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Database: PDB
Entry: 3RV5
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HEADER    CONTRACTILE PROTEIN                     06-MAY-11   3RV5              
TITLE     CRYSTAL STRUCTURE OF HUMAN CARDIAC TROPONIN C REGULATORY DOMAIN IN    
TITLE    2 COMPLEX WITH CADMIUM AND DEOXYCHOLIC ACID                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TROPONIN C, SLOW SKELETAL AND CARDIAC MUSCLES;             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN (N-CTNC), UNP RESIDUES 1-89;             
COMPND   5 SYNONYM: TN-C;                                                       
COMPND   6 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: TNNC, TNNC1, TNNC1 (AMINO ACIDS 1-89);                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    HELIX-LOOP-HELIX EF-HAND MOTIF, METAL ION COORDINATION, CALCIUM       
KEYWDS   2 SENSOR, CONTRACTILE PROTEIN                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.Y.LI,J.LEE,D.BOREK,Z.OTWINOWSKI,G.TIBBITS,M.PAETZEL                 
REVDAT   5   16-NOV-11 3RV5    1       JRNL                                     
REVDAT   4   26-OCT-11 3RV5    1       JRNL                                     
REVDAT   3   14-SEP-11 3RV5    1                                                
REVDAT   2   07-SEP-11 3RV5    1       JRNL   TITLE                             
REVDAT   1   31-AUG-11 3RV5    0                                                
JRNL        AUTH   A.Y.LI,J.LEE,D.BOREK,Z.OTWINOWSKI,G.F.TIBBITS,M.PAETZEL      
JRNL        TITL   CRYSTAL STRUCTURE OF CARDIAC TROPONIN C REGULATORY DOMAIN IN 
JRNL        TITL 2 COMPLEX WITH CADMIUM AND DEOXYCHOLIC ACID REVEALS NOVEL      
JRNL        TITL 3 CONFORMATION.                                                
JRNL        REF    J.MOL.BIOL.                   V. 413   699 2011              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   21920370                                                     
JRNL        DOI    10.1016/J.JMB.2011.08.049                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 20909                          
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) : 0.228                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1128                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1541                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 84                           
REMARK   3   BIN FREE R VALUE                    : 0.2650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2518                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 164                                     
REMARK   3   SOLVENT ATOMS            : 133                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.69000                                             
REMARK   3    B22 (A**2) : 1.52000                                              
REMARK   3    B33 (A**2) : -0.84000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
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): 0.274         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.232         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.150         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.948         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.879                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2815 ; 0.032 ; 0.023       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3661 ; 1.887 ; 2.050       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   318 ; 5.976 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   132 ;40.992 ;27.273       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   488 ;18.301 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ; 8.612 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   430 ; 0.123 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1934 ; 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):  1638 ; 1.338 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2554 ; 1.509 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1173 ; 4.030 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1107 ; 4.325 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A    15                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.1437  13.2906 -16.7578              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2294 T22:   0.2204                                     
REMARK   3      T33:   0.2493 T12:  -0.0029                                     
REMARK   3      T13:   0.0099 T23:  -0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0341 L22:   1.6549                                     
REMARK   3      L33:   3.3316 L12:   0.3324                                     
REMARK   3      L13:  -0.1029 L23:   0.3967                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0115 S12:   0.4064 S13:   0.1484                       
REMARK   3      S21:  -0.4134 S22:  -0.0036 S23:   0.2872                       
REMARK   3      S31:  -0.0986 S32:  -0.1668 S33:  -0.0080                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    16        A    25                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.4587  12.6204  -5.8927              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1499 T22:   0.1291                                     
REMARK   3      T33:   0.1304 T12:  -0.0011                                     
REMARK   3      T13:  -0.0047 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7571 L22:   3.2705                                     
REMARK   3      L33:   3.3306 L12:  -1.3302                                     
REMARK   3      L13:   0.4860 L23:   0.2382                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0916 S12:   0.1619 S13:  -0.4296                       
REMARK   3      S21:  -0.1505 S22:   0.0238 S23:  -0.0945                       
REMARK   3      S31:   0.2650 S32:   0.0545 S33:   0.0677                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    26        A    48                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.3977  20.4410  -1.5538              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1043 T22:   0.0949                                     
REMARK   3      T33:   0.0837 T12:   0.0035                                     
REMARK   3      T13:  -0.0018 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6671 L22:   0.4912                                     
REMARK   3      L33:   0.2240 L12:   0.8747                                     
REMARK   3      L13:  -0.2187 L23:   0.1645                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0050 S12:  -0.0370 S13:  -0.1104                       
REMARK   3      S21:   0.0196 S22:  -0.0190 S23:  -0.0497                       
REMARK   3      S31:   0.0625 S32:   0.0242 S33:   0.0240                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    49        A    63                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.6065  31.1948  -7.3507              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2375 T22:   0.1829                                     
REMARK   3      T33:   0.1765 T12:  -0.0107                                     
REMARK   3      T13:  -0.0001 T23:   0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1442 L22:   0.6144                                     
REMARK   3      L33:   0.1582 L12:  -1.9721                                     
REMARK   3      L13:   0.9190 L23:  -0.2048                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0600 S12:   0.3946 S13:   0.2741                       
REMARK   3      S21:  -0.1430 S22:  -0.0931 S23:  -0.0642                       
REMARK   3      S31:  -0.0855 S32:   0.0719 S33:   0.0330                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    64        A    80                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.8696  24.7572  -7.3017              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1156 T22:   0.1231                                     
REMARK   3      T33:   0.1233 T12:  -0.0006                                     
REMARK   3      T13:   0.0014 T23:   0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4758 L22:   2.6514                                     
REMARK   3      L33:   3.2255 L12:   0.5345                                     
REMARK   3      L13:   0.5802 L23:   1.4951                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0456 S12:   0.0211 S13:   0.2948                       
REMARK   3      S21:  -0.1380 S22:  -0.0259 S23:  -0.0213                       
REMARK   3      S31:  -0.3822 S32:  -0.0492 S33:  -0.0196                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    81        A    85                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4600  23.6766 -17.4914              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3895 T22:   0.2557                                     
