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Database: PDB
Entry: 2XH1
LinkDB: 2XH1
Original site: 2XH1 
HEADER    TRANSFERASE                             08-JUN-10   2XH1              
TITLE     CRYSTAL STRUCTURE OF HUMAN KAT II-INHIBITOR COMPLEX                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KYNURENINE/ALPHA-AMINOADIPATE AMINOTRANSFERASE,            
COMPND   3  MITOCHONDRIAL;                                                      
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: KYNURENINE AMINOTRANSFERASE II, KYNURENINE--OXOGLUTARATE    
COMPND   6  AMINOTRANSFERASE II, KYNURENINE--OXOGLUTARATE TRANSAMINASE II,      
COMPND   7  2-AMINOADIPATE TRANSAMINASE, 2-AMINOADIPATE AMINOTRANSFERASE,       
COMPND   8  ALPHA-AMINOADIPATE AMINOTRANSFERASE, AADAT;                         
COMPND   9 EC: 2.6.1.7, 2.6.1.39;                                               
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET16B                                    
KEYWDS    TRANSFERASE, COVALENT INHIBITION                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.ROSSI,V.CASAZZA,S.GARAVAGLIA,K.V.SATHYASAIKUMAR,R.SCHWARCZ,         
AUTHOR   2 S.I.KOJIMA,K.OKUWAKI,S.I.ONO,Y.KAJII,M.RIZZI                         
REVDAT   2   26-OCT-11 2XH1    1       JRNL   REMARK VERSN                      
REVDAT   1   28-JUL-10 2XH1    0                                                
JRNL        AUTH   F.ROSSI,V.CASAZZA,S.GARAVAGLIA,K.V.SATHYASAIKUMAR,           
JRNL        AUTH 2 R.SCHWARCZ,S.I.KOJIMA,K.OKUWAKI,S.I.ONO,Y.KAJII,M.RIZZI      
JRNL        TITL   CRYSTAL STRUCTURE-BASED SELECTIVE TARGETING OF THE           
JRNL        TITL 2 PYRIDOXAL 5'-PHSOSPHATE DEPENDENT ENZYME KYNURENINE          
JRNL        TITL 3 AMINOTRANSFERASE II FOR COGNITIVE ENHANCEMENT                
JRNL        REF    J.MED.CHEM.                   V.  53  5684 2010              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   20684605                                                     
JRNL        DOI    10.1021/JM100464K                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.00                         
REMARK   3   NUMBER OF REFLECTIONS             : 53172                          
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) : 0.18929                         
REMARK   3   R VALUE            (WORKING SET) : 0.18814                         
REMARK   3   FREE R VALUE                     : 0.24123                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1113                            
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) : 2.100                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.154                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3846                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.198                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 68                           
REMARK   3   BIN FREE R VALUE                    : 0.268                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6467                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 89                                      
REMARK   3   SOLVENT ATOMS            : 416                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.306                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.81                                                 
REMARK   3    B22 (A**2) : -0.47                                                
REMARK   3    B33 (A**2) : -0.34                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.209         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.185         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.126         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.583         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6722 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9139 ; 1.795 ; 1.987       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   820 ; 6.941 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   284 ;43.159 ;24.789       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1136 ;17.867 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;19.735 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1004 ; 0.147 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5068 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3051 ; 0.226 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4584 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   448 ; 0.176 ; 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):    44 ; 0.278 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.149 ; 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):  4174 ; 1.117 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6694 ; 1.888 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2906 ; 2.776 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2445 ; 4.355 ; 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 : BABINET MODEL WITH 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          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 2XH1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUN-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-44188.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.981                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 210)                  
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53172                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.10                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.9                                
REMARK 200  R MERGE                    (I) : 0.12                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.10                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.0                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.40                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.80                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 2R2N                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       49.16150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       76.42850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.16150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       76.42850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.1 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, MET 1 TO GLU                          
