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Database: PDB
Entry: 3COJ
LinkDB: 3COJ
Original site: 3COJ 
HEADER    ANTITUMOR PROTEIN/LIGASE                28-MAR-08   3COJ              
TITLE     CRYSTAL STRUCTURE OF THE BRCT DOMAINS OF HUMAN BRCA1 IN COMPLEX WITH A
TITLE    2 PHOSPHORYLATED PEPTIDE FROM HUMAN ACETYL-COA CARBOXYLASE 1           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN;               
COMPND   3 CHAIN: X, A, B, C, D, E, F, G;                                       
COMPND   4 FRAGMENT: BRCT1 AND BRCT2 DOMAINS;                                   
COMPND   5 SYNONYM: RING FINGER PROTEIN 53;                                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: ACETYL-COA CARBOXYLASE 1;                                  
COMPND   9 CHAIN: H, I, J, K, L, M, N, O;                                       
COMPND  10 FRAGMENT: RESIDUES 1258-1270;                                        
COMPND  11 SYNONYM: ACC-ALPHA;                                                  
COMPND  12 EC: 6.4.1.2;                                                         
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRCA1, RNF53;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21/STAR (DE3);                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  14 ORGANISM_TAXID: 32630;                                               
SOURCE  15 OTHER_DETAILS: SYNTHESIZED HUMAN ACC1 PEPTIDE WITH SER1263           
SOURCE  16 PHOSPHORYLATED.                                                      
KEYWDS    BREAST CANCER, OVARIAN CANCER, FATTY ACID BIOSYNTHESIS, LIPID         
KEYWDS   2 SYNTHESIS, OBESITY, PROTEIN-PEPTIDE COMPLEX, PROTEIN PROTEIN         
KEYWDS   3 INTERACTION, ANTI-ONCOGENE, CELL CYCLE, DISEASE MUTATION, DNA        
KEYWDS   4 DAMAGE, DNA REPAIR, DNA-BINDING, METAL-BINDING, NUCLEUS,             
KEYWDS   5 PHOSPHOPROTEIN, ZINC-FINGER, ALTERNATIVE PROMOTER USAGE, ATP-        
KEYWDS   6 BINDING, BIOTIN, LIGASE, MANGANESE, MULTIFUNCTIONAL ENZYME,          
KEYWDS   7 NUCLEOTIDE-BINDING, ANTITUMOR PROTEIN-LIGASE COMPLEX                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.SHEN,L.TONG                                                         
REVDAT   5   25-OCT-17 3COJ    1       SOURCE REMARK                            
REVDAT   4   13-JUL-11 3COJ    1       VERSN                                    
REVDAT   3   16-FEB-10 3COJ    1       DBREF                                    
REVDAT   2   24-FEB-09 3COJ    1       VERSN                                    
REVDAT   1   27-MAY-08 3COJ    0                                                
JRNL        AUTH   Y.SHEN,L.TONG                                                
JRNL        TITL   STRUCTURAL EVIDENCE FOR DIRECT INTERACTIONS BETWEEN THE BRCT 
JRNL        TITL 2 DOMAINS OF HUMAN BRCA1 AND A PHOSPHO-PEPTIDE FROM HUMAN ACC1 
JRNL        REF    BIOCHEMISTRY                  V.  47  5767 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   18452305                                                     
JRNL        DOI    10.1021/BI800314M                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.21 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0003                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.21                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 42426                          
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) : 0.260                           
REMARK   3   R VALUE            (WORKING SET) : 0.257                           
REMARK   3   FREE R VALUE                     : 0.308                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2249                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.21                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.30                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2370                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 71.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3680                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 137                          
REMARK   3   BIN FREE R VALUE                    : 0.3870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13867                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 87.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.91000                                             
REMARK   3    B22 (A**2) : 0.58000                                              
REMARK   3    B33 (A**2) : 0.33000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.592         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.575         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 77.017        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.888                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.840                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14199 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 19246 ; 1.162 ; 1.930       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1699 ; 6.207 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   644 ;36.547 ;23.696       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2429 ;21.392 ;15.049       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    88 ;19.375 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2140 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10587 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  6509 ; 0.213 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9399 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   438 ; 0.154 ; 0.200       
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):    60 ; 0.212 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.070 ; 0.200       
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):  8796 ; 0.138 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14001 ; 0.244 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6118 ; 0.305 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5245 ; 0.525 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : X A B C D E F G                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     X   1648       X    1859      4                      
REMARK   3           1     A   1648       A    1859      4                      
REMARK   3           1     B   1648       B    1859      4                      
REMARK   3           1     C   1648       C    1859      4                      
REMARK   3           1     D   1649       D    1859      4                      
REMARK   3           1     E   1649       E    1859      4                      
REMARK   3           1     F   1649       F    1859      4                      
REMARK   3           1     G   1648       G    1859      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    X    (A):   1633 ;  0.59 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1633 ;  0.65 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1633 ;  0.64 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1633 ;  0.59 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1633 ;  0.68 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   1633 ;  0.61 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    F    (A):   1633 ;  0.60 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    G    (A):   1633 ;  0.60 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    X (A**2):   1633 ;  0.21 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1633 ;  0.19 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1633 ;  0.22 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1633 ;  0.21 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1633 ;  0.15 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    E (A**2):   1633 ;  0.15 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    F (A**2):   1633 ;  0.17 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    G (A**2):   1633 ;  0.17 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : H I J K L M N O                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     H   1261       H    1270      4                      
REMARK   3           1     I   1261       I    1270      4                      
REMARK   3           1     J   1261       J    1270      4                      
REMARK   3           1     K   1261       K    1270      4                      
REMARK   3           1     L   1261       L    1270      4                      
REMARK   3           1     M   1261       M    1267      4                      
REMARK   3           1     N   1262       N    1266      4                      
REMARK   3           1     O   1261       O    1267      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    H    (A):     44 ;  0.36 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    I    (A):     44 ;  0.47 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    J    (A):     44 ;  0.37 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    K    (A):     44 ;  0.35 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    L    (A):     44 ;  0.57 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    M    (A):     44 ;  0.62 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    N    (A):     44 ;  0.72 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    O    (A):     44 ;  0.82 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    H (A**2):     44 ;  0.20 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    I (A**2):     44 ;  0.24 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    J (A**2):     44 ;  0.43 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    K (A**2):     44 ;  0.13 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    L (A**2):     44 ;  0.15 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    M (A**2):     44 ;  0.12 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    N (A**2):     44 ;  0.17 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    O (A**2):     44 ;  0.26 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
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 :   X  1649        X  1859                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2500 -20.1340 -22.3120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2807 T22:  -0.5786                                     
REMARK   3      T33:  -0.2324 T12:  -0.1346                                     
REMARK   3      T13:  -0.1056 T23:   0.0685                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1641 L22:   3.2091                                     
REMARK   3      L33:  11.3435 L12:  -0.3844                                     
REMARK   3      L13:   3.1129 L23:  -1.2292                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0354 S12:   0.2076 S13:  -0.1394                       
REMARK   3      S21:  -0.0025 S22:   0.1498 S23:  -0.0262                       
REMARK   3      S31:   0.3333 S32:  -0.0472 S33:  -0.1852                       
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  1649        A  1859                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.9080   2.2550   2.9220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0469 T22:  -0.3279                                     
REMARK   3      T33:  -0.4108 T12:   0.2262                                     
REMARK   3      T13:  -0.2316 T23:   0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4011 L22:   9.2122                                     
REMARK   3      L33:   5.0932 L12:   1.5303                                     
