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Database: PDB
Entry: 5E1J
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Original site: 5E1J 
HEADER    METAL TRANSPORT                         29-SEP-15   5E1J              
TITLE     STRUCTURE OF VOLTAGE-GATED TWO-PORE CHANNEL TPC1 FROM ARABIDOPSIS     
TITLE    2 THALIANA                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TWO PORE CALCIUM CHANNEL PROTEIN 1;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CALCIUM CHANNEL PROTEIN 1,ATCCH1,FATTY ACID OXYGENATION UP- 
COMPND   5 REGULATED PROTEIN 2,VOLTAGE-DEPENDENT CALCIUM CHANNEL PROTEIN TPC1,  
COMPND   6 ATTPC1;                                                              
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: TPC1, CCH1, FOU2, AT4G03560, F9H3.19, T5L23.5;                 
SOURCE   6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SMD1163;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPICZ                                     
KEYWDS    TWO-PORE CHANNEL, VOLTAGE-GATED, CALCIUM MODULATION, METAL TRANSPORT  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.GUO,W.ZENG,Q.CHEN,C.LEE,L.CHEN,Y.YANG,Y.JIANG                       
REVDAT   4   06-SEP-17 5E1J    1       JRNL   REMARK                            
REVDAT   3   23-MAR-16 5E1J    1       JRNL                                     
REVDAT   2   06-JAN-16 5E1J    1       JRNL                                     
REVDAT   1   16-DEC-15 5E1J    0                                                
JRNL        AUTH   J.GUO,W.ZENG,Q.CHEN,C.LEE,L.CHEN,Y.YANG,C.CANG,D.REN,Y.JIANG 
JRNL        TITL   STRUCTURE OF THE VOLTAGE-GATED TWO-PORE CHANNEL TPC1 FROM    
JRNL        TITL 2 ARABIDOPSIS THALIANA.                                        
JRNL        REF    NATURE                        V. 531   196 2016              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   26689363                                                     
JRNL        DOI    10.1038/NATURE16446                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.31 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.31                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.71                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.920                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 77.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 22635                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.325                           
REMARK   3   R VALUE            (WORKING SET) : 0.325                           
REMARK   3   FREE R VALUE                     : 0.332                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1741                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 39.7153 -  7.5579    0.96     3339   173  0.2741 0.3110        
REMARK   3     2  7.5579 -  6.0056    1.00     3518   178  0.3522 0.4014        
REMARK   3     3  6.0056 -  5.2484    1.00     3496   183  0.3748 0.3487        
REMARK   3     4  5.2484 -  4.7694    1.00     3480   181  0.3061 0.3344        
REMARK   3     5  4.7694 -  4.4280    1.00     3463   204  0.2895 0.3257        
REMARK   3     6  4.4280 -  4.1673    1.00     3485   195  0.3236 0.2692        
REMARK   3     7  4.1673 -  3.9588    0.97     3354   188  0.3500 0.2987        
REMARK   3     8  3.9588 -  3.7866    0.83     2874   165  0.3609 0.3360        
REMARK   3     9  3.7866 -  3.6409    0.66     2334   124  0.3632 0.3533        
REMARK   3    10  3.6409 -  3.5154    0.49     1734    80  0.3750 0.4133        
REMARK   3    11  3.5154 -  3.4055    0.28      970    56  0.3841 0.3778        
REMARK   3    12  3.4055 -  3.3080    0.09      331    14  0.3768 0.3570        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.740           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 91.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           5097                                  
REMARK   3   ANGLE     :  0.854           6894                                  
REMARK   3   CHIRALITY :  0.030            803                                  
REMARK   3   PLANARITY :  0.005            849                                  
REMARK   3   DIHEDRAL  : 11.681           1758                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 32:91 )                            
REMARK   3    ORIGIN FOR THE GROUP (A): -34.5956 -25.0782  26.0597              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6668 T22:   2.0419                                     
REMARK   3      T33:   1.8308 T12:  -0.1187                                     
