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Database: PDB
Entry: 2VFX
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Original site: 2VFX 
HEADER    CELL CYCLE                              05-NOV-07   2VFX              
TITLE     STRUCTURE OF THE SYMMETRIC MAD2 DIMER                                 
CAVEAT     2VFX    ALA H 115 HAS WRONG CHIRALITY FOR AN L-AMINO ACID            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A;         
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 SYNONYM: MITOTIC ARREST DEFICIENT 2, MAD2-LIKE 1, HSMAD2;            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: M15-PREP4;                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PGEX-KT;                                   
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: MAD2-L13A                                 
KEYWDS    MAD2, MAD1, CDC2, NUCLEUS, MITOSIS, ANAPHASE, CELL CYCLE, CELL        
KEYWDS   2 DIVISION, SPINDLE CHECKPOINT, ANAPHASE-PROMOTING COMPLEX             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.YANG,B.LI,C.-J.LIU,D.R.TOMCHICK,M.MACHIUS,J.RIZO,H.YU,X.LUO         
REVDAT   5   08-MAY-19 2VFX    1       REMARK                                   
REVDAT   4   30-JAN-19 2VFX    1       REMARK                                   
REVDAT   3   13-JUL-11 2VFX    1       VERSN                                    
REVDAT   2   24-FEB-09 2VFX    1       VERSN                                    
REVDAT   1   18-MAR-08 2VFX    0                                                
JRNL        AUTH   M.YANG,B.LI,C.-J.LIU,D.R.TOMCHICK,M.MACHIUS,J.RIZO,H.YU,     
JRNL        AUTH 2 X.LUO                                                        
JRNL        TITL   INSIGHTS INTO MAD2 REGULATION IN THE SPINDLE CHECKPOINT      
JRNL        TITL 2 REVEALED BY THE CRYSTAL STRUCTURE OF THE SYMMETRIC MAD2      
JRNL        TITL 3 DIMER.                                                       
JRNL        REF    PLOS BIOL.                    V.   6   E50 2008              
JRNL        REFN                   ISSN 1544-9173                               
JRNL        PMID   18318601                                                     
JRNL        DOI    10.1371/JOURNAL.PBIO.0060050                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 220725                         
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) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2700                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 15243                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 189                          
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 19613                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 151                                     
REMARK   3   SOLVENT ATOMS            : 1591                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 23.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.81000                                              
REMARK   3    B22 (A**2) : -0.83000                                             
REMARK   3    B33 (A**2) : 0.02000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.20000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.165         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.153         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.115         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.407         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 20370 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 27614 ; 1.501 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2493 ; 2.008 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   913 ;37.022 ;24.677       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3744 ;14.773 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   122 ;18.857 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3241 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 17410 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  8407 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 14075 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1462 ; 0.139 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   554 ; 0.171 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):   166 ; 0.211 ; 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): 12843 ; 0.706 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 20329 ; 1.156 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8629 ; 1.788 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7285 ; 2.877 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
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    10        A   205                          
REMARK   3    ORIGIN FOR THE GROUP (A): 111.4586    .3001  94.3765              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0583 T22:  -0.0521                                     
REMARK   3      T33:  -0.0617 T12:   0.0165                                     
REMARK   3      T13:  -0.0042 T23:   0.0160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0312 L22:   1.2883                                     
REMARK   3      L33:   1.1840 L12:   0.1478                                     
REMARK   3      L13:  -0.1970 L23:  -0.2239                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0382 S12:  -0.0986 S13:  -0.1958                       
REMARK   3      S21:   0.1575 S22:  -0.0128 S23:   0.0034                       
REMARK   3      S31:   0.1780 S32:  -0.0172 S33:   0.0510                       
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    10        B   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.2582 -23.9506  59.7361              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0911 T22:  -0.0931                                     
REMARK   3      T33:  -0.0960 T12:  -0.0088                                     
REMARK   3      T13:   0.0230 T23:  -0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5097 L22:   1.6203                                     
REMARK   3      L33:   1.2899 L12:   0.5672                                     
REMARK   3      L13:  -0.3238 L23:   0.1180                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0691 S12:   0.0990 S13:  -0.1160                       
REMARK   3      S21:  -0.0996 S22:   0.0368 S23:  -0.1747                       
REMARK   3      S31:  -0.0202 S32:   0.1210 S33:   0.0322                       
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    10        C   205                          
REMARK   3    ORIGIN FOR THE GROUP (A): 111.4700  -3.7013  17.1909              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0168 T22:  -0.0928                                     
REMARK   3      T33:  -0.1121 T12:   0.0017                                     
REMARK   3      T13:  -0.0074 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3293 L22:   1.4034                                     
REMARK   3      L33:   1.1928 L12:   0.2889                                     
REMARK   3      L13:  -0.2260 L23:  -0.2881                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0202 S12:  -0.1502 S13:  -0.2366                       
REMARK   3      S21:   0.1721 S22:  -0.0515 S23:  -0.0230                       
REMARK   3      S31:   0.1536 S32:  -0.0154 S33:   0.0313                       
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    10        D   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  90.7052  27.7385  93.8832              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1052 T22:  -0.0885                                     
REMARK   3      T33:  -0.1047 T12:   0.0062                                     
REMARK   3      T13:   0.0207 T23:   0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1454 L22:   2.4387                                     
REMARK   3      L33:   1.5067 L12:   0.3433                                     
REMARK   3      L13:  -0.3623 L23:   0.0249                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0096 S12:  -0.0451 S13:   0.0942                       
REMARK   3      S21:   0.1591 S22:   0.0367 S23:   0.2031                       
REMARK   3      S31:  -0.0897 S32:  -0.0891 S33:  -0.0270                       
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    10        E   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  72.9525 -20.0992  94.2212              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0735 T22:  -0.0964                                     
REMARK   3      T33:  -0.0949 T12:   0.0000                                     
REMARK   3      T13:  -0.0260 T23:   0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0753 L22:   2.1035                                     
REMARK   3      L33:   1.4607 L12:   0.3101                                     
REMARK   3      L13:   0.2867 L23:  -0.0932                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0059 S12:  -0.0387 S13:  -0.1066                       
REMARK   3      S21:   0.1975 S22:   0.0312 S23:  -0.1844                       
REMARK   3      S31:   0.0504 S32:   0.0812 S33:  -0.0254                       
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    10        F   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.5221   3.6380  17.2114              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0248 T22:  -0.1143                                     
REMARK   3      T33:  -0.1124 T12:   0.0177                                     
REMARK   3      T13:   0.0035 T23:  -0.0166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0539 L22:   1.2582                                     
REMARK   3      L33:   1.3147 L12:   0.0820                                     
REMARK   3      L13:   0.1686 L23:   0.1784                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0215 S12:  -0.0863 S13:   0.1768                       
REMARK   3      S21:   0.1496 S22:  -0.0066 S23:  -0.0189                       
REMARK   3      S31:  -0.1995 S32:   0.0170 S33:   0.0281                       
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    10        G   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  93.7208  31.8630  59.7178              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0924 T22:  -0.0965                                     
REMARK   3      T33:  -0.0993 T12:  -0.0132                                     
REMARK   3      T13:  -0.0275 T23:   0.0209                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7032 L22:   1.5982                                     
REMARK   3      L33:   1.4231 L12:   0.4951                                     
REMARK   3      L13:   0.2838 L23:  -0.1785                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0488 S12:   0.1157 S13:   0.1168                       
