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Database: PDB
Entry: 1SZU
LinkDB: 1SZU
Original site: 1SZU 
HEADER    TRANSFERASE                             06-APR-04   1SZU              
TITLE     THE STRUCTURE OF GAMMA-AMINOBUTYRATE AMINOTRANSFERASE MUTANT: V241A   
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 TRANSAMINASE,     
COMPND   5 GLUTAMATE:SUCCINIC SEMIALDEHYDE TRANSAMINASE, GABA AMINOTRANSFERASE, 
COMPND   6 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 GENE: GABT, B2662;                                                   
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GABA-AT, TRANSFERASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.LIU,P.E.PETERSON,J.A.LANGSTON,X.JIN,X.ZHOU,A.J.FISHER,M.D.TONEY     
REVDAT   4   16-NOV-11 1SZU    1       HETATM                                   
REVDAT   3   13-JUL-11 1SZU    1       VERSN                                    
REVDAT   2   24-FEB-09 1SZU    1       VERSN                                    
REVDAT   1   01-MAR-05 1SZU    0                                                
JRNL        AUTH   W.LIU,P.E.PETERSON,J.A.LANGSTON,X.JIN,X.ZHOU,A.J.FISHER,     
JRNL        AUTH 2 M.D.TONEY                                                    
JRNL        TITL   KINETIC AND CRYSTALLOGRAPHIC ANALYSIS OF ACTIVE SITE MUTANTS 
JRNL        TITL 2 OF ESCHERICHIA COLIGAMMA-AMINOBUTYRATE AMINOTRANSFERASE.     
JRNL        REF    BIOCHEMISTRY                  V.  44  2982 2005              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15723541                                                     
JRNL        DOI    10.1021/BI048657A                                            
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             : 68806                          
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) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3422                            
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            : 12816                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 235                                     
REMARK   3   SOLVENT ATOMS            : 955                                     
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.44                            
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) : 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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1SZU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022135.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-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                       : BL9-1                              
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                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MARXDS                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68806                              
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     (%) : 98.2                               
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) : 2.52                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
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   (%): 55.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, AMMONIUM SULFATE, PLP, PH 7.6,    
REMARK 280  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      201.10667            
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      100.55333            
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      100.55333            
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      201.10667            
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: 32520 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 48610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -188.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1692  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     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 D  1808     O    HOH D  1811              2.14            
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    ASN A  32     -105.21     59.75                                   
REMARK 500    ILE A  50       68.07     68.07                                   
REMARK 500    LEU A  53       50.05   -109.60                                   
REMARK 500    LYS A  72      -63.86   -100.43                                   
REMARK 500    THR A  76      -20.45   -141.75                                   
REMARK 500    CYS A  77       98.53     76.62                                   
REMARK 500    VAL A 108     -150.24   -128.26                                   
REMARK 500    LYS A 151      114.79   -163.12                                   
REMARK 500    CYS A 173       84.39   -160.91                                   
REMARK 500    ALA A 267     -154.85   -174.47                                   
REMARK 500    LYS A 268     -105.22     47.35                                   
REMARK 500    ALA A 299      125.63    -28.86                                   
REMARK 500    HIS A 365       32.18    -57.51                                   
REMARK 500    ASN A 366       12.69   -157.85                                   
