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Database: PDB
Entry: 1GC4
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HEADER    TRANSFERASE                             19-JUL-00   1GC4              
TITLE     THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2        
TITLE    2 COMPLEXED WITH ASPARTATE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ASPARTATE AMINOTRANSFERASE;                                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 2.6.1.1;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   3 ORGANISM_TAXID: 300852;                                              
SOURCE   4 STRAIN: HB8;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET3A                                     
KEYWDS    AMINOTRANSFERASE, DUAL-SUBSTRATE ENZYME, PYRIDOXAL ENZYME,            
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.URA,T.NAKAI,K.HIROTSU,S.KURAMITSU                                   
REVDAT   8   27-DEC-23 1GC4    1       REMARK                                   
REVDAT   7   10-NOV-21 1GC4    1       REMARK SEQADV LINK                       
REVDAT   6   04-DEC-19 1GC4    1       REMARK                                   
REVDAT   5   16-OCT-19 1GC4    1       JRNL   LINK                              
REVDAT   4   13-JUL-11 1GC4    1       VERSN                                    
REVDAT   3   24-FEB-09 1GC4    1       VERSN                                    
REVDAT   2   28-JAN-03 1GC4    1       REMARK                                   
REVDAT   1   05-SEP-01 1GC4    0                                                
JRNL        AUTH   H.URA,T.NAKAI,S.I.KAWAGUCHI,I.MIYAHARA,K.HIROTSU,S.KURAMITSU 
JRNL        TITL   SUBSTRATE RECOGNITION MECHANISM OF THERMOPHILIC              
JRNL        TITL 2 DUAL-SUBSTRATE ENZYME.                                       
JRNL        REF    J.BIOCHEM.                    V. 130    89 2001              
JRNL        REFN                   ISSN 0021-924X                               
JRNL        PMID   11432784                                                     
JRNL        DOI    10.1093/OXFORDJOURNALS.JBCHEM.A002966                        
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.NAKAI,K.OKADA,S.AKUTSU,I.MIYAHARA,S.KAWAGUCHI,R.KATO,      
REMARK   1  AUTH 2 S.KURAMITSU,K.HIROTSU                                        
REMARK   1  TITL   STRUCTURE OF THERMUS THERMUOPHILUS HB8 ASPARTATE             
REMARK   1  TITL 2 AMINOTRANSFERASE AND ITS COMPLEX WITH MALEATE                
REMARK   1  REF    BIOCHEMISTRY                  V.  38  2413 1999              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  DOI    10.1021/BI9819881                                            
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.NOBE,S.KAWAGUCHI,H.URA,T.NAKAI,K.HIROTSU,R.KATO,           
REMARK   1  AUTH 2 S.KURAMITSU                                                  
REMARK   1  TITL   THE NOVEL SUBSTRATE RECOGNITION MECHANISM UTILIZED BY        
REMARK   1  TITL 2 ASPARTATE AMINOTRANSFERSE OF THE EXTREME THERMOPHILE THERMUS 
REMARK   1  TITL 3 THERMOPHILUS HB8                                             
REMARK   1  REF    J.BIOL.CHEM.                  V. 273 29554 1998              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  DOI    10.1074/JBC.273.45.29554                                     
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   A.OKAMOTO,R.KATO,R.MASUI,A.YAMAGISHI,T.OSHIMA,S.KURAMITSU    
REMARK   1  TITL   AN ASPARTATE AMINOTRANSFERASE FROM AN EXTREMELY THERMOPHILIC 
REMARK   1  TITL 2 BACTERIUM, THERMUS THERMOPHILUS HB8                          
REMARK   1  REF    J.BIOCHEM.(TOKYO)             V. 119   135 1996              
REMARK   1  REFN                   ISSN 0021-924X                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
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)   (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 22781                          
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) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.934                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2263                            
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            : 11792                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 96                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.30                          
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) : 2.051                           
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  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 1GC4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JUL-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000005026.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 293.0                              
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22781                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 1.600                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15300                            
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: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, HEPES, SODIUM ACETATE, PH      
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       51.17000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     GLY A   383                                                      
REMARK 465     ARG A   384                                                      
REMARK 465     ALA A   385                                                      
REMARK 465     GLY B   883                                                      
REMARK 465     ARG B   884                                                      
REMARK 465     ALA B   885                                                      
REMARK 465     GLY C  1383                                                      
REMARK 465     ARG C  1384                                                      
REMARK 465     ALA C  1385                                                      
REMARK 465     GLY D  1883                                                      
REMARK 465     ARG D  1884                                                      
REMARK 465     ALA D  1885                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    ARG B   528     OE1  GLU D  1525     1445     2.19            
