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Database: PDB
Entry: 1SFF
LinkDB: 1SFF
Original site: 1SFF 
HEADER    TRANSFERASE                             19-FEB-04   1SFF              
TITLE     STRUCTURE OF GAMMA-AMINOBUTYRATE AMINOTRANSFERASE COMPLEX             
TITLE    2 WITH AMINOOXYACETATE                                                 
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                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: GABT, B2662;                                                   
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ENZYME COMPLEXES, AMINOTRANSFERASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.LIU,P.E.PETERSON,R.J.CARTER,X.ZHOU,J.A.LANGSTON,                    
AUTHOR   2 A.J.FISHER,M.D.TONEY                                                 
REVDAT   2   24-FEB-09 1SFF    1       VERSN                                    
REVDAT   1   14-SEP-04 1SFF    0                                                
JRNL        AUTH   W.LIU,P.E.PETERSON,R.J.CARTER,X.ZHOU,J.A.LANGSTON,           
JRNL        AUTH 2 A.J.FISHER,M.D.TONEY                                         
JRNL        TITL   CRYSTAL STRUCTURES OF UNBOUND AND                            
JRNL        TITL 2 AMINOOXYACETATE-BOUND ESCHERICHIA COLI                       
JRNL        TITL 3 GAMMA-AMINOBUTYRATE AMINOTRANSFERASE.                        
JRNL        REF    BIOCHEMISTRY                  V.  43 10896 2004              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15323550                                                     
JRNL        DOI    10.1021/BI049218E                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 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) : 1.90                           
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             : 159733                         
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) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.186                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 7895                            
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            : 12872                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 195                                     
REMARK   3   SOLVENT ATOMS            : 1208                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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) : 0.016                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.05                            
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
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  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : PLP_SO4_EGL.PARAM                              
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : PLP_SO4_EGL.TOP                                
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1SFF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB021662.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-DEC-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) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 159733                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
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     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.68                                     
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      200.98667            
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      100.49333            
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      100.49333            
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      200.98667            
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: 31330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 48800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -175.0 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  1730     O    HOH D  1717              1.88            
REMARK 500   O    HOH A  1739     O    HOH B  1549              2.07            
REMARK 500   O    HOH A  1566     O    HOH A  1737              2.13            
REMARK 500   N4A  IK2 D   450     O    HOH D  1718              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  31      118.62   -160.62                                   
REMARK 500    ASN A  32     -108.38     56.61                                   
REMARK 500    LYS A  72      -67.85   -106.35                                   
REMARK 500    CYS A  77      104.96     76.18                                   
REMARK 500    VAL A  80      -62.11    -94.47                                   
REMARK 500    VAL A 108     -144.67   -130.49                                   
REMARK 500    LYS A 151      116.07   -167.08                                   
REMARK 500    CYS A 173       83.18   -159.90                                   
REMARK 500    ASP A 194      -30.40   -132.61                                   
REMARK 500    ALA A 267     -143.34   -174.94                                   
REMARK 500    LYS A 268     -109.06     40.63                                   
REMARK 500    ALA A 299      126.76    -29.85                                   
REMARK 500    LYS A 367       79.38   -115.36                                   
