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Database: PDB
Entry: 2R2N
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HEADER    TRANSFERASE                             27-AUG-07   2R2N              
TITLE     THE CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE II IN      
TITLE    2 COMPLEX WITH KYNURENINE                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KYNURENINE/ALPHA-AMINOADIPATE AMINOTRANSFERASE             
COMPND   3 MITOCHONDRIAL;                                                       
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 SYNONYM: KAT/AADAT, KYNURENINE--OXOGLUTARATE TRANSAMINASE II,        
COMPND   6 KYNURENINE AMINOTRANSFERASE II, KYNURENINE--OXOGLUTARATE             
COMPND   7 AMINOTRANSFERASE II, 2-AMINOADIPATE TRANSAMINASE, 2- AMINOADIPATE    
COMPND   8 AMINOTRANSFERASE, ALPHA-AMINOADIPATE AMINOTRANSFERASE, AADAT;        
COMPND   9 EC: 2.6.1.7, 2.6.1.39;                                               
COMPND  10 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: AADAT, KAT2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTYB                                      
KEYWDS    ALPHA & BETA PROTEIN, PLP-DEPENDENT TRANSFERASE, AMINOTRANSFERASE,    
KEYWDS   2 MITOCHONDRION, MULTIFUNCTIONAL ENZYME, PYRIDOXAL PHOSPHATE, TRANSIT  
KEYWDS   3 PEPTIDE, TRANSFERASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.HAN,H.ROBINSON,J.LI                                                 
REVDAT   4   13-JUL-11 2R2N    1       VERSN                                    
REVDAT   3   24-FEB-09 2R2N    1       VERSN                                    
REVDAT   2   18-MAR-08 2R2N    1       JRNL                                     
REVDAT   1   04-DEC-07 2R2N    0                                                
JRNL        AUTH   Q.HAN,H.ROBINSON,J.LI                                        
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE II.   
JRNL        REF    J.BIOL.CHEM.                  V. 283  3567 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18056995                                                     
JRNL        DOI    10.1074/JBC.M708358200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 116774                         
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6185                            
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5436                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 59.53                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 307                          
REMARK   3   BIN FREE R VALUE                    : 0.2850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13330                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 160                                     
REMARK   3   SOLVENT ATOMS            : 1341                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
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): 0.200         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.161         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13812 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18742 ; 1.796 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1696 ; 7.676 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   576 ;40.658 ;24.583       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2364 ;18.237 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    64 ;18.484 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2064 ; 0.207 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10440 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  7209 ; 0.231 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9437 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1282 ; 0.165 ; 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):    86 ; 0.268 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    27 ; 0.139 ; 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):  8538 ; 0.958 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13856 ; 1.710 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5274 ; 2.827 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4886 ; 4.300 ; 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 2R2N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044347.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0809                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 132070                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY                : 11.500                             
REMARK 200  R MERGE                    (I) : 0.09200                            
