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Database: PDB
Entry: 1SZK
LinkDB: 1SZK
Original site: 1SZK 
HEADER    TRANSFERASE                             05-APR-04   1SZK              
TITLE     THE STRUCTURE OF GAMMA-AMINOBUTYRATE AMINOTRANSFERASE                 
TITLE    2 MUTANT: E211S                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 4-AMINOBUTYRATE AMINOTRANSFERASE;                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: GAMMA-AMINO-N-BUTYRATE TRANSAMINASE, GABA                   
COMPND   5 TRANSAMINASE, GLUTAMATE:SUCCINIC SEMIALDEHYDE TRANSAMINASE,          
COMPND   6 GABA AMINOTRANSFERASE, GABA-AT;                                      
COMPND   7 EC: 2.6.1.19;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET23A(+)                                 
KEYWDS    GABA-AT, TRANSFERASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.LIU,P.E.PETERSON,J.A.LANGSTON,X.JIN,A.J.FISHER,M.D.TONEY            
REVDAT   2   24-FEB-09 1SZK    1       VERSN                                    
REVDAT   1   01-MAR-05 1SZK    0                                                
JRNL        AUTH   W.LIU,P.E.PETERSON,J.A.LANGSTON,X.JIN,X.ZHOU,                
JRNL        AUTH 2 A.J.FISHER,M.D.TONEY                                         
JRNL        TITL   KINETIC AND CRYSTALLOGRAPHIC ANALYSIS OF ACTIVE              
JRNL        TITL 2 SITE MUTANTS OF ESCHERICHIA                                  
JRNL        TITL 3 COLIGAMMA-AMINOBUTYRATE AMINOTRANSFERASE.                    
JRNL        REF    BIOCHEMISTRY                  V.  44  2982 2005              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15723541                                                     
JRNL        DOI    10.1021/BI048657A                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.52 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.52                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 69873                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3515                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
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) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12824                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 191                                     
REMARK   3   SOLVENT ATOMS            : 673                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.37400                                             
REMARK   3    B22 (A**2) : -4.37400                                             
REMARK   3    B33 (A**2) : 8.74800                                              
REMARK   3    B12 (A**2) : -5.05900                                             
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.31                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.215 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.027 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.780 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.641 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : PMP_SO4_EGL.PAR                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1SZK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022126.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-AUG-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
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 RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69873                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.520                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.52                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1SF2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, AMMONIUM SULFATE, PLP, PH         
REMARK 280  7.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      200.55333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      100.27667            
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      100.27667            
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      200.55333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 31320 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 49040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -265.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     1                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET D     1                                                      
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  32      -99.36     55.26                                   
REMARK 500    ILE A  50       63.76     78.01                                   
REMARK 500    LYS A  72      -63.13    -98.60                                   
REMARK 500    THR A  76      -24.85   -147.37                                   
REMARK 500    CYS A  77       99.37     83.14                                   
REMARK 500    VAL A 108     -150.18   -119.35                                   
REMARK 500    LYS A 151      112.88   -169.63                                   
REMARK 500    PRO A 163      140.72    -37.88                                   
REMARK 500    CYS A 173       76.57   -150.07                                   
REMARK 500    ALA A 267     -147.53   -170.33                                   
REMARK 500    LYS A 268     -107.31     45.30                                   
REMARK 500    PRO A 275       98.94    -56.68                                   
REMARK 500    ALA A 299      126.44    -29.13                                   