REMARK   3      S21:  -0.1126 S22:   0.0298 S23:   0.1827                       
REMARK   3      S31:   0.0159 S32:  -0.1320 S33:   0.0190                       
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    10        H   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.4992   7.6444  94.3547              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0022 T22:  -0.1027                                     
REMARK   3      T33:  -0.1165 T12:  -0.0027                                     
REMARK   3      T13:   0.0056 T23:  -0.0230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1845 L22:   1.4425                                     
REMARK   3      L33:   1.1911 L12:   0.2506                                     
REMARK   3      L13:   0.1138 L23:   0.2588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0300 S12:  -0.1442 S13:   0.2223                       
REMARK   3      S21:   0.1645 S22:  -0.0577 S23:   0.0080                       
REMARK   3      S31:  -0.1279 S32:   0.0052 S33:   0.0277                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I    10        I   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  90.7465  23.7293  16.7370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1182 T22:  -0.0952                                     
REMARK   3      T33:  -0.1023 T12:  -0.0016                                     
REMARK   3      T13:   0.0274 T23:  -0.0055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1403 L22:   2.2821                                     
REMARK   3      L33:   1.4249 L12:   0.2650                                     
REMARK   3      L13:  -0.3028 L23:   0.0766                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0002 S12:  -0.0234 S13:   0.0931                       
REMARK   3      S21:   0.1787 S22:   0.0200 S23:   0.1715                       
REMARK   3      S31:  -0.0410 S32:  -0.1052 S33:  -0.0198                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J    10        J   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  73.3241 -23.8312  16.6369              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1196 T22:  -0.0926                                     
REMARK   3      T33:  -0.0954 T12:   0.0073                                     
REMARK   3      T13:  -0.0268 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1525 L22:   2.3781                                     
REMARK   3      L33:   1.4930 L12:   0.4062                                     
REMARK   3      L13:   0.2732 L23:  -0.0309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0105 S12:  -0.0397 S13:  -0.1210                       
REMARK   3      S21:   0.1661 S22:   0.0387 S23:  -0.1850                       
REMARK   3      S31:   0.0727 S32:   0.0940 S33:  -0.0283                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K    10        K   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.3707 -27.6241 -17.6712              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0595 T22:  -0.0400                                     
REMARK   3      T33:  -0.0333 T12:  -0.0173                                     
REMARK   3      T13:   0.0354 T23:  -0.0256                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5050 L22:   1.4869                                     
REMARK   3      L33:   1.5812 L12:   0.4897                                     
REMARK   3      L13:  -0.2175 L23:   0.0543                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0581 S12:   0.1251 S13:  -0.0922                       
REMARK   3      S21:  -0.1311 S22:   0.0405 S23:  -0.1953                       
REMARK   3      S31:  -0.0319 S32:   0.1267 S33:   0.0176                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L    10        L   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  93.7507  27.8788 -17.4612              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0683 T22:  -0.0424                                     
REMARK   3      T33:  -0.0438 T12:  -0.0099                                     
REMARK   3      T13:  -0.0233 T23:   0.0210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6779 L22:   1.7632                                     
REMARK   3      L33:   1.3736 L12:   0.5166                                     
REMARK   3      L13:   0.3641 L23:  -0.1146                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0670 S12:   0.1059 S13:   0.1167                       
REMARK   3      S21:  -0.0994 S22:   0.0309 S23:   0.1544                       
REMARK   3      S31:  -0.0016 S32:  -0.1162 S33:   0.0361                       
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 2VFX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-NOV-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290034358.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-AUG-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97929                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 223558                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1KLQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP, 20        
REMARK 280  DEGREES C. 1 MICROLITER PROTEIN: 3 MG/ML IN 20 MM TRIS, PH 8.0,     
REMARK 280  50 MM NACL, 2 MM TCEP PLUS 1 MICROLITER RESERVOIR: 19% PEG2000,     
REMARK 280  16% GLYCEROL, 100 MM TRIS, PH 8.0, 0.3 M MGCL2, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       54.66850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       95.70350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       54.66850            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       95.70350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12                   
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 8                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 9                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 10                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 11                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 12                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CL    CL A1209  LIES ON A SPECIAL POSITION.                          
REMARK 375 MG    MG K1206  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH G2053  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH L2051  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LEU 13 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 79 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 106 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, LEU 13 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 79 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 106 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, LEU 13 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, CYS 79 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, CYS 106 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, LEU 13 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, CYS 79 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, CYS 106 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, LEU 13 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, CYS 79 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, CYS 106 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, LEU 13 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, CYS 79 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, CYS 106 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, LEU 13 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, CYS 79 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, CYS 106 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, LEU 13 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, CYS 79 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, CYS 106 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN I, LEU 13 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN I, CYS 79 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN I, CYS 106 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN J, LEU 13 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN J, CYS 79 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN J, CYS 106 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN K, LEU 13 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN K, CYS 79 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN K, CYS 106 TO SER                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN L, LEU 13 TO ALA                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN L, CYS 79 TO SER                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN L, CYS 106 TO SER                        
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     LYS A   111                                                      
REMARK 465     ASP A   112                                                      
REMARK 465     ASP A   113                                                      
REMARK 465     LYS B   111                                                      
REMARK 465     ASP B   112                                                      
REMARK 465     ASP B   113                                                      
REMARK 465     LYS C   111                                                      
REMARK 465     ASP C   112                                                      
REMARK 465     ASP C   113                                                      
REMARK 465     LYS D   111                                                      
REMARK 465     ASP D   112                                                      
REMARK 465     ASP D   113                                                      
REMARK 465     SER D   114                                                      
REMARK 465     LYS F   111                                                      
REMARK 465     ASP F   112                                                      
REMARK 465     ASP F   113                                                      
REMARK 465     ASP G   112                                                      
REMARK 465     ASP G   113                                                      
REMARK 465     SER G   114                                                      
REMARK 465     LYS H   111                                                      
REMARK 465     ASP H   112                                                      
REMARK 465     ASP H   113                                                      
REMARK 465     LYS I   111                                                      
REMARK 465     ASP I   112                                                      
REMARK 465     ASP I   113                                                      
