GenomeNet

Database: PDB
Entry: 6T8Q
LinkDB: 6T8Q
Original site: 6T8Q 
HEADER    TRANSFERASE                             24-OCT-19   6T8Q              
TITLE     HKATII IN COMPLEX WITH LIGAND (2R)-N-BENZYL-1-[6-METHYL-5-(OXAN-4-YL)-
TITLE    2 7-OXO-6H,7H-[1,3]THIAZOLO[5,4-D]PYRIMIDIN-2-YL]PYRROLIDINE-2-        
TITLE    3 CARBOXAMIDE                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KYNURENINE/ALPHA-AMINOADIPATE AMINOTRANSFERASE,            
COMPND   3 MITOCHONDRIAL;                                                       
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: NONE;                                                      
COMPND   6 SYNONYM: KAT/AADAT,2-AMINOADIPATE AMINOTRANSFERASE,2-AMINOADIPATE    
COMPND   7 TRANSAMINASE,ALPHA-AMINOADIPATE AMINOTRANSFERASE,AADAT,KYNURENINE    
COMPND   8 AMINOTRANSFERASE II,KYNURENINE--OXOGLUTARATE AMINOTRANSFERASE II,    
COMPND   9 KYNURENINE--OXOGLUTARATE TRANSAMINASE 2,KYNURENINE--OXOGLUTARATE     
COMPND  10 TRANSAMINASE II;                                                     
COMPND  11 EC: 2.6.1.39,2.6.1.7;                                                
COMPND  12 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: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    ALPHA & BETA PROTEIN, PLP-DEPENDENT TRANSFERASE, KAT II, KYNURENINE   
KEYWDS   2 AM, PROTEROS BIOSTRUCTURES GMBH, TRANSFERASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.BLAESSE,J.VENALAINEN                                                
REVDAT   3   18-MAR-20 6T8Q    1       JRNL                                     
REVDAT   2   11-MAR-20 6T8Q    1       JRNL                                     
REVDAT   1   04-MAR-20 6T8Q    0                                                
JRNL        AUTH   T.KALLIOKOSKI,P.RUMMAKKO,M.RANTANEN,M.BLAESSE,M.AUGUSTIN,    
JRNL        AUTH 2 G.R.UMMENTHALA,S.CHOUDHARY,J.VENALAINEN                      
JRNL        TITL   DISCOVERY OF SULFONAMIDES AND                                
JRNL        TITL 2 9-OXO-2,8-DIAZASPIRO[5,5]UNDECANE-2-CARBOXAMIDES AS HUMAN    
JRNL        TITL 3 KYNURENINE AMINOTRANSFERASE 2 (KAT2) INHIBITORS.             
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  30 27060 2020              
JRNL        REFN                   ESSN 1464-3405                               
JRNL        PMID   32113843                                                     
JRNL        DOI    10.1016/J.BMCL.2020.127060                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.51 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0155                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.51                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 125.43                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 27915                          
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) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 928                             
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) : 2.51                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.58                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2044                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.38                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 73                           
REMARK   3   BIN FREE R VALUE                    : 0.3730                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3369                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 157                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.17                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.60000                                              
REMARK   3    B22 (A**2) : 0.60000                                              
REMARK   3    B33 (A**2) : -1.94000                                             
REMARK   3    B12 (A**2) : 0.30000                                              
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): 0.233         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.198         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.146         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.996        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3482 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3303 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4717 ; 1.673 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7607 ; 1.296 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   433 ; 7.087 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   138 ;40.202 ;24.710       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   567 ;13.599 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;16.421 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   523 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3919 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   754 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    15                          
REMARK   3    RESIDUE RANGE :   A    75        A   325                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.3050  -9.8600 -20.5540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2835 T22:   0.1202                                     
REMARK   3      T33:   0.0306 T12:  -0.0184                                     
REMARK   3      T13:   0.0054 T23:  -0.0233                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6062 L22:   1.4878                                     
REMARK   3      L33:   2.2235 L12:  -0.0246                                     
REMARK   3      L13:   0.2264 L23:   0.4780                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0380 S12:  -0.1008 S13:   0.0254                       
REMARK   3      S21:   0.1421 S22:  -0.0972 S23:   0.1981                       
REMARK   3      S31:   0.0853 S32:  -0.3861 S33:   0.1352                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    16        A    40                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.9980 -17.6210 -50.7230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5515 T22:   0.3157                                     
