GenomeNet

Database: PDB
Entry: 6T8P
LinkDB: 6T8P
Original site: 6T8P 
HEADER    TRANSFERASE                             24-OCT-19   6T8P              
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, B;                                                         
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 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606                                                 
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 6T8P    1       JRNL                                     
REVDAT   2   11-MAR-20 6T8P    1       JRNL                                     
REVDAT   1   04-MAR-20 6T8P    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.    2.02 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) : 2.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 74.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 60258                          
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                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1816                            
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) : 2.02                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4392                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.24                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 132                          
REMARK   3   BIN FREE R VALUE                    : 0.3050                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6512                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 135                                     
REMARK   3   SOLVENT ATOMS            : 567                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.17                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.05000                                             
REMARK   3    B22 (A**2) : -0.23000                                             
REMARK   3    B33 (A**2) : 1.27000                                              
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): 0.178         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.160         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.134         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.706         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
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):  6852 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6485 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9329 ; 1.674 ; 1.993       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14961 ; 1.315 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   843 ; 6.910 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   281 ;40.977 ;24.733       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1116 ;13.223 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;19.259 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1013 ; 0.097 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7712 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1522 ; 0.002 ; 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):     2 ;74.875 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):     5 ;31.930 ; 5.000       
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  : 8                                          
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    -3        A    15                          
REMARK   3    RESIDUE RANGE :   A    75        A   325                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.7390  19.1080  12.9010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0150 T22:   0.0065                                     
REMARK   3      T33:   0.2394 T12:   0.0013                                     
REMARK   3      T13:   0.0032 T23:  -0.0148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7838 L22:   1.0060                                     
REMARK   3      L33:   0.7645 L12:   0.1209                                     
REMARK   3      L13:   0.2838 L23:   0.2236                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0323 S12:  -0.0085 S13:  -0.0014                       
REMARK   3      S21:   0.1124 S22:  -0.0043 S23:  -0.0771                       
REMARK   3      S31:   0.0603 S32:   0.0555 S33:  -0.0281                       
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):   2.3210  -7.8690  -6.8830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4446 T22:   0.4535                                     
REMARK   3      T33:   0.5137 T12:   0.1093                                     
REMARK   3      T13:   0.0893 T23:  -0.0295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9949 L22:   1.4241                                     
REMARK   3      L33:  11.4033 L12:   0.2225                                     
REMARK   3      L13:   7.2137 L23:  -0.8353                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0862 S12:   0.4559 S13:   0.0277                       
REMARK   3      S21:   0.3734 S22:  -0.2764 S23:  -0.2652                       
REMARK   3      S31:  -0.2507 S32:   0.9414 S33:   0.1902                       
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):  -7.2540  12.7760 -15.4620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2223 T22:   0.1299                                     
REMARK   3      T33:   0.2477 T12:  -0.0803                                     
REMARK   3      T13:   0.0156 T23:  -0.0163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4472 L22:   3.5067                                     
REMARK   3      L33:   3.2280 L12:  -1.7442                                     
REMARK   3      L13:   0.6748 L23:   0.9621                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1306 S12:   0.1795 S13:   0.2172                       
