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Database: PDB
Entry: 2EO5
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HEADER    TRANSFERASE                             29-MAR-07   2EO5              
TITLE     CRYSTAL STRUCTURE OF 4-AMINOBUTYRATE AMINOTRANSFERASE FROM SULFOLOBUS 
TITLE    2 TOKODAII STRAIN7                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 419AA LONG HYPOTHETICAL AMINOTRANSFERASE;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: 4-AMINOBUTYRATE AMINOTRANSFERASE;                           
COMPND   5 EC: 2.6.1.19;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SULFOLOBUS TOKODAII;                            
SOURCE   3 ORGANISM_TAXID: 273063;                                              
SOURCE   4 STRAIN: 7;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;                   
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    PLP ENZYME, AMINOTRANSFERASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL   
KEYWDS   2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN         
KEYWDS   3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSFERASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.MIZUTANI,N.KUNISHIMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS           
AUTHOR   2 INITIATIVE (RSGI)                                                    
REVDAT   3   13-JUL-11 2EO5    1       VERSN                                    
REVDAT   2   24-FEB-09 2EO5    1       VERSN                                    
REVDAT   1   02-OCT-07 2EO5    0                                                
JRNL        AUTH   H.MIZUTANI,N.KUNISHIMA                                       
JRNL        TITL   CRYSTAL STRUCTURE OF 4-AMINOBUTYRATE AMINOTRANSFERASE FROM   
JRNL        TITL 2 SULFOLOBUS TOKODAII STRAIN7                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2414482.230                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 41170                          
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) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2029                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6306                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2050                       
REMARK   3   BIN FREE R VALUE                    : 0.2400                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 312                          
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            : 3216                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 376                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.78000                                             
REMARK   3    B22 (A**2) : 0.86000                                              
REMARK   3    B33 (A**2) : 0.92000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
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) : 0.19                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.09                            
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) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.13                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.77                            
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) : 1.210 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.800 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.030 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.030 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 49.67                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : PLP_SCHIFF.PARAM                               
REMARK   3  PARAMETER FILE  5  : EDO.PARAM                                      
REMARK   3  PARAMETER FILE  6  : 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   : PLP_SCHIFF.TOP                                 
REMARK   3  TOPOLOGY FILE  5   : EDO.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2EO5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB026899.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
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                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS VII                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41187                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.34100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.680                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1SF2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25%(W/V) PEG 3350, 0.1M TRIS-HCL, 0.2M   