REMARK 500    HIS A 365       43.44    -56.08                                   
REMARK 500    ASN A 366       10.12   -164.45                                   
REMARK 500    PRO B  24       46.59    -77.54                                   
REMARK 500    ASN B  32     -110.71     55.20                                   
REMARK 500    ILE B  50       62.20     78.50                                   
REMARK 500    LEU B  53       52.36   -117.02                                   
REMARK 500    THR B  76      -25.45   -148.42                                   
REMARK 500    CYS B  77      101.43     82.45                                   
REMARK 500    VAL B 108     -152.78   -126.44                                   
REMARK 500    LYS B 151      106.83   -169.26                                   
REMARK 500    TYR B 155      -18.14    -42.08                                   
REMARK 500    SER B 156       24.72   -154.61                                   
REMARK 500    CYS B 173       80.95   -164.60                                   
REMARK 500    LEU B 175      -19.33    -48.59                                   
REMARK 500    ALA B 267     -141.96   -171.11                                   
REMARK 500    LYS B 268     -110.91     38.52                                   
REMARK 500    PRO B 275      101.49    -58.26                                   
REMARK 500    ARG B 282      127.10    -38.88                                   
REMARK 500    ALA B 299      123.66    -30.29                                   
REMARK 500    HIS B 365       34.91    -65.32                                   
REMARK 500    ASN B 366      -16.68   -144.79                                   
REMARK 500    CYS B 390     -175.89   -174.63                                   
REMARK 500    PRO C  24       47.83    -74.61                                   
REMARK 500    GLU C  31      112.79   -162.64                                   
REMARK 500    ASN C  32      -98.13     60.30                                   
REMARK 500    ILE C  50       69.29     70.19                                   
REMARK 500    LEU C  58       59.94     36.58                                   
REMARK 500    LYS C  72      -61.12    -92.61                                   
REMARK 500    THR C  76      -20.31   -142.10                                   
REMARK 500    CYS C  77       99.84     77.75                                   
REMARK 500    VAL C 108     -152.62   -115.57                                   
REMARK 500    LYS C 151      114.96   -170.80                                   
REMARK 500    CYS C 173       85.21   -169.46                                   
REMARK 500    ALA C 267     -145.34   -169.97                                   
REMARK 500    LYS C 268     -110.60     46.08                                   
REMARK 500    PRO C 275       95.14    -52.22                                   
REMARK 500    ALA C 299      127.93    -39.31                                   
REMARK 500    HIS C 365        8.78    -63.52                                   
REMARK 500    CYS C 390     -173.29   -175.78                                   
REMARK 500    THR C 404       31.42    -90.18                                   
REMARK 500    ASP D  28      -50.43   -120.12                                   
REMARK 500    GLU D  31      112.97   -163.98                                   
REMARK 500    ASN D  32     -101.78     59.22                                   
REMARK 500    ILE D  50       56.50     81.52                                   
REMARK 500    LEU D  53       55.15   -117.35                                   
REMARK 500    LYS D  72      -64.81    -91.49                                   
REMARK 500    THR D  76      -23.25   -147.34                                   
REMARK 500    CYS D  77       98.08     79.20                                   
REMARK 500    VAL D  80      -61.72   -105.50                                   
REMARK 500    VAL D 108     -137.45   -124.31                                   
REMARK 500    THR D 109      -41.14   -134.50                                   
REMARK 500    LYS D 151      119.18   -171.31                                   
REMARK 500    TYR D 155      -31.22    -38.74                                   
REMARK 500    ALA D 157      125.15    -38.01                                   
REMARK 500    CYS D 173       82.35   -166.95                                   
REMARK 500    ALA D 267     -146.54   -172.35                                   
REMARK 500    LYS D 268     -110.38     43.09                                   
REMARK 500    ARG D 282      119.28    -34.42                                   
REMARK 500    ALA D 299      127.21    -26.27                                   
REMARK 500    HIS D 342       84.33   -155.86                                   
REMARK 500    ASP D 364      116.63    -31.19                                   
REMARK 500    CYS D 390     -159.01   -171.49                                   
