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Database: PDB
Entry: 3IHJ
LinkDB: 3IHJ
Original site: 3IHJ 
HEADER    TRANSFERASE                             30-JUL-09   3IHJ              
TITLE     HUMAN ALANINE AMINOTRANSFERASE 2 IN COMPLEX WITH PLP                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE AMINOTRANSFERASE 2;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 49-523;                                       
COMPND   5 SYNONYM: ALT2, GLUTAMIC-PYRUVIC TRANSAMINASE 2, GLUTAMATE PYRUVATE   
COMPND   6 TRANSAMINASE 2, GPT 2, GLUTAMIC-ALANINE TRANSAMINASE 2;              
COMPND   7 EC: 2.6.1.2;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GPT2, AAT2, ALT2;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) R3 PRARE;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PNIC-BSA4                             
KEYWDS    HELIX, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,      
KEYWDS   2 AMINOTRANSFERASE, PYRIDOXAL PHOSPHATE, TRANSFERASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.WISNIEWSKA,M.I.SIPONEN,C.H.ARROWSMITH,H.BERGLUND,C.BOUNTRA,         
AUTHOR   2 R.COLLINS,A.M.EDWARDS,S.FLODIN,A.FLORES,S.GRASLUND,M.HAMMARSTROM,    
AUTHOR   3 A.JOHANSSON,I.JOHANSSON,T.KARLBERG,T.KOTENYOVA,A.KOTZSCH,M.MOCHE,    
AUTHOR   4 T.K.NIELSEN,P.NORDLUND,T.NYMAN,C.PERSSON,A.K.ROOS,P.SCHUTZ,          
AUTHOR   5 L.SVENSSON,A.G.THORSELL,L.TRESAUGUES,S.VAN DEN BERG,J.WEIGELT,       
AUTHOR   6 M.WELIN,H.SCHULER,STRUCTURAL GENOMICS CONSORTIUM (SGC)               
REVDAT   2   13-JUL-11 3IHJ    1       VERSN                                    
REVDAT   1   18-AUG-09 3IHJ    0                                                
JRNL        AUTH   M.WISNIEWSKA,M.I.SIPONEN,C.H.ARROWSMITH,H.BERGLUND,          
JRNL        AUTH 2 C.BOUNTRA,R.COLLINS,A.M.EDWARDS,S.FLODIN,A.FLORES,           
JRNL        AUTH 3 S.GRASLUND,M.HAMMARSTROM,A.JOHANSSON,I.JOHANSSON,T.KARLBERG, 
JRNL        AUTH 4 T.KOTENYOVA,A.KOTZSCH,M.MOCHE,T.K.NIELSEN,P.NORDLUND,        
JRNL        AUTH 5 T.NYMAN,C.PERSSON,A.K.ROOS,P.SCHUTZ,L.SVENSSON,A.G.THORSELL, 
JRNL        AUTH 6 L.TRESAUGUES,S.VAN DEN BERG,J.WEIGELT,M.WELIN,H.SCHULER      
JRNL        TITL   HUMAN GLUTAMATE PYRUVATE TRANSAMINASE 2                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 29051                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1529                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2070                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 109                          
REMARK   3   BIN FREE R VALUE                    : 0.2680                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3570                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 93                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : 0.01000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.226         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.198         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.135         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.420         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3682 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2487 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5001 ; 1.761 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6088 ; 0.994 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   462 ; 6.686 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   161 ;32.436 ;24.472       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   613 ;14.216 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;21.084 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   554 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4087 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   710 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   756 ; 0.229 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2438 ; 0.193 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1801 ; 0.184 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1896 ; 0.092 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   115 ; 0.181 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    20 ; 0.229 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    55 ; 0.282 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.129 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2534 ; 1.370 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   924 ; 0.254 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3728 ; 1.925 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1487 ; 2.988 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1271 ; 4.266 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3IHJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB054418.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 4.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30795                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
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) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1XI9                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CITRIC ACID, 40% PEG300, 0.1M       