REMARK 280  AMMONIUM SULFATE, PH 8.5, MICROBATCH, TEMPERATURE 295K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       44.02300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.58500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       66.23150            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       44.02300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.58500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       66.23150            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       44.02300            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.58500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       66.23150            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       44.02300            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       45.58500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       66.23150            
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: 24540 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 52030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -183.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       91.17000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000       91.17000            
REMARK 350   BIOMT3   4  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 A1329  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1330  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     PRO A   303                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     MET A   305                                                      
REMARK 465     HIS A   306                                                      
REMARK 465     SER A   307                                                      
REMARK 465     ASN A   308                                                      
REMARK 465     LYS A   419                                                      
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    ASN A  54       44.12   -108.06                                   
REMARK 500    SER A  60     -176.30   -176.58                                   
REMARK 500    LYS A  74      -65.35   -105.12                                   
REMARK 500    ALA A  76     -134.54    -82.74                                   
REMARK 500    ALA A 151       59.07   -156.38                                   
REMARK 500    SER A 152      -68.64    -92.86                                   
REMARK 500    ILE A 159      -57.26     66.83                                   
REMARK 500    PHE A 163     -169.93   -109.88                                   
REMARK 500    TYR A 202      -63.55   -126.76                                   
REMARK 500    ALA A 280     -148.77   -173.34                                   
REMARK 500    LYS A 281      -93.88     39.86                                   
REMARK 500    ASP A 298        4.15    -66.74                                   
REMARK 500    PHE A 301     -168.23    -70.53                                   
REMARK 500    PHE A 310       83.30   -157.73                                   
REMARK 500    ASN A 313       35.38    -73.31                                   
REMARK 500    SER A 389       45.52   -148.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1323        DISTANCE =  5.45 ANGSTROMS                       
REMARK 525    HOH A1327        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH A1334        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH A1356        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH A1367        DISTANCE =  5.49 ANGSTROMS                       
REMARK 525    HOH A1372        DISTANCE =  5.52 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: STO001000735.1   RELATED DB: TARGETDB                    
DBREF  2EO5 A    1   419  UNP    Q974B8   Q974B8_SULTO     1    419             
SEQRES   1 A  419  MET LEU SER ARG LYS ILE ILE GLU GLU SER ASP ILE TYR          
SEQRES   2 A  419  LEU ALA THR SER THR ARG ASP PRO GLU LEU PHE PRO LEU          
SEQRES   3 A  419  VAL ILE ASP HIS GLY GLU GLY VAL TRP ILE TYR ASP VAL          
SEQRES   4 A  419  ASP GLY ASN LYS TYR LEU ASP PHE THR SER GLY ILE GLY          
SEQRES   5 A  419  VAL ASN ASN LEU GLY TRP PRO SER HIS PRO GLU VAL ILE          
SEQRES   6 A  419  LYS ILE GLY ILE GLU GLN MET GLN LYS LEU ALA HIS ALA          
SEQRES   7 A  419  ALA ALA ASN ASP PHE TYR ASN ILE PRO GLN LEU GLU LEU          
SEQRES   8 A  419  ALA LYS LYS LEU VAL THR TYR SER PRO GLY ASN PHE GLN          
SEQRES   9 A  419  LYS LYS VAL PHE PHE SER ASN SER GLY THR GLU ALA ILE          
SEQRES  10 A  419  GLU ALA SER ILE LYS VAL VAL LYS ASN THR GLY ARG LYS          
SEQRES  11 A  419  TYR ILE ILE ALA PHE LEU GLY GLY PHE HIS GLY ARG THR          
SEQRES  12 A  419  PHE GLY SER ILE SER LEU THR ALA SER LYS ALA VAL GLN          
SEQRES  13 A  419  ARG SER ILE VAL GLY PRO PHE MET PRO GLY VAL ILE HIS          
SEQRES  14 A  419  VAL PRO TYR PRO ASN PRO TYR ARG ASN PRO TRP HIS ILE          
SEQRES  15 A  419  ASN GLY TYR GLU ASN PRO SER GLU LEU VAL ASN ARG VAL          
SEQRES  16 A  419  ILE GLU PHE ILE GLU ASP TYR ILE PHE VAL ASN LEU VAL          
SEQRES  17 A  419  PRO PRO GLU GLU VAL ALA GLY ILE PHE PHE GLU PRO ILE          
SEQRES  18 A  419  GLN GLY GLU GLY GLY TYR VAL ILE PRO PRO LYS ASN PHE          