REMARK 500    TYR D 394       38.09     38.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 701                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 702                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 703                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 704                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 705                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 706                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 707                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 708                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 709                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 710                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 711                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 712                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 713                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 714                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 715                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 801                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 802                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 803                 
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 804                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 805                 
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 806                 
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 807                 
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 808                 
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 809                 
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 810                 
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 811                 
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 812                 
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 813                 
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP A 750                 
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP B 751                 
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP C 752                 
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP D 753                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SF2   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF GAMMA-AMINOBUTYRATE AMINOTRANSFERASE                
REMARK 900 RELATED ID: 1SFF   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF GAMMA-AMINOBUTYRATE AMINOTRANSFERASE                
REMARK 900 COMPLEX WITH AMINOOXYACETATE                                         
DBREF  1SZK A    1   426  UNP    P22256   GABT_ECOLI       1    426             
DBREF  1SZK B    1   426  UNP    P22256   GABT_ECOLI       1    426             
DBREF  1SZK C    1   426  UNP    P22256   GABT_ECOLI       1    426             
DBREF  1SZK D    1   426  UNP    P22256   GABT_ECOLI       1    426             
SEQADV 1SZK SER A  211  UNP  P22256    GLU   211 ENGINEERED                     
SEQADV 1SZK SER B  211  UNP  P22256    GLU   211 ENGINEERED                     
SEQADV 1SZK SER C  211  UNP  P22256    GLU   211 ENGINEERED                     
SEQADV 1SZK SER D  211  UNP  P22256    GLU   211 ENGINEERED                     
SEQRES   1 A  426  MET ASN SER ASN LYS GLU LEU MET GLN ARG ARG SER GLN          
SEQRES   2 A  426  ALA ILE PRO ARG GLY VAL GLY GLN ILE HIS PRO ILE PHE          
SEQRES   3 A  426  ALA ASP ARG ALA GLU ASN CYS ARG VAL TRP ASP VAL GLU          
SEQRES   4 A  426  GLY ARG GLU TYR LEU ASP PHE ALA GLY GLY ILE ALA VAL          
SEQRES   5 A  426  LEU ASN THR GLY HIS LEU HIS PRO LYS VAL VAL ALA ALA          
SEQRES   6 A  426  VAL GLU ALA GLN LEU LYS LYS LEU SER HIS THR CYS PHE          
SEQRES   7 A  426  GLN VAL LEU ALA TYR GLU PRO TYR LEU GLU LEU CYS GLU          
SEQRES   8 A  426  ILE MET ASN GLN LYS VAL PRO GLY ASP PHE ALA LYS LYS          
SEQRES   9 A  426  THR LEU LEU VAL THR THR GLY SER GLU ALA VAL GLU ASN          
SEQRES  10 A  426  ALA VAL LYS ILE ALA ARG ALA ALA THR LYS ARG SER GLY          
SEQRES  11 A  426  THR ILE ALA PHE SER GLY ALA TYR HIS GLY ARG THR HIS          
SEQRES  12 A  426  TYR THR LEU ALA LEU THR GLY LYS VAL ASN PRO TYR SER          
SEQRES  13 A  426  ALA GLY MET GLY LEU MET PRO GLY HIS VAL TYR ARG ALA          
SEQRES  14 A  426  LEU TYR PRO CYS PRO LEU HIS GLY ILE SER GLU ASP ASP          
SEQRES  15 A  426  ALA ILE ALA SER ILE HIS ARG ILE PHE LYS ASN ASP ALA          
SEQRES  16 A  426  ALA PRO GLU ASP ILE ALA ALA ILE VAL ILE GLU PRO VAL          
SEQRES  17 A  426  GLN GLY SER GLY GLY PHE TYR ALA SER SER PRO ALA PHE          
SEQRES  18 A  426  MET GLN ARG LEU ARG ALA LEU CYS ASP GLU HIS GLY ILE          
SEQRES  19 A  426  MET LEU ILE ALA ASP GLU VAL GLN SER GLY ALA GLY ARG          
SEQRES  20 A  426  THR GLY THR LEU PHE ALA MET GLU GLN MET GLY VAL ALA          
SEQRES  21 A  426  PRO ASP LEU THR THR PHE ALA LYS SER ILE ALA GLY GLY          
SEQRES  22 A  426  PHE PRO LEU ALA GLY VAL THR GLY ARG ALA GLU VAL MET          
SEQRES  23 A  426  ASP ALA VAL ALA PRO GLY GLY LEU GLY GLY THR TYR ALA          
SEQRES  24 A  426  GLY ASN PRO ILE ALA CYS VAL ALA ALA LEU GLU VAL LEU          
SEQRES  25 A  426  LYS VAL PHE GLU GLN GLU ASN LEU LEU GLN LYS ALA ASN          
SEQRES  26 A  426  ASP LEU GLY GLN LYS LEU LYS ASP GLY LEU LEU ALA ILE          
SEQRES  27 A  426  ALA GLU LYS HIS PRO GLU ILE GLY ASP VAL ARG GLY LEU          
SEQRES  28 A  426  GLY ALA MET ILE ALA ILE GLU LEU PHE GLU ASP GLY ASP          
SEQRES  29 A  426  HIS ASN LYS PRO ASP ALA LYS LEU THR ALA GLU ILE VAL          
SEQRES  30 A  426  ALA ARG ALA ARG ASP LYS GLY LEU ILE LEU LEU SER CYS          
SEQRES  31 A  426  GLY PRO TYR TYR ASN VAL LEU ARG ILE LEU VAL PRO LEU          
SEQRES  32 A  426  THR ILE GLU ASP ALA GLN ILE ARG GLN GLY LEU GLU ILE          
