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Database: PDB
Entry: 3CMM
LinkDB: 3CMM
Original site: 3CMM 
HEADER    LIGASE/PROTEIN BINDING                  23-MAR-08   3CMM              
TITLE     CRYSTAL STRUCTURE OF THE UBA1-UBIQUITIN COMPLEX                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-ACTIVATING ENZYME E1 1;                          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: RESIDUES 10-1024;                                          
COMPND   5 EC: 6.3.2.19;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: UBIQUITIN;                                                 
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 GENE: UBA1;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21 ROSETTA;                              
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  11 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  12 GENE: UBI1, RPL40A;                                                  
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PTXB1                                     
KEYWDS    UBIQUITIN, E1, UBA1, PROTEIN TURNOVER, LIGASE, CONFORMATIONAL CHANGE, 
KEYWDS   2 THIOESTER, ADENYLATION, TRANSTHIOESTERIFICATION, ATP-BINDING,        
KEYWDS   3 NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, UBL CONJUGATION         
KEYWDS   4 PATHWAY, DNA DAMAGE, DNA REPAIR, LIGASE-PROTEIN BINDING COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.LEE,H.SCHINDELIN                                                    
REVDAT   5   25-OCT-17 3CMM    1       REMARK                                   
REVDAT   4   13-JUL-11 3CMM    1       VERSN                                    
REVDAT   3   27-OCT-09 3CMM    1       JRNL                                     
REVDAT   2   24-FEB-09 3CMM    1       VERSN                                    
REVDAT   1   05-AUG-08 3CMM    0                                                
JRNL        AUTH   I.LEE,H.SCHINDELIN                                           
JRNL        TITL   STRUCTURAL INSIGHTS INTO E1-CATALYZED UBIQUITIN ACTIVATION   
JRNL        TITL 2 AND TRANSFER TO CONJUGATING ENZYMES.                         
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 134   268 2008              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   18662542                                                     
JRNL        DOI    10.1016/J.CELL.2008.05.046                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 73486                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3899                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4539                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.12                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2860                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 229                          
REMARK   3   BIN FREE R VALUE                    : 0.4060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 17051                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 176                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.35000                                              
REMARK   3    B22 (A**2) : 0.74000                                              
REMARK   3    B33 (A**2) : -1.09000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.029         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.330         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.248         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.795        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 17403 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 23536 ; 1.366 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2152 ; 6.289 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   825 ;38.155 ;25.394       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3100 ;19.808 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    74 ;21.119 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2639 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 13144 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  7770 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 11833 ; 0.311 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   601 ; 0.141 ; 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):    44 ; 0.213 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.116 ; 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): 10973 ; 0.413 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17451 ; 0.737 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7042 ; 1.228 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6085 ; 2.084 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     14       A     905      5                      
REMARK   3           1     C     14       C     905      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3512 ;  0.50 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):   3408 ;  0.70 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3512 ;  0.44 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):   3408 ;  1.05 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      1       B      76      5                      