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    GLU D1525   CG    GLU D1525   CD     -0.109                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    VAL A  31   N   -  CA  -  C   ANGL. DEV. =  16.5 DEGREES          
REMARK 500    ARG A 159   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG A 159   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ASN A 175   N   -  CA  -  C   ANGL. DEV. = -17.0 DEGREES          
REMARK 500    ARG A 361   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ARG B 659   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B 659   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASN C1175   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    ASN D1675   N   -  CA  -  C   ANGL. DEV. = -16.8 DEGREES          
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    SER A   5     -176.23    -68.09                                   
REMARK 500    VAL A  31      106.41     23.80                                   
REMARK 500    LEU A  36       38.93    -91.23                                   
REMARK 500    THR A  37      -79.60    -81.77                                   
REMARK 500    PRO A  41      167.06    -47.19                                   
REMARK 500    LYS A  61       47.80    -87.92                                   
REMARK 500    GLU A  84      -70.94    -75.08                                   
REMARK 500    ASN A  85        1.88    -67.85                                   
REMARK 500    VAL A 126      -32.20    -31.06                                   
REMARK 500    TYR A 128      -48.57    -26.72                                   
REMARK 500    PHE A 150       -5.68     59.28                                   
REMARK 500    PRO A 154      -10.57    -45.98                                   
REMARK 500    THR A 165      108.27    -40.72                                   
REMARK 500    LYS A 183      -49.63    -26.45                                   
REMARK 500    ASP A 197       76.18     56.73                                   
REMARK 500    ASN A 230     -168.50   -100.44                                   
REMARK 500    MET A 238       48.67    -98.40                                   
REMARK 500    THR A 265      -60.21     85.36                                   
REMARK 500    GLU A 305      -74.44    -78.89                                   
REMARK 500    ALA A 314      147.59   -170.01                                   
REMARK 500    ALA A 320     -155.49     53.17                                   
REMARK 500    ALA A 356       65.38   -115.48                                   
REMARK 500    ARG A 380      -70.46    -47.04                                   
REMARK 500    SER B 505     -176.03    -67.39                                   
REMARK 500    VAL B 531      112.85     22.76                                   
REMARK 500    LEU B 536       39.26    -92.11                                   
REMARK 500    THR B 537      -79.36    -80.11                                   
REMARK 500    PRO B 541      166.98    -47.75                                   
REMARK 500    PRO B 546      144.98    -39.23                                   
REMARK 500    LYS B 561       47.89    -87.41                                   
REMARK 500    GLU B 584      -72.53    -70.79                                   
REMARK 500    ASN B 585        1.31    -65.90                                   
REMARK 500    VAL B 626      -31.30    -31.82                                   
REMARK 500    TYR B 628      -47.42    -27.17                                   
REMARK 500    PHE B 650       -7.91     60.53                                   
REMARK 500    PRO B 654      -10.15    -45.49                                   
REMARK 500    THR B 665      107.64    -41.05                                   
REMARK 500    LYS B 683      -50.13    -26.72                                   
REMARK 500    ASP B 697       75.39     52.17                                   
REMARK 500    ASN B 730     -167.71   -100.41                                   
REMARK 500    MET B 738       48.69    -98.36                                   
REMARK 500    THR B 765      -59.44     84.87                                   
REMARK 500    GLU B 805      -74.73    -78.50                                   
REMARK 500    ALA B 820     -155.16     53.80                                   
REMARK 500    ALA B 856       65.65   -115.77                                   
REMARK 500    SER C1005     -175.78    -67.15                                   
REMARK 500    VAL C1031      112.04     23.74                                   
REMARK 500    LEU C1036       38.20    -90.14                                   
REMARK 500    THR C1037      -79.91    -82.86                                   
REMARK 500    PRO C1041      167.35    -47.76                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      94 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    ARG A  82         0.11    SIDE CHAIN                              
REMARK 500    ARG B 528         0.11    SIDE CHAIN                              
REMARK 500    ARG B 872         0.12    SIDE CHAIN                              
REMARK 500    ARG C1159         0.10    SIDE CHAIN                              
REMARK 500    ARG D1659         0.11    SIDE CHAIN                              
REMARK 500    ARG D1786         0.11    SIDE CHAIN                              
REMARK 500    ARG D1872         0.13    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLN D1782         12.75                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASP A 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASP B 914                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASP C 1414                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASP D 1914                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 913                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 1413                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 1913                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BJW   RELATED DB: PDB                                   
REMARK 900 1BJW CONTAINS THE WILD TYPE PROTEIN.                                 
REMARK 900 RELATED ID: 1BKG   RELATED DB: PDB                                   
REMARK 900 1BKG CONTAINS THE WILD TYPE PROTEIN COMPLEXED WITH MALEATE.          
REMARK 900 RELATED ID: 5BJ4   RELATED DB: PDB                                   
REMARK 900 5BJ4 CONTAINS THE SAME MUTANT PROTEIN.                               