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) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 62.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37300                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 2QLR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 15% PEG 10000, PH 7.5,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       54.68000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10110 ANGSTROM**2                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11250 ANGSTROM**2                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    PRO A  16   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG A 257   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A 257   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG A 283   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B 242   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG B 257   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG B 257   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG B 283   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG C 283   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG C 283   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG C 321   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG C 321   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP D 231   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG D 242   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG D 242   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG D 283   NE  -  CZ  -  NH1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG D 283   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 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  16      -86.72    -19.63                                   
REMARK 500    SER A  17      -58.91   -159.36                                   
REMARK 500    ILE A  19      -74.19     22.59                                   
REMARK 500    ASN A  96       66.05     30.71                                   
REMARK 500    ASP A 162     -157.40   -145.48                                   
REMARK 500    ASP A 182      -47.77     13.02                                   
REMARK 500    LYS A 184       -1.19    -44.86                                   
REMARK 500    PRO A 186     -176.99    -56.92                                   
REMARK 500    GLN A 187      -21.18     62.45                                   
REMARK 500    ASN A 189       47.26     81.58                                   
REMARK 500    SER A 266      128.34   -178.74                                   
REMARK 500    SER A 291      -85.72   -118.57                                   
REMARK 500    LEU A 293      -50.70     74.45                                   
REMARK 500    MET A 354       16.50   -140.49                                   
REMARK 500    SER B  17     -139.29    -52.85                                   
REMARK 500    ARG B  20       33.90    -87.15                                   
REMARK 500    ASN B  96       65.30     29.55                                   
REMARK 500    ASP B 162     -158.91   -139.22                                   
REMARK 500    ASP B 224       62.37     39.11                                   
REMARK 500    SER B 266      122.42   -177.31                                   
REMARK 500    SER B 291      -89.48   -120.86                                   
REMARK 500    LEU B 293      -50.40     76.69                                   
REMARK 500    GLU B 372      -65.55   -107.03                                   
REMARK 500    PRO C  18      -83.08   -107.00                                   
REMARK 500    ILE C  19      -77.18     -0.38                                   
REMARK 500    MET C  22      -64.93    -98.38                                   
REMARK 500    THR C  23      -34.92    -39.97                                   
REMARK 500    TYR C  74      153.74    -49.52                                   
REMARK 500    ASN C  96       68.12     29.30                                   
REMARK 500    ASP C 162     -154.90   -131.57                                   
REMARK 500    PRO C 186      -64.09    -17.19                                   
REMARK 500    LYS C 240       35.59    -81.55                                   
REMARK 500    SER C 266      130.61   -179.37                                   
REMARK 500    SER C 291      -88.57   -116.97                                   
REMARK 500    LEU C 293      -48.61     79.41                                   
REMARK 500    SER D  17     -169.35    -77.79                                   
REMARK 500    PRO D  18      -75.86   -105.05                                   
REMARK 500    ILE D  19      -78.14     -3.41                                   