REMARK   3      L13:  -0.0941 L23:  -2.7865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1756 S12:  -0.0657 S13:   0.0655                       
REMARK   3      S21:   0.4301 S22:   0.0681 S23:   0.0063                       
REMARK   3      S31:  -0.3927 S32:  -0.4557 S33:   0.1076                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1649        B  1859                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.8350 -22.7050  25.1420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0732 T22:  -0.3559                                     
REMARK   3      T33:  -0.5310 T12:   0.1268                                     
REMARK   3      T13:  -0.1012 T23:   0.0449                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6630 L22:   8.3943                                     
REMARK   3      L33:   2.6954 L12:  -2.6045                                     
REMARK   3      L13:   0.1973 L23:   0.6395                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2283 S12:  -0.1083 S13:   0.4026                       
REMARK   3      S21:   0.2417 S22:   0.0431 S23:  -0.4627                       
REMARK   3      S31:  -0.0805 S32:   0.1497 S33:   0.1852                       
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 :   C  1649        C  1859                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.1800 -49.8100  46.4570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3904 T22:  -0.4770                                     
REMARK   3      T33:  -0.2773 T12:   0.1037                                     
REMARK   3      T13:   0.2109 T23:   0.1206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1639 L22:   4.8604                                     
REMARK   3      L33:   9.8292 L12:  -0.1083                                     
REMARK   3      L13:   1.1154 L23:   1.8893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2423 S12:   0.0434 S13:   0.0865                       
REMARK   3      S21:   0.2291 S22:   0.2188 S23:   0.3588                       
REMARK   3      S31:   0.1041 S32:   0.1844 S33:   0.0235                       
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 :   D  1649        D  1859                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.5270 -19.1740 -45.6330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2865 T22:   0.1083                                     
REMARK   3      T33:   0.4388 T12:  -0.0024                                     
REMARK   3      T13:   0.2075 T23:   0.3674                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3479 L22:   1.6846                                     
REMARK   3      L33:   2.3647 L12:   0.8483                                     
REMARK   3      L13:  -0.1058 L23:   0.1995                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2058 S12:   0.2156 S13:  -0.5312                       
REMARK   3      S21:  -0.2996 S22:  -0.1403 S23:  -1.1105                       
REMARK   3      S31:   0.5674 S32:   0.5612 S33:   0.3461                       
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 :   E  1649        E  1859                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.2140  -0.8410  28.0020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2751 T22:   0.1667                                     
REMARK   3      T33:   0.4715 T12:  -0.0322                                     
REMARK   3      T13:  -0.2364 T23:  -0.3618                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.9444 L22:   0.3504                                     
REMARK   3      L33:   2.8881 L12:  -0.8598                                     
REMARK   3      L13:   2.7560 L23:  -0.9924                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1704 S12:   0.5383 S13:   0.1848                       
REMARK   3      S21:  -0.3696 S22:   0.2442 S23:  -0.3370                       
REMARK   3      S31:  -0.1414 S32:   0.9553 S33:  -0.0738                       
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 :   F  1649        F  1859                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.7480  29.8670  -3.7050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9295 T22:  -0.1453                                     
REMARK   3      T33:  -0.1306 T12:   0.7081                                     
REMARK   3      T13:   0.0334 T23:   0.0424                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4156 L22:   4.9333                                     
REMARK   3      L33:   5.4473 L12:   1.9935                                     
REMARK   3      L13:   1.6929 L23:  -0.2970                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3491 S12:  -0.0567 S13:   0.0139                       
REMARK   3      S21:   1.0036 S22:   0.6974 S23:   0.7942                       
REMARK   3      S31:  -0.5993 S32:  -1.1226 S33:  -0.3484                       
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 :   G  1649        G  1859                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.6640  46.7180 -23.4830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5277 T22:  -0.0925                                     
REMARK   3      T33:   0.2105 T12:   0.1402                                     
REMARK   3      T13:  -0.5262 T23:  -0.1221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7521 L22:   5.8583                                     
REMARK   3      L33:   4.1594 L12:  -2.0263                                     
REMARK   3      L13:  -1.2525 L23:  -0.3988                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4402 S12:  -0.1914 S13:   0.2784                       
REMARK   3      S21:   0.5174 S22:   0.1875 S23:  -1.3789                       
REMARK   3      S31:  -0.1123 S32:   0.9776 S33:   0.2527                       
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 :   H  1261        H  1270                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6860 -14.8510 -16.9600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3732 T22:   0.0960                                     
REMARK   3      T33:  -0.0911 T12:   0.0319                                     
REMARK   3      T13:  -0.0639 T23:  -0.0553                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.7702 L22:  15.7838                                     
REMARK   3      L33:   0.2555 L12:  -2.1544                                     
REMARK   3      L13:  -1.8216 L23:  -0.1897                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -2.0493 S12:  -2.3021 S13:   1.1553                       
REMARK   3      S21:   1.3986 S22:   0.7691 S23:   0.6077                       
REMARK   3      S31:  -1.2759 S32:  -1.7339 S33:   1.2801                       
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 :   I  1261        I  1270                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8940   8.7660  11.1660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2875 T22:   0.0047                                     
REMARK   3      T33:   0.1414 T12:   0.1366                                     
REMARK   3      T13:  -0.1098 T23:   0.0819                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2131 L22:  17.1476                                     
REMARK   3      L33:   5.0305 L12:  -3.9049                                     
REMARK   3      L13:   1.9101 L23:   6.4173                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.9208 S12:  -0.8466 S13:   0.4429                       
REMARK   3      S21:  -1.1457 S22:  -0.3885 S23:   2.2041                       
REMARK   3      S31:   1.0834 S32:  -2.0592 S33:  -1.5323                       
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 :   J  1261        J  1270                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.7060 -27.7070  32.1220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0572 T22:   0.0336                                     
REMARK   3      T33:   0.0152 T12:  -0.0889                                     
REMARK   3      T13:  -0.2933 T23:  -0.0385                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.4115 L22:  45.4439                                     
REMARK   3      L33:  35.9875 L12:  13.7649                                     
REMARK   3      L13: -22.3507 L23: -14.8093                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.2022 S12:   2.9006 S13:   3.7896                       
REMARK   3      S21:   1.8501 S22:  -4.3158 S23:  -4.2489                       
REMARK   3      S31:   0.2980 S32:   2.9825 S33:   5.5180                       
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 :   K  1258        K  1270                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.6900 -58.6300  51.9140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0400 T22:   0.2049                                     
REMARK   3      T33:   0.0627 T12:  -0.2015                                     
REMARK   3      T13:   0.1573 T23:   0.0805                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3262 L22:   6.6754                                     
REMARK   3      L33:  21.5480 L12:   3.4324                                     
REMARK   3      L13:   1.5081 L23:   4.3048                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.3294 S12:  -1.0905 S13:  -1.3187                       
REMARK   3      S21:   0.9807 S22:  -1.1119 S23:   0.8874                       
REMARK   3      S31:   0.0428 S32:  -1.4704 S33:  -0.2174                       
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 :   L  1261        L  1270                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.2840  -7.6010 -42.8670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5215 T22:   0.3093                                     
REMARK   3      T33:   0.0608 T12:  -0.3371                                     
REMARK   3      T13:  -0.3567 T23:   0.0222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  59.8464 L22:  63.6514                                     
REMARK   3      L33:  46.9539 L12:  25.0520                                     
REMARK   3      L13: -50.9921 L23: -15.1773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.2495 S12:  -0.0568 S13:   0.7351                       
REMARK   3      S21:  -3.2620 S22:  -1.0318 S23:   2.2169                       
REMARK   3      S31:  -0.2646 S32:  -0.8267 S33:  -0.2178                       
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 :   M  1261        M  1267                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.7010  -5.0140  39.4140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7319 T22:   0.1213                                     
REMARK   3      T33:   0.4299 T12:   0.0265                                     
REMARK   3      T13:  -0.4423 T23:   0.2515                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  30.9281 L22:  39.4493                                     
REMARK   3      L33:  50.4734 L12:   3.0850                                     
REMARK   3      L13: -24.1383 L23:  32.7806                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   3.4587 S12:  -3.2812 S13:  -3.3024                       
REMARK   3      S21:   4.3157 S22:   1.0651 S23:  -0.3703                       
REMARK   3      S31:   1.5247 S32:   0.0456 S33:  -4.5238                       
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 :   N  1262        N  1266                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5520  42.4550  -1.5180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5031 T22:  -0.0799                                     