SEQRES  19 A  419  PHE ALA GLU LEU GLN LYS LEU ALA LYS LYS TYR GLY ILE          
SEQRES  20 A  419  LEU LEU VAL ASP ASP GLU VAL GLN MET GLY LEU GLY ARG          
SEQRES  21 A  419  THR GLY LYS LEU PHE ALA ILE GLU ASN PHE ASN THR VAL          
SEQRES  22 A  419  PRO ASP VAL ILE THR LEU ALA LYS ALA LEU GLY GLY GLY          
SEQRES  23 A  419  ILE MET PRO ILE GLY ALA THR ILE PHE ARG LYS ASP LEU          
SEQRES  24 A  419  ASP PHE LYS PRO GLY MET HIS SER ASN THR PHE GLY GLY          
SEQRES  25 A  419  ASN ALA LEU ALA CYS ALA ILE GLY SER LYS VAL ILE ASP          
SEQRES  26 A  419  ILE VAL LYS ASP LEU LEU PRO HIS VAL ASN GLU ILE GLY          
SEQRES  27 A  419  LYS ILE PHE ALA GLU GLU LEU GLN GLY LEU ALA ASP ASP          
SEQRES  28 A  419  VAL ARG GLY ILE GLY LEU ALA TRP GLY LEU GLU TYR ASN          
SEQRES  29 A  419  GLU LYS LYS VAL ARG ASP ARG ILE ILE GLY GLU SER PHE          
SEQRES  30 A  419  LYS ARG GLY LEU LEU LEU LEU PRO ALA GLY ARG SER ALA          
SEQRES  31 A  419  ILE ARG VAL ILE PRO PRO LEU VAL ILE SER GLU GLU GLU          
SEQRES  32 A  419  ALA LYS GLN GLY LEU ASP ILE LEU LYS LYS VAL ILE LYS          
SEQRES  33 A  419  VAL VAL LYS                                                  
HET    SO4  A1002       5                                                       
HET    PLP  A1001      15                                                       
HET    EDO  A1003       4                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  PLP    C8 H10 N O6 P                                                
FORMUL   4  EDO    C2 H6 O2                                                     
FORMUL   5  HOH   *376(H2 O)                                                    
HELIX    1   1 MET A    1  LEU A   14  1                                  14    
HELIX    2   2 THR A   48  VAL A   53  5                                   6    
HELIX    3   3 HIS A   61  GLN A   73  1                                  13    
HELIX    4   4 ASN A   85  SER A   99  1                                  15    
HELIX    5   5 SER A  112  ASN A  126  1                                  15    
HELIX    6   6 THR A  143  THR A  150  1                                   8    
HELIX    7   7 LYS A  153  SER A  158  5                                   6    
HELIX    8   8 ASN A  187  TYR A  202  1                                  16    
HELIX    9   9 TYR A  202  LEU A  207  1                                   6    
HELIX   10  10 PRO A  209  GLU A  211  5                                   3    
HELIX   11  11 ASN A  233  TYR A  245  1                                  13    
HELIX   12  12 PHE A  265  ASN A  271  5                                   7    
HELIX   13  13 ALA A  280  GLY A  285  5                                   6    
HELIX   14  14 ASP A  298  ASP A  300  5                                   3    
HELIX   15  15 ASN A  313  GLN A  346  1                                  34    
HELIX   16  16 GLU A  365  ARG A  379  1                                  15    
HELIX   17  17 SER A  400  VAL A  418  1                                  19    
SHEET    1   A 4 ILE A  28  GLU A  32  0                                        
SHEET    2   A 4 TRP A  35  ASP A  38 -1  O  TYR A  37   N  ASP A  29           
SHEET    3   A 4 LYS A  43  ASP A  46 -1  O  TYR A  44   N  ILE A  36           
SHEET    4   A 4 LEU A 381  LEU A 382  1  O  LEU A 382   N  LEU A  45           
SHEET    1   B 7 LYS A 105  SER A 110  0                                        
SHEET    2   B 7 GLY A 291  ARG A 296 -1  O  GLY A 291   N  SER A 110           
SHEET    3   B 7 VAL A 276  LEU A 279 -1  N  ILE A 277   O  ILE A 294           
SHEET    4   B 7 LEU A 248  ASP A 252  1  N  ASP A 251   O  VAL A 276           
SHEET    5   B 7 VAL A 213  PHE A 218  1  N  PHE A 218   O  ASP A 252           
SHEET    6   B 7 TYR A 131  PHE A 135  1  N  ILE A 133   O  PHE A 217           
SHEET    7   B 7 VAL A 167  VAL A 170  1  O  ILE A 168   N  ILE A 132           
SHEET    1   C 4 ASP A 351  ILE A 355  0                                        
SHEET    2   C 4 ALA A 358  GLU A 362 -1  O  GLY A 360   N  ARG A 353           
SHEET    3   C 4 ALA A 390  VAL A 393 -1  O  VAL A 393   N  TRP A 359           
SHEET    4   C 4 LEU A 384  ALA A 386 -1  N  LEU A 384   O  ARG A 392           
LINK         C4A PLP A1001                 NZ  LYS A 281     1555   1555  1.40  
CISPEP   1 ASP A   20    PRO A   21          0         0.11                     
CISPEP   2 TRP A   58    PRO A   59          0        -0.29                     
CISPEP   3 GLY A  161    PRO A  162          0         0.06                     
CRYST1   88.046   91.170  132.463  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011358  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010969  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007549        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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