REMARK 500    ASN B  32     -103.04     54.99                                   
REMARK 500    ILE B  50       64.28     70.39                                   
REMARK 500    THR B  76      -18.36   -142.10                                   
REMARK 500    CYS B  77      100.14     74.08                                   
REMARK 500    VAL B 108     -154.69   -125.89                                   
REMARK 500    LYS B 151      115.46   -174.44                                   
REMARK 500    TYR B 155      -28.58    -37.57                                   
REMARK 500    CYS B 173       80.91   -162.08                                   
REMARK 500    ALA B 267     -149.13   -175.00                                   
REMARK 500    LYS B 268     -100.04     39.08                                   
REMARK 500    ALA B 299      124.32    -29.26                                   
REMARK 500    ASP B 347      134.69   -172.04                                   
REMARK 500    HIS B 365       -2.66    -56.95                                   
REMARK 500    GLU C  31      117.42   -160.71                                   
REMARK 500    ASN C  32     -107.60     55.23                                   
REMARK 500    ILE C  50       70.42     69.47                                   
REMARK 500    LEU C  53       50.02   -113.81                                   
REMARK 500    CYS C  77       93.62     81.55                                   
REMARK 500    VAL C 108     -152.51   -121.39                                   
REMARK 500    PRO C 163      130.65    -37.92                                   
REMARK 500    CYS C 173       77.89   -165.24                                   
REMARK 500    ASP C 194      -33.46   -131.00                                   
REMARK 500    ALA C 267     -153.75   -174.29                                   
REMARK 500    LYS C 268     -105.93     42.23                                   
REMARK 500    ALA C 299      128.50    -27.85                                   
REMARK 500    HIS C 365      -12.94    -44.97                                   
REMARK 500    CYS C 390     -169.08   -178.96                                   
REMARK 500    LYS C 425       58.73   -112.11                                   
REMARK 500    ASN D  32     -109.12     57.98                                   
REMARK 500    ILE D  50       64.37     74.26                                   
REMARK 500    LEU D  53       51.08   -119.31                                   
REMARK 500    LYS D  72      -60.39    -94.07                                   
REMARK 500    THR D  76      -19.33   -143.94                                   
REMARK 500    CYS D  77       98.74     76.98                                   
REMARK 500    VAL D 108     -149.56   -121.09                                   
REMARK 500    PRO D 163      141.69    -39.76                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      58 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B1773        DISTANCE =  5.66 ANGSTROMS                       
REMARK 525    HOH B1790        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH C1720        DISTANCE =  5.49 ANGSTROMS                       
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 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1024                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1025                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1026                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1027                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1028                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1029                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1030                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1031                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1032                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1033                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1034                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 1466                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 1467                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 1468                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 1469                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP A 1566                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP B 1567                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP C 1568                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP D 1569                
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                                         
REMARK 900 RELATED ID: 1SZK   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF GAMMA-AMINOBUTYRATE AMINOTRANSFERASE                
REMARK 900 MUTANT: E211S                                                        
REMARK 900 RELATED ID: 1SZS   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF GAMMA-AMINOBUTYRATE AMINOTRANSFERASE: I50Q          
DBREF  1SZU A    1   426  UNP    P22256   GABT_ECOLI       1    426             