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, MET 1 TO GLU                          
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     ARG A    20                                                      
REMARK 465     THR A    21                                                      
REMARK 465     MET A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     ASP A    24                                                      
REMARK 465     ILE A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     ARG A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     PRO A    30                                                      
REMARK 465     LYS A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     ARG B    20                                                      
REMARK 465     THR B    21                                                      
REMARK 465     MET B    22                                                      
REMARK 465     THR B    23                                                      
REMARK 465     ASP B    24                                                      
REMARK 465     ILE B    25                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     ARG B    28                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     PRO B    30                                                      
REMARK 465     LYS B    31                                                      
REMARK 465     SER B    32                                                      
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   OH   TYR B   195     OD2  ASP B   230              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   OE1  GLU A   211     OE1  GLU A   211     2565     1.73            
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 B 282   CD    GLU B 282   OE1     0.071                       
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    ASP A 169   CB  -  CG  -  OD1 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG A 270   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    LEU A 380   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    GLY B 107   C   -  N   -  CA  ANGL. DEV. = -19.8 DEGREES          
REMARK 500    LEU B 137   CA  -  CB  -  CG  ANGL. DEV. =  18.2 DEGREES          
REMARK 500    ARG B 283   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    ARG B 283   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 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    PRO A  18       21.78    -77.73                                   
REMARK 500    ASN A  96       65.30     28.72                                   
REMARK 500    ASP A 162     -154.49   -146.93                                   
REMARK 500    ASN A 189       48.74    -98.92                                   
REMARK 500    LYS A 240       15.61     58.04                                   
REMARK 500    SER A 266      128.98   -177.86                                   
REMARK 500    SER A 291      -90.51   -116.80                                   
REMARK 500    LEU A 293      -55.22     77.94                                   
REMARK 500    GLU A 372      -63.13   -124.78                                   
REMARK 500    PRO B  18     -166.30    -67.83                                   
REMARK 500    TYR B  74      151.46    -48.10                                   
REMARK 500    ASN B  96       66.17     32.82                                   
REMARK 500    ASP B 162     -152.72   -142.65                                   
REMARK 500    ASN B 189       57.95    -92.06                                   
REMARK 500    LYS B 240       13.29    -54.58                                   
REMARK 500    ILE B 265      -54.00   -120.34                                   
REMARK 500    SER B 266      125.70   -175.23                                   
REMARK 500    SER B 291      -87.29   -120.84                                   
REMARK 500    LEU B 293      -49.13     63.18                                   
REMARK 500    MET B 354       14.82   -141.74                                   
REMARK 500    GLU B 371      -66.21    -99.97                                   
REMARK 500    MET B 377      -80.40   -102.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A   -1     ASN A    2                  123.73                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR A  60        24.0      L          L   OUTSIDE RANGE           
REMARK 500    HIS B 101        24.4      L          L   OUTSIDE RANGE           
REMARK 500    THR B 145        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE B 228        24.5      L          L   OUTSIDE RANGE           
REMARK 500    THR B 297        23.3      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 322        23.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 BF5-PLP: COVALENT LINK BETWEEN THE PLP COFACTOR AND                  
REMARK 600  THE SYNTHETIC INHIBITOR NAMED BFF-122.                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BF5 A1426                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A1427                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BF5 B1426                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B1427                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1428                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1428                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VGZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN KYNURENINE                               
REMARK 900  AMINOTRANSFERASE II                                                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEGMENT 20-32 IS MISSING FROM THE COORDINATES FILE.              