REMARK 465     SER I   114                                                      
REMARK 465     LYS J   111                                                      
REMARK 465     ASP J   112                                                      
REMARK 465     ASP J   113                                                      
REMARK 465     SER J   114                                                      
REMARK 465     LYS J   159                                                      
REMARK 465     ASP L   112                                                      
REMARK 465     ASP L   113                                                      
REMARK 465     SER L   114                                                      
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   OE1  GLN D   101     O    HOH D  2074              2.00            
REMARK 500   OE1  GLN D   101     O    HOH D  2073              2.06            
REMARK 500   NE2  GLN D   101     O    HOH D  2071              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500  MG     MG B  1206    MG     MG B  1206     2656     1.48            
REMARK 500   NH2  ARG J     7     OH   TYR L    38     4645     2.16            
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    GLU K   8   CD    GLU K   8   OE2     0.089                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU I 161   CA  -  CB  -  CG  ANGL. DEV. =  15.7 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    GLU A   8      104.43    -50.70                                   
REMARK 500    LYS A 166      -22.30     88.12                                   
REMARK 500    THR A 189      -17.17     87.35                                   
REMARK 500    GLN B   9     -162.69   -109.15                                   
REMARK 500    LYS B 166       -9.13     81.40                                   
REMARK 500    THR B 189      -24.67     89.75                                   
REMARK 500    TYR C  49       19.93     58.85                                   
REMARK 500    ALA C 115      137.04    158.25                                   
REMARK 500    LYS C 166      -16.61     82.57                                   
REMARK 500    THR C 189      -21.00     86.87                                   
REMARK 500    GLN D   9     -160.46   -102.98                                   
REMARK 500    ASP D 158       -4.12     14.04                                   
REMARK 500    LYS D 166      -10.14     82.46                                   
REMARK 500    THR D 189      -19.35     87.60                                   
REMARK 500    LYS E 166       -9.11     81.80                                   
REMARK 500    THR E 189      -22.13     88.48                                   
REMARK 500    GLU F 118       47.78    -85.78                                   
REMARK 500    LYS F 166      -24.80     86.32                                   
REMARK 500    THR F 189      -16.49     85.43                                   
REMARK 500    ALA G 110       71.37    -68.08                                   
REMARK 500    LYS G 166      -16.01     84.80                                   
REMARK 500    THR G 189      -24.73     91.02                                   
REMARK 500    LYS H 166      -18.77     78.78                                   
REMARK 500    THR H 189      -23.08     88.43                                   
REMARK 500    GLU I   8      104.18    -55.55                                   
REMARK 500    LYS I 166      -15.99     81.40                                   
REMARK 500    THR I 189      -20.83     91.06                                   
REMARK 500    LYS J 166       -4.15     81.70                                   
REMARK 500    THR J 189      -19.00     85.65                                   
REMARK 500    LYS K 166      -11.49     82.03                                   
REMARK 500    THR K 189      -21.28     88.83                                   
REMARK 500    LYS L 166      -12.67     82.99                                   
REMARK 500    THR L 189      -21.19     89.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C2027        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH D2037        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH I2038        DISTANCE =  5.87 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PE4 A 1210                                                       
REMARK 610     PE3 B 1210                                                       
REMARK 610     PE3 C 1210                                                       
REMARK 610     PE4 E 1210                                                       
REMARK 610     PE3 F 1208                                                       
REMARK 610     PE3 G 1208                                                       
REMARK 610     PE3 H 3104                                                       
REMARK 610     PE3 K 1209                                                       
REMARK 610     PE4 L 1209                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 205   OD1                                                    
REMARK 620 2 HOH A2139   O    95.1                                              
REMARK 620 3 HOH A2143   O    94.5  96.0                                        
REMARK 620 4 HOH A2144   O    91.2  88.8 172.2                                  
REMARK 620 5 ASP A 205   OD1 171.5  93.3  83.7  89.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2130   O                                                      
REMARK 620 2 ASP B 205   OD2  71.9                                              
REMARK 620 3 HOH B2126   O   115.7  78.1                                        
REMARK 620 4 HOH B2126   O   144.7  94.0  29.2                                  
REMARK 620 5 HOH B2130   O    35.6 100.2 144.9 162.1                            
REMARK 620 6 ASP B 205   OD2  86.9 140.3  81.9  84.4  77.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I 205   OD1                                                    
REMARK 620 2 HOH C2119   O    89.0                                              
REMARK 620 3 HOH I2137   O    92.8 167.0                                        
REMARK 620 4 HOH I2133   O    93.4  96.3  96.5                                  
REMARK 620 5 ASP C 205   OD2 168.5  82.9  93.3  95.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E1206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH E2131   O                                                      
REMARK 620 2 HOH E2129   O    90.5                                              
REMARK 620 3 HOH H2118   O   168.8 100.4                                        
REMARK 620 4 ASP E 205   OD2  91.1  92.1  91.1                                  
REMARK 620 5 ASP H 205   OD1  92.0 100.7  83.4 166.8                            
REMARK 620 6 HOH H2117   O    93.0 175.2  76.3  84.6  82.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F1206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 205   OD1                                                    
REMARK 620 2 HOH F2126   O    94.3                                              
REMARK 620 3 ASP J 205   OD1 173.2  92.2                                        
REMARK 620 4 HOH F2129   O    89.1  89.9  89.0                                  
REMARK 620 5 HOH F2130   O    86.1  98.1  95.0 170.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G1206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH G2129   O                                                      
REMARK 620 2 ASP G 205   OD2  94.2                                              
REMARK 620 3 HOH G2125   O   144.2 106.2                                        
REMARK 620 4 HOH G2125   O   163.8 101.2  34.3                                  
REMARK 620 5 HOH G2129   O    40.0  72.3 175.7 141.6                            
REMARK 620 6 HOH G2130   O    95.3  85.4 115.0  80.9  61.1                      
REMARK 620 7 HOH G2130   O    62.8  98.3  85.0 119.2  99.2 157.9                
REMARK 620 8 ASP G 205   OD2  68.0 159.7  94.1  96.0  87.6  86.8  82.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG K1206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH K2134   O                                                      
REMARK 620 2 HOH K2134   O    19.2                                              
REMARK 620 3 HOH K2138   O   173.3 155.9                                        
REMARK 620 4 HOH K2138   O   154.3 171.4  31.4                                  
REMARK 620 5 HOH K2139   O    86.5 105.6  96.9  69.9                            
REMARK 620 6 HOH K2139   O   106.3  87.3  70.5  97.3 167.1                      
REMARK 620 7 ASP K 205   OD2  96.1  98.1  89.5  75.1  91.8  85.8                
REMARK 620 8 ASP K 205   OD2  98.8  97.1  75.8  89.9  85.8  93.2 164.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG L1206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH L2121   O                                                      
REMARK 620 2 HOH L2125   O   153.9                                              
REMARK 620 3 ASP L 205   OD2 102.1 100.0                                        
REMARK 620 4 HOH L2121   O    25.6 161.2  77.1                                  
REMARK 620 5 HOH L2127   O   100.1  85.4 108.8 113.2                            
REMARK 620 6 HOH L2127   O    85.5  86.9  75.8  74.3 171.6                      
REMARK 620 7 HOH L2125   O   147.3  30.3  76.9 133.6 111.2  62.4                