SEQRES  33 A  426  ILE SER GLN CYS PHE ASP GLU ALA LYS GLN                      
SEQRES   1 B  426  MET ASN SER ASN LYS GLU LEU MET GLN ARG ARG SER GLN          
SEQRES   2 B  426  ALA ILE PRO ARG GLY VAL GLY GLN ILE HIS PRO ILE PHE          
SEQRES   3 B  426  ALA ASP ARG ALA GLU ASN CYS ARG VAL TRP ASP VAL GLU          
SEQRES   4 B  426  GLY ARG GLU TYR LEU ASP PHE ALA GLY GLY ILE ALA VAL          
SEQRES   5 B  426  LEU ASN THR GLY HIS LEU HIS PRO LYS VAL VAL ALA ALA          
SEQRES   6 B  426  VAL GLU ALA GLN LEU LYS LYS LEU SER HIS THR CYS PHE          
SEQRES   7 B  426  GLN VAL LEU ALA TYR GLU PRO TYR LEU GLU LEU CYS GLU          
SEQRES   8 B  426  ILE MET ASN GLN LYS VAL PRO GLY ASP PHE ALA LYS LYS          
SEQRES   9 B  426  THR LEU LEU VAL THR THR GLY SER GLU ALA VAL GLU ASN          
SEQRES  10 B  426  ALA VAL LYS ILE ALA ARG ALA ALA THR LYS ARG SER GLY          
SEQRES  11 B  426  THR ILE ALA PHE SER GLY ALA TYR HIS GLY ARG THR HIS          
SEQRES  12 B  426  TYR THR LEU ALA LEU THR GLY LYS VAL ASN PRO TYR SER          
SEQRES  13 B  426  ALA GLY MET GLY LEU MET PRO GLY HIS VAL TYR ARG ALA          
SEQRES  14 B  426  LEU TYR PRO CYS PRO LEU HIS GLY ILE SER GLU ASP ASP          
SEQRES  15 B  426  ALA ILE ALA SER ILE HIS ARG ILE PHE LYS ASN ASP ALA          
SEQRES  16 B  426  ALA PRO GLU ASP ILE ALA ALA ILE VAL ILE GLU PRO VAL          
SEQRES  17 B  426  GLN GLY SER GLY GLY PHE TYR ALA SER SER PRO ALA PHE          
SEQRES  18 B  426  MET GLN ARG LEU ARG ALA LEU CYS ASP GLU HIS GLY ILE          
SEQRES  19 B  426  MET LEU ILE ALA ASP GLU VAL GLN SER GLY ALA GLY ARG          
SEQRES  20 B  426  THR GLY THR LEU PHE ALA MET GLU GLN MET GLY VAL ALA          
SEQRES  21 B  426  PRO ASP LEU THR THR PHE ALA LYS SER ILE ALA GLY GLY          
SEQRES  22 B  426  PHE PRO LEU ALA GLY VAL THR GLY ARG ALA GLU VAL MET          
SEQRES  23 B  426  ASP ALA VAL ALA PRO GLY GLY LEU GLY GLY THR TYR ALA          
SEQRES  24 B  426  GLY ASN PRO ILE ALA CYS VAL ALA ALA LEU GLU VAL LEU          
SEQRES  25 B  426  LYS VAL PHE GLU GLN GLU ASN LEU LEU GLN LYS ALA ASN          
SEQRES  26 B  426  ASP LEU GLY GLN LYS LEU LYS ASP GLY LEU LEU ALA ILE          
SEQRES  27 B  426  ALA GLU LYS HIS PRO GLU ILE GLY ASP VAL ARG GLY LEU          
SEQRES  28 B  426  GLY ALA MET ILE ALA ILE GLU LEU PHE GLU ASP GLY ASP          
SEQRES  29 B  426  HIS ASN LYS PRO ASP ALA LYS LEU THR ALA GLU ILE VAL          
SEQRES  30 B  426  ALA ARG ALA ARG ASP LYS GLY LEU ILE LEU LEU SER CYS          
SEQRES  31 B  426  GLY PRO TYR TYR ASN VAL LEU ARG ILE LEU VAL PRO LEU          
SEQRES  32 B  426  THR ILE GLU ASP ALA GLN ILE ARG GLN GLY LEU GLU ILE          
SEQRES  33 B  426  ILE SER GLN CYS PHE ASP GLU ALA LYS GLN                      
SEQRES   1 C  426  MET ASN SER ASN LYS GLU LEU MET GLN ARG ARG SER GLN          
SEQRES   2 C  426  ALA ILE PRO ARG GLY VAL GLY GLN ILE HIS PRO ILE PHE          
SEQRES   3 C  426  ALA ASP ARG ALA GLU ASN CYS ARG VAL TRP ASP VAL GLU          
SEQRES   4 C  426  GLY ARG GLU TYR LEU ASP PHE ALA GLY GLY ILE ALA VAL          
SEQRES   5 C  426  LEU ASN THR GLY HIS LEU HIS PRO LYS VAL VAL ALA ALA          
SEQRES   6 C  426  VAL GLU ALA GLN LEU LYS LYS LEU SER HIS THR CYS PHE          
SEQRES   7 C  426  GLN VAL LEU ALA TYR GLU PRO TYR LEU GLU LEU CYS GLU          
SEQRES   8 C  426  ILE MET ASN GLN LYS VAL PRO GLY ASP PHE ALA LYS LYS          
SEQRES   9 C  426  THR LEU LEU VAL THR THR GLY SER GLU ALA VAL GLU ASN          
SEQRES  10 C  426  ALA VAL LYS ILE ALA ARG ALA ALA THR LYS ARG SER GLY          
SEQRES  11 C  426  THR ILE ALA PHE SER GLY ALA TYR HIS GLY ARG THR HIS          
SEQRES  12 C  426  TYR THR LEU ALA LEU THR GLY LYS VAL ASN PRO TYR SER          
SEQRES  13 C  426  ALA GLY MET GLY LEU MET PRO GLY HIS VAL TYR ARG ALA          
SEQRES  14 C  426  LEU TYR PRO CYS PRO LEU HIS GLY ILE SER GLU ASP ASP          
SEQRES  15 C  426  ALA ILE ALA SER ILE HIS ARG ILE PHE LYS ASN ASP ALA          
SEQRES  16 C  426  ALA PRO GLU ASP ILE ALA ALA ILE VAL ILE GLU PRO VAL          
SEQRES  17 C  426  GLN GLY SER GLY GLY PHE TYR ALA SER SER PRO ALA PHE          
SEQRES  18 C  426  MET GLN ARG LEU ARG ALA LEU CYS ASP GLU HIS GLY ILE          
SEQRES  19 C  426  MET LEU ILE ALA ASP GLU VAL GLN SER GLY ALA GLY ARG          
SEQRES  20 C  426  THR GLY THR LEU PHE ALA MET GLU GLN MET GLY VAL ALA          
SEQRES  21 C  426  PRO ASP LEU THR THR PHE ALA LYS SER ILE ALA GLY GLY          
SEQRES  22 C  426  PHE PRO LEU ALA GLY VAL THR GLY ARG ALA GLU VAL MET          
SEQRES  23 C  426  ASP ALA VAL ALA PRO GLY GLY LEU GLY GLY THR TYR ALA          
SEQRES  24 C  426  GLY ASN PRO ILE ALA CYS VAL ALA ALA LEU GLU VAL LEU          
SEQRES  25 C  426  LYS VAL PHE GLU GLN GLU ASN LEU LEU GLN LYS ALA ASN          
SEQRES  26 C  426  ASP LEU GLY GLN LYS LEU LYS ASP GLY LEU LEU ALA ILE          
SEQRES  27 C  426  ALA GLU LYS HIS PRO GLU ILE GLY ASP VAL ARG GLY LEU          
SEQRES  28 C  426  GLY ALA MET ILE ALA ILE GLU LEU PHE GLU ASP GLY ASP          
SEQRES  29 C  426  HIS ASN LYS PRO ASP ALA LYS LEU THR ALA GLU ILE VAL          
SEQRES  30 C  426  ALA ARG ALA ARG ASP LYS GLY LEU ILE LEU LEU SER CYS          
SEQRES  31 C  426  GLY PRO TYR TYR ASN VAL LEU ARG ILE LEU VAL PRO LEU          
SEQRES  32 C  426  THR ILE GLU ASP ALA GLN ILE ARG GLN GLY LEU GLU ILE          
SEQRES  33 C  426  ILE SER GLN CYS PHE ASP GLU ALA LYS GLN                      
SEQRES   1 D  426  MET ASN SER ASN LYS GLU LEU MET GLN ARG ARG SER GLN          
SEQRES   2 D  426  ALA ILE PRO ARG GLY VAL GLY GLN ILE HIS PRO ILE PHE          
