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Database: PDB
Entry: 2OME
LinkDB: 2OME
Original site: 2OME 
HEADER    OXIDOREDUCTASE                          22-JAN-07   2OME              
TITLE     CRYSTAL STRUCTURE OF HUMAN CTBP2 DEHYDROGENASE COMPLEXED WITH NAD(H)  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C-TERMINAL-BINDING PROTEIN 2;                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: RESIDUES 31-364;                                           
COMPND   5 SYNONYM: CTBP2;                                                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CTBP2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    C-TERMINAL BINDING PROTEIN, CTBP2, DEHYDROGENASE, STRUCTURAL GENOMICS 
KEYWDS   2 CONSORTIUM, SGC, OXIDOREDUCTASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.S.PILKA,K.GUO,A.ROJKOVA,J.E.DEBRECZENI,K.L.KAVANAGH,F.VON DELFT,    
AUTHOR   2 C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,M.SUNDSTROM,U.OPPERMANN,          
AUTHOR   3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   4   18-OCT-17 2OME    1       REMARK                                   
REVDAT   3   13-JUL-11 2OME    1       VERSN                                    
REVDAT   2   24-FEB-09 2OME    1       VERSN                                    
REVDAT   1   06-FEB-07 2OME    0                                                
JRNL        AUTH   E.S.PILKA,K.GUO,A.ROJKOVA,J.E.DEBRECZENI,K.L.KAVANAGH,       
JRNL        AUTH 2 F.VON DELFT,C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,M.SUNDSTROM,  
JRNL        AUTH 3 U.OPPERMANN                                                  
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN CTBP2 DEHYDROGENASE COMPLEXED     
JRNL        TITL 2 WITH NAD(H)                                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 78004                          
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) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4104                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5765                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3610                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 298                          
REMARK   3   BIN FREE R VALUE                    : 0.3870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 20223                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 352                                     
REMARK   3   SOLVENT ATOMS            : 184                                     
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) : 40.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.63000                                              
REMARK   3    B22 (A**2) : -4.83000                                             
REMARK   3    B33 (A**2) : 3.03000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.55000                                             
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): 0.378         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.300         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.465        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 20977 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A): 13837 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 28515 ; 1.458 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 33574 ; 1.116 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2635 ; 6.348 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   972 ;35.744 ;23.508       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3379 ;17.854 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   188 ;17.542 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3283 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 23591 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  4305 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4159 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 14266 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 10078 ; 0.184 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A): 11775 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   404 ; 0.149 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.023 ; 0.200       
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):    10 ; 0.181 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    18 ; 0.178 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.270 ; 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): 13575 ; 0.349 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5390 ; 0.128 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 20924 ; 0.548 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8470 ; 1.253 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7591 ; 2.014 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D E F G H                 
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     34       A     362      3                      
REMARK   3           1     B     34       B     362      3                      
REMARK   3           1     C     34       C     362      3                      
REMARK   3           1     D     34       D     362      3                      
REMARK   3           1     E     34       E     362      3                      
REMARK   3           1     F     34       F     362      3                      
REMARK   3           1     G     34       G     362      3                      
REMARK   3           1     H     34       H     362      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1930 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1930 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   1930 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   1930 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    E    (A):   1930 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    F    (A):   1930 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    G    (A):   1930 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    H    (A):   1930 ;  0.04 ;  0.05           
REMARK   3   LOOSE POSITIONAL   1    A    (A):   2050 ;  0.40 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   2050 ;  0.37 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    C    (A):   2050 ;  0.39 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    D    (A):   2050 ;  0.45 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    E    (A):   2050 ;  0.51 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    F    (A):   2050 ;  0.40 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    G    (A):   2050 ;  0.47 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    H    (A):   2050 ;  0.42 ;  5.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1930 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):   1930 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):   1930 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):   1930 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      1    E (A**2):   1930 ;  0.06 ;  0.50           
REMARK   3   TIGHT THERMAL      1    F (A**2):   1930 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      1    G (A**2):   1930 ;  0.06 ;  0.50           
REMARK   3   TIGHT THERMAL      1    H (A**2):   1930 ;  0.07 ;  0.50           
REMARK   3   LOOSE THERMAL      1    A (A**2):   2050 ;  1.23 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   2050 ;  1.16 ; 10.00           
REMARK   3   LOOSE THERMAL      1    C (A**2):   2050 ;  1.11 ; 10.00           
REMARK   3   LOOSE THERMAL      1    D (A**2):   2050 ;  1.01 ; 10.00           
REMARK   3   LOOSE THERMAL      1    E (A**2):   2050 ;  1.14 ; 10.00           
REMARK   3   LOOSE THERMAL      1    F (A**2):   2050 ;  1.08 ; 10.00           
REMARK   3   LOOSE THERMAL      1    G (A**2):   2050 ;  1.05 ; 10.00           
REMARK   3   LOOSE THERMAL      1    H (A**2):   2050 ;  1.06 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    33        A   362                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.5250  -3.5471   5.2843              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1701 T22:  -0.1656                                     
REMARK   3      T33:  -0.0942 T12:   0.0778                                     
REMARK   3      T13:  -0.2226 T23:  -0.1082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2218 L22:   3.4584                                     
REMARK   3      L33:   1.6492 L12:   0.4041                                     
REMARK   3      L13:  -0.1077 L23:  -0.6024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1284 S12:   0.1556 S13:  -0.3536                       
REMARK   3      S21:  -0.4701 S22:  -0.1088 S23:   0.2122                       
REMARK   3      S31:   0.2852 S32:   0.1155 S33:  -0.0196                       
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 :   B    33        B   362                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.1865  27.7267   6.9872              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1784 T22:  -0.0580                                     
REMARK   3      T33:  -0.1626 T12:  -0.0076                                     
REMARK   3      T13:   0.0327 T23:  -0.0437                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5598 L22:   2.7668                                     
REMARK   3      L33:   2.1457 L12:  -0.5827                                     
REMARK   3      L13:  -0.5366 L23:   0.5926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2530 S12:   0.2205 S13:   0.2951                       
REMARK   3      S21:  -0.4782 S22:  -0.0566 S23:  -0.4660                       
REMARK   3      S31:  -0.3931 S32:   0.3094 S33:  -0.1964                       
