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Database: PDB
Entry: 3UJ4
LinkDB: 3UJ4
Original site: 3UJ4 
HEADER    SIGNALING PROTEIN                       07-NOV-11   3UJ4              
TITLE     CRYSTAL STRUCTURE OF THE APO-INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR TYPE 1;              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: IP-3-R, IP3R 1, INSP3R1, TYPE 1 INOSITOL 1,4,5-TRISPHOSPHATE
COMPND   5 RECEPTOR, TYPE 1 INSP3 RECEPTOR;                                     
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;                                 
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: ITPR1, INSP3R;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3);                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-2                                 
KEYWDS    INOSITOL 1,4,5-TRISPHOSPHATE, APO-STATE, SUPPRESSOR DOMAIN, IP3-      
KEYWDS   2 BINDING CORE DOMAIN, SIGNALING PROTEIN                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.IKURA,M.D.SEO,N.ISHIYAMA,P.STATHOPULOS                              
REVDAT   2   09-JAN-13 3UJ4    1       JRNL                                     
REVDAT   1   15-FEB-12 3UJ4    0                                                
JRNL        AUTH   M.D.SEO,S.VELAMAKANNI,N.ISHIYAMA,P.B.STATHOPULOS,A.M.ROSSI,  
JRNL        AUTH 2 S.A.KHAN,P.DALE,C.LI,J.B.AMES,M.IKURA,C.W.TAYLOR             
JRNL        TITL   STRUCTURAL AND FUNCTIONAL CONSERVATION OF KEY DOMAINS IN     
JRNL        TITL 2 INSP3 AND RYANODINE RECEPTORS.                               
JRNL        REF    NATURE                        V. 483   108 2012              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   22286060                                                     
JRNL        DOI    10.1038/NATURE10751                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 34787                          
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) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1746                            
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2429                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.03                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 110                          
REMARK   3   BIN FREE R VALUE                    : 0.3190                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7421                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 28                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 87.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.18000                                              
REMARK   3    B22 (A**2) : -0.35000                                             
REMARK   3    B33 (A**2) : -1.19000                                             
REMARK   3    B12 (A**2) : -3.12000                                             
REMARK   3    B13 (A**2) : 1.93000                                              
REMARK   3    B23 (A**2) : 0.31000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.374         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.275         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.007        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7569 ; 0.007 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10288 ; 1.125 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   960 ; 5.862 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   326 ;35.582 ;24.509       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1199 ;18.362 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;16.455 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1194 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5694 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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     7        A   228                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.2090 -24.2820  31.1020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0105 T22:   0.1434                                     
REMARK   3      T33:   0.2347 T12:  -0.0209                                     
REMARK   3      T13:   0.0332 T23:  -0.0230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1982 L22:   3.8670                                     
REMARK   3      L33:   3.0196 L12:   0.2078                                     
REMARK   3      L13:  -0.5075 L23:  -1.4766                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0630 S12:   0.2858 S13:   0.2231                       
REMARK   3      S21:  -0.0650 S22:  -0.1145 S23:  -0.2599                       
REMARK   3      S31:  -0.0098 S32:   0.1292 S33:   0.0515                       
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   229        A   435                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.9970  -9.5810  19.0810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0543 T22:   0.3840                                     
REMARK   3      T33:   0.3642 T12:   0.0469                                     
REMARK   3      T13:   0.0420 T23:   0.0628                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6887 L22:   4.7277                                     
REMARK   3      L33:   4.3832 L12:  -0.2515                                     
REMARK   3      L13:   0.1399 L23:  -0.1270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1507 S12:   0.7847 S13:   0.3045                       
REMARK   3      S21:  -0.4089 S22:   0.0317 S23:   0.1666                       
REMARK   3      S31:  -0.1861 S32:  -0.1657 S33:  -0.1824                       
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   436        A   577                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1920 -15.0480   2.6290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4455 T22:   0.9482                                     
REMARK   3      T33:   0.2603 T12:   0.0899                                     