REMARK   3           1     D      1       D      76      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    B    (A):    304 ;  0.20 ;  0.50           
REMARK   3   LOOSE POSITIONAL   2    B    (A):    297 ;  0.47 ;  5.00           
REMARK   3   MEDIUM THERMAL     2    B (A**2):    304 ;  0.38 ;  2.00           
REMARK   3   LOOSE THERMAL      2    B (A**2):    297 ;  0.96 ; 10.00           
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 : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    12        A   177                          
REMARK   3    RESIDUE RANGE :   A   263        A   426                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2000  12.3340 -29.8820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0982 T22:  -0.1361                                     
REMARK   3      T33:  -0.1755 T12:  -0.0396                                     
REMARK   3      T13:  -0.0040 T23:  -0.0535                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8182 L22:   1.1996                                     
REMARK   3      L33:   1.4485 L12:   0.2077                                     
REMARK   3      L13:  -0.0925 L23:  -0.3631                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0873 S12:  -0.3700 S13:   0.0969                       
REMARK   3      S21:   0.1637 S22:  -0.0512 S23:   0.0182                       
REMARK   3      S31:  -0.2202 S32:   0.0187 S33:  -0.0361                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   178        A   262                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.7680  -7.4280 -52.8140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0957 T22:  -0.1525                                     
REMARK   3      T33:  -0.0542 T12:  -0.0016                                     
REMARK   3      T13:  -0.0411 T23:  -0.0778                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8331 L22:   5.5023                                     
REMARK   3      L33:   6.3209 L12:   0.6772                                     
REMARK   3      L13:   1.1285 L23:   1.0519                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0995 S12:   0.3379 S13:  -0.6377                       
REMARK   3      S21:   0.0012 S22:   0.0472 S23:   0.0881                       
REMARK   3      S31:   0.4092 S32:   0.0124 S33:  -0.1467                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   427        A   596                          
REMARK   3    RESIDUE RANGE :   A   862        A   916                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.9730  16.1720 -54.3210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0848 T22:  -0.0806                                     
REMARK   3      T33:  -0.1381 T12:  -0.0329                                     
REMARK   3      T13:  -0.0254 T23:   0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6615 L22:   1.8641                                     
REMARK   3      L33:   1.6196 L12:   0.5036                                     
REMARK   3      L13:  -0.4673 L23:  -0.3541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0040 S12:   0.4991 S13:   0.1271                       
REMARK   3      S21:  -0.2453 S22:   0.0318 S23:   0.1219                       
REMARK   3      S31:  -0.1867 S32:   0.1081 S33:  -0.0277                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   597        A   860                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.4660  19.3370 -76.4510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0853 T22:   0.0768                                     
REMARK   3      T33:  -0.1763 T12:  -0.0212                                     
REMARK   3      T13:   0.0294 T23:  -0.0255                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6626 L22:   6.3927                                     
REMARK   3      L33:   2.0500 L12:   0.6584                                     
REMARK   3      L13:   0.1593 L23:  -1.0001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0782 S12:   0.4499 S13:   0.0695                       
REMARK   3      S21:  -0.6860 S22:   0.1025 S23:  -0.4454                       
REMARK   3      S31:  -0.0193 S32:   0.1545 S33:  -0.0243                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   920        A  1024                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.7080   4.8900 -83.2320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0486 T22:   0.5260                                     
REMARK   3      T33:   0.0062 T12:  -0.0558                                     
REMARK   3      T13:   0.0651 T23:  -0.2128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7285 L22:   3.6417                                     
REMARK   3      L33:   8.4079 L12:   2.3229                                     
REMARK   3      L13:  -0.5106 L23:   0.3507                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1914 S12:   0.7176 S13:  -0.1348                       
REMARK   3      S21:  -0.6869 S22:   0.5592 S23:  -0.5954                       
REMARK   3      S31:  -0.2375 S32:   0.7536 S33:  -0.3678                       