REMARK   3      T13:  -0.0527 T23:   0.6279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8221 L22:   0.7825                                     
REMARK   3      L33:   0.1903 L12:  -0.9697                                     
REMARK   3      L13:  -0.4188 L23:   0.3808                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2559 S12:  -1.2094 S13:  -1.4829                       
REMARK   3      S21:   0.3226 S22:  -0.3980 S23:   0.1199                       
REMARK   3      S31:   0.3121 S32:  -0.0507 S33:   0.1184                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 92:398 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -27.5427 -17.2753   8.2530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4175 T22:   0.5105                                     
REMARK   3      T33:   0.7420 T12:   0.0645                                     
REMARK   3      T13:  -0.1590 T23:  -0.2070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0025 L22:   1.2835                                     
REMARK   3      L33:   1.2087 L12:   0.0198                                     
REMARK   3      L13:   0.0355 L23:   0.0605                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3140 S12:  -0.5767 S13:  -1.1242                       
REMARK   3      S21:   0.2691 S22:   0.0045 S23:  -0.1441                       
REMARK   3      S31:   0.4323 S32:  -0.2139 S33:  -0.0482                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 399:547 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.7758   0.2121  37.7422              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9684 T22:   1.4557                                     
REMARK   3      T33:   0.6085 T12:  -0.3414                                     
REMARK   3      T13:  -0.3894 T23:  -0.3084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2273 L22:   0.3959                                     
REMARK   3      L33:   1.1104 L12:   0.0276                                     
REMARK   3      L13:   0.2685 L23:  -0.0526                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1712 S12:  -0.3113 S13:  -0.1339                       
REMARK   3      S21:   0.3821 S22:  -0.0295 S23:  -0.1892                       
REMARK   3      S31:   0.1561 S32:  -0.1691 S33:  -0.0930                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 548:686 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.5933  -9.6206   6.3042              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2497 T22:   0.4432                                     
REMARK   3      T33:   0.5208 T12:   0.0548                                     
REMARK   3      T13:  -0.1843 T23:  -0.3687                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5403 L22:   1.1603                                     
REMARK   3      L33:   0.9349 L12:   0.3850                                     
REMARK   3      L13:   0.2034 L23:   0.0463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0847 S12:  -0.1640 S13:  -0.0888                       
REMARK   3      S21:   0.1200 S22:   0.0940 S23:  -0.6370                       
REMARK   3      S31:   0.1318 S32:   0.3367 S33:  -0.3416                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5E1J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214168.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5-7.0                            
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34119                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 36.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG400, 150 MM BACL2, 100MM HEPES,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      108.62000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      108.62000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       44.21500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       79.42500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       44.21500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       79.42500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      108.62000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       44.21500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       79.42500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      108.62000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       44.21500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       79.42500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 66250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -176.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 BA    BA A 801  LIES ON A SPECIAL POSITION.                          