REMARK   3      T33:   0.2925 T12:   0.0395                                     
REMARK   3      T13:   0.0743 T23:  -0.0661                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8805 L22:   4.6849                                     
REMARK   3      L33:   6.3774 L12:   4.0178                                     
REMARK   3      L13:   4.2107 L23:   4.5380                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1097 S12:  -0.7495 S13:   0.8896                       
REMARK   3      S21:   0.2964 S22:  -0.6100 S23:   1.0598                       
REMARK   3      S31:  -0.0792 S32:  -1.0390 S33:   0.7198                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    41        A    74                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.0180 -34.2510 -39.8080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7003 T22:   0.2026                                     
REMARK   3      T33:   0.1626 T12:  -0.1823                                     
REMARK   3      T13:   0.0332 T23:  -0.0517                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8091 L22:   4.0021                                     
REMARK   3      L33:   6.3443 L12:  -1.4702                                     
REMARK   3      L13:   3.2036 L23:  -3.2671                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3083 S12:  -0.2730 S13:  -0.3904                       
REMARK   3      S21:  -0.1598 S22:   0.2045 S23:   0.2670                       
REMARK   3      S31:   1.0200 S32:  -0.7165 S33:  -0.5128                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   326        A   440                          
REMARK   3    ORIGIN FOR THE GROUP (A):  87.7280 -15.6000  -5.1770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4670 T22:   0.3317                                     
REMARK   3      T33:   0.0742 T12:   0.0354                                     
REMARK   3      T13:  -0.0710 T23:   0.0251                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8117 L22:   3.6828                                     
REMARK   3      L33:   2.9988 L12:  -1.7832                                     
REMARK   3      L13:   1.2293 L23:  -0.1290                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2029 S12:  -0.3636 S13:   0.3374                       
REMARK   3      S21:   0.3738 S22:  -0.0116 S23:  -0.4609                       
REMARK   3      S31:   0.1267 S32:   0.5531 S33:   0.2145                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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: U VALUES : WITH TLS ADDED HYDROGENS       
REMARK   3  HAVE BEEN ADDED IN THE RIDING POSITIONS                             
REMARK   4                                                                      
REMARK   4 6T8Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-OCT-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292103294.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUL-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28843                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.510                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 125.430                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.51                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 46.86                              
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: 5TF5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, CADMIUM CHLORIDE, SODIUM        
REMARK 280  ACETATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       93.10200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       46.55100            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       69.82650            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       23.27550            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      116.37750            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       93.10200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       46.55100            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       23.27550            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       69.82650            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      116.37750            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11370 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 30420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -153.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      144.82900            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -69.82650            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CL    CL A 510  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 601  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 652  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -26                                                      
REMARK 465     SER A   -25                                                      
REMARK 465     TYR A   -24                                                      
REMARK 465     TYR A   -23                                                      
REMARK 465     HIS A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     ASP A   -16                                                      
REMARK 465     TYR A   -15                                                      
REMARK 465     ASP A   -14                                                      
REMARK 465     ILE A   -13                                                      
REMARK 465     PRO A   -12                                                      
REMARK 465     THR A   -11                                                      
REMARK 465     THR A   -10                                                      
REMARK 465     GLU A    -9                                                      
REMARK 465     ASN A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     TYR A    -6                                                      