REMARK 620 8 ASP L 205   OD2  75.7  78.2 152.4  95.6  98.6  76.6  90.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C1206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E1206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F1206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G1206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K1206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L1206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E1207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E3102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL I3103                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL J3104                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D1206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL I1206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL J1206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F1207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D1207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B3111                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G1207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL L1207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E1208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D1208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL J1207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL K1207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D1209                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL L1208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL I1207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL K1208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1209                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL I1208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1209                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E1209                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D1210                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL J1208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 L1209                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 C1210                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 F1208                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 H3104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 G1208                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 B1210                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG I1209                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE3 K1209                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A1210                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 E1210                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2V64   RELATED DB: PDB                                   
REMARK 900 CRYSTALLOGRAPHIC STRUCTURE OF THE CONFORMATIONAL DIMER OF THE        
REMARK 900 SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2.                            
REMARK 900 RELATED ID: 1KLQ   RELATED DB: PDB                                   
REMARK 900 THE MAD2 SPINDLE CHECKPOINT PROTEIN UNDERGOES SIMILAR                
REMARK 900 MAJORCONFORMATIONAL CHANGES UPON BINDING TO EITHER MAD1 OR CDC20     
REMARK 900 RELATED ID: 1S2H   RELATED DB: PDB                                   
REMARK 900 THE MAD2 SPINDLE CHECKPOINT PROTEIN POSSESSES TWO DISTINCTNATIVELY   
REMARK 900 FOLDED STATES                                                        
REMARK 900 RELATED ID: 1GO4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MAD1-MAD2 REVEALS A CONSERVED MAD2 BINDING      
REMARK 900 MOTIF IN MAD1 AND CDC20.                                             
REMARK 900 RELATED ID: 1DUJ   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY CHECKPOINTPROTEIN HUMAN   
REMARK 900 MAD2                                                                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE FIRST GLYCINE IS PART OF THE CLONING LINKER. L13 HAS             
REMARK 999 BEEN MUTATED TO A                                                    
DBREF  2VFX A    0     0  PDB    2VFX     2VFX             0      0             
DBREF  2VFX A    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  2VFX B    0     0  PDB    2VFX     2VFX             0      0             
DBREF  2VFX B    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  2VFX C    0     0  PDB    2VFX     2VFX             0      0             
DBREF  2VFX C    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  2VFX D    0     0  PDB    2VFX     2VFX             0      0             
DBREF  2VFX D    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  2VFX E    0     0  PDB    2VFX     2VFX             0      0             
DBREF  2VFX E    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  2VFX F    0     0  PDB    2VFX     2VFX             0      0             
DBREF  2VFX F    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  2VFX G    0     0  PDB    2VFX     2VFX             0      0             
DBREF  2VFX G    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  2VFX H    0     0  PDB    2VFX     2VFX             0      0             
DBREF  2VFX H    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  2VFX I    0     0  PDB    2VFX     2VFX             0      0             
DBREF  2VFX I    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  2VFX J    0     0  PDB    2VFX     2VFX             0      0             
DBREF  2VFX J    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  2VFX K    0     0  PDB    2VFX     2VFX             0      0             
DBREF  2VFX K    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  2VFX L    0     0  PDB    2VFX     2VFX             0      0             
DBREF  2VFX L    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
SEQADV 2VFX ALA A   13  UNP  Q13257    LEU    13 ENGINEERED MUTATION            
SEQADV 2VFX SER A   79  UNP  Q13257    CYS    79 ENGINEERED MUTATION            
SEQADV 2VFX SER A  106  UNP  Q13257    CYS   106 ENGINEERED MUTATION            
SEQADV 2VFX ALA B   13  UNP  Q13257    LEU    13 ENGINEERED MUTATION            
SEQADV 2VFX SER B   79  UNP  Q13257    CYS    79 ENGINEERED MUTATION            
SEQADV 2VFX SER B  106  UNP  Q13257    CYS   106 ENGINEERED MUTATION            
SEQADV 2VFX ALA C   13  UNP  Q13257    LEU    13 ENGINEERED MUTATION            
SEQADV 2VFX SER C   79  UNP  Q13257    CYS    79 ENGINEERED MUTATION            
SEQADV 2VFX SER C  106  UNP  Q13257    CYS   106 ENGINEERED MUTATION            
SEQADV 2VFX ALA D   13  UNP  Q13257    LEU    13 ENGINEERED MUTATION            
SEQADV 2VFX SER D   79  UNP  Q13257    CYS    79 ENGINEERED MUTATION            
SEQADV 2VFX SER D  106  UNP  Q13257    CYS   106 ENGINEERED MUTATION            
SEQADV 2VFX ALA E   13  UNP  Q13257    LEU    13 ENGINEERED MUTATION            
SEQADV 2VFX SER E   79  UNP  Q13257    CYS    79 ENGINEERED MUTATION            
SEQADV 2VFX SER E  106  UNP  Q13257    CYS   106 ENGINEERED MUTATION            
SEQADV 2VFX ALA F   13  UNP  Q13257    LEU    13 ENGINEERED MUTATION            
SEQADV 2VFX SER F   79  UNP  Q13257    CYS    79 ENGINEERED MUTATION            
SEQADV 2VFX SER F  106  UNP  Q13257    CYS   106 ENGINEERED MUTATION            
SEQADV 2VFX ALA G   13  UNP  Q13257    LEU    13 ENGINEERED MUTATION            
SEQADV 2VFX SER G   79  UNP  Q13257    CYS    79 ENGINEERED MUTATION            
SEQADV 2VFX SER G  106  UNP  Q13257    CYS   106 ENGINEERED MUTATION            
SEQADV 2VFX ALA H   13  UNP  Q13257    LEU    13 ENGINEERED MUTATION            
SEQADV 2VFX SER H   79  UNP  Q13257    CYS    79 ENGINEERED MUTATION            
SEQADV 2VFX SER H  106  UNP  Q13257    CYS   106 ENGINEERED MUTATION            
SEQADV 2VFX ALA I   13  UNP  Q13257    LEU    13 ENGINEERED MUTATION            
SEQADV 2VFX SER I   79  UNP  Q13257    CYS    79 ENGINEERED MUTATION            
SEQADV 2VFX SER I  106  UNP  Q13257    CYS   106 ENGINEERED MUTATION            
SEQADV 2VFX ALA J   13  UNP  Q13257    LEU    13 ENGINEERED MUTATION            
SEQADV 2VFX SER J   79  UNP  Q13257    CYS    79 ENGINEERED MUTATION            
SEQADV 2VFX SER J  106  UNP  Q13257    CYS   106 ENGINEERED MUTATION            
SEQADV 2VFX ALA K   13  UNP  Q13257    LEU    13 ENGINEERED MUTATION            
SEQADV 2VFX SER K   79  UNP  Q13257    CYS    79 ENGINEERED MUTATION            
SEQADV 2VFX SER K  106  UNP  Q13257    CYS   106 ENGINEERED MUTATION            
SEQADV 2VFX ALA L   13  UNP  Q13257    LEU    13 ENGINEERED MUTATION            
SEQADV 2VFX SER L   79  UNP  Q13257    CYS    79 ENGINEERED MUTATION            
SEQADV 2VFX SER L  106  UNP  Q13257    CYS   106 ENGINEERED MUTATION            
SEQRES   1 A  206  GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR          
SEQRES   2 A  206  ALA ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER          
SEQRES   3 A  206  PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR          
SEQRES   4 A  206  PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU          
SEQRES   5 A  206  THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR          
SEQRES   6 A  206  LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR          
SEQRES   7 A  206  LYS SER SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN          
SEQRES   8 A  206  ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP          
SEQRES   9 A  206  ILE GLU SER ASP LYS THR ALA LYS ASP ASP SER ALA PRO          
SEQRES  10 A  206  ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG          
SEQRES  11 A  206  SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE LEU          
SEQRES  12 A  206  PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE          
SEQRES  13 A  206  TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU          
SEQRES  14 A  206  GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL          
SEQRES  15 A  206  ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN          
SEQRES  16 A  206  SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                  
SEQRES   1 B  206  GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR          
SEQRES   2 B  206  ALA ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER          
SEQRES   3 B  206  PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR          
SEQRES   4 B  206  PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU          
SEQRES   5 B  206  THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR          
SEQRES   6 B  206  LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR          
SEQRES   7 B  206  LYS SER SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN          
SEQRES   8 B  206  ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP          
SEQRES   9 B  206  ILE GLU SER ASP LYS THR ALA LYS ASP ASP SER ALA PRO          
SEQRES  10 B  206  ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG          
SEQRES  11 B  206  SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE LEU          
SEQRES  12 B  206  PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE          
SEQRES  13 B  206  TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU          
SEQRES  14 B  206  GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL          
SEQRES  15 B  206  ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN          
SEQRES  16 B  206  SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                  
SEQRES   1 C  206  GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR          
SEQRES   2 C  206  ALA ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER          
SEQRES   3 C  206  PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR          
SEQRES   4 C  206  PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU          
SEQRES   5 C  206  THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR          
SEQRES   6 C  206  LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR          