REMARK   3      T33:  -0.0745 T12:   0.2387                                     
REMARK   3      T13:   0.0287 T23:  -0.2147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  96.9020 L22:  79.8136                                     
REMARK   3      L33:  47.0212 L12:  11.6783                                     
REMARK   3      L13:  21.4068 L23:  -4.7889                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   2.4167 S12:  -2.7479 S13:  -1.4383                       
REMARK   3      S21:   0.9159 S22:  -4.4141 S23:  -0.6739                       
REMARK   3      S31:  -0.7456 S32:   0.4809 S33:   1.9974                       
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 :   O  1261        O  1267                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.2280  50.1880 -11.4730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5688 T22:   0.0832                                     
REMARK   3      T33:   0.4112 T12:   0.2091                                     
REMARK   3      T13:  -0.3552 T23:  -0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11: 153.8320 L22:  42.6651                                     
REMARK   3      L33:  42.4008 L12:  52.4709                                     
REMARK   3      L13: -73.6182 L23: -33.8555                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   3.8470 S12:   2.9738 S13:   2.1561                       
REMARK   3      S21:   2.2264 S22:   0.3501 S23:   1.8069                       
REMARK   3      S31:  -1.7043 S32:  -0.3133 S33:  -4.1970                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3COJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000047025.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97905                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42426                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.11800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7876                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.843                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: SNB THEN SOLVE/RESOLVE, PHASER                        
REMARK 200 STARTING MODEL: PDB ENTRY 1JNX                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE (PH 4.5), 25-27%   
REMARK 280  (V/V) PEG400, AND 200 MM CALCIUM ACETATE, VAPOR DIFFUSION,          
REMARK 280  SITTING DROP, TEMPERATURE 294K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       41.66500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       97.32150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       90.75650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       97.32150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       41.66500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       90.75650            
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, 6, 7, 8                                  
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.2 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, H                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.6 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.9 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, J                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, K                                  
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.9 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, L                                  
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 680 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.1 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, M                                  
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: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, N                                  
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: 8                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 770 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, O                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET X  1625                                                      
REMARK 465     GLY X  1626                                                      
REMARK 465     SER X  1627                                                      
REMARK 465     SER X  1628                                                      
REMARK 465     HIS X  1629                                                      
REMARK 465     HIS X  1630                                                      
REMARK 465     HIS X  1631                                                      
REMARK 465     HIS X  1632                                                      
REMARK 465     HIS X  1633                                                      
REMARK 465     HIS X  1634                                                      
REMARK 465     SER X  1635                                                      
REMARK 465     SER X  1636                                                      
REMARK 465     GLY X  1637                                                      
REMARK 465     LEU X  1638                                                      
REMARK 465     VAL X  1639                                                      
REMARK 465     PRO X  1640                                                      
REMARK 465     ARG X  1641                                                      
REMARK 465     GLY X  1642                                                      
REMARK 465     SER X  1643                                                      
REMARK 465     HIS X  1644                                                      
REMARK 465     MET X  1645                                                      
REMARK 465     VAL X  1646                                                      
REMARK 465     ASN X  1647                                                      
REMARK 465     GLU X  1694                                                      
REMARK 465     GLU X  1817                                                      
REMARK 465     ASP X  1818                                                      
REMARK 465     ASN X  1819                                                      
REMARK 465     MET A  1625                                                      
REMARK 465     GLY A  1626                                                      
REMARK 465     SER A  1627                                                      
REMARK 465     SER A  1628                                                      
REMARK 465     HIS A  1629                                                      
REMARK 465     HIS A  1630                                                      
REMARK 465     HIS A  1631                                                      
REMARK 465     HIS A  1632                                                      
REMARK 465     HIS A  1633                                                      
REMARK 465     HIS A  1634                                                      
REMARK 465     SER A  1635                                                      
REMARK 465     SER A  1636                                                      
REMARK 465     GLY A  1637                                                      
REMARK 465     LEU A  1638                                                      
REMARK 465     VAL A  1639                                                      
REMARK 465     PRO A  1640                                                      
REMARK 465     ARG A  1641                                                      
REMARK 465     GLY A  1642                                                      
REMARK 465     SER A  1643                                                      
REMARK 465     HIS A  1644                                                      
REMARK 465     MET A  1645                                                      
REMARK 465     VAL A  1646                                                      
REMARK 465     ASN A  1647                                                      
REMARK 465     GLU A  1694                                                      
REMARK 465     GLU A  1817                                                      
REMARK 465     ASP A  1818                                                      
REMARK 465     ASN A  1819                                                      
REMARK 465     MET B  1625                                                      
REMARK 465     GLY B  1626                                                      
REMARK 465     SER B  1627                                                      
REMARK 465     SER B  1628                                                      
REMARK 465     HIS B  1629                                                      
REMARK 465     HIS B  1630                                                      
REMARK 465     HIS B  1631                                                      
REMARK 465     HIS B  1632                                                      
REMARK 465     HIS B  1633                                                      
REMARK 465     HIS B  1634                                                      
REMARK 465     SER B  1635                                                      
REMARK 465     SER B  1636                                                      
REMARK 465     GLY B  1637                                                      
REMARK 465     LEU B  1638                                                      
REMARK 465     VAL B  1639                                                      
REMARK 465     PRO B  1640                                                      
REMARK 465     ARG B  1641                                                      
REMARK 465     GLY B  1642                                                      
REMARK 465     SER B  1643                                                      
REMARK 465     HIS B  1644                                                      
REMARK 465     MET B  1645                                                      
REMARK 465     VAL B  1646                                                      
REMARK 465     ASN B  1647                                                      
REMARK 465     GLU B  1694                                                      
REMARK 465     GLU B  1817                                                      
REMARK 465     ASP B  1818                                                      
REMARK 465     ASN B  1819                                                      
REMARK 465     MET C  1625                                                      
REMARK 465     GLY C  1626                                                      
REMARK 465     SER C  1627                                                      
REMARK 465     SER C  1628                                                      
REMARK 465     HIS C  1629                                                      
REMARK 465     HIS C  1630                                                      
REMARK 465     HIS C  1631                                                      
REMARK 465     HIS C  1632                                                      
REMARK 465     HIS C  1633                                                      
REMARK 465     HIS C  1634                                                      
REMARK 465     SER C  1635                                                      
