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Database: PDB
Entry: 2Z0B
LinkDB: 2Z0B
Original site: 2Z0B 
HEADER    HYDROLASE                               07-MAY-07   2Z0B              
TITLE     CRYSTAL STRUCTURE OF CBM20 DOMAIN OF HUMAN PUTATIVE                   
TITLE    2 GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE 5 (KIAA1434)                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE 5;        
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: CBM20 DOMAIN;                                              
COMPND   5 SYNONYM: GDE5, KIAA1434;                                             
COMPND   6 EC: 3.1.-.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GDE5, KIAA1434;                                                
SOURCE   6 EXPRESSION_SYSTEM: CELL-FREE PROTEIN SYNTHESIS;                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PK051017-07                               
KEYWDS    GDE5, KIAA1434, CBM20 DOMAIN, STARCH-BINDING, HYDROLASE, STRUCTURAL   
KEYWDS   2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND         
KEYWDS   3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS            
KEYWDS   4 INITIATIVE, RSGI                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SAIJO,A.NISHINO,S.KISHISHITA,M.SHIROUZU,S.YOKOYAMA,RIKEN STRUCTURAL 
AUTHOR   2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)                                
REVDAT   3   13-JUL-11 2Z0B    1       VERSN                                    
REVDAT   2   24-FEB-09 2Z0B    1       VERSN                                    
REVDAT   1   06-MAY-08 2Z0B    0                                                
JRNL        AUTH   S.SAIJO,A.NISHINO,S.KISHISHITA,M.SHIROUZU,S.YOKOYAMA         
JRNL        TITL   CRYSTAL STRUCTURE OF CBM20 DOMAIN OF HUMAN PUTATIVE          
JRNL        TITL 2 GLYCEROPHOSPHODIESTER PHOSPHODIESTERASE 5 (KIAA1434)         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 62030                          
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) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3302                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2582                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 51.19                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 162                          
REMARK   3   BIN FREE R VALUE                    : 0.3220                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5132                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 448                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 10.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.54000                                              
REMARK   3    B22 (A**2) : 0.54000                                              
REMARK   3    B33 (A**2) : -0.80000                                             
REMARK   3    B12 (A**2) : 0.27000                                              
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): 0.175         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.154         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.110         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.127         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5308 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7220 ; 1.233 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   659 ; 4.169 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   226 ;29.833 ;24.336       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   847 ;11.578 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;13.216 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   799 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4007 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2176 ; 0.184 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3514 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   461 ; 0.181 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    52 ; 0.174 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.193 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3407 ; 0.552 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5334 ; 0.880 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2222 ; 1.049 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1880 ; 1.568 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
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     6        A   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.4030  57.1110   4.0950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1019 T22:   0.0383                                     
REMARK   3      T33:  -0.1025 T12:   0.0539                                     
REMARK   3      T13:   0.0182 T23:   0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6963 L22:   4.7796                                     
REMARK   3      L33:   5.2408 L12:  -1.8079                                     
REMARK   3      L13:   1.2533 L23:  -2.3274                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0761 S12:  -0.0925 S13:  -0.0835                       
REMARK   3      S21:   0.0359 S22:   0.1673 S23:   0.1908                       
REMARK   3      S31:   0.3168 S32:   0.2957 S33:  -0.2434                       