REMARK 500    MET D  22      -67.37    -95.04                                   
REMARK 500    ASN D  96       65.21     29.01                                   
REMARK 500    SER D 266      119.59    178.31                                   
REMARK 500    ARG D 270       65.64     63.10                                   
REMARK 500    SER D 291      -87.80   -117.53                                   
REMARK 500    LEU D 293      -53.45     76.96                                   
REMARK 500    GLU D 372      -64.99   -109.35                                   
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 PRO A  180     GLU A  181                 -139.56                    
REMARK 500 GLU A  181     ASP A  182                  123.45                    
REMARK 500 GLN A  187     LYS A  188                  141.35                    
REMARK 500 LEU A  341     THR A  342                 -127.21                    
REMARK 500 THR A  342     GLY A  343                 -126.34                    
REMARK 500 PRO C   16     SER C   17                 -148.73                    
REMARK 500 GLN C  187     LYS C  188                  142.96                    
REMARK 500 LYS C  240     PHE C  241                  147.34                    
REMARK 500 PRO D   16     SER D   17                 -148.99                    
REMARK 500 LYS D  240     PHE D  241                  147.13                    
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    ILE A 288        24.8      L          L   OUTSIDE RANGE           
REMARK 500    THR A 297        24.2      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 322        24.5      L          L   OUTSIDE RANGE           
REMARK 500    ILE B 228        23.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 319        23.5      L          L   OUTSIDE RANGE           
REMARK 500    VAL C 319        24.3      L          L   OUTSIDE RANGE           
REMARK 500    VAL C 322        22.9      L          L   OUTSIDE RANGE           
REMARK 500    GLU D  65        24.1      L          L   OUTSIDE RANGE           
REMARK 500    VAL D 284        24.2      L          L   OUTSIDE RANGE           
REMARK 500    ASP D 324        21.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP A 426                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP B 426                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP C 426                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMP D 426                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KYN A 427                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KYN C 427                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KYN A 428                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KYN C 428                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 427                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 429                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 428                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 429                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 430                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 429                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2QLR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE II            
DBREF  2R2N A    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  2R2N B    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  2R2N C    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  2R2N D    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
SEQRES   1 A  425  MET 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  MET 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                          
SEQRES   1 C  425  MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA          
SEQRES   2 C  425  ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU          
SEQRES   3 C  425  SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY          
SEQRES   4 C  425  LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL          
SEQRES   5 C  425  ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU          
SEQRES   6 C  425  GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA          
SEQRES   7 C  425  GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN          
SEQRES   8 C  425  ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO          
SEQRES   9 C  425  SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER          
SEQRES  10 C  425  GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN          
SEQRES  11 C  425  PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER          