REMARK 465     SER C  1636                                                      
REMARK 465     GLY C  1637                                                      
REMARK 465     LEU C  1638                                                      
REMARK 465     VAL C  1639                                                      
REMARK 465     PRO C  1640                                                      
REMARK 465     ARG C  1641                                                      
REMARK 465     GLY C  1642                                                      
REMARK 465     SER C  1643                                                      
REMARK 465     HIS C  1644                                                      
REMARK 465     MET C  1645                                                      
REMARK 465     VAL C  1646                                                      
REMARK 465     ASN C  1647                                                      
REMARK 465     GLU C  1694                                                      
REMARK 465     GLU C  1817                                                      
REMARK 465     ASP C  1818                                                      
REMARK 465     ASN C  1819                                                      
REMARK 465     MET D  1625                                                      
REMARK 465     GLY D  1626                                                      
REMARK 465     SER D  1627                                                      
REMARK 465     SER D  1628                                                      
REMARK 465     HIS D  1629                                                      
REMARK 465     HIS D  1630                                                      
REMARK 465     HIS D  1631                                                      
REMARK 465     HIS D  1632                                                      
REMARK 465     HIS D  1633                                                      
REMARK 465     HIS D  1634                                                      
REMARK 465     SER D  1635                                                      
REMARK 465     SER D  1636                                                      
REMARK 465     GLY D  1637                                                      
REMARK 465     LEU D  1638                                                      
REMARK 465     VAL D  1639                                                      
REMARK 465     PRO D  1640                                                      
REMARK 465     ARG D  1641                                                      
REMARK 465     GLY D  1642                                                      
REMARK 465     SER D  1643                                                      
REMARK 465     HIS D  1644                                                      
REMARK 465     MET D  1645                                                      
REMARK 465     VAL D  1646                                                      
REMARK 465     ASN D  1647                                                      
REMARK 465     LYS D  1648                                                      
REMARK 465     GLU D  1694                                                      
REMARK 465     GLU D  1817                                                      
REMARK 465     ASP D  1818                                                      
REMARK 465     ASN D  1819                                                      
REMARK 465     MET E  1625                                                      
REMARK 465     GLY E  1626                                                      
REMARK 465     SER E  1627                                                      
REMARK 465     SER E  1628                                                      
REMARK 465     HIS E  1629                                                      
REMARK 465     HIS E  1630                                                      
REMARK 465     HIS E  1631                                                      
REMARK 465     HIS E  1632                                                      
REMARK 465     HIS E  1633                                                      
REMARK 465     HIS E  1634                                                      
REMARK 465     SER E  1635                                                      
REMARK 465     SER E  1636                                                      
REMARK 465     GLY E  1637                                                      
REMARK 465     LEU E  1638                                                      
REMARK 465     VAL E  1639                                                      
REMARK 465     PRO E  1640                                                      
REMARK 465     ARG E  1641                                                      
REMARK 465     GLY E  1642                                                      
REMARK 465     SER E  1643                                                      
REMARK 465     HIS E  1644                                                      
REMARK 465     MET E  1645                                                      
REMARK 465     VAL E  1646                                                      
REMARK 465     ASN E  1647                                                      
REMARK 465     LYS E  1648                                                      
REMARK 465     GLU E  1694                                                      
REMARK 465     GLU E  1817                                                      
REMARK 465     ASP E  1818                                                      
REMARK 465     ASN E  1819                                                      
REMARK 465     MET F  1625                                                      
REMARK 465     GLY F  1626                                                      
REMARK 465     SER F  1627                                                      
REMARK 465     SER F  1628                                                      
REMARK 465     HIS F  1629                                                      
REMARK 465     HIS F  1630                                                      
REMARK 465     HIS F  1631                                                      
REMARK 465     HIS F  1632                                                      
REMARK 465     HIS F  1633                                                      
REMARK 465     HIS F  1634                                                      
REMARK 465     SER F  1635                                                      
REMARK 465     SER F  1636                                                      
REMARK 465     GLY F  1637                                                      
REMARK 465     LEU F  1638                                                      
REMARK 465     VAL F  1639                                                      
REMARK 465     PRO F  1640                                                      
REMARK 465     ARG F  1641                                                      
REMARK 465     GLY F  1642                                                      
REMARK 465     SER F  1643                                                      
REMARK 465     HIS F  1644                                                      
REMARK 465     MET F  1645                                                      
REMARK 465     VAL F  1646                                                      
REMARK 465     ASN F  1647                                                      
REMARK 465     LYS F  1648                                                      
REMARK 465     GLU F  1694                                                      
REMARK 465     GLU F  1817                                                      
REMARK 465     ASP F  1818                                                      
REMARK 465     ASN F  1819                                                      
REMARK 465     MET G  1625                                                      
REMARK 465     GLY G  1626                                                      
REMARK 465     SER G  1627                                                      
REMARK 465     SER G  1628                                                      
REMARK 465     HIS G  1629                                                      
REMARK 465     HIS G  1630                                                      
REMARK 465     HIS G  1631                                                      
REMARK 465     HIS G  1632                                                      
REMARK 465     HIS G  1633                                                      
REMARK 465     HIS G  1634                                                      
REMARK 465     SER G  1635                                                      
REMARK 465     SER G  1636                                                      
REMARK 465     GLY G  1637                                                      
REMARK 465     LEU G  1638                                                      
REMARK 465     VAL G  1639                                                      
REMARK 465     PRO G  1640                                                      
REMARK 465     ARG G  1641                                                      
REMARK 465     GLY G  1642                                                      
REMARK 465     SER G  1643                                                      
REMARK 465     HIS G  1644                                                      
REMARK 465     MET G  1645                                                      
REMARK 465     VAL G  1646                                                      
REMARK 465     ASN G  1647                                                      
REMARK 465     GLU G  1694                                                      
REMARK 465     TRP G  1815                                                      
REMARK 465     THR G  1816                                                      
REMARK 465     GLU G  1817                                                      
REMARK 465     ASP G  1818                                                      
REMARK 465     ASN G  1819                                                      
REMARK 465     ASP H  1258                                                      
REMARK 465     SER H  1259                                                      
REMARK 465     PRO H  1260                                                      
REMARK 465     ASP I  1258                                                      
REMARK 465     SER I  1259                                                      
REMARK 465     PRO I  1260                                                      
REMARK 465     ASP J  1258                                                      
REMARK 465     SER J  1259                                                      
REMARK 465     PRO J  1260                                                      
REMARK 465     ASP L  1258                                                      
REMARK 465     SER L  1259                                                      
REMARK 465     PRO L  1260                                                      
REMARK 465     ASP M  1258                                                      
REMARK 465     SER M  1259                                                      
REMARK 465     PRO M  1260                                                      