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 :   B     6        B   118                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.9010  48.3630 -25.2990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0137 T22:  -0.0516                                     
REMARK   3      T33:   0.1124 T12:  -0.0730                                     
REMARK   3      T13:  -0.0859 T23:  -0.0219                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9578 L22:   4.7749                                     
REMARK   3      L33:   4.0849 L12:  -1.3194                                     
REMARK   3      L13:   1.3472 L23:   0.6785                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0855 S12:   0.1493 S13:  -0.3894                       
REMARK   3      S21:  -0.1337 S22:  -0.1321 S23:   1.1496                       
REMARK   3      S31:   0.3371 S32:  -0.5028 S33:   0.0466                       
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 :   C     1        C   121                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.3710  37.3350 -13.5240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1115 T22:   0.0829                                     
REMARK   3      T33:  -0.1248 T12:  -0.0562                                     
REMARK   3      T13:   0.0244 T23:  -0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6515 L22:   1.5498                                     
REMARK   3      L33:   4.6720 L12:  -0.3491                                     
REMARK   3      L13:   1.0136 L23:  -0.1524                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0429 S12:   0.0088 S13:   0.1437                       
REMARK   3      S21:  -0.0359 S22:   0.0528 S23:   0.0292                       
REMARK   3      S31:  -0.3299 S32:   0.3049 S33:  -0.0099                       
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 :   D     4        D   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.5030  90.6460 -10.6880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0956 T22:   0.0744                                     
REMARK   3      T33:  -0.1371 T12:   0.0551                                     
REMARK   3      T13:  -0.0218 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3070 L22:   1.7369                                     
REMARK   3      L33:   5.1356 L12:   0.3645                                     
REMARK   3      L13:  -1.0426 L23:  -0.3606                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0641 S12:  -0.0056 S13:  -0.1346                       
REMARK   3      S21:   0.0271 S22:   0.0628 S23:   0.0410                       
REMARK   3      S31:   0.3580 S32:   0.3226 S33:   0.0013                       
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 :   E     8        E   119                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.1230  80.2020   0.9910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0302 T22:  -0.0662                                     
REMARK   3      T33:   0.0885 T12:   0.0723                                     
REMARK   3      T13:   0.0990 T23:  -0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1217 L22:   5.8521                                     
REMARK   3      L33:   4.2059 L12:   1.5249                                     
REMARK   3      L13:  -1.3795 L23:   0.8073                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0936 S12:  -0.1027 S13:   0.4412                       
REMARK   3      S21:   0.2120 S22:  -0.1171 S23:   1.2119                       
REMARK   3      S31:  -0.3998 S32:  -0.5018 S33:   0.0235                       
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 :   F     8        F   118                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.3220  70.9940 -28.4650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1035 T22:   0.0417                                     
REMARK   3      T33:  -0.1019 T12:  -0.0542                                     
REMARK   3      T13:  -0.0155 T23:   0.0091                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4741 L22:   4.5053                                     
REMARK   3      L33:   5.1056 L12:   1.6934                                     
REMARK   3      L13:  -1.0222 L23:  -2.4981                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0682 S12:   0.0720 S13:   0.0882                       
REMARK   3      S21:  -0.0152 S22:   0.1651 S23:   0.1833                       
REMARK   3      S31:  -0.2968 S32:   0.3071 S33:  -0.2333                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE STRUCTURE WAS REFINED ALSO WITH CNS   
REMARK   3  1.1                                                                 
REMARK   4                                                                      
REMARK   4 2Z0B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-AUG-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB027359.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL26B2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979270, 0.979740, 0.96400        
REMARK 200  MONOCHROMATOR                  : FIXED EXIT DOUBLE CRYSTAL          
REMARK 200                                   MONOCHROMETER                      