REMARK 900 RELATED ID: 1GC3   RELATED DB: PDB                                   
REMARK 900 THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2       
REMARK 900 COMPLEXED WITH TRYPTOPHAN.                                           
DBREF  1GC4 A    1   385  UNP    Q56232   AAT_THETH        1    385             
DBREF  1GC4 B  501   885  UNP    Q56232   AAT_THETH        1    385             
DBREF  1GC4 C 1001  1385  UNP    Q56232   AAT_THETH        1    385             
DBREF  1GC4 D 1501  1885  UNP    Q56232   AAT_THETH        1    385             
SEQADV 1GC4 ASP A   14  UNP  Q56232    SER    14 ENGINEERED MUTATION            
SEQADV 1GC4 VAL A   16  UNP  Q56232    THR    16 ENGINEERED MUTATION            
SEQADV 1GC4 SER A  101  UNP  Q56232    LYS   101 ENGINEERED MUTATION            
SEQADV 1GC4 ARG A  261  UNP  Q56232    SER   261 ENGINEERED MUTATION            
SEQADV 1GC4 ASP B  514  UNP  Q56232    SER    14 ENGINEERED MUTATION            
SEQADV 1GC4 VAL B  516  UNP  Q56232    THR    16 ENGINEERED MUTATION            
SEQADV 1GC4 SER B  601  UNP  Q56232    LYS   101 ENGINEERED MUTATION            
SEQADV 1GC4 ARG B  761  UNP  Q56232    SER   261 ENGINEERED MUTATION            
SEQADV 1GC4 ASP C 1014  UNP  Q56232    SER    14 ENGINEERED MUTATION            
SEQADV 1GC4 VAL C 1016  UNP  Q56232    THR    16 ENGINEERED MUTATION            
SEQADV 1GC4 SER C 1101  UNP  Q56232    LYS   101 ENGINEERED MUTATION            
SEQADV 1GC4 ARG C 1261  UNP  Q56232    SER   261 ENGINEERED MUTATION            
SEQADV 1GC4 ASP D 1514  UNP  Q56232    SER    14 ENGINEERED MUTATION            
SEQADV 1GC4 VAL D 1516  UNP  Q56232    THR    16 ENGINEERED MUTATION            
SEQADV 1GC4 SER D 1601  UNP  Q56232    LYS   101 ENGINEERED MUTATION            
SEQADV 1GC4 ARG D 1761  UNP  Q56232    SER   261 ENGINEERED MUTATION            
SEQRES   1 A  385  MET ARG GLY LEU SER ARG ARG VAL GLN ALA MET LYS PRO          
SEQRES   2 A  385  ASP ALA VAL VAL ALA VAL ASN ALA LYS ALA LEU GLU LEU          
SEQRES   3 A  385  ARG ARG GLN GLY VAL ASP LEU VAL ALA LEU THR ALA GLY          
SEQRES   4 A  385  GLU PRO ASP PHE ASP THR PRO GLU HIS VAL LYS GLU ALA          
SEQRES   5 A  385  ALA ARG ARG ALA LEU ALA GLN GLY LYS THR LYS TYR ALA          
SEQRES   6 A  385  PRO PRO ALA GLY ILE PRO GLU LEU ARG GLU ALA LEU ALA          
SEQRES   7 A  385  GLU LYS PHE ARG ARG GLU ASN GLY LEU SER VAL THR PRO          
SEQRES   8 A  385  GLU GLU THR ILE VAL THR VAL GLY GLY SER GLN ALA LEU          
SEQRES   9 A  385  PHE ASN LEU PHE GLN ALA ILE LEU ASP PRO GLY ASP GLU          
SEQRES  10 A  385  VAL ILE VAL LEU SER PRO TYR TRP VAL SER TYR PRO GLU          
SEQRES  11 A  385  MET VAL ARG PHE ALA GLY GLY VAL VAL VAL GLU VAL GLU          
SEQRES  12 A  385  THR LEU PRO GLU GLU GLY PHE VAL PRO ASP PRO GLU ARG          
SEQRES  13 A  385  VAL ARG ARG ALA ILE THR PRO ARG THR LYS ALA LEU VAL          
SEQRES  14 A  385  VAL ASN SER PRO ASN ASN PRO THR GLY ALA VAL TYR PRO          
SEQRES  15 A  385  LYS GLU VAL LEU GLU ALA LEU ALA ARG LEU ALA VAL GLU          
SEQRES  16 A  385  HIS ASP PHE TYR LEU VAL SER ASP GLU ILE TYR GLU HIS          
SEQRES  17 A  385  LEU LEU TYR GLU GLY GLU HIS PHE SER PRO GLY ARG VAL          
SEQRES  18 A  385  ALA PRO GLU HIS THR LEU THR VAL ASN GLY ALA ALA LYS          
SEQRES  19 A  385  ALA PHE ALA MET THR GLY TRP ARG ILE GLY TYR ALA CYS          
SEQRES  20 A  385  GLY PRO LYS GLU VAL ILE LYS ALA MET ALA SER VAL SER          
SEQRES  21 A  385  ARG GLN SER THR THR SER PRO ASP THR ILE ALA GLN TRP          
SEQRES  22 A  385  ALA THR LEU GLU ALA LEU THR ASN GLN GLU ALA SER ARG          
SEQRES  23 A  385  ALA PHE VAL GLU MET ALA ARG GLU ALA TYR ARG ARG ARG          
SEQRES  24 A  385  ARG ASP LEU LEU LEU GLU GLY LEU THR ALA LEU GLY LEU          
SEQRES  25 A  385  LYS ALA VAL ARG PRO SER GLY ALA PHE TYR VAL LEU MET          
SEQRES  26 A  385  ASP THR SER PRO ILE ALA PRO ASP GLU VAL ARG ALA ALA          
SEQRES  27 A  385  GLU ARG LEU LEU GLU ALA GLY VAL ALA VAL VAL PRO GLY          
SEQRES  28 A  385  THR ASP PHE ALA ALA PHE GLY HIS VAL ARG LEU SER TYR          
SEQRES  29 A  385  ALA THR SER GLU GLU ASN LEU ARG LYS ALA LEU GLU ARG          