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 :   C    33        C   362                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.2374  38.4504  35.2989              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1343 T22:  -0.2394                                     
REMARK   3      T33:  -0.2701 T12:   0.0680                                     
REMARK   3      T13:  -0.0124 T23:  -0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5388 L22:   3.3065                                     
REMARK   3      L33:   1.4577 L12:   0.5130                                     
REMARK   3      L13:   0.4424 L23:   0.5640                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0320 S12:  -0.0899 S13:  -0.0585                       
REMARK   3      S21:   0.3652 S22:  -0.1072 S23:   0.4182                       
REMARK   3      S31:  -0.2301 S32:  -0.0419 S33:   0.1392                       
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 :   D    33        D   362                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.6206   7.5268  32.1255              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1511 T22:  -0.1283                                     
REMARK   3      T33:   0.3615 T12:  -0.0073                                     
REMARK   3      T13:   0.1554 T23:  -0.0569                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4804 L22:   1.8088                                     
REMARK   3      L33:   1.5408 L12:   0.3421                                     
REMARK   3      L13:   0.2570 L23:   0.5216                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0559 S12:  -0.2185 S13:  -0.3540                       
REMARK   3      S21:   0.2975 S22:  -0.1423 S23:   0.8519                       
REMARK   3      S31:   0.1522 S32:  -0.4137 S33:   0.1982                       
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 :   E    33        E   362                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.0779 -28.3094  53.5182              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1340 T22:  -0.0617                                     
REMARK   3      T33:   0.4669 T12:  -0.0296                                     
REMARK   3      T13:   0.4479 T23:  -0.0873                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6382 L22:   2.6596                                     
REMARK   3      L33:   1.3104 L12:   0.4488                                     
REMARK   3      L13:   0.3100 L23:   0.4010                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0973 S12:  -0.4086 S13:   0.3956                       
REMARK   3      S21:   0.8789 S22:  -0.2255 S23:   1.2529                       
REMARK   3      S31:  -0.0532 S32:  -0.3991 S33:   0.1282                       
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 :   F    33        F   362                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.8168 -59.1611  38.2784              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1371 T22:  -0.2191                                     
REMARK   3      T33:  -0.0524 T12:  -0.0082                                     
REMARK   3      T13:   0.0471 T23:   0.0708                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0443 L22:   3.5448                                     
REMARK   3      L33:   2.1079 L12:   0.5653                                     
REMARK   3      L13:   0.2327 L23:   1.1432                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2259 S12:  -0.0160 S13:   0.1313                       
REMARK   3      S21:   0.2820 S22:  -0.1182 S23:   0.7620                       
REMARK   3      S31:   0.1945 S32:  -0.1163 S33:  -0.1077                       
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 :   G    33        G   362                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.4720 -47.9929  38.4223              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1185 T22:   0.0354                                     
REMARK   3      T33:   0.0584 T12:   0.1163                                     
REMARK   3      T13:   0.0934 T23:   0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6275 L22:   3.4489                                     
REMARK   3      L33:   1.8890 L12:   0.8143                                     
REMARK   3      L13:  -0.0785 L23:   0.3194                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1475 S12:   0.0704 S13:  -0.8363                       
REMARK   3      S21:   0.1622 S22:   0.0470 S23:  -0.8612                       
REMARK   3      S31:   0.4368 S32:   0.5415 S33:   0.1004                       
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 :   H    33        H   362                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.3738 -16.9758  52.5326              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0124 T22:  -0.1073                                     
REMARK   3      T33:  -0.3224 T12:  -0.0605                                     
REMARK   3      T13:  -0.0434 T23:   0.0528                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3617 L22:   4.6161                                     
REMARK   3      L33:   1.6389 L12:  -0.5220                                     
REMARK   3      L13:   0.4036 L23:  -0.2360                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0117 S12:   0.0110 S13:   0.1897                       
REMARK   3      S21:   0.6038 S22:  -0.1399 S23:  -0.2861                       
REMARK   3      S31:  -0.2328 S32:   0.2213 S33:   0.1516                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2OME COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000041316.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-DEC-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99991                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 84796                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.770                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.310                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.14800                            
REMARK 200  R SYM                      (I) : 0.16200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.77                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.81000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.89000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1MX3, 1HL3                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M KSCN, 0.1M BIS-TRIS PROPANE, 20%    
REMARK 280  PEG3350, 10% ETHYLENE GLYCOL, PH 6.5, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       70.78700            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
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: 8460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 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: 8510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, 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 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     SER A    29                                                      
REMARK 465     MET A    30                                                      
REMARK 465     HIS A    31                                                      
REMARK 465     PRO A    32                                                      
REMARK 465     VAL A   363                                                      
REMARK 465     THR A   364                                                      
REMARK 465     SER B    29                                                      
REMARK 465     MET B    30                                                      
REMARK 465     HIS B    31                                                      
REMARK 465     PRO B    32                                                      
REMARK 465     VAL B   363                                                      
REMARK 465     THR B   364                                                      
REMARK 465     SER C    29                                                      
REMARK 465     MET C    30                                                      
REMARK 465     HIS C    31                                                      
REMARK 465     PRO C    32                                                      
REMARK 465     VAL C   363                                                      
REMARK 465     THR C   364                                                      
REMARK 465     SER D    29                                                      
REMARK 465     MET D    30                                                      
REMARK 465     HIS D    31                                                      
REMARK 465     PRO D    32                                                      
REMARK 465     VAL D   363                                                      
REMARK 465     THR D   364                                                      
REMARK 465     SER E    29                                                      
REMARK 465     MET E    30                                                      
REMARK 465     HIS E    31                                                      
REMARK 465     PRO E    32                                                      
REMARK 465     VAL E   363                                                      
REMARK 465     THR E   364                                                      
REMARK 465     SER F    29                                                      
REMARK 465     MET F    30                                                      
REMARK 465     HIS F    31                                                      
REMARK 465     PRO F    32                                                      