SEQRES  12 C  425  GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE          
SEQRES  13 C  425  ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP          
SEQRES  14 C  425  SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP          
SEQRES  15 C  425  ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR          
SEQRES  16 C  425  THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU          
SEQRES  17 C  425  THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG          
SEQRES  18 C  425  LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR          
SEQRES  19 C  425  PHE LEU GLN PHE ASN LYS PHE ARG VAL PRO THR PHE LEU          
SEQRES  20 C  425  SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER          
SEQRES  21 C  425  PHE SER LYS ILE ILE SER SER GLY LEU ARG ILE GLY PHE          
SEQRES  22 C  425  LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU          
SEQRES  23 C  425  HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN          
SEQRES  24 C  425  GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU          
SEQRES  25 C  425  GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE          
SEQRES  26 C  425  TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP          
SEQRES  27 C  425  LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA          
SEQRES  28 C  425  ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN          
SEQRES  29 C  425  ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET          
SEQRES  30 C  425  GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP          
SEQRES  31 C  425  SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER          
SEQRES  32 C  425  SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL          
SEQRES  33 C  425  LEU ALA GLN LEU ILE LYS GLU SER LEU                          
SEQRES   1 D  425  MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA          
SEQRES   2 D  425  ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU          
SEQRES   3 D  425  SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY          
SEQRES   4 D  425  LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL          
SEQRES   5 D  425  ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU          
SEQRES   6 D  425  GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA          
SEQRES   7 D  425  GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN          
SEQRES   8 D  425  ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO          
SEQRES   9 D  425  SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER          
SEQRES  10 D  425  GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN          
SEQRES  11 D  425  PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER          
SEQRES  12 D  425  GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE          
SEQRES  13 D  425  ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP          
SEQRES  14 D  425  SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP          
SEQRES  15 D  425  ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR          
SEQRES  16 D  425  THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU          
SEQRES  17 D  425  THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG          
SEQRES  18 D  425  LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR          
SEQRES  19 D  425  PHE LEU GLN PHE ASN LYS PHE ARG VAL PRO THR PHE LEU          
SEQRES  20 D  425  SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER          
SEQRES  21 D  425  PHE SER LYS ILE ILE SER SER GLY LEU ARG ILE GLY PHE          
SEQRES  22 D  425  LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU          
SEQRES  23 D  425  HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN          
SEQRES  24 D  425  GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU          
SEQRES  25 D  425  GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE          
SEQRES  26 D  425  TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP          
SEQRES  27 D  425  LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA          
SEQRES  28 D  425  ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN          
SEQRES  29 D  425  ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET          
SEQRES  30 D  425  GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP          
SEQRES  31 D  425  SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER          
SEQRES  32 D  425  SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL          
SEQRES  33 D  425  LEU ALA GLN LEU ILE LYS GLU SER LEU                          
HET    PMP  A 426      16                                                       