SEQRES  30 A  385  PHE ALA ARG VAL LEU GLY ARG ALA                              
SEQRES   1 B  385  MET ARG GLY LEU SER ARG ARG VAL GLN ALA MET LYS PRO          
SEQRES   2 B  385  ASP ALA VAL VAL ALA VAL ASN ALA LYS ALA LEU GLU LEU          
SEQRES   3 B  385  ARG ARG GLN GLY VAL ASP LEU VAL ALA LEU THR ALA GLY          
SEQRES   4 B  385  GLU PRO ASP PHE ASP THR PRO GLU HIS VAL LYS GLU ALA          
SEQRES   5 B  385  ALA ARG ARG ALA LEU ALA GLN GLY LYS THR LYS TYR ALA          
SEQRES   6 B  385  PRO PRO ALA GLY ILE PRO GLU LEU ARG GLU ALA LEU ALA          
SEQRES   7 B  385  GLU LYS PHE ARG ARG GLU ASN GLY LEU SER VAL THR PRO          
SEQRES   8 B  385  GLU GLU THR ILE VAL THR VAL GLY GLY SER GLN ALA LEU          
SEQRES   9 B  385  PHE ASN LEU PHE GLN ALA ILE LEU ASP PRO GLY ASP GLU          
SEQRES  10 B  385  VAL ILE VAL LEU SER PRO TYR TRP VAL SER TYR PRO GLU          
SEQRES  11 B  385  MET VAL ARG PHE ALA GLY GLY VAL VAL VAL GLU VAL GLU          
SEQRES  12 B  385  THR LEU PRO GLU GLU GLY PHE VAL PRO ASP PRO GLU ARG          
SEQRES  13 B  385  VAL ARG ARG ALA ILE THR PRO ARG THR LYS ALA LEU VAL          
SEQRES  14 B  385  VAL ASN SER PRO ASN ASN PRO THR GLY ALA VAL TYR PRO          
SEQRES  15 B  385  LYS GLU VAL LEU GLU ALA LEU ALA ARG LEU ALA VAL GLU          
SEQRES  16 B  385  HIS ASP PHE TYR LEU VAL SER ASP GLU ILE TYR GLU HIS          
SEQRES  17 B  385  LEU LEU TYR GLU GLY GLU HIS PHE SER PRO GLY ARG VAL          
SEQRES  18 B  385  ALA PRO GLU HIS THR LEU THR VAL ASN GLY ALA ALA LYS          
SEQRES  19 B  385  ALA PHE ALA MET THR GLY TRP ARG ILE GLY TYR ALA CYS          
SEQRES  20 B  385  GLY PRO LYS GLU VAL ILE LYS ALA MET ALA SER VAL SER          
SEQRES  21 B  385  ARG GLN SER THR THR SER PRO ASP THR ILE ALA GLN TRP          
SEQRES  22 B  385  ALA THR LEU GLU ALA LEU THR ASN GLN GLU ALA SER ARG          
SEQRES  23 B  385  ALA PHE VAL GLU MET ALA ARG GLU ALA TYR ARG ARG ARG          
SEQRES  24 B  385  ARG ASP LEU LEU LEU GLU GLY LEU THR ALA LEU GLY LEU          
SEQRES  25 B  385  LYS ALA VAL ARG PRO SER GLY ALA PHE TYR VAL LEU MET          
SEQRES  26 B  385  ASP THR SER PRO ILE ALA PRO ASP GLU VAL ARG ALA ALA          
SEQRES  27 B  385  GLU ARG LEU LEU GLU ALA GLY VAL ALA VAL VAL PRO GLY          
SEQRES  28 B  385  THR ASP PHE ALA ALA PHE GLY HIS VAL ARG LEU SER TYR          
SEQRES  29 B  385  ALA THR SER GLU GLU ASN LEU ARG LYS ALA LEU GLU ARG          
SEQRES  30 B  385  PHE ALA ARG VAL LEU GLY ARG ALA                              
SEQRES   1 C  385  MET ARG GLY LEU SER ARG ARG VAL GLN ALA MET LYS PRO          
SEQRES   2 C  385  ASP ALA VAL VAL ALA VAL ASN ALA LYS ALA LEU GLU LEU          
SEQRES   3 C  385  ARG ARG GLN GLY VAL ASP LEU VAL ALA LEU THR ALA GLY          
SEQRES   4 C  385  GLU PRO ASP PHE ASP THR PRO GLU HIS VAL LYS GLU ALA          
SEQRES   5 C  385  ALA ARG ARG ALA LEU ALA GLN GLY LYS THR LYS TYR ALA          
SEQRES   6 C  385  PRO PRO ALA GLY ILE PRO GLU LEU ARG GLU ALA LEU ALA          
SEQRES   7 C  385  GLU LYS PHE ARG ARG GLU ASN GLY LEU SER VAL THR PRO          
SEQRES   8 C  385  GLU GLU THR ILE VAL THR VAL GLY GLY SER GLN ALA LEU          
SEQRES   9 C  385  PHE ASN LEU PHE GLN ALA ILE LEU ASP PRO GLY ASP GLU          
SEQRES  10 C  385  VAL ILE VAL LEU SER PRO TYR TRP VAL SER TYR PRO GLU          
SEQRES  11 C  385  MET VAL ARG PHE ALA GLY GLY VAL VAL VAL GLU VAL GLU          
SEQRES  12 C  385  THR LEU PRO GLU GLU GLY PHE VAL PRO ASP PRO GLU ARG          
SEQRES  13 C  385  VAL ARG ARG ALA ILE THR PRO ARG THR LYS ALA LEU VAL          
SEQRES  14 C  385  VAL ASN SER PRO ASN ASN PRO THR GLY ALA VAL TYR PRO          
SEQRES  15 C  385  LYS GLU VAL LEU GLU ALA LEU ALA ARG LEU ALA VAL GLU          
SEQRES  16 C  385  HIS ASP PHE TYR LEU VAL SER ASP GLU ILE TYR GLU HIS          
SEQRES  17 C  385  LEU LEU TYR GLU GLY GLU HIS PHE SER PRO GLY ARG VAL          
SEQRES  18 C  385  ALA PRO GLU HIS THR LEU THR VAL ASN GLY ALA ALA LYS          
SEQRES  19 C  385  ALA PHE ALA MET THR GLY TRP ARG ILE GLY TYR ALA CYS          
SEQRES  20 C  385  GLY PRO LYS GLU VAL ILE LYS ALA MET ALA SER VAL SER          