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 :   B     1        B    76                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.2340 -10.8330 -53.0380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0291 T22:  -0.0388                                     
REMARK   3      T33:   0.2522 T12:  -0.0170                                     
REMARK   3      T13:  -0.0325 T23:  -0.1928                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2633 L22:  10.6417                                     
REMARK   3      L33:   2.1361 L12:   0.0428                                     
REMARK   3      L13:   0.9795 L23:   1.2129                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2359 S12:   0.7776 S13:  -1.5325                       
REMARK   3      S21:  -0.2924 S22:   0.0396 S23:   0.1041                       
REMARK   3      S31:   0.3420 S32:   0.0520 S33:  -0.2756                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    12        C   177                          
REMARK   3    RESIDUE RANGE :   C   263        C   426                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.5030  24.1020 -44.4420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0506 T22:  -0.1351                                     
REMARK   3      T33:  -0.1940 T12:  -0.0302                                     
REMARK   3      T13:   0.0073 T23:   0.0119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5352 L22:   1.1354                                     
REMARK   3      L33:   1.2875 L12:  -0.2628                                     
REMARK   3      L13:  -0.2925 L23:  -0.1209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0712 S12:   0.3084 S13:   0.1156                       
REMARK   3      S21:  -0.1311 S22:  -0.0525 S23:  -0.0331                       
REMARK   3      S31:  -0.1394 S32:   0.0473 S33:  -0.0187                       
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 :   C   178        C   262                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1820 -11.0380 -29.4480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0276 T22:  -0.1654                                     
REMARK   3      T33:  -0.0120 T12:  -0.0151                                     
REMARK   3      T13:  -0.0086 T23:   0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7969 L22:   5.4484                                     
REMARK   3      L33:   6.4501 L12:  -0.1744                                     
REMARK   3      L13:   0.8286 L23:  -0.7785                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0981 S12:  -0.1795 S13:  -0.5480                       
REMARK   3      S21:   0.0120 S22:   0.1224 S23:  -0.0417                       
REMARK   3      S31:   0.6147 S32:  -0.0362 S33:  -0.2205                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   427        C   596                          
REMARK   3    RESIDUE RANGE :   C   862        C   916                          
REMARK   3    ORIGIN FOR THE GROUP (A): -50.4580  21.7010 -19.9110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0222 T22:  -0.0783                                     
REMARK   3      T33:  -0.1848 T12:  -0.0377                                     
REMARK   3      T13:   0.0065 T23:  -0.0163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8456 L22:   1.8641                                     
REMARK   3      L33:   1.4796 L12:  -0.1228                                     
REMARK   3      L13:  -0.5695 L23:   0.0653                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0137 S12:  -0.3401 S13:   0.0215                       
REMARK   3      S21:   0.3935 S22:  -0.0049 S23:  -0.0066                       
REMARK   3      S31:  -0.1567 S32:  -0.0263 S33:  -0.0087                       
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 :   C   920        C  1024                          
REMARK   3    ORIGIN FOR THE GROUP (A): -71.4660   6.4130   3.3340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0758 T22:   0.3045                                     
REMARK   3      T33:   0.0511 T12:  -0.0518                                     
REMARK   3      T13:   0.0806 T23:   0.0664                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3395 L22:   2.0797                                     
REMARK   3      L33:   8.8103 L12:  -0.3794                                     
REMARK   3      L13:  -3.2574 L23:  -2.4090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2210 S12:  -0.3639 S13:   0.2722                       
REMARK   3      S21:   0.3833 S22:   0.2254 S23:   0.0271                       
REMARK   3      S31:  -0.3080 S32:  -0.2373 S33:  -0.4464                       
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 :   C   597        C   860                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.7170   7.2710   0.9560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0127 T22:   0.0044                                     
REMARK   3      T33:  -0.1913 T12:   0.0001                                     
REMARK   3      T13:  -0.0256 T23:   0.0527                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4266 L22:   2.5174                                     