REMARK 465     GLU M  1268                                                      
REMARK 465     ALA M  1269                                                      
REMARK 465     GLY M  1270                                                      
REMARK 465     ASP N  1258                                                      
REMARK 465     SER N  1259                                                      
REMARK 465     PRO N  1260                                                      
REMARK 465     PRO N  1261                                                      
REMARK 465     PRO N  1267                                                      
REMARK 465     GLU N  1268                                                      
REMARK 465     ALA N  1269                                                      
REMARK 465     GLY N  1270                                                      
REMARK 465     ASP O  1258                                                      
REMARK 465     SER O  1259                                                      
REMARK 465     PRO O  1260                                                      
REMARK 465     GLU O  1268                                                      
REMARK 465     ALA O  1269                                                      
REMARK 465     GLY O  1270                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PHE F1821    CB   CG   CD1  CD2  CE1  CE2  CZ                    
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 X1739   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B1840   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP E1757   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP G1733   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR X1681     -159.14   -120.37                                   
REMARK 500    THR X1691     -137.64   -138.18                                   
REMARK 500    ASP X1692      -19.15   -155.57                                   
REMARK 500    GLU X1725     -109.88    -77.04                                   
REMARK 500    ARG X1726      -37.68   -162.17                                   
REMARK 500    ASP X1739      -69.18   -163.05                                   
REMARK 500    VAL X1740       -7.34   -177.77                                   
REMARK 500    VAL X1741      -86.28    -64.56                                   
REMARK 500    ARG X1744       18.20    -60.92                                   
REMARK 500    ASN X1745      -78.47    -95.45                                   
REMARK 500    GLN X1747       91.60    -53.30                                   
REMARK 500    ASP X1757        7.88    -68.75                                   
REMARK 500    ARG X1758       65.55   -159.17                                   
REMARK 500    PHE X1761       35.00    -88.35                                   
REMARK 500    ARG X1762      -71.46    -41.27                                   
REMARK 500    THR X1773     -135.04    -79.17                                   
REMARK 500    ASN X1774       47.79    -68.25                                   
REMARK 500    MET X1775      104.61   -160.42                                   
REMARK 500    CYS X1787       41.94    -85.99                                   
REMARK 500    ASP X1813      -30.19    -31.81                                   
REMARK 500    TRP X1815     -142.16   -119.44                                   
REMARK 500    PHE X1821        4.35   -157.52                                   
REMARK 500    ALA X1823      -71.51    -62.24                                   
REMARK 500    ILE X1824      -62.29     -6.82                                   
REMARK 500    GLN X1846      -24.39   -140.59                                   
REMARK 500    CYS X1847       72.14     65.51                                   
REMARK 500    ARG A1726        4.67     84.10                                   
REMARK 500    MET A1728       98.60    -64.26                                   
REMARK 500    ASP A1739      -75.81   -163.39                                   
REMARK 500    VAL A1740      -16.82   -166.84                                   
REMARK 500    ASN A1745     -151.91    -88.96                                   
REMARK 500    GLN A1756      -24.14   -156.59                                   
REMARK 500    ARG A1762      -90.33     10.80                                   
REMARK 500    THR A1773     -118.70    -99.29                                   
REMARK 500    ASN A1774       21.44    -69.73                                   
REMARK 500    THR A1802       75.56    -60.08                                   
REMARK 500    ALA A1830      143.03   -176.00                                   
REMARK 500    GLU A1836      -18.85    -48.80                                   
REMARK 500    ASP A1851      -80.48    -29.39                                   
REMARK 500    HIS B1673       -3.92     67.45                                   
REMARK 500    GLU B1698     -117.70    -80.49                                   
REMARK 500    ARG B1699       83.86   -177.46                                   
REMARK 500    GLU B1725     -128.72    -84.40                                   
REMARK 500    ARG B1726      -24.44   -149.24                                   
REMARK 500    HIS B1732       -7.53    -53.83                                   
REMARK 500    ASP B1739      -93.82   -161.62                                   
REMARK 500    VAL B1740       27.47   -165.52                                   
REMARK 500    VAL B1741      -79.97   -108.72                                   
REMARK 500    ARG B1744     -120.21   -114.08                                   
REMARK 500    ASN B1745      -65.84     24.71                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     144 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2AZM   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MDC1 BRCT REPEAT IN COMPLEX WITH THE        
REMARK 900 HISTONE TAIL OF GAMMA-H2AX                                           
REMARK 900 RELATED ID: 1T2V   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL BASIS OF PHOSPHO-PEPTIDE RECOGNITION BY THE BRCT DOMAIN   
REMARK 900 OF BRCA1, STRUCTURE WITH PHOSPHOPEPTIDE                              
REMARK 900 RELATED ID: 1T29   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE BRCA1 BRCT REPEATS BOUND TO A               
REMARK 900 PHOSPHORYLATED BACH1 PEPTIDE                                         
REMARK 900 RELATED ID: 1T15   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE BRCA1 BRCT DOMAINS IN COMPLEX WITH THE      
REMARK 900 PHOSPHORYLATED INTERACTING REGION FROM BACH1 HELICASE                
REMARK 900 RELATED ID: 1Y98   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE BRCT REPEATS OF BRCA1 BOUND TO A CTIP               
REMARK 900 PHOSPHOPEPTIDE                                                       
DBREF  3COJ X 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  3COJ A 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  3COJ B 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  3COJ C 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  3COJ D 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  3COJ E 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  3COJ F 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  3COJ G 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  3COJ H 1258  1270  UNP    Q13085   ACACA_HUMAN   1258   1270             
DBREF  3COJ I 1258  1270  UNP    Q13085   ACACA_HUMAN   1258   1270             
DBREF  3COJ J 1258  1270  UNP    Q13085   ACACA_HUMAN   1258   1270             
DBREF  3COJ K 1258  1270  UNP    Q13085   ACACA_HUMAN   1258   1270             
DBREF  3COJ L 1258  1270  UNP    Q13085   ACACA_HUMAN   1258   1270             
DBREF  3COJ M 1258  1270  UNP    Q13085   ACACA_HUMAN   1258   1270             
DBREF  3COJ N 1258  1270  UNP    Q13085   ACACA_HUMAN   1258   1270             
DBREF  3COJ O 1258  1270  UNP    Q13085   ACACA_HUMAN   1258   1270             
SEQADV 3COJ MET X 1625  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY X 1626  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER X 1627  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER X 1628  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS X 1629  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS X 1630  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS X 1631  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS X 1632  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS X 1633  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS X 1634  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER X 1635  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER X 1636  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY X 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ LEU X 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ VAL X 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ PRO X 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ ARG X 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY X 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER X 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS X 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET X 1645  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET A 1625  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY A 1626  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER A 1627  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER A 1628  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS A 1629  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS A 1630  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS A 1631  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS A 1632  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS A 1633  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS A 1634  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER A 1635  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER A 1636  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY A 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ LEU A 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ VAL A 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ PRO A 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ ARG A 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY A 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER A 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS A 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET A 1645  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET B 1625  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY B 1626  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER B 1627  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER B 1628  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS B 1629  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS B 1630  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS B 1631  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS B 1632  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS B 1633  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS B 1634  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER B 1635  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER B 1636  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY B 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ LEU B 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ VAL B 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ PRO B 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ ARG B 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY B 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER B 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS B 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET B 1645  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET C 1625  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY C 1626  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER C 1627  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER C 1628  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS C 1629  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS C 1630  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS C 1631  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS C 1632  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS C 1633  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS C 1634  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER C 1635  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER C 1636  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY C 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ LEU C 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ VAL C 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ PRO C 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ ARG C 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY C 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER C 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS C 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET C 1645  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET D 1625  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY D 1626  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER D 1627  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER D 1628  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS D 1629  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS D 1630  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS D 1631  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS D 1632  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS D 1633  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS D 1634  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER D 1635  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER D 1636  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY D 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ LEU D 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ VAL D 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ PRO D 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ ARG D 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY D 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER D 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS D 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET D 1645  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET E 1625  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY E 1626  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER E 1627  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER E 1628  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS E 1629  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS E 1630  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS E 1631  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS E 1632  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS E 1633  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS E 1634  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER E 1635  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER E 1636  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY E 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ LEU E 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ VAL E 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ PRO E 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ ARG E 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY E 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER E 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS E 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET E 1645  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET F 1625  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY F 1626  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER F 1627  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER F 1628  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS F 1629  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS F 1630  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS F 1631  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS F 1632  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS F 1633  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS F 1634  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER F 1635  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER F 1636  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY F 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ LEU F 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ VAL F 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ PRO F 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ ARG F 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY F 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER F 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS F 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET F 1645  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET G 1625  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY G 1626  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER G 1627  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER G 1628  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS G 1629  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS G 1630  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS G 1631  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS G 1632  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS G 1633  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS G 1634  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER G 1635  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER G 1636  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY G 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ LEU G 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ VAL G 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ PRO G 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ ARG G 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ GLY G 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ SER G 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ HIS G 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 3COJ MET G 1645  UNP  P38398              EXPRESSION TAG                 
SEQRES   1 X  235  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 X  235  LEU VAL PRO ARG GLY SER HIS MET VAL ASN LYS ARG MET          
SEQRES   3 X  235  SER MET VAL VAL SER GLY LEU THR PRO GLU GLU PHE MET          
SEQRES   4 X  235  LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE THR LEU          
SEQRES   5 X  235  THR ASN LEU ILE THR GLU GLU THR THR HIS VAL VAL MET          
SEQRES   6 X  235  LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR LEU LYS          
SEQRES   7 X  235  TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL VAL SER          
SEQRES   8 X  235  TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG LYS MET          
SEQRES   9 X  235  LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP VAL VAL          
SEQRES  10 X  235  ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA ARG GLU          
SEQRES  11 X  235  SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU ILE CYS          
SEQRES  12 X  235  CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP GLN LEU          
SEQRES  13 X  235  GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL VAL LYS          
SEQRES  14 X  235  GLU LEU SER SER PHE THR LEU GLY THR GLY VAL HIS PRO          
SEQRES  15 X  235  ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU ASP ASN          
SEQRES  16 X  235  GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA PRO VAL          
SEQRES  17 X  235  VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA LEU TYR          
SEQRES  18 X  235  GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO GLN ILE          
SEQRES  19 X  235  PRO                                                          
SEQRES   1 A  235  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  235  LEU VAL PRO ARG GLY SER HIS MET VAL ASN LYS ARG MET          
SEQRES   3 A  235  SER MET VAL VAL SER GLY LEU THR PRO GLU GLU PHE MET          
SEQRES   4 A  235  LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE THR LEU          
SEQRES   5 A  235  THR ASN LEU ILE THR GLU GLU THR THR HIS VAL VAL MET          
SEQRES   6 A  235  LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR LEU LYS          
SEQRES   7 A  235  TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL VAL SER          
SEQRES   8 A  235  TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG LYS MET          
SEQRES   9 A  235  LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP VAL VAL          
SEQRES  10 A  235  ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA ARG GLU          
SEQRES  11 A  235  SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU ILE CYS          
SEQRES  12 A  235  CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP GLN LEU          
SEQRES  13 A  235  GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL VAL LYS          
SEQRES  14 A  235  GLU LEU SER SER PHE THR LEU GLY THR GLY VAL HIS PRO          
SEQRES  15 A  235  ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU ASP ASN          
SEQRES  16 A  235  GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA PRO VAL          
SEQRES  17 A  235  VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA LEU TYR          
SEQRES  18 A  235  GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO GLN ILE          
SEQRES  19 A  235  PRO                                                          
SEQRES   1 B  235  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  235  LEU VAL PRO ARG GLY SER HIS MET VAL ASN LYS ARG MET          
SEQRES   3 B  235  SER MET VAL VAL SER GLY LEU THR PRO GLU GLU PHE MET          
SEQRES   4 B  235  LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE THR LEU          
SEQRES   5 B  235  THR ASN LEU ILE THR GLU GLU THR THR HIS VAL VAL MET          
SEQRES   6 B  235  LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR LEU LYS          
SEQRES   7 B  235  TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL VAL SER          
SEQRES   8 B  235  TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG LYS MET          
SEQRES   9 B  235  LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP VAL VAL          
SEQRES  10 B  235  ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA ARG GLU          
SEQRES  11 B  235  SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU ILE CYS          
SEQRES  12 B  235  CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP GLN LEU          
SEQRES  13 B  235  GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL VAL LYS          
SEQRES  14 B  235  GLU LEU SER SER PHE THR LEU GLY THR GLY VAL HIS PRO          
SEQRES  15 B  235  ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU ASP ASN          
SEQRES  16 B  235  GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA PRO VAL          
SEQRES  17 B  235  VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA LEU TYR          