SEQRES  21 C  385  ARG GLN SER THR THR SER PRO ASP THR ILE ALA GLN TRP          
SEQRES  22 C  385  ALA THR LEU GLU ALA LEU THR ASN GLN GLU ALA SER ARG          
SEQRES  23 C  385  ALA PHE VAL GLU MET ALA ARG GLU ALA TYR ARG ARG ARG          
SEQRES  24 C  385  ARG ASP LEU LEU LEU GLU GLY LEU THR ALA LEU GLY LEU          
SEQRES  25 C  385  LYS ALA VAL ARG PRO SER GLY ALA PHE TYR VAL LEU MET          
SEQRES  26 C  385  ASP THR SER PRO ILE ALA PRO ASP GLU VAL ARG ALA ALA          
SEQRES  27 C  385  GLU ARG LEU LEU GLU ALA GLY VAL ALA VAL VAL PRO GLY          
SEQRES  28 C  385  THR ASP PHE ALA ALA PHE GLY HIS VAL ARG LEU SER TYR          
SEQRES  29 C  385  ALA THR SER GLU GLU ASN LEU ARG LYS ALA LEU GLU ARG          
SEQRES  30 C  385  PHE ALA ARG VAL LEU GLY ARG ALA                              
SEQRES   1 D  385  MET ARG GLY LEU SER ARG ARG VAL GLN ALA MET LYS PRO          
SEQRES   2 D  385  ASP ALA VAL VAL ALA VAL ASN ALA LYS ALA LEU GLU LEU          
SEQRES   3 D  385  ARG ARG GLN GLY VAL ASP LEU VAL ALA LEU THR ALA GLY          
SEQRES   4 D  385  GLU PRO ASP PHE ASP THR PRO GLU HIS VAL LYS GLU ALA          
SEQRES   5 D  385  ALA ARG ARG ALA LEU ALA GLN GLY LYS THR LYS TYR ALA          
SEQRES   6 D  385  PRO PRO ALA GLY ILE PRO GLU LEU ARG GLU ALA LEU ALA          
SEQRES   7 D  385  GLU LYS PHE ARG ARG GLU ASN GLY LEU SER VAL THR PRO          
SEQRES   8 D  385  GLU GLU THR ILE VAL THR VAL GLY GLY SER GLN ALA LEU          
SEQRES   9 D  385  PHE ASN LEU PHE GLN ALA ILE LEU ASP PRO GLY ASP GLU          
SEQRES  10 D  385  VAL ILE VAL LEU SER PRO TYR TRP VAL SER TYR PRO GLU          
SEQRES  11 D  385  MET VAL ARG PHE ALA GLY GLY VAL VAL VAL GLU VAL GLU          
SEQRES  12 D  385  THR LEU PRO GLU GLU GLY PHE VAL PRO ASP PRO GLU ARG          
SEQRES  13 D  385  VAL ARG ARG ALA ILE THR PRO ARG THR LYS ALA LEU VAL          
SEQRES  14 D  385  VAL ASN SER PRO ASN ASN PRO THR GLY ALA VAL TYR PRO          
SEQRES  15 D  385  LYS GLU VAL LEU GLU ALA LEU ALA ARG LEU ALA VAL GLU          
SEQRES  16 D  385  HIS ASP PHE TYR LEU VAL SER ASP GLU ILE TYR GLU HIS          
SEQRES  17 D  385  LEU LEU TYR GLU GLY GLU HIS PHE SER PRO GLY ARG VAL          
SEQRES  18 D  385  ALA PRO GLU HIS THR LEU THR VAL ASN GLY ALA ALA LYS          
SEQRES  19 D  385  ALA PHE ALA MET THR GLY TRP ARG ILE GLY TYR ALA CYS          
SEQRES  20 D  385  GLY PRO LYS GLU VAL ILE LYS ALA MET ALA SER VAL SER          
SEQRES  21 D  385  ARG GLN SER THR THR SER PRO ASP THR ILE ALA GLN TRP          
SEQRES  22 D  385  ALA THR LEU GLU ALA LEU THR ASN GLN GLU ALA SER ARG          
SEQRES  23 D  385  ALA PHE VAL GLU MET ALA ARG GLU ALA TYR ARG ARG ARG          
SEQRES  24 D  385  ARG ASP LEU LEU LEU GLU GLY LEU THR ALA LEU GLY LEU          
SEQRES  25 D  385  LYS ALA VAL ARG PRO SER GLY ALA PHE TYR VAL LEU MET          
SEQRES  26 D  385  ASP THR SER PRO ILE ALA PRO ASP GLU VAL ARG ALA ALA          
SEQRES  27 D  385  GLU ARG LEU LEU GLU ALA GLY VAL ALA VAL VAL PRO GLY          
SEQRES  28 D  385  THR ASP PHE ALA ALA PHE GLY HIS VAL ARG LEU SER TYR          
SEQRES  29 D  385  ALA THR SER GLU GLU ASN LEU ARG LYS ALA LEU GLU ARG          
SEQRES  30 D  385  PHE ALA ARG VAL LEU GLY ARG ALA                              
HET    ASP  A 414       9                                                       
HET    PLP  A 413      15                                                       
HET    ASP  B 914       9                                                       
HET    PLP  B 913      15                                                       
HET    ASP  C1414       9                                                       
HET    PLP  C1413      15                                                       
HET    ASP  D1914       9                                                       
HET    PLP  D1913      15                                                       
HETNAM     ASP ASPARTIC ACID                                                    
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   5  ASP    4(C4 H7 N O4)                                                
FORMUL   6  PLP    4(C8 H10 N O6 P)                                             