REMARK   3      T33:   0.4993 T12:  -0.0215                                     
REMARK   3      T13:   0.1796 T23:  -0.0314                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.1501 L22:   4.8615                                     
REMARK   3      L33:   9.2685 L12:   3.6866                                     
REMARK   3      L13:  -0.8972 L23:  -5.3387                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0871 S12:   0.5307 S13:  -0.1010                       
REMARK   3      S21:  -0.5952 S22:  -0.1050 S23:  -0.7424                       
REMARK   3      S31:   0.2605 S32:   0.5725 S33:   0.1921                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     5        B    19                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9422  19.8790 -32.6952              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3098 T22:   0.2919                                     
REMARK   3      T33:   0.3301 T12:   0.0108                                     
REMARK   3      T13:   0.0295 T23:   0.0471                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1332 L22:   1.5728                                     
REMARK   3      L33:   3.3923 L12:   0.7740                                     
REMARK   3      L13:  -1.7699 L23:   0.5664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0179 S12:   0.0525 S13:   0.0455                       
REMARK   3      S21:  -0.1079 S22:   0.0700 S23:  -0.3738                       
REMARK   3      S31:   0.1156 S32:   0.3153 S33:  -0.0879                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    20        B    48                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9297  13.6954 -15.8513              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1111 T22:   0.1324                                     
REMARK   3      T33:   0.1358 T12:   0.0015                                     
REMARK   3      T13:   0.0047 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0288 L22:   1.9603                                     
REMARK   3      L33:   1.8174 L12:  -0.1056                                     
REMARK   3      L13:   0.7590 L23:   0.4323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0054 S12:   0.1750 S13:  -0.0422                       
REMARK   3      S21:  -0.2069 S22:  -0.0067 S23:  -0.0834                       
REMARK   3      S31:   0.0741 S32:   0.0588 S33:   0.0122                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    49        B    54                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.3356   1.7010 -21.3899              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2682 T22:   0.2566                                     
REMARK   3      T33:   0.2704 T12:   0.0049                                     
REMARK   3      T13:   0.0283 T23:  -0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2098 L22:   8.7481                                     
REMARK   3      L33:  11.6937 L12:   1.0053                                     
REMARK   3      L13:  -1.1999 L23: -10.0051                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0428 S12:   0.1011 S13:   0.0976                       
REMARK   3      S21:  -0.0423 S22:  -0.0390 S23:  -0.1144                       
REMARK   3      S31:  -0.1703 S32:   0.1227 S33:  -0.0038                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    55        B    64                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.6069   0.0544 -11.6031              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1851 T22:   0.1801                                     
REMARK   3      T33:   0.1847 T12:   0.0026                                     
REMARK   3      T13:   0.0099 T23:   0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8534 L22:   2.1319                                     
REMARK   3      L33:   4.1828 L12:   1.6672                                     
REMARK   3      L13:   3.8056 L23:   2.2794                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0463 S12:   0.0854 S13:  -0.1708                       
REMARK   3      S21:   0.0059 S22:   0.0139 S23:  -0.1043                       
REMARK   3      S31:   0.1467 S32:   0.1022 S33:  -0.0603                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    65        B    74                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.5572   7.4583  -2.7898              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1428 T22:   0.1666                                     
REMARK   3      T33:   0.2257 T12:  -0.0159                                     
REMARK   3      T13:  -0.0401 T23:   0.0434                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8893 L22:   6.8597                                     
REMARK   3      L33:   3.3231 L12:   1.1658                                     
REMARK   3      L13:  -0.9456 L23:  -2.8472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0021 S12:  -0.2268 S13:  -0.3632                       
REMARK   3      S21:   0.2233 S22:  -0.0907 S23:  -0.2978                       
REMARK   3      S31:   0.3980 S32:   0.1476 S33:   0.0886                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    75        B    82                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7273  10.4754  -8.4178              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2850 T22:   0.1126                                     
REMARK   3      T33:   0.2329 T12:   0.0331                                     
REMARK   3      T13:   0.1482 T23:   0.0302                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4176 L22:   5.3340                                     
REMARK   3      L33:   2.3582 L12:  -2.8669                                     
REMARK   3      L13:   1.6768 L23:   1.2648                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1057 S12:   0.5174 S13:  -0.1380                       
REMARK   3      S21:  -0.4333 S22:  -0.0073 S23:  -0.4713                       
REMARK   3      S31:   0.1764 S32:   0.4455 S33:  -0.0984                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     3        C    19                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.0093  20.4839 -16.5263              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2074 T22:   0.1683                                     
REMARK   3      T33:   0.2430 T12:   0.0023                                     
REMARK   3      T13:   0.0043 T23:  -0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8341 L22:   0.5003                                     
REMARK   3      L33:   2.1470 L12:  -0.9204                                     
REMARK   3      L13:  -1.1188 L23:   0.0202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0025 S12:   0.0232 S13:   0.0784                       
REMARK   3      S21:   0.0359 S22:   0.0190 S23:   0.2540                       
REMARK   3      S31:   0.0381 S32:  -0.3006 S33:  -0.0165                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    20        C    35                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.0010  18.5386 -34.8117              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1598 T22:   0.1553                                     
REMARK   3      T33:   0.1952 T12:   0.0015                                     
REMARK   3      T13:  -0.0003 T23:   0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0187 L22:   2.0602                                     
REMARK   3      L33:   9.1553 L12:  -0.0080                                     
REMARK   3      L13:   0.8318 L23:   1.9552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0013 S12:  -0.1172 S13:   0.1239                       
REMARK   3      S21:   0.0927 S22:   0.0023 S23:   0.0532                       
REMARK   3      S31:  -0.1877 S32:  -0.0288 S33:  -0.0036                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    36        C    51                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.9019   9.4839 -31.1489              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2186 T22:   0.2176                                     
REMARK   3      T33:   0.2441 T12:  -0.0061                                     
REMARK   3      T13:   0.0056 T23:   0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9599 L22:   1.6200                                     
REMARK   3      L33:   6.0381 L12:  -0.4010                                     
REMARK   3      L13:   1.6658 L23:   0.5347                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0092 S12:  -0.3199 S13:  -0.0871                       
REMARK   3      S21:   0.2941 S22:   0.0116 S23:  -0.0761                       
REMARK   3      S31:   0.1093 S32:   0.0780 S33:  -0.0024                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    52        C    67                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.7547   1.6027 -38.3804              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3069 T22:   0.3019                                     