REMARK 465     PHE A    -5                                                      
REMARK 465     GLN A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A    0   CD   OE1  OE2                                       
REMARK 480     ARG A   20   NE   CZ   NH1  NH2                                  
REMARK 480     ARG A   28   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS A   59   CD   CE   NZ                                        
REMARK 480     LYS A   93   CD   CE   NZ                                        
REMARK 480     LYS A  179   CE   NZ                                             
REMARK 480     LYS A  184   CE   NZ                                             
REMARK 480     GLN A  187   CG   CD   OE1  NE2                                  
REMARK 480     GLU A  218   CD   OE1  OE2                                       
REMARK 480     LYS A  240   CG   CD   CE   NZ                                   
REMARK 480     PHE A  241   CD1  CD2  CE1  CE2  CZ                              
REMARK 480     GLU A  313   CD   OE1  OE2                                       
REMARK 480     ILE A  363   CD1                                                 
REMARK 480     LYS A  367   NZ                                                  
REMARK 480     GLU A  368   CG   CD   OE1  OE2                                  
REMARK 480     GLU A  372   CD   OE1  OE2                                       
REMARK 480     LYS A  373   NZ                                                  
REMARK 480     LYS A  376   CD   CE   NZ                                        
REMARK 480     LYS A  422   NZ                                                  
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    ARG A 270   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  32       94.67    -63.36                                   
REMARK 500    ASN A  96       64.95     31.43                                   
REMARK 500    ILE A 265      -54.46   -123.89                                   
REMARK 500    SER A 266      133.87   -175.58                                   
REMARK 500    ARG A 270       60.90     60.10                                   
REMARK 500    SER A 291      -90.84   -108.25                                   
REMARK 500    LEU A 293      -55.41     71.76                                   
REMARK 500    SER A 296      122.44    -38.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 507  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 149   O                                                      
REMARK 620 2 CYS A 154   O   165.5                                              
REMARK 620 3 CYS A 154   SG   89.2  85.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 503  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 169   OD1                                                    
REMARK 620 2 GLU A 215   OE1  95.4                                              
REMARK 620 3 GLU A 215   OE2 142.9  51.0                                        
REMARK 620 4 ASP A 169   OD1   0.0  95.4 142.9                                  
REMARK 620 5 GLU A 215   OE1  95.4   0.0  51.0  95.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 504  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 224   OD1                                                    
REMARK 620 2 HOH A 679   O    79.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 509  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 282   OE1                                                    
REMARK 620 2 GLU A 282   OE2  52.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 502  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 287   NE2                                                    
REMARK 620 2 CYS A 122   SG   68.8                                              
REMARK 620 3 GLU A 126   OE1  49.6  23.8                                        
REMARK 620 4 GLU A 126   OE2  69.8  30.4  24.5                                  
REMARK 620 5 HOH A 702   O    95.4  52.4  73.2  81.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 505  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 320   OD2                                                    
REMARK 620 2 ASP A 324   OD2 120.8                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MVQ A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 505                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 506                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 510                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 511                 
DBREF  6T8Q A    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
SEQADV 6T8Q MET A  -26  UNP  Q8N5Z0              INITIATING METHIONINE          
SEQADV 6T8Q SER A  -25  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q TYR A  -24  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q TYR A  -23  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q HIS A  -22  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q HIS A  -21  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q HIS A  -20  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q HIS A  -19  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q HIS A  -18  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q HIS A  -17  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q ASP A  -16  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q TYR A  -15  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q ASP A  -14  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q ILE A  -13  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q PRO A  -12  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q THR A  -11  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q THR A  -10  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q GLU A   -9  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q ASN A   -8  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q LEU A   -7  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q TYR A   -6  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q PHE A   -5  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q GLN A   -4  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q GLY A   -3  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q ALA A   -2  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q MET A   -1  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8Q GLU A    0  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQRES   1 A  452  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 A  452  ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET          
