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Database: PDB
Entry: 1SZS
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Original site: 1SZS 
HEADER    TRANSFERASE                             06-APR-04   1SZS              
TITLE     THE STRUCTURE OF GAMMA-AMINOBUTYRATE AMINOTRANSFERASE MUTANT: I50Q    
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   3   13-JUL-11 1SZS    1       VERSN                                    
REVDAT   2   24-FEB-09 1SZS    1       VERSN                                    
REVDAT   1   01-MAR-05 1SZS    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.    2.10 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) : 2.10                           
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             : 115032                         
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) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 5637                            
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            : 12828                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 267                                     
REMARK   3   SOLVENT ATOMS            : 1122                                    
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) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.53                            
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 1SZS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022134.                                      
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) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : SIEMENS                            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS HI-STAR                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 115032                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
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     (%) : 95.8                               
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) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
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): 2.76                     
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      201.13333            
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      100.56667            
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      100.56667            
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      201.13333            
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: 33900 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 48140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -258.0 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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLN B  426   OXT                                                 
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   O1   EDO B  1229     O    HOH B  1568              2.08            
REMARK 500   O1   EDO C  1230     O    HOH C  1527              2.12            
REMARK 500   OE1  GLU D   255     O    HOH D  1511              2.17            
REMARK 500   OE1  GLU C    84     O    HOH C  1486              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS D 268   CE    LYS D 268   NZ     -0.194                       
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      119.74   -161.74                                   
REMARK 500    ASN A  32     -104.23     54.24                                   
REMARK 500    GLN A  50       55.96     71.39                                   
REMARK 500    LYS A  72      -67.05    -98.49                                   
REMARK 500    CYS A  77      100.92     75.47                                   
REMARK 500    VAL A 108     -145.00   -129.20                                   
REMARK 500    LYS A 151      114.32   -172.31                                   
REMARK 500    CYS A 173       81.54   -160.45                                   
REMARK 500    ALA A 267     -144.99   -177.56                                   
REMARK 500    LYS A 268     -107.21     39.32                                   
REMARK 500    PRO A 275       99.06    -66.58                                   
REMARK 500    ALA A 299      128.53    -31.42                                   
REMARK 500    HIS A 365       -6.48    -48.61                                   
REMARK 500    LYS A 367       78.74   -119.44                                   
REMARK 500    CYS A 390     -172.45   -170.58                                   
REMARK 500    ASN B  32     -101.90     53.78                                   
REMARK 500    GLN B  50       61.19     70.70                                   
REMARK 500    LYS B  72      -61.29   -101.77                                   
REMARK 500    HIS B  75      139.62   -171.96                                   
REMARK 500    CYS B  77       99.58     78.53                                   
REMARK 500    VAL B 108     -145.81   -127.70                                   
REMARK 500    LYS B 151      110.37   -170.88                                   
REMARK 500    CYS B 173       83.79   -162.66                                   
REMARK 500    ALA B 267     -136.24   -174.70                                   
REMARK 500    LYS B 268     -106.54     31.49                                   