REMARK   3      T33:   0.3233 T12:  -0.0002                                     
REMARK   3      T13:  -0.0010 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3438 L22:   0.2269                                     
REMARK   3      L33:   2.9376 L12:  -0.2485                                     
REMARK   3      L13:   0.9993 L23:  -0.6839                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0224 S12:  -0.1048 S13:  -0.0626                       
REMARK   3      S21:  -0.0387 S22:   0.0638 S23:   0.1640                       
REMARK   3      S31:   0.0356 S32:  -0.3406 S33:  -0.0862                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    68        C    79                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.1356  10.3035 -44.3062              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1888 T22:   0.1845                                     
REMARK   3      T33:   0.1846 T12:  -0.0118                                     
REMARK   3      T13:   0.0010 T23:   0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0815 L22:   1.9721                                     
REMARK   3      L33:   2.6978 L12:  -0.0317                                     
REMARK   3      L13:   1.3782 L23:  -1.0343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0301 S12:   0.1390 S13:  -0.3973                       
REMARK   3      S21:  -0.0174 S22:  -0.0526 S23:   0.1114                       
REMARK   3      S31:   0.2879 S32:   0.0368 S33:   0.0826                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    80        C    85                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.9651   9.1824 -35.8811              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4718 T22:   0.3403                                     
REMARK   3      T33:   0.4131 T12:  -0.0435                                     
REMARK   3      T13:   0.1029 T23:  -0.0343                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.5459 L22:   4.0671                                     
REMARK   3      L33:   6.9528 L12:   2.6787                                     
REMARK   3      L13:  -0.6316 L23:  -4.6306                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0615 S12:  -0.5234 S13:   0.0593                       
REMARK   3      S21:   0.5055 S22:   0.0426 S23:   0.4016                       
REMARK   3      S31:  -0.1070 S32:  -0.4299 S33:  -0.1041                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     5        D    23                          
REMARK   3    ORIGIN FOR THE GROUP (A): -38.1639  12.6177 -36.9820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2310 T22:   0.2721                                     
REMARK   3      T33:   0.2320 T12:  -0.0002                                     
REMARK   3      T13:  -0.0045 T23:   0.0258                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9811 L22:   0.8570                                     
REMARK   3      L33:   3.9503 L12:   0.3195                                     
REMARK   3      L13:  -1.5224 L23:  -0.6594                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0183 S12:  -0.3421 S13:  -0.1341                       
REMARK   3      S21:   0.3766 S22:  -0.0070 S23:   0.0102                       
REMARK   3      S31:   0.1817 S32:   0.0956 S33:   0.0253                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    24        D    33                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.9686  15.0556 -48.4030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1581 T22:   0.1510                                     
REMARK   3      T33:   0.1592 T12:   0.0064                                     
REMARK   3      T13:  -0.0077 T23:  -0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9505 L22:   1.5885                                     
REMARK   3      L33:   3.6536 L12:   2.5291                                     
REMARK   3      L13:  -3.9865 L23:  -2.3827                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0656 S12:   0.1105 S13:  -0.0935                       
REMARK   3      S21:  -0.0750 S22:   0.0278 S23:   0.0441                       
REMARK   3      S31:   0.0936 S32:  -0.0667 S33:   0.0378                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    34        D    51                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.2140  23.8753 -47.8129              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2126 T22:   0.2123                                     
REMARK   3      T33:   0.2164 T12:  -0.0005                                     
REMARK   3      T13:  -0.0055 T23:  -0.0305                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2670 L22:   0.5348                                     
REMARK   3      L33:   0.7815 L12:  -0.1080                                     
REMARK   3      L13:  -0.1375 L23:  -0.5338                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0296 S12:  -0.0071 S13:   0.1515                       
REMARK   3      S21:   0.0908 S22:   0.0335 S23:   0.1909                       
REMARK   3      S31:  -0.1351 S32:  -0.2182 S33:  -0.0631                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    52        D    65                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.0317  32.8202 -44.0039              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3019 T22:   0.2913                                     
REMARK   3      T33:   0.2850 T12:   0.0048                                     
REMARK   3      T13:   0.0068 T23:  -0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6637 L22:   0.0799                                     
REMARK   3      L33:   0.0723 L12:  -0.0666                                     
REMARK   3      L13:   0.1153 L23:  -0.0391                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0487 S12:  -0.3343 S13:   0.2067                       
REMARK   3      S21:   0.1322 S22:   0.0243 S23:   0.0392                       
REMARK   3      S31:  -0.1010 S32:  -0.0968 S33:   0.0244                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    66        D    76                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4830  25.3780 -45.7351              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1610 T22:   0.1687                                     
REMARK   3      T33:   0.1671 T12:  -0.0014                                     
REMARK   3      T13:   0.0075 T23:  -0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9260 L22:   2.5089                                     
REMARK   3      L33:   5.2494 L12:  -1.9878                                     
REMARK   3      L13:   0.9236 L23:  -2.9644                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0268 S12:  -0.0573 S13:   0.3652                       
REMARK   3      S21:   0.1894 S22:  -0.1032 S23:  -0.2969                       
REMARK   3      S31:  -0.4547 S32:   0.3880 S33:   0.0764                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    77        D    82                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6725  22.9815 -37.1273              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3987 T22:   0.2835                                     
REMARK   3      T33:   0.2851 T12:   0.1019                                     
REMARK   3      T13:   0.1051 T23:   0.0640                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6085 L22:   5.2074                                     
REMARK   3      L33:   7.9707 L12:   0.2502                                     
REMARK   3      L13:   0.4763 L23:   6.0366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0456 S12:  -0.6030 S13:   0.4005                       
REMARK   3      S21:   0.3388 S22:  -0.1636 S23:   0.4256                       
REMARK   3      S31:  -0.1382 S32:  -0.5383 S33:   0.2092                       
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 3RV5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065415.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98066                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200                                   (DCM)                              
REMARK 200  OPTICS                         : VERTICAL COLLIMATING MIRROR        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21706                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXS                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL (PH 8), 50 MM CADMIUM    
REMARK 280  SULFATE, 900 MM SODIUM ACETATE (RESERVOIR) AND 50 MM DEOXYCHOLIC    
REMARK 280  ACID (ADDITIVE), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       25.92200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.89150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.92200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.89150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 24710 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -445.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000       51.84400            