SEQRES   7 C  206  LYS SER SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN          
SEQRES   8 C  206  ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP          
SEQRES   9 C  206  ILE GLU SER ASP LYS THR ALA LYS ASP ASP SER ALA PRO          
SEQRES  10 C  206  ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG          
SEQRES  11 C  206  SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE LEU          
SEQRES  12 C  206  PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE          
SEQRES  13 C  206  TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU          
SEQRES  14 C  206  GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL          
SEQRES  15 C  206  ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN          
SEQRES  16 C  206  SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                  
SEQRES   1 D  206  GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR          
SEQRES   2 D  206  ALA ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER          
SEQRES   3 D  206  PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR          
SEQRES   4 D  206  PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU          
SEQRES   5 D  206  THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR          
SEQRES   6 D  206  LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR          
SEQRES   7 D  206  LYS SER SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN          
SEQRES   8 D  206  ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP          
SEQRES   9 D  206  ILE GLU SER ASP LYS THR ALA LYS ASP ASP SER ALA PRO          
SEQRES  10 D  206  ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG          
SEQRES  11 D  206  SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE LEU          
SEQRES  12 D  206  PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE          
SEQRES  13 D  206  TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU          
SEQRES  14 D  206  GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL          
SEQRES  15 D  206  ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN          
SEQRES  16 D  206  SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                  
SEQRES   1 E  206  GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR          
SEQRES   2 E  206  ALA ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER          
SEQRES   3 E  206  PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR          
SEQRES   4 E  206  PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU          
SEQRES   5 E  206  THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR          
SEQRES   6 E  206  LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR          
SEQRES   7 E  206  LYS SER SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN          
SEQRES   8 E  206  ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP          
SEQRES   9 E  206  ILE GLU SER ASP LYS THR ALA LYS ASP ASP SER ALA PRO          
SEQRES  10 E  206  ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG          
SEQRES  11 E  206  SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE LEU          
SEQRES  12 E  206  PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE          
SEQRES  13 E  206  TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU          
SEQRES  14 E  206  GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL          
SEQRES  15 E  206  ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN          
SEQRES  16 E  206  SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                  
SEQRES   1 F  206  GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR          
SEQRES   2 F  206  ALA ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER          
SEQRES   3 F  206  PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR          
SEQRES   4 F  206  PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU          
SEQRES   5 F  206  THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR          
SEQRES   6 F  206  LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR          
SEQRES   7 F  206  LYS SER SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN          
SEQRES   8 F  206  ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP          
SEQRES   9 F  206  ILE GLU SER ASP LYS THR ALA LYS ASP ASP SER ALA PRO          
SEQRES  10 F  206  ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG          
SEQRES  11 F  206  SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE LEU          
SEQRES  12 F  206  PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE          
SEQRES  13 F  206  TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU          
SEQRES  14 F  206  GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL          
SEQRES  15 F  206  ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN          
SEQRES  16 F  206  SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                  
SEQRES   1 G  206  GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR          
SEQRES   2 G  206  ALA ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER          
SEQRES   3 G  206  PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR          
SEQRES   4 G  206  PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU          
SEQRES   5 G  206  THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR          
SEQRES   6 G  206  LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR          
SEQRES   7 G  206  LYS SER SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN          
SEQRES   8 G  206  ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP          
SEQRES   9 G  206  ILE GLU SER ASP LYS THR ALA LYS ASP ASP SER ALA PRO          
SEQRES  10 G  206  ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG          
SEQRES  11 G  206  SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE LEU          
SEQRES  12 G  206  PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE          
SEQRES  13 G  206  TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU          
SEQRES  14 G  206  GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL          
SEQRES  15 G  206  ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN          
SEQRES  16 G  206  SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                  
SEQRES   1 H  206  GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR          
SEQRES   2 H  206  ALA ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER          
SEQRES   3 H  206  PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR          
SEQRES   4 H  206  PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU          
SEQRES   5 H  206  THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR          
SEQRES   6 H  206  LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR          
SEQRES   7 H  206  LYS SER SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN          
SEQRES   8 H  206  ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP          
SEQRES   9 H  206  ILE GLU SER ASP LYS THR ALA LYS ASP ASP SER ALA PRO          
SEQRES  10 H  206  ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG          
SEQRES  11 H  206  SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE LEU          
SEQRES  12 H  206  PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE          
SEQRES  13 H  206  TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU          
SEQRES  14 H  206  GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL          
SEQRES  15 H  206  ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN          
SEQRES  16 H  206  SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                  
SEQRES   1 I  206  GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR          
SEQRES   2 I  206  ALA ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER          
SEQRES   3 I  206  PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR          
SEQRES   4 I  206  PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU          
SEQRES   5 I  206  THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR          
SEQRES   6 I  206  LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR          
SEQRES   7 I  206  LYS SER SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN          
SEQRES   8 I  206  ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP          
SEQRES   9 I  206  ILE GLU SER ASP LYS THR ALA LYS ASP ASP SER ALA PRO          
SEQRES  10 I  206  ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG          
SEQRES  11 I  206  SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE LEU          
SEQRES  12 I  206  PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE          
SEQRES  13 I  206  TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU          
SEQRES  14 I  206  GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL          
SEQRES  15 I  206  ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN          
SEQRES  16 I  206  SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                  
SEQRES   1 J  206  GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR          
SEQRES   2 J  206  ALA ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER          
SEQRES   3 J  206  PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR          
SEQRES   4 J  206  PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU          
SEQRES   5 J  206  THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR          
SEQRES   6 J  206  LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR          
SEQRES   7 J  206  LYS SER SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN          
SEQRES   8 J  206  ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP          
SEQRES   9 J  206  ILE GLU SER ASP LYS THR ALA LYS ASP ASP SER ALA PRO          
SEQRES  10 J  206  ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG          
SEQRES  11 J  206  SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE LEU          
SEQRES  12 J  206  PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE          
SEQRES  13 J  206  TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU          
SEQRES  14 J  206  GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL          
SEQRES  15 J  206  ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN          
SEQRES  16 J  206  SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                  
SEQRES   1 K  206  GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR          
SEQRES   2 K  206  ALA ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER          
SEQRES   3 K  206  PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR          
SEQRES   4 K  206  PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU          
SEQRES   5 K  206  THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR          