REMARK   3      T13:   0.1757 T23:   0.0953                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3298 L22:  10.9144                                     
REMARK   3      L33:  16.1531 L12:  -0.1975                                     
REMARK   3      L13:  -4.6379 L23:  -5.6204                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0041 S12:   0.6228 S13:   0.1094                       
REMARK   3      S21:  -1.6068 S22:  -0.4117 S23:  -0.8886                       
REMARK   3      S31:   0.1852 S32:   1.6545 S33:   0.4076                       
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 :   B     7        B   228                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.9890 -49.8180  49.5070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2413 T22:   0.1886                                     
REMARK   3      T33:   0.3361 T12:  -0.0174                                     
REMARK   3      T13:   0.0041 T23:   0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1856 L22:   6.9153                                     
REMARK   3      L33:   5.1915 L12:   0.5729                                     
REMARK   3      L13:   0.3413 L23:  -2.9012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1168 S12:  -0.2938 S13:  -0.2812                       
REMARK   3      S21:   0.2226 S22:  -0.4055 S23:  -0.8066                       
REMARK   3      S31:   0.6361 S32:   0.4471 S33:   0.2887                       
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 :   B   229        B   435                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.4050 -75.5090  48.9910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1563 T22:   0.1368                                     
REMARK   3      T33:   0.4091 T12:  -0.0722                                     
REMARK   3      T13:   0.0920 T23:  -0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4695 L22:   6.3631                                     
REMARK   3      L33:   6.7130 L12:   1.3024                                     
REMARK   3      L13:   0.0785 L23:   0.5506                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1619 S12:  -0.2863 S13:  -0.0935                       
REMARK   3      S21:   0.6586 S22:  -0.1702 S23:   0.4420                       
REMARK   3      S31:   0.2560 S32:  -0.2234 S33:   0.0083                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   436        B   577                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.4160 -61.4310  74.8740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0676 T22:   1.1387                                     
REMARK   3      T33:   0.3211 T12:   0.0084                                     
REMARK   3      T13:   0.1121 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2395 L22:   7.5484                                     
REMARK   3      L33:   9.8415 L12:   2.1012                                     
REMARK   3      L13:   1.3186 L23:  -2.7012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1983 S12:  -0.4455 S13:  -0.0009                       
REMARK   3      S21:   1.1262 S22:  -0.2624 S23:  -0.1359                       
REMARK   3      S31:  -0.2717 S32:   0.2305 S33:   0.0641                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 3UJ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB068819.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 133458                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
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     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, (NH4)2SO4),                 
REMARK 280  TRIMETHYLAMINE N-OXIDE, PH 8.4, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     MET A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     PRO A    78                                                      
REMARK 465     GLY A    79                                                      
REMARK 465     ALA A    80                                                      
REMARK 465     ASN A    81                                                      
REMARK 465     SER A    82                                                      
REMARK 465     THR A    83                                                      
REMARK 465     THR A    84                                                      
REMARK 465     ARG A   269                                                      
REMARK 465     GLN A   270                                                      
REMARK 465     PRO A   320                                                      
REMARK 465     ASP A   321                                                      
REMARK 465     PHE A   322                                                      
REMARK 465     GLU A   323                                                      
REMARK 465     GLU A   324                                                      
REMARK 465     GLU A   325                                                      
REMARK 465     ALA A   326                                                      
REMARK 465     LEU A   327                                                      
REMARK 465     GLU A   328                                                      
REMARK 465     PHE A   329                                                      
REMARK 465     GLN A   330                                                      
REMARK 465     PRO A   331                                                      
REMARK 465     SER A   332                                                      
REMARK 465     VAL A   333                                                      
REMARK 465     ASP A   334                                                      
REMARK 465     PRO A   335                                                      
REMARK 465     ASP A   336                                                      
REMARK 465     GLN A   337                                                      
REMARK 465     ASP A   338                                                      
