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Database: PDB
Entry: 3JXI
LinkDB: 3JXI
Original site: 3JXI 
HEADER    MEMBRANE PROTEIN                        19-SEP-09   3JXI              
TITLE     CRYSTAL STRUCTURE OF THE CHICKEN TRPV4 ANKYRIN REPEAT DOMAIN          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VANILLOID RECEPTOR-RELATED OSMOTICALLY ACTIVATED CHANNEL   
COMPND   3 PROTEIN;                                                             
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 FRAGMENT: UNP RESIDUES 133-382, ANKYRIN REPEAT DOMAIN;               
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE   3 ORGANISM_COMMON: CHICKEN;                                            
SOURCE   4 ORGANISM_TAXID: 9031;                                                
SOURCE   5 GENE: TRPV4, VR-OAC;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21-C6H                                 
KEYWDS    ANKYRIN REPEATS, ANK REPEAT, ION TRANSPORT, IONIC CHANNEL, RECEPTOR,  
KEYWDS   2 TRANSMEMBRANE, TRANSPORT, MEMBRANE PROTEIN                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.B.PHELPS,R.R.WANG,R.GAUDET                                          
REVDAT   5   06-SEP-23 3JXI    1       SEQADV                                   
REVDAT   4   01-NOV-17 3JXI    1       REMARK                                   
REVDAT   3   13-JUL-11 3JXI    1       VERSN                                    
REVDAT   2   09-FEB-10 3JXI    1       JRNL                                     
REVDAT   1   22-DEC-09 3JXI    0                                                
JRNL        AUTH   G.LANDOURE,A.A.ZDEBIK,T.L.MARTINEZ,B.G.BURNETT,H.C.STANESCU, 
JRNL        AUTH 2 H.INADA,Y.SHI,A.A.TAYE,L.KONG,C.H.MUNNS,S.S.CHOO,C.B.PHELPS, 
JRNL        AUTH 3 R.PAUDEL,H.HOULDEN,C.L.LUDLOW,M.J.CATERINA,R.GAUDET,R.KLETA, 
JRNL        AUTH 4 K.H.FISCHBECK,C.J.SUMNER                                     
JRNL        TITL   MUTATIONS IN TRPV4 CAUSE CHARCOT-MARIE-TOOTH DISEASE TYPE    
JRNL        TITL 2 2C.                                                          
JRNL        REF    NAT.GENET.                    V.  42   170 2010              
JRNL        REFN                   ISSN 1061-4036                               
JRNL        PMID   20037586                                                     
JRNL        DOI    10.1038/NG.512                                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0066                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 57722                          
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) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1178                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4089                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.66                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2490                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 79                           
REMARK   3   BIN FREE R VALUE                    : 0.4170                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8005                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 534                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.51                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.21000                                             
REMARK   3    B22 (A**2) : 0.23000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.02000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.294         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.221         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.167         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.892        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8184 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  5703 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11049 ; 1.473 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13845 ; 1.007 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1009 ; 6.744 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   389 ;34.767 ;23.111       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1466 ;17.951 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    73 ;18.067 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1239 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9056 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1705 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5019 ; 0.563 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2036 ; 0.133 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8073 ; 1.049 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3165 ; 1.745 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2972 ; 2.792 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
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   132        A   165                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.3551 -13.9962  10.3746              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0761 T22:   0.1603                                     
REMARK   3      T33:   0.3049 T12:  -0.0019                                     
REMARK   3      T13:  -0.0886 T23:   0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5523 L22:   2.9501                                     
REMARK   3      L33:   6.1402 L12:  -0.3693                                     
REMARK   3      L13:  -4.8108 L23:   0.7147                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0307 S12:  -0.5343 S13:  -0.1605                       
REMARK   3      S21:   0.2561 S22:  -0.1746 S23:  -0.2555                       
REMARK   3      S31:   0.1199 S32:   0.2434 S33:   0.2053                       
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   166        A   210                          
REMARK   3    ORIGIN FOR THE GROUP (A): -35.7376 -10.6721   2.6802              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0539 T22:   0.0886                                     
REMARK   3      T33:   0.2225 T12:   0.0106                                     