SEQRES   6 K  206  LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR          
SEQRES   7 K  206  LYS SER SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN          
SEQRES   8 K  206  ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP          
SEQRES   9 K  206  ILE GLU SER ASP LYS THR ALA LYS ASP ASP SER ALA PRO          
SEQRES  10 K  206  ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG          
SEQRES  11 K  206  SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE LEU          
SEQRES  12 K  206  PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE          
SEQRES  13 K  206  TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU          
SEQRES  14 K  206  GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL          
SEQRES  15 K  206  ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN          
SEQRES  16 K  206  SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                  
SEQRES   1 L  206  GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR          
SEQRES   2 L  206  ALA ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER          
SEQRES   3 L  206  PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR          
SEQRES   4 L  206  PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU          
SEQRES   5 L  206  THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR          
SEQRES   6 L  206  LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR          
SEQRES   7 L  206  LYS SER SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN          
SEQRES   8 L  206  ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP          
SEQRES   9 L  206  ILE GLU SER ASP LYS THR ALA LYS ASP ASP SER ALA PRO          
SEQRES  10 L  206  ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG          
SEQRES  11 L  206  SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE LEU          
SEQRES  12 L  206  PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE          
SEQRES  13 L  206  TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU          
SEQRES  14 L  206  GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL          
SEQRES  15 L  206  ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN          
SEQRES  16 L  206  SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                  
HET     MG  A1206       1                                                       
HET     CL  A1207       1                                                       
HET     CL  A1208       1                                                       
HET     CL  A1209       1                                                       
HET    PE4  A1210      13                                                       
HET     MG  B1206       1                                                       
HET     CL  B1207       1                                                       
HET     CL  B1208       1                                                       
HET     CL  B1209       1                                                       
HET    PE3  B1210      10                                                       
HET     CL  B3111       1                                                       
HET     MG  C1206       1                                                       
HET     CL  C1207       1                                                       
HET     CL  C1208       1                                                       
HET     CL  C1209       1                                                       
HET    PE3  C1210      10                                                       
HET     CL  D1206       1                                                       
HET     CL  D1207       1                                                       
HET     CL  D1208       1                                                       
HET     CL  D1209       1                                                       
HET     CL  D1210       1                                                       
HET     MG  E1206       1                                                       
HET     CL  E1207       1                                                       
HET     CL  E1208       1                                                       
HET     CL  E1209       1                                                       
HET    PE4  E1210      13                                                       
HET     CL  E3102       1                                                       
HET     CL  E3129       1                                                       
HET     MG  F1206       1                                                       
HET     CL  F1207       1                                                       
HET    PE3  F1208      10                                                       
HET     CL  F3132       1                                                       
HET     MG  G1206       1                                                       
HET     CL  G1207       1                                                       
HET    PE3  G1208      10                                                       
HET    PE3  H3104      10                                                       
HET     CL  I1206       1                                                       
HET     CL  I1207       1                                                       
HET     CL  I1208       1                                                       
HET    PEG  I1209       7                                                       
HET     CL  I3103       1                                                       
HET     CL  J1206       1                                                       
HET     CL  J1207       1                                                       
HET     CL  J1208       1                                                       
HET     CL  J3104       1                                                       
HET     CL  J3128       1                                                       
HET     MG  K1206       1                                                       
HET     CL  K1207       1                                                       
HET     CL  K1208       1                                                       
HET    PE3  K1209      10                                                       
HET     MG  L1206       1                                                       
HET     CL  L1207       1                                                       
HET     CL  L1208       1                                                       
HET    PE4  L1209      13                                                       
HET     CL  L3127       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-              
HETNAM   2 PE4  ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL                                 
HETNAM     PE3 3,6,9,12,15,18,21,24,27,30,33,36,39-                             
HETNAM   2 PE3  TRIDECAOXAHENTETRACONTANE-1,41-DIOL                             
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     PE4 POLYETHYLENE GLYCOL PEG4000                                      
HETSYN     PE3 POLYETHYLENE GLYCOL                                              
FORMUL  13   MG    8(MG 2+)                                                     
FORMUL  14   CL    37(CL 1-)                                                    
FORMUL  17  PE4    3(C16 H34 O8)                                                
FORMUL  22  PE3    6(C28 H58 O15)                                               
FORMUL  52  PEG    C4 H10 O3                                                    
FORMUL  68  HOH   *1591(H2 O)                                                   
HELIX    1   1 THR A   12  ARG A   35  1                                  24    
HELIX    2   2 PRO A   39  GLU A   41  5                                   3    
HELIX    3   3 ASP A   58  LYS A   78  1                                  21    
HELIX    4   4 SER A  120  THR A  140  1                                  21    
HELIX    5   5 THR B   12  ARG B   35  1                                  24    
HELIX    6   6 PRO B   39  GLU B   41  5                                   3    
HELIX    7   7 ASP B   58  LYS B   78  1                                  21    
HELIX    8   8 SER B  120  THR B  140  1                                  21    
HELIX    9   9 THR C   12  ARG C   35  1                                  24    
HELIX   10  10 PRO C   39  GLU C   41  5                                   3    
HELIX   11  11 ASP C   58  LYS C   78  1                                  21    
HELIX   12  12 SER C  120  THR C  140  1                                  21    
HELIX   13  13 THR D   12  ARG D   35  1                                  24    
HELIX   14  14 PRO D   39  GLU D   41  5                                   3    
HELIX   15  15 ASP D   58  LYS D   78  1                                  21    
HELIX   16  16 SER D  120  THR D  140  1                                  21    
HELIX   17  17 THR E   12  ARG E   35  1                                  24    
HELIX   18  18 PRO E   39  GLU E   41  5                                   3    
HELIX   19  19 ASP E   58  LYS E   78  1                                  21    
HELIX   20  20 THR E  109  ASP E  113  5                                   5    
HELIX   21  21 SER E  120  THR E  140  1                                  21    
HELIX   22  22 THR F   12  ARG F   35  1                                  24    
HELIX   23  23 PRO F   39  GLU F   41  5                                   3    
HELIX   24  24 ASP F   58  LYS F   78  1                                  21    
HELIX   25  25 SER F  120  THR F  140  1                                  21    
HELIX   26  26 THR G   12  ARG G   35  1                                  24    
HELIX   27  27 PRO G   39  GLU G   41  5                                   3    
HELIX   28  28 ASP G   58  LYS G   78  1                                  21    
HELIX   29  29 SER G  120  LEU G  142  1                                  23    
HELIX   30  30 THR H   12  ARG H   35  1                                  24    
HELIX   31  31 PRO H   39  GLU H   41  5                                   3    
HELIX   32  32 ASP H   58  LYS H   78  1                                  21    
HELIX   33  33 SER H  120  THR H  140  1                                  21    
HELIX   34  34 THR I   12  ARG I   35  1                                  24    
HELIX   35  35 PRO I   39  GLU I   41  5                                   3    
HELIX   36  36 ASP I   58  LYS I   78  1                                  21    
HELIX   37  37 SER I  120  THR I  140  1                                  21    
HELIX   38  38 THR J   12  ARG J   35  1                                  24    