REMARK 375 BA    BA A 803  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 904  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     ASP A    17                                                      
REMARK 465     ARG A    18                                                      
REMARK 465     VAL A    19                                                      
REMARK 465     ARG A    20                                                      
REMARK 465     ARG A    21                                                      
REMARK 465     SER A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     ILE A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     HIS A    27                                                      
REMARK 465     GLY A    28                                                      
REMARK 465     THR A    29                                                      
REMARK 465     PRO A    30                                                      
REMARK 465     PHE A    31                                                      
REMARK 465     GLN A    54                                                      
REMARK 465     SER A    55                                                      
REMARK 465     SER A    56                                                      
REMARK 465     PHE A    57                                                      
REMARK 465     GLY A    58                                                      
REMARK 465     GLU A    59                                                      
REMARK 465     SER A    60                                                      
REMARK 465     ALA A    61                                                      
REMARK 465     LEU A   174                                                      
REMARK 465     SER A   175                                                      
REMARK 465     PRO A   176                                                      
REMARK 465     LEU A   177                                                      
REMARK 465     ALA A   178                                                      
REMARK 465     PHE A   179                                                      
REMARK 465     ASP A   180                                                      
REMARK 465     PHE A   181                                                      
REMARK 465     LEU A   182                                                      
REMARK 465     PRO A   183                                                      
REMARK 465     GLU A   403                                                      
REMARK 465     VAL A   404                                                      
REMARK 465     PRO A   405                                                      
REMARK 465     SER A   406                                                      
REMARK 465     LEU A   407                                                      
REMARK 465     PHE A   408                                                      
REMARK 465     GLU A   409                                                      
REMARK 465     HIS A   410                                                      
REMARK 465     PHE A   411                                                      
REMARK 465     PRO A   412                                                      
REMARK 465     GLN A   413                                                      
REMARK 465     ILE A   414                                                      
REMARK 465     ASP A   519                                                      
REMARK 465     GLU A   520                                                      
REMARK 465     ASN A   521                                                      
REMARK 465     THR A   522                                                      
REMARK 465     PHE A   523                                                      
REMARK 465     VAL A   591                                                      
REMARK 465     ASN A   592                                                      
REMARK 465     ALA A   593                                                      
REMARK 465     GLY A   594                                                      
REMARK 465     CYS A   687                                                      
REMARK 465     GLN A   688                                                      
REMARK 465     GLY A   689                                                      
REMARK 465     GLN A   690                                                      
REMARK 465     ASP A   691                                                      
REMARK 465     SER A   692                                                      
REMARK 465     GLN A   693                                                      
REMARK 465     GLU A   694                                                      
REMARK 465     LYS A   695                                                      