REMARK 465     ALA A   339                                                      
REMARK 465     SER A   340                                                      
REMARK 465     ARG A   341                                                      
REMARK 465     SER A   342                                                      
REMARK 465     ARG A   343                                                      
REMARK 465     LEU A   344                                                      
REMARK 465     ARG A   345                                                      
REMARK 465     ASN A   346                                                      
REMARK 465     ALA A   347                                                      
REMARK 465     GLN A   348                                                      
REMARK 465     GLU A   349                                                      
REMARK 465     LYS A   350                                                      
REMARK 465     MET A   351                                                      
REMARK 465     ASP A   426                                                      
REMARK 465     LYS A   427                                                      
REMARK 465     GLY A   486                                                      
REMARK 465     GLY A   487                                                      
REMARK 465     THR A   488                                                      
REMARK 465     ASN A   489                                                      
REMARK 465     SER A   490                                                      
REMARK 465     GLY A   491                                                      
REMARK 465     GLN A   492                                                      
REMARK 465     ASP A   493                                                      
REMARK 465     VAL A   494                                                      
REMARK 465     LEU A   495                                                      
REMARK 465     GLU A   496                                                      
REMARK 465     VAL A   497                                                      
REMARK 465     VAL A   498                                                      
REMARK 465     PHE A   499                                                      
REMARK 465     SER A   500                                                      
REMARK 465     ALA A   525                                                      
REMARK 465     PRO A   526                                                      
REMARK 465     PHE A   527                                                      
REMARK 465     THR A   528                                                      
REMARK 465     ASP A   529                                                      
REMARK 465     ALA A   530                                                      
REMARK 465     GLY A   531                                                      
REMARK 465     ASP A   532                                                      
REMARK 465     GLY A   533                                                      
REMARK 465     PRO A   534                                                      
REMARK 465     MET A   535                                                      
REMARK 465     LEU A   536                                                      
REMARK 465     ARG A   537                                                      
REMARK 465     LEU A   538                                                      
REMARK 465     GLU A   539                                                      
REMARK 465     GLU A   540                                                      
REMARK 465     LEU A   541                                                      
REMARK 465     GLY A   542                                                      
REMARK 465     ASP A   543                                                      
REMARK 465     GLN A   544                                                      
REMARK 465     ARG A   545                                                      
REMARK 465     HIS A   546                                                      
REMARK 465     ALA A   547                                                      
REMARK 465     PRO A   548                                                      
REMARK 465     PHE A   549                                                      
REMARK 465     ARG A   550                                                      
REMARK 465     PHE A   578                                                      
REMARK 465     GLY A   579                                                      
REMARK 465     PHE A   580                                                      
REMARK 465     MET A   581                                                      
REMARK 465     GLN A   582                                                      
REMARK 465     LYS A   583                                                      
REMARK 465     GLN A   584                                                      
REMARK 465     ILE A   585                                                      
REMARK 465     GLY A   586                                                      
REMARK 465     TYR A   587                                                      
REMARK 465     ASP A   588                                                      
REMARK 465     VAL A   589                                                      
REMARK 465     LEU A   590                                                      
REMARK 465     ALA A   591                                                      
REMARK 465     GLU A   592                                                      
REMARK 465     ASP A   593                                                      
REMARK 465     THR A   594                                                      
REMARK 465     ILE A   595                                                      
REMARK 465     THR A   596                                                      