REMARK 500    ARG B 282      124.08    -36.80                                   
REMARK 500    ALA B 299      127.16    -36.20                                   
REMARK 500    HIS B 365       -6.56    -54.14                                   
REMARK 500    CYS B 390     -168.81   -173.14                                   
REMARK 500    PRO C  24       48.11    -78.26                                   
REMARK 500    ASN C  32     -103.30     57.81                                   
REMARK 500    GLN C  50       62.04     65.77                                   
REMARK 500    LEU C  53       53.66   -107.97                                   
REMARK 500    LYS C  72      -62.82    -95.39                                   
REMARK 500    CYS C  77       95.81     80.35                                   
REMARK 500    VAL C 108     -147.08   -127.54                                   
REMARK 500    LYS C 151      115.55   -171.27                                   
REMARK 500    CYS C 173       81.91   -156.46                                   
REMARK 500    ASP C 194      -34.87   -130.82                                   
REMARK 500    ALA C 267     -142.96   -174.19                                   
REMARK 500    LYS C 268     -106.26     37.84                                   
REMARK 500    ALA C 299      129.02    -33.35                                   
REMARK 500    HIS C 365      -16.95    -46.61                                   
REMARK 500    LYS C 367       74.76   -116.05                                   
REMARK 500    CYS C 390     -166.67   -178.08                                   
REMARK 500    PRO D  24       46.50    -73.49                                   
REMARK 500    ASN D  32     -111.89     55.26                                   
REMARK 500    GLN D  50       59.17     75.82                                   
REMARK 500    LYS D  72      -63.16    -94.21                                   
REMARK 500    CYS D  77       95.94     78.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      58 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR D 393         0.08    SIDE CHAIN                              
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 C1298        DISTANCE =  5.51 ANGSTROMS                       
REMARK 525    HOH C1433        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH D1515        DISTANCE =  5.59 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PLP D 1264                                                       
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 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1207                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1208                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1209                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1211                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1212                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1213                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1214                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1215                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1216                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1217                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1218                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1219                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1220                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1221                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1222                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1223                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1224                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1225                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1226                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1227                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1228                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1229                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1230                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1231                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1232                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 1261                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 1262                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 1263                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 1264                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP A 1271                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP B 1272                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP C 1273                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP D 1274                
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: 1SZU   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF GAMMA-AMINOBUTYRATE AMINOTRANSFERASE                
REMARK 900 MUTANT: V241A                                                        
DBREF  1SZS A    1   426  UNP    P22256   GABT_ECOLI       1    426             
DBREF  1SZS B    1   426  UNP    P22256   GABT_ECOLI       1    426             
