP ALA          
SEQRES  19 B  267  SER THR GLN LEU PRO LEU SER GLN LEU GLU GLY ILE ILE          
SEQRES  20 B  267  GLU ALA ILE LEU GLU ILE ARG GLU VAL ALA SER LYS TYR          
SEQRES  21 B  267  TYR GLU THR ILE PRO VAL LYS                                  
HET    PO4  A1269       5                                                       
HET     CD  A1270       1                                                       
HET    PEP  A1268      10                                                       
HET    PO4  B2269       5                                                       
HET     CD  B2270       1                                                       
HET    PEP  B2268      10                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      CD CADMIUM ION                                                      
HETNAM     PEP PHOSPHOENOLPYRUVATE                                              
FORMUL   3  PO4    2(O4 P 3-)                                                   
FORMUL   4   CD    2(CD 2+)                                                     
FORMUL   5  PEP    2(C3 H5 O6 P)                                                
FORMUL   9  HOH   *483(H2 O)                                                    
HELIX    1   1 SER A 1015  PHE A 1033  1                                  19    
HELIX    2   2 GLY A 1059  GLY A 1075  1                                  17    
HELIX    3   3 GLU A 1084  TRP A 1086  5                                   3    
HELIX    4   4 GLN A 1087  GLU A 1093  1                                   7    
HELIX    5   5 PRO A 1101  CYS A 1105  5                                   5    
HELIX    6   6 GLN A 1107  LYS A 1116  1                                  10    
HELIX    7   7 ALA A 1130  ASP A 1133  5                                   4    
HELIX    8   8 THR A 1134  GLY A 1144  1                                  11    
HELIX    9   9 ARG A 1168  LYS A 1174  1                                   7    
HELIX   10  10 THR A 1184  GLN A 1188  5                                   5    
HELIX   11  11 MET A 1200  GLU A 1202  5                                   3    
HELIX   12  12 PHE A 1203  GLY A 1215  1                                  13    
HELIX   13  13 GLU A 1226  ALA A 1230  5                                   5    
HELIX   14  14 GLN A 1242  LYS A 1259  1                                  18    
HELIX   15  15 SER B 2015  PHE B 2033  1                                  19    
HELIX   16  16 GLY B 2059  GLY B 2075  1                                  17    
HELIX   17  17 GLU B 2084  TRP B 2086  5                                   3    
HELIX   18  18 GLN B 2087  GLU B 2093  1                                   7    
HELIX   19  19 PRO B 2101  CYS B 2105  5                                   5    
HELIX   20  20 GLN B 2107  THR B 2117  1                                  11    
HELIX   21  21 ALA B 2130  ASP B 2133  5                                   4    
HELIX   22  22 THR B 2134  GLY B 2144  1                                  11    
HELIX   23  23 ARG B 2168  LYS B 2174  1                                   7    
HELIX   24  24 THR B 2184  GLN B 2188  5                                   5    
HELIX   25  25 MET B 2200  GLU B 2202  5                                   3    
HELIX   26  26 PHE B 2203  GLY B 2215  1                                  13    
HELIX   27  27 GLU B 2226  ALA B 2230  5                                   5    
HELIX   28  28 GLN B 2242  SER B 2258  1                                  17    
HELIX   29  29 LYS B 2259  TYR B 2261  5                                   3    
SHEET    1   A10 LEU A1238  PRO A1239  0                                        
SHEET    2   A10 GLY A1218  HIS A1224  1  N  GLU A1222   O  LEU A1238           
SHEET    3   A10 LYS A1178  ASP A1182  1  N  TYR A1181   O  PHE A1220           
SHEET    4   A10 ILE A1149  GLU A1153  1  N  GLU A1153   O  ILE A1180           
SHEET    5   A10 ALA A1120  LYS A1124  1  N  VAL A1123   O  THR A1152           
SHEET    6   A10 ILE A1097  ILE A1100  1  N  ILE A1098   O  ALA A1120           