REMARK 465     ALA A   597                                                      
REMARK 465     LEU A   598                                                      
REMARK 465     LEU A   599                                                      
REMARK 465     HIS A   600                                                      
REMARK 465     ASN A   601                                                      
REMARK 465     ASN A   602                                                      
REMARK 465     ARG A   603                                                      
REMARK 465     LYS A   604                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     MET B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     LYS B    77                                                      
REMARK 465     PRO B    78                                                      
REMARK 465     GLY B    79                                                      
REMARK 465     ALA B    80                                                      
REMARK 465     ASN B    81                                                      
REMARK 465     SER B    82                                                      
REMARK 465     THR B    83                                                      
REMARK 465     GLY B   268                                                      
REMARK 465     ARG B   269                                                      
REMARK 465     GLN B   270                                                      
REMARK 465     ASP B   321                                                      
REMARK 465     PHE B   322                                                      
REMARK 465     GLU B   323                                                      
REMARK 465     GLU B   324                                                      
REMARK 465     GLU B   325                                                      
REMARK 465     ALA B   326                                                      
REMARK 465     LEU B   327                                                      
REMARK 465     GLU B   328                                                      
REMARK 465     PHE B   329                                                      
REMARK 465     GLN B   330                                                      
REMARK 465     PRO B   331                                                      
REMARK 465     SER B   332                                                      
REMARK 465     VAL B   333                                                      
REMARK 465     ASP B   334                                                      
REMARK 465     PRO B   335                                                      
REMARK 465     ASP B   336                                                      
REMARK 465     GLN B   337                                                      
REMARK 465     ASP B   338                                                      
REMARK 465     ALA B   339                                                      
REMARK 465     SER B   340                                                      
REMARK 465     ARG B   341                                                      
REMARK 465     SER B   342                                                      
REMARK 465     ARG B   343                                                      
REMARK 465     LEU B   344                                                      
REMARK 465     ARG B   345                                                      
REMARK 465     ASN B   346                                                      
REMARK 465     ALA B   347                                                      
REMARK 465     GLN B   348                                                      
REMARK 465     GLU B   349                                                      
REMARK 465     LYS B   350                                                      
REMARK 465     MET B   351                                                      
REMARK 465     LEU B   375                                                      
REMARK 465     GLU B   411                                                      
REMARK 465     GLY B   486                                                      
REMARK 465     GLY B   487                                                      
REMARK 465     THR B   488                                                      
REMARK 465     ASN B   489                                                      
REMARK 465     SER B   490                                                      
REMARK 465     GLY B   491                                                      
REMARK 465     GLN B   492                                                      
REMARK 465     ASP B   493                                                      
REMARK 465     VAL B   494                                                      
REMARK 465     LEU B   495                                                      
REMARK 465     GLU B   496                                                      
REMARK 465     VAL B   497                                                      
REMARK 465     VAL B   498                                                      
REMARK 465     LEU B   523                                                      
REMARK 465     GLN B   524                                                      
REMARK 465     ALA B   525                                                      
REMARK 465     PRO B   526                                                      
REMARK 465     PHE B   527                                                      
REMARK 465     THR B   528                                                      
REMARK 465     ASP B   529                                                      
REMARK 465     ALA B   530                                                      
REMARK 465     GLY B   531                                                      
REMARK 465     ASP B   532                                                      