DBREF  1SZS C    1   426  UNP    P22256   GABT_ECOLI       1    426             
DBREF  1SZS D    1   426  UNP    P22256   GABT_ECOLI       1    426             
SEQADV 1SZS GLN A   50  UNP  P22256    ILE    50 ENGINEERED                     
SEQADV 1SZS GLN B   50  UNP  P22256    ILE    50 ENGINEERED                     
SEQADV 1SZS GLN C   50  UNP  P22256    ILE    50 ENGINEERED                     
SEQADV 1SZS GLN D   50  UNP  P22256    ILE    50 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 GLN 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 GLN 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 GLN 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 GLN 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  A1201       5                                                       
HET    SO4  B1202       5                                                       
HET    SO4  B1203       5                                                       
HET    SO4  C1204       5                                                       
HET    SO4  D1205       5                                                       
HET    SO4  D1206       5                                                       
HET    SO4  A1207       5                                                       
HET    SO4  B1208       5                                                       
HET    SO4  D1209       5                                                       
HET    SO4  C1210       5                                                       
HET    SO4  D1211       5                                                       
HET    SO4  A1212       5                                                       
HET    SO4  A1213       5                                                       
HET    SO4  D1214       5                                                       
HET    SO4  C1215       5                                                       
HET    EDO  B1216       4                                                       
HET    EDO  B1217       4                                                       
HET    EDO  A1218       4                                                       
HET    EDO  B1219       4                                                       
HET    EDO  D1220       4                                                       
HET    EDO  D1221       4                                                       
HET    EDO  D1222       4                                                       
HET    EDO  A1223       4                                                       
HET    EDO  C1224       4                                                       
HET    EDO  A1225       4                                                       
HET    EDO  C1226       4                                                       
HET    EDO  D1227       4                                                       
HET    EDO  A1228       4                                                       
HET    EDO  B1229       4                                                       
HET    EDO  C1230       4                                                       
HET    EDO  D1231       4                                                       
HET    EDO  A1232       4                                                       
HET    PLP  A1261      15                                                       
HET    PLP  B1262      15                                                       
HET    PLP  C1263      15                                                       
HET    PLP  D1264      15                                                       
HET    PMP  A1271      16                                                       
HET    PMP  B1272      16                                                       
HET    PMP  C1273      16                                                       
HET    PMP  D1274      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    15(O4 S 2-)                                                  
FORMUL  20  EDO    17(C2 H6 O2)                                                 
FORMUL  37  PLP    4(C8 H10 N O6 P)                                             
FORMUL  41  PMP    4(C8 H13 N2 O5 P)                                            
FORMUL  45  HOH   *1122(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  HIS A  342  1                                  24    
HELIX   16  16 GLU A  361  ASP A  364  5                                   4    
HELIX   17  17 ASP A  369  LYS A  383  1                                  15    
HELIX   18  18 GLU A  406  GLN A  426  1                                  21    
HELIX   19  19 SER B    3  ILE B   15  1                                  13    
HELIX   20  20 ALA B   47  VAL B   52  1                                   6    
HELIX   21  21 HIS B   59  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  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  ALA B  424  1                                  19    
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 ALA C  253  GLY C  258  1                                   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  GLN C  426  1                                  21    
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  VAL A 279   N  LEU A 106           