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 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000       51.84400            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  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     MSE A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     LYS A    86                                                      
REMARK 465     ASP A    87                                                      
REMARK 465     ASP A    88                                                      
REMARK 465     SER A    89                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     ARG B    83                                                      
REMARK 465     CYS B    84                                                      
REMARK 465     MSE B    85                                                      
REMARK 465     LYS B    86                                                      
REMARK 465     ASP B    87                                                      
REMARK 465     ASP B    88                                                      
REMARK 465     SER B    89                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     LYS C    86                                                      
REMARK 465     ASP C    87                                                      
REMARK 465     ASP C    88                                                      
REMARK 465     SER C    89                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     ASP D     3                                                      
REMARK 465     ILE D     4                                                      
REMARK 465     ARG D    83                                                      
REMARK 465     CYS D    84                                                      
REMARK 465     MSE D    85                                                      
REMARK 465     LYS D    86                                                      
REMARK 465     ASP D    87                                                      
REMARK 465     ASP D    88                                                      
REMARK 465     SER D    89                                                      
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    HOH A   115     O    HOH A   119              1.90            
REMARK 500   O    HOH C   111     O    HOH C   143              1.93            
REMARK 500   OE2  GLU C    66     O    HOH C   139              2.07            
REMARK 500   O    HOH B   121     O    HOH B   148              2.14            
REMARK 500   OE1  GLU A    40     O    HOH A   113              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU D    19    CD     CD D   103     4454     2.15            
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    CYS A  35   CB    CYS A  35   SG      0.118                       
REMARK 500    CYS A  84   CB    CYS A  84   SG      0.198                       
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    ASP A  33   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 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    THR A  53       73.23   -116.06                                   
REMARK 500    ASP C  65       71.81    -67.45                                   
REMARK 500    THR D  53       76.15   -103.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 112        DISTANCE =  7.66 ANGSTROMS                       
REMARK 525    HOH C 125        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH D 111        DISTANCE =  6.34 ANGSTROMS                       
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                              CD D 101  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  33   OD1                                                    
REMARK 620 2 CYS D  35   SG  112.8                                              
REMARK 620 3 GLY D  30   O    74.7 154.8                                        
REMARK 620 4 ASP D  33   OD2  58.9  80.9  83.6                                  
REMARK 620 5 GLU D  40   OE1 135.0  99.4  89.4 161.7                            
REMARK 620 6 GLU D  40   OE2  81.0 127.6  76.5 138.8  54.2                      
REMARK 620 7 CYS D  35   O   130.3  83.1  74.7  79.6  82.3 127.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 104  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 132   O                                                      
REMARK 620 2 ASP A  73   OD2 113.7                                              
REMARK 620 3 ASP A  75   OD1 132.3  80.8                                        
REMARK 620 4 HOH A 127   O    78.3 163.8  99.4                                  
REMARK 620 5 ASP A  75   OD2  81.2 113.1  52.3  78.7                            
REMARK 620 6 HOH A 120   O    81.9  80.0 145.5  91.4 161.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 103  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 119   O                                                      
REMARK 620 2 HOH A 115   O    53.9                                              
REMARK 620 3 CYS A  35   SG  101.4 123.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 101  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  33   OD2                                                    
REMARK 620 2 GLY A  30   O    82.5                                              
REMARK 620 3 GLU A  40   OE1  86.4  85.3                                        
REMARK 620 4 ASP A  33   OD1  56.1  79.6 140.8                                  
REMARK 620 5 CYS A  35   SG  110.8 156.0 114.6  91.2                            
REMARK 620 6 CYS A  35   O   136.1  78.6 130.4  81.7  78.1                      
REMARK 620 7 GLU A  40   OE2 137.2  93.5  50.9 164.6  89.7  83.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 102  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  65   OD2                                                    
REMARK 620 2 ASP A  67   OD1  80.3                                              
REMARK 620 3 SER A  69   OG  104.7  83.1                                        
REMARK 620 4 HOH A 110   O   166.7  87.3  78.5                                  
REMARK 620 5 GLU A  76   OE1  90.3 130.6 145.5  94.1                            
REMARK 620 6 THR A  71   O    91.7 149.1  70.1 101.5  78.7                      
REMARK 620 7 GLU A  76   OE2  82.3  77.8 158.3  90.3  52.9 131.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD D 104  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  73   OD2                                                    
REMARK 620 2 HOH D 120   O   125.4                                              
REMARK 620 3 HOH D 118   O   152.6  79.3                                        
REMARK 620 4 ASP D  75   OD1  80.8 125.3  94.2                                  
REMARK 620 5 ASP D  75   OD2 115.9  74.8  79.3  50.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD B 102  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  76   OE1                                                    
REMARK 620 2 ASP B  65   OD1 100.4                                              
REMARK 620 3 HOH B 110   O   102.4 156.9                                        
REMARK 620 4 SER B  69   OG  149.6  97.1  64.3                                  
REMARK 620 5 ASP B  67   OD1 121.4  74.4  90.3  87.2                            
REMARK 620 6 THR B  71   O    76.6  89.1 100.0  79.1 157.1                      
REMARK 620 7 GLU B  76   OE2  53.9  90.1 100.1 150.9  67.7 129.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD D 102  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  65   OD1                                                    
REMARK 620 2 GLU D  76   OE1 106.0                                              
REMARK 620 3 HOH D 110   O   166.2  84.8                                        
REMARK 620 4 THR D  71   O    95.5  76.9  95.4                                  
REMARK 620 5 ASP D  67   OD1  75.0 132.8  91.3 150.1                            
REMARK 620 6 GLU D  76   OE2  79.7  54.8 100.4 126.9  80.1                      
REMARK 620 7 SER D  69   OG   98.5 138.6  77.8  67.8  85.3 165.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD B 104  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 138   O                                                      
REMARK 620 2 ASP B  75   OD1  77.8                                              
REMARK 620 3 HOH B 114   O   151.5 128.4                                        
REMARK 620 4 ASP B  73   OD2  76.2  91.6 109.9                                  
REMARK 620 5 HOH B 113   O    76.8 154.2  77.4  78.2                            
REMARK 620 6 HOH B 115   O    85.2  94.9  81.7 158.5  87.2                      