SEQRES   3 A  452  GLU MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA          
SEQRES   4 A  452  ALA ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE          
SEQRES   5 A  452  LEU SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY          
SEQRES   6 A  452  GLY LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA          
SEQRES   7 A  452  VAL ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY          
SEQRES   8 A  452  GLU GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER          
SEQRES   9 A  452  ALA GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU          
SEQRES  10 A  452  GLN ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO          
SEQRES  11 A  452  PRO SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY          
SEQRES  12 A  452  SER GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE          
SEQRES  13 A  452  ASN PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR          
SEQRES  14 A  452  SER GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN          
SEQRES  15 A  452  ILE ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO          
SEQRES  16 A  452  ASP SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU          
SEQRES  17 A  452  ASP ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU          
SEQRES  18 A  452  TYR THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER          
SEQRES  19 A  452  LEU THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA          
SEQRES  20 A  452  ARG LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR          
SEQRES  21 A  452  TYR PHE LEU GLN PHE ASN LYS PHE ARG VAL PRO THR PHE          
SEQRES  22 A  452  LEU SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP          
SEQRES  23 A  452  SER PHE SER LLP ILE ILE SER SER GLY LEU ARG ILE GLY          
SEQRES  24 A  452  PHE LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE          
SEQRES  25 A  452  LEU HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE          
SEQRES  26 A  452  ASN GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY          
SEQRES  27 A  452  GLU GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP          
SEQRES  28 A  452  PHE TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA          
SEQRES  29 A  452  ASP LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO          
SEQRES  30 A  452  ALA ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE          
SEQRES  31 A  452  ASN ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS          
SEQRES  32 A  452  MET GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL          
SEQRES  33 A  452  ASP SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE          
SEQRES  34 A  452  SER SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN          
SEQRES  35 A  452  VAL LEU ALA GLN LEU ILE LYS GLU SER LEU                      
MODRES 6T8Q LLP A  263  LYS  MODIFIED RESIDUE                                   
HET    LLP  A 263      24                                                       
HET    MVQ  A 501      32                                                       
HET     CD  A 502       1                                                       
HET     CD  A 503       1                                                       
HET     CD  A 504       1                                                       
HET     CD  A 505       1                                                       
HET     CD  A 506       1                                                       
HET     CD  A 507       1                                                       
HET     CD  A 508       1                                                       
HET     CD  A 509       2                                                       
HET     CL  A 510       1                                                       
HET    ACT  A 511       4                                                       
HETNAM     LLP (2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-                           
HETNAM   2 LLP  (PHOSPHONOOXYMETHYL)PYRIDIN-4-                                  
HETNAM   3 LLP  YL]METHYLIDENEAMINO]HEXANOIC ACID                               
HETNAM     MVQ (2~{R})-1-[6-METHYL-5-(OXAN-4-YL)-7-OXIDANYLIDENE-[1,            
HETNAM   2 MVQ  3]THIAZOLO[5,4-D]PYRIMIDIN-2-YL]-~{N}-(PHENYLMETHYL)            
HETNAM   3 MVQ  PYRROLIDINE-2-CARBOXAMIDE                                       
HETNAM      CD CADMIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ACT ACETATE ION                                                      
HETSYN     LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE                             
FORMUL   1  LLP    C14 H22 N3 O7 P                                              
FORMUL   2  MVQ    C23 H27 N5 O3 S                                              
FORMUL   3   CD    8(CD 2+)                                                     
FORMUL  11   CL    CL 1-                                                        
FORMUL  12  ACT    C2 H3 O2 1-                                                  
FORMUL  13  HOH   *157(H2 O)                                                    
HELIX    1 AA1 ASN A    2  ILE A    7  5                                   6    
HELIX    2 AA2 THR A    8  ARG A   14  1                                   7    
HELIX    3 AA3 SER A   17  ARG A   28  1                                  12    
HELIX    4 AA4 ASN A   42  PHE A   46  5                                   5    
HELIX    5 AA5 GLY A   64  LEU A   72  1                                   9    