REMARK 465     VAL F   363                                                      
REMARK 465     THR F   364                                                      
REMARK 465     SER G    29                                                      
REMARK 465     MET G    30                                                      
REMARK 465     HIS G    31                                                      
REMARK 465     PRO G    32                                                      
REMARK 465     VAL G   363                                                      
REMARK 465     THR G   364                                                      
REMARK 465     SER H    29                                                      
REMARK 465     MET H    30                                                      
REMARK 465     HIS H    31                                                      
REMARK 465     PRO H    32                                                      
REMARK 465     VAL H   363                                                      
REMARK 465     THR H   364                                                      
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     LYS A  52    CD   CE   NZ                                        
REMARK 470     LYS A  71    CG   CD   CE   NZ                                   
REMARK 470     LYS A  94    NZ                                                  
REMARK 470     LYS A  96    NZ                                                  
REMARK 470     ILE A 207    CD1                                                 
REMARK 470     ILE A 217    CD1                                                 
REMARK 470     GLU A 247    CD   OE1  OE2                                       
REMARK 470     LYS A 279    NZ                                                  
REMARK 470     LYS A 311    CD   CE   NZ                                        
REMARK 470     ILE A 349    CD1                                                 
REMARK 470     ARG B  33    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  52    NZ                                                  
REMARK 470     HIS B  69    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU B  70    OE1  OE2                                            
REMARK 470     LYS B  96    CD   CE   NZ                                        
REMARK 470     LYS B 114    CD   CE   NZ                                        
REMARK 470     GLN B 214    CG   CD   OE1  NE2                                  
REMARK 470     ILE B 217    CD1                                                 
REMARK 470     GLU B 247    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 259    CE   NZ                                             
REMARK 470     LYS B 279    CD   CE   NZ                                        
REMARK 470     GLN B 283    CD   OE1  NE2                                       
REMARK 470     LYS B 311    NZ                                                  
REMARK 470     ARG B 348    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 349    CD1                                                 
REMARK 470     LYS C  52    NZ                                                  
REMARK 470     ARG C 161    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS C 311    CG   CD   CE   NZ                                   
REMARK 470     ASP C 312    CG   OD1  OD2                                       
REMARK 470     ARG D  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  52    CD   CE   NZ                                        
REMARK 470     GLN D  66    CG   CD   OE1  NE2                                  
REMARK 470     GLU D  67    CG   CD   OE1  OE2                                  
REMARK 470     HIS D  69    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU D  90    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  96    CG   CD   CE   NZ                                   
REMARK 470     ILE D 207    CD1                                                 
REMARK 470     GLU D 247    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 286    NZ                                                  
REMARK 470     ILE D 349    CD1                                                 
REMARK 470     ARG E  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG E  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE E  50    CG1  CG2  CD1                                       
REMARK 470     LYS E  52    CG   CD   CE   NZ                                   
REMARK 470     GLN E  63    OE1  NE2                                            
REMARK 470     THR E  65    OG1  CG2                                            
REMARK 470     GLN E  66    CG   CD   OE1  NE2                                  
REMARK 470     ILE E  68    CG1  CG2  CD1                                       
REMARK 470     HIS E  69    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU E  70    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  71    CG   CD   CE   NZ                                   
REMARK 470     GLU E  90    CD   OE1  OE2                                       
REMARK 470     LYS E  96    CG   CD   CE   NZ                                   
REMARK 470     LYS E 114    CE   NZ                                             
REMARK 470     GLU E 170    CG   CD   OE1  OE2                                  
REMARK 470     ILE E 207    CD1                                                 
REMARK 470     GLU E 247    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 279    CG   CD   CE   NZ                                   
REMARK 470     LYS E 311    CG   CD   CE   NZ                                   
REMARK 470     ASP E 312    CG   OD1  OD2                                       
REMARK 470     ILE E 349    CG1  CG2  CD1                                       
REMARK 470     GLU E 351    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 359    CD   CE   NZ                                        
REMARK 470     LYS F  52    NZ                                                  
REMARK 470     LYS F  71    NZ                                                  
REMARK 470     LYS F  96    CG   CD   CE   NZ                                   
REMARK 470     ARG F 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 200    CG   CD   CE   NZ                                   
REMARK 470     ILE F 217    CD1                                                 
REMARK 470     LYS F 279    CG   CD   CE   NZ                                   
REMARK 470     LYS F 311    CG   CD   CE   NZ                                   
REMARK 470     ASP F 312    CG   OD1  OD2                                       
REMARK 470     ARG G  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL G  36    CG1  CG2                                            
REMARK 470     LEU G  38    CD1  CD2                                            
REMARK 470     LYS G  52    CG   CD   CE   NZ                                   
REMARK 470     ASP G  53    CG   OD1  OD2                                       
REMARK 470     GLN G  66    CG   CD   OE1  NE2                                  
REMARK 470     HIS G  69    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU G  70    CG   CD   OE1  OE2                                  
REMARK 470     LYS G  71    CG   CD   CE   NZ                                   
REMARK 470     GLU G  75    CG   CD   OE1  OE2                                  
REMARK 470     LYS G  96    CG   CD   CE   NZ                                   
REMARK 470     ARG G  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE G 207    CD1                                                 
REMARK 470     ILE G 217    CD1                                                 
REMARK 470     LYS G 279    CG   CD   CE   NZ                                   
REMARK 470     LYS G 311    CG   CD   CE   NZ                                   
REMARK 470     ARG G 348    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE G 349    CG1  CG2  CD1                                       
REMARK 470     GLU G 351    CG   CD   OE1  OE2                                  
REMARK 470     LYS H  52    CE   NZ                                             
REMARK 470     LYS H  96    CG   CD   CE   NZ                                   
REMARK 470     LYS H 114    CG   CD   CE   NZ                                   
REMARK 470     ARG H 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE H 207    CD1                                                 
REMARK 470     GLN H 214    CG   CD   OE1  NE2                                  
REMARK 470     LYS H 279    CG   CD   CE   NZ                                   
REMARK 470     LYS H 311    CG   CD   CE   NZ                                   
REMARK 470     ILE H 349    CD1                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP G    40     OG1  THR G    84              2.14            
REMARK 500   O    LYS D   311     O    HOH D   909              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS H 356   CB    CYS H 356   SG     -0.097                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  34   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG A 147   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 147   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    PRO B  34   C   -  N   -  CA  ANGL. DEV. = -10.4 DEGREES          
REMARK 500    ARG F 147   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG G 147   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    CYS H  44   CA  -  CB  -  SG  ANGL. DEV. =   8.7 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    CYS A  44       25.86   -144.05                                   
REMARK 500    TYR A  82     -154.23    -94.49                                   