REMARK   3      S21:  -0.5584 S22:   0.0647 S23:  -0.4289                       
REMARK   3      S31:  -0.2018 S32:   0.3518 S33:  -0.1953                       
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   425                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0090  40.2020  17.9320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1385 T22:   0.1220                                     
REMARK   3      T33:   0.3950 T12:   0.0387                                     
REMARK   3      T13:   0.0265 T23:  -0.0661                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2472 L22:   3.1668                                     
REMARK   3      L33:   2.4372 L12:  -0.3357                                     
REMARK   3      L13:  -0.1852 L23:  -0.5198                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0184 S12:  -0.1764 S13:   0.1845                       
REMARK   3      S21:   0.2933 S22:   0.0223 S23:   0.4142                       
REMARK   3      S31:  -0.3467 S32:  -0.4258 S33:  -0.0039                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    -2        B    15                          
REMARK   3    RESIDUE RANGE :   B    75        B   325                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.0100  -3.2830   6.5210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0482 T22:   0.0060                                     
REMARK   3      T33:   0.2602 T12:  -0.0122                                     
REMARK   3      T13:  -0.0221 T23:   0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5735 L22:   1.0951                                     
REMARK   3      L33:   0.7872 L12:  -0.0139                                     
REMARK   3      L13:   0.1146 L23:  -0.5319                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0589 S12:  -0.0330 S13:  -0.1110                       
REMARK   3      S21:  -0.0450 S22:   0.0176 S23:   0.1202                       
REMARK   3      S31:   0.1577 S32:  -0.0557 S33:  -0.0764                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    16        B    40                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1530  25.2950   9.1800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2496 T22:   0.3559                                     
REMARK   3      T33:   0.6515 T12:   0.1020                                     
REMARK   3      T13:  -0.0149 T23:  -0.0633                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5769 L22:   0.1482                                     
REMARK   3      L33:   1.8618 L12:  -0.5636                                     
REMARK   3      L13:   2.1771 L23:  -0.4799                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1196 S12:  -0.1424 S13:  -0.0325                       
REMARK   3      S21:   0.0622 S22:   0.1190 S23:   0.0351                       
REMARK   3      S31:  -0.1729 S32:  -0.1272 S33:   0.0006                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    41        B    74                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.7000  22.9460  -9.7190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0523 T22:   0.0524                                     
REMARK   3      T33:   0.2775 T12:  -0.0120                                     
REMARK   3      T13:  -0.0347 T23:   0.0218                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4057 L22:   1.7634                                     
REMARK   3      L33:   2.9497 L12:   0.2137                                     
REMARK   3      L13:   0.1689 L23:   1.0280                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1004 S12:   0.1199 S13:   0.1716                       
REMARK   3      S21:  -0.2325 S22:  -0.0737 S23:   0.1769                       
REMARK   3      S31:  -0.2623 S32:  -0.1204 S33:   0.1742                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   326        B   425                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9130 -19.3360 -10.5540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4346 T22:   0.2084                                     
REMARK   3      T33:   0.5651 T12:   0.1854                                     
REMARK   3      T13:  -0.0153 T23:  -0.0829                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4848 L22:   1.6210                                     
REMARK   3      L33:   3.4992 L12:  -0.3838                                     
REMARK   3      L13:   0.4661 L23:  -0.5006                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2180 S12:   0.3481 S13:  -0.3901                       
REMARK   3      S21:  -0.3863 S22:  -0.1593 S23:  -0.4765                       
REMARK   3      S31:   0.7664 S32:   0.7404 S33:  -0.0588                       
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 6T8P 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_1292104155.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUL-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.000                            
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) : 0.99995                            
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   : 62074                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.020                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 74.450                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : 0.08500                            
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) : 2.02                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.469                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC 5.8.0155                                       
