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Database: PDB
Entry: 1FY6
LinkDB: 1FY6
Original site: 1FY6 
HEADER    LYASE                                   28-SEP-00   1FY6              
TITLE     AQUIFEX AEOLICUS KDO8P SYNTHASE IN COMPLEX WITH CADMIUM AND A5P       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE;                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: KDO8P SYNTHASE, PHOSPHO-2-DEHYDRO-3-DEOXYOCTONATE ALDOLASE, 
COMPND   5 3-DEOXY-D-MANNO-OCTULOSONIC ACID 8-PHOSPHATE SYNTHETASE, KDO-8-      
COMPND   6 PHOSPHATE SYNTHETASE;                                                
COMPND   7 EC: 4.1.2.16;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;                               
SOURCE   3 ORGANISM_TAXID: 63363;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PAAKDSA                                   
KEYWDS    KDO8PS, KDO8P, KDO, PEP, A5P, BETA/ALPHA BARREL, LYASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.S.DUEWEL,S.RADAEV,J.WANG,R.W.WOODARD,D.L.GATTI                      
REVDAT   5   04-OCT-17 1FY6    1       REMARK                                   
REVDAT   4   13-JUL-11 1FY6    1       VERSN                                    
REVDAT   3   24-FEB-09 1FY6    1       VERSN                                    
REVDAT   2   01-APR-03 1FY6    1       JRNL                                     
REVDAT   1   21-APR-01 1FY6    0                                                
JRNL        AUTH   H.S.DUEWEL,S.RADAEV,J.WANG,R.W.WOODARD,D.L.GATTI             
JRNL        TITL   SUBSTRATE AND METAL COMPLEXES OF                             
JRNL        TITL 2 3-DEOXY-D-MANNO-OCTULOSONATE-8-PHOSPHATE SYNTHASE FROM       
JRNL        TITL 3 AQUIFEX AEOLICUS AT 1.9-A RESOLUTION. IMPLICATIONS FOR THE   
JRNL        TITL 4 CONDENSATION MECHANISM.                                      
JRNL        REF    J.BIOL.CHEM.                  V. 276  8393 2001              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   11115499                                                     
JRNL        DOI    10.1074/JBC.M007884200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.89 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 11218917.400                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 84.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 45480                          
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) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4584                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.89                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.01                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 65.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5271                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE                    : 0.3310                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 579                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.014                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4043                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 289                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.97000                                              
REMARK   3    B22 (A**2) : 1.97000                                              
REMARK   3    B33 (A**2) : -3.94000                                             
REMARK   3    B12 (A**2) : 4.35000                                              
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) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.24                            
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) : 0.30                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.28                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.760                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.350 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.050 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.000 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.870 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 50.22                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PA                                 
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARA                                 
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : PEP_A5P_MOD4.                                  
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : PEP_A5P.TOPH                                   
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FY6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000012005.                                   
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                             : 4.8                                
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          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS HI-STAR                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SIEMENS                            
REMARK 200  DATA SCALING SOFTWARE          : SAINT                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45480                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.890                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.140                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.7                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 65.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.43                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NA-ACETATE, 6% PEG 4000, PH       
REMARK 280  4.8, VAPOR DIFFUSION, HANGING DROP AT 278K, TEMPERATURE 278.0K      
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       53.34533            
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      106.69067            
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      106.69067            
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       53.34533            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER CONSTRUCTED FROM       
REMARK 300 CHAIN A AND CHAIN B AND THEIR SYMMETRY PARTNERS GENERATED BY         
REMARK 300 APPLICATION OF THE SYMMETRY OPERATION (X=Y, Y=X, Z=-Z)               
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: 16120 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -131.0 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 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  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  2191                                                      
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     0.079                       
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      140.46   -170.92                                   