HET    KYN  A 427      15                                                       
HET    KYN  A 428      15                                                       
HET    PMP  B 426      16                                                       
HET    PMP  C 426      16                                                       
HET    KYN  C 427      15                                                       
HET    KYN  C 428      15                                                       
HET    PMP  D 426      16                                                       
HET    GOL  A 429       6                                                       
HET    GOL  C 429       6                                                       
HET    GOL  D 427       6                                                       
HET    GOL  D 428       6                                                       
HET    GOL  D 429       6                                                       
HET    GOL  D 430       6                                                       
HETNAM     PMP 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE                          
HETNAM     KYN (2S)-2-AMINO-4-(2-AMINOPHENYL)-4-OXOBUTANOIC ACID                
HETNAM     GOL GLYCEROL                                                         
HETSYN     PMP PYRIDOXAMINE-5'-PHOSPHATE                                        
HETSYN     KYN L-KYNURENINE                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  PMP    4(C8 H13 N2 O5 P)                                            
FORMUL   6  KYN    4(C10 H12 N2 O3)                                             
FORMUL  13  GOL    6(C3 H8 O3)                                                  
FORMUL  19  HOH   *1341(H2 O)                                                   
HELIX    1   1 ASN A    2  ILE A    7  5                                   6    
HELIX    2   2 THR A    8  ALA A   13  1                                   6    
HELIX    3   3 PRO A   18  ARG A   20  5                                   3    
HELIX    4   4 THR A   21  GLY A   29  1                                   9    
HELIX    5   5 ASN A   42  PHE A   46  5                                   5    
HELIX    6   6 GLY A   64  LEU A   72  1                                   9    
HELIX    7   7 ILE A   80  ASN A   96  1                                  17    
HELIX    8   8 PRO A  103  GLY A  107  5                                   5    
HELIX    9   9 GLY A  116  ILE A  129  1                                  14    
HELIX   10  10 TYR A  142  HIS A  150  1                                   9    
HELIX   11  11 PRO A  151  GLY A  153  5                                   3    
HELIX   12  12 VAL A  167  SER A  176  1                                  10    
HELIX   13  13 THR A  209  TYR A  223  1                                  15    
HELIX   14  14 TYR A  233  GLN A  237  5                                   5    
HELIX   15  15 PHE A  246  ASP A  250  5                                   5    
HELIX   16  16 LYS A  278  VAL A  290  1                                  13    
HELIX   17  17 SER A  296  LEU A  341  1                                  46    
HELIX   18  18 VAL A  366  GLU A  372  1                                   7    
HELIX   19  19 GLU A  372  MET A  377  1                                   6    
HELIX   20  20 ASN A  385  TYR A  388  5                                   4    
HELIX   21  21 SER A  406  LEU A  425  1                                  20    
HELIX   22  22 ASN B    2  ILE B    7  5                                   6    
HELIX   23  23 THR B    8  ARG B   14  1                                   7    
HELIX   24  24 THR B   21  ARG B   28  1                                   8    
HELIX   25  25 ASN B   42  PHE B   46  5                                   5    
HELIX   26  26 GLY B   64  LEU B   72  1                                   9    
HELIX   27  27 ILE B   80  ASN B   96  1                                  17    
HELIX   28  28 PRO B   97  TYR B  102  5                                   6    
HELIX   29  29 GLY B  116  ILE B  129  1                                  14    
HELIX   30  30 TYR B  142  HIS B  150  1                                   9    
HELIX   31  31 PRO B  151  GLY B  153  5                                   3    
HELIX   32  32 VAL B  167  SER B  176  1                                  10    
HELIX   33  33 ARG B  177  TRP B  178  5                                   2    
HELIX   34  34 LYS B  179  ASN B  189  5                                  11    
HELIX   35  35 THR B  209  TYR B  223  1                                  15    
HELIX   36  36 TYR B  233  GLN B  237  5                                   5    