SEQRES   3 D  426  ALA ASP ARG ALA GLU ASN CYS ARG VAL TRP ASP VAL GLU          
SEQRES   4 D  426  GLY ARG GLU TYR LEU ASP PHE ALA GLY GLY ILE ALA VAL          
SEQRES   5 D  426  LEU ASN THR GLY HIS LEU HIS PRO LYS VAL VAL ALA ALA          
SEQRES   6 D  426  VAL GLU ALA GLN LEU LYS LYS LEU SER HIS THR CYS PHE          
SEQRES   7 D  426  GLN VAL LEU ALA TYR GLU PRO TYR LEU GLU LEU CYS GLU          
SEQRES   8 D  426  ILE MET ASN GLN LYS VAL PRO GLY ASP PHE ALA LYS LYS          
SEQRES   9 D  426  THR LEU LEU VAL THR THR GLY SER GLU ALA VAL GLU ASN          
SEQRES  10 D  426  ALA VAL LYS ILE ALA ARG ALA ALA THR LYS ARG SER GLY          
SEQRES  11 D  426  THR ILE ALA PHE SER GLY ALA TYR HIS GLY ARG THR HIS          
SEQRES  12 D  426  TYR THR LEU ALA LEU THR GLY LYS VAL ASN PRO TYR SER          
SEQRES  13 D  426  ALA GLY MET GLY LEU MET PRO GLY HIS VAL TYR ARG ALA          
SEQRES  14 D  426  LEU TYR PRO CYS PRO LEU HIS GLY ILE SER GLU ASP ASP          
SEQRES  15 D  426  ALA ILE ALA SER ILE HIS ARG ILE PHE LYS ASN ASP ALA          
SEQRES  16 D  426  ALA PRO GLU ASP ILE ALA ALA ILE VAL ILE GLU PRO VAL          
SEQRES  17 D  426  GLN GLY SER GLY GLY PHE TYR ALA SER SER PRO ALA PHE          
SEQRES  18 D  426  MET GLN ARG LEU ARG ALA LEU CYS ASP GLU HIS GLY ILE          
SEQRES  19 D  426  MET LEU ILE ALA ASP GLU VAL GLN SER GLY ALA GLY ARG          
SEQRES  20 D  426  THR GLY THR LEU PHE ALA MET GLU GLN MET GLY VAL ALA          
SEQRES  21 D  426  PRO ASP LEU THR THR PHE ALA LYS SER ILE ALA GLY GLY          
SEQRES  22 D  426  PHE PRO LEU ALA GLY VAL THR GLY ARG ALA GLU VAL MET          
SEQRES  23 D  426  ASP ALA VAL ALA PRO GLY GLY LEU GLY GLY THR TYR ALA          
SEQRES  24 D  426  GLY ASN PRO ILE ALA CYS VAL ALA ALA LEU GLU VAL LEU          
SEQRES  25 D  426  LYS VAL PHE GLU GLN GLU ASN LEU LEU GLN LYS ALA ASN          
SEQRES  26 D  426  ASP LEU GLY GLN LYS LEU LYS ASP GLY LEU LEU ALA ILE          
SEQRES  27 D  426  ALA GLU LYS HIS PRO GLU ILE GLY ASP VAL ARG GLY LEU          
SEQRES  28 D  426  GLY ALA MET ILE ALA ILE GLU LEU PHE GLU ASP GLY ASP          
SEQRES  29 D  426  HIS ASN LYS PRO ASP ALA LYS LEU THR ALA GLU ILE VAL          
SEQRES  30 D  426  ALA ARG ALA ARG ASP LYS GLY LEU ILE LEU LEU SER CYS          
SEQRES  31 D  426  GLY PRO TYR TYR ASN VAL LEU ARG ILE LEU VAL PRO LEU          
SEQRES  32 D  426  THR ILE GLU ASP ALA GLN ILE ARG GLN GLY LEU GLU ILE          
SEQRES  33 D  426  ILE SER GLN CYS PHE ASP GLU ALA LYS GLN                      
HET    SO4  A 701       5                                                       
HET    SO4  B 702       5                                                       
HET    SO4  B 703       5                                                       
HET    SO4  C 704       5                                                       
HET    SO4  D 705       5                                                       
HET    SO4  D 706       5                                                       
HET    SO4  A 707       5                                                       
HET    SO4  B 708       5                                                       
HET    SO4  D 709       5                                                       
HET    SO4  C 710       5                                                       
HET    SO4  D 711       5                                                       
HET    SO4  A 712       5                                                       
HET    SO4  B 713       5                                                       
HET    SO4  C 714       5                                                       
HET    SO4  D 715       5                                                       
HET    EDO  B 801       4                                                       
HET    EDO  B 802       4                                                       
HET    EDO  C 803       4                                                       
HET    EDO  B 804       4                                                       
HET    EDO  D 805       4                                                       
HET    EDO  D 806       4                                                       
HET    EDO  D 807       4                                                       
HET    EDO  A 808       4                                                       
HET    EDO  C 809       4                                                       
HET    EDO  A 810       4                                                       
HET    EDO  C 811       4                                                       
HET    EDO  D 812       4                                                       
HET    EDO  A 813       4                                                       
HET    PMP  A 750      16                                                       
HET    PMP  B 751      16                                                       
HET    PMP  C 752      16                                                       
HET    PMP  D 753      16                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PMP 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE                          
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     PMP PYRIDOXAMINE-5'-PHOSPHATE                                        
FORMUL   5  SO4    15(O4 S 2-)                                                  
FORMUL  20  EDO    13(C2 H6 O2)                                                 
FORMUL  33  PMP    4(C8 H13 N2 O5 P)                                            