REMARK 465     GLY B   533                                                      
REMARK 465     PRO B   534                                                      
REMARK 465     MET B   535                                                      
REMARK 465     LEU B   536                                                      
REMARK 465     ARG B   537                                                      
REMARK 465     LEU B   538                                                      
REMARK 465     GLU B   539                                                      
REMARK 465     GLU B   540                                                      
REMARK 465     LEU B   541                                                      
REMARK 465     GLY B   542                                                      
REMARK 465     ASP B   543                                                      
REMARK 465     GLN B   544                                                      
REMARK 465     ARG B   545                                                      
REMARK 465     HIS B   546                                                      
REMARK 465     ALA B   547                                                      
REMARK 465     PRO B   548                                                      
REMARK 465     PHE B   549                                                      
REMARK 465     ARG B   550                                                      
REMARK 465     HIS B   562                                                      
REMARK 465     GLN B   582                                                      
REMARK 465     LYS B   583                                                      
REMARK 465     GLN B   584                                                      
REMARK 465     ILE B   585                                                      
REMARK 465     GLY B   586                                                      
REMARK 465     TYR B   587                                                      
REMARK 465     ASP B   588                                                      
REMARK 465     VAL B   589                                                      
REMARK 465     LEU B   590                                                      
REMARK 465     ALA B   591                                                      
REMARK 465     GLU B   592                                                      
REMARK 465     ASP B   593                                                      
REMARK 465     THR B   594                                                      
REMARK 465     ILE B   595                                                      
REMARK 465     THR B   596                                                      
REMARK 465     ALA B   597                                                      
REMARK 465     LEU B   598                                                      
REMARK 465     LEU B   599                                                      
REMARK 465     HIS B   600                                                      
REMARK 465     ASN B   601                                                      
REMARK 465     ASN B   602                                                      
REMARK 465     ARG B   603                                                      
REMARK 465     LYS B   604                                                      
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     LYS A  52    CG   CD   CE   NZ                                   
REMARK 470     LYS A  70    CG   CD   CE   NZ                                   
REMARK 470     ASP A  85    CG   OD1  OD2                                       
REMARK 470     ASP A  97    CG   OD1  OD2                                       
REMARK 470     LYS A 101    CG   CD   CE   NZ                                   
REMARK 470     GLU A 104    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 136    CG   CD   CE   NZ                                   
REMARK 470     ARG A 137    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 144    CG   CD   CE   NZ                                   
REMARK 470     ASN A 145    CG   OD1  ND2                                       
REMARK 470     GLU A 157    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 213    CG   OD1  ND2                                       
REMARK 470     ASP A 231    CG   OD1  OD2                                       
REMARK 470     GLU A 246    CG   CD   OE1  OE2                                  
REMARK 470     SER A 271    OG                                                  
REMARK 470     SER A 274    OG                                                  
REMARK 470     GLU A 285    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 376    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 425    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 444    CG   OD1  OD2                                       
REMARK 470     GLU A 461    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 467    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 468    CG   OD1  ND2                                       
REMARK 470     ARG A 470    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 471    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 501    CG   CD   CE   NZ                                   
REMARK 470     LYS A 517    CG   CD   CE   NZ                                   
REMARK 470     LYS A 521    CG   CD   CE   NZ                                   
REMARK 470     ARG A 554    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A 557    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 558    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 561    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 565    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 566    CG   OD1  OD2                                       
REMARK 470     LYS A 569    CG   CD   CE   NZ                                   
REMARK 470     LYS A 576    CG   CD   CE   NZ                                   