REMARK 200  OPTICS                         : RHODIUM COATED MIRROR              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 65368                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 50.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.28700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M SODIUM/POTASSIUM PHOSPHATE, PH      
REMARK 280  5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       25.79500            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       51.59000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9                               
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: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 7                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 8                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 9                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
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     GLY A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ILE A    84                                                      
REMARK 465     GLY A    85                                                      
REMARK 465     GLY A    86                                                      
REMARK 465     PRO A    87                                                      
REMARK 465     HIS A   121                                                      
REMARK 465     ASN A   122                                                      
REMARK 465     GLY A   123                                                      
REMARK 465     VAL A   124                                                      
REMARK 465     GLU A   125                                                      
REMARK 465     SER A   126                                                      
REMARK 465     GLY A   127                                                      
REMARK 465     PRO A   128                                                      
REMARK 465     SER A   129                                                      
REMARK 465     SER A   130                                                      
REMARK 465     GLY A   131                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     ASN B    49                                                      
REMARK 465     ASP B    50                                                      
REMARK 465     THR B    51                                                      
REMARK 465     GLY B    52                                                      
REMARK 465     GLU B    53                                                      
REMARK 465     LEU B    99                                                      
REMARK 465     GLN B   100                                                      
REMARK 465     ILE B   120                                                      
REMARK 465     HIS B   121                                                      
REMARK 465     ASN B   122                                                      
REMARK 465     GLY B   123                                                      
REMARK 465     VAL B   124                                                      
REMARK 465     GLU B   125                                                      
REMARK 465     SER B   126                                                      
REMARK 465     GLY B   127                                                      
REMARK 465     PRO B   128                                                      
REMARK 465     SER B   129                                                      
REMARK 465     SER B   130                                                      
REMARK 465     GLY B   131                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     THR C    51                                                      
REMARK 465     GLY C    52                                                      
REMARK 465     GLU C    53                                                      
REMARK 465     SER C    54                                                      
REMARK 465     ASN C   122                                                      
REMARK 465     GLY C   123                                                      
REMARK 465     VAL C   124                                                      
REMARK 465     GLU C   125                                                      
REMARK 465     SER C   126                                                      
REMARK 465     GLY C   127                                                      
REMARK 465     PRO C   128                                                      
REMARK 465     SER C   129                                                      
REMARK 465     SER C   130                                                      
REMARK 465     GLY C   131                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     GLU D    53                                                      
REMARK 465     HIS D   121                                                      
REMARK 465     ASN D   122                                                      
REMARK 465     GLY D   123                                                      
REMARK 465     VAL D   124                                                      
REMARK 465     GLU D   125                                                      
REMARK 465     SER D   126                                                      