REMARK 999 THE FIRST RESIDUE IS A GLU THAT REPLACES A MET AS A RESULT           
REMARK 999 OF CLONING STRATEGY                                                  
DBREF  2XH1 A   -1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  2XH1 B   -1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
SEQADV 2XH1 GLU A   -1  UNP  Q8N5Z0    MET     1 ENGINEERED MUTATION            
SEQADV 2XH1 GLU B   -1  UNP  Q8N5Z0    MET     1 ENGINEERED MUTATION            
SEQRES   1 A  425  GLU ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA          
SEQRES   2 A  425  ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU          
SEQRES   3 A  425  SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY          
SEQRES   4 A  425  LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL          
SEQRES   5 A  425  ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU          
SEQRES   6 A  425  GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA          
SEQRES   7 A  425  GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN          
SEQRES   8 A  425  ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO          
SEQRES   9 A  425  SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER          
SEQRES  10 A  425  GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN          
SEQRES  11 A  425  PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER          
SEQRES  12 A  425  GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE          
SEQRES  13 A  425  ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP          
SEQRES  14 A  425  SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP          
SEQRES  15 A  425  ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR          
SEQRES  16 A  425  THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU          
SEQRES  17 A  425  THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG          
SEQRES  18 A  425  LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR          
SEQRES  19 A  425  PHE LEU GLN PHE ASN LYS PHE ARG VAL PRO THR PHE LEU          
SEQRES  20 A  425  SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER          
SEQRES  21 A  425  PHE SER LYS ILE ILE SER SER GLY LEU ARG ILE GLY PHE          
SEQRES  22 A  425  LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU          
SEQRES  23 A  425  HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN          
SEQRES  24 A  425  GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU          
SEQRES  25 A  425  GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE          
SEQRES  26 A  425  TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP          
SEQRES  27 A  425  LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA          
SEQRES  28 A  425  ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN          
SEQRES  29 A  425  ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET          
SEQRES  30 A  425  GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP          
SEQRES  31 A  425  SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER          
SEQRES  32 A  425  SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL          
SEQRES  33 A  425  LEU ALA GLN LEU ILE LYS GLU SER LEU                          
SEQRES   1 B  425  GLU ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA          
SEQRES   2 B  425  ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU          
SEQRES   3 B  425  SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY          
SEQRES   4 B  425  LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL          
SEQRES   5 B  425  ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU          
SEQRES   6 B  425  GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA          
SEQRES   7 B  425  GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN          
SEQRES   8 B  425  ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO          
SEQRES   9 B  425  SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER          
SEQRES  10 B  425  GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN          
SEQRES  11 B  425  PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER          
SEQRES  12 B  425  GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE          
SEQRES  13 B  425  ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP          
SEQRES  14 B  425  SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP          
SEQRES  15 B  425  ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR          
SEQRES  16 B  425  THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU          
SEQRES  17 B  425  THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG          
SEQRES  18 B  425  LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR          
SEQRES  19 B  425  PHE LEU GLN PHE ASN LYS PHE ARG VAL PRO THR PHE LEU          
SEQRES  20 B  425  SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER          
SEQRES  21 B  425  PHE SER LYS ILE ILE SER SER GLY LEU ARG ILE GLY PHE          
SEQRES  22 B  425  LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU          