HELIX    1   1 ASP A   14  GLN A   29  1                                  16    
HELIX    2   2 PRO A   46  GLN A   59  1                                  14    
HELIX    3   3 ILE A   70  GLU A   84  1                                  15    
HELIX    4   4 THR A   90  GLU A   92  5                                   3    
HELIX    5   5 VAL A   98  LEU A  112  1                                  15    
HELIX    6   6 VAL A  126  ALA A  135  1                                  10    
HELIX    7   7 LEU A  145  GLY A  149  5                                   5    
HELIX    8   8 ASP A  153  ILE A  161  1                                   9    
HELIX    9   9 PRO A  182  HIS A  196  1                                  15    
HELIX   10  10 SER A  217  VAL A  221  5                                   5    
HELIX   11  11 PRO A  249  THR A  264  1                                  16    
HELIX   12  12 ASP A  268  ASN A  281  1                                  14    
HELIX   13  13 ASN A  281  LEU A  310  1                                  30    
HELIX   14  14 ASP A  333  ALA A  344  1                                  12    
HELIX   15  15 SER A  367  LEU A  382  1                                  16    
HELIX   16  16 ASP B  514  ARG B  528  1                                  15    
HELIX   17  17 PRO B  546  GLN B  559  1                                  14    
HELIX   18  18 ILE B  570  GLU B  584  1                                  15    
HELIX   19  19 THR B  590  GLU B  592  5                                   3    
HELIX   20  20 VAL B  598  LEU B  612  1                                  15    
HELIX   21  21 VAL B  626  ALA B  635  1                                  10    
HELIX   22  22 LEU B  645  GLY B  649  5                                   5    
HELIX   23  23 ASP B  653  ILE B  661  1                                   9    
HELIX   24  24 PRO B  682  HIS B  696  1                                  15    
HELIX   25  25 SER B  717  VAL B  721  5                                   5    
HELIX   26  26 PRO B  749  THR B  764  1                                  16    
HELIX   27  27 ASP B  768  ASN B  781  1                                  14    
HELIX   28  28 ASN B  781  LEU B  810  1                                  30    
HELIX   29  29 ASP B  833  ALA B  844  1                                  12    
HELIX   30  30 SER B  867  LEU B  882  1                                  16    
HELIX   31  31 ASP C 1014  GLN C 1029  1                                  16    
HELIX   32  32 PRO C 1046  GLN C 1059  1                                  14    
HELIX   33  33 ILE C 1070  GLU C 1084  1                                  15    
HELIX   34  34 THR C 1090  GLU C 1092  5                                   3    
HELIX   35  35 VAL C 1098  LEU C 1112  1                                  15    
HELIX   36  36 VAL C 1126  ALA C 1135  1                                  10    
HELIX   37  37 LEU C 1145  GLY C 1149  5                                   5    
HELIX   38  38 ASP C 1153  ILE C 1161  1                                   9    
HELIX   39  39 PRO C 1182  HIS C 1196  1                                  15    
HELIX   40  40 SER C 1217  VAL C 1221  5                                   5    
HELIX   41  41 PRO C 1249  THR C 1264  1                                  16    
HELIX   42  42 ASP C 1268  ASN C 1281  1                                  14    
HELIX   43  43 ASN C 1281  LEU C 1310  1                                  30    
HELIX   44  44 ASP C 1333  ALA C 1344  1                                  12    
HELIX   45  45 SER C 1367  LEU C 1382  1                                  16    
HELIX   46  46 ASP D 1514  GLN D 1529  1                                  16    
HELIX   47  47 PRO D 1546  GLN D 1559  1                                  14    
HELIX   48  48 ILE D 1570  GLU D 1584  1                                  15    
HELIX   49  49 THR D 1590  GLU D 1592  5                                   3    
HELIX   50  50 VAL D 1598  LEU D 1612  1                                  15    
HELIX   51  51 VAL D 1626  ALA D 1635  1                                  10    
HELIX   52  52 LEU D 1645  GLY D 1649  5                                   5    