REMARK 470     ARG B  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  51    CG   CD   CE   NZ                                   
REMARK 470     LYS B  52    CG   CD   CE   NZ                                   
REMARK 470     LYS B  70    CG   CD   CE   NZ                                   
REMARK 470     ASP B  85    CG   OD1  OD2                                       
REMARK 470     LYS B 100    CG   CD   CE   NZ                                   
REMARK 470     LYS B 101    CG   CD   CE   NZ                                   
REMARK 470     GLU B 104    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 135    CG   OD1  ND2                                       
REMARK 470     LYS B 136    CG   CD   CE   NZ                                   
REMARK 470     ARG B 137    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 144    CG   CD   CE   NZ                                   
REMARK 470     ASN B 188    CG   OD1  ND2                                       
REMARK 470     ASN B 213    CG   OD1  ND2                                       
REMARK 470     GLU B 246    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 257    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 258    CG   CD   CE   NZ                                   
REMARK 470     LYS B 259    CG   CD   CE   NZ                                   
REMARK 470     GLU B 285    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 379    CG   OD1  OD2                                       
REMARK 470     ARG B 384    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 408    CG   CD   CE   NZ                                   
REMARK 470     LYS B 412    CG   CD   CE   NZ                                   
REMARK 470     LYS B 417    CG   CD   CE   NZ                                   
REMARK 470     LYS B 424    CG   CD   CE   NZ                                   
REMARK 470     GLU B 428    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 451    CG   CD   CE   NZ                                   
REMARK 470     ILE B 456    CG1  CG2  CD1                                       
REMARK 470     LYS B 459    CG   CD   CE   NZ                                   
REMARK 470     GLU B 461    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 468    CG   OD1  ND2                                       
REMARK 470     ARG B 470    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 471    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 474    OG1  CG2                                            
REMARK 470     GLU B 478    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 479    CG   OD1  OD2                                       
REMARK 470     PHE B 499    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN B 514    CG   OD1  ND2                                       
REMARK 470     LYS B 521    CG   CD   CE   NZ                                   
REMARK 470     ARG B 554    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 555    CG   CD1  CD2                                       
REMARK 470     TYR B 557    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG B 558    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 561    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B 578    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE B 580    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET B 581    CG   SD   CE                                        
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    LYS A  52       48.02    -81.09                                   
REMARK 500    ALA A  75       43.27    -90.72                                   
REMARK 500    ASN A 129       37.10     71.37                                   
REMARK 500    LYS A 144      -70.39    -43.44                                   
REMARK 500    ASN A 156     -166.23   -166.82                                   
REMARK 500    PRO A 192      150.59    -49.17                                   
REMARK 500    PHE A 223      -71.41    -85.51                                   
REMARK 500    LYS A 412       71.48     61.87                                   
REMARK 500    ASN A 468        0.67    -66.25                                   
REMARK 500    ASP B  45     -168.86   -100.97                                   
REMARK 500    ASN B 156     -154.38   -152.98                                   
REMARK 500    PRO B 204      -75.23    -45.51                                   
REMARK 500    ASN B 213       98.64    -64.61                                   
REMARK 500    ASN B 215       79.71    -68.04                                   
REMARK 500    ASP B 232       32.17    -94.61                                   
REMARK 500    THR B 266      102.51    -54.07                                   
REMARK 500    ASN B 385       59.88     36.97                                   
REMARK 500    GLU B 425      -36.97    -34.59                                   
REMARK 500    VAL B 484        0.16    -63.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 605                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UJ0   RELATED DB: PDB                                   
DBREF  3UJ4 A    1   604  UNP    P29994   ITPR1_RAT        1    604             
DBREF  3UJ4 B    1   604  UNP    P29994   ITPR1_RAT        1    604             