REMARK 465     GLY D   127                                                      
REMARK 465     PRO D   128                                                      
REMARK 465     SER D   129                                                      
REMARK 465     SER D   130                                                      
REMARK 465     GLY D   131                                                      
REMARK 465     GLY E     1                                                      
REMARK 465     SER E     2                                                      
REMARK 465     SER E     3                                                      
REMARK 465     GLY E     4                                                      
REMARK 465     SER E     5                                                      
REMARK 465     SER E     6                                                      
REMARK 465     GLY E     7                                                      
REMARK 465     ASP E    50                                                      
REMARK 465     THR E    51                                                      
REMARK 465     GLY E    52                                                      
REMARK 465     GLU E    53                                                      
REMARK 465     LEU E    99                                                      
REMARK 465     GLN E   100                                                      
REMARK 465     ILE E   120                                                      
REMARK 465     HIS E   121                                                      
REMARK 465     ASN E   122                                                      
REMARK 465     GLY E   123                                                      
REMARK 465     VAL E   124                                                      
REMARK 465     GLU E   125                                                      
REMARK 465     SER E   126                                                      
REMARK 465     GLY E   127                                                      
REMARK 465     PRO E   128                                                      
REMARK 465     SER E   129                                                      
REMARK 465     SER E   130                                                      
REMARK 465     GLY E   131                                                      
REMARK 465     GLY F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     SER F     3                                                      
REMARK 465     GLY F     4                                                      
REMARK 465     SER F     5                                                      
REMARK 465     SER F     6                                                      
REMARK 465     GLY F     7                                                      
REMARK 465     ILE F    84                                                      
REMARK 465     GLY F    85                                                      
REMARK 465     GLY F    86                                                      
REMARK 465     PRO F    87                                                      
REMARK 465     GLY F   119                                                      
REMARK 465     ILE F   120                                                      
REMARK 465     HIS F   121                                                      
REMARK 465     ASN F   122                                                      
REMARK 465     GLY F   123                                                      
REMARK 465     VAL F   124                                                      
REMARK 465     GLU F   125                                                      
REMARK 465     SER F   126                                                      
REMARK 465     GLY F   127                                                      
REMARK 465     PRO F   128                                                      
REMARK 465     SER F   129                                                      
REMARK 465     SER F   130                                                      
REMARK 465     GLY F   131                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ILE C  84    CG1  CG2  CD1                                       
REMARK 470     HIS C 121    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE D  84    CG1  CG2  CD1                                       
REMARK 470     LYS E  58    CD   CE   NZ                                        
REMARK 470     GLN F 100    CD   OE1  NE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG D    72     O    HOH D   217              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A   8   C   -  N   -  CA  ANGL. DEV. =  10.1 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    PRO A   8      149.54    -28.46                                   
REMARK 500    THR A  97     -176.41    -58.70                                   
REMARK 500    HIS A  98       76.11    -50.28                                   
REMARK 500    SER C   2     -146.01    -74.26                                   
REMARK 500    ILE C 120       89.85     84.80                                   
REMARK 500    THR D  51       30.42   -160.42                                   
