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Database: PDB
Entry: 6FTQ
LinkDB: 6FTQ
Original site: 6FTQ 
HEADER    HYDROLASE                               23-FEB-18   6FTQ              
TITLE     CRYSTAL STRUCTURE OF HUMAN BETA-UREIDOPROPIONASE (BETA-ALANINE        
TITLE    2 SYNTHASE) - MUTANT T299C                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-UREIDOPROPIONASE;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: BUP-1,BETA-ALANINE SYNTHASE,N-CARBAMOYL-BETA-ALANINE        
COMPND   5 AMIDOHYDROLASE;                                                      
COMPND   6 EC: 3.5.1.6;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: THE FIRST 6 AMINO ACIDS ARE A REMAINDER OF A CLEAVED  
COMPND  10 HIS-TAG C233 IS OXIDIZED TO CYSTEINE SULFINIC ACID T299 IS MUTATED TO
COMPND  11 CYSTEINE                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: UPB1, BUP1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: AI;                                       
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET151/D-TOPO                             
KEYWDS    PYRIMIDINE DEGRADATION, N-CARBAMYL-BETA-ALANINE AMIDOHYDROLASE, 5-    
KEYWDS   2 FLUOROURACIL METABOLIZING ENZYME, HYDROLASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.DOBRITZSCH,D.MAURER                                                 
REVDAT   1   21-NOV-18 6FTQ    0                                                
JRNL        AUTH   D.MAURER,B.LOHKAMP,M.KRUMPEL,M.WIDERSTEN,D.DOBRITZSCH        
JRNL        TITL   CRYSTAL STRUCTURE AND PH-DEPENDENT ALLOSTERIC REGULATION OF  
JRNL        TITL 2 HUMAN BETA-UREIDOPROPIONASE, AN ENZYME INVOLVED IN           
JRNL        TITL 3 ANTICANCER DRUG METABOLISM.                                  
JRNL        REF    BIOCHEM. J.                   V. 475  2395 2018              
JRNL        REFN                   ESSN 1470-8728                               
JRNL        PMID   29976570                                                     
JRNL        DOI    10.1042/BCJ20180222                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.08 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
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) : 2.08                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 26915                          
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1453                            
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) : 2.08                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1957                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.95                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 113                          
REMARK   3   BIN FREE R VALUE                    : 0.2530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2621                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 208                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.84000                                             
REMARK   3    B22 (A**2) : 2.32000                                              
REMARK   3    B33 (A**2) : -0.48000                                             
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): 0.159         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.137         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.095         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.925         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2711 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2474 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3682 ; 1.322 ; 1.940       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5725 ; 0.918 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   335 ; 6.273 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   133 ;34.189 ;23.233       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   441 ;11.340 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;16.153 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   399 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3042 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   586 ; 0.001 ; 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):  1331 ; 0.619 ; 1.707       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1330 ; 0.619 ; 1.707       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1660 ; 1.112 ; 2.553       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1661 ; 1.111 ; 2.553       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1380 ; 0.522 ; 1.786       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1377 ; 0.522 ; 1.787       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2018 ; 0.906 ; 2.658       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3033 ; 4.956 ;20.947       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2992 ; 4.853 ;20.386       
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  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    33        A    66                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.5870 -44.8228  -5.3623              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2118 T22:   0.1754                                     
REMARK   3      T33:   0.1389 T12:   0.0698                                     
REMARK   3      T13:  -0.0440 T23:   0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8689 L22:   5.4762                                     