REMARK 200 STARTING MODEL: 5TF5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, AMMONIUM IODIDE, VAPOR         
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       43.52850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.13000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.46800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.13000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.52850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.46800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     THR A    23                                                      
REMARK 465     ASP A    24                                                      
REMARK 465     ILE A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     ARG A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     PRO A    30                                                      
REMARK 465     LYS A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     LYS A   367                                                      
REMARK 465     GLU A   368                                                      
REMARK 465     LEU A   369                                                      
REMARK 465     ILE A   370                                                      
REMARK 465     GLU A   371                                                      
REMARK 465     GLU A   372                                                      
REMARK 465     LYS A   373                                                      
REMARK 465     ALA A   374                                                      
REMARK 465     VAL A   375                                                      
REMARK 465     LYS A   376                                                      
REMARK 465     MET B   -26                                                      
REMARK 465     SER B   -25                                                      
REMARK 465     TYR B   -24                                                      
REMARK 465     TYR B   -23                                                      
REMARK 465     HIS B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     ASP B   -16                                                      
REMARK 465     TYR B   -15                                                      
REMARK 465     ASP B   -14                                                      
REMARK 465     ILE B   -13                                                      
REMARK 465     PRO B   -12                                                      
REMARK 465     THR B   -11                                                      
REMARK 465     THR B   -10                                                      
REMARK 465     GLU B    -9                                                      
REMARK 465     ASN B    -8                                                      
REMARK 465     LEU B    -7                                                      
REMARK 465     TYR B    -6                                                      
REMARK 465     PHE B    -5                                                      
REMARK 465     GLN B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     ARG B    20                                                      
REMARK 465     THR B    21                                                      
REMARK 465     MET B    22                                                      
REMARK 465     THR B    23                                                      
REMARK 465     ASP B    24                                                      
REMARK 465     ILE B    25                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     ARG B    28                                                      
REMARK 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     ARG A   20   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ILE A  100   CD1                                                 
REMARK 480     LYS A  361   CE   NZ                                             
REMARK 480     SER B   35   OG                                                  
REMARK 480     MET B   67   CE                                                  
REMARK 480     GLU B  313   CD   OE1  OE2                                       
REMARK 480     LYS B  367   CE   NZ                                             
REMARK 480     GLU B  368   CG   CD   OE1  OE2                                  
REMARK 480     GLU B  372   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  373   CG   CD   CE   NZ                                   
REMARK 480     LYS B  376   CG   CD   CE   NZ                                   
REMARK 480     LEU B  380   CD1  CD2                                            
REMARK 480     GLU B  408   CG   CD   OE1  OE2                                  
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 172   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 270   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 270   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B 270   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 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    ASN A  96       57.98     39.91                                   
REMARK 500    ILE A 265      -51.12   -120.47                                   
REMARK 500    SER A 266      133.58   -176.96                                   
REMARK 500    SER A 291      -95.07   -126.88                                   
REMARK 500    LEU A 293      -55.96     76.48                                   
REMARK 500    TYR B  74      155.24    -46.52                                   
REMARK 500    ASN B  96       63.19     31.30                                   
REMARK 500    ILE B 265      -50.92   -120.18                                   