REMARK   3      T13:  -0.0542 T23:  -0.0055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0708 L22:   2.5197                                     
REMARK   3      L33:   3.0843 L12:   0.5182                                     
REMARK   3      L13:  -0.9839 L23:  -1.4267                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0027 S12:  -0.0217 S13:  -0.0853                       
REMARK   3      S21:   0.0378 S22:  -0.0653 S23:  -0.0099                       
REMARK   3      S31:   0.0473 S32:  -0.0305 S33:   0.0625                       
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   211        A   261                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.5085  -3.2286  -6.1198              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0523 T22:   0.1127                                     
REMARK   3      T33:   0.2035 T12:   0.0196                                     
REMARK   3      T13:  -0.0301 T23:  -0.0261                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2828 L22:   2.4853                                     
REMARK   3      L33:   2.7721 L12:  -0.1231                                     
REMARK   3      L13:   0.2367 L23:  -1.2666                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0604 S12:   0.1360 S13:   0.0837                       
REMARK   3      S21:  -0.0903 S22:  -0.0896 S23:  -0.1450                       
REMARK   3      S31:   0.0114 S32:   0.1829 S33:   0.0291                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   262        A   326                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.7688  -1.3657 -17.1689              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0961 T22:   0.1592                                     
REMARK   3      T33:   0.1826 T12:   0.0513                                     
REMARK   3      T13:  -0.0436 T23:  -0.0337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1606 L22:   2.3027                                     
REMARK   3      L33:   2.8685 L12:  -0.9289                                     
REMARK   3      L13:   0.4722 L23:  -0.9238                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1579 S12:   0.4374 S13:  -0.0602                       
REMARK   3      S21:  -0.4254 S22:  -0.1554 S23:  -0.1489                       
REMARK   3      S31:   0.1562 S32:   0.0907 S33:  -0.0026                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   327        A   374                          
REMARK   3    ORIGIN FOR THE GROUP (A): -57.0505   2.0703 -23.6111              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1454 T22:   0.2938                                     
REMARK   3      T33:   0.1395 T12:   0.0783                                     
REMARK   3      T13:  -0.1152 T23:  -0.0176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8272 L22:   5.6191                                     
REMARK   3      L33:   3.9147 L12:  -0.2735                                     
REMARK   3      L13:  -0.2383 L23:   1.3650                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1482 S12:   0.5582 S13:  -0.2524                       
REMARK   3      S21:  -0.2251 S22:  -0.1387 S23:   0.1605                       
REMARK   3      S31:   0.3334 S32:  -0.1875 S33:  -0.0096                       
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 :   A   375        A   384                          
REMARK   3    ORIGIN FOR THE GROUP (A): -62.8170   0.9677 -34.2671              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4804 T22:   0.4412                                     
REMARK   3      T33:   0.4700 T12:   0.1755                                     
REMARK   3      T13:   0.0219 T23:   0.0402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.8771 L22:   9.1745                                     
REMARK   3      L33:   6.7891 L12:  10.8463                                     
REMARK   3      L13:   9.3481 L23:   7.8633                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0195 S12:  -0.4913 S13:  -0.6072                       
REMARK   3      S21:  -0.0128 S22:   0.1926 S23:   1.3890                       
REMARK   3      S31:   0.2837 S32:  -0.4199 S33:  -0.2121                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   132        B   162                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.0220   9.0799 -10.5763              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0559 T22:   0.1419                                     
REMARK   3      T33:   0.2625 T12:  -0.0068                                     
REMARK   3      T13:  -0.0786 T23:   0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9106 L22:   2.7097                                     
REMARK   3      L33:   5.8251 L12:   0.8017                                     
REMARK   3      L13:  -4.1716 L23:  -1.5704                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0106 S12:   0.4106 S13:  -0.0125                       
REMARK   3      S21:  -0.1447 S22:  -0.0620 S23:   0.2437                       
REMARK   3      S31:   0.1600 S32:  -0.2887 S33:   0.0726                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   163        B   178                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.3224  20.1546  -9.7931              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1157 T22:   0.1006                                     
REMARK   3      T33:   0.2280 T12:  -0.0156                                     
REMARK   3      T13:  -0.0401 T23:   0.0358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9630 L22:   8.9174                                     
REMARK   3      L33:   9.4657 L12:  -3.0602                                     
REMARK   3      L13:  -2.9715 L23:   9.1146                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0965 S12:   0.1687 S13:   0.2454                       
REMARK   3      S21:  -0.4444 S22:   0.0921 S23:  -0.2234                       