REMARK   3      L33:   6.7811 L12:   1.7142                                     
REMARK   3      L13:  -2.7756 L23:  -2.2247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1699 S12:  -0.0628 S13:  -0.5977                       
REMARK   3      S21:  -0.1455 S22:  -0.1001 S23:  -0.5059                       
REMARK   3      S31:   0.4983 S32:   0.7323 S33:   0.2700                       
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    67        A   127                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.7884 -34.4195   0.2332              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1119 T22:   0.1279                                     
REMARK   3      T33:   0.0734 T12:  -0.0011                                     
REMARK   3      T13:   0.0107 T23:   0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8823 L22:   2.0126                                     
REMARK   3      L33:   2.4052 L12:  -0.1855                                     
REMARK   3      L13:  -0.9572 L23:  -0.1543                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0452 S12:  -0.1125 S13:  -0.2562                       
REMARK   3      S21:   0.1750 S22:   0.1036 S23:   0.3325                       
REMARK   3      S31:   0.1105 S32:  -0.2233 S33:  -0.0585                       
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   128        A   201                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.3890 -21.7487   0.4372              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1326 T22:   0.1852                                     
REMARK   3      T33:   0.0565 T12:   0.0127                                     
REMARK   3      T13:   0.0066 T23:  -0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1143 L22:   1.3175                                     
REMARK   3      L33:   1.5966 L12:  -0.0365                                     
REMARK   3      L13:  -0.6698 L23:   0.0253                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0575 S12:  -0.1985 S13:   0.3002                       
REMARK   3      S21:   0.0662 S22:   0.0845 S23:   0.1021                       
REMARK   3      S31:  -0.2858 S32:  -0.2525 S33:  -0.0270                       
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   212        A   356                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.7454 -30.5144 -13.7879              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0373 T22:   0.0887                                     
REMARK   3      T33:   0.0068 T12:   0.0006                                     
REMARK   3      T13:  -0.0033 T23:  -0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2316 L22:   2.9676                                     
REMARK   3      L33:   3.0501 L12:   0.0392                                     
REMARK   3      L13:   0.4059 L23:  -0.1841                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0125 S12:   0.0156 S13:  -0.0021                       
REMARK   3      S21:  -0.0153 S22:  -0.0026 S23:   0.1268                       
REMARK   3      S31:   0.0451 S32:  -0.0528 S33:   0.0151                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   357        A   384                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.8480 -11.7739 -33.9955              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4137 T22:   0.1892                                     
REMARK   3      T33:   0.2975 T12:  -0.0581                                     
REMARK   3      T13:  -0.0539 T23:   0.0396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4842 L22:   3.3669                                     
REMARK   3      L33:   6.0286 L12:   0.0649                                     
REMARK   3      L13:  -2.5886 L23:   2.0042                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1678 S12:   0.2385 S13:   0.1641                       
REMARK   3      S21:  -0.3700 S22:  -0.1568 S23:   0.4122                       
REMARK   3      S31:  -0.7864 S32:  -0.4156 S33:  -0.0110                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6FTQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200008904.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-SEP-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.75                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9762                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28448                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.080                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.630                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 13.40                              
REMARK 200  R MERGE                    (I) : 0.12600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.13                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.81400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2VHH                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% (W/V) PEG 3350 0.1 M HEPES PH 7.75   
REMARK 280  300 MM NASCN 3 MG/ML ENZYME VARIANT, VAPOR DIFFUSION, HANGING       