REMARK 500    SER B 266      132.25   -175.98                                   
REMARK 500    SER B 291      -95.19   -118.10                                   
REMARK 500    LEU B 293      -53.79     72.61                                   
REMARK 500    SER B 404      -40.98   -132.09                                   
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 MVT A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MVT A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MVT A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MVT B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 507                 
DBREF  6T8P A    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  6T8P B    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
SEQADV 6T8P MET A  -26  UNP  Q8N5Z0              INITIATING METHIONINE          
SEQADV 6T8P SER A  -25  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P TYR A  -24  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P TYR A  -23  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P HIS A  -22  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P HIS A  -21  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P HIS A  -20  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P HIS A  -19  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P HIS A  -18  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P HIS A  -17  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P ASP A  -16  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P TYR A  -15  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P ASP A  -14  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P ILE A  -13  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P PRO A  -12  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P THR A  -11  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P THR A  -10  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P GLU A   -9  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P ASN A   -8  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P LEU A   -7  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P TYR A   -6  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P PHE A   -5  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P GLN A   -4  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P GLY A   -3  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P ALA A   -2  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P MET A   -1  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P GLU A    0  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P MET B  -26  UNP  Q8N5Z0              INITIATING METHIONINE          
SEQADV 6T8P SER B  -25  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P TYR B  -24  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P TYR B  -23  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P HIS B  -22  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P HIS B  -21  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P HIS B  -20  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P HIS B  -19  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P HIS B  -18  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P HIS B  -17  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P ASP B  -16  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P TYR B  -15  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P ASP B  -14  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P ILE B  -13  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P PRO B  -12  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P THR B  -11  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P THR B  -10  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P GLU B   -9  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P ASN B   -8  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P LEU B   -7  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P TYR B   -6  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P PHE B   -5  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P GLN B   -4  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P GLY B   -3  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P ALA B   -2  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P MET B   -1  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6T8P GLU B    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                      
SEQRES   1 B  452  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 B  452  ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET          
SEQRES   3 B  452  GLU MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA          
SEQRES   4 B  452  ALA ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE          
SEQRES   5 B  452  LEU SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY          
SEQRES   6 B  452  GLY LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA          
SEQRES   7 B  452  VAL ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY          
SEQRES   8 B  452  GLU GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER          
SEQRES   9 B  452  ALA GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU          
SEQRES  10 B  452  GLN ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO          
SEQRES  11 B  452  PRO SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY          
SEQRES  12 B  452  SER GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE          
SEQRES  13 B  452  ASN PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR          
SEQRES  14 B  452  SER GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN          
SEQRES  15 B  452  ILE ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO          
SEQRES  16 B  452  ASP SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU          