REMARK 620 7 ASP B  75   OD2 128.5  53.3  75.2 115.9 152.2  84.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD C 102  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  65   OD1                                                    
REMARK 620 2 GLU C  76   OE2 101.9                                              
REMARK 620 3 ASP C  67   OD1  71.6 130.9                                        
REMARK 620 4 HOH C 110   O   157.8 100.1  92.1                                  
REMARK 620 5 SER C  69   OG   96.8 145.8  82.2  65.4                            
REMARK 620 6 GLU C  76   OE1  80.4  55.6  75.6 110.7 157.3                      
REMARK 620 7 THR C  71   O    91.0  75.7 149.9  96.7  75.6 126.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD C 101  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  33   OD2                                                    
REMARK 620 2 GLY C  30   O    69.4                                              
REMARK 620 3 GLU C  40   OE2  76.5  77.7                                        
REMARK 620 4 CYS C  35   O   128.0  79.9 136.7                                  
REMARK 620 5 GLU C  40   OE1 133.3  97.9  56.8  90.7                            
REMARK 620 6 CYS C  35   SG  125.7 153.1 125.1  73.4  86.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD B 103  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 144   O                                                      
REMARK 620 2 HOH B 119   O    92.5                                              
REMARK 620 3 HOH B 147   O    62.0 103.7                                        
REMARK 620 4 HOH B 150   O   125.6  70.8  72.1                                  
REMARK 620 5 CYS B  35   SG  108.3 157.5  93.8 102.1                            
REMARK 620 6 HOH B 146   O    57.1  96.4 116.2 166.5  88.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD D 103  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 128   O                                                      
REMARK 620 2 CYS D  35   SG   95.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 108  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  63   OE2                                                    
REMARK 620 2 GLU B  59   OE2  87.0                                              
REMARK 620 3 HOH B 145   O   100.8 131.8                                        
REMARK 620 4 GLU B  63   OE1  45.6 117.6  55.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD C 104  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 119   O                                                      
REMARK 620 2 ASP C  73   OD1  83.1                                              
REMARK 620 3 HOH C 113   O    78.0  76.8                                        
REMARK 620 4 ASP C  75   OD1 151.6  87.9  73.7                                  
REMARK 620 5 ASP C  75   OD2 153.3 113.3 125.0  54.0                            
REMARK 620 6 HOH C 130   O    82.2 159.6  86.3  98.4  85.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 105  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  66   OE2                                                    
REMARK 620 2 HOH A 140   O    91.1                                              
REMARK 620 3 HOH C 123   O    95.2  90.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD C 105  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  59   OE2                                                    
REMARK 620 2 GLU C  59   OE1  53.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD B 106  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  59   OE1                                                    
REMARK 620 2 HOH B 133   O    84.1                                              
REMARK 620 3 HOH B 135   O   124.6 130.2                                        
REMARK 620 4 GLU B  59   OE2  55.2 139.3  80.1                                  
REMARK 620 5 HOH B 134   O    92.9  84.1  57.7  95.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD C 103  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  33   OD1                                                    
REMARK 620 2 HOH C 133   O   150.6                                              
REMARK 620 3 HOH C 143   O    73.2  82.8                                        
REMARK 620 4 HOH C 111   O    76.8  98.7  46.1                                  
REMARK 620 5 CYS C  35   SG   83.0  98.1 125.6 159.7                            
REMARK 620 6 HOH C 116   O    88.0 121.3 142.0  98.1  82.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD B 105  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 142   O                                                      
REMARK 620 2 GLU C  15   OE2  97.9                                              
REMARK 620 3 HOH C 138   O   149.2  75.0                                        
REMARK 620 4 GLU B  32   OE2 121.2  98.0  89.5                                  
REMARK 620 5 HOH B 148   O    92.1 159.1  87.0  92.3                            
REMARK 620 6 GLU B  32   OE1  71.2 117.1 138.9  51.3  83.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD B 101  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  40   OE2                                                    
REMARK 620 2 GLU B  40   OE1  56.8                                              
REMARK 620 3 GLY B  30   O    81.8  86.7                                        
REMARK 620 4 CYS B  35   O   134.4  81.6  77.6                                  
REMARK 620 5 ASP B  33   OD1 127.7 158.1  73.8  84.4                            
REMARK 620 6 ASP B  33   OD2  85.5 142.1  92.4 135.1  51.0                      
REMARK 620 7 CYS B  35   SG  122.1  95.5 152.4  75.6  97.3 102.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 106  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  32   OE1                                                    
REMARK 620 2 ASP D  75   OD2  74.4                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 103                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 104                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 105                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DXC A 92                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DXC B 92                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DXC A 91                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 109                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 108                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 103                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 104                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 105                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 106                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 107                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 103                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 104                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD C 105                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 106                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DXC C 92                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD D 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD D 103                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD D 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD D 104                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DXC D 92                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1J1D   RELATED DB: PDB                                   
REMARK 900 FULL LENGTH & CALCUIM SATURATED HUMAN CTNC IN COMPLEX WITH           
REMARK 900 CTNI AND CTNT                                                        
REMARK 900 RELATED ID: 1WRK   RELATED DB: PDB                                   
REMARK 900 CALCIUM BOUND HUMAN N-CTNC IN COMPLEX WITH TRIFLUOROPERAZINE         
REMARK 900 RELATED ID: 1AP4   RELATED DB: PDB                                   
REMARK 900 CALCIUM BOUND HUMAN N-CTNC                                           
REMARK 900 RELATED ID: 1SPY   RELATED DB: PDB                                   
REMARK 900 CALCIUM FREE HUMAN N-CTNC                                            
REMARK 900 RELATED ID: 1MXL   RELATED DB: PDB                                   
REMARK 900 CALCIUM BOUND HUMAN N-CTNC IN COMPLEX WITH CTNI (147-163)            
REMARK 900 RELATED ID: 1LXF   RELATED DB: PDB                                   
REMARK 900 CALCIUM BOUND HUMAN N-CTNC IN COMPLEX WITH CTNI (147-163)            
REMARK 900 AND BEPRIDIL                                                         
DBREF  3RV5 A    1    89  UNP    P63316   TNNC1_HUMAN      1     89             
DBREF  3RV5 B    1    89  UNP    P63316   TNNC1_HUMAN      1     89             
DBREF  3RV5 C    1    89  UNP    P63316   TNNC1_HUMAN      1     89             
DBREF  3RV5 D    1    89  UNP    P63316   TNNC1_HUMAN      1     89             