REMARK 500    ASP A 369       78.71   -101.00                                   
REMARK 500    CYS A 390     -173.44   -170.26                                   
REMARK 500    ASN B  32     -108.09     56.20                                   
REMARK 500    ILE B  50       63.58     68.74                                   
REMARK 500    LYS B  72      -62.30    -99.78                                   
REMARK 500    CYS B  77      105.31     74.95                                   
REMARK 500    VAL B 108     -142.72   -127.23                                   
REMARK 500    LYS B 151      115.63   -167.95                                   
REMARK 500    CYS B 173       80.54   -159.40                                   
REMARK 500    ALA B 267     -139.86   -174.87                                   
REMARK 500    LYS B 268     -110.05     37.27                                   
REMARK 500    ARG B 282      121.77    -39.56                                   
REMARK 500    ALA B 299      125.97    -31.98                                   
REMARK 500    ASN B 319       53.93     37.75                                   
REMARK 500    HIS B 365       -9.66    -54.82                                   
REMARK 500    ASN C  32     -106.46     54.75                                   
REMARK 500    ILE C  50       63.08     67.46                                   
REMARK 500    LEU C  53       51.73   -114.45                                   
REMARK 500    LYS C  72      -63.28   -100.04                                   
REMARK 500    CYS C  77      103.21     76.57                                   
REMARK 500    VAL C 108     -145.96   -130.23                                   
REMARK 500    LYS C 151      118.48   -167.52                                   
REMARK 500    PRO C 163      135.64    -39.68                                   
REMARK 500    CYS C 173       83.47   -159.41                                   
REMARK 500    ASP C 194      -33.97   -130.74                                   
REMARK 500    ALA C 267     -139.11   -169.88                                   
REMARK 500    LYS C 268     -105.59     36.99                                   
REMARK 500    ALA C 299      127.25    -30.02                                   
REMARK 500    HIS C 365      -16.32    -47.76                                   
REMARK 500    ASN D  32     -110.88     57.32                                   
REMARK 500    ILE D  50       62.31     68.28                                   
REMARK 500    LYS D  72      -65.15    -95.80                                   
REMARK 500    CYS D  77      102.00     74.88                                   
REMARK 500    VAL D  80      -61.49    -98.16                                   
REMARK 500    VAL D 108     -143.29   -128.26                                   
REMARK 500    LYS D 151      119.06   -169.40                                   
REMARK 500    CYS D 173       82.13   -161.83                                   
REMARK 500    ALA D 267     -140.46   -176.59                                   
REMARK 500    LYS D 268     -106.83     34.25                                   
REMARK 500    ALA D 299      127.88    -32.95                                   
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 1301                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1302                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1303                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1304                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1305                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1306                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1307                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1308                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1309                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1310                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1311                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1401                
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1402                
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1403                
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1404                
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1405                
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1406                
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1407                
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1408                
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1409                
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1410                
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1411                
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1412                
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1413                
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1414                
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IK2 A 450                 
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IK2 B 450                 
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IK2 C 450                 