REMARK 465     ARG A   696                                                      
REMARK 465     ASN A   697                                                      
REMARK 465     ARG A   698                                                      
REMARK 465     ARG A   699                                                      
REMARK 465     ARG A   700                                                      
REMARK 465     SER A   701                                                      
REMARK 465     ALA A   702                                                      
REMARK 465     GLY A   703                                                      
REMARK 465     SER A   704                                                      
REMARK 465     LYS A   705                                                      
REMARK 465     SER A   706                                                      
REMARK 465     ARG A   707                                                      
REMARK 465     SER A   708                                                      
REMARK 465     GLN A   709                                                      
REMARK 465     ARG A   710                                                      
REMARK 465     VAL A   711                                                      
REMARK 465     ASP A   712                                                      
REMARK 465     THR A   713                                                      
REMARK 465     LEU A   714                                                      
REMARK 465     LEU A   715                                                      
REMARK 465     HIS A   716                                                      
REMARK 465     HIS A   717                                                      
REMARK 465     MET A   718                                                      
REMARK 465     LEU A   719                                                      
REMARK 465     GLY A   720                                                      
REMARK 465     ASP A   721                                                      
REMARK 465     GLU A   722                                                      
REMARK 465     LEU A   723                                                      
REMARK 465     SER A   724                                                      
REMARK 465     LYS A   725                                                      
REMARK 465     PRO A   726                                                      
REMARK 465     GLU A   727                                                      
REMARK 465     CYS A   728                                                      
REMARK 465     SER A   729                                                      
REMARK 465     THR A   730                                                      
REMARK 465     SER A   731                                                      
REMARK 465     ASP A   732                                                      
REMARK 465     THR A   733                                                      
REMARK 465     SER A   734                                                      
REMARK 465     THR A   735                                                      
REMARK 465     ALA A   736                                                      
REMARK 465     GLY A   737                                                      
REMARK 465     LEU A   738                                                      
REMARK 465     VAL A   739                                                      
REMARK 465     PRO A   740                                                      
REMARK 465     ARG A   741                                                      
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     GLN A  32    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  33    CG   CD   CE   NZ                                   
REMARK 470     PRO A  48    CG   CD                                             
REMARK 470     VAL A  49    CG1  CG2                                            
REMARK 470     GLU A  50    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  51    CG1  CG2  CD1                                       
REMARK 470     LEU A  52    CG   CD1  CD2                                       
REMARK 470     ASP A  53    CG   OD1  OD2                                       
REMARK 470     ARG A  69    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A  78    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TRP A  92    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A  92    CZ3  CH2                                            
REMARK 470     SER A 100    OG                                                  
REMARK 470     CYS A 101    SG                                                  
REMARK 470     LYS A 102    CG   CD   CE   NZ                                   