SEQRES  23 B  425  HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN          
SEQRES  24 B  425  GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU          
SEQRES  25 B  425  GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE          
SEQRES  26 B  425  TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP          
SEQRES  27 B  425  LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA          
SEQRES  28 B  425  ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN          
SEQRES  29 B  425  ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET          
SEQRES  30 B  425  GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP          
SEQRES  31 B  425  SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER          
SEQRES  32 B  425  SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL          
SEQRES  33 B  425  LEU ALA GLN LEU ILE LYS GLU SER LEU                          
HET    BF5  A1426      26                                                       
HET    PLP  A1427      15                                                       
HET    BF5  B1426      26                                                       
HET    PLP  B1427      15                                                       
HET    IOD  A1428       1                                                       
HET    GOL  B1428       6                                                       
HETNAM     BF5 (3S)-10-(4-AMINOPIPERAZIN-1-YL)-9-FLUORO-7-                      
HETNAM   2 BF5  HYDROXY-3-METHYL-2,3-DIHYDRO-8H-[1,4]OXAZINO[2,                 
HETNAM   3 BF5  3,4-IJ]QUINOLINE-6-CARBOXYLATE                                  
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     IOD IODIDE ION                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   3  BF5    2(C17 H19 F N4 O4)                                           
FORMUL   4  PLP    2(C8 H10 N O6 P)                                             
FORMUL   5  IOD    I 1-                                                         
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL   7  HOH   *416(H2 O)                                                    
HELIX    1   1 TYR A    3  ILE A    7  5                                   5    
HELIX    2   2 THR A    8  ALA A   13  1                                   6    
HELIX    3   3 ASN A   42  PHE A   46  5                                   5    
HELIX    4   4 GLY A   64  LEU A   72  1                                   9    
HELIX    5   5 ILE A   80  ASN A   96  1                                  17    
HELIX    6   6 PRO A   97  TYR A  102  5                                   6    
HELIX    7   7 PRO A  103  GLY A  107  5                                   5    
HELIX    8   8 GLY A  116  ILE A  129  1                                  14    
HELIX    9   9 TYR A  142  HIS A  150  1                                   9    
HELIX   10  10 PRO A  151  GLY A  153  5                                   3    
HELIX   11  11 VAL A  167  SER A  176  1                                  10    
HELIX   12  12 LYS A  179  ALA A  183  5                                   5    
HELIX   13  13 THR A  209  TYR A  223  1                                  15    
HELIX   14  14 PHE A  246  ASP A  250  5                                   5    
HELIX   15  15 LYS A  278  VAL A  290  1                                  13    
HELIX   16  16 SER A  296  THR A  342  1                                  47    
HELIX   17  17 VAL A  366  GLU A  372  1                                   7    
HELIX   18  18 GLU A  372  MET A  377  1                                   6    
HELIX   19  19 ASN A  385  TYR A  388  5                                   4    
HELIX   20  20 SER A  406  LEU A  425  1                                  20    
HELIX   21  21 TYR B    3  ILE B    7  5                                   5    
HELIX   22  22 THR B    8  ARG B   14  1                                   7    
HELIX   23  23 ASN B   42  PHE B   46  5                                   5    
HELIX   24  24 GLY B   64  LEU B   72  1                                   9    
HELIX   25  25 ILE B   80  ASN B   96  1                                  17    
HELIX   26  26 PRO B   97  TYR B  102  5                                   6    
HELIX   27  27 GLY B  116  ILE B  129  1                                  14    
HELIX   28  28 TYR B  142  HIS B  150  1                                   9    
HELIX   29  29 PRO B  151  GLY B  153  5                                   3    
HELIX   30  30 VAL B  167  SER B  176  1                                  10    
HELIX   31  31 LYS B  179  ALA B  183  5                                   5    
HELIX   32  32 THR B  209  TYR B  223  1                                  15    
HELIX   33  33 PHE B  246  ASP B  250  5                                   5    
HELIX   34  34 LYS B  278  VAL B  290  1                                  13    
HELIX   35  35 SER B  296  THR B  342  1                                  47    
HELIX   36  36 VAL B  366  GLU B  372  1                                   7    
HELIX   37  37 ASN B  385  TYR B  388  5                                   4    