HELIX   53  53 ASP D 1653  ILE D 1661  1                                   9    
HELIX   54  54 PRO D 1682  HIS D 1696  1                                  15    
HELIX   55  55 SER D 1717  VAL D 1721  5                                   5    
HELIX   56  56 PRO D 1749  THR D 1764  1                                  16    
HELIX   57  57 ASP D 1768  ASN D 1781  1                                  14    
HELIX   58  58 ASN D 1781  LEU D 1810  1                                  30    
HELIX   59  59 GLU D 1834  ALA D 1844  1                                  11    
HELIX   60  60 SER D 1867  LEU D 1882  1                                  16    
SHEET    1   A 2 VAL A  34  ALA A  35  0                                        
SHEET    2   A 2 VAL A 346  ALA A 347  1  N  ALA A 347   O  VAL A  34           
SHEET    1   B 7 THR A  94  THR A  97  0                                        
SHEET    2   B 7 GLY A 244  CYS A 247 -1  N  GLY A 244   O  THR A  97           
SHEET    3   B 7 THR A 226  GLY A 231 -1  O  THR A 228   N  CYS A 247           
SHEET    4   B 7 TYR A 199  SER A 202  1  O  LEU A 200   N  LEU A 227           
SHEET    5   B 7 THR A 165  VAL A 170  1  O  LYS A 166   N  TYR A 199           
SHEET    6   B 7 GLU A 117  SER A 122  1  O  GLU A 117   N  LYS A 166           
SHEET    7   B 7 VAL A 138  GLU A 143  1  O  VAL A 138   N  VAL A 118           
SHEET    1   C 3 TYR A 322  LEU A 324  0                                        
SHEET    2   C 3 VAL A 360  SER A 363 -1  O  LEU A 362   N  VAL A 323           
SHEET    3   C 3 VAL A 349  PRO A 350 -1  O  VAL A 349   N  ARG A 361           
SHEET    1   D 2 VAL B 534  ALA B 535  0                                        
SHEET    2   D 2 VAL B 846  ALA B 847  1  N  ALA B 847   O  VAL B 534           
SHEET    1   E 7 THR B 594  THR B 597  0                                        
SHEET    2   E 7 GLY B 744  CYS B 747 -1  N  GLY B 744   O  THR B 597           
SHEET    3   E 7 THR B 726  GLY B 731 -1  O  THR B 728   N  CYS B 747           
SHEET    4   E 7 TYR B 699  SER B 702  1  O  LEU B 700   N  LEU B 727           
SHEET    5   E 7 THR B 665  VAL B 670  1  O  LYS B 666   N  TYR B 699           
SHEET    6   E 7 GLU B 617  SER B 622  1  O  GLU B 617   N  LYS B 666           
SHEET    7   E 7 VAL B 638  GLU B 643  1  O  VAL B 638   N  VAL B 618           
SHEET    1   F 3 TYR B 822  LEU B 824  0                                        
SHEET    2   F 3 VAL B 860  SER B 863 -1  N  LEU B 862   O  VAL B 823           
SHEET    3   F 3 VAL B 849  PRO B 850 -1  O  VAL B 849   N  ARG B 861           
SHEET    1   G 2 VAL C1034  ALA C1035  0                                        
SHEET    2   G 2 VAL C1346  ALA C1347  1  N  ALA C1347   O  VAL C1034           
SHEET    1   H 7 THR C1094  THR C1097  0                                        
SHEET    2   H 7 GLY C1244  CYS C1247 -1  N  GLY C1244   O  THR C1097           
SHEET    3   H 7 THR C1226  GLY C1231 -1  O  THR C1228   N  CYS C1247           
SHEET    4   H 7 TYR C1199  SER C1202  1  O  LEU C1200   N  LEU C1227           
SHEET    5   H 7 THR C1165  VAL C1170  1  O  LYS C1166   N  TYR C1199           
SHEET    6   H 7 GLU C1117  SER C1122  1  O  GLU C1117   N  LYS C1166           
SHEET    7   H 7 VAL C1138  GLU C1143  1  O  VAL C1138   N  VAL C1118           
SHEET    1   I 3 TYR C1322  LEU C1324  0                                        
SHEET    2   I 3 VAL C1360  SER C1363 -1  N  LEU C1362   O  VAL C1323           
SHEET    3   I 3 VAL C1349  PRO C1350 -1  O  VAL C1349   N  ARG C1361           
SHEET    1   J 2 VAL D1534  ALA D1535  0                                        
SHEET    2   J 2 VAL D1846  ALA D1847  1  N  ALA D1847   O  VAL D1534           
SHEET    1   K 7 THR D1594  THR D1597  0                                        
SHEET    2   K 7 GLY D1744  CYS D1747 -1  N  GLY D1744   O  THR D1597           
SHEET    3   K 7 THR D1726  GLY D1731 -1  O  THR D1728   N  CYS D1747           
SHEET    4   K 7 TYR D1699  SER D1702  1  O  LEU D1700   N  LEU D1727           
SHEET    5   K 7 THR D1665  VAL D1670  1  O  LYS D1666   N  TYR D1699           
