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Database: PDB
Entry: 3SUI
LinkDB: 3SUI
Original site: 3SUI 
HEADER    CALCIUM-BINDING PROTEIN                 11-JUL-11   3SUI              
TITLE     CRYSTAL STRUCTURE OF CA2+-CALMODULIN IN COMPLEX WITH A TRPV1 C-       
TITLE    2 TERMINAL PEPTIDE                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CAM;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY V    
COMPND   8 MEMBER 1;                                                            
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: UNP RESIDUES 767-801;                                      
COMPND  11 SYNONYM: TRPV1, CAPSAICIN RECEPTOR, OSM-9-LIKE TRP CHANNEL 1, OTRPC1,
COMPND  12 VANILLOID RECEPTOR 1, VANILLOID RECEPTOR TYPE 1-LIKE;                
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CALM, CALM1, CALM2, CALM3, CALML2, CAM, CAM1, CAM2, CAM3,      
SOURCE   6 CAMB, CAMC, CAMIII;                                                  
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET21;                                    
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  14 ORGANISM_COMMON: RAT;                                                
SOURCE  15 ORGANISM_TAXID: 10116;                                               
SOURCE  16 GENE: TRPV1, VR1, VR1L;                                              
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PMALC2                                    
KEYWDS    CALMODULIN, CALCIUM-CALMODULIN, TRPV1, TRPV1 C-TERMINUS, CALMODULIN   
KEYWDS   2 COMPLEX, THERMOSENSOR, TRP CHANNEL, EF HANDS, 1-10 MOTIF, CALCIUM    
KEYWDS   3 CHANNEL, CALMODULIN-BINDING, ION CHANNEL, CALCIUM BINDING PROTEIN,   
KEYWDS   4 CALCIUM-BINDING PROTEIN                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.-Y.LAU,R.GAUDET                                                     
REVDAT   4   13-SEP-23 3SUI    1       REMARK SEQADV LINK                       
REVDAT   3   08-NOV-17 3SUI    1       REMARK                                   
REVDAT   2   14-NOV-12 3SUI    1       JRNL                                     
REVDAT   1   12-SEP-12 3SUI    0                                                
JRNL        AUTH   S.Y.LAU,E.PROCKO,R.GAUDET                                    
JRNL        TITL   DISTINCT PROPERTIES OF CA2+-CALMODULIN BINDING TO N- AND     
JRNL        TITL 2 C-TERMINAL REGULATORY REGIONS OF THE TRPV1 CHANNEL.          
JRNL        REF    J.GEN.PHYSIOL.                V. 140   541 2012              
JRNL        REFN                   ISSN 0022-1295                               
JRNL        PMID   23109716                                                     
JRNL        DOI    10.1085/JGP.201210810                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 13172                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 690                             
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 885                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.11                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 47                           
REMARK   3   BIN FREE R VALUE                    : 0.3220                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1268                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 9                                       
REMARK   3   SOLVENT ATOMS            : 91                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.47000                                              
REMARK   3    B22 (A**2) : 0.47000                                              
REMARK   3    B33 (A**2) : -0.70000                                             
REMARK   3    B12 (A**2) : 0.23000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.168         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.164         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.107         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.173         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1372 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1866 ; 1.519 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   182 ; 4.707 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    81 ;36.926 ;26.296       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   256 ;16.447 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;19.427 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   202 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1077 ; 0.007 ; 0.020       
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):   830 ; 0.972 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1341 ; 1.728 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   542 ; 2.525 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   513 ; 4.141 ; 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  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A    80                          
REMARK   3    RESIDUE RANGE :   A   501        A   502                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.9420 -25.8990 -17.7520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3192 T22:   0.1938                                     
REMARK   3      T33:   0.0356 T12:   0.0009                                     
REMARK   3      T13:   0.0272 T23:  -0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3932 L22:   3.2130                                     
REMARK   3      L33:   5.9637 L12:  -1.1152                                     
REMARK   3      L13:   1.2655 L23:  -1.8376                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1125 S12:   0.1300 S13:  -0.0104                       
REMARK   3      S21:  -0.2230 S22:  -0.0082 S23:  -0.0218                       
REMARK   3      S31:   0.2080 S32:  -0.2905 S33:  -0.1043                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    81        A   148                          
REMARK   3    RESIDUE RANGE :   A   503        A   504                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.4150  -9.6580  -6.2110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3531 T22:   0.1727                                     
REMARK   3      T33:   0.0478 T12:  -0.0116                                     
REMARK   3      T13:   0.0095 T23:   0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2946 L22:   3.7392                                     
REMARK   3      L33:   2.6175 L12:  -1.8878                                     
REMARK   3      L13:  -0.4618 L23:   0.0066                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0013 S12:   0.1104 S13:  -0.0225                       