SHEET    3   C 7 LEU A 263  PHE A 266 -1  N  PHE A 266   O  GLY A 278           
SHEET    4   C 7 MET A 235  ASP A 239  1  N  ALA A 238   O  LEU A 263           
SHEET    5   C 7 ILE A 200  ILE A 205  1  N  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  ARG A 349  0                                        
SHEET    2   D 4 ILE A 355  LEU A 359 -1  O  GLU A 358   N  GLY A 346           
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  TYR B 167   N  THR B 131           
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  MET B 354   N  LEU B 351           
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 5 LEU C 385  ILE C 386  0                                        
SHEET    2   H 5 GLU C  42  ASP C  45  1  N  LEU C  44   O  ILE C 386           
SHEET    3   H 5 ARG C  34  ASP C  37 -1  N  VAL C  35   O  TYR C  43           
SHEET    4   H 5 HIS C  23  GLU C  31 -1  N  ASP C  28   O  TRP C  36           
SHEET    5   H 5 LEU D  81  ALA D  82  1  O  ALA D  82   N  ALA C  27           
SHEET    1   I 5 LEU C  81  ALA C  82  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  ASP D  28           
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  VAL C 279   N  LEU C 106           
SHEET    3   J 7 LEU C 263  PHE C 266 -1  N  PHE C 266   O  GLY C 278           
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  GLY C 130   O  ALA C 201           
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  ALA C 356   N  ARG C 349           
SHEET    3   L 4 VAL C 396  ILE C 399 -1  O  LEU C 397   N  ILE C 357           
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  ALA D 169   N  ALA D 133           
SHEET    1   N 2 VAL D 208  GLN D 209  0                                        
SHEET    2   N 2 TYR D 215  ALA D 216 -1  O  TYR D 215   N  GLN D 209           
SHEET    1   O 4 ILE D 345  LEU D 351  0                                        
SHEET    2   O 4 MET D 354  LEU D 359 -1  O  MET D 354   N  LEU D 351           
SHEET    3   O 4 VAL D 396  ILE D 399 -1  O  ILE D 399   N  ILE D 355           
SHEET    4   O 4 LEU D 388  CYS D 390 -1  N  LEU D 388   O  ARG D 398           
LINK         NZ ALYS A 268                 C4AAPLP A1261     1555   1555  1.27  
LINK         NZ ALYS B 268                 C4AAPLP B1262     1555   1555  1.29  
LINK         NZ ALYS C 268                 C4AAPLP C1263     1555   1555  1.26  
CISPEP   1 ASN A  153    PRO A  154          0         0.64                     
CISPEP   2 ASN B  153    PRO B  154          0         0.55                     
CISPEP   3 ASN C  153    PRO C  154          0         0.64                     
CISPEP   4 ASN D  153    PRO D  154          0         0.57                     
SITE     1 AC1  3 ILE A 184  HIS A 188  ARG A 224                               
SITE     1 AC2  4 LYS B   5  ARG B 381  HOH B1430  HOH B1507                    
SITE     1 AC3  5 ILE B 184  HIS B 188  ARG B 224  HOH B1429                    
SITE     2 AC3  5 HOH B1525                                                     
SITE     1 AC4  3 HIS C 188  ARG C 224  HOH C1513                               
SITE     1 AC5  2 HIS D 188  ARG D 224                                          
SITE     1 AC6  4 HOH B1446  LYS D   5  ARG D 381  HOH D1347                    
SITE     1 AC7  5 LYS A 151  ASN A 153  TYR A 394  HOH A1326                    
SITE     2 AC7  5 LYS C 192                                                     
SITE     1 AC8  4 LYS B 151  ASN B 153  TYR B 394  LYS D 192                    
SITE     1 AC9  5 LYS B 192  LYS D 151  ASN D 153  TYR D 394                    
SITE     2 AC9  5 HOH D1523                                                     
SITE     1 BC1  5 LYS A 192  HOH A1361  LYS C 151  ASN C 153                    
SITE     2 BC1  5 TYR C 394                                                     
SITE     1 BC2  7 GLN A 419  HOH A1477  LYS C  71  HOH C1385                    
SITE     2 BC2  7 ARG D  29  HOH D1399  HOH D1534                               
SITE     1 BC3  9 GLN A  50  TYR A 138  ARG A 141  HOH A1351                    
SITE     2 BC3  9 HOH A1458  HOH A1548  CYS B  77  GLN B  79                    
SITE     3 BC3  9 GLY B 296                                                     
SITE     1 BC4 11 CYS A  77  GLN A  79  GLY A 295  GLY A 296                    
SITE     2 BC4 11 HOH A1448  GLN B  50  TYR B 138  ARG B 141                    
SITE     3 BC4 11 HOH B1273  HOH B1568  HOH B1569                               
SITE     1 BC5 11 GLN C  50  ARG C 141  EDO C1230  HOH C1287                    
SITE     2 BC5 11 HOH C1527  CYS D  77  GLN D  79  GLY D 295                    
SITE     3 BC5 11 GLY D 296  HOH D1315  HOH D1559                               
SITE     1 BC6  6 GLN C  79  GLY C 296  GLN D  50  ARG D 141                    
SITE     2 BC6  6 HOH D1305  HOH D1432                                          
SITE     1 BC7  8 THR A  76  VAL A  80  LEU A  81  ASP B  45                    
SITE     2 BC7  8 ALA B  47  GLY B  48  GLY B  49  HIS B  57                    
SITE     1 BC8  4 ILE B  22  HIS B  23  ARG B 381  HOH B1404                    
SITE     1 BC9 10 GLY A 164  HIS A 165  VAL A 166  TYR A 167                    
SITE     2 BC9 10 HOH A1507  GLY C 164  HIS C 165  VAL C 166                    
SITE     3 BC9 10 TYR C 167  HOH C1484                                          