REMARK   3      S31:  -0.4407 S32:   0.1229 S33:  -0.1886                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   179        B   209                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.4834   9.2500  -1.6064              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0887 T22:   0.0734                                     
REMARK   3      T33:   0.2204 T12:  -0.0175                                     
REMARK   3      T13:  -0.0575 T23:   0.0282                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3610 L22:   2.2902                                     
REMARK   3      L33:   4.2121 L12:   0.1893                                     
REMARK   3      L13:  -1.2107 L23:   1.8057                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1051 S12:  -0.1131 S13:  -0.1411                       
REMARK   3      S21:   0.1778 S22:  -0.0482 S23:   0.1312                       
REMARK   3      S31:   0.1906 S32:  -0.1203 S33:   0.1532                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   210        B   234                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.9416  21.4338   3.4107              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0541 T22:   0.1683                                     
REMARK   3      T33:   0.3071 T12:  -0.0071                                     
REMARK   3      T13:  -0.0622 T23:   0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1147 L22:   8.1922                                     
REMARK   3      L33:   5.0712 L12:  -0.7717                                     
REMARK   3      L13:   1.0602 L23:   2.1732                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0573 S12:  -0.0925 S13:   0.2050                       
REMARK   3      S21:  -0.1386 S22:  -0.0859 S23:   0.2336                       
REMARK   3      S31:  -0.2910 S32:  -0.3732 S33:   0.0286                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   235        B   259                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.6942  17.6365   6.1611              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0657 T22:   0.1251                                     
REMARK   3      T33:   0.1899 T12:  -0.0034                                     
REMARK   3      T13:  -0.0685 T23:   0.0264                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5827 L22:   1.3635                                     
REMARK   3      L33:   2.4531 L12:   0.8543                                     
REMARK   3      L13:   0.0922 L23:   0.9678                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0225 S12:  -0.0940 S13:  -0.0345                       
REMARK   3      S21:   0.0421 S22:  -0.0019 S23:   0.1323                       
REMARK   3      S31:   0.1718 S32:  -0.1044 S33:   0.0244                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   264        B   376                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6640  22.7511  19.9028              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0834 T22:   0.1358                                     
REMARK   3      T33:   0.1461 T12:  -0.0076                                     
REMARK   3      T13:  -0.0336 T23:   0.0241                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2032 L22:   1.9755                                     
REMARK   3      L33:   2.1132 L12:   1.1701                                     
REMARK   3      L13:   0.9772 L23:   0.8375                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1356 S12:  -0.3592 S13:  -0.0450                       
REMARK   3      S21:   0.2525 S22:  -0.0857 S23:   0.0973                       
REMARK   3      S31:   0.2071 S32:  -0.1582 S33:  -0.0499                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   377        B   387                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.4860  20.4208  34.1708              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3397 T22:   0.2788                                     
REMARK   3      T33:   0.2405 T12:  -0.0367                                     
REMARK   3      T13:  -0.1142 T23:   0.0410                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7364 L22:   4.0802                                     
REMARK   3      L33:   4.9871 L12:   0.8969                                     
REMARK   3      L13:   5.4510 L23:  -0.6172                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3687 S12:  -0.1195 S13:  -0.6806                       
REMARK   3      S21:   0.2714 S22:  -0.1443 S23:  -0.6267                       
REMARK   3      S31:   0.6744 S32:   0.4536 S33:  -0.2244                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   132        C   210                          
REMARK   3    ORIGIN FOR THE GROUP (A): -47.5239  24.5657 -59.0692              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3071 T22:   0.3773                                     
REMARK   3      T33:   0.1285 T12:   0.0833                                     
REMARK   3      T13:  -0.1391 T23:   0.0744                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0456 L22:   0.8946                                     
REMARK   3      L33:   3.6871 L12:   0.2411                                     
REMARK   3      L13:  -0.5826 L23:   0.1077                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0159 S12:   0.4143 S13:   0.2494                       
REMARK   3      S21:  -0.0731 S22:   0.0790 S23:   0.2208                       
REMARK   3      S31:  -0.2461 S32:  -0.3489 S33:  -0.0631                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   211        C   269                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.2312  17.6152 -50.1398              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2881 T22:   0.3078                                     
REMARK   3      T33:   0.0690 T12:   0.0588                                     
REMARK   3      T13:  -0.1164 T23:   0.0281                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5341 L22:   3.1800                                     
REMARK   3      L33:   3.4503 L12:   0.4383                                     