HELIX   37  37 PHE B  246  ASP B  250  5                                   5    
HELIX   38  38 LYS B  278  VAL B  290  1                                  13    
HELIX   39  39 SER B  296  THR B  342  1                                  47    
HELIX   40  40 VAL B  366  GLU B  372  1                                   7    
HELIX   41  41 GLU B  372  MET B  377  1                                   6    
HELIX   42  42 ASN B  385  TYR B  388  5                                   4    
HELIX   43  43 SER B  406  SER B  424  1                                  19    
HELIX   44  44 ASN C    2  ILE C    7  5                                   6    
HELIX   45  45 THR C    8  ARG C   14  1                                   7    
HELIX   46  46 PRO C   18  THR C   21  5                                   4    
HELIX   47  47 MET C   22  ARG C   28  1                                   7    
HELIX   48  48 ASN C   42  PHE C   46  5                                   5    
HELIX   49  49 GLY C   64  LEU C   72  1                                   9    
HELIX   50  50 ILE C   80  ASN C   96  1                                  17    
HELIX   51  51 PRO C  103  GLY C  107  5                                   5    
HELIX   52  52 GLY C  116  ILE C  129  1                                  14    
HELIX   53  53 TYR C  142  HIS C  150  1                                   9    
HELIX   54  54 PRO C  151  GLY C  153  5                                   3    
HELIX   55  55 VAL C  167  SER C  176  1                                  10    
HELIX   56  56 ARG C  177  TRP C  178  5                                   2    
HELIX   57  57 LYS C  179  ASN C  185  5                                   7    
HELIX   58  58 THR C  209  TYR C  223  1                                  15    
HELIX   59  59 TYR C  233  GLN C  237  5                                   5    
HELIX   60  60 PHE C  246  ASP C  250  5                                   5    
HELIX   61  61 LYS C  278  SER C  291  1                                  14    
HELIX   62  62 SER C  296  THR C  342  1                                  47    
HELIX   63  63 VAL C  366  MET C  377  1                                  12    
HELIX   64  64 ASN C  385  TYR C  388  5                                   4    
HELIX   65  65 SER C  406  LEU C  425  1                                  20    
HELIX   66  66 ASN D    2  ILE D    7  5                                   6    
HELIX   67  67 THR D    8  ARG D   14  1                                   7    
HELIX   68  68 PRO D   18  MET D   22  5                                   5    
HELIX   69  69 ILE D   25  GLY D   29  5                                   5    
HELIX   70  70 ASN D   42  PHE D   46  5                                   5    
HELIX   71  71 GLY D   64  LEU D   72  1                                   9    
HELIX   72  72 ILE D   80  ASN D   96  1                                  17    
HELIX   73  73 PRO D  103  GLY D  107  5                                   5    
HELIX   74  74 GLY D  116  ILE D  129  1                                  14    
HELIX   75  75 TYR D  142  HIS D  150  1                                   9    
HELIX   76  76 PRO D  151  GLY D  153  5                                   3    
HELIX   77  77 VAL D  167  SER D  176  1                                  10    
HELIX   78  78 ARG D  177  TRP D  178  5                                   2    
HELIX   79  79 LYS D  179  ASN D  189  5                                  11    
HELIX   80  80 THR D  209  TYR D  223  1                                  15    
HELIX   81  81 TYR D  233  GLN D  237  5                                   5    
HELIX   82  82 PHE D  246  ASP D  250  5                                   5    
HELIX   83  83 LYS D  278  SER D  291  1                                  14    
HELIX   84  84 SER D  296  THR D  342  1                                  47    
HELIX   85  85 VAL D  366  GLU D  372  1                                   7    
HELIX   86  86 GLU D  372  MET D  377  1                                   6    
HELIX   87  87 ASN D  385  TYR D  388  5                                   4    
HELIX   88  88 SER D  406  GLU D  423  1                                  18    
SHEET    1   A 2 ILE A  34  SER A  35  0                                        
SHEET    2   A 2 VAL B 379  LEU B 380  1  O  LEU B 380   N  ILE A  34           
SHEET    1   B 4 ILE A  61  PHE A  63  0                                        
SHEET    2   B 4 PHE A  48  VAL A  55 -1  N  ILE A  53   O  ILE A  61           
SHEET    3   B 4 PHE B  48  VAL B  55 -1  O  LYS B  49   N  THR A  54           
SHEET    4   B 4 ILE B  61  PHE B  63 -1  O  ILE B  61   N  ILE B  53           
SHEET    1   C 7 MET A 109  THR A 114  0                                        