SHEET    6   K 7 GLU D1617  SER D1622  1  O  GLU D1617   N  LYS D1666           
SHEET    7   K 7 VAL D1638  GLU D1643  1  O  VAL D1638   N  VAL D1618           
SHEET    1   L 3 TYR D1822  ASP D1826  0                                        
SHEET    2   L 3 HIS D1859  SER D1863 -1  O  VAL D1860   N  MET D1825           
SHEET    3   L 3 VAL D1849  PRO D1850 -1  O  VAL D1849   N  ARG D1861           
LINK         C4A PLP A 413                 N   ASP A 414     1555   1555  1.59  
LINK         C4A PLP B 913                 N   ASP B 914     1555   1555  1.52  
LINK         C4A PLP C1413                 N   ASP C1414     1555   1555  1.45  
LINK         C4A PLP D1913                 N   ASP D1914     1555   1555  1.62  
CISPEP   1 SER A  122    PRO A  123          0        -0.02                     
CISPEP   2 SER A  172    PRO A  173          0        -0.18                     
CISPEP   3 ASN A  175    PRO A  176          0         0.20                     
CISPEP   4 SER B  622    PRO B  623          0         0.04                     
CISPEP   5 SER B  672    PRO B  673          0        -0.40                     
CISPEP   6 ASN B  675    PRO B  676          0        -0.11                     
CISPEP   7 SER C 1122    PRO C 1123          0        -0.07                     
CISPEP   8 SER C 1172    PRO C 1173          0        -0.70                     
CISPEP   9 ASN C 1175    PRO C 1176          0         0.31                     
CISPEP  10 SER D 1622    PRO D 1623          0         0.23                     
CISPEP  11 SER D 1672    PRO D 1673          0        -0.60                     
CISPEP  12 ASN D 1675    PRO D 1676          0         0.20                     
SITE     1 AC1  9 GLY A  39  TRP A 125  ASN A 175  LYS A 234                    
SITE     2 AC1  9 TYR A 322  ARG A 361  PLP A 413  TYR B 564                    
SITE     3 AC1  9 ARG B 761                                                     
SITE     1 AC2 10 TYR A  64  ARG A 261  VAL B 516  TRP B 625                    
SITE     2 AC2 10 ASN B 675  TYR B 706  LYS B 734  TYR B 822                    
SITE     3 AC2 10 ARG B 861  PLP B 913                                          
SITE     1 AC3  8 TRP C1125  ASN C1175  LYS C1234  TYR C1322                    
SITE     2 AC3  8 ARG C1361  PLP C1413  TYR D1564  ARG D1761                    
SITE     1 AC4  8 TYR C1064  ARG C1261  TRP D1625  ASN D1675                    
SITE     2 AC4  8 LYS D1734  TYR D1822  ARG D1861  PLP D1913                    
SITE     1 AC5 14 GLY A  99  GLY A 100  SER A 101  TRP A 125                    
SITE     2 AC5 14 ASN A 171  ASN A 175  ASP A 203  ILE A 205                    
SITE     3 AC5 14 TYR A 206  ALA A 233  ARG A 242  ASP A 414                    
SITE     4 AC5 14 TYR B 564  THR B 765                                          
SITE     1 AC6 13 TYR A  64  GLY B 599  GLY B 600  SER B 601                    
SITE     2 AC6 13 TRP B 625  ASN B 671  ASN B 675  ASP B 703                    
SITE     3 AC6 13 TYR B 706  ALA B 733  LYS B 734  ARG B 742                    
SITE     4 AC6 13 ASP B 914                                                     
SITE     1 AC7 15 GLY C1099  GLY C1100  SER C1101  TRP C1125                    
SITE     2 AC7 15 ASN C1171  ASN C1175  ASP C1203  ILE C1205                    
SITE     3 AC7 15 TYR C1206  ALA C1233  LYS C1234  ARG C1242                    
SITE     4 AC7 15 ASP C1414  TYR D1564  THR D1765                               
SITE     1 AC8 13 TYR C1064  GLY D1599  GLY D1600  SER D1601                    
SITE     2 AC8 13 TRP D1625  ASN D1671  ASN D1675  ASP D1703                    
SITE     3 AC8 13 ILE D1705  TYR D1706  ALA D1733  ARG D1742                    
SITE     4 AC8 13 ASP D1914                                                     
CRYST1   82.670  102.340  100.410  90.00 112.14  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012096  0.000000  0.004922        0.00000                         
SCALE2      0.000000  0.009771  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010752        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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