REMARK 280  DISODIUM HYDROGEN PHOSPHATE , PH 4.2, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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       87.62333            
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      175.24667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      131.43500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      219.05833            
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       43.81167            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       87.62333            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      175.24667            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      219.05833            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      131.43500            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       43.81167            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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   BIOMT1   2  0.500000  0.866025  0.000000      -46.36500            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000       80.30654            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       43.81167            
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    26                                                      
REMARK 465     HIS A    27                                                      
REMARK 465     HIS A    28                                                      
REMARK 465     HIS A    29                                                      
REMARK 465     HIS A    30                                                      
REMARK 465     HIS A    31                                                      
REMARK 465     HIS A    32                                                      
REMARK 465     SER A    33                                                      
REMARK 465     SER A    34                                                      
REMARK 465     GLY A    35                                                      
REMARK 465     VAL A    36                                                      
REMARK 465     ASP A    37                                                      
REMARK 465     LEU A    38                                                      
REMARK 465     GLY A    39                                                      
REMARK 465     THR A    40                                                      
REMARK 465     GLU A    41                                                      
REMARK 465     ILE A    95                                                      
REMARK 465     GLY A    96                                                      
REMARK 465     ASP A    97                                                      
REMARK 465     ALA A    98                                                      
REMARK 465     GLN A    99                                                      
REMARK 465     ALA A   100                                                      
REMARK 465     MET A   101                                                      
REMARK 465     GLY A   102                                                      
REMARK 465     GLN A   103                                                      
REMARK 465     GLN A   104                                                      
REMARK 465     GLY A   143                                                      
REMARK 465     GLY A   144                                                      
REMARK 465     ASN A   145                                                      
REMARK 465     SER A   146                                                      
REMARK 465     LEU A   147                                                      
REMARK 465     GLY A   148                                                      
REMARK 465     SER A   149                                                      
REMARK 465     TYR A   150                                                      
REMARK 465     SER A   151                                                      
REMARK 465     ALA A   152                                                      
REMARK 465     ALA A   523                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A  42    CG   OD1                                            
REMARK 470     TYR A  44    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A  84    CG   CD   CE   NZ                                   
REMARK 470     LYS A 133    CE   NZ                                             
REMARK 470     ARG A 137    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 204    CG   CD   CE   NZ                                   
REMARK 470     GLU A 254    CD   OE1  OE2                                       
REMARK 470     ASP A 257    CG   OD1  OD2                                       
REMARK 470     LYS A 280    CG   CD   CE   NZ                                   
REMARK 470     LYS A 293    CE   NZ                                             
REMARK 470     GLU A 346    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 406    CG   CD   CE   NZ                                   
REMARK 470     LYS A 450    CG   CD   CE   NZ                                   
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   NZ   LYS A   341     C4A  PLP A     1              1.60            