REMARK   3      S21:  -0.1786 S22:  -0.0292 S23:  -0.1591                       
REMARK   3      S31:   0.1166 S32:   0.0833 S33:   0.0279                       
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 :   B   784        B   798                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.3290 -17.9790 -12.6830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3192 T22:   0.2687                                     
REMARK   3      T33:   0.0575 T12:   0.0318                                     
REMARK   3      T13:   0.0243 T23:  -0.0702                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.4538 L22:  30.8631                                     
REMARK   3      L33:  13.1870 L12:   0.7982                                     
REMARK   3      L13:  -1.6430 L23:   0.5393                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1270 S12:   0.2760 S13:  -0.1402                       
REMARK   3      S21:  -0.8867 S22:  -0.2584 S23:   0.2787                       
REMARK   3      S31:  -0.0152 S32:  -0.2764 S33:   0.1314                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3SUI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000066667.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13862                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46900                            
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: 3DVE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH6.0, 2.2-2.8M AMMONIUM        
REMARK 280  SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.84433            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      227.68867            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      170.76650            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      284.61083            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       56.92217            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      113.84433            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      227.68867            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      284.61083            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      170.76650            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       56.92217            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8590 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     GLY B   765                                                      
REMARK 465     PRO B   766                                                      
REMARK 465     GLU B   767                                                      
REMARK 465     GLY B   768                                                      
REMARK 465     VAL B   769                                                      
REMARK 465     LYS B   770                                                      
REMARK 465     ARG B   771                                                      
REMARK 465     THR B   772                                                      
REMARK 465     LEU B   773                                                      
REMARK 465     SER B   774                                                      
REMARK 465     PHE B   775                                                      
REMARK 465     SER B   776                                                      
REMARK 465     LEU B   777                                                      
REMARK 465     ARG B   778                                                      
REMARK 465     SER B   779                                                      
REMARK 465     GLY B   780                                                      
REMARK 465     ARG B   781                                                      
REMARK 465     VAL B   782                                                      
REMARK 465     SER B   783                                                      
REMARK 465     ALA B   799                                                      
REMARK 465     SER B   800                                                      
REMARK 465     THR B   801                                                      
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     GLU A   7    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 148    CG   CD   CE   NZ                                   
REMARK 470     ASP B 798    CG   OD1  OD2                                       
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   OD1  ASN A    53     O    HOH A   234              2.02            
REMARK 500   OE2  GLU A   139     O    HOH A   227              2.05            
REMARK 500   OE2  GLU A   123     NH1  ARG A   126              2.09            
REMARK 500   OD1  ASN A    53     O    HOH A   235              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP B 787   CB    TRP B 787   CG      0.139                       
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    TRP B 787   CA  -  CB  -  CG  ANGL. DEV. =  13.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD1                                                    
REMARK 620 2 ASP A  22   OD1  75.9                                              
REMARK 620 3 ASP A  24   OD2  83.1  79.6                                        
REMARK 620 4 THR A  26   O    83.8 153.8  81.7                                  
REMARK 620 5 GLU A  31   OE2  94.3  76.1 155.4 122.5                            
REMARK 620 6 GLU A  31   OE1 117.2 126.8 148.5  77.2  52.8                      
REMARK 620 7 HOH A 195   O   157.6  81.8  90.3 116.5  82.9  78.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD2                                                    
REMARK 620 2 ASP A  58   OD2  82.3                                              
REMARK 620 3 ASN A  60   OD1  87.0  78.6                                        
REMARK 620 4 THR A  62   O    90.6 156.9  79.1                                  
REMARK 620 5 GLU A  67   OE1 109.4 122.9 153.7  80.2                            
REMARK 620 6 GLU A  67   OE2  90.6  73.4 152.0 128.9  51.5                      
REMARK 620 7 HOH A 175   O   159.3  77.8  83.4 105.5  86.6  89.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD2                                                    
REMARK 620 2 ASP A  95   OD1  84.9                                              
REMARK 620 3 ASN A  97   OD1  90.2  75.1                                        
REMARK 620 4 TYR A  99   O    90.4 156.5  82.0                                  
REMARK 620 5 GLU A 104   OE2  99.9 126.4 156.7  77.1                            
REMARK 620 6 GLU A 104   OE1  95.2  73.8 147.7 129.6  52.6                      