SHEET    2   C 7 GLY A 272  PRO A 277 -1  O  GLY A 276   N  ASP A 110           
SHEET    3   C 7 VAL A 255  SER A 260 -1  N  ASP A 259   O  PHE A 273           
SHEET    4   C 7 LEU A 226  ASP A 230  1  N  ILE A 227   O  ILE A 256           
SHEET    5   C 7 PHE A 193  THR A 196  1  N  LEU A 194   O  ILE A 228           
SHEET    6   C 7 ASN A 134  ASP A 138  1  N  LEU A 136   O  TYR A 195           
SHEET    7   C 7 ASN A 155  VAL A 159  1  O  ILE A 157   N  VAL A 135           
SHEET    1   D 2 SER A 161  ASP A 162  0                                        
SHEET    2   D 2 GLY A 165  ILE A 166 -1  O  GLY A 165   N  ASP A 162           
SHEET    1   E 4 ALA A 345  TRP A 347  0                                        
SHEET    2   E 4 PHE A 355  VAL A 360 -1  O  LYS A 359   N  GLU A 346           
SHEET    3   E 4 TYR A 397  SER A 401 -1  O  ALA A 400   N  LEU A 356           
SHEET    4   E 4 LEU A 382  PRO A 383 -1  N  LEU A 382   O  ARG A 399           
SHEET    1   F 2 VAL A 379  LEU A 380  0                                        
SHEET    2   F 2 ILE B  34  SER B  35  1  O  ILE B  34   N  LEU A 380           
SHEET    1   G 7 MET B 109  THR B 114  0                                        
SHEET    2   G 7 GLY B 272  PRO B 277 -1  O  LEU B 274   N  CYS B 112           
SHEET    3   G 7 VAL B 255  SER B 260 -1  N  ARG B 257   O  THR B 275           
SHEET    4   G 7 LEU B 226  ASP B 230  1  N  GLU B 229   O  ILE B 256           
SHEET    5   G 7 PHE B 193  THR B 196  1  N  LEU B 194   O  ILE B 228           
SHEET    6   G 7 ASN B 134  ASP B 138  1  N  LEU B 136   O  TYR B 195           
SHEET    7   G 7 ASN B 155  VAL B 159  1  O  ILE B 157   N  VAL B 135           
SHEET    1   H 2 SER B 161  ASP B 162  0                                        
SHEET    2   H 2 GLY B 165  ILE B 166 -1  O  GLY B 165   N  ASP B 162           
SHEET    1   I 4 ALA B 345  TRP B 347  0                                        
SHEET    2   I 4 PHE B 355  VAL B 360 -1  O  LYS B 359   N  GLU B 346           
SHEET    3   I 4 TYR B 397  SER B 401 -1  O  LEU B 398   N  ILE B 358           
SHEET    4   I 4 LEU B 382  PRO B 383 -1  N  LEU B 382   O  ARG B 399           
SHEET    1   J 2 ILE C  34  SER C  35  0                                        
SHEET    2   J 2 VAL D 379  LEU D 380  1  O  LEU D 380   N  ILE C  34           
SHEET    1   K 4 ILE C  61  PHE C  63  0                                        
SHEET    2   K 4 PHE C  48  VAL C  55 -1  N  ILE C  53   O  ILE C  61           
SHEET    3   K 4 PHE D  48  VAL D  55 -1  O  THR D  54   N  LYS C  49           
SHEET    4   K 4 ILE D  61  PHE D  63 -1  O  ILE D  61   N  ILE D  53           
SHEET    1   L 7 MET C 109  THR C 114  0                                        
SHEET    2   L 7 GLY C 272  PRO C 277 -1  O  LEU C 274   N  CYS C 112           
SHEET    3   L 7 VAL C 255  SER C 260 -1  N  ARG C 257   O  THR C 275           
SHEET    4   L 7 LEU C 226  ASP C 230  1  N  GLU C 229   O  ALA C 258           
SHEET    5   L 7 PHE C 193  THR C 196  1  N  LEU C 194   O  ILE C 228           
SHEET    6   L 7 ASN C 134  ASP C 138  1  N  LEU C 136   O  TYR C 195           
SHEET    7   L 7 ASN C 155  VAL C 159  1  O  ILE C 157   N  VAL C 135           
SHEET    1   M 2 SER C 161  ASP C 162  0                                        
SHEET    2   M 2 GLY C 165  ILE C 166 -1  O  GLY C 165   N  ASP C 162           
SHEET    1   N 4 ALA C 345  GLU C 346  0                                        
SHEET    2   N 4 PHE C 355  VAL C 360 -1  O  LYS C 359   N  GLU C 346           
SHEET    3   N 4 TYR C 397  SER C 401 -1  O  ALA C 400   N  LEU C 356           
SHEET    4   N 4 LEU C 382  PRO C 383 -1  N  LEU C 382   O  ARG C 399           
SHEET    1   O 2 VAL C 379  LEU C 380  0                                        
SHEET    2   O 2 ILE D  34  SER D  35  1  O  ILE D  34   N  LEU C 380           
SHEET    1   P 7 MET D 109  THR D 114  0                                        
SHEET    2   P 7 GLY D 272  PRO D 277 -1  O  GLY D 276   N  ASP D 110           
SHEET    3   P 7 VAL D 255  SER D 260 -1  N  ARG D 257   O  THR D 275           
SHEET    4   P 7 LEU D 226  ASP D 230  1  N  GLU D 229   O  ILE D 256           
SHEET    5   P 7 PHE D 193  THR D 196  1  N  LEU D 194   O  ILE D 228           
SHEET    6   P 7 ASN D 134  LEU D 137  1  N  LEU D 136   O  TYR D 195           
SHEET    7   P 7 ASN D 155  ASN D 158  1  O  ILE D 157   N  VAL D 135           
SHEET    1   Q 2 SER D 161  ASP D 162  0                                        
SHEET    2   Q 2 GLY D 165  ILE D 166 -1  O  GLY D 165   N  ASP D 162           
SHEET    1   R 4 ALA D 345  GLU D 346  0                                        