SHEET    7   A10 LYS A1077  ASP A1081  1  N  THR A1080   O  GLN A1099           
SHEET    8   A10 VAL A1036  LYS A1041  1  N  PHE A1040   O  LYS A1077           
SHEET    9   A10 PHE A1004  GLY A1009  1  N  PHE A1004   O  GLU A1037           
SHEET   10   A10 GLY A1218  HIS A1224  1  O  MET A1221   N  ILE A1007           
SHEET    1   B 2 THR A1156  THR A1157  0                                        
SHEET    2   B 2 LEU A1163  VAL A1164 -1  O  VAL A1164   N  THR A1156           
SHEET    1   C10 LEU B2238  PRO B2239  0                                        
SHEET    2   C10 GLY B2218  HIS B2224  1  N  GLU B2222   O  LEU B2238           
SHEET    3   C10 LYS B2178  ASP B2182  1  N  TYR B2181   O  PHE B2220           
SHEET    4   C10 ILE B2149  GLU B2153  1  N  GLU B2153   O  ILE B2180           
SHEET    5   C10 ALA B2120  LYS B2124  1  N  VAL B2123   O  THR B2152           
SHEET    6   C10 ILE B2097  ILE B2100  1  N  ILE B2098   O  ALA B2120           
SHEET    7   C10 LYS B2077  ASP B2081  1  N  THR B2080   O  GLN B2099           
SHEET    8   C10 VAL B2036  LYS B2041  1  N  PHE B2040   O  LYS B2077           
SHEET    9   C10 PHE B2004  GLY B2009  1  N  PHE B2004   O  GLU B2037           
SHEET   10   C10 GLY B2218  HIS B2224  1  O  MET B2221   N  ILE B2007           
SHEET    1   D 2 THR B2156  THR B2157  0                                        
SHEET    2   D 2 LEU B2163  VAL B2164 -1  O  VAL B2164   N  THR B2156           
LINK         SG  CYS A1011                CD    CD A1270     1555   1555  2.52  
LINK         NE2 HIS A1185                CD    CD A1270     1555   1555  2.51  
LINK         OE2 GLU A1222                CD    CD A1270     1555   1555  2.33  
LINK         OE1 GLU A1222                CD    CD A1270     1555   1555  2.35  
LINK         OD2 ASP A1233                CD    CD A1270     1555   1555  2.18  
LINK        CD    CD A1270                 O   HOH A3419     1555   1555  2.29  
LINK         SG  CYS B2011                CD    CD B2270     1555   1555  2.60  
LINK         NE2 HIS B2185                CD    CD B2270     1555   1555  2.44  
LINK         OE1 GLU B2222                CD    CD B2270     1555   1555  2.40  
LINK         OE2 GLU B2222                CD    CD B2270     1555   1555  2.49  
LINK         OD2 ASP B2233                CD    CD B2270     1555   1555  2.02  
LINK        CD    CD B2270                 O   HOH B3046     1555   1555  2.54  
SITE     1 AC1  7 ARG A1049  SER A1050  HOH A3111  HOH A3313                    
SITE     2 AC1  7 HOH A3345  HOH A3456  HOH A3665                               
SITE     1 AC2  6 ARG B2049  SER B2050  HOH B3063  HOH B3134                    
SITE     2 AC2  6 HOH B3169  HOH B3251                                          
SITE     1 AC3  5 CYS A1011  HIS A1185  GLU A1222  ASP A1233                    
SITE     2 AC3  5 HOH A3419                                                     
SITE     1 AC4  5 CYS B2011  HIS B2185  GLU B2222  ASP B2233                    
SITE     2 AC4  5 HOH B3046                                                     
SITE     1 AC5 14 LYS A1041  SER A1043  LYS A1046  GLN A1099                    
SITE     2 AC5 14 PRO A1101  ALA A1102  LYS A1124  ARG A1154                    
SITE     3 AC5 14 HIS A1185  PHE A1220  HOH A3024  HOH A3082                    
SITE     4 AC5 14 HOH A3107  HOH A3242                                          
SITE     1 AC6 14 LYS B2041  SER B2043  LYS B2046  GLN B2099                    
SITE     2 AC6 14 PRO B2101  ALA B2102  LYS B2124  ARG B2154                    
SITE     3 AC6 14 HIS B2185  PHE B2220  HOH B3007  HOH B3029                    
SITE     4 AC6 14 HOH B3226  HOH B3252                                          
CRYST1   85.028   85.028  161.151  90.00  90.00 120.00 P 31 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011761  0.006790  0.000000        0.00000                         
SCALE2      0.000000  0.013580  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006205        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system