SEQRES   1 A   89  MSE ASP ASP ILE TYR LYS ALA ALA VAL GLU GLN LEU THR          
SEQRES   2 A   89  GLU GLU GLN LYS ASN GLU PHE LYS ALA ALA PHE ASP ILE          
SEQRES   3 A   89  PHE VAL LEU GLY ALA GLU ASP GLY CYS ILE SER THR LYS          
SEQRES   4 A   89  GLU LEU GLY LYS VAL MSE ARG MSE LEU GLY GLN ASN PRO          
SEQRES   5 A   89  THR PRO GLU GLU LEU GLN GLU MSE ILE ASP GLU VAL ASP          
SEQRES   6 A   89  GLU ASP GLY SER GLY THR VAL ASP PHE ASP GLU PHE LEU          
SEQRES   7 A   89  VAL MSE MSE VAL ARG CYS MSE LYS ASP ASP SER                  
SEQRES   1 B   89  MSE ASP ASP ILE TYR LYS ALA ALA VAL GLU GLN LEU THR          
SEQRES   2 B   89  GLU GLU GLN LYS ASN GLU PHE LYS ALA ALA PHE ASP ILE          
SEQRES   3 B   89  PHE VAL LEU GLY ALA GLU ASP GLY CYS ILE SER THR LYS          
SEQRES   4 B   89  GLU LEU GLY LYS VAL MSE ARG MSE LEU GLY GLN ASN PRO          
SEQRES   5 B   89  THR PRO GLU GLU LEU GLN GLU MSE ILE ASP GLU VAL ASP          
SEQRES   6 B   89  GLU ASP GLY SER GLY THR VAL ASP PHE ASP GLU PHE LEU          
SEQRES   7 B   89  VAL MSE MSE VAL ARG CYS MSE LYS ASP ASP SER                  
SEQRES   1 C   89  MSE ASP ASP ILE TYR LYS ALA ALA VAL GLU GLN LEU THR          
SEQRES   2 C   89  GLU GLU GLN LYS ASN GLU PHE LYS ALA ALA PHE ASP ILE          
SEQRES   3 C   89  PHE VAL LEU GLY ALA GLU ASP GLY CYS ILE SER THR LYS          
SEQRES   4 C   89  GLU LEU GLY LYS VAL MSE ARG MSE LEU GLY GLN ASN PRO          
SEQRES   5 C   89  THR PRO GLU GLU LEU GLN GLU MSE ILE ASP GLU VAL ASP          
SEQRES   6 C   89  GLU ASP GLY SER GLY THR VAL ASP PHE ASP GLU PHE LEU          
SEQRES   7 C   89  VAL MSE MSE VAL ARG CYS MSE LYS ASP ASP SER                  
SEQRES   1 D   89  MSE ASP ASP ILE TYR LYS ALA ALA VAL GLU GLN LEU THR          
SEQRES   2 D   89  GLU GLU GLN LYS ASN GLU PHE LYS ALA ALA PHE ASP ILE          
SEQRES   3 D   89  PHE VAL LEU GLY ALA GLU ASP GLY CYS ILE SER THR LYS          
SEQRES   4 D   89  GLU LEU GLY LYS VAL MSE ARG MSE LEU GLY GLN ASN PRO          
SEQRES   5 D   89  THR PRO GLU GLU LEU GLN GLU MSE ILE ASP GLU VAL ASP          
SEQRES   6 D   89  GLU ASP GLY SER GLY THR VAL ASP PHE ASP GLU PHE LEU          
SEQRES   7 D   89  VAL MSE MSE VAL ARG CYS MSE LYS ASP ASP SER                  
MODRES 3RV5 MSE A   45  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE A   47  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE A   60  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE A   80  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE A   81  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE A   85  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE B   45  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE B   47  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE B   60  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE B   80  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE B   81  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE C   45  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE C   47  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE C   60  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE C   80  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE C   81  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE C   85  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE D   45  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE D   47  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE D   60  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE D   80  MET  SELENOMETHIONINE                                   
MODRES 3RV5 MSE D   81  MET  SELENOMETHIONINE                                   
HET    MSE  A  45       8                                                       
HET    MSE  A  47       8                                                       
HET    MSE  A  60       8                                                       
HET    MSE  A  80       8                                                       
HET    MSE  A  81       8                                                       
HET    MSE  A  85       8                                                       
HET    MSE  B  45       8                                                       
HET    MSE  B  47       8                                                       
HET    MSE  B  60       8                                                       
HET    MSE  B  80       8                                                       
HET    MSE  B  81       8                                                       
HET    MSE  C  45       8                                                       
HET    MSE  C  47       8                                                       
HET    MSE  C  60       8                                                       
HET    MSE  C  80       8                                                       
HET    MSE  C  81       8                                                       
HET    MSE  C  85       8                                                       
HET    MSE  D  45       8                                                       
HET    MSE  D  47       8                                                       
HET    MSE  D  60       8                                                       
HET    MSE  D  80       8                                                       
HET    MSE  D  81       8                                                       
HET     CD  A 101       1                                                       
HET     CD  A 102       1                                                       
HET     CD  A 103       1                                                       
HET     CD  A 104       1                                                       
HET     CD  A 105       1                                                       
HET    DXC  A  92      28                                                       
HET    DXC  B  92      28                                                       
HET    DXC  A  91      28                                                       
HET     CA  B 109       1                                                       
HET     CA  B 108       1                                                       
HET     CD  B 101       1                                                       
HET     CD  B 102       1                                                       
HET     CD  B 103       1                                                       
HET     CD  B 104       1                                                       
HET     CD  B 105       1                                                       
HET     CD  B 106       1                                                       
HET     CD  B 107       1                                                       
HET     CD  C 101       1                                                       
HET     CD  C 102       1                                                       
HET     CD  C 103       1                                                       
HET     CD  C 104       1                                                       
HET     CD  C 105       1                                                       
HET     CA  C 106       1                                                       
HET    DXC  C  92      28                                                       
HET     CD  D 101       1                                                       
HET     CD  D 102       1                                                       
HET     CD  D 103       1                                                       
HET     CD  D 104       1                                                       
HET    DXC  D  92      28                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CD CADMIUM ION                                                      
HETNAM     DXC (3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC ACID          
HETNAM      CA CALCIUM ION                                                      
HETSYN     DXC DEOXYCHOLIC ACID                                                 
FORMUL   1  MSE    22(C5 H11 N O2 SE)                                           
FORMUL   5   CD    21(CD 2+)                                                    
FORMUL  10  DXC    5(C24 H40 O4)                                                
FORMUL  13   CA    3(CA 2+)                                                     
FORMUL  34  HOH   *133(H2 O)                                                    
HELIX    1   1 ASP A    3  GLN A   11  1                                   9    
HELIX    2   2 THR A   13  GLU A   32  1                                  20    
HELIX    3   3 SER A   37  LEU A   48  1                                  12    
HELIX    4   4 THR A   53  ASP A   65  1                                  13    
HELIX    5   5 ASP A   73  MSE A   85  1                                  13    
HELIX    6   6 ALA B    7  LEU B   12  5                                   6    
HELIX    7   7 THR B   13  GLU B   32  1                                  20    