REMARK   3      L13:   0.7961 L23:  -0.3524                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1347 S12:   0.2491 S13:  -0.1608                       
REMARK   3      S21:  -0.2464 S22:   0.0911 S23:  -0.1206                       
REMARK   3      S31:   0.0615 S32:   0.1538 S33:   0.0435                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   270        C   376                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.4426  16.7254 -38.3691              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2966 T22:   0.3078                                     
REMARK   3      T33:   0.1516 T12:   0.0233                                     
REMARK   3      T13:  -0.1121 T23:   0.0498                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9722 L22:   1.8855                                     
REMARK   3      L33:   2.4602 L12:  -1.4703                                     
REMARK   3      L13:   1.4177 L23:  -0.8052                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1329 S12:   0.0019 S13:   0.1814                       
REMARK   3      S21:   0.0253 S22:   0.0367 S23:  -0.1176                       
REMARK   3      S31:  -0.2864 S32:   0.0277 S33:   0.0962                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   377        C   388                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.6232  18.9707 -23.6512              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2732 T22:   0.2839                                     
REMARK   3      T33:   0.3505 T12:   0.0246                                     
REMARK   3      T13:  -0.0249 T23:   0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4654 L22:   4.8655                                     
REMARK   3      L33:  15.6154 L12:  -0.3995                                     
REMARK   3      L13:  -1.5508 L23:   2.4331                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1419 S12:  -0.1463 S13:   0.2806                       
REMARK   3      S21:   0.2202 S22:  -0.1185 S23:   0.4397                       
REMARK   3      S31:   0.0474 S32:  -0.6022 S33:   0.2604                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   132        D   136                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.3813  35.7214 -65.7347              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5702 T22:   0.8547                                     
REMARK   3      T33:   1.3237 T12:   0.3984                                     
REMARK   3      T13:  -0.5261 T23:   0.0826                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.1204 L22:   1.3234                                     
REMARK   3      L33:   2.1939 L12:   3.8363                                     
REMARK   3      L13:  -4.9393 L23:  -1.7040                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.9924 S12:   0.2645 S13:   0.2263                       
REMARK   3      S21:   1.4259 S22:  -0.7789 S23:  -1.3884                       
REMARK   3      S31:   0.9824 S32:   1.5341 S33:  -1.2135                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   137        D   149                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.4400  35.1046 -64.1616              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6119 T22:   0.9061                                     
REMARK   3      T33:   1.1220 T12:   0.2028                                     
REMARK   3      T13:  -0.4664 T23:   0.0407                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2785 L22:   5.7180                                     
REMARK   3      L33:   4.1316 L12:   0.3803                                     
REMARK   3      L13:  -3.0600 L23:  -0.1588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8643 S12:   0.7561 S13:  -0.4753                       
REMARK   3      S21:  -1.2846 S22:  -0.0322 S23:   0.9949                       
REMARK   3      S31:  -0.4956 S32:  -0.2772 S33:  -0.8321                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   150        D   181                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.4045  29.8195 -59.0233              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2903 T22:   0.7385                                     
REMARK   3      T33:   1.6922 T12:   0.1975                                     
REMARK   3      T13:  -0.5441 T23:   0.2578                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7553 L22:   3.9613                                     
REMARK   3      L33:   7.6035 L12:  -1.6587                                     
REMARK   3      L13:  -2.1150 L23:   5.3767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0499 S12:   0.9527 S13:  -0.7750                       
REMARK   3      S21:   0.2304 S22:   0.4004 S23:   0.9645                       
REMARK   3      S31:   0.5468 S32:  -0.7890 S33:  -0.3506                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   182        D   223                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1666  29.6848 -53.0975              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3248 T22:   0.6494                                     
REMARK   3      T33:   0.8807 T12:   0.0479                                     
REMARK   3      T13:  -0.3175 T23:   0.1352                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0601 L22:   9.2469                                     
REMARK   3      L33:   5.3037 L12:  -1.6376                                     
REMARK   3      L13:  -2.9757 L23:  -0.3732                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2047 S12:   0.0184 S13:  -0.8819                       
REMARK   3      S21:  -0.1306 S22:  -0.1384 S23:   1.0507                       
REMARK   3      S31:  -0.0128 S32:  -0.0681 S33:  -0.0664                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   224        D   268                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.9307  26.3123 -47.7821              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1781 T22:   0.4641                                     