DBREF  1SZU B    1   426  UNP    P22256   GABT_ECOLI       1    426             
DBREF  1SZU C    1   426  UNP    P22256   GABT_ECOLI       1    426             
DBREF  1SZU D    1   426  UNP    P22256   GABT_ECOLI       1    426             
SEQADV 1SZU ALA A  241  UNP  P22256    VAL   241 ENGINEERED                     
SEQADV 1SZU ALA B  241  UNP  P22256    VAL   241 ENGINEERED                     
SEQADV 1SZU ALA C  241  UNP  P22256    VAL   241 ENGINEERED                     
SEQADV 1SZU ALA D  241  UNP  P22256    VAL   241 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 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 ALA 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 ALA 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 ALA 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 ALA 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  A1001       5                                                       
HET    SO4  B1002       5                                                       
HET    SO4  B1003       5                                                       
HET    SO4  C1004       5                                                       
HET    SO4  D1005       5                                                       
HET    SO4  D1006       5                                                       
HET    SO4  A1007       5                                                       
HET    SO4  B1008       5                                                       
HET    SO4  B1009       5                                                       
HET    SO4  C1010       5                                                       
HET    SO4  C1011       5                                                       
HET    EDO  B1021       4                                                       
HET    EDO  B1022       4                                                       
HET    EDO  A1023       4                                                       
HET    EDO  B1024       4                                                       
HET    EDO  D1025       4                                                       
HET    EDO  D1026       4                                                       
HET    EDO  D1027       4                                                       
HET    EDO  A1028       4                                                       
HET    EDO  C1029       4                                                       
HET    EDO  A1030       4                                                       
HET    EDO  C1031       4                                                       
HET    EDO  D1032       4                                                       
HET    EDO  A1033       4                                                       
HET    EDO  C1034       4                                                       
HET    PLP  A1466      15                                                       
HET    PLP  B1467      15                                                       
HET    PLP  C1468      15                                                       
HET    PLP  D1469      15                                                       
HET    PMP  A1566      16                                                       
HET    PMP  B1567      16                                                       
HET    PMP  C1568      16                                                       
HET    PMP  D1569      16                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     PMP 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE                          
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
HETSYN     PMP PYRIDOXAMINE-5'-PHOSPHATE                                        
FORMUL   5  SO4    11(O4 S 2-)                                                  
FORMUL  16  EDO    14(C2 H6 O2)                                                 
FORMUL  30  PLP    4(C8 H10 N O6 P)                                             
FORMUL  34  PMP    4(C8 H13 N2 O5 P)                                            
FORMUL  38  HOH   *955(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  HIS B  232  1                                  15    
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  LYS B  341  1                                  23    
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  GLN B  426  1                                  21    
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  LEU C   70  1                                  12    
HELIX   40  40 GLU C   84  VAL C   97  1                                  14    
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  HIS C  342  1                                  24    
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 4 ALA A  27  GLU A  31  0                                        
SHEET    2   A 4 ARG A  34  ASP A  37 -1  O  TRP A  36   N  ASP A  28           
SHEET    3   A 4 GLU A  42  ASP A  45 -1  O  TYR A  43   N  VAL A  35           
SHEET    4   A 4 LEU A 385  ILE A 386  1  O  ILE A 386   N  LEU A  44           
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  THR A 264   O  THR A 280           