REMARK 470     ASP A 103    CG   OD1  OD2                                       
REMARK 470     ARG A 104    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 112    CG   CD1  CD2                                       
REMARK 470     PHE A 171    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TYR A 173    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 276    CG   CD   CE   NZ                                   
REMARK 470     ILE A 342    CG1  CG2  CD1                                       
REMARK 470     ARG A 379    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 381    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 400    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 401    CG   CD   CE   NZ                                   
REMARK 470     GLU A 402    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 415    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TRP A 492    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 492    CZ3  CH2                                            
REMARK 470     PHE A 524    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TRP A 529    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 529    CZ3  CH2                                            
REMARK 470     PHE A 599    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE A 611    CG   CD1  CD2  CE1  CE2  CZ                         
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    TYR A    63     CD2  PHE A    67              1.85            
REMARK 500   OD2  ASP A   337     ND2  ASN A   339              2.01            
REMARK 500   O    PHE A   195     OG   SER A   198              2.03            
REMARK 500   OH   TYR A   216     O    VAL A   657              2.19            
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    LEU A  37   CB  -  CG  -  CD1 ANGL. DEV. =  11.2 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    GLU A  50     -149.68   -103.92                                   
REMARK 500    ILE A  51       55.20   -159.85                                   
REMARK 500    PRO A  99       72.00      6.65                                   
REMARK 500    ASP A 105     -157.86   -116.83                                   
REMARK 500    TYR A 106       74.95   -119.76                                   
REMARK 500    PRO A 113     -166.53   -105.50                                   
REMARK 500    ARG A 185      -67.24    -92.30                                   
REMARK 500    PHE A 238       53.61   -116.24                                   
REMARK 500    GLN A 243     -151.71   -128.94                                   
REMARK 500    PHE A 248      -58.36    -29.45                                   
REMARK 500    THR A 249       51.06   -116.60                                   
REMARK 500    SER A 250     -131.90     55.24                                   
REMARK 500    ASN A 266       23.84   -148.79                                   
REMARK 500    ARG A 358      -87.50   -121.72                                   
REMARK 500    PRO A 361      -96.33    -98.48                                   
REMARK 500    LYS A 365     -159.62   -131.95                                   
REMARK 500    ASN A 384     -169.49   -104.21                                   
REMARK 500    SER A 417       37.82    -90.04                                   
REMARK 500    ALA A 418      -59.52   -123.58                                   
REMARK 500    SER A 458       47.39   -104.45                                   
REMARK 500    LEU A 534       34.82    -93.65                                   
REMARK 500    PHE A 587       52.31   -100.12                                   
REMARK 500    LEU A 603     -161.33   -115.50                                   
REMARK 500    ALA A 604      -75.49    -65.98                                   
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 810  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 120   OG                                                     
REMARK 620 2 GLU A 124   OE1  93.2                                              
REMARK 620 3 GLU A 124   OE2  93.1  55.3                                        
REMARK 620 4 ASP A 170   OD2 141.0 119.3 122.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 809  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 335   OD1                                                    
REMARK 620 2 ASP A 337   OD1  63.5                                              
REMARK 620 3 ASP A 337   OD2 105.6  55.5                                        
REMARK 620 4 ASN A 339   OD1  63.0  96.5  85.3                                  
REMARK 620 5 GLU A 341   O    78.9 142.1 147.4  67.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA A 805  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 454   OD1                                                    
REMARK 620 2 ASP A 454   OD2  46.9                                              