SEQRES  18 B  235  GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO GLN ILE          
SEQRES  19 B  235  PRO                                                          
SEQRES   1 C  235  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  235  LEU VAL PRO ARG GLY SER HIS MET VAL ASN LYS ARG MET          
SEQRES   3 C  235  SER MET VAL VAL SER GLY LEU THR PRO GLU GLU PHE MET          
SEQRES   4 C  235  LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE THR LEU          
SEQRES   5 C  235  THR ASN LEU ILE THR GLU GLU THR THR HIS VAL VAL MET          
SEQRES   6 C  235  LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR LEU LYS          
SEQRES   7 C  235  TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL VAL SER          
SEQRES   8 C  235  TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG LYS MET          
SEQRES   9 C  235  LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP VAL VAL          
SEQRES  10 C  235  ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA ARG GLU          
SEQRES  11 C  235  SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU ILE CYS          
SEQRES  12 C  235  CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP GLN LEU          
SEQRES  13 C  235  GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL VAL LYS          
SEQRES  14 C  235  GLU LEU SER SER PHE THR LEU GLY THR GLY VAL HIS PRO          
SEQRES  15 C  235  ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU ASP ASN          
SEQRES  16 C  235  GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA PRO VAL          
SEQRES  17 C  235  VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA LEU TYR          
SEQRES  18 C  235  GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO GLN ILE          
SEQRES  19 C  235  PRO                                                          
SEQRES   1 D  235  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  235  LEU VAL PRO ARG GLY SER HIS MET VAL ASN LYS ARG MET          
SEQRES   3 D  235  SER MET VAL VAL SER GLY LEU THR PRO GLU GLU PHE MET          
SEQRES   4 D  235  LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE THR LEU          
SEQRES   5 D  235  THR ASN LEU ILE THR GLU GLU THR THR HIS VAL VAL MET          
SEQRES   6 D  235  LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR LEU LYS          
SEQRES   7 D  235  TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL VAL SER          
SEQRES   8 D  235  TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG LYS MET          
SEQRES   9 D  235  LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP VAL VAL          
SEQRES  10 D  235  ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA ARG GLU          
SEQRES  11 D  235  SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU ILE CYS          
SEQRES  12 D  235  CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP GLN LEU          
SEQRES  13 D  235  GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL VAL LYS          
SEQRES  14 D  235  GLU LEU SER SER PHE THR LEU GLY THR GLY VAL HIS PRO          
SEQRES  15 D  235  ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU ASP ASN          
SEQRES  16 D  235  GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA PRO VAL          
SEQRES  17 D  235  VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA LEU TYR          
SEQRES  18 D  235  GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO GLN ILE          
SEQRES  19 D  235  PRO                                                          
SEQRES   1 E  235  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 E  235  LEU VAL PRO ARG GLY SER HIS MET VAL ASN LYS ARG MET          
SEQRES   3 E  235  SER MET VAL VAL SER GLY LEU THR PRO GLU GLU PHE MET          
SEQRES   4 E  235  LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE THR LEU          
SEQRES   5 E  235  THR ASN LEU ILE THR GLU GLU THR THR HIS VAL VAL MET          
SEQRES   6 E  235  LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR LEU LYS          
SEQRES   7 E  235  TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL VAL SER          
SEQRES   8 E  235  TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG LYS MET          
SEQRES   9 E  235  LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP VAL VAL          
SEQRES  10 E  235  ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA ARG GLU          
SEQRES  11 E  235  SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU ILE CYS          
SEQRES  12 E  235  CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP GLN LEU          
SEQRES  13 E  235  GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL VAL LYS          
SEQRES  14 E  235  GLU LEU SER SER PHE THR LEU GLY THR GLY VAL HIS PRO          
SEQRES  15 E  235  ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU ASP ASN          
SEQRES  16 E  235  GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA PRO VAL          
SEQRES  17 E  235  VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA LEU TYR          
SEQRES  18 E  235  GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO GLN ILE          
SEQRES  19 E  235  PRO                                                          
SEQRES   1 F  235  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 F  235  LEU VAL PRO ARG GLY SER HIS MET VAL ASN LYS ARG MET          
SEQRES   3 F  235  SER MET VAL VAL SER GLY LEU THR PRO GLU GLU PHE MET          
SEQRES   4 F  235  LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE THR LEU          
SEQRES   5 F  235  THR ASN LEU ILE THR GLU GLU THR THR HIS VAL VAL MET          
SEQRES   6 F  235  LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR LEU LYS          
SEQRES   7 F  235  TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL VAL SER          
SEQRES   8 F  235  TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG LYS MET          
SEQRES   9 F  235  LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP VAL VAL          
SEQRES  10 F  235  ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA ARG GLU          
SEQRES  11 F  235  SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU ILE CYS          
SEQRES  12 F  235  CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP GLN LEU          
SEQRES  13 F  235  GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL VAL LYS          
SEQRES  14 F  235  GLU LEU SER SER PHE THR LEU GLY THR GLY VAL HIS PRO          
SEQRES  15 F  235  ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU ASP ASN          
SEQRES  16 F  235  GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA PRO VAL          
SEQRES  17 F  235  VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA LEU TYR          
SEQRES  18 F  235  GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO GLN ILE          
SEQRES  19 F  235  PRO                                                          
SEQRES   1 G  235  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 G  235  LEU VAL PRO ARG GLY SER HIS MET VAL ASN LYS ARG MET          
SEQRES   3 G  235  SER MET VAL VAL SER GLY LEU THR PRO GLU GLU PHE MET          
SEQRES   4 G  235  LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE THR LEU          
SEQRES   5 G  235  THR ASN LEU ILE THR GLU GLU THR THR HIS VAL VAL MET          
SEQRES   6 G  235  LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR LEU LYS          
SEQRES   7 G  235  TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL VAL SER          
SEQRES   8 G  235  TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG LYS MET          
SEQRES   9 G  235  LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP VAL VAL          
SEQRES  10 G  235  ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA ARG GLU          
SEQRES  11 G  235  SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU ILE CYS          
SEQRES  12 G  235  CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP GLN LEU          
SEQRES  13 G  235  GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL VAL LYS          
SEQRES  14 G  235  GLU LEU SER SER PHE THR LEU GLY THR GLY VAL HIS PRO          
SEQRES  15 G  235  ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU ASP ASN          
SEQRES  16 G  235  GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA PRO VAL          
SEQRES  17 G  235  VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA LEU TYR          
SEQRES  18 G  235  GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO GLN ILE          
SEQRES  19 G  235  PRO                                                          
SEQRES   1 H   13  ASP SER PRO PRO GLN SEP PRO THR PHE PRO GLU ALA GLY          
SEQRES   1 I   13  ASP SER PRO PRO GLN SEP PRO THR PHE PRO GLU ALA GLY          
SEQRES   1 J   13  ASP SER PRO PRO GLN SEP PRO THR PHE PRO GLU ALA GLY          
SEQRES   1 K   13  ASP SER PRO PRO GLN SEP PRO THR PHE PRO GLU ALA GLY          
SEQRES   1 L   13  ASP SER PRO PRO GLN SEP PRO THR PHE PRO GLU ALA GLY          
SEQRES   1 M   13  ASP SER PRO PRO GLN SEP PRO THR PHE PRO GLU ALA GLY          
SEQRES   1 N   13  ASP SER PRO PRO GLN SEP PRO THR PHE PRO GLU ALA GLY          
SEQRES   1 O   13  ASP SER PRO PRO GLN SEP PRO THR PHE PRO GLU ALA GLY          
MODRES 3COJ SEP H 1263  SER  PHOSPHOSERINE                                      
MODRES 3COJ SEP I 1263  SER  PHOSPHOSERINE                                      
MODRES 3COJ SEP J 1263  SER  PHOSPHOSERINE                                      
MODRES 3COJ SEP K 1263  SER  PHOSPHOSERINE                                      
MODRES 3COJ SEP L 1263  SER  PHOSPHOSERINE                                      
MODRES 3COJ SEP M 1263  SER  PHOSPHOSERINE                                      
MODRES 3COJ SEP N 1263  SER  PHOSPHOSERINE                                      
MODRES 3COJ SEP O 1263  SER  PHOSPHOSERINE                                      
HET    SEP  H1263      10                                                       
HET    SEP  I1263      10                                                       
HET    SEP  J1263      10                                                       
HET    SEP  K1263      10                                                       
HET    SEP  L1263      10                                                       
HET    SEP  M1263      10                                                       
HET    SEP  N1263      10                                                       
HET    SEP  O1263      10                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   9  SEP    8(C3 H8 N O6 P)                                              
HELIX    1   1 THR X 1658  HIS X 1672  1                                  15    
HELIX    2   2 THR X 1700  GLY X 1710  1                                  11    
HELIX    3   3 TYR X 1716  GLU X 1725  1                                  10    
HELIX    4   4 ASN X 1730  PHE X 1734  5                                   5    
HELIX    5   5 GLN X 1747  SER X 1755  1                                   9    
HELIX    6   6 PRO X 1776  CYS X 1787  1                                  12    
HELIX    7   7 GLU X 1794  PHE X 1798  5                                   5    
HELIX    8   8 GLN X 1811  TRP X 1815  5                                   5    
HELIX    9   9 ALA X 1823  MET X 1827  5                                   5    
HELIX   10  10 ARG X 1835  TYR X 1845  1                                  11    
HELIX   11  11 LEU X 1850  LEU X 1854  5                                   5    
HELIX   12  12 THR A 1658  HIS A 1673  1                                  16    
HELIX   13  13 THR A 1700  GLY A 1709  1                                  10    
HELIX   14  14 TYR A 1716  ARG A 1726  1                                  11    