REMARK 500   OD1  ASN A   246     O    HOH A   586              2.13            
REMARK 500   OE1  GLU A   237     O    HOH A     8              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 A 247   CB    GLU A 247   CG      0.124                       
REMARK 500    CYS A 281   CB    CYS A 281   SG     -0.101                       
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    ARG A  65       79.35   -111.76                                   
REMARK 500    ARG A  92      -63.89    -97.94                                   
REMARK 500    ALA A  93       84.81     78.64                                   
REMARK 500    CYS A 376      149.45    -38.81                                   
REMARK 500    ALA A 438     -161.38     64.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A    1                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 524                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 2                   
DBREF  3IHJ A   49   523  UNP    Q8TD30   ALAT2_HUMAN     49    523             
SEQADV 3IHJ MET A   26  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ HIS A   27  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ HIS A   28  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ HIS A   29  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ HIS A   30  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ HIS A   31  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ HIS A   32  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ SER A   33  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ SER A   34  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ GLY A   35  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ VAL A   36  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ ASP A   37  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ LEU A   38  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ GLY A   39  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ THR A   40  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ GLU A   41  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ ASN A   42  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ LEU A   43  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ TYR A   44  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ PHE A   45  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ GLN A   46  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ SER A   47  UNP  Q8TD30              EXPRESSION TAG                 
SEQADV 3IHJ MET A   48  UNP  Q8TD30              EXPRESSION TAG                 
SEQRES   1 A  498  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  498  GLY THR GLU ASN LEU TYR PHE GLN SER MET THR LEU GLU          
SEQRES   3 A  498  SER MET ASN PRO GLN VAL LYS ALA VAL GLU TYR ALA VAL          
SEQRES   4 A  498  ARG GLY PRO ILE VAL LEU LYS ALA GLY GLU ILE GLU LEU          
SEQRES   5 A  498  GLU LEU GLN ARG GLY ILE LYS LYS PRO PHE THR GLU VAL          
SEQRES   6 A  498  ILE ARG ALA ASN ILE GLY ASP ALA GLN ALA MET GLY GLN          
SEQRES   7 A  498  GLN PRO ILE THR PHE LEU ARG GLN VAL MET ALA LEU CYS          
SEQRES   8 A  498  THR TYR PRO ASN LEU LEU ASP SER PRO SER PHE PRO GLU          
SEQRES   9 A  498  ASP ALA LYS LYS ARG ALA ARG ARG ILE LEU GLN ALA CYS          
SEQRES  10 A  498  GLY GLY ASN SER LEU GLY SER TYR SER ALA SER GLN GLY          
SEQRES  11 A  498  VAL ASN CYS ILE ARG GLU ASP VAL ALA ALA TYR ILE THR          
SEQRES  12 A  498  ARG ARG ASP GLY GLY VAL PRO ALA ASP PRO ASP ASN ILE          
SEQRES  13 A  498  TYR LEU THR THR GLY ALA SER ASP GLY ILE SER THR ILE          
SEQRES  14 A  498  LEU LYS ILE LEU VAL SER GLY GLY GLY LYS SER ARG THR          
SEQRES  15 A  498  GLY VAL MET ILE PRO ILE PRO GLN TYR PRO LEU TYR SER          
SEQRES  16 A  498  ALA VAL ILE SER GLU LEU ASP ALA ILE GLN VAL ASN TYR          
SEQRES  17 A  498  TYR LEU ASP GLU GLU ASN CYS TRP ALA LEU ASN VAL ASN          
SEQRES  18 A  498  GLU LEU ARG ARG ALA VAL GLN GLU ALA LYS ASP HIS CYS          
SEQRES  19 A  498  ASP PRO LYS VAL LEU CYS ILE ILE ASN PRO GLY ASN PRO          
SEQRES  20 A  498  THR GLY GLN VAL GLN SER ARG LYS CYS ILE GLU ASP VAL          
SEQRES  21 A  498  ILE HIS PHE ALA TRP GLU GLU LYS LEU PHE LEU LEU ALA          
SEQRES  22 A  498  ASP GLU VAL TYR GLN ASP ASN VAL TYR SER PRO ASP CYS          
SEQRES  23 A  498  ARG PHE HIS SER PHE LYS LYS VAL LEU TYR GLU MET GLY          
SEQRES  24 A  498  PRO GLU TYR SER SER ASN VAL GLU LEU ALA SER PHE HIS          
SEQRES  25 A  498  SER THR SER LYS GLY TYR MET GLY GLU CYS GLY TYR ARG          
SEQRES  26 A  498  GLY GLY TYR MET GLU VAL ILE ASN LEU HIS PRO GLU ILE          
SEQRES  27 A  498  LYS GLY GLN LEU VAL LYS LEU LEU SER VAL ARG LEU CYS          
SEQRES  28 A  498  PRO PRO VAL SER GLY GLN ALA ALA MET ASP ILE VAL VAL          
SEQRES  29 A  498  ASN PRO PRO VAL ALA GLY GLU GLU SER PHE GLU GLN PHE          
SEQRES  30 A  498  SER ARG GLU LYS GLU SER VAL LEU GLY ASN LEU ALA LYS          
SEQRES  31 A  498  LYS ALA LYS LEU THR GLU ASP LEU PHE ASN GLN VAL PRO          
SEQRES  32 A  498  GLY ILE HIS CYS ASN PRO LEU GLN GLY ALA MET TYR ALA          
SEQRES  33 A  498  PHE PRO ARG ILE PHE ILE PRO ALA LYS ALA VAL GLU ALA          