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IK2 D 450                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SF2   RELATED DB: PDB                                   
DBREF  1SFF A    1   426  UNP    P22256   GABT_ECOLI       1    426             
DBREF  1SFF B    1   426  UNP    P22256   GABT_ECOLI       1    426             
DBREF  1SFF C    1   426  UNP    P22256   GABT_ECOLI       1    426             
DBREF  1SFF D    1   426  UNP    P22256   GABT_ECOLI       1    426             
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 GLU 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 GLU 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 GLU 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 GLU 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  A1301       5                                                       
HET    SO4  B1302       5                                                       
HET    SO4  C1303       5                                                       
HET    SO4  D1304       5                                                       
HET    SO4  B1305       5                                                       
HET    SO4  D1306       5                                                       
HET    SO4  A1307       5                                                       
HET    SO4  B1308       5                                                       
HET    SO4  C1309       5                                                       
HET    SO4  D1310       5                                                       
HET    SO4  C1311       5                                                       
HET    EDO  A1401       4                                                       
HET    EDO  B1402       4                                                       
HET    EDO  C1403       4                                                       
HET    EDO  D1404       4                                                       
HET    EDO  B1405       4                                                       
HET    EDO  A1406       4                                                       
HET    EDO  C1407       4                                                       
HET    EDO  D1408       4                                                       
HET    EDO  C1409       4                                                       
HET    EDO  A1410       4                                                       
HET    EDO  A1411       4                                                       
HET    EDO  D1412       4                                                       
HET    EDO  D1413       4                                                       
HET    EDO  B1414       4                                                       
HET    IK2  A 450      21                                                       
HET    IK2  B 450      21                                                       
HET    IK2  C 450      21                                                       
HET    IK2  D 450      21                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     IK2 4'-DEOXY-4'-ACETYLYAMINO-PYRIDOXAL-5'-PHOSPHATE                  
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  SO4    11(O4 S 2-)                                                  
FORMUL  16  EDO    14(C2 H6 O2)                                                 
FORMUL  30  IK2    4(C10 H15 N2 O8 P)                                           
FORMUL  34  HOH   *1208(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  LEU A   70  1                                  12    
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  LYS A  341  1                                  23    
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  LYS A  425  1                                  20    
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  LYS B   71  1                                  13    
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  GLY B  272  5                                   6    
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  GLU B  340  1                                  22    
HELIX   34  34 GLU B  361  ASP B  364  5                                   4    
HELIX   35  35 ASP B  369  LYS B  383  1                                  15    
HELIX   36  36 GLU B  406  LYS B  425  1                                  20    
HELIX   37  37 SER C    3  ILE C   15  1                                  13    
HELIX   38  38 ALA C   47  VAL C   52  1                                   6    
HELIX   39  39 HIS C   59  LYS C   71  1                                  13    
HELIX   40  40 TYR C   83  VAL C   97  1                                  15    
HELIX   41  41 THR C  110  LYS C  127  1                                  18    
HELIX   42  42 THR C  142  THR C  149  1                                   8    
HELIX   43  43 CYS C  173  GLY C  177  5                                   5    
HELIX   44  44 SER C  179  ASP C  194  1                                  16    
HELIX   45  45 ALA C  196  GLU C  198  5                                   3    
HELIX   46  46 SER C  218  GLY C  233  1                                  16    
HELIX   47  47 PHE C  252  MET C  257  5                                   6    
HELIX   48  48 ALA C  267  GLY C  272  5                                   6    