REMARK 620 3 GLU A 528   OE1  76.5  68.5                                        
REMARK 620 4 ASP A 240   OD2  85.9 132.6 100.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA A 804  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 457   OE2                                                    
REMARK 620 2 GLU A 239   O   175.4                                              
REMARK 620 3 ASP A 240   OD1 175.1   0.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA A 801  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 605   OE1                                                    
REMARK 620 2 GLU A 605   OE1   0.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA A 803  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 903   O                                                      
REMARK 620 2 HOH A 904   O    90.7                                              
REMARK 620 3 HOH A 903   O   178.5  90.7                                        
REMARK 620 4 HOH A 904   O    90.7   0.0  90.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              BA A 803  BA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 902   O                                                      
REMARK 620 2 HOH A 901   O   122.0                                              
REMARK 620 3 HOH A 901   O    84.7  92.9                                        
REMARK 620 4 HOH A 902   O   142.9  84.7 122.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BA A 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BA A 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BA A 804                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BA A 805                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BA A 806                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 809                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 810                  
DBREF  5E1J A    1   733  UNP    Q94KI8   TPC1_ARATH       1    733             
SEQADV 5E1J SER A  734  UNP  Q94KI8              EXPRESSION TAG                 
SEQADV 5E1J THR A  735  UNP  Q94KI8              EXPRESSION TAG                 
SEQADV 5E1J ALA A  736  UNP  Q94KI8              EXPRESSION TAG                 
SEQADV 5E1J GLY A  737  UNP  Q94KI8              EXPRESSION TAG                 
SEQADV 5E1J LEU A  738  UNP  Q94KI8              EXPRESSION TAG                 
SEQADV 5E1J VAL A  739  UNP  Q94KI8              EXPRESSION TAG                 
SEQADV 5E1J PRO A  740  UNP  Q94KI8              EXPRESSION TAG                 
SEQADV 5E1J ARG A  741  UNP  Q94KI8              EXPRESSION TAG                 
SEQRES   1 A  741  MET GLU ASP PRO LEU ILE GLY ARG ASP SER LEU GLY GLY          
SEQRES   2 A  741  GLY GLY THR ASP ARG VAL ARG ARG SER GLU ALA ILE THR          
SEQRES   3 A  741  HIS GLY THR PRO PHE GLN LYS ALA ALA ALA LEU VAL ASP          
SEQRES   4 A  741  LEU ALA GLU ASP GLY ILE GLY LEU PRO VAL GLU ILE LEU          
SEQRES   5 A  741  ASP GLN SER SER PHE GLY GLU SER ALA ARG TYR TYR PHE          
SEQRES   6 A  741  ILE PHE THR ARG LEU ASP LEU ILE TRP SER LEU ASN TYR          
SEQRES   7 A  741  PHE ALA LEU LEU PHE LEU ASN PHE PHE GLU GLN PRO LEU          
SEQRES   8 A  741  TRP CYS GLU LYS ASN PRO LYS PRO SER CYS LYS ASP ARG          
SEQRES   9 A  741  ASP TYR TYR TYR LEU GLY GLU LEU PRO TYR LEU THR ASN          
SEQRES  10 A  741  ALA GLU SER ILE ILE TYR GLU VAL ILE THR LEU ALA ILE          
SEQRES  11 A  741  LEU LEU VAL HIS THR PHE PHE PRO ILE SER TYR GLU GLY          
SEQRES  12 A  741  SER ARG ILE PHE TRP THR SER ARG LEU ASN LEU VAL LYS          
SEQRES  13 A  741  VAL ALA CYS VAL VAL ILE LEU PHE VAL ASP VAL LEU VAL          
SEQRES  14 A  741  ASP PHE LEU TYR LEU SER PRO LEU ALA PHE ASP PHE LEU          
SEQRES  15 A  741  PRO PHE ARG ILE ALA PRO TYR VAL ARG VAL ILE ILE PHE          
SEQRES  16 A  741  ILE LEU SER ILE ARG GLU LEU ARG ASP THR LEU VAL LEU          
SEQRES  17 A  741  LEU SER GLY MET LEU GLY THR TYR LEU ASN ILE LEU ALA          
SEQRES  18 A  741  LEU TRP MET LEU PHE LEU LEU PHE ALA SER TRP ILE ALA          
SEQRES  19 A  741  PHE VAL MET PHE GLU ASP THR GLN GLN GLY LEU THR VAL          
SEQRES  20 A  741  PHE THR SER TYR GLY ALA THR LEU TYR GLN MET PHE ILE          
SEQRES  21 A  741  LEU PHE THR THR SER ASN ASN PRO ASP VAL TRP ILE PRO          
SEQRES  22 A  741  ALA TYR LYS SER SER ARG TRP SER SER VAL PHE PHE VAL          
SEQRES  23 A  741  LEU TYR VAL LEU ILE GLY VAL TYR PHE VAL THR ASN LEU          
SEQRES  24 A  741  ILE LEU ALA VAL VAL TYR ASP SER PHE LYS GLU GLN LEU          
SEQRES  25 A  741  ALA LYS GLN VAL SER GLY MET ASP GLN MET LYS ARG ARG          
SEQRES  26 A  741  MET LEU GLU LYS ALA PHE GLY LEU ILE ASP SER ASP LYS          
SEQRES  27 A  741  ASN GLY GLU ILE ASP LYS ASN GLN CYS ILE LYS LEU PHE          
SEQRES  28 A  741  GLU GLN LEU THR ASN TYR ARG THR LEU PRO LYS ILE SER          