REMARK   3      T33:   0.8602 T12:   0.1619                                     
REMARK   3      T13:  -0.2516 T23:   0.1830                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1119 L22:   8.2052                                     
REMARK   3      L33:   4.4846 L12:   0.3619                                     
REMARK   3      L13:   1.3805 L23:  -3.7057                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0783 S12:  -0.0208 S13:  -0.8367                       
REMARK   3      S21:  -0.5635 S22:   0.3833 S23:   1.5060                       
REMARK   3      S31:   0.0040 S32:  -0.2501 S33:  -0.4616                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   269        D   367                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.8202  20.9840 -37.6292              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1606 T22:   0.4179                                     
REMARK   3      T33:   0.6040 T12:   0.1824                                     
REMARK   3      T13:  -0.0355 T23:   0.1225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5430 L22:   3.9736                                     
REMARK   3      L33:   4.2346 L12:  -2.4528                                     
REMARK   3      L13:   0.8157 L23:  -1.8759                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0401 S12:  -0.4641 S13:  -0.2400                       
REMARK   3      S21:   0.3975 S22:   0.3450 S23:   1.2995                       
REMARK   3      S31:  -0.3066 S32:  -0.3705 S33:  -0.3049                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   368        D   388                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.2430  18.9499 -28.9143              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3111 T22:   0.3721                                     
REMARK   3      T33:   0.2446 T12:   0.1297                                     
REMARK   3      T13:  -0.0079 T23:   0.0413                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0051 L22:   2.0996                                     
REMARK   3      L33:   7.7122 L12:  -0.1799                                     
REMARK   3      L13:   3.1373 L23:   1.3300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1807 S12:  -0.1688 S13:   0.2496                       
REMARK   3      S21:   0.4543 S22:   0.0810 S23:   0.3116                       
REMARK   3      S31:  -0.1955 S32:  -0.0152 S33:   0.0997                       
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 ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3JXI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000055283.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-AUG-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 65393                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59800                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2ETB (TRPV2 ANKYRIN REPEATS)               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE PH 5.0, 10% MPD,    
REMARK 280  2% PEG8000, 4.3% TRIFLUOROETHANOL, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       24.05950            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 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     ALA A   385                                                      
REMARK 465     HIS A   386                                                      
REMARK 465     HIS A   387                                                      
REMARK 465     HIS A   388                                                      
REMARK 465     HIS A   389                                                      
REMARK 465     HIS A   390                                                      
REMARK 465     HIS A   391                                                      
REMARK 465     HIS B   388                                                      
REMARK 465     HIS B   389                                                      
REMARK 465     HIS B   390                                                      
REMARK 465     HIS B   391                                                      
REMARK 465     PHE C   259                                                      
REMARK 465     GLN C   260                                                      
REMARK 465     PRO C   261                                                      
REMARK 465     LYS C   262                                                      
REMARK 465     ASP C   263                                                      
REMARK 465     GLU C   264                                                      
REMARK 465     GLY C   265                                                      
REMARK 465     GLY C   266                                                      
REMARK 465     HIS C   389                                                      
REMARK 465     HIS C   390                                                      
REMARK 465     HIS C   391                                                      
REMARK 465     PHE D   259                                                      
REMARK 465     GLN D   260                                                      
REMARK 465     PRO D   261                                                      
REMARK 465     LYS D   262                                                      
REMARK 465     ASP D   263                                                      
REMARK 465     GLU D   264                                                      
REMARK 465     GLY D   265                                                      
REMARK 465     GLY D   266                                                      
REMARK 465     HIS D   389                                                      
REMARK 465     HIS D   390                                                      
REMARK 465     HIS D   391                                                      
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   O    ASP B   319     O    HOH B   753              2.08            
REMARK 500   O    HOH B   551     O    HOH B   775              2.11            