REMARK   3      L33:   3.2570 L12:  -0.5651                                     
REMARK   3      L13:  -0.1506 L23:   0.8610                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0906 S12:  -0.3527 S13:  -0.1396                       
REMARK   3      S21:   0.4878 S22:   0.1633 S23:   0.0163                       
REMARK   3      S31:   0.0983 S32:   0.0613 S33:  -0.0727                       
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 :   D     1        D    76                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.5940  -5.3990 -29.8290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0026 T22:  -0.0820                                     
REMARK   3      T33:   0.0675 T12:  -0.0671                                     
REMARK   3      T13:   0.0146 T23:  -0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8457 L22:   6.3775                                     
REMARK   3      L33:   2.4430 L12:  -0.3126                                     
REMARK   3      L13:   0.5941 L23:  -0.1237                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0056 S12:  -0.0303 S13:  -0.9605                       
REMARK   3      S21:  -0.1580 S22:   0.0668 S23:   0.1511                       
REMARK   3      S31:   0.4265 S32:  -0.0650 S33:  -0.0611                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3CMM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000046958.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-APR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77706                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.11500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: L-PROLINE, PEG 5000 MME, PH 7.6, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       57.68150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      103.78350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.28200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      103.78350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       57.68150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.28200            
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                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 47550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.6 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 47040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ALA A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     GLN A   647                                                      
REMARK 465     SER A   648                                                      
REMARK 465     GLY A   649                                                      
REMARK 465     ASN A   788                                                      
REMARK 465     ALA A   789                                                      
REMARK 465     ASN A   790                                                      
REMARK 465     ALA A   791                                                      
REMARK 465     ALA A   792                                                      
REMARK 465     ASN A   793                                                      
REMARK 465     GLY A   794                                                      
REMARK 465     SER A   795                                                      
REMARK 465     ASP A   796                                                      
REMARK 465     ALA C    10                                                      
REMARK 465     ASP C   786                                                      
REMARK 465     PRO C   787                                                      
REMARK 465     ASN C   788                                                      
REMARK 465     ALA C   789                                                      
REMARK 465     ASN C   790                                                      
REMARK 465     ALA C   791                                                      
REMARK 465     ALA C   792                                                      
REMARK 465     ASN C   793                                                      
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   NE2  GLN C   272     O    PRO C   276              2.13            
REMARK 500   O    GLU C   797     N    ASP C   799              2.17            
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    GLN A 637   CD    GLN A 637   OE1     0.170                       
REMARK 500    LYS A 646   C     LYS A 646   O       0.127                       
REMARK 500    LYS C 922   CG    LYS C 922   CD      0.228                       
REMARK 500    LYS C 922   CD    LYS C 922   CE      0.170                       
REMARK 500    GLU B  16   CD    GLU B  16   OE1     0.173                       
REMARK 500    GLU B  16   CD    GLU B  16   OE2     0.150                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 299   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500    LEU A 872   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    PRO A 995   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    LEU C 369   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    LEU C 872   CA  -  CB  -  CG  ANGL. DEV. =  14.3 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    ILE A  14       95.12     73.62                                   