REMARK 500    SER B2015      143.93    170.37                                   
REMARK 500    SER B2042      143.09   -172.49                                   
REMARK 500    PRO B2227      -36.88    -37.75                                   
REMARK 500    ASP B2233       48.79     35.43                                   
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 HIS A1185   NE2                                                    
REMARK 620 2 GLU A1222   OE2  94.9                                              
REMARK 620 3 GLU A1222   OE1  82.0  52.8                                        
REMARK 620 4 A5P A1269   O2   76.2 123.4 157.6                                  
REMARK 620 5 ASP A1233   OD2  90.9 136.8  86.0  99.5                            
REMARK 620 6 CYS A1011   SG  165.3  86.3  87.2 115.2  78.4                      
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 HIS B2185   NE2                                                    
REMARK 620 2 ASP B2233   OD1  78.3                                              
REMARK 620 3 HOH B3094   O    75.0 117.8                                        
REMARK 620 4 GLU B2222   OE1 100.8  75.2 164.3                                  
REMARK 620 5 GLU B2222   OE2 106.7 122.6 118.6  47.5                            
REMARK 620 6 CYS B2011   SG  164.1  86.7 108.3  79.9  85.6                      
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 1268                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 2268                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 2269                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1270                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 2270                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A5P A 1269                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FWN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1FWS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1FWT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1FWW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1FX6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1FXP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1FXQ   RELATED DB: PDB                                   
DBREF  1FY6 A 1001  1267  UNP    O66496   KDSA_AQUAE       1    267             
DBREF  1FY6 B 2001  2267  UNP    O66496   KDSA_AQUAE       1    267             
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 ARG 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 ARG 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  A1268       5                                                       
HET     CD  A1270       1                                                       
HET    A5P  A1269      14                                                       
HET    PO4  B2268       5                                                       
HET    PO4  B2269       5                                                       
HET     CD  B2270       1                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      CD CADMIUM ION                                                      
HETNAM     A5P ARABINOSE-5-PHOSPHATE                                            
FORMUL   3  PO4    3(O4 P 3-)                                                   
FORMUL   4   CD    2(CD 2+)                                                     
FORMUL   5  A5P    C5 H13 O8 P                                                  
FORMUL   9  HOH   *289(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  TRP A 1132  5                                   3    
HELIX    8   8 ASP A 1133  GLY A 1144  1                                  12    
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  TRP B 2132  5                                   3    
HELIX   22  22 ASP B 2133  GLY B 2144  1                                  12    
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   A 2 THR A1156  THR A1157  0                                        
SHEET    2   A 2 LEU A1163  VAL A1164 -1  O  VAL A1164   N  THR A1156           
SHEET    1   B 2 THR B2156  THR B2157  0                                        
SHEET    2   B 2 LEU B2163  VAL B2164 -1  O  VAL B2164   N  THR B2156           
LINK        CD    CD A1270                 NE2 HIS A1185     1555   1555  2.24  
LINK        CD    CD A1270                 OE2 GLU A1222     1555   1555  2.65  
LINK        CD    CD A1270                 OE1 GLU A1222     1555   1555  2.26  
LINK        CD    CD A1270                 O2  A5P A1269     1555   1555  2.92  
LINK        CD    CD A1270                 OD2 ASP A1233     1555   1555  2.33  
LINK        CD    CD A1270                 SG  CYS A1011     1555   1555  2.72  
LINK        CD    CD B2270                 NE2 HIS B2185     1555   1555  2.17  
LINK        CD    CD B2270                 OD1 ASP B2233     1555   1555  2.28  
LINK        CD    CD B2270                 O   HOH B3094     1555   1555  2.78  
LINK        CD    CD B2270                 OE1 GLU B2222     1555   1555  2.44  
LINK        CD    CD B2270                 OE2 GLU B2222     1555   1555  2.93  
LINK        CD    CD B2270                 SG  CYS B2011     1555   1555  3.07  
SITE     1 AC1  9 PRO A1101  ALA A1102  LYS A1124  ARG A1154                    
SITE     2 AC1  9 A5P A1269  HOH A3029  HOH A3037  HOH A3039                    
SITE     3 AC1  9 HOH A3334                                                     
SITE     1 AC2 10 PRO B2101  ALA B2102  LYS B2124  ARG B2154                    
SITE     2 AC2 10 HOH B3018  HOH B3030  HOH B3052  HOH B3094                    
SITE     3 AC2 10 HOH B3116  HOH B3219                                          
SITE     1 AC3  4 ARG A1106  ARG B2049  SER B2050  HOH B3046                    
SITE     1 AC4  5 CYS A1011  HIS A1185  GLU A1222  ASP A1233                    
SITE     2 AC4  5 A5P A1269                                                     
SITE     1 AC5  5 CYS B2011  HIS B2185  GLU B2222  ASP B2233                    
SITE     2 AC5  5 HOH B3094                                                     
SITE     1 AC6 12 CYS A1011  LYS A1046  ASN A1048  ARG A1049                    
SITE     2 AC6 12 SER A1050  HIS A1185  ASP A1233  PO4 A1268                    
SITE     3 AC6 12  CD A1270  HOH A3035  HOH A3037  HOH A3200                    
CRYST1   84.671   84.671  160.036  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      0.011810  0.006819  0.000000        0.00000                         
SCALE2      0.000000  0.013638  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006249        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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