REMARK 500    TYR A 108       25.72   -141.60                                   
REMARK 500    HIS A 242       34.07   -141.67                                   
REMARK 500    ALA A 271      -87.93    -97.11                                   
REMARK 500    CYS B  44       16.98   -140.33                                   
REMARK 500    TYR B  82     -155.52    -96.84                                   
REMARK 500    TYR B 108       27.03   -140.15                                   
REMARK 500    SER B 128       22.44   -140.56                                   
REMARK 500    HIS B 242       36.55   -144.66                                   
REMARK 500    ALA B 271      -89.19    -95.63                                   
REMARK 500    CYS C  44       23.59   -140.53                                   
REMARK 500    TYR C  82     -152.92    -99.03                                   
REMARK 500    TYR C 108       26.50   -140.67                                   
REMARK 500    SER C 128       28.51   -144.06                                   
REMARK 500    HIS C 242       36.72   -145.18                                   
REMARK 500    ALA C 271      -89.79    -95.76                                   
REMARK 500    PRO C 320       58.35    -90.54                                   
REMARK 500    CYS D  44       24.34   -144.52                                   
REMARK 500    TYR D  82     -158.89    -94.34                                   
REMARK 500    SER D 128       28.00   -144.48                                   
REMARK 500    HIS D 242       34.25   -142.44                                   
REMARK 500    ALA D 271      -86.39    -96.91                                   
REMARK 500    PRO D 320       58.65    -93.14                                   
REMARK 500    TYR E  82     -157.06    -96.79                                   
REMARK 500    SER E 128       25.87   -143.33                                   
REMARK 500    HIS E 242       36.55   -145.07                                   
REMARK 500    ALA E 271      -88.83    -95.65                                   
REMARK 500    TYR F  82     -153.13    -96.52                                   
REMARK 500    SER F 128       27.58   -145.68                                   
REMARK 500    HIS F 242       35.07   -143.74                                   
REMARK 500    ALA F 271      -90.26    -94.04                                   
REMARK 500    CYS G  44       22.57   -142.55                                   
REMARK 500    TYR G  82     -156.39    -96.77                                   
REMARK 500    SER G 128       26.09   -142.52                                   
REMARK 500    HIS G 242       35.16   -144.16                                   
REMARK 500    ALA G 271      -89.50    -95.82                                   
REMARK 500    CYS H  44       22.60   -144.05                                   
REMARK 500    TYR H  82     -151.57    -97.13                                   
REMARK 500    TYR H 108       26.19   -141.46                                   
REMARK 500    SER H 128       24.70   -142.07                                   
REMARK 500    HIS H 242       31.87   -141.30                                   
REMARK 500    ALA H 271      -89.13    -95.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A  359     GLU A  360                  149.99                    
REMARK 500 ARG B   33     PRO B   34                 -145.37                    
REMARK 500 LYS B  359     GLU B  360                  147.60                    
REMARK 500 LYS C  359     GLU C  360                  147.51                    
REMARK 500 LYS D  359     GLU D  360                  148.33                    
REMARK 500 LYS E  359     GLU E  360                  148.94                    
REMARK 500 LYS F  359     GLU F  360                  147.94                    
REMARK 500 LYS G  359     GLU G  360                  149.04                    
REMARK 500 LYS H  359     GLU H  360                  149.60                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD E 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD F 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD G 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD H 901                 
DBREF  2OME A   31   364  UNP    P56545   CTBP2_HUMAN     31    364             
DBREF  2OME B   31   364  UNP    P56545   CTBP2_HUMAN     31    364             
DBREF  2OME C   31   364  UNP    P56545   CTBP2_HUMAN     31    364             
DBREF  2OME D   31   364  UNP    P56545   CTBP2_HUMAN     31    364             
DBREF  2OME E   31   364  UNP    P56545   CTBP2_HUMAN     31    364             
DBREF  2OME F   31   364  UNP    P56545   CTBP2_HUMAN     31    364             
DBREF  2OME G   31   364  UNP    P56545   CTBP2_HUMAN     31    364             
DBREF  2OME H   31   364  UNP    P56545   CTBP2_HUMAN     31    364             
SEQADV 2OME SER A   29  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME MET A   30  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME SER B   29  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME MET B   30  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME SER C   29  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME MET C   30  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME SER D   29  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME MET D   30  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME SER E   29  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME MET E   30  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME SER F   29  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME MET F   30  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME SER G   29  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME MET G   30  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME SER H   29  UNP  P56545              CLONING ARTIFACT               
SEQADV 2OME MET H   30  UNP  P56545              CLONING ARTIFACT               
SEQRES   1 A  336  SER MET HIS PRO ARG PRO LEU VAL ALA LEU LEU ASP GLY          
SEQRES   2 A  336  ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS ASP LEU          
SEQRES   3 A  336  ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR GLN GLU          
SEQRES   4 A  336  ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY ALA MET          
SEQRES   5 A  336  MET TYR HIS THR ILE THR LEU THR ARG GLU ASP LEU GLU          
SEQRES   6 A  336  LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE GLY SER          
SEQRES   7 A  336  GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY GLU LEU          
SEQRES   8 A  336  GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA VAL GLU          
SEQRES   9 A  336  GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU ASN LEU          
SEQRES  10 A  336  TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU ARG GLU          
SEQRES  11 A  336  GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG GLU VAL          
SEQRES  12 A  336  ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR LEU GLY          
SEQRES  13 A  336  LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL ALA VAL          
SEQRES  14 A  336  ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE TYR ASP          
SEQRES  15 A  336  PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU GLY VAL          
SEQRES  16 A  336  GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR GLN SER          
SEQRES  17 A  336  ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU HIS ASN          
SEQRES  18 A  336  HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN MET ARG          
SEQRES  19 A  336  GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY GLY LEU          
SEQRES  20 A  336  VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS GLU GLY          
SEQRES  21 A  336  ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU SER GLU          
SEQRES  22 A  336  PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP ALA PRO          
SEQRES  23 A  336  ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR SER GLU          
SEQRES  24 A  336  GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA THR GLU          
SEQRES  25 A  336  ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU SER LEU          
SEQRES  26 A  336  ARG ASN CYS VAL ASN LYS GLU PHE PHE VAL THR                  
SEQRES   1 B  336  SER MET HIS PRO ARG PRO LEU VAL ALA LEU LEU ASP GLY          
SEQRES   2 B  336  ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS ASP LEU          
SEQRES   3 B  336  ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR GLN GLU          
SEQRES   4 B  336  ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY ALA MET          
SEQRES   5 B  336  MET TYR HIS THR ILE THR LEU THR ARG GLU ASP LEU GLU          
SEQRES   6 B  336  LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE GLY SER          
SEQRES   7 B  336  GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY GLU LEU          
SEQRES   8 B  336  GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA VAL GLU          
SEQRES   9 B  336  GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU ASN LEU          
SEQRES  10 B  336  TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU ARG GLU          
SEQRES  11 B  336  GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG GLU VAL          
SEQRES  12 B  336  ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR LEU GLY          
SEQRES  13 B  336  LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL ALA VAL          
SEQRES  14 B  336  ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE TYR ASP          
SEQRES  15 B  336  PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU GLY VAL          