SEQRES  34 A  498  ALA GLN ALA HIS GLN MET ALA PRO ASP MET PHE TYR CYS          
SEQRES  35 A  498  MET LYS LEU LEU GLU GLU THR GLY ILE CYS VAL VAL PRO          
SEQRES  36 A  498  GLY SER GLY PHE GLY GLN ARG GLU GLY THR TYR HIS PHE          
SEQRES  37 A  498  ARG MET THR ILE LEU PRO PRO VAL GLU LYS LEU LYS THR          
SEQRES  38 A  498  VAL LEU GLN LYS VAL LYS ASP PHE HIS ILE ASN PHE LEU          
SEQRES  39 A  498  GLU LYS TYR ALA                                              
HET    PLP  A   1      15                                                       
HET    PO4  A 524       5                                                       
HET    PO4  A   2       5                                                       
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   2  PLP    C8 H10 N O6 P                                                
FORMUL   3  PO4    2(O4 P 3-)                                                   
FORMUL   5  HOH   *93(H2 O)                                                     
HELIX    1   1 GLY A   66  ARG A   81  1                                  16    
HELIX    2   2 ILE A  106  TYR A  118  1                                  13    
HELIX    3   3 PRO A  119  SER A  124  5                                   6    
HELIX    4   4 PRO A  128  CYS A  142  1                                  15    
HELIX    5   5 VAL A  156  ASP A  171  1                                  16    
HELIX    6   6 ASP A  177  ASP A  179  5                                   3    
HELIX    7   7 GLY A  186  VAL A  199  1                                  14    
HELIX    8   8 GLY A  202  SER A  205  5                                   4    
HELIX    9   9 PRO A  217  LEU A  226  1                                  10    
HELIX   10  10 ASP A  236  CYS A  240  5                                   5    
HELIX   11  11 ASN A  244  LYS A  256  1                                  13    
HELIX   12  12 SER A  278  LYS A  293  1                                  16    
HELIX   13  13 SER A  315  MET A  323  1                                   9    
HELIX   14  14 GLY A  324  SER A  329  1                                   6    
HELIX   15  15 HIS A  360  ARG A  374  1                                  15    
HELIX   16  16 PRO A  378  VAL A  389  1                                  12    
HELIX   17  17 SER A  398  GLN A  426  1                                  29    
HELIX   18  18 PRO A  448  HIS A  458  1                                  11    
HELIX   19  19 ALA A  461  GLY A  475  1                                  15    
HELIX   20  20 SER A  482  PHE A  484  5                                   3    
HELIX   21  21 PRO A  500  TYR A  522  1                                  23    
SHEET    1   A 2 LEU A  43  SER A  52  0                                        
SHEET    2   A 2 VAL A  57  VAL A  64 -1  O  ALA A  59   N  THR A  49           
SHEET    1   B 7 ILE A 181  THR A 184  0                                        
SHEET    2   B 7 GLY A 352  ILE A 357 -1  O  MET A 354   N  TYR A 182           
SHEET    3   B 7 LEU A 333  SER A 338 -1  N  LEU A 333   O  ILE A 357           
SHEET    4   B 7 PHE A 295  ASP A 299  1  N  ALA A 298   O  ALA A 334           
SHEET    5   B 7 ASP A 260  ILE A 267  1  N  ILE A 266   O  ASP A 299           
SHEET    6   B 7 THR A 207  ILE A 213  1  N  MET A 210   O  VAL A 263           
SHEET    7   B 7 ILE A 229  TYR A 234  1  O  ILE A 229   N  VAL A 209           
SHEET    1   C 2 ILE A 430  HIS A 431  0                                        
SHEET    2   C 2 ARG A 444  ILE A 445 -1  O  ARG A 444   N  HIS A 431           
SHEET    1   D 3 TYR A 440  ALA A 441  0                                        
SHEET    2   D 3 PHE A 493  THR A 496 -1  O  MET A 495   N  ALA A 441           
SHEET    3   D 3 VAL A 479  PRO A 480 -1  N  VAL A 479   O  ARG A 494           
CISPEP   1 ASN A   54    PRO A   55          0        -0.72                     
CISPEP   2 ILE A  213    PRO A  214          0        -1.26                     
CISPEP   3 ASN A  268    PRO A  269          0        -4.93                     
CISPEP   4 ASN A  271    PRO A  272          0        12.06                     
SITE     1 AC1 13 HOH A   3  GLY A 186  ALA A 187  SER A 188                    
SITE     2 AC1 13 TYR A 216  ILE A 267  ASN A 271  ASP A 299                    
SITE     3 AC1 13 VAL A 301  TYR A 302  SER A 338  LYS A 341                    
SITE     4 AC1 13 ARG A 350                                                     
SITE     1 AC2  6 SER A  52  MET A  53  ASN A  54  ASN A  94                    
SITE     2 AC2  6 TYR A 440  ARG A 494                                          
SITE     1 AC3  5 ARG A 312  HIS A 314  LYS A 318  LYS A 469                    
SITE     2 AC3  5 LYS A 521                                                     
CRYST1   92.730   92.730  262.870  90.00  90.00 120.00 P 61 2 2     12          
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      0.010784  0.006226  0.000000        0.00000                         
SCALE2      0.000000  0.012452  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003804        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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