HELIX   39  39 PRO J   39  GLU J   41  5                                   3    
HELIX   40  40 ASP J   58  LYS J   78  1                                  21    
HELIX   41  41 SER J  120  THR J  140  1                                  21    
HELIX   42  42 THR K   12  ARG K   35  1                                  24    
HELIX   43  43 PRO K   39  GLU K   41  5                                   3    
HELIX   44  44 ASP K   58  LYS K   78  1                                  21    
HELIX   45  45 THR K  109  ASP K  113  5                                   5    
HELIX   46  46 SER K  120  THR K  140  1                                  21    
HELIX   47  47 THR L   12  ARG L   35  1                                  24    
HELIX   48  48 PRO L   39  GLU L   41  5                                   3    
HELIX   49  49 ASP L   58  LYS L   78  1                                  21    
HELIX   50  50 SER L  120  THR L  140  1                                  21    
SHEET    1  EA 7 TRP E 167  GLU E 169  0                                        
SHEET    2  EA 7 MET A   1  LEU A   5 -1  O  GLN A   4   N  GLU E 168           
SHEET    3  EA 7 CYS E 149  THR E 157 -1  O  ILE E 155   N  LEU A   3           
SHEET    4  EA 7 VAL E  81  ASN E  90 -1  N  GLN E  82   O  TYR E 156           
SHEET    5  EA 7 VAL E  96  SER E 106 -1  N  LEU E  97   O  ILE E  88           
SHEET    6  EA 7 HIS E 191  LYS E 200 -1  O  LYS E 192   N  GLU E 105           
SHEET    7  EA 7 SER E 178  ARG E 182 -1  O  GLU E 179   N  TYR E 199           
SHEET    1  EB 7 TRP E 167  GLU E 169  0                                        
SHEET    2  EB 7 MET A   1  LEU A   5 -1  O  GLN A   4   N  GLU E 168           
SHEET    3  EB 7 CYS E 149  THR E 157 -1  O  ILE E 155   N  LEU A   3           
SHEET    4  EB 7 VAL E  81  ASN E  90 -1  N  GLN E  82   O  TYR E 156           
SHEET    5  EB 7 VAL E  96  SER E 106 -1  N  LEU E  97   O  ILE E  88           
SHEET    6  EB 7 HIS E 191  LYS E 200 -1  O  LYS E 192   N  GLU E 105           
SHEET    7  EB 7 PHE E 186  THR E 187 -1  O  PHE E 186   N  VAL E 193           
SHEET    1  AA 2 PHE A  43  LYS A  48  0                                        
SHEET    2  AA 2 LEU A  51  THR A  56 -1  O  LEU A  51   N  LYS A  48           
SHEET    1  AB 5 CYS A 149  THR A 157  0                                        
SHEET    2  AB 5 VAL A  81  ASN A  90 -1  N  GLN A  82   O  TYR A 156           
SHEET    3  AB 5 VAL A  96  SER A 106 -1  N  LEU A  97   O  ILE A  88           
SHEET    4  AB 5 HIS A 191  LYS A 200 -1  O  LYS A 192   N  GLU A 105           
SHEET    5  AB 5 SER A 178  ARG A 182 -1  O  GLU A 179   N  TYR A 199           
SHEET    1  AC 5 CYS A 149  THR A 157  0                                        
SHEET    2  AC 5 VAL A  81  ASN A  90 -1  N  GLN A  82   O  TYR A 156           
SHEET    3  AC 5 VAL A  96  SER A 106 -1  N  LEU A  97   O  ILE A  88           
SHEET    4  AC 5 HIS A 191  LYS A 200 -1  O  LYS A 192   N  GLU A 105           
SHEET    5  AC 5 PHE A 186  THR A 187 -1  O  PHE A 186   N  VAL A 193           
SHEET    1  BA 2 PHE B  43  LYS B  48  0                                        
SHEET    2  BA 2 LEU B  51  THR B  56 -1  O  LEU B  51   N  LYS B  48           
SHEET    1  BB 5 CYS B 149  THR B 157  0                                        
SHEET    2  BB 5 VAL B  81  ASN B  90 -1  N  GLN B  82   O  TYR B 156           
SHEET    3  BB 5 VAL B  96  SER B 106 -1  N  LEU B  97   O  ILE B  88           
SHEET    4  BB 5 HIS B 191  LYS B 200 -1  O  LYS B 192   N  GLU B 105           
SHEET    5  BB 5 SER B 178  ARG B 182 -1  O  GLU B 179   N  TYR B 199           
SHEET    1  BC 5 CYS B 149  THR B 157  0                                        
SHEET    2  BC 5 VAL B  81  ASN B  90 -1  N  GLN B  82   O  TYR B 156           
SHEET    3  BC 5 VAL B  96  SER B 106 -1  N  LEU B  97   O  ILE B  88           
SHEET    4  BC 5 HIS B 191  LYS B 200 -1  O  LYS B 192   N  GLU B 105           
SHEET    5  BC 5 PHE B 186  THR B 187 -1  O  PHE B 186   N  VAL B 193           
SHEET    1  JA10 TRP J 167  GLU J 169  0                                        
SHEET    2  JA10 ALA C   2  LEU C   5 -1  O  GLN C   4   N  GLU J 168           
SHEET    3  JA10 CYS J 149  TYR J 156 -1  O  ILE J 155   N  LEU C   3           
SHEET    4  JA10 LYS J  83  ASN J  90 -1  O  LYS J  83   N  TYR J 156           
SHEET    5  JA10 VAL J  96  SER J 106 -1  N  LEU J  97   O  ILE J  88           
SHEET    6  JA10 HIS J 191  LYS J 200 -1  O  LYS J 192   N  GLU J 105           
SHEET    7  JA10 SER J 178  ARG J 182 -1  O  GLU J 179   N  TYR J 199           
SHEET    8  JA10 HIS J 191  LYS J 200 -1  O  VAL J 197   N  VAL J 181           
SHEET    9  JA10 PHE J 186  THR J 187 -1  O  PHE J 186   N  VAL J 193           
SHEET   10  JA10 HIS J 191  LYS J 200 -1  O  VAL J 193   N  PHE J 186           
SHEET    1  CA 2 PHE C  43  LYS C  48  0                                        
SHEET    2  CA 2 LEU C  51  THR C  56 -1  O  LEU C  51   N  LYS C  48           
SHEET    1  CB 8 CYS C 149  THR C 157  0                                        
SHEET    2  CB 8 VAL C  81  ASN C  90 -1  N  GLN C  82   O  TYR C 156           
SHEET    3  CB 8 VAL C  96  SER C 106 -1  N  LEU C  97   O  ILE C  88           
SHEET    4  CB 8 HIS C 191  LYS C 200 -1  O  LYS C 192   N  GLU C 105           
SHEET    5  CB 8 SER C 178  ARG C 182 -1  O  GLU C 179   N  TYR C 199           
SHEET    6  CB 8 HIS C 191  LYS C 200 -1  O  VAL C 197   N  VAL C 181           
SHEET    7  CB 8 PHE C 186  THR C 187 -1  O  PHE C 186   N  VAL C 193           
SHEET    8  CB 8 HIS C 191  LYS C 200 -1  O  VAL C 193   N  PHE C 186           
SHEET    1  DA 2 PHE D  43  LYS D  48  0                                        
SHEET    2  DA 2 LEU D  51  THR D  56 -1  O  LEU D  51   N  LYS D  48           
SHEET    1  DB10 TRP D 167  GLU D 169  0                                        
SHEET    2  DB10 ALA H   2  LEU H   5 -1  O  GLN H   4   N  GLU D 168           
SHEET    3  DB10 CYS D 149  TYR D 156 -1  O  ILE D 155   N  LEU H   3           
SHEET    4  DB10 LYS D  83  ASN D  90 -1  O  LYS D  83   N  TYR D 156           
SHEET    5  DB10 VAL D  96  SER D 106 -1  N  LEU D  97   O  ILE D  88           
SHEET    6  DB10 HIS D 191  LYS D 200 -1  O  LYS D 192   N  GLU D 105           
SHEET    7  DB10 SER D 178  ARG D 182 -1  O  GLU D 179   N  TYR D 199           
SHEET    8  DB10 HIS D 191  LYS D 200 -1  O  VAL D 197   N  VAL D 181           
SHEET    9  DB10 PHE D 186  THR D 187 -1  O  PHE D 186   N  VAL D 193           
SHEET   10  DB10 HIS D 191  LYS D 200 -1  O  VAL D 193   N  PHE D 186           
SHEET    1  EC 2 PHE E  43  LYS E  48  0                                        
SHEET    2  EC 2 LEU E  51  THR E  56 -1  O  LEU E  51   N  LYS E  48           
SHEET    1  IA10 TRP I 167  GLU I 169  0                                        
SHEET    2  IA10 MET F   1  LEU F   5 -1  O  GLN F   4   N  GLU I 168           
SHEET    3  IA10 CYS I 149  THR I 157 -1  O  ILE I 155   N  LEU F   3           
SHEET    4  IA10 VAL I  81  ASN I  90 -1  N  GLN I  82   O  TYR I 156           
SHEET    5  IA10 VAL I  96  SER I 106 -1  N  LEU I  97   O  ILE I  88           
SHEET    6  IA10 HIS I 191  LYS I 200 -1  O  LYS I 192   N  GLU I 105           
SHEET    7  IA10 SER I 178  ARG I 182 -1  O  GLU I 179   N  TYR I 199           
SHEET    8  IA10 HIS I 191  LYS I 200 -1  O  VAL I 197   N  VAL I 181           
SHEET    9  IA10 PHE I 186  THR I 187 -1  O  PHE I 186   N  VAL I 193           
SHEET   10  IA10 HIS I 191  LYS I 200 -1  O  VAL I 193   N  PHE I 186           
SHEET    1  FA 2 PHE F  43  LYS F  48  0                                        
SHEET    2  FA 2 LEU F  51  THR F  56 -1  O  LEU F  51   N  LYS F  48           
SHEET    1  FB 5 CYS F 149  THR F 157  0                                        
SHEET    2  FB 5 VAL F  81  ASN F  90 -1  N  GLN F  82   O  TYR F 156           
SHEET    3  FB 5 VAL F  96  SER F 106 -1  N  LEU F  97   O  ILE F  88           
SHEET    4  FB 5 HIS F 191  LYS F 200 -1  O  LYS F 192   N  GLU F 105           
SHEET    5  FB 5 SER F 178  THR F 187 -1  O  GLU F 179   N  TYR F 199           
SHEET    1  GA 2 PHE G  43  LYS G  48  0                                        
SHEET    2  GA 2 LEU G  51  THR G  56 -1  O  LEU G  51   N  LYS G  48           
SHEET    1  GB 8 CYS G 149  THR G 157  0                                        
SHEET    2  GB 8 VAL G  81  ASN G  90 -1  N  GLN G  82   O  TYR G 156           
SHEET    3  GB 8 VAL G  96  SER G 106 -1  N  LEU G  97   O  ILE G  88           
SHEET    4  GB 8 HIS G 191  LYS G 200 -1  O  LYS G 192   N  GLU G 105           
SHEET    5  GB 8 SER G 178  ARG G 182 -1  O  GLU G 179   N  TYR G 199           
SHEET    6  GB 8 HIS G 191  LYS G 200 -1  O  VAL G 197   N  VAL G 181           
SHEET    7  GB 8 PHE G 186  THR G 187 -1  O  PHE G 186   N  VAL G 193           
SHEET    8  GB 8 HIS G 191  LYS G 200 -1  O  VAL G 193   N  PHE G 186           
SHEET    1  HA 2 PHE H  43  LYS H  48  0                                        
SHEET    2  HA 2 LEU H  51  THR H  56 -1  O  LEU H  51   N  LYS H  48           
SHEET    1  HB 8 CYS H 149  THR H 157  0                                        
SHEET    2  HB 8 VAL H  81  ASN H  90 -1  N  GLN H  82   O  TYR H 156           
SHEET    3  HB 8 VAL H  96  SER H 106 -1  N  LEU H  97   O  ILE H  88           
SHEET    4  HB 8 HIS H 191  LYS H 200 -1  O  LYS H 192   N  GLU H 105           
SHEET    5  HB 8 SER H 178  ARG H 182 -1  O  GLU H 179   N  TYR H 199           
SHEET    6  HB 8 HIS H 191  LYS H 200 -1  O  VAL H 197   N  VAL H 181           
SHEET    7  HB 8 PHE H 186  THR H 187 -1  O  PHE H 186   N  VAL H 193           
SHEET    8  HB 8 HIS H 191  LYS H 200 -1  O  VAL H 193   N  PHE H 186           
SHEET    1  IB 2 PHE I  43  LYS I  48  0                                        
SHEET    2  IB 2 LEU I  51  THR I  56 -1  O  LEU I  51   N  LYS I  48           
SHEET    1  JB 2 PHE J  43  LYS J  48  0                                        
SHEET    2  JB 2 LEU J  51  THR J  56 -1  O  LEU J  51   N  LYS J  48           
SHEET    1  KA 2 PHE K  43  LYS K  48  0                                        
SHEET    2  KA 2 LEU K  51  THR K  56 -1  O  LEU K  51   N  LYS K  48           
SHEET    1  KB 8 CYS K 149  THR K 157  0                                        
SHEET    2  KB 8 VAL K  81  ASN K  90 -1  N  GLN K  82   O  TYR K 156           
SHEET    3  KB 8 VAL K  96  SER K 106 -1  N  LEU K  97   O  ILE K  88           
SHEET    4  KB 8 HIS K 191  LYS K 200 -1  O  LYS K 192   N  GLU K 105           
SHEET    5  KB 8 SER K 178  ARG K 182 -1  O  GLU K 179   N  TYR K 199           
SHEET    6  KB 8 HIS K 191  LYS K 200 -1  O  VAL K 197   N  VAL K 181           
SHEET    7  KB 8 PHE K 186  THR K 187 -1  O  PHE K 186   N  VAL K 193           