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  ALA A 169   N  ALA A 133           
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 2 VAL B 208  GLN B 209  0                                        
SHEET    2   F 2 TYR B 215  ALA B 216 -1  O  TYR B 215   N  GLN B 209           
SHEET    1   G 4 ILE B 345  LEU B 351  0                                        
SHEET    2   G 4 MET B 354  LEU B 359 -1  O  ALA B 356   N  ARG B 349           
SHEET    3   G 4 VAL B 396  ILE B 399 -1  O  LEU B 397   N  ILE B 357           
SHEET    4   G 4 LEU B 388  CYS B 390 -1  N  CYS B 390   O  VAL B 396           
SHEET    1   H 4 ALA C  27  GLU C  31  0                                        
SHEET    2   H 4 ARG C  34  ASP C  37 -1  O  TRP C  36   N  ASP C  28           
SHEET    3   H 4 GLU C  42  ASP C  45 -1  O  TYR C  43   N  VAL C  35           
SHEET    4   H 4 LEU C 385  ILE C 386  1  O  ILE C 386   N  LEU C  44           
SHEET    1   I 5 LEU C  81  TYR C  83  0                                        
SHEET    2   I 5 HIS D  23  GLU D  31  1  O  ALA D  27   N  ALA C  82           
SHEET    3   I 5 ARG D  34  ASP D  37 -1  O  TRP D  36   N  ARG D  29           
SHEET    4   I 5 GLU D  42  ASP D  45 -1  O  TYR D  43   N  VAL D  35           
SHEET    5   I 5 LEU D 385  ILE D 386  1  O  ILE D 386   N  LEU D  44           
SHEET    1   J 7 LYS C 103  VAL C 108  0                                        
SHEET    2   J 7 ALA C 277  ARG C 282 -1  O  GLY C 281   N  LYS C 104           
SHEET    3   J 7 LEU C 263  PHE C 266 -1  N  THR C 264   O  THR C 280           
SHEET    4   J 7 MET C 235  ASP C 239  1  N  ALA C 238   O  LEU C 263           
SHEET    5   J 7 ILE C 200  ILE C 205  1  N  ILE C 203   O  ILE C 237           
SHEET    6   J 7 GLY C 130  PHE C 134  1  N  ILE C 132   O  VAL C 204           
SHEET    7   J 7 VAL C 166  ALA C 169  1  O  TYR C 167   N  THR C 131           
SHEET    1   K 2 VAL C 208  GLN C 209  0                                        
SHEET    2   K 2 TYR C 215  ALA C 216 -1  O  TYR C 215   N  GLN C 209           
SHEET    1   L 4 ILE C 345  LEU C 351  0                                        
SHEET    2   L 4 MET C 354  LEU C 359 -1  O  MET C 354   N  LEU C 351           
SHEET    3   L 4 VAL C 396  ILE C 399 -1  O  ILE C 399   N  ILE C 355           
SHEET    4   L 4 LEU C 388  CYS C 390 -1  N  LEU C 388   O  ARG C 398           
SHEET    1   M 7 LYS D 103  VAL D 108  0                                        
SHEET    2   M 7 ALA D 277  ARG D 282 -1  O  VAL D 279   N  LEU D 106           
SHEET    3   M 7 LEU D 263  PHE D 266 -1  N  THR D 264   O  THR D 280           
SHEET    4   M 7 MET D 235  ASP D 239  1  N  ALA D 238   O  LEU D 263           
SHEET    5   M 7 ILE D 200  ILE D 205  1  N  ILE D 205   O  ASP D 239           
SHEET    6   M 7 GLY D 130  PHE D 134  1  N  ILE D 132   O  VAL D 204           
SHEET    7   M 7 VAL D 166  ALA D 169  1  O  TYR D 167   N  ALA D 133           
SHEET    1   N 4 ILE D 345  LEU D 351  0                                        
SHEET    2   N 4 MET D 354  LEU D 359 -1  O  MET D 354   N  LEU D 351           
SHEET    3   N 4 VAL D 396  ILE D 399 -1  O  ILE D 399   N  ILE D 355           
SHEET    4   N 4 LEU D 388  CYS D 390 -1  N  LEU D 388   O  ARG D 398           
LINK         NZ ALYS A 268                 C4AAPLP A1466     1555   1555  1.28  
LINK         NZ ALYS B 268                 C4AAPLP B1467     1555   1555  1.27  
LINK         NZ ALYS C 268                 C4AAPLP C1468     1555   1555  1.27  
LINK         NZ ALYS D 268                 C4AAPLP D1469     1555   1555  1.28  
CISPEP   1 ASN A  153    PRO A  154          0         0.63                     
CISPEP   2 ASN B  153    PRO B  154          0         0.51                     
CISPEP   3 ASN C  153    PRO C  154          0         0.39                     
CISPEP   4 ASN D  153    PRO D  154          0         0.46                     
SITE     1 AC1  3 ARG A 224  HOH A1725  HOH A1808                               
SITE     1 AC2  3 LYS B   5  ARG B 381  HOH B1710                               
SITE     1 AC3  3 ILE B 184  HIS B 188  ARG B 224                               
SITE     1 AC4  2 HIS C 188  ARG C 224                                          
SITE     1 AC5  2 ILE D 184  ARG D 224                                          
SITE     1 AC6  3 HOH B1725  LYS D   5  ARG D 381                               
SITE     1 AC7  4 LYS A 151  ASN A 153  TYR A 394  LYS C 192                    
SITE     1 AC8  3 ASN B 153  TYR B 394  LYS D 192                               
SITE     1 AC9  3 LYS B 192  LYS D 151  TYR D 394                               
SITE     1 BC1  3 LYS A 192  ASN C 153  TYR C 394                               
SITE     1 BC2  4 GLN A 419  HOH A1768  LYS C  71  ARG D  29                    
SITE     1 BC3  8 THR A  76  VAL A  80  LEU A  81  ASP B  45                    
SITE     2 BC3  8 ALA B  47  GLY B  48  GLY B  49  HIS B  57                    
SITE     1 BC4  3 HIS B  23  ARG B 381  HOH B1820                               
SITE     1 BC5  7 GLY A 164  HIS A 165  TYR A 167  GLY C 164                    