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    ARG A 137   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 137   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG B 378   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B 378   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 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    ASP A 219     -152.43   -126.55                                   
REMARK 500    ARG A 235       34.91     72.29                                   
REMARK 500    ASP A 263      109.57    -42.80                                   
REMARK 500    GLU A 272      -35.43     62.85                                   
REMARK 500    ASP B 219     -154.94   -124.01                                   
REMARK 500    CYS B 236       77.96   -100.95                                   
REMARK 500    ASP B 263      -20.02     91.39                                   
REMARK 500    GLU B 272      -37.11     63.23                                   
REMARK 500    GLN B 283       71.67   -119.53                                   
REMARK 500    LYS B 296      116.99   -175.08                                   
REMARK 500    LYS C 133      -72.26    -44.40                                   
REMARK 500    ASN C 187       52.74   -150.46                                   
REMARK 500    GLU C 272      -45.38     69.22                                   
REMARK 500    HIS C 295      -68.88   -105.87                                   
REMARK 500    LEU D 160      -55.51   -143.32                                   
REMARK 500    LYS D 163       65.71     62.68                                   
REMARK 500    THR D 176      -33.49   -136.57                                   
REMARK 500    ASN D 208       -5.76   -146.49                                   
REMARK 500    ASN D 214       31.38    -86.42                                   
REMARK 500    PHE D 217     -161.49   -127.46                                   
REMARK 500    ARG D 235       42.35     72.35                                   
REMARK 500    ARG D 257       58.74   -164.12                                   
REMARK 500    GLU D 272      -53.62     70.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS B  262     ASP B  263                  130.47                    
REMARK 500 ASP B  263     GLU B  264                 -133.49                    
REMARK 500 GLY C  207     ASN C  208                 -149.52                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2PNN   RELATED DB: PDB                                   
REMARK 900 TRPV1 ANKYRIN REPEATS                                                
REMARK 900 RELATED ID: 2ETB   RELATED DB: PDB                                   
REMARK 900 TRPV2 ANKYRIN REPEATS                                                
REMARK 900 RELATED ID: 2RFA   RELATED DB: PDB                                   
REMARK 900 TRPV6 ANKYRIN REPEATS                                                
REMARK 900 RELATED ID: 3JZJ   RELATED DB: PDB                                   
DBREF  3JXI A  133   382  UNP    Q9DFS3   Q9DFS3_CHICK   133    382             
DBREF  3JXI B  133   382  UNP    Q9DFS3   Q9DFS3_CHICK   133    382             
DBREF  3JXI C  133   382  UNP    Q9DFS3   Q9DFS3_CHICK   133    382             
DBREF  3JXI D  133   382  UNP    Q9DFS3   Q9DFS3_CHICK   133    382             
SEQADV 3JXI MET A  132  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI ALA A  383  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI ALA A  384  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI ALA A  385  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS A  386  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS A  387  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS A  388  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS A  389  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS A  390  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS A  391  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI MET B  132  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI ALA B  383  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI ALA B  384  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI ALA B  385  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS B  386  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS B  387  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS B  388  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS B  389  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS B  390  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS B  391  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI MET C  132  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI ALA C  383  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI ALA C  384  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI ALA C  385  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS C  386  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS C  387  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS C  388  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS C  389  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS C  390  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS C  391  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI MET D  132  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI ALA D  383  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI ALA D  384  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI ALA D  385  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS D  386  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS D  387  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS D  388  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS D  389  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS D  390  UNP  Q9DFS3              EXPRESSION TAG                 
SEQADV 3JXI HIS D  391  UNP  Q9DFS3              EXPRESSION TAG                 
SEQRES   1 A  260  MET LYS VAL PHE ASN ARG PRO ILE LEU PHE ASP ILE VAL          
SEQRES   2 A  260  SER ARG GLY SER PRO ASP GLY LEU GLU GLY LEU LEU SER          
SEQRES   3 A  260  PHE LEU LEU THR HIS LYS LYS ARG LEU THR ASP GLU GLU          