REMARK 500    SER A  20      -78.60    -22.51                                   
REMARK 500    ASP A  67       90.29   -163.24                                   
REMARK 500    LEU A  76        1.57    -66.04                                   
REMARK 500    THR A  78       -4.72   -140.46                                   
REMARK 500    ASN A 103       98.52   -161.37                                   
REMARK 500    ASP A 116      167.01    170.88                                   
REMARK 500    ASP A 199      105.49    -21.09                                   
REMARK 500    ASP A 200      -33.10     95.24                                   
REMARK 500    LYS A 244      -33.96    -39.03                                   
REMARK 500    PHE A 382      167.33     80.70                                   
REMARK 500    GLN A 387      -75.79    102.61                                   
REMARK 500    ASN A 414       62.83     69.95                                   
REMARK 500    TYR A 465      168.80    178.76                                   
REMARK 500    ASP A 470      127.46   -174.04                                   
REMARK 500    GLN A 482       76.84   -112.33                                   
REMARK 500    PHE A 528       69.86   -100.20                                   
REMARK 500    LEU A 582      -55.37   -137.48                                   
REMARK 500    SER A 604      -30.63   -130.45                                   
REMARK 500    ASN A 607       13.07   -149.64                                   
REMARK 500    VAL A 651      -57.25   -129.90                                   
REMARK 500    THR A 701     -160.29    -79.56                                   
REMARK 500    ASN A 703      -60.80     85.94                                   
REMARK 500    VAL A 802      -75.75    -72.57                                   
REMARK 500    SER A 803       32.58    -80.32                                   
REMARK 500    PRO A 806       41.21    -82.75                                   
REMARK 500    ASP A 807      125.63     59.40                                   
REMARK 500    HIS A 829       -3.97     76.59                                   
REMARK 500    ASP A 936       40.53    -93.72                                   
REMARK 500    ILE A 937      138.31    -13.82                                   
REMARK 500    LYS A 991      -37.81    -36.56                                   
REMARK 500    ALA A 996      -50.38     94.97                                   
REMARK 500    PRO A1018      159.17    -48.96                                   
REMARK 500    ASP C  15       94.34    -65.00                                   
REMARK 500    SER C  20      -73.48    -20.32                                   
REMARK 500    LYS C  45     -169.77    -68.61                                   
REMARK 500    ASN C 103       98.42   -160.62                                   
REMARK 500    ASP C 130       -0.78    -59.99                                   
REMARK 500    ASP C 199     -106.90     28.44                                   
REMARK 500    ASP C 224      -39.93     -9.53                                   
REMARK 500    PRO C 235      -34.63    -38.86                                   
REMARK 500    LYS C 250      -65.74   -121.39                                   
REMARK 500    GLU C 277      104.67     69.35                                   
REMARK 500    PHE C 382      163.09     78.53                                   
REMARK 500    GLN C 387      -77.57    113.39                                   
REMARK 500    GLN C 482       75.21   -113.14                                   
REMARK 500    PHE C 528       73.59   -101.11                                   
REMARK 500    ARG C 560       56.88     29.31                                   
REMARK 500    LEU C 582      -53.33   -125.32                                   
REMARK 500    ASN C 607       10.75   -144.70                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      68 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS C  386     GLN C  387                  146.55                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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     PRO A 5119                                                       
REMARK 610     PRO C 5129                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PRO A 5119                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PRO C 5129                
DBREF  3CMM A   10  1024  UNP    P22515   UBA1_YEAST      10   1024             
DBREF  3CMM C   10  1024  UNP    P22515   UBA1_YEAST      10   1024             
DBREF  3CMM B    1    76  UNP    P61864   UBIQ_YEAST       1     76             
DBREF  3CMM D    1    76  UNP    P61864   UBIQ_YEAST       1     76             
SEQRES   1 A 1015  ALA ALA GLY GLU ILE ASP GLU SER LEU TYR SER ARG GLN          
SEQRES   2 A 1015  LEU TYR VAL LEU GLY LYS GLU ALA MET LEU LYS MET GLN          