SITE     2 BC5  7 HIS C 165  VAL C 166  TYR C 167                               
SITE     1 BC6  8 GLY B 164  HIS B 165  VAL B 166  TYR B 167                    
SITE     2 BC6  8 HOH B1579  HIS D 165  VAL D 166  TYR D 167                    
SITE     1 BC7  7 THR C  76  VAL C  80  ASP D  45  ALA D  47                    
SITE     2 BC7  7 GLY D  48  GLY D  49  HIS D  57                               
SITE     1 BC8  5 PRO C 275  ASN C 301  PRO D 275  ASN D 301                    
SITE     2 BC8  5 ILE D 303                                                     
SITE     1 BC9  3 ILE D  22  HIS D  23  ARG D 381                               
SITE     1 CC1  8 ASP A  45  ALA A  47  GLY A  48  GLY A  49                    
SITE     2 CC1  8 HIS A  57  THR B  76  VAL B  80  LEU B  81                    
SITE     1 CC2  8 ASP C  45  ALA C  47  GLY C  48  GLY C  49                    
SITE     2 CC2  8 HIS C  57  THR D  76  VAL D  80  LEU D  81                    
SITE     1 CC3  6 GLN A  69  LYS A  72  LEU A  73  PRO A  85                    
SITE     2 CC3  6 ASP B  28  HOH B1747                                          
SITE     1 CC4  6 GLN C  69  LEU C  73  PRO C  85  HOH C1658                    
SITE     2 CC4  6 ALA D  27  ASP D  28                                          
SITE     1 CC5  5 TYR B 167  HOH B1745  TYR D 167  ARG D 168                    
SITE     2 CC5  5 HOH D1695                                                     
SITE     1 CC6  5 GLN A   9  GLN D  95  LYS D  96  PRO D  98                    
SITE     2 CC6  5 GLU D 255                                                     
SITE     1 CC7  7 GLN C  79  GLY C 292  LEU C 294  HOH C1775                    
SITE     2 CC7  7 GLY D  18  GLY D  20  ILE D  22                               
SITE     1 CC8 15 GLY A 111  SER A 112  TYR A 138  GLU A 206                    
SITE     2 CC8 15 ASP A 239  ALA A 241  GLN A 242  LYS A 268                    
SITE     3 CC8 15 HOH A1568  HOH A1572  HOH A1577  HOH A1814                    
SITE     4 CC8 15 GLY B 296  THR B 297  HOH B1636                               
SITE     1 CC9 16 THR A 297  HOH A1614  THR B 110  GLY B 111                    
SITE     2 CC9 16 SER B 112  TYR B 138  HIS B 139  GLU B 206                    
SITE     3 CC9 16 ASP B 239  ALA B 241  GLN B 242  LYS B 268                    
SITE     4 CC9 16 HOH B1574  HOH B1582  HOH B1611  HOH B1814                    
SITE     1 DC1 17 THR C 110  GLY C 111  SER C 112  TYR C 138                    
SITE     2 DC1 17 HIS C 139  GLU C 206  ASP C 239  ALA C 241                    
SITE     3 DC1 17 GLN C 242  LYS C 268  HOH C1582  HOH C1585                    
SITE     4 DC1 17 HOH C1588  HOH C1627  GLY D 296  THR D 297                    
SITE     5 DC1 17 HOH D1613                                                     
SITE     1 DC2 17 THR C 297  HOH C1586  THR D 110  GLY D 111                    
SITE     2 DC2 17 SER D 112  TYR D 138  HIS D 139  GLU D 206                    
SITE     3 DC2 17 ASP D 239  ALA D 241  GLN D 242  LYS D 268                    
SITE     4 DC2 17 HOH D1570  HOH D1580  HOH D1583  HOH D1808                    
SITE     5 DC2 17 HOH D1811                                                     
SITE     1 DC3 18 THR A 110  GLY A 111  SER A 112  TYR A 138                    
SITE     2 DC3 18 HIS A 139  GLU A 206  GLU A 211  ASP A 239                    
SITE     3 DC3 18 ALA A 241  GLN A 242  LYS A 268  HOH A1568                    
SITE     4 DC3 18 HOH A1572  HOH A1577  HOH A1811  HOH A1814                    
SITE     5 DC3 18 THR B 297  HOH B1636                                          
SITE     1 DC4 20 THR A 297  HOH A1614  THR B 110  GLY B 111                    
SITE     2 DC4 20 SER B 112  TYR B 138  HIS B 139  GLU B 206                    
SITE     3 DC4 20 GLU B 211  ASP B 239  ALA B 241  GLN B 242                    
SITE     4 DC4 20 LYS B 268  HOH B1574  HOH B1582  HOH B1611                    
SITE     5 DC4 20 HOH B1616  HOH B1811  HOH B1814  HOH B1817                    
SITE     1 DC5 17 THR C 110  GLY C 111  SER C 112  TYR C 138                    
SITE     2 DC5 17 HIS C 139  GLU C 206  ASP C 239  ALA C 241                    
SITE     3 DC5 17 GLN C 242  LYS C 268  HOH C1582  HOH C1585                    
SITE     4 DC5 17 HOH C1588  HOH C1627  HOH C1774  THR D 297                    
SITE     5 DC5 17 HOH D1613                                                     
SITE     1 DC6 19 THR C 297  HOH C1586  THR D 110  GLY D 111                    
SITE     2 DC6 19 SER D 112  TYR D 138  HIS D 139  GLU D 206                    
SITE     3 DC6 19 GLU D 211  ASP D 239  ALA D 241  GLN D 242                    
SITE     4 DC6 19 LYS D 268  HOH D1570  HOH D1580  HOH D1583                    
SITE     5 DC6 19 HOH D1808  HOH D1810  HOH D1811                               
CRYST1  108.200  108.200  301.660  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      0.009242  0.005336  0.000000        0.00000                         
SCALE2      0.000000  0.010672  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003315        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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