SEQRES   4 A  260  PHE ARG GLU PRO SER THR GLY LYS THR CYS LEU PRO LYS          
SEQRES   5 A  260  ALA LEU LEU ASN LEU SER ALA GLY ARG ASN ASP THR ILE          
SEQRES   6 A  260  PRO ILE LEU LEU ASP ILE ALA GLU LYS THR GLY ASN MET          
SEQRES   7 A  260  ARG GLU PHE ILE ASN SER PRO PHE ARG ASP VAL TYR TYR          
SEQRES   8 A  260  ARG GLY GLN THR ALA LEU HIS ILE ALA ILE GLU ARG ARG          
SEQRES   9 A  260  CYS LYS HIS TYR VAL GLU LEU LEU VAL GLU LYS GLY ALA          
SEQRES  10 A  260  ASP VAL HIS ALA GLN ALA ARG GLY ARG PHE PHE GLN PRO          
SEQRES  11 A  260  LYS ASP GLU GLY GLY TYR PHE TYR PHE GLY GLU LEU PRO          
SEQRES  12 A  260  LEU SER LEU ALA ALA CYS THR ASN GLN PRO HIS ILE VAL          
SEQRES  13 A  260  HIS TYR LEU THR GLU ASN GLY HIS LYS GLN ALA ASP LEU          
SEQRES  14 A  260  ARG ARG GLN ASP SER ARG GLY ASN THR VAL LEU HIS ALA          
SEQRES  15 A  260  LEU VAL ALA ILE ALA ASP ASN THR ARG GLU ASN THR LYS          
SEQRES  16 A  260  PHE VAL THR LYS MET TYR ASP LEU LEU LEU ILE LYS CYS          
SEQRES  17 A  260  ALA LYS LEU PHE PRO ASP THR ASN LEU GLU ALA LEU LEU          
SEQRES  18 A  260  ASN ASN ASP GLY LEU SER PRO LEU MET MET ALA ALA LYS          
SEQRES  19 A  260  THR GLY LYS ILE GLY ILE PHE GLN HIS ILE ILE ARG ARG          
SEQRES  20 A  260  GLU ILE ALA ASP ALA ALA ALA HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  260  MET LYS VAL PHE ASN ARG PRO ILE LEU PHE ASP ILE VAL          
SEQRES   2 B  260  SER ARG GLY SER PRO ASP GLY LEU GLU GLY LEU LEU SER          
SEQRES   3 B  260  PHE LEU LEU THR HIS LYS LYS ARG LEU THR ASP GLU GLU          
SEQRES   4 B  260  PHE ARG GLU PRO SER THR GLY LYS THR CYS LEU PRO LYS          
SEQRES   5 B  260  ALA LEU LEU ASN LEU SER ALA GLY ARG ASN ASP THR ILE          
SEQRES   6 B  260  PRO ILE LEU LEU ASP ILE ALA GLU LYS THR GLY ASN MET          
SEQRES   7 B  260  ARG GLU PHE ILE ASN SER PRO PHE ARG ASP VAL TYR TYR          
SEQRES   8 B  260  ARG GLY GLN THR ALA LEU HIS ILE ALA ILE GLU ARG ARG          
SEQRES   9 B  260  CYS LYS HIS TYR VAL GLU LEU LEU VAL GLU LYS GLY ALA          
SEQRES  10 B  260  ASP VAL HIS ALA GLN ALA ARG GLY ARG PHE PHE GLN PRO          
SEQRES  11 B  260  LYS ASP GLU GLY GLY TYR PHE TYR PHE GLY GLU LEU PRO          
SEQRES  12 B  260  LEU SER LEU ALA ALA CYS THR ASN GLN PRO HIS ILE VAL          
SEQRES  13 B  260  HIS TYR LEU THR GLU ASN GLY HIS LYS GLN ALA ASP LEU          
SEQRES  14 B  260  ARG ARG GLN ASP SER ARG GLY ASN THR VAL LEU HIS ALA          
SEQRES  15 B  260  LEU VAL ALA ILE ALA ASP ASN THR ARG GLU ASN THR LYS          
SEQRES  16 B  260  PHE VAL THR LYS MET TYR ASP LEU LEU LEU ILE LYS CYS          
SEQRES  17 B  260  ALA LYS LEU PHE PRO ASP THR ASN LEU GLU ALA LEU LEU          
SEQRES  18 B  260  ASN ASN ASP GLY LEU SER PRO LEU MET MET ALA ALA LYS          
SEQRES  19 B  260  THR GLY LYS ILE GLY ILE PHE GLN HIS ILE ILE ARG ARG          
SEQRES  20 B  260  GLU ILE ALA ASP ALA ALA ALA HIS HIS HIS HIS HIS HIS          
SEQRES   1 C  260  MET LYS VAL PHE ASN ARG PRO ILE LEU PHE ASP ILE VAL          
SEQRES   2 C  260  SER ARG GLY SER PRO ASP GLY LEU GLU GLY LEU LEU SER          
SEQRES   3 C  260  PHE LEU LEU THR HIS LYS LYS ARG LEU THR ASP GLU GLU          
SEQRES   4 C  260  PHE ARG GLU PRO SER THR GLY LYS THR CYS LEU PRO LYS          
SEQRES   5 C  260  ALA LEU LEU ASN LEU SER ALA GLY ARG ASN ASP THR ILE          
SEQRES   6 C  260  PRO ILE LEU LEU ASP ILE ALA GLU LYS THR GLY ASN MET          
SEQRES   7 C  260  ARG GLU PHE ILE ASN SER PRO PHE ARG ASP VAL TYR TYR          
SEQRES   8 C  260  ARG GLY GLN THR ALA LEU HIS ILE ALA ILE GLU ARG ARG          
SEQRES   9 C  260  CYS LYS HIS TYR VAL GLU LEU LEU VAL GLU LYS GLY ALA          
SEQRES  10 C  260  ASP VAL HIS ALA GLN ALA ARG GLY ARG PHE PHE GLN PRO          
SEQRES  11 C  260  LYS ASP GLU GLY GLY TYR PHE TYR PHE GLY GLU LEU PRO          
SEQRES  12 C  260  LEU SER LEU ALA ALA CYS THR ASN GLN PRO HIS ILE VAL          
SEQRES  13 C  260  HIS TYR LEU THR GLU ASN GLY HIS LYS GLN ALA ASP LEU          
SEQRES  14 C  260  ARG ARG GLN ASP SER ARG GLY ASN THR VAL LEU HIS ALA          
SEQRES  15 C  260  LEU VAL ALA ILE ALA ASP ASN THR ARG GLU ASN THR LYS          
SEQRES  16 C  260  PHE VAL THR LYS MET TYR ASP LEU LEU LEU ILE LYS CYS          
SEQRES  17 C  260  ALA LYS LEU PHE PRO ASP THR ASN LEU GLU ALA LEU LEU          
SEQRES  18 C  260  ASN ASN ASP GLY LEU SER PRO LEU MET MET ALA ALA LYS          
SEQRES  19 C  260  THR GLY LYS ILE GLY ILE PHE GLN HIS ILE ILE ARG ARG          
SEQRES  20 C  260  GLU ILE ALA ASP ALA ALA ALA HIS HIS HIS HIS HIS HIS          
SEQRES   1 D  260  MET LYS VAL PHE ASN ARG PRO ILE LEU PHE ASP ILE VAL          
SEQRES   2 D  260  SER ARG GLY SER PRO ASP GLY LEU GLU GLY LEU LEU SER          
SEQRES   3 D  260  PHE LEU LEU THR HIS LYS LYS ARG LEU THR ASP GLU GLU          
SEQRES   4 D  260  PHE ARG GLU PRO SER THR GLY LYS THR CYS LEU PRO LYS          
SEQRES   5 D  260  ALA LEU LEU ASN LEU SER ALA GLY ARG ASN ASP THR ILE          
SEQRES   6 D  260  PRO ILE LEU LEU ASP ILE ALA GLU LYS THR GLY ASN MET          
SEQRES   7 D  260  ARG GLU PHE ILE ASN SER PRO PHE ARG ASP VAL TYR TYR          
SEQRES   8 D  260  ARG GLY GLN THR ALA LEU HIS ILE ALA ILE GLU ARG ARG          
SEQRES   9 D  260  CYS LYS HIS TYR VAL GLU LEU LEU VAL GLU LYS GLY ALA          
SEQRES  10 D  260  ASP VAL HIS ALA GLN ALA ARG GLY ARG PHE PHE GLN PRO          
SEQRES  11 D  260  LYS ASP GLU GLY GLY TYR PHE TYR PHE GLY GLU LEU PRO          
SEQRES  12 D  260  LEU SER LEU ALA ALA CYS THR ASN GLN PRO HIS ILE VAL          
SEQRES  13 D  260  HIS TYR LEU THR GLU ASN GLY HIS LYS GLN ALA ASP LEU          
SEQRES  14 D  260  ARG ARG GLN ASP SER ARG GLY ASN THR VAL LEU HIS ALA          
SEQRES  15 D  260  LEU VAL ALA ILE ALA ASP ASN THR ARG GLU ASN THR LYS          
SEQRES  16 D  260  PHE VAL THR LYS MET TYR ASP LEU LEU LEU ILE LYS CYS          
SEQRES  17 D  260  ALA LYS LEU PHE PRO ASP THR ASN LEU GLU ALA LEU LEU          
SEQRES  18 D  260  ASN ASN ASP GLY LEU SER PRO LEU MET MET ALA ALA LYS          
SEQRES  19 D  260  THR GLY LYS ILE GLY ILE PHE GLN HIS ILE ILE ARG ARG          