SEQADV 3UJ4 ALA A   15  UNP  P29994    CYS    15 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA A   37  UNP  P29994    CYS    37 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA A   56  UNP  P29994    CYS    56 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA A   61  UNP  P29994    CYS    61 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA A  206  UNP  P29994    CYS   206 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA A  214  UNP  P29994    CYS   214 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA A  253  UNP  P29994    CYS   253 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA A  292  UNP  P29994    CYS   292 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA A  326  UNP  P29994    CYS   326 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA A  394  UNP  P29994    CYS   394 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA A  530  UNP  P29994    CYS   530 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA A  553  UNP  P29994    CYS   553 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA A  556  UNP  P29994    CYS   556 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA B   15  UNP  P29994    CYS    15 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA B   37  UNP  P29994    CYS    37 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA B   56  UNP  P29994    CYS    56 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA B   61  UNP  P29994    CYS    61 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA B  206  UNP  P29994    CYS   206 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA B  214  UNP  P29994    CYS   214 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA B  253  UNP  P29994    CYS   253 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA B  292  UNP  P29994    CYS   292 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA B  326  UNP  P29994    CYS   326 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA B  394  UNP  P29994    CYS   394 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA B  530  UNP  P29994    CYS   530 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA B  553  UNP  P29994    CYS   553 ENGINEERED MUTATION            
SEQADV 3UJ4 ALA B  556  UNP  P29994    CYS   556 ENGINEERED MUTATION            
SEQRES   1 A  604  MET SER ASP LYS MET SER SER PHE LEU HIS ILE GLY ASP          
SEQRES   2 A  604  ILE ALA SER LEU TYR ALA GLU GLY SER THR ASN GLY PHE          
SEQRES   3 A  604  ILE SER THR LEU GLY LEU VAL ASP ASP ARG ALA VAL VAL          
SEQRES   4 A  604  GLN PRO GLU ALA GLY ASP LEU ASN ASN PRO PRO LYS LYS          
SEQRES   5 A  604  PHE ARG ASP ALA LEU PHE LYS LEU ALA PRO MET ASN ARG          
SEQRES   6 A  604  TYR SER ALA GLN LYS GLN PHE TRP LYS ALA ALA LYS PRO          
SEQRES   7 A  604  GLY ALA ASN SER THR THR ASP ALA VAL LEU LEU ASN LYS          
SEQRES   8 A  604  LEU HIS HIS ALA ALA ASP LEU GLU LYS LYS GLN ASN GLU          
SEQRES   9 A  604  THR GLU ASN ARG LYS LEU LEU GLY THR VAL ILE GLN TYR          
SEQRES  10 A  604  GLY ASN VAL ILE GLN LEU LEU HIS LEU LYS SER ASN LYS          
SEQRES  11 A  604  TYR LEU THR VAL ASN LYS ARG LEU PRO ALA LEU LEU GLU          
SEQRES  12 A  604  LYS ASN ALA MET ARG VAL THR LEU ASP GLU ALA GLY ASN          
SEQRES  13 A  604  GLU GLY SER TRP PHE TYR ILE GLN PRO PHE TYR LYS LEU          
SEQRES  14 A  604  ARG SER ILE GLY ASP SER VAL VAL ILE GLY ASP LYS VAL          
SEQRES  15 A  604  VAL LEU ASN PRO VAL ASN ALA GLY GLN PRO LEU HIS ALA          
SEQRES  16 A  604  SER SER HIS GLN LEU VAL ASP ASN PRO GLY ALA ASN GLU          
SEQRES  17 A  604  VAL ASN SER VAL ASN ALA ASN THR SER TRP LYS ILE VAL          
SEQRES  18 A  604  LEU PHE MET LYS TRP SER ASP ASN LYS ASP ASP ILE LEU          
SEQRES  19 A  604  LYS GLY GLY ASP VAL VAL ARG LEU PHE HIS ALA GLU GLN          
SEQRES  20 A  604  GLU LYS PHE LEU THR ALA ASP GLU HIS ARG LYS LYS GLN          
SEQRES  21 A  604  HIS VAL PHE LEU ARG THR THR GLY ARG GLN SER ALA THR          
SEQRES  22 A  604  SER ALA THR SER SER LYS ALA LEU TRP GLU VAL GLU VAL          
SEQRES  23 A  604  VAL GLN HIS ASP PRO ALA ARG GLY GLY ALA GLY TYR TRP          
SEQRES  24 A  604  ASN SER LEU PHE ARG PHE LYS HIS LEU ALA THR GLY HIS          
SEQRES  25 A  604  TYR LEU ALA ALA GLU VAL ASP PRO ASP PHE GLU GLU GLU          
SEQRES  26 A  604  ALA LEU GLU PHE GLN PRO SER VAL ASP PRO ASP GLN ASP          
SEQRES  27 A  604  ALA SER ARG SER ARG LEU ARG ASN ALA GLN GLU LYS MET          
SEQRES  28 A  604  VAL TYR SER LEU VAL SER VAL PRO GLU GLY ASN ASP ILE          
SEQRES  29 A  604  SER SER ILE PHE GLU LEU ASP PRO THR THR LEU ARG GLY          
SEQRES  30 A  604  GLY ASP SER LEU VAL PRO ARG ASN SER TYR VAL ARG LEU          
SEQRES  31 A  604  ARG HIS LEU ALA THR ASN THR TRP VAL HIS SER THR ASN          
SEQRES  32 A  604  ILE PRO ILE ASP LYS GLU GLU GLU LYS PRO VAL MET LEU          
SEQRES  33 A  604  LYS ILE GLY THR SER PRO LEU LYS GLU ASP LYS GLU ALA          
SEQRES  34 A  604  PHE ALA ILE VAL PRO VAL SER PRO ALA GLU VAL ARG ASP          
SEQRES  35 A  604  LEU ASP PHE ALA ASN ASP ALA SER LYS VAL LEU GLY SER          
SEQRES  36 A  604  ILE ALA GLY LYS LEU GLU LYS GLY THR ILE THR GLN ASN          
SEQRES  37 A  604  GLU ARG ARG SER VAL THR LYS LEU LEU GLU ASP LEU VAL          
SEQRES  38 A  604  TYR PHE VAL THR GLY GLY THR ASN SER GLY GLN ASP VAL          
SEQRES  39 A  604  LEU GLU VAL VAL PHE SER LYS PRO ASN ARG GLU ARG GLN          
SEQRES  40 A  604  LYS LEU MET ARG GLU GLN ASN ILE LEU LYS GLN ILE PHE          
SEQRES  41 A  604  LYS LEU LEU GLN ALA PRO PHE THR ASP ALA GLY ASP GLY          
SEQRES  42 A  604  PRO MET LEU ARG LEU GLU GLU LEU GLY ASP GLN ARG HIS          
SEQRES  43 A  604  ALA PRO PHE ARG HIS ILE ALA ARG LEU ALA TYR ARG VAL          
SEQRES  44 A  604  LEU ARG HIS SER GLN GLN ASP TYR ARG LYS ASN GLN GLU          
SEQRES  45 A  604  TYR ILE ALA LYS GLN PHE GLY PHE MET GLN LYS GLN ILE          
SEQRES  46 A  604  GLY TYR ASP VAL LEU ALA GLU ASP THR ILE THR ALA LEU          
SEQRES  47 A  604  LEU HIS ASN ASN ARG LYS                                      
SEQRES   1 B  604  MET SER ASP LYS MET SER SER PHE LEU HIS ILE GLY ASP          
SEQRES   2 B  604  ILE ALA SER LEU TYR ALA GLU GLY SER THR ASN GLY PHE          
SEQRES   3 B  604  ILE SER THR LEU GLY LEU VAL ASP ASP ARG ALA VAL VAL          
SEQRES   4 B  604  GLN PRO GLU ALA GLY ASP LEU ASN ASN PRO PRO LYS LYS          
SEQRES   5 B  604  PHE ARG ASP ALA LEU PHE LYS LEU ALA PRO MET ASN ARG          
SEQRES   6 B  604  TYR SER ALA GLN LYS GLN PHE TRP LYS ALA ALA LYS PRO          
SEQRES   7 B  604  GLY ALA ASN SER THR THR ASP ALA VAL LEU LEU ASN LYS          
SEQRES   8 B  604  LEU HIS HIS ALA ALA ASP LEU GLU LYS LYS GLN ASN GLU          
SEQRES   9 B  604  THR GLU ASN ARG LYS LEU LEU GLY THR VAL ILE GLN TYR          