FORMUL  37  HOH   *673(H2 O)                                                    
HELIX    1   1 SER A    3  ILE A   15  1                                  13    
HELIX    2   2 ALA A   47  VAL A   52  1                                   6    
HELIX    3   3 HIS A   59  LYS A   71  1                                  13    
HELIX    4   4 TYR A   83  VAL A   97  1                                  15    
HELIX    5   5 THR A  110  LYS A  127  1                                  18    
HELIX    6   6 THR A  142  THR A  149  1                                   8    
HELIX    7   7 CYS A  173  GLY A  177  5                                   5    
HELIX    8   8 SER A  179  ASP A  194  1                                  16    
HELIX    9   9 ALA A  196  GLU A  198  5                                   3    
HELIX   10  10 SER A  218  GLY A  233  1                                  16    
HELIX   11  11 PHE A  252  MET A  257  5                                   6    
HELIX   12  12 ALA A  267  GLY A  272  5                                   6    
HELIX   13  13 ALA A  283  ASP A  287  1                                   5    
HELIX   14  14 ASN A  301  GLU A  318  1                                  18    
HELIX   15  15 ASN A  319  GLU A  340  1                                  22    
HELIX   16  16 GLU A  361  ASP A  364  5                                   4    
HELIX   17  17 ASP A  369  LYS A  383  1                                  15    
HELIX   18  18 GLU A  406  GLN A  426  1                                  21    
HELIX   19  19 SER B    3  ILE B   15  1                                  13    
HELIX   20  20 ALA B   47  VAL B   52  1                                   6    
HELIX   21  21 HIS B   59  LEU B   73  1                                  15    
HELIX   22  22 TYR B   83  VAL B   97  1                                  15    
HELIX   23  23 THR B  110  LYS B  127  1                                  18    
HELIX   24  24 THR B  142  THR B  149  1                                   8    
HELIX   25  25 CYS B  173  GLY B  177  5                                   5    
HELIX   26  26 SER B  179  ASP B  194  1                                  16    
HELIX   27  27 ALA B  196  GLU B  198  5                                   3    
HELIX   28  28 SER B  218  GLY B  233  1                                  16    
HELIX   29  29 PHE B  252  MET B  257  5                                   6    
HELIX   30  30 ALA B  267  ALA B  271  5                                   5    
HELIX   31  31 ALA B  283  ASP B  287  1                                   5    
HELIX   32  32 ASN B  301  GLU B  318  1                                  18    
HELIX   33  33 ASN B  319  ALA B  339  1                                  21    
HELIX   34  34 ASP B  369  LYS B  383  1                                  15    
HELIX   35  35 GLU B  406  ALA B  424  1                                  19    
HELIX   36  36 SER C    3  ILE C   15  1                                  13    
HELIX   37  37 ALA C   47  VAL C   52  1                                   6    
HELIX   38  38 HIS C   59  LYS C   71  1                                  13    
HELIX   39  39 GLU C   84  VAL C   97  1                                  14    
HELIX   40  40 THR C  110  LYS C  127  1                                  18    
HELIX   41  41 THR C  142  THR C  149  1                                   8    
HELIX   42  42 CYS C  173  GLY C  177  5                                   5    
HELIX   43  43 SER C  179  ASP C  194  1                                  16    
HELIX   44  44 ALA C  196  GLU C  198  5                                   3    
HELIX   45  45 SER C  218  GLY C  233  1                                  16    
HELIX   46  46 PHE C  252  GLY C  258  5                                   7    
HELIX   47  47 ALA C  267  GLY C  272  5                                   6    
HELIX   48  48 ALA C  283  ASP C  287  1                                   5    
HELIX   49  49 ASN C  301  GLU C  318  1                                  18    
HELIX   50  50 ASN C  319  ALA C  339  1                                  21    
HELIX   51  51 ASP C  369  LYS C  383  1                                  15    
HELIX   52  52 GLU C  406  ALA C  424  1                                  19    
HELIX   53  53 SER D    3  ILE D   15  1                                  13    
HELIX   54  54 ALA D   47  VAL D   52  1                                   6    
HELIX   55  55 HIS D   59  LEU D   73  1                                  15    
HELIX   56  56 TYR D   83  VAL D   97  1                                  15    
HELIX   57  57 THR D  110  LYS D  127  1                                  18    
HELIX   58  58 THR D  142  THR D  149  1                                   8    
HELIX   59  59 CYS D  173  GLY D  177  5                                   5    
HELIX   60  60 SER D  179  ASP D  194  1                                  16    
HELIX   61  61 ALA D  196  GLU D  198  5                                   3    
HELIX   62  62 SER D  218  GLY D  233  1                                  16    
HELIX   63  63 PHE D  252  GLY D  258  5                                   7    
HELIX   64  64 ALA D  267  GLY D  272  5                                   6    
HELIX   65  65 ALA D  283  ASP D  287  1                                   5    
HELIX   66  66 ASN D  301  GLU D  318  1                                  18    
HELIX   67  67 ASN D  319  ALA D  339  1                                  21    