HELIX   49  49 ALA C  283  ASP C  287  1                                   5    
HELIX   50  50 ASN C  301  GLU C  318  1                                  18    
HELIX   51  51 ASN C  319  GLU C  340  1                                  22    
HELIX   52  52 GLU C  361  ASP C  364  5                                   4    
HELIX   53  53 ASP C  369  LYS C  383  1                                  15    
HELIX   54  54 GLU C  406  LYS C  425  1                                  20    
HELIX   55  55 SER D    3  ILE D   15  1                                  13    
HELIX   56  56 ALA D   47  VAL D   52  1                                   6    
HELIX   57  57 HIS D   59  LYS D   71  1                                  13    
HELIX   58  58 TYR D   83  VAL D   97  1                                  15    
HELIX   59  59 THR D  110  LYS D  127  1                                  18    
HELIX   60  60 THR D  142  THR D  149  1                                   8    
HELIX   61  61 CYS D  173  GLY D  177  5                                   5    
HELIX   62  62 SER D  179  ASP D  194  1                                  16    
HELIX   63  63 ALA D  196  GLU D  198  5                                   3    
HELIX   64  64 SER D  218  GLY D  233  1                                  16    
HELIX   65  65 PHE D  252  GLY D  258  5                                   7    
HELIX   66  66 ALA D  267  GLY D  272  5                                   6    
HELIX   67  67 ALA D  283  ASP D  287  1                                   5    
HELIX   68  68 ASN D  301  GLU D  318  1                                  18    
HELIX   69  69 ASN D  319  GLU D  340  1                                  22    
HELIX   70  70 GLU D  361  ASP D  364  5                                   4    
HELIX   71  71 ASP D  369  LYS D  383  1                                  15    
HELIX   72  72 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  ALA A 277   N  VAL A 108           
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  ILE A 203   O  ILE A 237           
SHEET    6   C 7 GLY A 130  PHE A 134  1  N  ILE A 132   O  VAL A 204           
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  LEU A 351  0                                        
SHEET    2   D 4 MET A 354  LEU A 359 -1  O  MET A 354   N  LEU A 351           
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  LEU A 388   O  ARG A 398           
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  PHE B 266   O  GLY B 278           
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 205   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  ALA B 356   N  ARG B 349           
SHEET    3   F 4 VAL B 396  ILE B 399 -1  O  LEU B 397   N  ILE B 357           
SHEET    4   F 4 LEU B 388  CYS B 390 -1  N  CYS B 390   O  VAL B 396           
SHEET    1   G 5 LEU C 385  ILE C 386  0                                        
SHEET    2   G 5 GLU C  42  ASP C  45  1  N  LEU C  44   O  ILE C 386           
SHEET    3   G 5 ARG C  34  ASP C  37 -1  N  VAL C  35   O  TYR C  43           
SHEET    4   G 5 HIS C  23  GLU C  31 -1  N  ASP C  28   O  TRP C  36           
SHEET    5   G 5 LEU D  81  ALA D  82  1  O  ALA D  82   N  ALA C  27           
SHEET    1   H 5 LEU C  81  ALA C  82  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  ARG D  29           
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  ALA C 277   N  VAL C 108           
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  GLY C 130   O  ALA C 201           
SHEET    7   I 7 VAL C 166  ALA C 169  1  O  TYR C 167   N  THR C 131           
SHEET    1   J 4 ILE C 345  LEU C 351  0                                        
SHEET    2   J 4 MET C 354  LEU C 359 -1  O  ALA C 356   N  ARG C 349           
SHEET    3   J 4 VAL C 396  ILE C 399 -1  O  LEU C 397   N  ILE C 357           
SHEET    4   J 4 LEU C 388  CYS C 390 -1  N  LEU C 388   O  ARG C 398           
SHEET    1   K 7 LYS D 103  VAL D 108  0                                        
SHEET    2   K 7 ALA D 277  ARG D 282 -1  O  GLY D 281   N  LYS D 104           
SHEET    3   K 7 LEU D 263  PHE D 266 -1  N  PHE D 266   O  GLY D 278           
SHEET    4   K 7 MET D 235  ASP D 239  1  N  ALA D 238   O  LEU D 263           
SHEET    5   K 7 ILE D 200  ILE D 205  1  N  ILE D 205   O  ILE D 237           
SHEET    6   K 7 GLY D 130  PHE D 134  1  N  ILE D 132   O  VAL D 204           
SHEET    7   K 7 VAL D 166  ALA D 169  1  O  ALA D 169   N  ALA D 133           
SHEET    1   L 4 ILE D 345  LEU D 351  0                                        
SHEET    2   L 4 MET D 354  LEU D 359 -1  O  ALA D 356   N  ARG D 349           
SHEET    3   L 4 VAL D 396  ILE D 399 -1  O  LEU D 397   N  ILE D 357           
SHEET    4   L 4 LEU D 388  CYS D 390 -1  N  CYS D 390   O  VAL D 396           
CISPEP   1 ASN A  153    PRO A  154          0         1.08                     
CISPEP   2 ASN B  153    PRO B  154          0         0.32                     
CISPEP   3 ASN C  153    PRO C  154          0         0.86                     
CISPEP   4 ASN D  153    PRO D  154          0         0.62                     
SITE     1 AC1  5 LYS A 151  ASN A 153  TYR A 394  HOH A1462                    
SITE     2 AC1  5 LYS C 192                                                     
SITE     1 AC2  4 LYS B 151  ASN B 153  TYR B 394  HOH D1512                    