SEQRES  16 B  336  GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR GLN SER          
SEQRES  17 B  336  ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU HIS ASN          
SEQRES  18 B  336  HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN MET ARG          
SEQRES  19 B  336  GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY GLY LEU          
SEQRES  20 B  336  VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS GLU GLY          
SEQRES  21 B  336  ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU SER GLU          
SEQRES  22 B  336  PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP ALA PRO          
SEQRES  23 B  336  ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR SER GLU          
SEQRES  24 B  336  GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA THR GLU          
SEQRES  25 B  336  ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU SER LEU          
SEQRES  26 B  336  ARG ASN CYS VAL ASN LYS GLU PHE PHE VAL THR                  
SEQRES   1 C  336  SER MET HIS PRO ARG PRO LEU VAL ALA LEU LEU ASP GLY          
SEQRES   2 C  336  ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS ASP LEU          
SEQRES   3 C  336  ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR GLN GLU          
SEQRES   4 C  336  ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY ALA MET          
SEQRES   5 C  336  MET TYR HIS THR ILE THR LEU THR ARG GLU ASP LEU GLU          
SEQRES   6 C  336  LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE GLY SER          
SEQRES   7 C  336  GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY GLU LEU          
SEQRES   8 C  336  GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA VAL GLU          
SEQRES   9 C  336  GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU ASN LEU          
SEQRES  10 C  336  TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU ARG GLU          
SEQRES  11 C  336  GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG GLU VAL          
SEQRES  12 C  336  ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR LEU GLY          
SEQRES  13 C  336  LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL ALA VAL          
SEQRES  14 C  336  ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE TYR ASP          
SEQRES  15 C  336  PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU GLY VAL          
SEQRES  16 C  336  GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR GLN SER          
SEQRES  17 C  336  ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU HIS ASN          
SEQRES  18 C  336  HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN MET ARG          
SEQRES  19 C  336  GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY GLY LEU          
SEQRES  20 C  336  VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS GLU GLY          
SEQRES  21 C  336  ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU SER GLU          
SEQRES  22 C  336  PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP ALA PRO          
SEQRES  23 C  336  ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR SER GLU          
SEQRES  24 C  336  GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA THR GLU          
SEQRES  25 C  336  ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU SER LEU          
SEQRES  26 C  336  ARG ASN CYS VAL ASN LYS GLU PHE PHE VAL THR                  
SEQRES   1 D  336  SER MET HIS PRO ARG PRO LEU VAL ALA LEU LEU ASP GLY          
SEQRES   2 D  336  ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS ASP LEU          
SEQRES   3 D  336  ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR GLN GLU          
SEQRES   4 D  336  ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY ALA MET          
SEQRES   5 D  336  MET TYR HIS THR ILE THR LEU THR ARG GLU ASP LEU GLU          
SEQRES   6 D  336  LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE GLY SER          
SEQRES   7 D  336  GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY GLU LEU          
SEQRES   8 D  336  GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA VAL GLU          
SEQRES   9 D  336  GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU ASN LEU          
SEQRES  10 D  336  TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU ARG GLU          
SEQRES  11 D  336  GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG GLU VAL          
SEQRES  12 D  336  ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR LEU GLY          
SEQRES  13 D  336  LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL ALA VAL          
SEQRES  14 D  336  ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE TYR ASP          
SEQRES  15 D  336  PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU GLY VAL          
SEQRES  16 D  336  GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR GLN SER          
SEQRES  17 D  336  ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU HIS ASN          
SEQRES  18 D  336  HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN MET ARG          
SEQRES  19 D  336  GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY GLY LEU          
SEQRES  20 D  336  VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS GLU GLY          
SEQRES  21 D  336  ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU SER GLU          
SEQRES  22 D  336  PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP ALA PRO          
SEQRES  23 D  336  ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR SER GLU          
SEQRES  24 D  336  GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA THR GLU          
SEQRES  25 D  336  ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU SER LEU          
SEQRES  26 D  336  ARG ASN CYS VAL ASN LYS GLU PHE PHE VAL THR                  
SEQRES   1 E  336  SER MET HIS PRO ARG PRO LEU VAL ALA LEU LEU ASP GLY          
SEQRES   2 E  336  ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS ASP LEU          
SEQRES   3 E  336  ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR GLN GLU          
SEQRES   4 E  336  ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY ALA MET          
SEQRES   5 E  336  MET TYR HIS THR ILE THR LEU THR ARG GLU ASP LEU GLU          
SEQRES   6 E  336  LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE GLY SER          
SEQRES   7 E  336  GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY GLU LEU          
SEQRES   8 E  336  GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA VAL GLU          
SEQRES   9 E  336  GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU ASN LEU          
SEQRES  10 E  336  TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU ARG GLU          
SEQRES  11 E  336  GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG GLU VAL          
SEQRES  12 E  336  ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR LEU GLY          
SEQRES  13 E  336  LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL ALA VAL          
SEQRES  14 E  336  ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE TYR ASP          
SEQRES  15 E  336  PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU GLY VAL          
SEQRES  16 E  336  GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR GLN SER          
SEQRES  17 E  336  ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU HIS ASN          
SEQRES  18 E  336  HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN MET ARG          
SEQRES  19 E  336  GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY GLY LEU          
SEQRES  20 E  336  VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS GLU GLY          
SEQRES  21 E  336  ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU SER GLU          
SEQRES  22 E  336  PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP ALA PRO          
SEQRES  23 E  336  ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR SER GLU          
SEQRES  24 E  336  GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA THR GLU          
SEQRES  25 E  336  ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU SER LEU          
SEQRES  26 E  336  ARG ASN CYS VAL ASN LYS GLU PHE PHE VAL THR                  
SEQRES   1 F  336  SER MET HIS PRO ARG PRO LEU VAL ALA LEU LEU ASP GLY          
SEQRES   2 F  336  ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS ASP LEU          
SEQRES   3 F  336  ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR GLN GLU          
SEQRES   4 F  336  ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY ALA MET          
SEQRES   5 F  336  MET TYR HIS THR ILE THR LEU THR ARG GLU ASP LEU GLU          
SEQRES   6 F  336  LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE GLY SER          
SEQRES   7 F  336  GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY GLU LEU          
SEQRES   8 F  336  GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA VAL GLU          
SEQRES   9 F  336  GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU ASN LEU          
SEQRES  10 F  336  TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU ARG GLU          
SEQRES  11 F  336  GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG GLU VAL          
SEQRES  12 F  336  ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR LEU GLY          
SEQRES  13 F  336  LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL ALA VAL          
SEQRES  14 F  336  ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE TYR ASP          
SEQRES  15 F  336  PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU GLY VAL          
SEQRES  16 F  336  GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR GLN SER          
SEQRES  17 F  336  ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU HIS ASN          
SEQRES  18 F  336  HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN MET ARG          
SEQRES  19 F  336  GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY GLY LEU          