HELIX   68  68 ASP D  369  ASP D  382  1                                  14    
HELIX   69  69 GLU D  406  GLN D  426  1                                  21    
SHEET    1   A 5 LEU A 385  ILE A 386  0                                        
SHEET    2   A 5 GLU A  42  ASP A  45  1  N  LEU A  44   O  ILE A 386           
SHEET    3   A 5 ARG A  34  ASP A  37 -1  N  VAL A  35   O  TYR A  43           
SHEET    4   A 5 HIS A  23  GLU A  31 -1  N  ASP A  28   O  TRP A  36           
SHEET    5   A 5 LEU B  81  ALA B  82  1  O  ALA B  82   N  ALA A  27           
SHEET    1   B 5 LEU A  81  ALA A  82  0                                        
SHEET    2   B 5 HIS B  23  GLU B  31  1  O  ALA B  27   N  ALA A  82           
SHEET    3   B 5 ARG B  34  ASP B  37 -1  O  TRP B  36   N  ASP B  28           
SHEET    4   B 5 GLU B  42  ASP B  45 -1  O  TYR B  43   N  VAL B  35           
SHEET    5   B 5 LEU B 385  ILE B 386  1  O  ILE B 386   N  LEU B  44           
SHEET    1   C 7 LYS A 103  VAL A 108  0                                        
SHEET    2   C 7 ALA A 277  ARG A 282 -1  O  VAL A 279   N  LEU A 106           
SHEET    3   C 7 LEU A 263  PHE A 266 -1  N  PHE A 266   O  GLY A 278           
SHEET    4   C 7 MET A 235  ASP A 239  1  N  ALA A 238   O  LEU A 263           
SHEET    5   C 7 ILE A 200  ILE A 205  1  N  ALA A 201   O  MET A 235           
SHEET    6   C 7 GLY A 130  PHE A 134  1  N  GLY A 130   O  ALA A 201           
SHEET    7   C 7 VAL A 166  ALA A 169  1  O  TYR A 167   N  THR A 131           
SHEET    1   D 4 ILE A 345  ARG A 349  0                                        
SHEET    2   D 4 ILE A 355  LEU A 359 -1  O  ALA A 356   N  ARG A 349           
SHEET    3   D 4 VAL A 396  ILE A 399 -1  O  ILE A 399   N  ILE A 355           
SHEET    4   D 4 LEU A 388  CYS A 390 -1  N  CYS A 390   O  VAL A 396           
SHEET    1   E 7 LYS B 103  VAL B 108  0                                        
SHEET    2   E 7 ALA B 277  ARG B 282 -1  O  VAL B 279   N  LEU B 106           
SHEET    3   E 7 LEU B 263  PHE B 266 -1  N  THR B 264   O  THR B 280           
SHEET    4   E 7 MET B 235  ASP B 239  1  N  ALA B 238   O  LEU B 263           
SHEET    5   E 7 ILE B 200  ILE B 205  1  N  ILE B 203   O  ILE B 237           
SHEET    6   E 7 GLY B 130  PHE B 134  1  N  ILE B 132   O  VAL B 204           
SHEET    7   E 7 VAL B 166  ALA B 169  1  O  ALA B 169   N  ALA B 133           
SHEET    1   F 4 ILE B 345  LEU B 351  0                                        
SHEET    2   F 4 MET B 354  LEU B 359 -1  O  MET B 354   N  LEU B 351           
SHEET    3   F 4 VAL B 396  ILE B 399 -1  O  ILE B 399   N  ILE B 355           
SHEET    4   F 4 LEU B 388  CYS B 390 -1  N  CYS B 390   O  VAL B 396           
SHEET    1   G 4 ALA C  27  GLU C  31  0                                        
SHEET    2   G 4 ARG C  34  ASP C  37 -1  O  TRP C  36   N  ASP C  28           
SHEET    3   G 4 GLU C  42  ASP C  45 -1  O  TYR C  43   N  VAL C  35           
SHEET    4   G 4 LEU C 385  ILE C 386  1  O  ILE C 386   N  LEU C  44           
SHEET    1   H 5 LEU C  81  TYR C  83  0                                        
SHEET    2   H 5 HIS D  23  GLU D  31  1  O  ALA D  27   N  ALA C  82           
SHEET    3   H 5 ARG D  34  ASP D  37 -1  O  TRP D  36   N  ASP D  28           
SHEET    4   H 5 GLU D  42  ASP D  45 -1  O  TYR D  43   N  VAL D  35           
SHEET    5   H 5 LEU D 385  ILE D 386  1  O  ILE D 386   N  LEU D  44           
SHEET    1   I 7 LYS C 103  VAL C 108  0                                        
SHEET    2   I 7 ALA C 277  ARG C 282 -1  O  VAL C 279   N  LEU C 106           
SHEET    3   I 7 LEU C 263  PHE C 266 -1  N  PHE C 266   O  GLY C 278           
SHEET    4   I 7 MET C 235  ASP C 239  1  N  ALA C 238   O  LEU C 263           
SHEET    5   I 7 ILE C 200  ILE C 205  1  N  ILE C 203   O  ILE C 237           
SHEET    6   I 7 GLY C 130  PHE C 134  1  N  ILE C 132   O  VAL C 204           
SHEET    7   I 7 VAL C 166  ALA C 169  1  O  ALA C 169   N  ALA C 133           
SHEET    1   J 3 ILE C 345  LEU C 351  0                                        
SHEET    2   J 3 MET C 354  GLU C 361 -1  O  ALA C 356   N  ARG C 349           
SHEET    3   J 3 ASP C 364  PRO C 368 -1  O  LYS C 367   N  GLU C 361           
SHEET    1   K 4 ILE C 345  LEU C 351  0                                        
SHEET    2   K 4 MET C 354  GLU C 361 -1  O  ALA C 356   N  ARG C 349           
SHEET    3   K 4 VAL C 396  ILE C 399 -1  O  LEU C 397   N  ILE C 357           
SHEET    4   K 4 LEU C 388  CYS C 390 -1  N  LEU C 388   O  ARG C 398           
SHEET    1   L 7 LYS D 103  VAL D 108  0                                        
SHEET    2   L 7 ALA D 277  ARG D 282 -1  O  VAL D 279   N  LEU D 106           
SHEET    3   L 7 LEU D 263  PHE D 266 -1  N  PHE D 266   O  GLY D 278           
SHEET    4   L 7 MET D 235  ASP D 239  1  N  ALA D 238   O  LEU D 263           
SHEET    5   L 7 ILE D 200  ILE D 205  1  N  ILE D 203   O  ILE D 237           
SHEET    6   L 7 GLY D 130  PHE D 134  1  N  ILE D 132   O  VAL D 204           
SHEET    7   L 7 VAL D 166  ALA D 169  1  O  ALA D 169   N  ALA D 133           
SHEET    1   M 4 ARG D 349  LEU D 351  0                                        
SHEET    2   M 4 MET D 354  GLU D 358 -1  O  MET D 354   N  LEU D 351           
SHEET    3   M 4 VAL D 396  ILE D 399 -1  O  ILE D 399   N  ILE D 355           
SHEET    4   M 4 LEU D 388  CYS D 390 -1  N  LEU D 388   O  ARG D 398           
CISPEP   1 ASN A  153    PRO A  154          0         0.68                     