REMARK 500    MSE D  55       89.44     54.26                                   
REMARK 500    SER E  30       34.91    -86.43                                   
REMARK 500    HIS F  98       93.37    -67.71                                   
REMARK 500    GLN F 100      124.44     73.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 167        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH A 204        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH B 150        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH E 166        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH F 161        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH F 192        DISTANCE =  6.17 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 132                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 132                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: HSK002101406.2   RELATED DB: TARGETDB                    
DBREF  2Z0B A    8   125  UNP    Q9NPB8   GDE5_HUMAN       3    120             
DBREF  2Z0B B    8   125  UNP    Q9NPB8   GDE5_HUMAN       3    120             
DBREF  2Z0B C    8   125  UNP    Q9NPB8   GDE5_HUMAN       3    120             
DBREF  2Z0B D    8   125  UNP    Q9NPB8   GDE5_HUMAN       3    120             
DBREF  2Z0B E    8   125  UNP    Q9NPB8   GDE5_HUMAN       3    120             
DBREF  2Z0B F    8   125  UNP    Q9NPB8   GDE5_HUMAN       3    120             
SEQADV 2Z0B GLY A    1  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER A    2  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER A    3  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY A    4  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER A    5  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER A    6  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY A    7  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER A  126  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY A  127  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B PRO A  128  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER A  129  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER A  130  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY A  131  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY B    1  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER B    2  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER B    3  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY B    4  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER B    5  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER B    6  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY B    7  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER B  126  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY B  127  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B PRO B  128  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER B  129  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER B  130  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY B  131  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY C    1  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER C    2  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER C    3  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY C    4  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER C    5  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER C    6  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY C    7  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER C  126  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY C  127  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B PRO C  128  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER C  129  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER C  130  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY C  131  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY D    1  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER D    2  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER D    3  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY D    4  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER D    5  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER D    6  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY D    7  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER D  126  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY D  127  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B PRO D  128  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER D  129  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER D  130  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY D  131  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY E    1  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER E    2  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER E    3  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY E    4  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER E    5  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER E    6  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY E    7  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER E  126  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY E  127  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B PRO E  128  