SITE     1 AC3  5 LYS A 192  HOH A1471  LYS C 151  ASN C 153                    
SITE     2 AC3  5 TYR C 394                                                     
SITE     1 AC4  4 LYS B 192  LYS D 151  ASN D 153  TYR D 394                    
SITE     1 AC5  2 LYS B   5  ARG B 381                                          
SITE     1 AC6  4 LYS D   5  ARG D 381  HOH D1587  HOH D1680                    
SITE     1 AC7  4 ILE A 184  ARG A 224  HOH A1500  HOH A1619                    
SITE     1 AC8  3 ARG B 224  HOH B1517  HOH B1643                               
SITE     1 AC9  3 ARG C 224  HOH C1521  HOH C1570                               
SITE     1 BC1  4 HIS D 188  ARG D 224  HOH D1564  HOH D1577                    
SITE     1 BC2  6 GLN A 419  HOH A1661  HOH A1665  LYS C  71                    
SITE     2 BC2  6 HOH C1547  ARG D  29                                          
SITE     1 BC3  8 ASP A  45  ALA A  47  GLY A  48  GLY A  49                    
SITE     2 BC3  8 HIS A  57  THR B  76  VAL B  80  LEU B  81                    
SITE     1 BC4  8 THR A  76  VAL A  80  LEU A  81  ASP B  45                    
SITE     2 BC4  8 ALA B  47  GLY B  48  GLY B  49  HIS B  57                    
SITE     1 BC5  8 ASP C  45  ALA C  47  GLY C  48  GLY C  49                    
SITE     2 BC5  8 HIS C  57  THR D  76  VAL D  80  LEU D  81                    
SITE     1 BC6  8 THR C  76  VAL C  80  LEU C  81  ASP D  45                    
SITE     2 BC6  8 ALA D  47  GLY D  48  GLY D  49  HIS D  57                    
SITE     1 BC7  8 GLY B 164  HIS B 165  TYR B 167  HOH B1550                    
SITE     2 BC7  8 HOH B1585  GLY D 164  HIS D 165  TYR D 167                    
SITE     1 BC8  7 GLN A  69  LYS A  72  LEU A  73  PRO A  85                    
SITE     2 BC8  7 HOH A1518  ALA B  27  ASP B  28                               
SITE     1 BC9  8 GLN C  69  LYS C  72  LEU C  73  PRO C  85                    
SITE     2 BC9  8 HOH C1598  ALA D  27  ASP D  28  HOH D1543                    
SITE     1 CC1  7 ALA C  27  ASP C  28  GLN D  69  LYS D  72                    
SITE     2 CC1  7 LEU D  73  PRO D  85  HOH D1555                               
SITE     1 CC2  7 MET A 162  PRO A 163  EDO A1410  HOH A1452                    
SITE     2 CC2  7 HOH A1568  TYR C 167  ASP C 194                               
SITE     1 CC3  9 GLY A 164  HIS A 165  TYR A 167  HOH A1532                    
SITE     2 CC3  9 HOH A1568  GLY C 164  HIS C 165  TYR C 167                    
SITE     3 CC3  9 EDO C1409                                                     
SITE     1 CC4  5 GLN A   9  GLN D  95  LYS D  96  PRO D  98                    
SITE     2 CC4  5 GLU D 255                                                     
SITE     1 CC5  4 ILE D  22  HIS D  23  PRO D  24  ARG D 381                    
SITE     1 CC6  6 PRO C 275  ASN C 301  ILE C 303  PRO D 275                    
SITE     2 CC6  6 ASN D 301  ILE D 303                                          
SITE     1 CC7  4 ILE B  22  HIS B  23  PRO B  24  ARG B 381                    
SITE     1 CC8 21 GLY A 111  SER A 112  TYR A 138  HIS A 139                    
SITE     2 CC8 21 ARG A 141  GLU A 206  ASP A 239  VAL A 241                    
SITE     3 CC8 21 GLN A 242  LYS A 268  HOH A1414  HOH A1416                    
SITE     4 CC8 21 HOH A1459  HOH A1523  HOH A1624  HOH A1650                    
SITE     5 CC8 21 HOH A1740  GLN B  79  GLY B 296  THR B 297                    
SITE     6 CC8 21 HOH B1450                                                     
SITE     1 CC9 21 GLN A  79  GLY A 296  THR A 297  THR B 110                    
SITE     2 CC9 21 GLY B 111  SER B 112  TYR B 138  HIS B 139                    
SITE     3 CC9 21 ARG B 141  GLU B 206  ASP B 239  VAL B 241                    
SITE     4 CC9 21 GLN B 242  LYS B 268  HOH B1427  HOH B1431                    
SITE     5 CC9 21 HOH B1432  HOH B1436  HOH B1440  HOH B1580                    
SITE     6 CC9 21 HOH B1635                                                     
SITE     1 DC1 20 THR C 110  GLY C 111  SER C 112  TYR C 138                    
SITE     2 DC1 20 HIS C 139  ARG C 141  GLU C 206  ASP C 239                    
SITE     3 DC1 20 VAL C 241  GLN C 242  LYS C 268  HOH C1410                    
SITE     4 DC1 20 HOH C1424  HOH C1445  HOH C1463  HOH C1516                    
SITE     5 DC1 20 HOH C1615  GLN D  79  THR D 297  HOH D1442                    
SITE     1 DC2 21 GLN C  79  GLY C 296  THR C 297  HOH C1428                    
SITE     2 DC2 21 GLY D 111  SER D 112  TYR D 138  HIS D 139                    
SITE     3 DC2 21 ARG D 141  GLU D 206  ASP D 239  VAL D 241                    
SITE     4 DC2 21 GLN D 242  LYS D 268  HOH D1416  HOH D1429                    
SITE     5 DC2 21 HOH D1435  HOH D1505  HOH D1559  HOH D1599                    
SITE     6 DC2 21 HOH D1718                                                     
CRYST1  108.150  108.150  301.480  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      0.009246  0.005338  0.000000        0.00000                         
SCALE2      0.000000  0.010677  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003317        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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