SEQRES  10 B  604  GLY ASN VAL ILE GLN LEU LEU HIS LEU LYS SER ASN LYS          
SEQRES  11 B  604  TYR LEU THR VAL ASN LYS ARG LEU PRO ALA LEU LEU GLU          
SEQRES  12 B  604  LYS ASN ALA MET ARG VAL THR LEU ASP GLU ALA GLY ASN          
SEQRES  13 B  604  GLU GLY SER TRP PHE TYR ILE GLN PRO PHE TYR LYS LEU          
SEQRES  14 B  604  ARG SER ILE GLY ASP SER VAL VAL ILE GLY ASP LYS VAL          
SEQRES  15 B  604  VAL LEU ASN PRO VAL ASN ALA GLY GLN PRO LEU HIS ALA          
SEQRES  16 B  604  SER SER HIS GLN LEU VAL ASP ASN PRO GLY ALA ASN GLU          
SEQRES  17 B  604  VAL ASN SER VAL ASN ALA ASN THR SER TRP LYS ILE VAL          
SEQRES  18 B  604  LEU PHE MET LYS TRP SER ASP ASN LYS ASP ASP ILE LEU          
SEQRES  19 B  604  LYS GLY GLY ASP VAL VAL ARG LEU PHE HIS ALA GLU GLN          
SEQRES  20 B  604  GLU LYS PHE LEU THR ALA ASP GLU HIS ARG LYS LYS GLN          
SEQRES  21 B  604  HIS VAL PHE LEU ARG THR THR GLY ARG GLN SER ALA THR          
SEQRES  22 B  604  SER ALA THR SER SER LYS ALA LEU TRP GLU VAL GLU VAL          
SEQRES  23 B  604  VAL GLN HIS ASP PRO ALA ARG GLY GLY ALA GLY TYR TRP          
SEQRES  24 B  604  ASN SER LEU PHE ARG PHE LYS HIS LEU ALA THR GLY HIS          
SEQRES  25 B  604  TYR LEU ALA ALA GLU VAL ASP PRO ASP PHE GLU GLU GLU          
SEQRES  26 B  604  ALA LEU GLU PHE GLN PRO SER VAL ASP PRO ASP GLN ASP          
SEQRES  27 B  604  ALA SER ARG SER ARG LEU ARG ASN ALA GLN GLU LYS MET          
SEQRES  28 B  604  VAL TYR SER LEU VAL SER VAL PRO GLU GLY ASN ASP ILE          
SEQRES  29 B  604  SER SER ILE PHE GLU LEU ASP PRO THR THR LEU ARG GLY          
SEQRES  30 B  604  GLY ASP SER LEU VAL PRO ARG ASN SER TYR VAL ARG LEU          
SEQRES  31 B  604  ARG HIS LEU ALA THR ASN THR TRP VAL HIS SER THR ASN          
SEQRES  32 B  604  ILE PRO ILE ASP LYS GLU GLU GLU LYS PRO VAL MET LEU          
SEQRES  33 B  604  LYS ILE GLY THR SER PRO LEU LYS GLU ASP LYS GLU ALA          
SEQRES  34 B  604  PHE ALA ILE VAL PRO VAL SER PRO ALA GLU VAL ARG ASP          
SEQRES  35 B  604  LEU ASP PHE ALA ASN ASP ALA SER LYS VAL LEU GLY SER          
SEQRES  36 B  604  ILE ALA GLY LYS LEU GLU LYS GLY THR ILE THR GLN ASN          
SEQRES  37 B  604  GLU ARG ARG SER VAL THR LYS LEU LEU GLU ASP LEU VAL          
SEQRES  38 B  604  TYR PHE VAL THR GLY GLY THR ASN SER GLY GLN ASP VAL          
SEQRES  39 B  604  LEU GLU VAL VAL PHE SER LYS PRO ASN ARG GLU ARG GLN          
SEQRES  40 B  604  LYS LEU MET ARG GLU GLN ASN ILE LEU LYS GLN ILE PHE          
SEQRES  41 B  604  LYS LEU LEU GLN ALA PRO PHE THR ASP ALA GLY ASP GLY          
SEQRES  42 B  604  PRO MET LEU ARG LEU GLU GLU LEU GLY ASP GLN ARG HIS          
SEQRES  43 B  604  ALA PRO PHE ARG HIS ILE ALA ARG LEU ALA TYR ARG VAL          
SEQRES  44 B  604  LEU ARG HIS SER GLN GLN ASP TYR ARG LYS ASN GLN GLU          
SEQRES  45 B  604  TYR ILE ALA LYS GLN PHE GLY PHE MET GLN LYS GLN ILE          
SEQRES  46 B  604  GLY TYR ASP VAL LEU ALA GLU ASP THR ILE THR ALA LEU          
SEQRES  47 B  604  LEU HIS ASN ASN ARG LYS                                      
HET    SO4  B 605       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  HOH   *28(H2 O)                                                     
HELIX    1   1 LYS A   52  ASP A   55  5                                   4    
HELIX    2   2 TYR A   66  ALA A   75  1                                  10    
HELIX    3   3 ALA A   86  LYS A  109  1                                  24    
HELIX    4   4 ASN A  156  SER A  159  5                                   4    
HELIX    5   5 LYS A  225  ASN A  229  5                                   5    
HELIX    6   6 SER A  277  LYS A  279  5                                   3    
HELIX    7   7 ASP A  363  SER A  366  5                                   4    
HELIX    8   8 SER A  436  GLY A  463  1                                  28    
HELIX    9   9 THR A  466  VAL A  484  1                                  19    
HELIX   10  10 ASN A  503  GLN A  513  1                                  11    
HELIX   11  11 ASN A  514  LEU A  523  1                                  10    
HELIX   12  12 ILE A  552  SER A  563  1                                  12    
HELIX   13  13 TYR A  567  LYS A  576  1                                  10    
HELIX   14  14 LYS B   52  ALA B   56  5                                   5    
HELIX   15  15 TYR B   66  LYS B   74  1                                   9    
HELIX   16  16 ASP B   85  LEU B  110  1                                  26    
HELIX   17  17 ASN B  156  SER B  159  5                                   4    
HELIX   18  18 LYS B  225  ASN B  229  5                                   5    
HELIX   19  19 SER B  277  ALA B  280  5                                   4    
HELIX   20  20 ASP B  363  SER B  366  5                                   4    
HELIX   21  21 LEU B  423  LYS B  427  5                                   5    
HELIX   22  22 SER B  436  GLY B  463  1                                  28    
HELIX   23  23 THR B  466  THR B  485  1                                  20    
HELIX   24  24 ASN B  503  GLN B  513  1                                  11    
HELIX   25  25 ASN B  514  LEU B  522  1                                   9    
HELIX   26  26 ILE B  552  ARG B  561  1                                  10    
HELIX   27  27 TYR B  567  MET B  581  1                                  15    
CISPEP   1 GLY B  378    ASP B  379          0        -0.77                     
SITE     1 AC1  4 HIS A 198  ASN A 396  LYS A 424  ARG B 391                    
CRYST1   63.108   77.191  101.509 105.36  99.98 101.04 P 1           2          
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      0.015846  0.003093  0.003932        0.00000                         
SCALE2      0.000000  0.013199  0.004278        0.00000                         
SCALE3      0.000000  0.000000  0.010515        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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