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER E  129  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER E  130  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY E  131  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY F    1  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER F    2  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER F    3  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY F    4  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER F    5  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER F    6  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY F    7  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER F  126  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY F  127  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B PRO F  128  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER F  129  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B SER F  130  UNP  Q9NPB8              EXPRESSION TAG                 
SEQADV 2Z0B GLY F  131  UNP  Q9NPB8              EXPRESSION TAG                 
SEQRES   1 A  131  GLY SER SER GLY SER SER GLY PRO SER GLN VAL ALA PHE          
SEQRES   2 A  131  GLU ILE ARG GLY THR LEU LEU PRO GLY GLU VAL PHE ALA          
SEQRES   3 A  131  ILE CYS GLY SER CYS ASP ALA LEU GLY ASN TRP ASN PRO          
SEQRES   4 A  131  GLN ASN ALA VAL ALA LEU LEU PRO GLU ASN ASP THR GLY          
SEQRES   5 A  131  GLU SER MSE LEU TRP LYS ALA THR ILE VAL LEU SER ARG          
SEQRES   6 A  131  GLY VAL SER VAL GLN TYR ARG TYR PHE LYS GLY TYR PHE          
SEQRES   7 A  131  LEU GLU PRO LYS THR ILE GLY GLY PRO CYS GLN VAL ILE          
SEQRES   8 A  131  VAL HIS LYS TRP GLU THR HIS LEU GLN PRO ARG SER ILE          
SEQRES   9 A  131  THR PRO LEU GLU SER GLU ILE ILE ILE ASP ASP GLY GLN          
SEQRES  10 A  131  PHE GLY ILE HIS ASN GLY VAL GLU SER GLY PRO SER SER          
SEQRES  11 A  131  GLY                                                          
SEQRES   1 B  131  GLY SER SER GLY SER SER GLY PRO SER GLN VAL ALA PHE          
SEQRES   2 B  131  GLU ILE ARG GLY THR LEU LEU PRO GLY GLU VAL PHE ALA          
SEQRES   3 B  131  ILE CYS GLY SER CYS ASP ALA LEU GLY ASN TRP ASN PRO          
SEQRES   4 B  131  GLN ASN ALA VAL ALA LEU LEU PRO GLU ASN ASP THR GLY          
SEQRES   5 B  131  GLU SER MSE LEU TRP LYS ALA THR ILE VAL LEU SER ARG          
SEQRES   6 B  131  GLY VAL SER VAL GLN TYR ARG TYR PHE LYS GLY TYR PHE          
SEQRES   7 B  131  LEU GLU PRO LYS THR ILE GLY GLY PRO CYS GLN VAL ILE          
SEQRES   8 B  131  VAL HIS LYS TRP GLU THR HIS LEU GLN PRO ARG SER ILE          
SEQRES   9 B  131  THR PRO LEU GLU SER GLU ILE ILE ILE ASP ASP GLY GLN          
SEQRES  10 B  131  PHE GLY ILE HIS ASN GLY VAL GLU SER GLY PRO SER SER          
SEQRES  11 B  131  GLY                                                          
SEQRES   1 C  131  GLY SER SER GLY SER SER GLY PRO SER GLN VAL ALA PHE          
SEQRES   2 C  131  GLU ILE ARG GLY THR LEU LEU PRO GLY GLU VAL PHE ALA          
SEQRES   3 C  131  ILE CYS GLY SER CYS ASP ALA LEU GLY ASN TRP ASN PRO          
SEQRES   4 C  131  GLN ASN ALA VAL ALA LEU LEU PRO GLU ASN ASP THR GLY          
SEQRES   5 C  131  GLU SER MSE LEU TRP LYS ALA THR ILE VAL LEU SER ARG          
SEQRES   6 C  131  GLY VAL SER VAL GLN TYR ARG TYR PHE LYS GLY TYR PHE          
SEQRES   7 C  131  LEU GLU PRO LYS THR ILE GLY GLY PRO CYS GLN VAL ILE          
SEQRES   8 C  131  VAL HIS LYS TRP GLU THR HIS LEU GLN PRO ARG SER ILE          
SEQRES   9 C  131  THR PRO LEU GLU SER GLU ILE ILE ILE ASP ASP GLY GLN          
SEQRES  10 C  131  PHE GLY ILE HIS ASN GLY VAL GLU SER GLY PRO SER SER          
SEQRES  11 C  131  GLY                                                          
SEQRES   1 D  131  GLY SER SER GLY SER SER GLY PRO SER GLN VAL ALA PHE          
SEQRES   2 D  131  GLU ILE ARG GLY THR LEU LEU PRO GLY GLU VAL PHE ALA          
SEQRES   3 D  131  ILE CYS GLY SER CYS ASP ALA LEU GLY ASN TRP ASN PRO          
SEQRES   4 D  131  GLN ASN ALA VAL ALA LEU LEU PRO GLU ASN ASP THR GLY          
SEQRES   5 D  131  GLU SER MSE LEU TRP LYS ALA THR ILE VAL LEU SER ARG          
SEQRES   6 D  131  GLY VAL SER VAL GLN TYR ARG TYR PHE LYS GLY TYR PHE          
SEQRES   7 D  131  LEU GLU PRO LYS THR ILE GLY GLY PRO CYS GLN VAL ILE          
SEQRES   8 D  131  VAL HIS LYS TRP GLU THR HIS LEU GLN PRO ARG SER ILE          
SEQRES   9 D  131  THR PRO LEU GLU SER GLU ILE ILE ILE ASP ASP GLY GLN          
SEQRES  10 D  131  PHE GLY ILE HIS ASN GLY VAL GLU SER GLY PRO SER SER          
SEQRES  11 D  131  GLY                                                          
SEQRES   1 E  131  GLY SER SER GLY SER SER GLY PRO SER GLN VAL ALA PHE          
SEQRES   2 E  131  GLU ILE ARG GLY THR LEU LEU PRO GLY GLU VAL PHE ALA          
SEQRES   3 E  131  ILE CYS GLY SER CYS ASP ALA LEU GLY ASN TRP ASN PRO          
SEQRES   4 E  131  GLN ASN ALA VAL ALA LEU LEU PRO GLU ASN ASP THR GLY          
SEQRES   5 E  131  GLU SER MSE LEU TRP LYS ALA THR ILE VAL LEU SER ARG          
SEQRES   6 E  131  GLY VAL SER VAL GLN TYR ARG TYR PHE LYS GLY TYR PHE          
SEQRES   7 E  131  LEU GLU PRO LYS THR ILE GLY GLY PRO CYS GLN VAL ILE          
SEQRES   8 E  131  VAL HIS LYS TRP GLU THR HIS LEU GLN PRO ARG SER ILE          
SEQRES   9 E  131  THR PRO LEU GLU SER GLU ILE ILE ILE ASP ASP GLY GLN          