SHEET    2   R 4 PHE D 355  VAL D 360 -1  O  LYS D 359   N  GLU D 346           
SHEET    3   R 4 TYR D 397  SER D 401 -1  O  ALA D 400   N  LEU D 356           
SHEET    4   R 4 LEU D 382  PRO D 383 -1  N  LEU D 382   O  ARG D 399           
CISPEP   1 SER A   17    PRO A   18          0       -14.72                     
CISPEP   2 GLU A  139    PRO A  140          0         6.85                     
CISPEP   3 ASN A  202    PRO A  203          0        17.24                     
CISPEP   4 SER B   17    PRO B   18          0       -28.70                     
CISPEP   5 GLU B  139    PRO B  140          0        -2.61                     
CISPEP   6 ASN B  202    PRO B  203          0        20.25                     
CISPEP   7 SER C   17    PRO C   18          0       -10.15                     
CISPEP   8 GLU C  139    PRO C  140          0         5.57                     
CISPEP   9 ASN C  202    PRO C  203          0        15.94                     
CISPEP  10 SER D   17    PRO D   18          0       -10.58                     
CISPEP  11 GLU D  139    PRO D  140          0         1.02                     
CISPEP  12 ASN D  202    PRO D  203          0        18.79                     
SITE     1 AC1 14 SER A 117  GLN A 118  TYR A 142  ASN A 202                    
SITE     2 AC1 14 ASP A 230  PRO A 232  TYR A 233  SER A 260                    
SITE     3 AC1 14 SER A 262  LYS A 263  ARG A 270  HOH A 572                    
SITE     4 AC1 14 HOH A 661  TYR B  74                                          
SITE     1 AC2 13 TYR A  74  SER B 117  GLN B 118  TYR B 142                    
SITE     2 AC2 13 ASN B 202  ASP B 230  PRO B 232  TYR B 233                    
SITE     3 AC2 13 SER B 260  SER B 262  LYS B 263  ARG B 270                    
SITE     4 AC2 13 HOH B 635                                                     
SITE     1 AC3 13 SER C 117  GLN C 118  TYR C 142  ASN C 202                    
SITE     2 AC3 13 ASP C 230  PRO C 232  TYR C 233  SER C 260                    
SITE     3 AC3 13 SER C 262  LYS C 263  ARG C 270  HOH C 694                    
SITE     4 AC3 13 TYR D  74                                                     
SITE     1 AC4 14 TYR C  74  GLY D 116  SER D 117  GLN D 118                    
SITE     2 AC4 14 TYR D 142  ASN D 202  ASP D 230  PRO D 232                    
SITE     3 AC4 14 TYR D 233  SER D 260  SER D 262  LYS D 263                    
SITE     4 AC4 14 ARG D 270  HOH D 667                                          
SITE     1 AC5  7 ILE A  19  ARG A  20  LEU A 293  HOH A 515                    
SITE     2 AC5  7 SER B 143  ASN B 202  ARG B 399                               
SITE     1 AC6  8 ILE C  19  ARG C  20  GLY C  39  LEU C  40                    
SITE     2 AC6  8 TYR C  74  HOH C 635  ASN D 202  ARG D 399                    
SITE     1 AC7 10 TYR A 142  ASN A 202  ARG A 399  HOH A 661                    
SITE     2 AC7 10 ILE B  19  ARG B  20  GLY B  39  TYR B  74                    
SITE     3 AC7 10 HOH B 453  HOH B 731                                          
SITE     1 AC8  8 ASN C 202  ARG C 399  HOH C 657  HOH C 703                    
SITE     2 AC8  8 ILE D  19  GLY D  39  LEU D  40  HOH D 638                    
SITE     1 AC9  8 PRO D  76  SER D  77  ALA D  78  GLY D  79                    
SITE     2 AC9  8 LEU D  84  HOH D 697  HOH D 726  HOH D 762                    
SITE     1 BC1  6 GLU C  56  ASN C  57  HIS C 318  ARG C 321                    
SITE     2 BC1  6 HOH C 629  HOH C 702                                          
SITE     1 BC2  7 GLU D 346  TRP D 347  HIS D 348  TRP D 357                    
SITE     2 BC2  7 TYR D 397  HOH D 535  HOH D 651                               
SITE     1 BC3  9 MET C  45  PHE C  46  PRO C  47  GLU D  56                    
SITE     2 BC3  9 ASN D  57  HIS D 318  ARG D 321  HOH D 660                    
SITE     3 BC3  9 HOH D 759                                                     
SITE     1 BC4  6 SER D 207  LEU D 208  THR D 209  HOH D 503                    
SITE     2 BC4  6 HOH D 533  HOH D 555                                          
SITE     1 BC5 11 PRO A  43  ASN A  44  PHE A  46  PHE A  48                    
SITE     2 BC5 11 LYS A  49  GLU A  65  MET A  68  LYS A  69                    
SITE     3 BC5 11 LEU A  72  HOH A 478  HOH A 532                               
CRYST1   70.843  109.360  119.354  90.00  94.68  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014116  0.000000  0.001155        0.00000                         
SCALE2      0.000000  0.009144  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008406        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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