HELIX    6 AA6 ILE A   80  ASN A   96  1                                  17    
HELIX    7 AA7 PRO A  103  GLY A  107  5                                   5    
HELIX    8 AA8 GLY A  116  ILE A  129  1                                  14    
HELIX    9 AA9 TYR A  142  HIS A  150  1                                   9    
HELIX   10 AB1 PRO A  151  GLY A  153  5                                   3    
HELIX   11 AB2 VAL A  167  SER A  176  1                                  10    
HELIX   12 AB3 ARG A  177  TRP A  178  5                                   2    
HELIX   13 AB4 LYS A  179  ASN A  189  5                                  11    
HELIX   14 AB5 THR A  209  TYR A  223  1                                  15    
HELIX   15 AB6 PHE A  246  ASP A  250  5                                   5    
HELIX   16 AB7 LYS A  278  SER A  291  1                                  14    
HELIX   17 AB8 SER A  296  THR A  342  1                                  47    
HELIX   18 AB9 ASP A  365  LYS A  373  1                                   9    
HELIX   19 AC1 ASN A  385  TYR A  388  5                                   4    
HELIX   20 AC2 SER A  406  GLU A  423  1                                  18    
SHEET    1 AA1 2 ALA A  51  ILE A  53  0                                        
SHEET    2 AA1 2 ILE A  61  PHE A  63 -1  O  PHE A  63   N  ALA A  51           
SHEET    1 AA2 5 MET A 109  THR A 114  0                                        
SHEET    2 AA2 5 GLY A 272  PRO A 277 -1  O  LEU A 274   N  CYS A 112           
SHEET    3 AA2 5 VAL A 255  SER A 260 -1  N  ARG A 257   O  THR A 275           
SHEET    4 AA2 5 LEU A 226  ASP A 230  1  N  GLU A 229   O  ALA A 258           
SHEET    5 AA2 5 PHE A 193  THR A 196  1  N  LEU A 194   O  ILE A 228           
SHEET    1 AA3 2 ASN A 134  LEU A 137  0                                        
SHEET    2 AA3 2 ASN A 155  ASN A 158  1  O  ILE A 157   N  VAL A 135           
SHEET    1 AA4 2 SER A 161  ASP A 162  0                                        
SHEET    2 AA4 2 GLY A 165  ILE A 166 -1  O  GLY A 165   N  ASP A 162           
SHEET    1 AA5 4 ALA A 345  TRP A 347  0                                        
SHEET    2 AA5 4 PHE A 355  VAL A 360 -1  O  LYS A 359   N  GLU A 346           
SHEET    3 AA5 4 TYR A 397  SER A 401 -1  O  ALA A 400   N  LEU A 356           
SHEET    4 AA5 4 LEU A 382  PRO A 383 -1  N  LEU A 382   O  ARG A 399           
LINK         OD1 ASP A 110                CD    CD A 508     1555   1555  2.46  
LINK         O   LEU A 149                CD    CD A 507     1555   1555  2.50  
LINK         O   CYS A 154                CD    CD A 507     1555   1555  2.55  
LINK         SG  CYS A 154                CD    CD A 507     1555   1555  2.55  
LINK         OD1 ASP A 169                CD    CD A 503     1555   1555  2.41  
LINK         OE1 GLU A 215                CD    CD A 503     1555   1555  2.62  
LINK         OE2 GLU A 215                CD    CD A 503     1555   1555  2.42  
LINK         OD1 ASP A 224                CD    CD A 504     1555   1555  2.45  
LINK         C   SER A 262                 N   LLP A 263     1555   1555  1.34  
LINK         C   LLP A 263                 N   ILE A 264     1555   1555  1.34  
LINK         OE1AGLU A 282                CD  A CD A 509     1555   1555  2.46  
LINK         OE1BGLU A 282                CD  B CD A 509     1555   1555  2.45  
LINK         OE2AGLU A 282                CD  A CD A 509     1555   1555  2.45  
LINK         NE2 HIS A 287                CD    CD A 502     1555   1555  2.35  
LINK         OD2 ASP A 320                CD    CD A 505     1555   1555  2.44  
LINK         OD2 ASP A 324                CD    CD A 505     1555   1555  2.43  
LINK        CD    CD A 504                 O   HOH A 679     1555   1555  2.45  
LINK         SG  CYS A 122                CD    CD A 502     1555  11654  2.56  
LINK         OE1 GLU A 126                CD    CD A 502     1555  11654  2.44  
LINK         OE2 GLU A 126                CD    CD A 502     1555  11654  2.46  
LINK         OD1 ASP A 169                CD    CD A 503     1555   8555  2.02  
LINK         OE1 GLU A 215                CD    CD A 503     1555   8555  2.40  
LINK        CD    CD A 502                 O   HOH A 702     1555  11654  2.43  
CISPEP   1 GLU A  139    PRO A  140          0         2.15                     
CISPEP   2 ASN A  202    PRO A  203          0        14.12                     
SITE     1 AC1 15 PRO A  18  ILE A  19  MET A  22  GLY A  38                    
SITE     2 AC1 15 GLY A  39  TYR A  74  SER A  75  PRO A  76                    
SITE     3 AC1 15 TYR A 142  SER A 143  ASN A 202  LLP A 263                    
SITE     4 AC1 15 LEU A 382  ARG A 399  HOH A 623                               
SITE     1 AC2  5 CYS A 122  GLU A 126  HIS A 287  HOH A 601                    
SITE     2 AC2  5 HOH A 702                                                     
SITE     1 AC3  3 ASP A 169  ARG A 172  GLU A 215                               
SITE     1 AC4  4 GLU A   0  MET A   1  ASP A 224  HOH A 679                    
SITE     1 AC5  2 ASP A 320  ASP A 324                                          
SITE     1 AC6  1 HIS A 348                                                     
SITE     1 AC7  2 LEU A 149  CYS A 154                                          
SITE     1 AC8  2 ASP A 110  HOH A 724                                          
SITE     1 AC9  1 GLU A 282                                                     
SITE     1 AD1  2 GLN A 119  LYS A 123                                          
SITE     1 AD2  7 SER A  35  GLY A  38  LEU A  40  SER A 401                    
SITE     2 AD2  7 SER A 403  SER A 404  HOH A 650                               
CRYST1  144.829  144.829  139.653  90.00  90.00 120.00 P 65 2 2     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006905  0.003986  0.000000        0.00000                         
SCALE2      0.000000  0.007973  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007161        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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