SEQRES  20 D  260  GLU ILE ALA ASP ALA ALA ALA HIS HIS HIS HIS HIS HIS          
FORMUL   5  HOH   *534(H2 O)                                                    
HELIX    1   1 ASN A  136  GLY A  147  1                                  12    
HELIX    2   2 SER A  148  GLU A  153  5                                   6    
HELIX    3   3 GLY A  154  LYS A  163  1                                  10    
HELIX    4   4 ASP A  168  ARG A  172  5                                   5    
HELIX    5   5 THR A  179  LEU A  186  1                                   8    
HELIX    6   6 ASP A  194  THR A  206  1                                  13    
HELIX    7   7 ASN A  208  ASN A  214  1                                   7    
HELIX    8   8 THR A  226  ARG A  234  1                                   9    
HELIX    9   9 CYS A  236  LYS A  246  1                                  11    
HELIX   10  10 LEU A  273  THR A  281  1                                   9    
HELIX   11  11 GLN A  283  ASN A  293  1                                  11    
HELIX   12  12 THR A  309  ALA A  318  1                                  10    
HELIX   13  13 THR A  321  PHE A  343  1                                  23    
HELIX   14  14 ASN A  347  LEU A  351  5                                   5    
HELIX   15  15 SER A  358  THR A  366  1                                   9    
HELIX   16  16 LYS A  368  ALA A  384  1                                  17    
HELIX   17  17 ASN B  136  GLY B  147  1                                  12    
HELIX   18  18 PRO B  149  GLU B  153  5                                   5    
HELIX   19  19 GLY B  154  LYS B  163  1                                  10    
HELIX   20  20 ASP B  168  ARG B  172  5                                   5    
HELIX   21  21 THR B  179  LEU B  186  1                                   8    
HELIX   22  22 ASP B  194  THR B  206  1                                  13    
HELIX   23  23 ASN B  208  SER B  215  1                                   8    
HELIX   24  24 THR B  226  ARG B  234  1                                   9    
HELIX   25  25 CYS B  236  LYS B  246  1                                  11    
HELIX   26  26 LEU B  273  THR B  281  1                                   9    
HELIX   27  27 GLN B  283  ASN B  293  1                                  11    
HELIX   28  28 THR B  309  ALA B  318  1                                  10    
HELIX   29  29 THR B  321  PHE B  343  1                                  23    
HELIX   30  30 ASN B  347  LEU B  351  5                                   5    
HELIX   31  31 SER B  358  THR B  366  1                                   9    
HELIX   32  32 LYS B  368  HIS B  387  1                                  20    
HELIX   33  33 ASN C  136  GLY C  147  1                                  12    
HELIX   34  34 GLY C  154  LYS C  163  1                                  10    
HELIX   35  35 ASP C  168  ARG C  172  5                                   5    
HELIX   36  36 THR C  179  LEU C  186  1                                   8    
HELIX   37  37 THR C  195  THR C  206  1                                  12    
HELIX   38  38 ASN C  208  SER C  215  1                                   8    
HELIX   39  39 THR C  226  ARG C  234  1                                   9    
HELIX   40  40 CYS C  236  LYS C  246  1                                  11    
HELIX   41  41 LEU C  273  THR C  281  1                                   9    
HELIX   42  42 GLN C  283  ASN C  293  1                                  11    
HELIX   43  43 THR C  309  ALA C  318  1                                  10    
HELIX   44  44 THR C  321  PHE C  343  1                                  23    
HELIX   45  45 ASN C  347  LEU C  351  5                                   5    
HELIX   46  46 SER C  358  GLY C  367  1                                  10    
HELIX   47  47 LYS C  368  HIS C  387  1                                  20    
HELIX   48  48 ASN D  136  GLY D  147  1                                  12    
HELIX   49  49 GLY D  154  HIS D  162  1                                   9    
HELIX   50  50 ASP D  168  ARG D  172  5                                   5    
HELIX   51  51 THR D  179  LEU D  186  1                                   8    
HELIX   52  52 THR D  195  THR D  206  1                                  12    
HELIX   53  53 MET D  209  ASN D  214  1                                   6    
HELIX   54  54 THR D  226  ARG D  234  1                                   9    
HELIX   55  55 CYS D  236  LYS D  246  1                                  11    
HELIX   56  56 LEU D  273  THR D  281  1                                   9    
HELIX   57  57 GLN D  283  ASN D  293  1                                  11    
HELIX   58  58 THR D  309  ALA D  318  1                                  10    
HELIX   59  59 THR D  321  PHE D  343  1                                  23    
HELIX   60  60 SER D  358  THR D  366  1                                   9    
HELIX   61  61 LYS D  368  HIS D  387  1                                  20    
SHEET    1   A 2 TYR A 222  ARG A 223  0                                        
SHEET    2   A 2 ARG A 255  GLY A 256 -1  O  ARG A 255   N  ARG A 223           
SHEET    1   B 2 TYR B 222  ARG B 223  0                                        
SHEET    2   B 2 ARG B 255  GLY B 256 -1  O  ARG B 255   N  ARG B 223           
SHEET    1   C 2 TYR C 222  ARG C 223  0                                        
SHEET    2   C 2 ARG C 255  GLY C 256 -1  O  ARG C 255   N  ARG C 223           
SHEET    1   D 3 PHE D 217  ARG D 218  0                                        
SHEET    2   D 3 TYR D 222  GLN D 225 -1  O  GLY D 224   N  PHE D 217           
SHEET    3   D 3 ARG D 255  GLY D 256 -1  O  ARG D 255   N  ARG D 223           
CRYST1  105.259   48.119  133.891  90.00 101.89  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009500  0.000000  0.002000        0.00000                         
SCALE2      0.000000  0.020782  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007633        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system