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.40400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.40400            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       43.40750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.12200            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       43.40750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.12200            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       51.40400            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       43.40750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       52.12200            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       51.40400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       43.40750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       52.12200            
REMARK 290   SMTRY3   8  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: 6170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 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        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -51.40400            
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      HOH A 527  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     GLY A    -5                                                      
REMARK 465     ILE A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     PHE A    -1                                                      
REMARK 465     THR A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     TRP A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     CYS A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     LYS A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     LEU A    19                                                      
REMARK 465     PRO A    20                                                      
REMARK 465     ASP A    21                                                      
REMARK 465     LEU A    22                                                      
REMARK 465     GLN A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     VAL A    25                                                      
REMARK 465     LYS A    26                                                      
REMARK 465     ARG A    27                                                      
REMARK 465     VAL A    28                                                      
REMARK 465     LEU A    29                                                      
REMARK 465     TYR A    30                                                      
REMARK 465     GLY A    31                                                      
REMARK 465     LYS A    32                                                      
REMARK 465     VAL A   202                                                      
REMARK 465     GLY A   203                                                      
REMARK 465     ASP A   204                                                      
REMARK 465     PHE A   205                                                      
REMARK 465     ASN A   206                                                      
REMARK 465     GLU A   207                                                      
REMARK 465     SER A   208                                                      
REMARK 465     THR A   209                                                      
REMARK 465     TYR A   210                                                      
REMARK 465     TYR A   211                                                      
REMARK 465     GLY A   301                                                      
REMARK 465     ASP A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     LYS A   304                                                      
REMARK 465     LYS A   305                                                      
REMARK 465     ALA A   306                                                      
REMARK 465     HIS A   307                                                      
REMARK 465     GLN A   308                                                      
REMARK 465     ASP A   309                                                      
REMARK 465     PHE A   310                                                      
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    ASP A 144       24.47   -151.37                                   
REMARK 500    CSD A 233     -123.76     57.61                                   
REMARK 500    SER A 324      -10.00     88.00                                   
REMARK 500    SER A 331      154.00    -48.61                                   
REMARK 500    VAL A 353      -63.24    -92.90                                   
REMARK 500    THR A 380       83.17    -67.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6FTQ A    1   384  UNP    Q9UBR1   BUP1_HUMAN       1    384             
SEQADV 6FTQ GLY A   -5  UNP  Q9UBR1              EXPRESSION TAG                 
SEQADV 6FTQ ILE A   -4  UNP  Q9UBR1              EXPRESSION TAG                 
SEQADV 6FTQ ASP A   -3  UNP  Q9UBR1              EXPRESSION TAG                 
SEQADV 6FTQ PRO A   -2  UNP  Q9UBR1              EXPRESSION TAG                 
SEQADV 6FTQ PHE A   -1  UNP  Q9UBR1              EXPRESSION TAG                 
SEQADV 6FTQ THR A    0  UNP  Q9UBR1              EXPRESSION TAG                 
SEQADV 6FTQ CYS A  299  UNP  Q9UBR1    THR   299 ENGINEERED MUTATION            
SEQRES   1 A  390  GLY ILE ASP PRO PHE THR MET ALA GLY ALA GLU TRP LYS          
SEQRES   2 A  390  SER LEU GLU GLU CYS LEU GLU LYS HIS LEU PRO LEU PRO          
SEQRES   3 A  390  ASP LEU GLN GLU VAL LYS ARG VAL LEU TYR GLY LYS GLU          
SEQRES   4 A  390  LEU ARG LYS LEU ASP LEU PRO ARG GLU ALA PHE GLU ALA          