SEQRES  20 F  336  VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS GLU GLY          
SEQRES  21 F  336  ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU SER GLU          
SEQRES  22 F  336  PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP ALA PRO          
SEQRES  23 F  336  ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR SER GLU          
SEQRES  24 F  336  GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA THR GLU          
SEQRES  25 F  336  ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU SER LEU          
SEQRES  26 F  336  ARG ASN CYS VAL ASN LYS GLU PHE PHE VAL THR                  
SEQRES   1 G  336  SER MET HIS PRO ARG PRO LEU VAL ALA LEU LEU ASP GLY          
SEQRES   2 G  336  ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS ASP LEU          
SEQRES   3 G  336  ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR GLN GLU          
SEQRES   4 G  336  ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY ALA MET          
SEQRES   5 G  336  MET TYR HIS THR ILE THR LEU THR ARG GLU ASP LEU GLU          
SEQRES   6 G  336  LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE GLY SER          
SEQRES   7 G  336  GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY GLU LEU          
SEQRES   8 G  336  GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA VAL GLU          
SEQRES   9 G  336  GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU ASN LEU          
SEQRES  10 G  336  TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU ARG GLU          
SEQRES  11 G  336  GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG GLU VAL          
SEQRES  12 G  336  ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR LEU GLY          
SEQRES  13 G  336  LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL ALA VAL          
SEQRES  14 G  336  ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE TYR ASP          
SEQRES  15 G  336  PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU GLY VAL          
SEQRES  16 G  336  GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR GLN SER          
SEQRES  17 G  336  ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU HIS ASN          
SEQRES  18 G  336  HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN MET ARG          
SEQRES  19 G  336  GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY GLY LEU          
SEQRES  20 G  336  VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS GLU GLY          
SEQRES  21 G  336  ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU SER GLU          
SEQRES  22 G  336  PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP ALA PRO          
SEQRES  23 G  336  ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR SER GLU          
SEQRES  24 G  336  GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA THR GLU          
SEQRES  25 G  336  ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU SER LEU          
SEQRES  26 G  336  ARG ASN CYS VAL ASN LYS GLU PHE PHE VAL THR                  
SEQRES   1 H  336  SER MET HIS PRO ARG PRO LEU VAL ALA LEU LEU ASP GLY          
SEQRES   2 H  336  ARG ASP CYS THR VAL GLU MET PRO ILE LEU LYS ASP LEU          
SEQRES   3 H  336  ALA THR VAL ALA PHE CYS ASP ALA GLN SER THR GLN GLU          
SEQRES   4 H  336  ILE HIS GLU LYS VAL LEU ASN GLU ALA VAL GLY ALA MET          
SEQRES   5 H  336  MET TYR HIS THR ILE THR LEU THR ARG GLU ASP LEU GLU          
SEQRES   6 H  336  LYS PHE LYS ALA LEU ARG VAL ILE VAL ARG ILE GLY SER          
SEQRES   7 H  336  GLY TYR ASP ASN VAL ASP ILE LYS ALA ALA GLY GLU LEU          
SEQRES   8 H  336  GLY ILE ALA VAL CYS ASN ILE PRO SER ALA ALA VAL GLU          
SEQRES   9 H  336  GLU THR ALA ASP SER THR ILE CYS HIS ILE LEU ASN LEU          
SEQRES  10 H  336  TYR ARG ARG ASN THR TRP LEU TYR GLN ALA LEU ARG GLU          
SEQRES  11 H  336  GLY THR ARG VAL GLN SER VAL GLU GLN ILE ARG GLU VAL          
SEQRES  12 H  336  ALA SER GLY ALA ALA ARG ILE ARG GLY GLU THR LEU GLY          
SEQRES  13 H  336  LEU ILE GLY PHE GLY ARG THR GLY GLN ALA VAL ALA VAL          
SEQRES  14 H  336  ARG ALA LYS ALA PHE GLY PHE SER VAL ILE PHE TYR ASP          
SEQRES  15 H  336  PRO TYR LEU GLN ASP GLY ILE GLU ARG SER LEU GLY VAL          
SEQRES  16 H  336  GLN ARG VAL TYR THR LEU GLN ASP LEU LEU TYR GLN SER          
SEQRES  17 H  336  ASP CYS VAL SER LEU HIS CYS ASN LEU ASN GLU HIS ASN          
SEQRES  18 H  336  HIS HIS LEU ILE ASN ASP PHE THR ILE LYS GLN MET ARG          
SEQRES  19 H  336  GLN GLY ALA PHE LEU VAL ASN ALA ALA ARG GLY GLY LEU          
SEQRES  20 H  336  VAL ASP GLU LYS ALA LEU ALA GLN ALA LEU LYS GLU GLY          
SEQRES  21 H  336  ARG ILE ARG GLY ALA ALA LEU ASP VAL HIS GLU SER GLU          
SEQRES  22 H  336  PRO PHE SER PHE ALA GLN GLY PRO LEU LYS ASP ALA PRO          
SEQRES  23 H  336  ASN LEU ILE CYS THR PRO HIS THR ALA TRP TYR SER GLU          
SEQRES  24 H  336  GLN ALA SER LEU GLU MET ARG GLU ALA ALA ALA THR GLU          
SEQRES  25 H  336  ILE ARG ARG ALA ILE THR GLY ARG ILE PRO GLU SER LEU          
SEQRES  26 H  336  ARG ASN CYS VAL ASN LYS GLU PHE PHE VAL THR                  
HET    NAD  A 901      44                                                       
HET    NAD  B 901      44                                                       
HET    NAD  C 901      44                                                       
HET    NAD  D 901      44                                                       
HET    NAD  E 901      44                                                       
HET    NAD  F 901      44                                                       
HET    NAD  G 901      44                                                       
HET    NAD  H 901      44                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   9  NAD    8(C21 H27 N7 O14 P2)                                         
FORMUL  17  HOH   *184(H2 O)                                                    
HELIX    1   1 VAL A   46  LYS A   52  1                                   7    
HELIX    2   2 SER A   64  ILE A   68  5                                   5    
HELIX    3   3 HIS A   69  GLU A   75  1                                   7    
HELIX    4   4 THR A   88  LYS A   94  1                                   7    
HELIX    5   5 ASP A  112  LEU A  119  1                                   8    
HELIX    6   6 ALA A  130  ARG A  148  1                                  19    
HELIX    7   7 ARG A  148  GLU A  158  1                                  11    
HELIX    8   8 SER A  164  ALA A  172  1                                   9    
HELIX    9   9 GLY A  189  LYS A  200  1                                  12    
HELIX   10  10 ALA A  201  GLY A  203  5                                   3    
HELIX   11  11 GLY A  216  LEU A  221  1                                   6    
HELIX   12  12 THR A  228  SER A  236  1                                   9    
HELIX   13  13 ASN A  254  LYS A  259  1                                   6    
HELIX   14  14 ARG A  272  VAL A  276  5                                   5    
HELIX   15  15 ASP A  277  GLU A  287  1                                  11    
HELIX   16  16 SER A  326  GLY A  347  1                                  22    
HELIX   17  17 VAL B   46  LYS B   52  1                                   7    
HELIX   18  18 SER B   64  ILE B   68  5                                   5    
HELIX   19  19 HIS B   69  GLU B   75  1                                   7    
HELIX   20  20 THR B   88  LYS B   94  1                                   7    
HELIX   21  21 ASP B  112  LEU B  119  1                                   8    
HELIX   22  22 ALA B  130  ARG B  148  1                                  19    
HELIX   23  23 ARG B  148  GLU B  158  1                                  11    
HELIX   24  24 SER B  164  ALA B  172  1                                   9    
HELIX   25  25 GLY B  189  LYS B  200  1                                  12    
HELIX   26  26 ALA B  201  GLY B  203  5                                   3    
HELIX   27  27 GLY B  216  LEU B  221  1                                   6    
HELIX   28  28 THR B  228  SER B  236  1                                   9    
HELIX   29  29 ASN B  254  LYS B  259  1                                   6    
HELIX   30  30 ASP B  277  GLU B  287  1                                  11    
HELIX   31  31 SER B  326  GLY B  347  1                                  22    
HELIX   32  32 VAL C   46  LYS C   52  1                                   7    
HELIX   33  33 SER C   64  ILE C   68  5                                   5    
HELIX   34  34 HIS C   69  GLU C   75  1                                   7    
HELIX   35  35 THR C   88  LYS C   94  1                                   7    
HELIX   36  36 ASP C  112  LEU C  119  1                                   8    
HELIX   37  37 ALA C  130  ARG C  148  1                                  19    
HELIX   38  38 ARG C  148  GLU C  158  1                                  11    
HELIX   39  39 SER C  164  ALA C  172  1                                   9    
HELIX   40  40 GLY C  189  LYS C  200  1                                  12    
HELIX   41  41 ALA C  201  GLY C  203  5                                   3    
HELIX   42  42 GLY C  216  LEU C  221  1                                   6    
HELIX   43  43 THR C  228  SER C  236  1                                   9    
HELIX   44  44 ASN C  254  LYS C  259  1                                   6    
HELIX   45  45 ASP C  277  GLU C  287  1                                  11    
HELIX   46  46 SER C  326  GLY C  347  1                                  22    
HELIX   47  47 VAL D   46  LYS D   52  1                                   7    
HELIX   48  48 SER D   64  ILE D   68  5                                   5    