SEQRES  10 E  131  PHE GLY ILE HIS ASN GLY VAL GLU SER GLY PRO SER SER          
SEQRES  11 E  131  GLY                                                          
SEQRES   1 F  131  GLY SER SER GLY SER SER GLY PRO SER GLN VAL ALA PHE          
SEQRES   2 F  131  GLU ILE ARG GLY THR LEU LEU PRO GLY GLU VAL PHE ALA          
SEQRES   3 F  131  ILE CYS GLY SER CYS ASP ALA LEU GLY ASN TRP ASN PRO          
SEQRES   4 F  131  GLN ASN ALA VAL ALA LEU LEU PRO GLU ASN ASP THR GLY          
SEQRES   5 F  131  GLU SER MSE LEU TRP LYS ALA THR ILE VAL LEU SER ARG          
SEQRES   6 F  131  GLY VAL SER VAL GLN TYR ARG TYR PHE LYS GLY TYR PHE          
SEQRES   7 F  131  LEU GLU PRO LYS THR ILE GLY GLY PRO CYS GLN VAL ILE          
SEQRES   8 F  131  VAL HIS LYS TRP GLU THR HIS LEU GLN PRO ARG SER ILE          
SEQRES   9 F  131  THR PRO LEU GLU SER GLU ILE ILE ILE ASP ASP GLY GLN          
SEQRES  10 F  131  PHE GLY ILE HIS ASN GLY VAL GLU SER GLY PRO SER SER          
SEQRES  11 F  131  GLY                                                          
MODRES 2Z0B MSE A   55  MET  SELENOMETHIONINE                                   
MODRES 2Z0B MSE B   55  MET  SELENOMETHIONINE                                   
MODRES 2Z0B MSE C   55  MET  SELENOMETHIONINE                                   
MODRES 2Z0B MSE D   55  MET  SELENOMETHIONINE                                   
MODRES 2Z0B MSE E   55  MET  SELENOMETHIONINE                                   
MODRES 2Z0B MSE F   55  MET  SELENOMETHIONINE                                   
HET    MSE  A  55       8                                                       
HET    MSE  B  55       8                                                       
HET    MSE  C  55       8                                                       
HET    MSE  D  55       8                                                       
HET    MSE  E  55       8                                                       
HET    MSE  F  55       8                                                       
HET    PO4  A 132       5                                                       
HET    PO4  F 132       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   1  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   7  PO4    2(O4 P 3-)                                                   
FORMUL   9  HOH   *448(H2 O)                                                    
HELIX    1   1 CYS A   31  GLY A   35  5                                   5    
HELIX    2   2 ASN A   38  ALA A   42  5                                   5    
HELIX    3   3 CYS B   31  GLY B   35  5                                   5    
HELIX    4   4 ASN B   38  ALA B   42  5                                   5    
HELIX    5   5 CYS C   31  GLY C   35  5                                   5    
HELIX    6   6 ASN C   38  ALA C   42  5                                   5    
HELIX    7   7 CYS D   31  GLY D   35  5                                   5    
HELIX    8   8 ASN D   38  ALA D   42  5                                   5    
HELIX    9   9 ASN E   38  ALA E   42  5                                   5    
HELIX   10  10 CYS F   31  GLY F   35  5                                   5    
HELIX   11  11 ASN F   38  ALA F   42  5                                   5    
SHEET    1   A 4 LEU A  46  PRO A  47  0                                        
SHEET    2   A 4 LEU A  56  LEU A  63 -1  O  LYS A  58   N  LEU A  46           
SHEET    3   A 4 SER A   9  ARG A  16 -1  N  SER A   9   O  LEU A  63           
SHEET    4   A 4 GLU A 110  GLN A 117  1  O  ILE A 113   N  ALA A  12           
SHEET    1   B 4 VAL A  43  ALA A  44  0                                        
SHEET    2   B 4 VAL A  24  GLY A  29 -1  N  ILE A  27   O  VAL A  43           
SHEET    3   B 4 VAL A  69  LEU A  79 -1  O  ARG A  72   N  CYS A  28           
SHEET    4   B 4 GLN A  89  TRP A  95 -1  O  GLN A  89   N  LEU A  79           
SHEET    1   C 4 VAL A  43  ALA A  44  0                                        
SHEET    2   C 4 VAL A  24  GLY A  29 -1  N  ILE A  27   O  VAL A  43           
SHEET    3   C 4 VAL A  69  LEU A  79 -1  O  ARG A  72   N  CYS A  28           
SHEET    4   C 4 ARG A 102  ILE A 104 -1  O  ILE A 104   N  VAL A  69           
SHEET    1   D 4 LEU B  46  PRO B  47  0                                        
SHEET    2   D 4 LEU B  56  SER B  64 -1  O  LYS B  58   N  LEU B  46           
SHEET    3   D 4 PRO B   8  ARG B  16 -1  N  VAL B  11   O  ILE B  61           
SHEET    4   D 4 GLU B 110  GLN B 117  1  O  ILE B 113   N  ALA B  12           
SHEET    1   E 4 VAL B  43  ALA B  44  0                                        
SHEET    2   E 4 VAL B  24  GLY B  29 -1  N  ILE B  27   O  VAL B  43           
SHEET    3   E 4 VAL B  69  LEU B  79 -1  O  PHE B  74   N  ALA B  26           
SHEET    4   E 4 GLN B  89  TRP B  95 -1  O  GLN B  89   N  LEU B  79           
SHEET    1   F 4 VAL B  43  ALA B  44  0                                        
SHEET    2   F 4 VAL B  24  GLY B  29 -1  N  ILE B  27   O  VAL B  43           
SHEET    3   F 4 VAL B  69  LEU B  79 -1  O  PHE B  74   N  ALA B  26           
SHEET    4   F 4 ARG B 102  ILE B 104 -1  O  ILE B 104   N  VAL B  69           
SHEET    1   G 4 LEU C  46  GLU C  48  0                                        
SHEET    2   G 4 LEU C  56  SER C  64 -1  O  LYS C  58   N  LEU C  46           