REMARK 620 7 HOH A 166   O   166.2  81.4  84.5 101.4  89.8  82.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 504  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD2                                                    
REMARK 620 2 ASP A 131   OD1  81.8                                              
REMARK 620 3 ASP A 133   OD2  92.5  78.2                                        
REMARK 620 4 GLN A 135   O    86.7 154.5  79.7                                  
REMARK 620 5 GLU A 140   OE1 110.0 124.1 149.5  81.2                            
REMARK 620 6 GLU A 140   OE2  85.7  77.1 155.2 124.7  51.1                      
REMARK 620 7 HOH A 159   O   165.7  84.7  80.0 103.8  81.6  96.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 149                 
DBREF  3SUI A    0   148  UNP    P62158   CALM_HUMAN       1    149             
DBREF  3SUI B  767   801  UNP    O35433   TRPV1_RAT      767    801             
SEQADV 3SUI GLY B  765  UNP  O35433              EXPRESSION TAG                 
SEQADV 3SUI PRO B  766  UNP  O35433              EXPRESSION TAG                 
SEQRES   1 A  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 A  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 A  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 A  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 A  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 A  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 A  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 A  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 A  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 A  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 A  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 A  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 B   37  GLY PRO GLU GLY VAL LYS ARG THR LEU SER PHE SER LEU          
SEQRES   2 B   37  ARG SER GLY ARG VAL SER GLY ARG ASN TRP LYS ASN PHE          
SEQRES   3 B   37  ALA LEU VAL PRO LEU LEU ARG ASP ALA SER THR                  
HET     CA  A 501       1                                                       
HET     CA  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     CA  A 504       1                                                       
HET    SO4  A 149       5                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   7  SO4    O4 S 2-                                                      
FORMUL   8  HOH   *91(H2 O)                                                     
HELIX    1   1 THR A    5  ASP A   20  1                                  16    
HELIX    2   2 THR A   28  LEU A   39  1                                  12    
HELIX    3   3 THR A   44  GLU A   54  1                                  11    
HELIX    4   4 ASP A   64  THR A   79  1                                  16    
HELIX    5   5 SER A   81  ASP A   93  1                                  13    
HELIX    6   6 SER A  101  GLY A  113  1                                  13    
HELIX    7   7 THR A  117  ASP A  129  1                                  13    
HELIX    8   8 TYR A  138  ALA A  147  1                                  10    
HELIX    9   9 TRP B  787  VAL B  793  1                                   7    
HELIX   10  10 PRO B  794  LEU B  796  5                                   3    
SHEET    1   A 2 TYR A  99  ILE A 100  0                                        
SHEET    2   A 2 VAL A 136  ASN A 137 -1  O  VAL A 136   N  ILE A 100           
LINK         OD1 ASP A  20                CA    CA A 501     1555   1555  2.37  
LINK         OD1 ASP A  22                CA    CA A 501     1555   1555  2.51  
LINK         OD2 ASP A  24                CA    CA A 501     1555   1555  2.42  
LINK         O   THR A  26                CA    CA A 501     1555   1555  2.30  
LINK         OE2 GLU A  31                CA    CA A 501     1555   1555  2.41  
LINK         OE1 GLU A  31                CA    CA A 501     1555   1555  2.48  
LINK         OD2 ASP A  56                CA    CA A 502     1555   1555  2.25  
LINK         OD2 ASP A  58                CA    CA A 502     1555   1555  2.35  
LINK         OD1 ASN A  60                CA    CA A 502     1555   1555  2.37  
LINK         O   THR A  62                CA    CA A 502     1555   1555  2.35  
LINK         OE1 GLU A  67                CA    CA A 502     1555   1555  2.38  
LINK         OE2 GLU A  67                CA    CA A 502     1555   1555  2.66  
LINK         OD2 ASP A  93                CA    CA A 503     1555   1555  2.32  
LINK         OD1 ASP A  95                CA    CA A 503     1555   1555  2.38  
LINK         OD1 ASN A  97                CA    CA A 503     1555   1555  2.37  
LINK         O   TYR A  99                CA    CA A 503     1555   1555  2.21  
LINK         OE2 GLU A 104                CA    CA A 503     1555   1555  2.44  
LINK         OE1 GLU A 104                CA    CA A 503     1555   1555  2.49  
LINK         OD2 ASP A 129                CA    CA A 504     1555   1555  2.24  
LINK         OD1 ASP A 131                CA    CA A 504     1555   1555  2.38  
LINK         OD2 ASP A 133                CA    CA A 504     1555   1555  2.32  
LINK         O   GLN A 135                CA    CA A 504     1555   1555  2.35  
LINK         OE1 GLU A 140                CA    CA A 504     1555   1555  2.44  
LINK         OE2 GLU A 140                CA    CA A 504     1555   1555  2.60  
LINK         O   HOH A 159                CA    CA A 504     1555   1555  2.46  
LINK         O   HOH A 166                CA    CA A 503     1555   1555  2.20  
LINK         O   HOH A 175                CA    CA A 502     1555   1555  2.14  
LINK         O   HOH A 195                CA    CA A 501     1555   1555  2.40  
SITE     1 AC1  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  6 GLU A  31  HOH A 195                                          
SITE     1 AC2  6 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  6 GLU A  67  HOH A 175                                          
SITE     1 AC3  6 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC3  6 GLU A 104  HOH A 166                                          
SITE     1 AC4  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC4  6 GLU A 140  HOH A 159                                          
SITE     1 AC5  3 GLN A  41  ASN A  42  ARG B 797                               
CRYST1   41.681   41.681  341.533  90.00  90.00 120.00 P 61 2 2     12          
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      0.023992  0.013852  0.000000        0.00000                         
SCALE2      0.000000  0.027703  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002928        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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