HELIX   15  15 ASN A 1730  PHE A 1734  5                                   5    
HELIX   16  16 GLN A 1747  SER A 1755  1                                   9    
HELIX   17  17 PRO A 1776  LEU A 1786  1                                  11    
HELIX   18  18 PRO A 1812  TRP A 1815  5                                   4    
HELIX   19  19 GLY A 1820  HIS A 1822  5                                   3    
HELIX   20  20 ALA A 1823  CYS A 1828  1                                   6    
HELIX   21  21 ARG A 1835  LEU A 1844  1                                  10    
HELIX   22  22 THR B 1658  HIS B 1672  1                                  15    
HELIX   23  23 THR B 1700  GLY B 1709  1                                  10    
HELIX   24  24 TYR B 1716  GLU B 1725  1                                  10    
HELIX   25  25 ASN B 1730  PHE B 1734  5                                   5    
HELIX   26  26 GLY B 1748  SER B 1755  1                                   8    
HELIX   27  27 PRO B 1776  CYS B 1787  1                                  12    
HELIX   28  28 GLU B 1794  PHE B 1798  5                                   5    
HELIX   29  29 ALA B 1823  CYS B 1828  1                                   6    
HELIX   30  30 ARG B 1835  TYR B 1845  1                                  11    
HELIX   31  31 LEU B 1850  LEU B 1854  5                                   5    
HELIX   32  32 THR C 1658  HIS C 1672  1                                  15    
HELIX   33  33 THR C 1700  GLY C 1710  1                                  11    
HELIX   34  34 TYR C 1716  ARG C 1726  1                                  11    
HELIX   35  35 ASN C 1730  GLU C 1735  5                                   6    
HELIX   36  36 GLN C 1747  SER C 1755  1                                   9    
HELIX   37  37 PRO C 1776  CYS C 1787  1                                  12    
HELIX   38  38 GLU C 1794  PHE C 1798  5                                   5    
HELIX   39  39 ARG C 1835  LEU C 1844  1                                  10    
HELIX   40  40 THR D 1658  HIS D 1672  1                                  15    
HELIX   41  41 THR D 1700  GLY D 1709  1                                  10    
HELIX   42  42 TYR D 1716  GLU D 1725  1                                  10    
HELIX   43  43 ASN D 1730  PHE D 1734  5                                   5    
HELIX   44  44 GLY D 1748  SER D 1755  1                                   8    
HELIX   45  45 PRO D 1776  CYS D 1787  1                                  12    
HELIX   46  46 GLN D 1811  TRP D 1815  5                                   5    
HELIX   47  47 ALA D 1823  CYS D 1828  1                                   6    
HELIX   48  48 ARG D 1835  LEU D 1844  1                                  10    
HELIX   49  49 THR E 1658  HIS E 1672  1                                  15    
HELIX   50  50 THR E 1700  GLY E 1709  1                                  10    
HELIX   51  51 TYR E 1716  ILE E 1723  1                                   8    
HELIX   52  52 ASN E 1730  PHE E 1734  5                                   5    
HELIX   53  53 GLN E 1747  SER E 1755  1                                   9    
HELIX   54  54 PRO E 1776  CYS E 1787  1                                  12    
HELIX   55  55 ALA E 1823  CYS E 1828  1                                   6    
HELIX   56  56 ARG E 1835  LEU E 1844  1                                  10    
HELIX   57  57 THR F 1658  HIS F 1672  1                                  15    
HELIX   58  58 THR F 1700  GLY F 1709  1                                  10    
HELIX   59  59 TYR F 1716  ARG F 1726  1                                  11    
HELIX   60  60 ASN F 1730  GLU F 1735  5                                   6    
HELIX   61  61 GLY F 1748  SER F 1755  1                                   8    
HELIX   62  62 PRO F 1776  CYS F 1787  1                                  12    
HELIX   63  63 GLN F 1811  TRP F 1815  5                                   5    
HELIX   64  64 ALA F 1823  CYS F 1828  1                                   6    
HELIX   65  65 ARG F 1835  TYR F 1845  1                                  11    
HELIX   66  66 THR G 1658  ARG G 1670  1                                  13    
HELIX   67  67 THR G 1700  GLY G 1709  1                                  10    
HELIX   68  68 TYR G 1716  ARG G 1726  1                                  11    
HELIX   69  69 ASN G 1730  GLU G 1735  5                                   6    
HELIX   70  70 GLY G 1748  SER G 1755  1                                   8    
HELIX   71  71 GLN G 1756  ARG G 1758  5                                   3    
HELIX   72  72 PRO G 1776  CYS G 1787  1                                  12    
HELIX   73  73 ARG G 1835  TYR G 1845  1                                  11    
SHEET    1   A 4 THR X1675  LEU X1676  0                                        
SHEET    2   A 4 SER X1651  SER X1655  1  N  MET X1652   O  THR X1675           
SHEET    3   A 4 HIS X1686  MET X1689  1  O  VAL X1688   N  VAL X1653           
SHEET    4   A 4 TRP X1712  SER X1715  1  O  TRP X1712   N  VAL X1687           
SHEET    1   B 4 SER X1790  VAL X1792  0                                        
SHEET    2   B 4 LEU X1764  CYS X1768  1  N  ILE X1766   O  SER X1790           
SHEET    3   B 4 HIS X1805  VAL X1810  1  O  VAL X1809   N  CYS X1767           
SHEET    4   B 4 VAL X1832  THR X1834  1  O  VAL X1833   N  VAL X1808           
SHEET    1   C 4 THR A1675  LEU A1676  0                                        
SHEET    2   C 4 SER A1651  SER A1655  1  N  MET A1652   O  THR A1675           
SHEET    3   C 4 HIS A1686  MET A1689  1  O  VAL A1688   N  VAL A1653           
SHEET    4   C 4 TRP A1712  SER A1715  1  O  VAL A1714   N  MET A1689           
SHEET    1   D 4 SER A1790  VAL A1792  0                                        
SHEET    2   D 4 LEU A1764  TYR A1769  1  N  ILE A1766   O  VAL A1792           
SHEET    3   D 4 HIS A1805  VAL A1810  1  O  VAL A1809   N  CYS A1767           
SHEET    4   D 4 VAL A1832  THR A1834  1  O  VAL A1833   N  VAL A1810           
SHEET    1   E 4 THR B1675  LEU B1676  0                                        
SHEET    2   E 4 SER B1651  SER B1655  1  N  MET B1652   O  THR B1675           
SHEET    3   E 4 THR B1684  MET B1689  1  O  HIS B1686   N  SER B1651           
SHEET    4   E 4 TRP B1712  SER B1715  1  O  TRP B1712   N  VAL B1687           
SHEET    1   F 4 SER B1790  VAL B1792  0                                        
SHEET    2   F 4 LEU B1764  CYS B1768  1  N  ILE B1766   O  SER B1790           
SHEET    3   F 4 HIS B1805  VAL B1810  1  O  ILE B1807   N  GLU B1765           
SHEET    4   F 4 VAL B1832  THR B1834  1  O  VAL B1833   N  VAL B1808           
SHEET    1   G 4 THR C1675  THR C1677  0                                        
SHEET    2   G 4 SER C1651  SER C1655  1  N  MET C1652   O  THR C1675           
SHEET    3   G 4 HIS C1686  MET C1689  1  O  VAL C1688   N  SER C1655           
SHEET    4   G 4 TRP C1712  SER C1715  1  O  TRP C1712   N  VAL C1687           
SHEET    1   H 4 SER C1790  VAL C1791  0                                        
SHEET    2   H 4 LEU C1764  CYS C1768  1  N  LEU C1764   O  SER C1790           
SHEET    3   H 4 HIS C1805  VAL C1810  1  O  HIS C1805   N  GLU C1765           
SHEET    4   H 4 VAL C1832  THR C1834  1  O  VAL C1833   N  VAL C1810           
SHEET    1   I 4 THR D1675  LEU D1676  0                                        
SHEET    2   I 4 SER D1651  SER D1655  1  N  MET D1652   O  THR D1675           
SHEET    3   I 4 THR D1684  MET D1689  1  O  THR D1685   N  SER D1651           
SHEET    4   I 4 TRP D1712  SER D1715  1  O  TRP D1712   N  VAL D1687           
SHEET    1   J 4 SER D1790  VAL D1791  0                                        
SHEET    2   J 4 LEU D1764  CYS D1768  1  N  LEU D1764   O  SER D1790           
SHEET    3   J 4 HIS D1805  VAL D1810  1  O  HIS D1805   N  GLU D1765           
SHEET    4   J 4 VAL D1832  THR D1834  1  O  VAL D1833   N  VAL D1808           
SHEET    1   K 4 THR E1675  THR E1677  0                                        
SHEET    2   K 4 SER E1651  SER E1655  1  N  MET E1652   O  THR E1675           
SHEET    3   K 4 HIS E1686  MET E1689  1  O  VAL E1688   N  VAL E1653           
SHEET    4   K 4 TRP E1712  SER E1715  1  O  TRP E1712   N  VAL E1687           
SHEET    1   L 4 SER E1790  VAL E1792  0                                        
SHEET    2   L 4 LEU E1764  CYS E1768  1  N  ILE E1766   O  SER E1790           
SHEET    3   L 4 HIS E1805  VAL E1810  1  O  HIS E1805   N  GLU E1765           
SHEET    4   L 4 VAL E1832  THR E1834  1  O  VAL E1833   N  VAL E1808           
SHEET    1   M 4 THR F1675  THR F1677  0                                        
SHEET    2   M 4 SER F1651  SER F1655  1  N  MET F1652   O  THR F1675           
SHEET    3   M 4 THR F1684  MET F1689  1  O  HIS F1686   N  VAL F1653           
SHEET    4   M 4 TRP F1712  SER F1715  1  O  VAL F1714   N  MET F1689           
SHEET    1   N 4 SER F1790  VAL F1791  0                                        
SHEET    2   N 4 LEU F1764  CYS F1768  1  N  ILE F1766   O  SER F1790           
SHEET    3   N 4 HIS F1805  VAL F1810  1  O  ILE F1807   N  GLU F1765           
SHEET    4   N 4 VAL F1832  THR F1834  1  O  VAL F1833   N  VAL F1808           
SHEET    1   O 4 THR G1675  THR G1677  0                                        
SHEET    2   O 4 SER G1651  SER G1655  1  N  MET G1652   O  THR G1675           
SHEET    3   O 4 HIS G1686  MET G1689  1  O  VAL G1688   N  SER G1655           
SHEET    4   O 4 TRP G1712  SER G1715  1  O  VAL G1714   N  MET G1689           
SHEET    1   P 4 VAL G1791  VAL G1792  0                                        
SHEET    2   P 4 LEU G1764  CYS G1767  1  N  ILE G1766   O  VAL G1792           
SHEET    3   P 4 HIS G1805  VAL G1810  1  O  HIS G1805   N  GLU G1765           
SHEET    4   P 4 VAL G1832  THR G1834  1  O  VAL G1833   N  VAL G1810           
LINK         C   GLN H1262                 N   SEP H1263     1555   1555  1.33  
LINK         C   SEP H1263                 N   PRO H1264     1555   1555  1.33  
LINK         C   GLN I1262                 N   SEP I1263     1555   1555  1.34  
LINK         C   SEP I1263                 N   PRO I1264     1555   1555  1.34  
LINK         C   GLN J1262                 N   SEP J1263     1555   1555  1.33  
LINK         C   SEP J1263                 N   PRO J1264     1555   1555  1.34  
LINK         C   GLN K1262                 N   SEP K1263     1555   1555  1.34  
LINK         C   SEP K1263                 N   PRO K1264     1555   1555  1.33  
LINK         C   GLN L1262                 N   SEP L1263     1555   1555  1.33  
LINK         C   SEP L1263                 N   PRO L1264     1555   1555  1.34  
LINK         C   GLN M1262                 N   SEP M1263     1555   1555  1.33  
LINK         C   SEP M1263                 N   PRO M1264     1555   1555  1.33  
LINK         C   GLN N1262                 N   SEP N1263     1555   1555  1.34  
LINK         C   SEP N1263                 N   PRO N1264     1555   1555  1.34  
LINK         C   GLN O1262                 N   SEP O1263     1555   1555  1.33  
LINK         C   SEP O1263                 N   PRO O1264     1555   1555  1.34  
CRYST1   83.330  181.513  194.643  90.00  90.00  90.00 P 21 21 21   32          
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      0.012000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005509  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005138        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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