HELIX   38  38 SER B  406  SER B  424  1                                  19    
SHEET    1  AA 2 ILE A  34  SER A  35  0                                        
SHEET    2  AA 2 VAL B 379  LEU B 380  1  N  LEU B 380   O  ILE A  34           
SHEET    1  AB 4 ILE A  61  PHE A  63  0                                        
SHEET    2  AB 4 PHE A  48  VAL A  55 -1  O  ALA A  51   N  PHE A  63           
SHEET    3  AB 4 PHE B  48  VAL B  55 -1  N  LYS B  49   O  THR A  54           
SHEET    4  AB 4 ILE B  61  PHE B  63 -1  O  ILE B  61   N  ILE B  53           
SHEET    1  AC 7 MET A 109  THR A 114  0                                        
SHEET    2  AC 7 GLY A 272  PRO A 277 -1  O  GLY A 272   N  THR A 114           
SHEET    3  AC 7 VAL A 255  SER A 260 -1  O  ARG A 257   N  THR A 275           
SHEET    4  AC 7 LEU A 226  ASP A 230  1  O  ILE A 227   N  ILE A 256           
SHEET    5  AC 7 PHE A 193  THR A 196  1  O  LEU A 194   N  ILE A 228           
SHEET    6  AC 7 ASN A 134  LEU A 137  1  O  LEU A 136   N  TYR A 195           
SHEET    7  AC 7 ASN A 155  ASN A 158  1  O  ASN A 155   N  VAL A 135           
SHEET    1  AD 2 SER A 161  ASP A 162  0                                        
SHEET    2  AD 2 GLY A 165  ILE A 166 -1  O  GLY A 165   N  ASP A 162           
SHEET    1  AE 4 ALA A 345  GLU A 346  0                                        
SHEET    2  AE 4 PHE A 355  VAL A 360 -1  O  LYS A 359   N  GLU A 346           
SHEET    3  AE 4 TYR A 397  SER A 401 -1  O  LEU A 398   N  ILE A 358           
SHEET    4  AE 4 LEU A 382  PRO A 383 -1  O  LEU A 382   N  ARG A 399           
SHEET    1  AF 2 VAL A 379  LEU A 380  0                                        
SHEET    2  AF 2 ILE B  34  SER B  35  1  O  ILE B  34   N  LEU A 380           
SHEET    1  BA 7 MET B 109  THR B 114  0                                        
SHEET    2  BA 7 GLY B 272  PRO B 277 -1  O  GLY B 272   N  THR B 114           
SHEET    3  BA 7 VAL B 255  SER B 260 -1  O  ARG B 257   N  THR B 275           
SHEET    4  BA 7 LEU B 226  ASP B 230  1  O  ILE B 227   N  ILE B 256           
SHEET    5  BA 7 PHE B 193  THR B 196  1  O  LEU B 194   N  ILE B 228           
SHEET    6  BA 7 ASN B 134  LEU B 137  1  O  LEU B 136   N  TYR B 195           
SHEET    7  BA 7 ASN B 155  ASN B 158  1  O  ASN B 155   N  VAL B 135           
SHEET    1  BB 2 SER B 161  ASP B 162  0                                        
SHEET    2  BB 2 GLY B 165  ILE B 166 -1  O  GLY B 165   N  ASP B 162           
SHEET    1  BC 4 ALA B 345  TRP B 347  0                                        
SHEET    2  BC 4 PHE B 355  VAL B 360 -1  O  LYS B 359   N  GLU B 346           
SHEET    3  BC 4 TYR B 397  SER B 401 -1  O  LEU B 398   N  ILE B 358           
SHEET    4  BC 4 LEU B 382  PRO B 383 -1  O  LEU B 382   N  ARG B 399           
LINK         N4  BF5 A1426                 C4A PLP A1427     1555   1555  1.42  
LINK         N4  BF5 B1426                 C4A PLP B1427     1555   1555  1.43  
CISPEP   1 GLU A  139    PRO A  140          0         1.38                     
CISPEP   2 ASN A  202    PRO A  203          0        15.10                     
CISPEP   3 GLU B  139    PRO B  140          0         3.06                     
CISPEP   4 ASN B  202    PRO B  203          0        12.12                     
SITE     1 AC1  8 TYR A 142  PLP A1427  HOH A2240  HOH A2241                    
SITE     2 AC1  8 GLY B  39  LEU B  40  SER B  75  PRO B  76                    
SITE     1 AC2 14 SER A 117  GLN A 118  TYR A 142  ASN A 202                    
SITE     2 AC2 14 ASP A 230  PRO A 232  TYR A 233  SER A 260                    
SITE     3 AC2 14 SER A 262  LYS A 263  ARG A 270  BF5 A1426                    
SITE     4 AC2 14 HOH A2187  TYR B  74                                          
SITE     1 AC3  6 GLY A  39  LEU A  40  TYR A  74  SER A  77                    
SITE     2 AC3  6 TYR B 142  PLP B1427                                          
SITE     1 AC4 13 TYR A  74  SER B 117  GLN B 118  TYR B 142                    
SITE     2 AC4 13 ASN B 202  ASP B 230  PRO B 232  TYR B 233                    
SITE     3 AC4 13 SER B 260  SER B 262  LYS B 263  ARG B 270                    
SITE     4 AC4 13 BF5 B1426                                                     
SITE     1 AC5  4 GLN A 119  LYS A 123  GLN B 119  LYS B 123                    
SITE     1 AC6  6 GLU B  -1  ASN B   2  SER B 105  PRO B 279                    
SITE     2 AC6  6 HOH B2173  HOH B2174                                          
CRYST1   98.323  152.857   60.800  90.00  90.00  90.00 P 21 21 2     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      0.010171  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006542  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016447        0.00000                         
MTRIX1   1 -0.999600 -0.003480  0.028090       29.79189    1                    
MTRIX2   1  0.017080 -0.865390  0.490000       71.86334    1                    
MTRIX3   1  0.022570  0.501090  0.865100      -19.65713    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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