HELIX    8   8 SER B   37  LEU B   48  1                                  12    
HELIX    9   9 THR B   53  GLU B   63  1                                  11    
HELIX   10  10 PHE B   74  MSE B   81  1                                   8    
HELIX   11  11 ILE C    4  GLN C   11  1                                   8    
HELIX   12  12 THR C   13  GLU C   32  1                                  20    
HELIX   13  13 SER C   37  LEU C   48  1                                  12    
HELIX   14  14 THR C   53  ASP C   65  1                                  13    
HELIX   15  15 PHE C   74  CYS C   84  1                                  11    
HELIX   16  16 LYS D    6  GLN D   11  1                                   6    
HELIX   17  17 THR D   13  GLU D   32  1                                  20    
HELIX   18  18 SER D   37  LEU D   48  1                                  12    
HELIX   19  19 THR D   53  ASP D   65  1                                  13    
HELIX   20  20 ASP D   73  VAL D   82  1                                  10    
SHEET    1   A 2 CYS B  35  ILE B  36  0                                        
SHEET    2   A 2 VAL B  72  ASP B  73 -1  O  VAL B  72   N  ILE B  36           
SHEET    1   B 2 CYS C  35  ILE C  36  0                                        
SHEET    2   B 2 VAL C  72  ASP C  73 -1  O  VAL C  72   N  ILE C  36           
LINK         C   VAL A  44                 N   MSE A  45     1555   1555  1.33  
LINK         C   MSE A  45                 N   ARG A  46     1555   1555  1.35  
LINK         C   ARG A  46                 N   MSE A  47     1555   1555  1.33  
LINK         C   MSE A  47                 N   LEU A  48     1555   1555  1.34  
LINK         C   GLU A  59                 N   MSE A  60     1555   1555  1.32  
LINK         C   MSE A  60                 N   ILE A  61     1555   1555  1.34  
LINK         C   VAL A  79                 N   MSE A  80     1555   1555  1.33  
LINK         C   MSE A  80                 N   MSE A  81     1555   1555  1.33  
LINK         C   MSE A  81                 N   VAL A  82     1555   1555  1.34  
LINK         C   CYS A  84                 N   MSE A  85     1555   1555  1.34  
LINK         C   VAL B  44                 N   MSE B  45     1555   1555  1.34  
LINK         C   MSE B  45                 N   ARG B  46     1555   1555  1.33  
LINK         C   ARG B  46                 N   MSE B  47     1555   1555  1.33  
LINK         C   MSE B  47                 N   LEU B  48     1555   1555  1.34  
LINK         C   GLU B  59                 N   MSE B  60     1555   1555  1.33  
LINK         C   MSE B  60                 N   ILE B  61     1555   1555  1.32  
LINK         C   VAL B  79                 N   MSE B  80     1555   1555  1.33  
LINK         C   MSE B  80                 N   MSE B  81     1555   1555  1.32  
LINK         C   MSE B  81                 N   VAL B  82     1555   1555  1.33  
LINK         C   VAL C  44                 N   MSE C  45     1555   1555  1.33  
LINK         C   MSE C  45                 N   ARG C  46     1555   1555  1.33  
LINK         C   ARG C  46                 N   MSE C  47     1555   1555  1.33  
LINK         C   MSE C  47                 N   LEU C  48     1555   1555  1.33  
LINK         C   GLU C  59                 N   MSE C  60     1555   1555  1.33  
LINK         C   MSE C  60                 N   ILE C  61     1555   1555  1.32  
LINK         C   VAL C  79                 N   MSE C  80     1555   1555  1.34  
LINK         C   MSE C  80                 N   MSE C  81     1555   1555  1.33  
LINK         C   MSE C  81                 N   VAL C  82     1555   1555  1.33  
LINK         C   CYS C  84                 N   MSE C  85     1555   1555  1.33  
LINK         C   VAL D  44                 N   MSE D  45     1555   1555  1.34  
LINK         C   MSE D  45                 N   ARG D  46     1555   1555  1.34  
LINK         C   ARG D  46                 N   MSE D  47     1555   1555  1.34  
LINK         C   MSE D  47                 N   LEU D  48     1555   1555  1.34  
LINK         C   GLU D  59                 N   MSE D  60     1555   1555  1.33  
LINK         C   MSE D  60                 N   ILE D  61     1555   1555  1.34  
LINK         C   VAL D  79                 N   MSE D  80     1555   1555  1.33  
LINK         C   MSE D  80                 N   MSE D  81     1555   1555  1.34  
LINK         C   MSE D  81                 N   VAL D  82     1555   1555  1.33  
LINK         OD1 ASP D  33                CD    CD D 101     1555   1555  1.94  
LINK        CD    CD A 104                 O   HOH A 132     1555   1555  2.05  
LINK        CD    CD A 103                 O   HOH A 119     1555   1555  2.07  
LINK         OD2 ASP A  33                CD    CD A 101     1555   1555  2.07  
LINK         OD2 ASP A  73                CD    CD A 104     1555   1555  2.10  
LINK         OD2 ASP A  65                CD    CD A 102     1555   1555  2.11  
LINK        CD    CD A 103                 O   HOH A 115     1555   1555  2.11  
LINK         OD2 ASP D  73                CD    CD D 104     1555   1555  2.12  
LINK        CD    CD D 104                 O   HOH D 120     1555   1555  2.13  
LINK         OE1 GLU B  76                CD    CD B 102     1555   1555  2.16  
LINK         OD1 ASP D  65                CD    CD D 102     1555   1555  2.17  
LINK         OD1 ASP B  65                CD    CD B 102     1555   1555  2.17  
LINK        CD    CD B 104                 O   HOH B 138     1555   1555  2.18  
LINK         OD1 ASP C  65                CD    CD C 102     1555   1555  2.19  
LINK         OD1 ASP B  75                CD    CD B 104     1555   1555  2.20  
LINK         OE2 GLU C  76                CD    CD C 102     1555   1555  2.22  
LINK         OD2 ASP C  33                CD    CD C 101     1555   1555  2.23  
LINK         O   GLY A  30                CD    CD A 101     1555   1555  2.23  
LINK        CD    CD B 102                 O   HOH B 110     1555   1555  2.23  
LINK        CD    CD B 104                 O   HOH B 114     1555   1555  2.23  
LINK        CD    CD B 103                 O   HOH B 144     1555   1555  2.23  
LINK         OD2 ASP B  73                CD    CD B 104     1555   1555  2.24  
LINK         SG  CYS D  35                CD    CD D 101     1555   1555  2.24  
LINK        CD    CD D 103                 O   HOH D 128     1555   1555  2.27  
LINK         OE2 GLU B  63                CA    CA B 108     1555   1555  2.27  
LINK        CD    CD C 104                 O   HOH C 119     1555   1555  2.27  
LINK         OE1 GLU D  76                CD    CD D 102     1555   1555  2.27  
LINK         OD1 ASP C  73                CD    CD C 104     1555   1555  2.27  
LINK         O   GLY C  30                CD    CD C 101     1555   1555  2.27  
LINK        CD    CD D 102                 O   HOH D 110     1555   1555  2.27  
LINK         OD1 ASP C  67                CD    CD C 102     1555   1555  2.27  
LINK         OE2 GLU A  66                CD    CD A 105     1555   1555  2.27  
LINK         O   THR D  71                CD    CD D 102     1555   1555  2.28  
LINK         OD1 ASP A  67                CD    CD A 102     1555   1555  2.28  
LINK        CD    CD C 104                 O   HOH C 113     1555   1555  2.28  
LINK         OG  SER B  69                CD    CD B 102     1555   1555  2.28  
LINK         OE2 GLU C  59                CD    CD C 105     1555   1555  2.29  
LINK         O   GLY D  30                CD    CD D 101     1555   1555  2.29  
LINK         OG  SER A  69                CD    CD A 102     1555   1555  2.29  
LINK        CD    CD A 102                 O   HOH A 110     1555   1555  2.29  
LINK         OD1 ASP C  75                CD    CD C 104     1555   1555  2.31  
LINK         OE1 GLU A  76                CD    CD A 102     1555   1555  2.31  
LINK        CD    CD B 104                 O   HOH B 113     1555   1555  2.31  
LINK         OE2 GLU C  40                CD    CD C 101     1555   1555  2.32  
LINK         OE2 GLU B  66                CA    CA B 109     1555   1555  2.32  
LINK        CD    CD C 102                 O   HOH C 110     1555   1555  2.32  
LINK         OE1 GLU B  59                CD    CD B 106     1555   1555  2.33  
LINK         OD1 ASP C  33                CD    CD C 103     1555   1555  2.33  
LINK        CD    CD B 105                 O   HOH B 142     1555   1555  2.35  
LINK        CD    CD B 106                 O   HOH B 133     1555   1555  2.35  
LINK         OE2 GLU C  15                CD    CD B 105     1555   1555  2.35  
LINK         OE2 GLU B  40                CD    CD B 101     1555   1555  2.35  
LINK        CD    CD B 105                 O   HOH C 138     1555   1555  2.35  
LINK         OD1 ASP B  67                CD    CD B 102     1555   1555  2.36  
LINK        CD    CD C 103                 O   HOH C 133     1555   1555  2.37  
LINK         OD1 ASP D  67                CD    CD D 102     1555   1555  2.37  
LINK         OE2 GLU B  32                CD    CD B 105     1555   1555  2.37  