CISPEP   2 ASN B  153    PRO B  154          0         0.17                     
CISPEP   3 ASN C  153    PRO C  154          0         0.08                     
CISPEP   4 ASN D  153    PRO D  154          0        -0.04                     
SITE     1 AC1  3 ILE A 184  ARG A 224  HOH A 950                               
SITE     1 AC2  3 LYS B   5  ARG B 381  HOH B 926                               
SITE     1 AC3  3 HIS B 188  ARG B 224  HOH B 925                               
SITE     1 AC4  2 HIS C 188  ARG C 224                                          
SITE     1 AC5  1 ARG D 224                                                     
SITE     1 AC6  3 LYS D   5  ARG D 381  HOH D 881                               
SITE     1 AC7  4 ASN A 153  TYR A 394  LYS C 192  HOH C 852                    
SITE     1 AC8  3 ASN B 153  TYR B 394  LYS D 192                               
SITE     1 AC9  3 LYS B 192  ASN D 153  TYR D 394                               
SITE     1 BC1  3 LYS A 192  ASN C 153  TYR C 394                               
SITE     1 BC2  3 GLN A 419  ARG D  29  HOH D 978                               
SITE     1 BC3  6 ILE A  50  TYR A 138  SER A 211  ARG A 398                    
SITE     2 BC3  6 PMP A 750  HOH A 991                                          
SITE     1 BC4  7 ILE B  50  TYR B 138  SER B 211  GLN B 242                    
SITE     2 BC4  7 LYS B 268  ARG B 398  PMP B 751                               
SITE     1 BC5  7 ILE C  50  TYR C 138  SER C 211  GLN C 242                    
SITE     2 BC5  7 ARG C 398  PMP C 752  HOH C 952                               
SITE     1 BC6  7 ILE D  50  TYR D 138  SER D 211  GLN D 242                    
SITE     2 BC6  7 ARG D 398  PMP D 753  HOH D 987                               
SITE     1 BC7  8 THR A  76  VAL A  80  LEU A  81  ASP B  45                    
SITE     2 BC7  8 ALA B  47  GLY B  48  GLY B  49  HIS B  57                    
SITE     1 BC8  2 HIS B  23  ARG B 381                                          
SITE     1 BC9  6 GLY A 164  HIS A 165  GLY C 164  HIS C 165                    
SITE     2 BC9  6 VAL C 166  TYR C 167                                          
SITE     1 CC1  6 GLY B 164  HIS B 165  VAL B 166  HIS D 165                    
SITE     2 CC1  6 VAL D 166  HOH D 968                                          
SITE     1 CC2  8 THR C  76  VAL C  80  LEU C  81  ASP D  45                    
SITE     2 CC2  8 ALA D  47  GLY D  48  GLY D  49  HIS D  57                    
SITE     1 CC3  4 PRO C 275  ASN C 301  PRO D 275  ASN D 301                    
SITE     1 CC4  4 HIS D  23  PRO D  24  ARG D 381  HOH D 959                    
SITE     1 CC5  8 ASP A  45  ALA A  47  GLY A  48  GLY A  49                    
SITE     2 CC5  8 HIS A  57  THR B  76  VAL B  80  LEU B  81                    
SITE     1 CC6  7 ASP C  45  ALA C  47  GLY C  48  GLY C  49                    
SITE     2 CC6  7 HIS C  57  THR D  76  LEU D  81                               
SITE     1 CC7  5 GLN A  69  LYS A  72  PRO A  85  ASP B  28                    
SITE     2 CC7  5 HOH B 936                                                     
SITE     1 CC8  5 GLN C  69  LYS C  72  LEU C  73  PRO C  85                    
SITE     2 CC8  5 ASP D  28                                                     
SITE     1 CC9  6 TYR B 167  VAL D 166  TYR D 167  HOH D 923                    
SITE     2 CC9  6 HOH D 956  HOH D 968                                          
SITE     1 DC1  5 GLN A   9  GLN D  95  LYS D  96  PRO D  98                    
SITE     2 DC1  5 GLU D 255                                                     
SITE     1 DC2 18 GLY A 111  SER A 112  TYR A 138  HIS A 139                    
SITE     2 DC2 18 GLU A 206  ASP A 239  VAL A 241  GLN A 242                    
SITE     3 DC2 18 LYS A 268  SO4 A 712  HOH A 815  HOH A 823                    
SITE     4 DC2 18 HOH A 890  HOH A 912  HOH A 987  HOH A 989                    
SITE     5 DC2 18 GLY B 296  THR B 297                                          
SITE     1 DC3 16 THR A 297  HOH A 859  THR B 110  GLY B 111                    
SITE     2 DC3 16 SER B 112  TYR B 138  HIS B 139  GLU B 206                    
SITE     3 DC3 16 ASP B 239  VAL B 241  GLN B 242  LYS B 268                    
SITE     4 DC3 16 SO4 B 713  HOH B 805  HOH B 811  HOH B 818                    
SITE     1 DC4 17 THR C 110  GLY C 111  SER C 112  TYR C 138                    
SITE     2 DC4 17 HIS C 139  GLU C 206  ASP C 239  VAL C 241                    
SITE     3 DC4 17 GLN C 242  LYS C 268  SO4 C 714  HOH C 825                    
SITE     4 DC4 17 HOH C 828  HOH C 867  THR D 297  HOH D 838                    
SITE     5 DC4 17 HOH D 984                                                     
SITE     1 DC5 16 THR C 297  GLY D 111  SER D 112  TYR D 138                    
SITE     2 DC5 16 HIS D 139  GLU D 206  ASP D 239  VAL D 241                    
SITE     3 DC5 16 GLN D 242  LYS D 268  SO4 D 715  HOH D 813                    
SITE     4 DC5 16 HOH D 823  HOH D 826  HOH D 836  HOH D 845                    
CRYST1  108.260  108.260  300.830  90.00  90.00 120.00 P 32 2 1     24          
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      0.009237  0.005333  0.000000        0.00000                         
SCALE2      0.000000  0.010666  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003324        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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