SEQRES   5 A  390  ALA SER ARG GLU ASP PHE GLU LEU GLN GLY TYR ALA PHE          
SEQRES   6 A  390  GLU ALA ALA GLU GLU GLN LEU ARG ARG PRO ARG ILE VAL          
SEQRES   7 A  390  HIS VAL GLY LEU VAL GLN ASN ARG ILE PRO LEU PRO ALA          
SEQRES   8 A  390  ASN ALA PRO VAL ALA GLU GLN VAL SER ALA LEU HIS ARG          
SEQRES   9 A  390  ARG ILE LYS ALA ILE VAL GLU VAL ALA ALA MET CYS GLY          
SEQRES  10 A  390  VAL ASN ILE ILE CYS PHE GLN GLU ALA TRP THR MET PRO          
SEQRES  11 A  390  PHE ALA PHE CYS THR ARG GLU LYS LEU PRO TRP THR GLU          
SEQRES  12 A  390  PHE ALA GLU SER ALA GLU ASP GLY PRO THR THR ARG PHE          
SEQRES  13 A  390  CYS GLN LYS LEU ALA LYS ASN HIS ASP MET VAL VAL VAL          
SEQRES  14 A  390  SER PRO ILE LEU GLU ARG ASP SER GLU HIS GLY ASP VAL          
SEQRES  15 A  390  LEU TRP ASN THR ALA VAL VAL ILE SER ASN SER GLY ALA          
SEQRES  16 A  390  VAL LEU GLY LYS THR ARG LYS ASN HIS ILE PRO ARG VAL          
SEQRES  17 A  390  GLY ASP PHE ASN GLU SER THR TYR TYR MET GLU GLY ASN          
SEQRES  18 A  390  LEU GLY HIS PRO VAL PHE GLN THR GLN PHE GLY ARG ILE          
SEQRES  19 A  390  ALA VAL ASN ILE CSD TYR GLY ARG HIS HIS PRO LEU ASN          
SEQRES  20 A  390  TRP LEU MET TYR SER ILE ASN GLY ALA GLU ILE ILE PHE          
SEQRES  21 A  390  ASN PRO SER ALA THR ILE GLY ALA LEU SER GLU SER LEU          
SEQRES  22 A  390  TRP PRO ILE GLU ALA ARG ASN ALA ALA ILE ALA ASN HIS          
SEQRES  23 A  390  CYS PHE THR CYS ALA ILE ASN ARG VAL GLY THR GLU HIS          
SEQRES  24 A  390  PHE PRO ASN GLU PHE CYS SER GLY ASP GLY LYS LYS ALA          
SEQRES  25 A  390  HIS GLN ASP PHE GLY TYR PHE TYR GLY SER SER TYR VAL          
SEQRES  26 A  390  ALA ALA PRO ASP SER SER ARG THR PRO GLY LEU SER ARG          
SEQRES  27 A  390  SER ARG ASP GLY LEU LEU VAL ALA LYS LEU ASP LEU ASN          
SEQRES  28 A  390  LEU CYS GLN GLN VAL ASN ASP VAL TRP ASN PHE LYS MET          
SEQRES  29 A  390  THR GLY ARG TYR GLU MET TYR ALA ARG GLU LEU ALA GLU          
SEQRES  30 A  390  ALA VAL LYS SER ASN TYR SER PRO THR ILE VAL LYS GLU          
MODRES 6FTQ CSD A  233  CYS  MODIFIED RESIDUE                                   
HET    CSD  A 233       8                                                       
HETNAM     CSD 3-SULFINOALANINE                                                 
HETSYN     CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE                       
FORMUL   1  CSD    C3 H7 N O4 S                                                 
FORMUL   2  HOH   *208(H2 O)                                                    
HELIX    1 AA1 PRO A   40  GLU A   50  1                                  11    
HELIX    2 AA2 PRO A   88  CYS A  110  1                                  23    
HELIX    3 AA3 PRO A  134  ALA A  139  1                                   6    
HELIX    4 AA4 GLY A  145  ASP A  159  1                                  15    
HELIX    5 AA5 SER A  171  GLY A  174  5                                   4    
HELIX    6 AA6 ILE A  232  HIS A  237  5                                   6    
HELIX    7 AA7 HIS A  238  ASN A  248  1                                  11    
HELIX    8 AA8 GLY A  261  HIS A  280  1                                  20    
HELIX    9 AA9 PRO A  295  CYS A  299  5                                   5    
HELIX   10 AB1 ASN A  345  ASN A  351  1                                   7    
HELIX   11 AB2 ASN A  355  GLY A  360  1                                   6    
HELIX   12 AB3 ARG A  361  LYS A  374  1                                  14    
SHEET    1 AA1 8 ARG A  35  LYS A  36  0                                        
SHEET    2 AA1 8 GLU A  53  PHE A  59 -1  O  ALA A  58   N  ARG A  35           
SHEET    3 AA1 8 GLY A 336  ASP A 343  1  O  LYS A 341   N  PHE A  59           
SHEET    4 AA1 8 ILE A  71  GLN A  78 -1  N  VAL A  72   O  LEU A 342           
SHEET    5 AA1 8 ILE A 114  CYS A 116  1  O  ILE A 114   N  GLY A  75           
SHEET    6 AA1 8 VAL A 161  ARG A 169  1  O  VAL A 161   N  ILE A 115           
SHEET    7 AA1 8 LEU A 177  ILE A 184 -1  O  ILE A 184   N  VAL A 162           
SHEET    8 AA1 8 VAL A 190  ARG A 195 -1  O  THR A 194   N  ALA A 181           
SHEET    1 AA2 5 PHE A 221  THR A 223  0                                        
SHEET    2 AA2 5 GLY A 226  VAL A 230 -1  O  ILE A 228   N  PHE A 221           
SHEET    3 AA2 5 ILE A 252  SER A 257  1  O  PHE A 254   N  ALA A 229           
SHEET    4 AA2 5 PHE A 282  ASN A 287  1  O  CYS A 284   N  ASN A 255           
SHEET    5 AA2 5 TYR A 318  ALA A 320 -1  O  TYR A 318   N  ALA A 285           
SHEET    1 AA3 2 VAL A 289  GLY A 290  0                                        
SHEET    2 AA3 2 PHE A 313  TYR A 314 -1  O  PHE A 313   N  GLY A 290           
SSBOND   1 CYS A  128    CYS A  299                          1555   1555  2.04  
LINK         C   ILE A 232                 N   CSD A 233     1555   1555  1.34  
LINK         C   CSD A 233                 N   TYR A 234     1555   1555  1.34  
CISPEP   1 LEU A  133    PRO A  134          0         5.91                     
CRYST1   86.815  104.244  102.808  90.00  90.00  90.00 C 2 2 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      0.011519  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009593  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009727        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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