LINK        CD    CD A 105                 O   HOH A 140     1555   1555  2.37  
LINK         OG  SER C  69                CD    CD C 102     1555   1555  2.38  
LINK         O   CYS C  35                CD    CD C 101     1555   1555  2.38  
LINK        CD    CD B 106                 O   HOH B 135     1555   1555  2.39  
LINK         OD2 ASP D  33                CD    CD D 101     1555   1555  2.39  
LINK         OD2 ASP C  75                CD    CD C 104     1555   1555  2.39  
LINK         OE1 GLU B  40                CD    CD B 101     1555   1555  2.39  
LINK         O   GLY B  30                CD    CD B 101     1555   1555  2.39  
LINK         OD1 ASP A  75                CD    CD A 104     1555   1555  2.40  
LINK         O   THR A  71                CD    CD A 102     1555   1555  2.40  
LINK         OE2 GLU B  59                CD    CD B 106     1555   1555  2.40  
LINK        CD    CD B 105                 O   HOH B 148     1555   1555  2.40  
LINK        CD    CD D 104                 O   HOH D 118     1555   1555  2.40  
LINK         O   CYS B  35                CD    CD B 101     1555   1555  2.41  
LINK         OE1 GLU D  40                CD    CD D 101     1555   1555  2.41  
LINK         OE1 GLU A  40                CD    CD A 101     1555   1555  2.41  
LINK         OE2 GLU D  76                CD    CD D 102     1555   1555  2.41  
LINK         OE2 GLU D  40                CD    CD D 101     1555   1555  2.42  
LINK        CD    CD C 104                 O   HOH C 130     1555   1555  2.42  
LINK         OE1 GLU C  76                CD    CD C 102     1555   1555  2.42  
LINK         OD1 ASP A  33                CD    CD A 101     1555   1555  2.42  
LINK        CD    CD A 104                 O   HOH A 127     1555   1555  2.43  
LINK        CD    CD B 104                 O   HOH B 115     1555   1555  2.43  
LINK        CD    CD B 106                 O   HOH B 134     1555   1555  2.44  
LINK         O   THR C  71                CD    CD C 102     1555   1555  2.45  
LINK         OE1 GLU C  40                CD    CD C 101     1555   1555  2.45  
LINK        CD    CD B 103                 O   HOH B 119     1555   1555  2.46  
LINK        CD    CD C 103                 O   HOH C 143     1555   1555  2.46  
LINK        CD    CD B 103                 O   HOH B 147     1555   1555  2.47  
LINK        CD    CD C 103                 O   HOH C 111     1555   1555  2.48  
LINK         SG  CYS A  35                CD    CD A 101     1555   1555  2.49  
LINK         O   CYS D  35                CD    CD D 101     1555   1555  2.49  
LINK         OD1 ASP B  33                CD    CD B 101     1555   1555  2.49  
LINK         SG  CYS C  35                CD    CD C 103     1555   1555  2.49  
LINK         OD2 ASP A  75                CD    CD A 104     1555   1555  2.49  
LINK         O   CYS A  35                CD    CD A 101     1555   1555  2.50  
LINK        CD    CD C 103                 O   HOH C 116     1555   1555  2.50  
LINK         SG  CYS C  35                CD    CD C 101     1555   1555  2.50  
LINK         OD1 ASP D  75                CD    CD D 104     1555   1555  2.50  
LINK         OD2 ASP B  75                CD    CD B 104     1555   1555  2.51  
LINK        CD    CD B 103                 O   HOH B 150     1555   1555  2.51  
LINK         OD2 ASP B  33                CD    CD B 101     1555   1555  2.51  
LINK         O   THR B  71                CD    CD B 102     1555   1555  2.52  
LINK        CD    CD A 105                 O   HOH C 123     1555   1555  2.52  
LINK         OE2 GLU B  76                CD    CD B 102     1555   1555  2.54  
LINK         OE2 GLU B  59                CA    CA B 108     1555   1555  2.54  
LINK         OG  SER D  69                CD    CD D 102     1555   1555  2.55  
LINK         SG  CYS B  35                CD    CD B 103     1555   1555  2.55  
LINK        CD    CD B 103                 O   HOH B 146     1555   1555  2.55  
LINK         OE2 GLU A  76                CD    CD A 102     1555   1555  2.56  
LINK        CD    CD A 104                 O   HOH A 120     1555   1555  2.56  
LINK         OE2 GLU A  40                CD    CD A 101     1555   1555  2.56  
LINK         OE1 GLU C  32                CA    CA C 106     1555   1555  2.57  
LINK         OD2 ASP D  75                CD    CD D 104     1555   1555  2.57  
LINK        CA    CA B 108                 O   HOH B 145     1555   1555  2.59  
LINK         OE1 GLU B  32                CD    CD B 105     1555   1555  2.59  
LINK         OE1 GLU C  59                CD    CD C 105     1555   1555  2.60  
LINK         SG  CYS B  35                CD    CD B 101     1555   1555  2.61  
LINK         SG  CYS D  35                CD    CD D 103     1555   1555  2.62  
LINK         SG  CYS A  35                CD    CD A 103     1555   1555  2.65  
LINK         OD2 ASP D  75                CA    CA C 106     1555   1555  2.89  
LINK         OE1 GLU B  63                CA    CA B 108     1555   1555  3.12  
SITE     1 AC1  4 GLY A  30  ASP A  33  CYS A  35  GLU A  40                    
SITE     1 AC2  5 GLU A  15  GLU A  19  CYS A  35  HOH A 115                    
SITE     2 AC2  5 HOH A 119                                                     
SITE     1 AC3  6 ASP A  65  ASP A  67  SER A  69  THR A  71                    
SITE     2 AC3  6 GLU A  76  HOH A 110                                          
SITE     1 AC4  5 ASP A  73  ASP A  75  HOH A 120  HOH A 127                    
SITE     2 AC4  5 HOH A 132                                                     
SITE     1 AC5  4 GLU A  66  HOH A 140  HOH C 123  HOH C 138                    
SITE     1 AC6  6 LYS A  17  PHE A  20  GLU B  59  VAL B  82                    
SITE     2 AC6  6  CD B 106  HOH B 135                                          
SITE     1 AC7  3 VAL A  79  VAL A  82  ARG A  83                               
SITE     1 AC8  5 PHE A  27  GLN A  50  PHE A  77  HOH A 135                    
SITE     2 AC8  5 ILE C   4                                                     
SITE     1 AC9  1 GLU B  66                                                     
SITE     1 BC1  3 GLU B  59  GLU B  63  HOH B 145                               
SITE     1 BC2  4 GLY B  30  ASP B  33  CYS B  35  GLU B  40                    
SITE     1 BC3  7 ASP B  33  CYS B  35  HOH B 119  HOH B 144                    
SITE     2 BC3  7 HOH B 146  HOH B 147  HOH B 150                               
SITE     1 BC4  6 ASP B  65  ASP B  67  SER B  69  THR B  71                    
SITE     2 BC4  6 GLU B  76  HOH B 110                                          
SITE     1 BC5  6 ASP B  73  ASP B  75  HOH B 113  HOH B 114                    
SITE     2 BC5  6 HOH B 115  HOH B 138                                          
SITE     1 BC6  5 GLU B  32  HOH B 142  HOH B 148  GLU C  15                    
SITE     2 BC6  5 HOH C 138                                                     
SITE     1 BC7  5 DXC A  92  GLU B  59  HOH B 133  HOH B 134                    
SITE     2 BC7  5 HOH B 135                                                     
SITE     1 BC8  2 GLU A  14  ASP B  62                                          
SITE     1 BC9  4 GLY C  30  ASP C  33  CYS C  35  GLU C  40                    
SITE     1 CC1  6 ASP C  33  CYS C  35  HOH C 111  HOH C 116                    
SITE     2 CC1  6 HOH C 133  HOH C 143                                          
SITE     1 CC2  6 ASP C  65  ASP C  67  SER C  69  THR C  71                    
SITE     2 CC2  6 GLU C  76  HOH C 110                                          
SITE     1 CC3  5 ASP C  73  ASP C  75  HOH C 113  HOH C 119                    
SITE     2 CC3  5 HOH C 130                                                     
SITE     1 CC4  3 GLU C  59  GLU D  10  DXC D  92                               
SITE     1 CC5  2 GLU C  32  ASP D  75                                          
SITE     1 CC6  5 PHE C  20  LYS C  21  PHE C  24  HOH C 121                    
SITE     2 CC6  5 VAL D  82                                                     
SITE     1 CC7  4 GLY D  30  ASP D  33  CYS D  35  GLU D  40                    
SITE     1 CC8  4 GLU D  15  GLU D  19  CYS D  35  HOH D 128                    
SITE     1 CC9  6 ASP D  65  ASP D  67  SER D  69  THR D  71                    
SITE     2 CC9  6 GLU D  76  HOH D 110                                          
SITE     1 DC1  4 ASP D  73  ASP D  75  HOH D 118  HOH D 120                    
SITE     1 DC2  6 TYR B   5  GLU C  59  VAL C  82   CD C 105                    
SITE     2 DC2  6 LYS D  17  PHE D  24                                          
CRYST1   51.844   81.783  100.469  90.00  90.00  90.00 P 21 21 2    16          
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      0.019289  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012227  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009953        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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