HELIX   49  49 HIS D   69  GLU D   75  1                                   7    
HELIX   50  50 THR D   88  LYS D   94  1                                   7    
HELIX   51  51 ASP D  112  LEU D  119  1                                   8    
HELIX   52  52 ALA D  130  ARG D  148  1                                  19    
HELIX   53  53 ARG D  148  GLU D  158  1                                  11    
HELIX   54  54 SER D  164  ALA D  172  1                                   9    
HELIX   55  55 GLY D  189  LYS D  200  1                                  12    
HELIX   56  56 ALA D  201  GLY D  203  5                                   3    
HELIX   57  57 GLY D  216  LEU D  221  1                                   6    
HELIX   58  58 THR D  228  SER D  236  1                                   9    
HELIX   59  59 ASN D  254  LYS D  259  1                                   6    
HELIX   60  60 ASP D  277  GLU D  287  1                                  11    
HELIX   61  61 SER D  326  GLY D  347  1                                  22    
HELIX   62  62 VAL E   46  LYS E   52  1                                   7    
HELIX   63  63 SER E   64  ILE E   68  5                                   5    
HELIX   64  64 HIS E   69  GLU E   75  1                                   7    
HELIX   65  65 THR E   88  LYS E   94  1                                   7    
HELIX   66  66 ASP E  112  LEU E  119  1                                   8    
HELIX   67  67 ALA E  130  ARG E  148  1                                  19    
HELIX   68  68 ARG E  148  GLU E  158  1                                  11    
HELIX   69  69 SER E  164  ALA E  172  1                                   9    
HELIX   70  70 GLY E  189  LYS E  200  1                                  12    
HELIX   71  71 ALA E  201  GLY E  203  5                                   3    
HELIX   72  72 GLY E  216  LEU E  221  1                                   6    
HELIX   73  73 THR E  228  SER E  236  1                                   9    
HELIX   74  74 ASN E  254  LYS E  259  1                                   6    
HELIX   75  75 ASP E  277  GLU E  287  1                                  11    
HELIX   76  76 SER E  326  GLY E  347  1                                  22    
HELIX   77  77 VAL F   46  LYS F   52  1                                   7    
HELIX   78  78 SER F   64  ILE F   68  5                                   5    
HELIX   79  79 HIS F   69  GLU F   75  1                                   7    
HELIX   80  80 THR F   88  LYS F   94  1                                   7    
HELIX   81  81 ASP F  112  LEU F  119  1                                   8    
HELIX   82  82 ALA F  130  ARG F  148  1                                  19    
HELIX   83  83 ARG F  148  GLU F  158  1                                  11    
HELIX   84  84 SER F  164  ALA F  172  1                                   9    
HELIX   85  85 GLY F  189  LYS F  200  1                                  12    
HELIX   86  86 ALA F  201  GLY F  203  5                                   3    
HELIX   87  87 GLY F  216  LEU F  221  1                                   6    
HELIX   88  88 THR F  228  SER F  236  1                                   9    
HELIX   89  89 ASN F  254  LYS F  259  1                                   6    
HELIX   90  90 ASP F  277  GLU F  287  1                                  11    
HELIX   91  91 SER F  326  GLY F  347  1                                  22    
HELIX   92  92 VAL G   46  LYS G   52  1                                   7    
HELIX   93  93 SER G   64  ILE G   68  5                                   5    
HELIX   94  94 HIS G   69  GLU G   75  1                                   7    
HELIX   95  95 THR G   88  LYS G   94  1                                   7    
HELIX   96  96 ASP G  112  LEU G  119  1                                   8    
HELIX   97  97 ALA G  130  ARG G  148  1                                  19    
HELIX   98  98 ARG G  148  GLU G  158  1                                  11    
HELIX   99  99 SER G  164  ALA G  172  1                                   9    
HELIX  100 100 GLY G  189  LYS G  200  1                                  12    
HELIX  101 101 ALA G  201  GLY G  203  5                                   3    
HELIX  102 102 GLY G  216  LEU G  221  1                                   6    
HELIX  103 103 THR G  228  SER G  236  1                                   9    
HELIX  104 104 ASN G  254  LYS G  259  1                                   6    
HELIX  105 105 ARG G  272  VAL G  276  5                                   5    
HELIX  106 106 ASP G  277  GLU G  287  1                                  11    
HELIX  107 107 SER G  326  GLY G  347  1                                  22    
HELIX  108 108 VAL H   46  LYS H   52  1                                   7    
HELIX  109 109 SER H   64  ILE H   68  5                                   5    
HELIX  110 110 HIS H   69  GLU H   75  1                                   7    
HELIX  111 111 THR H   88  LYS H   94  1                                   7    
HELIX  112 112 ASP H  112  LEU H  119  1                                   8    
HELIX  113 113 ALA H  130  ARG H  148  1                                  19    
HELIX  114 114 ARG H  148  GLU H  158  1                                  11    
HELIX  115 115 SER H  164  ALA H  172  1                                   9    
HELIX  116 116 GLY H  189  LYS H  200  1                                  12    
HELIX  117 117 ALA H  201  GLY H  203  5                                   3    
HELIX  118 118 GLY H  216  LEU H  221  1                                   6    
HELIX  119 119 THR H  228  SER H  236  1                                   9    
HELIX  120 120 ASN H  254  LYS H  259  1                                   6    
HELIX  121 121 ASP H  277  GLU H  287  1                                  11    
HELIX  122 122 SER H  326  GLY H  347  1                                  22    
SHEET    1   A 5 THR A  56  PHE A  59  0                                        
SHEET    2   A 5 LEU A  35  LEU A  38  1  N  LEU A  38   O  ALA A  58           
SHEET    3   A 5 ALA A  76  MET A  81  1  O  VAL A  77   N  LEU A  35           
SHEET    4   A 5 VAL A 100  ARG A 103  1  O  VAL A 102   N  ALA A  79           
SHEET    5   A 5 ALA A 122  CYS A 124  1  O  CYS A 124   N  ARG A 103           
SHEET    1   B 7 GLN A 224  ARG A 225  0                                        
SHEET    2   B 7 SER A 205  TYR A 209  1  N  PHE A 208   O  GLN A 224           
SHEET    3   B 7 THR A 182  ILE A 186  1  N  LEU A 183   O  SER A 205           
SHEET    4   B 7 CYS A 238  LEU A 241  1  O  CYS A 238   N  GLY A 184           
SHEET    5   B 7 ALA A 265  ASN A 269  1  O  PHE A 266   N  VAL A 239           
SHEET    6   B 7 ILE A 290  LEU A 295  1  O  ALA A 294   N  ASN A 269           
SHEET    7   B 7 LEU A 316  CYS A 318  1  O  ILE A 317   N  ALA A 293           
SHEET    1   C 5 THR B  56  PHE B  59  0                                        
SHEET    2   C 5 LEU B  35  LEU B  38  1  N  LEU B  38   O  ALA B  58           
SHEET    3   C 5 ALA B  76  MET B  81  1  O  VAL B  77   N  LEU B  35           
SHEET    4   C 5 VAL B 100  ARG B 103  1  O  VAL B 102   N  ALA B  79           
SHEET    5   C 5 ALA B 122  CYS B 124  1  O  CYS B 124   N  ARG B 103           
SHEET    1   D 7 GLN B 224  ARG B 225  0                                        
SHEET    2   D 7 SER B 205  TYR B 209  1  N  VAL B 206   O  GLN B 224           
SHEET    3   D 7 THR B 182  ILE B 186  1  N  LEU B 185   O  ILE B 207           
SHEET    4   D 7 CYS B 238  LEU B 241  1  O  CYS B 238   N  GLY B 184           
SHEET    5   D 7 ALA B 265  ASN B 269  1  O  VAL B 268   N  VAL B 239           
SHEET    6   D 7 ILE B 290  LEU B 295  1  O  ALA B 294   N  ASN B 269           
SHEET    7   D 7 LEU B 316  CYS B 318  1  O  ILE B 317   N  LEU B 295           
SHEET    1   E 5 THR C  56  PHE C  59  0                                        
SHEET    2   E 5 LEU C  35  LEU C  38  1  N  LEU C  38   O  ALA C  58           
SHEET    3   E 5 ALA C  76  MET C  81  1  O  GLY C  78   N  ALA C  37           
SHEET    4   E 5 VAL C 100  ARG C 103  1  O  VAL C 102   N  ALA C  79           
SHEET    5   E 5 ALA C 122  CYS C 124  1  O  CYS C 124   N  ARG C 103           
SHEET    1   F 7 GLN C 224  ARG C 225  0                                        
SHEET    2   F 7 SER C 205  TYR C 209  1  N  VAL C 206   O  GLN C 224           
SHEET    3   F 7 THR C 182  ILE C 186  1  N  LEU C 185   O  ILE C 207           
SHEET    4   F 7 CYS C 238  LEU C 241  1  O  CYS C 238   N  GLY C 184           
SHEET    5   F 7 ALA C 265  ASN C 269  1  O  VAL C 268   N  VAL C 239           
SHEET    6   F 7 ILE C 290  LEU C 295  1  O  ALA C 294   N  ASN C 269           
SHEET    7   F 7 LEU C 316  CYS C 318  1  O  ILE C 317   N  LEU C 295           
SHEET    1   G 5 THR D  56  PHE D  59  0                                        
SHEET    2   G 5 LEU D  35  LEU D  38  1  N  LEU D  38   O  ALA D  58           
SHEET    3   G 5 ALA D  76  MET D  81  1  O  GLY D  78   N  ALA D  37           
SHEET    4   G 5 VAL D 100  ARG D 103  1  O  VAL D 102   N  ALA D  79           
SHEET    5   G 5 ALA D 122  CYS D 124  1  O  CYS D 124   N  ARG D 103           
SHEET    1   H 7 GLN D 224  ARG D 225  0                                        
SHEET    2   H 7 SER D 205  TYR D 209  1  N  PHE D 208   O  GLN D 224           
SHEET    3   H 7 THR D 182  ILE D 186  1  N  LEU D 183   O  SER D 205           
SHEET    4   H 7 CYS D 238  LEU D 241  1  O  CYS D 238   N  GLY D 184           
SHEET    5   H 7 ALA D 265  ASN D 269  1  O  VAL D 268   N  VAL D 239           
SHEET    6   H 7 ILE D 290  LEU D 295  1  O  ALA D 294   N  ASN D 269           