SEQRES  17 B  452  ASP ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU          
SEQRES  18 B  452  TYR THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER          
SEQRES  19 B  452  LEU THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA          
SEQRES  20 B  452  ARG LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR          
SEQRES  21 B  452  TYR PHE LEU GLN PHE ASN LYS PHE ARG VAL PRO THR PHE          
SEQRES  22 B  452  LEU SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP          
SEQRES  23 B  452  SER PHE SER LLP ILE ILE SER SER GLY LEU ARG ILE GLY          
SEQRES  24 B  452  PHE LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE          
SEQRES  25 B  452  LEU HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE          
SEQRES  26 B  452  ASN GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY          
SEQRES  27 B  452  GLU GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP          
SEQRES  28 B  452  PHE TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA          
SEQRES  29 B  452  ASP LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO          
SEQRES  30 B  452  ALA ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE          
SEQRES  31 B  452  ASN ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS          
SEQRES  32 B  452  MET GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL          
SEQRES  33 B  452  ASP SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE          
SEQRES  34 B  452  SER SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN          
SEQRES  35 B  452  VAL LEU ALA GLN LEU ILE LYS GLU SER LEU                      
MODRES 6T8P LLP A  263  LYS  MODIFIED RESIDUE                                   
MODRES 6T8P LLP B  263  LYS  MODIFIED RESIDUE                                   
HET    LLP  A 263      24                                                       
HET    LLP  B 263      24                                                       
HET    MVT  A 501      29                                                       
HET    MVT  A 502      29                                                       
HET    MVT  A 503      29                                                       
HET    IOD  A 504       1                                                       
HET    IOD  A 505       1                                                       
HET    IOD  A 506       1                                                       
HET    IOD  A 507       1                                                       
HET    MVT  B 501      29                                                       
HET    IOD  B 502       1                                                       
HET    IOD  B 503       1                                                       
HET    IOD  B 504       1                                                       
HET    EDO  B 505       4                                                       
HET    EDO  B 506       4                                                       
HET    EDO  B 507       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     MVT 3,5-BIS(FLUORANYL)-~{N}-[5-[(2~{R})-2-(3-FLUOROPHENYL)-          
HETNAM   2 MVT  3-METHYL-BUTYL]-1,3,4-THIADIAZOL-2-                             
HETNAM   3 MVT  YL]BENZENESULFONAMIDE                                           
HETNAM     IOD IODIDE ION                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  LLP    2(C14 H22 N3 O7 P)                                           
FORMUL   3  MVT    4(C19 H18 F3 N3 O2 S2)                                       
FORMUL   6  IOD    7(I 1-)                                                      
FORMUL  14  EDO    3(C2 H6 O2)                                                  
FORMUL  17  HOH   *567(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  MET A   22  5                                   6    
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  185  5                                   7    
HELIX   14 AB5 THR A  209  TYR A  223  1                                  15    
HELIX   15 AB6 TYR A  233  GLN A  237  5                                   5    
HELIX   16 AB7 PHE A  246  ASP A  250  5                                   5    
HELIX   17 AB8 LYS A  278  GLN A  289  1                                  12    
HELIX   18 AB9 SER A  296  LEU A  341  1                                  46    
HELIX   19 AC1 ASN A  385  TYR A  388  5                                   4    
HELIX   20 AC2 SER A  406  LEU A  425  1                                  20    
HELIX   21 AC3 ASN B    2  ILE B    7  5                                   6    
HELIX   22 AC4 THR B    8  ARG B   14  1                                   7    
HELIX   23 AC5 SER B   32  ALA B   37  1                                   6    
HELIX   24 AC6 ASN B   42  PHE B   46  5                                   5    
HELIX   25 AC7 GLY B   64  LEU B   72  1                                   9    
HELIX   26 AC8 ILE B   80  ASN B   96  1                                  17    
HELIX   27 AC9 PRO B  103  GLY B  107  5                                   5    
HELIX   28 AD1 GLY B  116  ILE B  129  1                                  14    
HELIX   29 AD2 TYR B  142  HIS B  150  1                                   9    
HELIX   30 AD3 PRO B  151  GLY B  153  5                                   3    
HELIX   31 AD4 VAL B  167  SER B  176  1                                  10    
HELIX   32 AD5 ARG B  177  TRP B  178  5                                   2    
HELIX   33 AD6 LYS B  179  ASN B  189  5                                  11    
HELIX   34 AD7 THR B  209  TYR B  223  1                                  15    
HELIX   35 AD8 TYR B  233  GLN B  237  5                                   5    