SHEET    3   G 4 PRO C   8  ARG C  16 -1  N  PHE C  13   O  ALA C  59           
SHEET    4   G 4 GLU C 110  GLN C 117  1  O  ILE C 113   N  ALA C  12           
SHEET    1   H 4 VAL C  43  ALA C  44  0                                        
SHEET    2   H 4 VAL C  24  GLY C  29 -1  N  ILE C  27   O  VAL C  43           
SHEET    3   H 4 VAL C  69  LEU C  79 -1  O  ARG C  72   N  CYS C  28           
SHEET    4   H 4 GLN C  89  TRP C  95 -1  O  GLN C  89   N  LEU C  79           
SHEET    1   I 4 VAL C  43  ALA C  44  0                                        
SHEET    2   I 4 VAL C  24  GLY C  29 -1  N  ILE C  27   O  VAL C  43           
SHEET    3   I 4 VAL C  69  LEU C  79 -1  O  ARG C  72   N  CYS C  28           
SHEET    4   I 4 ARG C 102  ILE C 104 -1  O  ARG C 102   N  TYR C  71           
SHEET    1   J 4 LEU D  46  GLU D  48  0                                        
SHEET    2   J 4 LEU D  56  SER D  64 -1  O  LEU D  56   N  GLU D  48           
SHEET    3   J 4 PRO D   8  ARG D  16 -1  N  VAL D  11   O  ILE D  61           
SHEET    4   J 4 GLU D 110  GLN D 117  1  O  ILE D 113   N  ALA D  12           
SHEET    1   K 4 VAL D  43  ALA D  44  0                                        
SHEET    2   K 4 VAL D  24  GLY D  29 -1  N  ILE D  27   O  VAL D  43           
SHEET    3   K 4 VAL D  69  LEU D  79 -1  O  ARG D  72   N  CYS D  28           
SHEET    4   K 4 GLN D  89  TRP D  95 -1  O  GLN D  89   N  LEU D  79           
SHEET    1   L 4 VAL D  43  ALA D  44  0                                        
SHEET    2   L 4 VAL D  24  GLY D  29 -1  N  ILE D  27   O  VAL D  43           
SHEET    3   L 4 VAL D  69  LEU D  79 -1  O  ARG D  72   N  CYS D  28           
SHEET    4   L 4 ARG D 102  ILE D 104 -1  O  ILE D 104   N  VAL D  69           
SHEET    1   M 4 LEU E  46  PRO E  47  0                                        
SHEET    2   M 4 MSE E  55  LEU E  63 -1  O  LYS E  58   N  LEU E  46           
SHEET    3   M 4 SER E   9  GLY E  17 -1  N  SER E   9   O  LEU E  63           
SHEET    4   M 4 GLU E 110  GLN E 117  1  O  ILE E 111   N  ALA E  12           
SHEET    1   N 4 VAL E  43  ALA E  44  0                                        
SHEET    2   N 4 VAL E  24  GLY E  29 -1  N  ILE E  27   O  VAL E  43           
SHEET    3   N 4 VAL E  69  LEU E  79 -1  O  PHE E  74   N  ALA E  26           
SHEET    4   N 4 GLN E  89  TRP E  95 -1  O  GLN E  89   N  LEU E  79           
SHEET    1   O 4 VAL E  43  ALA E  44  0                                        
SHEET    2   O 4 VAL E  24  GLY E  29 -1  N  ILE E  27   O  VAL E  43           
SHEET    3   O 4 VAL E  69  LEU E  79 -1  O  PHE E  74   N  ALA E  26           
SHEET    4   O 4 ARG E 102  ILE E 104 -1  O  ARG E 102   N  TYR E  71           
SHEET    1   P 4 LEU F  46  PRO F  47  0                                        
SHEET    2   P 4 LEU F  56  LEU F  63 -1  O  LYS F  58   N  LEU F  46           
SHEET    3   P 4 SER F   9  ARG F  16 -1  N  SER F   9   O  LEU F  63           
SHEET    4   P 4 GLU F 110  GLN F 117  1  O  ILE F 113   N  ALA F  12           
SHEET    1   Q 4 VAL F  43  ALA F  44  0                                        
SHEET    2   Q 4 VAL F  24  GLY F  29 -1  N  ILE F  27   O  VAL F  43           
SHEET    3   Q 4 VAL F  69  LEU F  79 -1  O  ARG F  72   N  CYS F  28           
SHEET    4   Q 4 GLN F  89  TRP F  95 -1  O  ILE F  91   N  TYR F  77           
SHEET    1   R 4 VAL F  43  ALA F  44  0                                        
SHEET    2   R 4 VAL F  24  GLY F  29 -1  N  ILE F  27   O  VAL F  43           
SHEET    3   R 4 VAL F  69  LEU F  79 -1  O  ARG F  72   N  CYS F  28           
SHEET    4   R 4 ARG F 102  ILE F 104 -1  O  ILE F 104   N  VAL F  69           
LINK         C   SER A  54                 N   MSE A  55     1555   1555  1.33  
LINK         C   MSE A  55                 N   LEU A  56     1555   1555  1.33  
LINK         C   SER B  54                 N   MSE B  55     1555   1555  1.33  
LINK         C   MSE B  55                 N   LEU B  56     1555   1555  1.33  
LINK         C   MSE C  55                 N   LEU C  56     1555   1555  1.33  
LINK         C   SER D  54                 N   MSE D  55     1555   1555  1.34  
LINK         C   MSE D  55                 N   LEU D  56     1555   1555  1.33  
LINK         C   SER E  54                 N   MSE E  55     1555   1555  1.33  
LINK         C   MSE E  55                 N   LEU E  56     1555   1555  1.33  
LINK         C   SER F  54                 N   MSE F  55     1555   1555  1.34  
LINK         C   MSE F  55                 N   LEU F  56     1555   1555  1.33  
SITE     1 AC1  8 THR A  18  LEU A  19  LEU A  20  GLU A  23                    
SITE     2 AC1  8 LYS A  75  HIS A  93  LYS A  94  HIS F  93                    
SITE     1 AC2  8 HIS A  93  THR F  18  LEU F  19  LEU F  20                    
SITE     2 AC2  8 GLU F  23  LYS F  75  HIS F  93  LYS F  94                    
CRYST1  111.040  111.040   77.385  90.00  90.00 120.00 P 31         18          
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      0.009006  0.005199  0.000000        0.00000                         
SCALE2      0.000000  0.010399  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012922        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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