SHEET    8  KB 8 HIS K 191  LYS K 200 -1  O  VAL K 193   N  PHE K 186           
SHEET    1  LA 2 PHE L  43  LYS L  48  0                                        
SHEET    2  LA 2 LEU L  51  THR L  56 -1  O  LEU L  51   N  LYS L  48           
SHEET    1  LB 8 CYS L 149  THR L 157  0                                        
SHEET    2  LB 8 VAL L  81  ASN L  90 -1  N  GLN L  82   O  TYR L 156           
SHEET    3  LB 8 VAL L  96  SER L 106 -1  N  LEU L  97   O  ILE L  88           
SHEET    4  LB 8 HIS L 191  LYS L 200 -1  O  LYS L 192   N  GLU L 105           
SHEET    5  LB 8 SER L 178  ARG L 182 -1  O  GLU L 179   N  TYR L 199           
SHEET    6  LB 8 HIS L 191  LYS L 200 -1  O  VAL L 197   N  VAL L 181           
SHEET    7  LB 8 PHE L 186  THR L 187 -1  O  PHE L 186   N  VAL L 193           
SHEET    8  LB 8 HIS L 191  LYS L 200 -1  O  VAL L 193   N  PHE L 186           
LINK        MG    MG A1206                 OD1 ASP D 205     1555   2756  2.08  
LINK        MG    MG A1206                 O   HOH A2139     1555   1555  2.14  
LINK        MG    MG A1206                 O   HOH A2143     1555   1555  2.02  
LINK        MG    MG A1206                 O   HOH A2144     1555   1555  2.07  
LINK        MG    MG A1206                 OD1 ASP A 205     1555   1555  1.98  
LINK        MG    MG B1206                 O   HOH B2130     1555   1555  2.60  
LINK        MG    MG B1206                 OD2 ASP B 205     1555   1555  2.11  
LINK        MG    MG B1206                 O   HOH B2126     1555   1555  2.60  
LINK        MG    MG B1206                 O   HOH B2126     1555   2656  2.23  
LINK        MG    MG B1206                 O   HOH B2130     1555   2656  2.23  
LINK        MG    MG B1206                 OD2 ASP B 205     1555   2656  2.23  
LINK        MG    MG C1206                 OD1 ASP I 205     1555   2755  2.03  
LINK        MG    MG C1206                 O   HOH C2119     1555   1555  1.90  
LINK        MG    MG C1206                 O   HOH I2137     1555   2755  2.01  
LINK        MG    MG C1206                 O   HOH I2133     1555   2755  2.07  
LINK        MG    MG C1206                 OD2 ASP C 205     1555   1555  2.03  
LINK        MG    MG E1206                 O   HOH E2131     1555   1555  2.06  
LINK        MG    MG E1206                 O   HOH E2129     1555   1555  2.08  
LINK        MG    MG E1206                 O   HOH H2118     1555   2656  1.90  
LINK        MG    MG E1206                 OD2 ASP E 205     1555   1555  2.05  
LINK        MG    MG E1206                 OD1 ASP H 205     1555   2656  2.11  
LINK        MG    MG E1206                 O   HOH H2117     1555   2656  2.36  
LINK        MG    MG F1206                 OD1 ASP F 205     1555   1555  2.06  
LINK        MG    MG F1206                 O   HOH F2126     1555   1555  2.10  
LINK        MG    MG F1206                 OD1 ASP J 205     1555   2655  2.09  
LINK        MG    MG F1206                 O   HOH F2129     1555   1555  2.03  
LINK        MG    MG F1206                 O   HOH F2130     1555   1555  1.95  
LINK        MG    MG G1206                 O   HOH G2129     1555   2756  2.35  
LINK        MG    MG G1206                 OD2 ASP G 205     1555   1555  1.90  
LINK        MG    MG G1206                 O   HOH G2125     1555   1555  2.11  
LINK        MG    MG G1206                 O   HOH G2125     1555   2756  2.15  
LINK        MG    MG G1206                 O   HOH G2129     1555   1555  2.35  
LINK        MG    MG G1206                 O   HOH G2130     1555   1555  2.20  
LINK        MG    MG G1206                 O   HOH G2130     1555   2756  2.06  
LINK        MG    MG G1206                 OD2 ASP G 205     1555   2756  2.17  
LINK        MG    MG K1206                 O   HOH K2134     1555   1555  2.08  
LINK        MG    MG K1206                 O   HOH K2134     1555   2655  2.08  
LINK        MG    MG K1206                 O   HOH K2138     1555   1555  2.26  
LINK        MG    MG K1206                 O   HOH K2138     1555   2655  2.27  
LINK        MG    MG K1206                 O   HOH K2139     1555   1555  2.03  
LINK        MG    MG K1206                 O   HOH K2139     1555   2655  2.00  
LINK        MG    MG K1206                 OD2 ASP K 205     1555   2655  2.01  
LINK        MG    MG K1206                 OD2 ASP K 205     1555   1555  1.99  
LINK        MG    MG L1206                 O   HOH L2121     1555   2755  2.18  
LINK        MG    MG L1206                 O   HOH L2125     1555   2755  2.10  
LINK        MG    MG L1206                 OD2 ASP L 205     1555   1555  1.98  
LINK        MG    MG L1206                 O   HOH L2121     1555   1555  2.25  
LINK        MG    MG L1206                 O   HOH L2127     1555   1555  1.78  
LINK        MG    MG L1206                 O   HOH L2127     1555   2755  2.75  
LINK        MG    MG L1206                 O   HOH L2125     1555   1555  2.29  
LINK        MG    MG L1206                 OD2 ASP L 205     1555   2755  2.13  
SITE     1 AC1  5 ASP A 205  HOH A2139  HOH A2143  HOH A2144                    
SITE     2 AC1  5 ASP D 205                                                     
SITE     1 AC2  3 ASP B 205  HOH B2126  HOH B2130                               
SITE     1 AC3  5 ASP C 205  HOH C2119  ASP I 205  HOH I2133                    
SITE     2 AC3  5 HOH I2137                                                     
SITE     1 AC4  6 ASP E 205  HOH E2129  HOH E2131  ASP H 205                    
SITE     2 AC4  6 HOH H2117  HOH H2118                                          
SITE     1 AC5  5 ASP F 205  HOH F2126  HOH F2129  HOH F2130                    
SITE     2 AC5  5 ASP J 205                                                     
SITE     1 AC6  4 ASP G 205  HOH G2125  HOH G2129  HOH G2130                    
SITE     1 AC7  4 ASP K 205  HOH K2134  HOH K2138  HOH K2139                    
SITE     1 AC8  4 ASP L 205  HOH L2121  HOH L2125  HOH L2127                    
SITE     1 AC9  5 ARG E  99  PHE E 174  ILE E 175  LYS H 192                    
SITE     2 AC9  5 HOH H2061                                                     
SITE     1 BC1  4 ARG B  99  ILE B 175  LYS E 192  HOH E2069                    
SITE     1 BC2  5 LYS I 192  HOH I2073  ARG L  99  PHE L 174                    
SITE     2 BC2  5 ILE L 175                                                     
SITE     1 BC3  4 LYS J 192  HOH J2074  ARG K  99  ILE K 175                    
SITE     1 BC4  5 LYS D 192  HOH D2077  ARG G  99  PHE G 174                    
SITE     2 BC4  5 ILE G 175                                                     
SITE     1 BC5  4 LYS C 192  ARG I  99  PHE I 174  ILE I 175                    
SITE     1 BC6  3 ARG A  99  ILE A 175  LYS G 192                               
SITE     1 BC7  5 LYS F 192  HOH F2066  ARG J  99  PHE J 174                    
SITE     2 BC7  5 ILE J 175                                                     
SITE     1 BC8  4 ARG F  99  ILE F 175  LYS K 192  HOH K2076                    
SITE     1 BC9  5 LYS A 192  HOH A2077  ARG D  99  PHE D 174                    
SITE     2 BC9  5 ILE D 175                                                     
SITE     1 CC1  5 LYS B 192  HOH B2074  ARG H  99  PHE H 174                    
SITE     2 CC1  5 ILE H 175                                                     
SITE     1 CC2  3 SER A 178  SER G 185  LYS G 192                               
SITE     1 CC3  5 ARG C  99  PHE C 174  ILE C 175  LYS L 192                    
SITE     2 CC3  5 HOH L2069                                                     
SITE     1 CC4  2 ALA C 137  HOH C2079                                          
SITE     1 CC5  3 SER E 178  SER H 185  LYS H 192                               
SITE     1 CC6  4 SER A 185  LYS A 192  HOH A2131  SER D 178                    
SITE     1 CC7  3 SER F 185  LYS F 192  SER J 178                               
SITE     1 CC8  5 ARG B 182  SER B 185  LYS B 192  SER H 178                    
SITE     2 CC8  5 HOH H2095                                                     
SITE     1 CC9  3 SER F 178  SER K 185  LYS K 192                               
SITE     1 DC1  3 SER D 185  LYS D 192  SER G 178                               
SITE     1 DC2  3 SER I 185  LYS I 192  SER L 178                               
SITE     1 DC3  3 SER C 178  SER L 185  LYS L 192                               
SITE     1 DC4  3 SER C 185  LYS C 192  SER I 178                               
SITE     1 DC5  3 SER J 185  LYS J 192  SER K 178                               
SITE     1 DC6  3 SER B 178  SER E 185  LYS E 192                               
SITE     1 DC7  3 ARG C  99  GLN C 101  HOH C2059                               
SITE     1 DC8  4 ALA I 137  HOH I2038  HOH I2092  ALA L 137                    
SITE     1 DC9  2 ALA E 137  HOH E2090                                          
SITE     1 EC1  1 SER E  40                                                     
SITE     1 EC2  2 ALA D 137  HOH D2037                                          
SITE     1 EC3  2 ALA J 137  HOH K2093                                          
SITE     1 EC4  6 TYR L  33  GLN L  34  GLY L  36  LEU L 145                    
SITE     2 EC4  6 VAL L 147  HOH L2128                                          
SITE     1 EC5  5 GLN C  34  LEU C 145  VAL C 147  HOH C2120                    
SITE     2 EC5  5 HOH C2121                                                     
SITE     1 EC6  5 TYR F  33  ARG F  35  GLY F  36  LEU F 145                    
SITE     2 EC6  5 HOH F2131                                                     
SITE     1 EC7  5 GLN H  34  ARG H  35  GLY H  36  LEU H 145                    
SITE     2 EC7  5 VAL H 147                                                     
SITE     1 EC8  2 GLN G  34  LEU G 145                                          
SITE     1 EC9  6 GLN B  34  ARG B  35  LEU B 145  VAL B 147                    
SITE     2 EC9  6 HOH B2020  HOH B2132                                          
SITE     1 FC1  4 TYR I  33  GLN I  34  ARG I  35  LEU I 145                    
SITE     1 FC2  4 TYR K  33  GLN K  34  GLY K  36  LEU K 145                    
SITE     1 FC3  7 GLN A  34  ARG A  35  GLY A  36  LEU A 145                    
SITE     2 FC3  7 VAL A 147  SER A 148  HOH A2145                               
SITE     1 FC4  4 TYR E  33  GLY E  36  LEU E 145  HOH E2018                    
CRYST1  109.337  191.407  154.307  90.00  90.02  90.00 C 1 2 1      48          
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      0.009146  0.000000  0.000003        0.00000                         
SCALE2      0.000000  0.005224  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006481        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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