SHEET    7   H 7 LEU D 316  CYS D 318  1  O  ILE D 317   N  LEU D 295           
SHEET    1   I 5 THR E  56  PHE E  59  0                                        
SHEET    2   I 5 LEU E  35  LEU E  38  1  N  LEU E  38   O  ALA E  58           
SHEET    3   I 5 ALA E  76  MET E  81  1  O  GLY E  78   N  ALA E  37           
SHEET    4   I 5 VAL E 100  ARG E 103  1  O  VAL E 102   N  ALA E  79           
SHEET    5   I 5 ALA E 122  CYS E 124  1  O  CYS E 124   N  ARG E 103           
SHEET    1   J 7 GLN E 224  ARG E 225  0                                        
SHEET    2   J 7 SER E 205  TYR E 209  1  N  VAL E 206   O  GLN E 224           
SHEET    3   J 7 THR E 182  ILE E 186  1  N  LEU E 183   O  SER E 205           
SHEET    4   J 7 CYS E 238  LEU E 241  1  O  CYS E 238   N  GLY E 184           
SHEET    5   J 7 ALA E 265  ASN E 269  1  O  PHE E 266   N  VAL E 239           
SHEET    6   J 7 ILE E 290  LEU E 295  1  O  ALA E 294   N  ASN E 269           
SHEET    7   J 7 LEU E 316  CYS E 318  1  O  ILE E 317   N  LEU E 295           
SHEET    1   K 5 THR F  56  PHE F  59  0                                        
SHEET    2   K 5 LEU F  35  LEU F  38  1  N  LEU F  38   O  ALA F  58           
SHEET    3   K 5 ALA F  76  MET F  81  1  O  VAL F  77   N  LEU F  35           
SHEET    4   K 5 VAL F 100  ARG F 103  1  O  VAL F 102   N  ALA F  79           
SHEET    5   K 5 ALA F 122  CYS F 124  1  O  CYS F 124   N  ARG F 103           
SHEET    1   L 7 GLN F 224  ARG F 225  0                                        
SHEET    2   L 7 SER F 205  TYR F 209  1  N  PHE F 208   O  GLN F 224           
SHEET    3   L 7 THR F 182  ILE F 186  1  N  LEU F 185   O  ILE F 207           
SHEET    4   L 7 CYS F 238  LEU F 241  1  O  CYS F 238   N  GLY F 184           
SHEET    5   L 7 ALA F 265  ASN F 269  1  O  VAL F 268   N  VAL F 239           
SHEET    6   L 7 ILE F 290  LEU F 295  1  O  ALA F 294   N  LEU F 267           
SHEET    7   L 7 LEU F 316  CYS F 318  1  O  ILE F 317   N  LEU F 295           
SHEET    1   M 5 THR G  56  PHE G  59  0                                        
SHEET    2   M 5 LEU G  35  LEU G  38  1  N  LEU G  38   O  ALA G  58           
SHEET    3   M 5 ALA G  76  MET G  81  1  O  MET G  80   N  ALA G  37           
SHEET    4   M 5 VAL G 100  ARG G 103  1  O  VAL G 102   N  ALA G  79           
SHEET    5   M 5 ALA G 122  CYS G 124  1  O  CYS G 124   N  ARG G 103           
SHEET    1   N 7 GLN G 224  ARG G 225  0                                        
SHEET    2   N 7 SER G 205  TYR G 209  1  N  PHE G 208   O  GLN G 224           
SHEET    3   N 7 THR G 182  ILE G 186  1  N  LEU G 185   O  ILE G 207           
SHEET    4   N 7 CYS G 238  LEU G 241  1  O  CYS G 238   N  GLY G 184           
SHEET    5   N 7 ALA G 265  ASN G 269  1  O  VAL G 268   N  VAL G 239           
SHEET    6   N 7 ILE G 290  LEU G 295  1  O  ALA G 294   N  ASN G 269           
SHEET    7   N 7 LEU G 316  CYS G 318  1  O  ILE G 317   N  ALA G 293           
SHEET    1   O 5 THR H  56  PHE H  59  0                                        
SHEET    2   O 5 LEU H  35  LEU H  38  1  N  LEU H  38   O  ALA H  58           
SHEET    3   O 5 ALA H  76  MET H  81  1  O  MET H  80   N  ALA H  37           
SHEET    4   O 5 VAL H 100  ARG H 103  1  O  VAL H 102   N  ALA H  79           
SHEET    5   O 5 ALA H 122  CYS H 124  1  O  CYS H 124   N  ARG H 103           
SHEET    1   P 7 GLN H 224  ARG H 225  0                                        
SHEET    2   P 7 SER H 205  TYR H 209  1  N  PHE H 208   O  GLN H 224           
SHEET    3   P 7 THR H 182  ILE H 186  1  N  LEU H 183   O  SER H 205           
SHEET    4   P 7 CYS H 238  LEU H 241  1  O  CYS H 238   N  GLY H 184           
SHEET    5   P 7 ALA H 265  ASN H 269  1  O  PHE H 266   N  VAL H 239           
SHEET    6   P 7 ILE H 290  LEU H 295  1  O  ALA H 294   N  ASN H 269           
SHEET    7   P 7 LEU H 316  CYS H 318  1  O  ILE H 317   N  LEU H 295           
CISPEP   1 GLU A  301    PRO A  302          0         8.56                     
CISPEP   2 ILE A  349    PRO A  350          0        13.62                     
CISPEP   3 GLU B  301    PRO B  302          0         5.23                     
CISPEP   4 ILE B  349    PRO B  350          0        15.60                     
CISPEP   5 GLU C  301    PRO C  302          0         8.85                     
CISPEP   6 ILE C  349    PRO C  350          0         9.55                     
CISPEP   7 GLU D  301    PRO D  302          0         6.77                     
CISPEP   8 ILE D  349    PRO D  350          0        13.11                     
CISPEP   9 GLU E  301    PRO E  302          0         8.25                     
CISPEP  10 ILE E  349    PRO E  350          0        16.17                     
CISPEP  11 GLU F  301    PRO F  302          0         9.60                     
CISPEP  12 ILE F  349    PRO F  350          0        13.69                     
CISPEP  13 GLU G  301    PRO G  302          0        11.47                     
CISPEP  14 ILE G  349    PRO G  350          0        14.72                     
CISPEP  15 GLU H  301    PRO H  302          0         5.94                     
CISPEP  16 ILE H  349    PRO H  350          0        11.10                     
SITE     1 AC1 26 SER A 106  THR A 134  ILE A 186  GLY A 187                    
SITE     2 AC1 26 GLY A 189  ARG A 190  THR A 191  TYR A 209                    
SITE     3 AC1 26 ASP A 210  PRO A 211  TYR A 212  LEU A 213                    
SITE     4 AC1 26 HIS A 242  CYS A 243  ASN A 244  ASN A 246                    
SITE     5 AC1 26 ASN A 249  ALA A 270  ALA A 271  ARG A 272                    
SITE     6 AC1 26 ASP A 296  HIS A 321  ALA A 323  TRP A 324                    
SITE     7 AC1 26 HOH A 917  HOH A 925                                          
SITE     1 AC2 24 SER B 106  GLY B 107  THR B 134  ILE B 186                    
SITE     2 AC2 24 GLY B 187  GLY B 189  ARG B 190  THR B 191                    
SITE     3 AC2 24 TYR B 209  ASP B 210  PRO B 211  TYR B 212                    
SITE     4 AC2 24 HIS B 242  CYS B 243  ASN B 244  ASN B 246                    
SITE     5 AC2 24 ASN B 249  ALA B 270  ALA B 271  ARG B 272                    
SITE     6 AC2 24 ASP B 296  HIS B 321  ALA B 323  TRP B 324                    
SITE     1 AC3 26 SER C 106  GLY C 107  THR C 134  ILE C 186                    
SITE     2 AC3 26 GLY C 187  GLY C 189  ARG C 190  THR C 191                    
SITE     3 AC3 26 TYR C 209  ASP C 210  PRO C 211  TYR C 212                    
SITE     4 AC3 26 LEU C 213  HIS C 242  CYS C 243  ASN C 244                    
SITE     5 AC3 26 ASN C 246  ASN C 249  ALA C 270  ALA C 271                    
SITE     6 AC3 26 ARG C 272  ASP C 296  ALA C 323  TRP C 324                    
SITE     7 AC3 26 HOH C 902  HOH C 903                                          
SITE     1 AC4 24 SER D 106  THR D 134  GLY D 187  GLY D 189                    
SITE     2 AC4 24 ARG D 190  THR D 191  TYR D 209  ASP D 210                    
SITE     3 AC4 24 PRO D 211  TYR D 212  HIS D 242  CYS D 243                    
SITE     4 AC4 24 ASN D 244  ASN D 246  ASN D 249  ALA D 270                    
SITE     5 AC4 24 ALA D 271  ARG D 272  ASP D 296  VAL D 297                    
SITE     6 AC4 24 HIS D 321  ALA D 323  TRP D 324  HOH D 906                    
SITE     1 AC5 23 SER E 106  GLY E 107  THR E 134  GLY E 187                    
SITE     2 AC5 23 GLY E 189  ARG E 190  THR E 191  TYR E 209                    
SITE     3 AC5 23 ASP E 210  PRO E 211  TYR E 212  HIS E 242                    
SITE     4 AC5 23 CYS E 243  ASN E 244  ASN E 246  ASN E 249                    
SITE     5 AC5 23 ALA E 270  ALA E 271  ARG E 272  ASP E 296                    
SITE     6 AC5 23 HIS E 321  ALA E 323  TRP E 324                               
SITE     1 AC6 25 SER F 106  GLY F 107  THR F 134  ILE F 186                    
SITE     2 AC6 25 GLY F 187  GLY F 189  ARG F 190  THR F 191                    
SITE     3 AC6 25 TYR F 209  ASP F 210  PRO F 211  TYR F 212                    
SITE     4 AC6 25 HIS F 242  CYS F 243  ASN F 244  ASN F 246                    
SITE     5 AC6 25 ASN F 249  ALA F 270  ALA F 271  ARG F 272                    
SITE     6 AC6 25 ASP F 296  HIS F 321  ALA F 323  TRP F 324                    
SITE     7 AC6 25 HOH F 910                                                     
SITE     1 AC7 23 SER G 106  THR G 134  GLY G 187  GLY G 189                    
SITE     2 AC7 23 ARG G 190  THR G 191  TYR G 209  ASP G 210                    
SITE     3 AC7 23 PRO G 211  TYR G 212  HIS G 242  CYS G 243                    
SITE     4 AC7 23 ASN G 244  ASN G 246  ASN G 249  ALA G 270                    
SITE     5 AC7 23 ALA G 271  ARG G 272  ASP G 296  VAL G 297                    
SITE     6 AC7 23 HIS G 321  ALA G 323  TRP G 324                               
SITE     1 AC8 25 SER H 106  THR H 134  ILE H 186  GLY H 187                    
SITE     2 AC8 25 GLY H 189  ARG H 190  THR H 191  TYR H 209                    
SITE     3 AC8 25 ASP H 210  PRO H 211  TYR H 212  LEU H 213                    
SITE     4 AC8 25 HIS H 242  CYS H 243  ASN H 244  ASN H 246                    
SITE     5 AC8 25 ASN H 249  ALA H 270  ALA H 271  ARG H 272                    
SITE     6 AC8 25 ASP H 296  ALA H 323  TRP H 324  HOH H 920                    
SITE     7 AC8 25 HOH H 927                                                     
CRYST1   87.754  141.574  138.215  90.00  98.93  90.00 P 1 21 1     16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011395  0.000000  0.001791        0.00000                         
SCALE2      0.000000  0.007063  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007324        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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