SEQRES  29 A  741  LYS GLU GLU PHE GLY LEU ILE PHE ASP GLU LEU ASP ASP          
SEQRES  30 A  741  THR ARG ASP PHE LYS ILE ASN LYS ASP GLU PHE ALA ASP          
SEQRES  31 A  741  LEU CYS GLN ALA ILE ALA LEU ARG PHE GLN LYS GLU GLU          
SEQRES  32 A  741  VAL PRO SER LEU PHE GLU HIS PHE PRO GLN ILE TYR HIS          
SEQRES  33 A  741  SER ALA LEU SER GLN GLN LEU ARG ALA PHE VAL ARG SER          
SEQRES  34 A  741  PRO ASN PHE GLY TYR ALA ILE SER PHE ILE LEU ILE ILE          
SEQRES  35 A  741  ASN PHE ILE ALA VAL VAL VAL GLU THR THR LEU ASP ILE          
SEQRES  36 A  741  GLU GLU SER SER ALA GLN LYS PRO TRP GLN VAL ALA GLU          
SEQRES  37 A  741  PHE VAL PHE GLY TRP ILE TYR VAL LEU GLU MET ALA LEU          
SEQRES  38 A  741  LYS ILE TYR THR TYR GLY PHE GLU ASN TYR TRP ARG GLU          
SEQRES  39 A  741  GLY ALA ASN ARG PHE ASP PHE LEU VAL THR TRP VAL ILE          
SEQRES  40 A  741  VAL ILE GLY GLU THR ALA THR PHE ILE THR PRO ASP GLU          
SEQRES  41 A  741  ASN THR PHE PHE SER ASN GLY GLU TRP ILE ARG TYR LEU          
SEQRES  42 A  741  LEU LEU ALA ARG MET LEU ARG LEU ILE ARG LEU LEU MET          
SEQRES  43 A  741  ASN VAL GLN ARG TYR ARG ALA PHE ILE ALA THR PHE ILE          
SEQRES  44 A  741  THR LEU ILE PRO SER LEU MET PRO TYR LEU GLY THR ILE          
SEQRES  45 A  741  PHE CYS VAL LEU CYS ILE TYR CYS SER ILE GLY VAL GLN          
SEQRES  46 A  741  VAL PHE GLY GLY LEU VAL ASN ALA GLY ASN LYS LYS LEU          
SEQRES  47 A  741  PHE GLU THR GLU LEU ALA GLU ASP ASP TYR LEU LEU PHE          
SEQRES  48 A  741  ASN PHE ASN ASP TYR PRO ASN GLY MET VAL THR LEU PHE          
SEQRES  49 A  741  ASN LEU LEU VAL MET GLY ASN TRP GLN VAL TRP MET GLU          
SEQRES  50 A  741  SER TYR LYS ASP LEU THR GLY THR TRP TRP SER ILE THR          
SEQRES  51 A  741  TYR PHE VAL SER PHE TYR VAL ILE THR ILE LEU LEU LEU          
SEQRES  52 A  741  LEU ASN LEU VAL VAL ALA PHE VAL LEU GLU ALA PHE PHE          
SEQRES  53 A  741  THR GLU LEU ASP LEU GLU GLU GLU GLU LYS CYS GLN GLY          
SEQRES  54 A  741  GLN ASP SER GLN GLU LYS ARG ASN ARG ARG ARG SER ALA          
SEQRES  55 A  741  GLY SER LYS SER ARG SER GLN ARG VAL ASP THR LEU LEU          
SEQRES  56 A  741  HIS HIS MET LEU GLY ASP GLU LEU SER LYS PRO GLU CYS          
SEQRES  57 A  741  SER THR SER ASP THR SER THR ALA GLY LEU VAL PRO ARG          
HET     BA  A 801       1                                                       
HET     BA  A 802       1                                                       
HET     BA  A 803       2                                                       
HET     BA  A 804       1                                                       
HET     BA  A 805       1                                                       
HET     BA  A 806       1                                                       
HET     BA  A 807       1                                                       
HET     BA  A 808       1                                                       
HET     CA  A 809       1                                                       
HET     CA  A 810       1                                                       
HETNAM      BA BARIUM ION                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   BA    8(BA 2+)                                                     
FORMUL  10   CA    2(CA 2+)                                                     
FORMUL  12  HOH   *4(H2 O)                                                      
HELIX    1 AA1 GLN A   32  GLY A   46  1                                  15    
HELIX    2 AA2 TYR A   63  TRP A   92  1                                  30    
HELIX    3 AA3 THR A  116  PHE A  137  1                                  22    
HELIX    4 AA4 PRO A  138  SER A  140  5                                   3    
HELIX    5 AA5 GLY A  143  TRP A  148  1                                   6    
HELIX    6 AA6 SER A  150  TYR A  173  1                                  24    
HELIX    7 AA7 PRO A  188  ILE A  199  1                                  12    
HELIX    8 AA8 ILE A  199  PHE A  238  1                                  40    
HELIX    9 AA9 GLN A  243  PHE A  248  1                                   6    
HELIX   10 AB1 THR A  249  THR A  263  1                                  15    
HELIX   11 AB2 ASN A  266  TRP A  271  1                                   6    
HELIX   12 AB3 TRP A  271  SER A  278  1                                   8    
HELIX   13 AB4 TRP A  280  TYR A  294  1                                  15    
HELIX   14 AB5 PHE A  295  ASP A  335  1                                  41    
HELIX   15 AB6 ASP A  343  ARG A  358  1                                  16    
HELIX   16 AB7 LYS A  365  ASP A  373  1                                   9    
HELIX   17 AB8 ASP A  386  PHE A  399  1                                  14    
HELIX   18 AB9 SER A  429  ILE A  455  1                                  27    