HELIX   36 AD9 PHE B  246  ASP B  250  5                                   5    
HELIX   37 AE1 LYS B  278  VAL B  290  1                                  13    
HELIX   38 AE2 SER B  296  THR B  342  1                                  47    
HELIX   39 AE3 VAL B  366  GLU B  372  1                                   7    
HELIX   40 AE4 GLU B  372  MET B  377  1                                   6    
HELIX   41 AE5 ASN B  385  TYR B  388  5                                   4    
HELIX   42 AE6 SER B  406  GLU B  423  1                                  18    
SHEET    1 AA1 2 ILE A  34  SER A  35  0                                        
SHEET    2 AA1 2 VAL B 379  LEU B 380  1  O  LEU B 380   N  ILE A  34           
SHEET    1 AA2 4 THR A  60  PHE A  63  0                                        
SHEET    2 AA2 4 PHE A  48  VAL A  55 -1  N  ILE A  53   O  ILE A  61           
SHEET    3 AA2 4 PHE B  48  VAL B  55 -1  O  LYS B  49   N  THR A  54           
SHEET    4 AA2 4 LYS B  59  PHE B  63 -1  O  PHE B  63   N  ALA B  51           
SHEET    1 AA3 7 MET A 109  THR A 114  0                                        
SHEET    2 AA3 7 GLY A 272  PRO A 277 -1  O  GLY A 276   N  ASP A 110           
SHEET    3 AA3 7 VAL A 255  SER A 260 -1  N  ARG A 257   O  THR A 275           
SHEET    4 AA3 7 LEU A 226  ASP A 230  1  N  GLU A 229   O  ALA A 258           
SHEET    5 AA3 7 PHE A 193  THR A 196  1  N  LEU A 194   O  ILE A 228           
SHEET    6 AA3 7 ASN A 134  LEU A 137  1  N  LEU A 136   O  TYR A 195           
SHEET    7 AA3 7 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  GLU A 346  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 MET A 381  PRO A 383 -1  N  LEU A 382   O  ARG A 399           
SHEET    1 AA6 7 MET B 109  THR B 114  0                                        
SHEET    2 AA6 7 GLY B 272  PRO B 277 -1  O  LEU B 274   N  CYS B 112           
SHEET    3 AA6 7 VAL B 255  SER B 260 -1  N  ARG B 257   O  THR B 275           
SHEET    4 AA6 7 LEU B 226  ASP B 230  1  N  ILE B 227   O  ILE B 256           
SHEET    5 AA6 7 PHE B 193  THR B 196  1  N  LEU B 194   O  ILE B 228           
SHEET    6 AA6 7 ASN B 134  LEU B 137  1  N  LEU B 136   O  TYR B 195           
SHEET    7 AA6 7 ASN B 155  ASN B 158  1  O  ILE B 157   N  VAL B 135           
SHEET    1 AA7 2 SER B 161  ASP B 162  0                                        
SHEET    2 AA7 2 GLY B 165  ILE B 166 -1  O  GLY B 165   N  ASP B 162           
SHEET    1 AA8 4 ALA B 345  GLU B 346  0                                        
SHEET    2 AA8 4 PHE B 355  VAL B 360 -1  O  LYS B 359   N  GLU B 346           
SHEET    3 AA8 4 TYR B 397  SER B 401 -1  O  ALA B 400   N  LEU B 356           
SHEET    4 AA8 4 LEU B 382  PRO B 383 -1  N  LEU B 382   O  ARG B 399           
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         C   SER B 262                 N   LLP B 263     1555   1555  1.34  
LINK         C   LLP B 263                 N   ILE B 264     1555   1555  1.33  
CISPEP   1 GLU A  139    PRO A  140          0         0.49                     
CISPEP   2 ASN A  202    PRO A  203          0        21.71                     
CISPEP   3 GLU B  139    PRO B  140          0         6.43                     
CISPEP   4 ASN B  202    PRO B  203          0        18.82                     
SITE     1 AC1 19 GLN A 118  TYR A 142  ASN A 202  LLP A 263                    
SITE     2 AC1 19 MET A 354  MET A 377  LEU A 380  ARG A 399                    
SITE     3 AC1 19 HOH A 625  HOH A 684  HOH A 771  ILE B  19                    
SITE     4 AC1 19 MET B  33  LEU B  36  LEU B  40  TYR B  74                    
SITE     5 AC1 19 LEU B 293  MVT B 501  HOH B 663                               
SITE     1 AC2 12 GLY A  38  GLY A  39  TYR A  74  SER A  75                    
SITE     2 AC2 12 LEU A 293  HOH A 786  GLN B 118  TYR B 142                    
SITE     3 AC2 12 ASN B 202  LLP B 263  MET B 354  ARG B 399                    
SITE     1 AC3 16 LEU A  90  LYS A  93  LEU A  94  GLN A 237                    
SITE     2 AC3 16 LYS A 240  ARG A 242  GLU A 312  MET A 316                    
SITE     3 AC3 16 VAL A 319  ASP A 320  HOH A 728  PRO B  81                    
SITE     4 AC3 16 GLU B  82  SER B  85  EDO B 507  HOH B 646                    
SITE     1 AC4  3 LYS A 123  GLN B 119  LYS B 123                               
SITE     1 AC5  1 SER A 304                                                     
SITE     1 AC6  2 TRP A  86  GLY B  29                                          
SITE     1 AC7  1 SER A  77                                                     
SITE     1 AC8 15 LYS A  93  MVT A 501  HOH A 714  SER B  17                    
SITE     2 AC8 15 ILE B  19  LYS B  31  SER B  32  MET B  33                    
SITE     3 AC8 15 TYR B  74  SER B  75  PRO B  76  SER B  77                    
SITE     4 AC8 15 GLN B 289  HOH B 666  HOH B 739                               
SITE     1 AC9  2 MET B  33  PRO B  81                                          
SITE     1 AD1  1 ARG B 321                                                     
SITE     1 AD2  2 HOH A 711  LYS B  59                                          
SITE     1 AD3  6 ASN A  44  MET A  45  GLU B  56  HIS B 318                    
SITE     2 AD3  6 ARG B 321  HOH B 667                                          
SITE     1 AD4  6 MET A 316  MVT A 503  SER B  85  HOH B 693                    
SITE     2 AD4  6 HOH B 736  HOH B 777                                          
CRYST1   87.057   96.936  116.260  90.00  90.00  90.00 P 21 21 21    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      0.011487  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010316  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008601        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system