SITE     1 CC1  9 GLY B 164  HIS B 165  VAL B 166  TYR B 167                    
SITE     2 CC1  9 HOH B1472  GLY D 164  HIS D 165  VAL D 166                    
SITE     3 CC1  9 TYR D 167                                                     
SITE     1 CC2  7 THR C  76  VAL C  80  ASP D  45  ALA D  47                    
SITE     2 CC2  7 GLY D  48  GLY D  49  HIS D  57                               
SITE     1 CC3  4 PRO C 275  ASN C 301  PRO D 275  ASN D 301                    
SITE     1 CC4  4 ILE D  22  HIS D  23  PRO D  24  ARG D 381                    
SITE     1 CC5  8 ASP A  45  ALA A  47  GLY A  48  GLY A  49                    
SITE     2 CC5  8 HIS A  57  THR B  76  VAL B  80  LEU B  81                    
SITE     1 CC6  8 ASP C  45  ALA C  47  GLY C  48  GLY C  49                    
SITE     2 CC6  8 HIS C  57  THR D  76  VAL D  80  LEU D  81                    
SITE     1 CC7  4 GLN A  69  PRO A  85  ALA B  27  ASP B  28                    
SITE     1 CC8  7 GLN C  69  LYS C  72  LEU C  73  PRO C  85                    
SITE     2 CC8  7 HOH C1444  ASP D  28  HOH D1389                               
SITE     1 CC9  5 TYR B 167  TYR D 167  ARG D 168  HOH D1403                    
SITE     2 CC9  5 HOH D1465                                                     
SITE     1 DC1  4 GLN A   9  LYS D  96  PRO D  98  GLU D 255                    
SITE     1 DC2  6 TYR B 155  GLU B 211  ARG B 398  HOH B1501                    
SITE     2 DC2  6 HOH B1568  HOH B1570                                          
SITE     1 DC3  7 GLN C  50  GLU C 211  GLN C 242  ARG C 398                    
SITE     2 DC3  7 HOH C1527  SO4 D1214  HOH D1559                               
SITE     1 DC4  8 GLN D  50  GLU D 211  GLN D 242  LYS D 268                    
SITE     2 DC4  8 ARG D 398  PMP D1274  HOH D1432  HOH D1560                    
SITE     1 DC5  6 GLN A  50  GLU A 211  GLN A 242  ARG A 398                    
SITE     2 DC5  6 PMP A1271  HOH A1458                                          
SITE     1 DC6 16 GLY A 111  SER A 112  TYR A 138  HIS A 139                    
SITE     2 DC6 16 GLU A 206  ASP A 239  VAL A 241  GLN A 242                    
SITE     3 DC6 16 LYS A 268  HOH A1273  HOH A1277  HOH A1281                    
SITE     4 DC6 16 HOH A1351  HOH A1378  THR B 297  HOH B1343                    
SITE     1 DC7 17 THR A 297  HOH A1315  THR B 110  GLY B 111                    
SITE     2 DC7 17 SER B 112  TYR B 138  HIS B 139  GLU B 206                    
SITE     3 DC7 17 ASP B 239  VAL B 241  GLN B 242  LYS B 268                    
SITE     4 DC7 17 HOH B1273  HOH B1280  HOH B1288  HOH B1318                    
SITE     5 DC7 17 HOH B1382                                                     
SITE     1 DC8 16 GLY C 111  SER C 112  TYR C 138  HIS C 139                    
SITE     2 DC8 16 GLU C 206  ASP C 239  VAL C 241  GLN C 242                    
SITE     3 DC8 16 LYS C 268  HOH C1287  HOH C1290  HOH C1293                    
SITE     4 DC8 16 HOH C1306  HOH C1331  HOH C1496  THR D 297                    
SITE     1 DC9 16 THR C 297  HOH C1291  GLY D 111  SER D 112                    
SITE     2 DC9 16 TYR D 138  HIS D 139  GLU D 206  ASP D 239                    
SITE     3 DC9 16 VAL D 241  GLN D 242  LYS D 268  HOH D1275                    
SITE     4 DC9 16 HOH D1285  HOH D1288  HOH D1305  HOH D1311                    
SITE     1 EC1 18 GLN A  50  THR A 110  GLY A 111  SER A 112                    
SITE     2 EC1 18 TYR A 138  HIS A 139  GLU A 206  ASP A 239                    
SITE     3 EC1 18 VAL A 241  GLN A 242  LYS A 268  EDO A1232                    
SITE     4 EC1 18 HOH A1273  HOH A1277  HOH A1281  HOH A1351                    
SITE     5 EC1 18 THR B 297  HOH B1343                                          
SITE     1 EC2 19 THR A 297  HOH A1315  GLN B  50  THR B 110                    
SITE     2 EC2 19 GLY B 111  SER B 112  TYR B 138  HIS B 139                    
SITE     3 EC2 19 GLU B 206  ASP B 239  VAL B 241  GLN B 242                    
SITE     4 EC2 19 LYS B 268  HOH B1273  HOH B1280  HOH B1288                    
SITE     5 EC2 19 HOH B1318  HOH B1382  HOH B1569                               
SITE     1 EC3 18 THR C 110  GLY C 111  SER C 112  TYR C 138                    
SITE     2 EC3 18 HIS C 139  GLU C 206  ASP C 239  VAL C 241                    
SITE     3 EC3 18 GLN C 242  LYS C 268  HOH C1287  HOH C1290                    
SITE     4 EC3 18 HOH C1293  HOH C1306  HOH C1331  HOH C1496                    
SITE     5 EC3 18 THR D 297  HOH D1559                                          
SITE     1 EC4 20 THR C 297  HOH C1291  GLN D  50  THR D 110                    
SITE     2 EC4 20 GLY D 111  SER D 112  TYR D 138  HIS D 139                    
SITE     3 EC4 20 GLU D 206  ASP D 239  VAL D 241  GLN D 242                    
SITE     4 EC4 20 LYS D 268  EDO D1231  HOH D1275  HOH D1285                    
SITE     5 EC4 20 HOH D1288  HOH D1305  HOH D1311  HOH D1563                    
CRYST1  108.100  108.100  301.700  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      0.009251  0.005341  0.000000        0.00000                         
SCALE2      0.000000  0.010682  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003315        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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