HELIX   19 AC1 GLN A  461  GLY A  487  1                                  27    
HELIX   20 AC2 GLU A  489  GLU A  494  1                                   6    
HELIX   21 AC3 GLU A  494  PHE A  515  1                                  22    
HELIX   22 AC4 SER A  525  LEU A  533  1                                   9    
HELIX   23 AC5 LEU A  534  VAL A  548  5                                  15    
HELIX   24 AC6 TYR A  551  LEU A  565  1                                  15    
HELIX   25 AC7 LEU A  565  PHE A  587  1                                  23    
HELIX   26 AC8 LYS A  597  GLU A  602  1                                   6    
HELIX   27 AC9 GLU A  605  LEU A  610  1                                   6    
HELIX   28 AD1 ASP A  615  VAL A  628  1                                  14    
HELIX   29 AD2 TRP A  632  GLY A  644  1                                  13    
HELIX   30 AD3 THR A  645  TRP A  647  5                                   3    
HELIX   31 AD4 SER A  648  ILE A  660  1                                  13    
HELIX   32 AD5 LEU A  662  GLU A  685  1                                  24    
SHEET    1 AA1 2 GLU A 341  ILE A 342  0                                        
SHEET    2 AA1 2 ILE A 383  ASN A 384 -1  O  ILE A 383   N  ILE A 342           
LINK         OG  SER A 120                CA    CA A 810     1555   1555  2.38  
LINK         OE1 GLU A 124                CA    CA A 810     1555   1555  2.36  
LINK         OE2 GLU A 124                CA    CA A 810     1555   1555  2.36  
LINK         OD2 ASP A 170                CA    CA A 810     1555   1555  2.36  
LINK         OD1 ASP A 335                CA    CA A 809     1555   1555  2.36  
LINK         OD1 ASP A 337                CA    CA A 809     1555   1555  2.36  
LINK         OD2 ASP A 337                CA    CA A 809     1555   1555  2.36  
LINK         OD1 ASN A 339                CA    CA A 809     1555   1555  2.38  
LINK         O   GLU A 341                CA    CA A 809     1555   1555  2.36  
LINK         OD1 ASP A 454                BA    BA A 805     1555   1555  2.75  
LINK         OD2 ASP A 454                BA    BA A 805     1555   1555  2.75  
LINK         OE2 GLU A 457                BA    BA A 804     1555   1555  2.75  
LINK         OE1 GLU A 528                BA    BA A 805     1555   1555  2.75  
LINK         OE1 GLU A 605                BA    BA A 801     1555   1555  2.75  
LINK        BA  A BA A 803                 O   HOH A 903     1555   1555  2.99  
LINK        BA  A BA A 803                 O   HOH A 904     1555   1555  2.75  
LINK        BA  B BA A 803                 O   HOH A 902     1555   1555  2.75  
LINK        BA  B BA A 803                 O   HOH A 901     1555   1555  2.75  
LINK         O   GLU A 239                BA    BA A 804     1555   4555  2.75  
LINK         OD1 ASP A 240                BA    BA A 804     1555   4555  2.75  
LINK         OD2 ASP A 240                BA    BA A 805     1555   4555  2.75  
LINK         OE1 GLU A 605                BA    BA A 801     1555   4555  2.75  
LINK        BA  A BA A 803                 O   HOH A 903     1555   4555  2.99  
LINK        BA  A BA A 803                 O   HOH A 904     1555   4555  2.75  
LINK        BA  B BA A 803                 O   HOH A 901     1555   4555  2.75  
LINK        BA  B BA A 803                 O   HOH A 902     1555   4555  2.75  
CISPEP   1 CYS A  101    LYS A  102          0         0.47                     
CISPEP   2 ASP A  103    ARG A  104          0         1.78                     
CISPEP   3 LEU A  112    PRO A  113          0        -4.47                     
CISPEP   4 GLN A  242    GLN A  243          0         1.81                     
CISPEP   5 ARG A  379    ASP A  380          0         6.67                     
CISPEP   6 ASP A  380    PHE A  381          0       -15.55                     
CISPEP   7 SER A  459    ALA A  460          0        -1.85                     
CISPEP   8 GLU A  602    LEU A  603          0         0.11                     
SITE     1 AC1  1 GLU A 605                                                     
SITE     1 AC2  4 HOH A 901  HOH A 902  HOH A 903  HOH A 904                    
SITE     1 AC3  3 GLU A 239  ASP A 240  GLU A 457                               
SITE     1 AC4  3 ASP A 240  ASP A 454  GLU A 528                               
SITE     1 AC5  1 ASN A 339                                                     
SITE     1 AC6  4 ASP A 335  ASP A 337  ASN A 339  GLU A 341                    
SITE     1 AC7  3 SER A 120  GLU A 124  ASP A 170                               
CRYST1   88.430  158.850  217.240  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011308  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006295  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004603        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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