SEQRES   3 A 1015  THR SER ASN VAL LEU ILE LEU GLY LEU LYS GLY LEU GLY          
SEQRES   4 A 1015  VAL GLU ILE ALA LYS ASN VAL VAL LEU ALA GLY VAL LYS          
SEQRES   5 A 1015  SER MET THR VAL PHE ASP PRO GLU PRO VAL GLN LEU ALA          
SEQRES   6 A 1015  ASP LEU SER THR GLN PHE PHE LEU THR GLU LYS ASP ILE          
SEQRES   7 A 1015  GLY GLN LYS ARG GLY ASP VAL THR ARG ALA LYS LEU ALA          
SEQRES   8 A 1015  GLU LEU ASN ALA TYR VAL PRO VAL ASN VAL LEU ASP SER          
SEQRES   9 A 1015  LEU ASP ASP VAL THR GLN LEU SER GLN PHE GLN VAL VAL          
SEQRES  10 A 1015  VAL ALA THR ASP THR VAL SER LEU GLU ASP LYS VAL LYS          
SEQRES  11 A 1015  ILE ASN GLU PHE CYS HIS SER SER GLY ILE ARG PHE ILE          
SEQRES  12 A 1015  SER SER GLU THR ARG GLY LEU PHE GLY ASN THR PHE VAL          
SEQRES  13 A 1015  ASP LEU GLY ASP GLU PHE THR VAL LEU ASP PRO THR GLY          
SEQRES  14 A 1015  GLU GLU PRO ARG THR GLY MET VAL SER ASP ILE GLU PRO          
SEQRES  15 A 1015  ASP GLY THR VAL THR MET LEU ASP ASP ASN ARG HIS GLY          
SEQRES  16 A 1015  LEU GLU ASP GLY ASN PHE VAL ARG PHE SER GLU VAL GLU          
SEQRES  17 A 1015  GLY LEU ASP LYS LEU ASN ASP GLY THR LEU PHE LYS VAL          
SEQRES  18 A 1015  GLU VAL LEU GLY PRO PHE ALA PHE ARG ILE GLY SER VAL          
SEQRES  19 A 1015  LYS GLU TYR GLY GLU TYR LYS LYS GLY GLY ILE PHE THR          
SEQRES  20 A 1015  GLU VAL LYS VAL PRO ARG LYS ILE SER PHE LYS SER LEU          
SEQRES  21 A 1015  LYS GLN GLN LEU SER ASN PRO GLU PHE VAL PHE SER ASP          
SEQRES  22 A 1015  PHE ALA LYS PHE ASP ARG ALA ALA GLN LEU HIS LEU GLY          
SEQRES  23 A 1015  PHE GLN ALA LEU HIS GLN PHE ALA VAL ARG HIS ASN GLY          
SEQRES  24 A 1015  GLU LEU PRO ARG THR MET ASN ASP GLU ASP ALA ASN GLU          
SEQRES  25 A 1015  LEU ILE LYS LEU VAL THR ASP LEU SER VAL GLN GLN PRO          
SEQRES  26 A 1015  GLU VAL LEU GLY GLU GLY VAL ASP VAL ASN GLU ASP LEU          
SEQRES  27 A 1015  ILE LYS GLU LEU SER TYR GLN ALA ARG GLY ASP ILE PRO          
SEQRES  28 A 1015  GLY VAL VAL ALA PHE PHE GLY GLY LEU VAL ALA GLN GLU          
SEQRES  29 A 1015  VAL LEU LYS ALA CYS SER GLY LYS PHE THR PRO LEU LYS          
SEQRES  30 A 1015  GLN PHE MET TYR PHE ASP SER LEU GLU SER LEU PRO ASP          
SEQRES  31 A 1015  PRO LYS ASN PHE PRO ARG ASN GLU LYS THR THR GLN PRO          
SEQRES  32 A 1015  VAL ASN SER ARG TYR ASP ASN GLN ILE ALA VAL PHE GLY          
SEQRES  33 A 1015  LEU ASP PHE GLN LYS LYS ILE ALA ASN SER LYS VAL PHE          
SEQRES  34 A 1015  LEU VAL GLY SER GLY ALA ILE GLY CYS GLU MET LEU LYS          
SEQRES  35 A 1015  ASN TRP ALA LEU LEU GLY LEU GLY SER GLY SER ASP GLY          
SEQRES  36 A 1015  TYR ILE VAL VAL THR ASP ASN ASP SER ILE GLU LYS SER          
SEQRES  37 A 1015  ASN LEU ASN ARG GLN PHE LEU PHE ARG PRO LYS ASP VAL          
SEQRES  38 A 1015  GLY LYS ASN LYS SER GLU VAL ALA ALA GLU ALA VAL CYS          
SEQRES  39 A 1015  ALA MET ASN PRO ASP LEU LYS GLY LYS ILE ASN ALA LYS          
SEQRES  40 A 1015  ILE ASP LYS VAL GLY PRO GLU THR GLU GLU ILE PHE ASN          
SEQRES  41 A 1015  ASP SER PHE TRP GLU SER LEU ASP PHE VAL THR ASN ALA          
SEQRES  42 A 1015  LEU ASP ASN VAL ASP ALA ARG THR TYR VAL ASP ARG ARG          
SEQRES  43 A 1015  CYS VAL PHE TYR ARG LYS PRO LEU LEU GLU SER GLY THR          
SEQRES  44 A 1015  LEU GLY THR LYS GLY ASN THR GLN VAL ILE ILE PRO ARG          
SEQRES  45 A 1015  LEU THR GLU SER TYR SER SER SER ARG ASP PRO PRO GLU          
SEQRES  46 A 1015  LYS SER ILE PRO LEU CYS THR LEU ARG SER PHE PRO ASN          
SEQRES  47 A 1015  LYS ILE ASP HIS THR ILE ALA TRP ALA LYS SER LEU PHE          
SEQRES  48 A 1015  GLN GLY TYR PHE THR ASP SER ALA GLU ASN VAL ASN MET          
SEQRES  49 A 1015  TYR LEU THR GLN PRO ASN PHE VAL GLU GLN THR LEU LYS          
SEQRES  50 A 1015  GLN SER GLY ASP VAL LYS GLY VAL LEU GLU SER ILE SER          
SEQRES  51 A 1015  ASP SER LEU SER SER LYS PRO HIS ASN PHE GLU ASP CYS          
SEQRES  52 A 1015  ILE LYS TRP ALA ARG LEU GLU PHE GLU LYS LYS PHE ASN          
SEQRES  53 A 1015  HIS ASP ILE LYS GLN LEU LEU PHE ASN PHE PRO LYS ASP          
SEQRES  54 A 1015  ALA LYS THR SER ASN GLY GLU PRO PHE TRP SER GLY ALA          
SEQRES  55 A 1015  LYS ARG ALA PRO THR PRO LEU GLU PHE ASP ILE TYR ASN          
SEQRES  56 A 1015  ASN ASP HIS PHE HIS PHE VAL VAL ALA GLY ALA SER LEU          
SEQRES  57 A 1015  ARG ALA TYR ASN TYR GLY ILE LYS SER ASP ASP SER ASN          
SEQRES  58 A 1015  SER LYS PRO ASN VAL ASP GLU TYR LYS SER VAL ILE ASP          
SEQRES  59 A 1015  HIS MET ILE ILE PRO GLU PHE THR PRO ASN ALA ASN LEU          
SEQRES  60 A 1015  LYS ILE GLN VAL ASN ASP ASP ASP PRO ASP PRO ASN ALA          
SEQRES  61 A 1015  ASN ALA ALA ASN GLY SER ASP GLU ILE ASP GLN LEU VAL          
SEQRES  62 A 1015  SER SER LEU PRO ASP PRO SER THR LEU ALA GLY PHE LYS          
SEQRES  63 A 1015  LEU GLU PRO VAL ASP PHE GLU LYS ASP ASP ASP THR ASN          
SEQRES  64 A 1015  HIS HIS ILE GLU PHE ILE THR ALA CYS SER ASN CYS ARG          
SEQRES  65 A 1015  ALA GLN ASN TYR PHE ILE GLU THR ALA ASP ARG GLN LYS          
SEQRES  66 A 1015  THR LYS PHE ILE ALA GLY ARG ILE ILE PRO ALA ILE ALA          
SEQRES  67 A 1015  THR THR THR SER LEU VAL THR GLY LEU VAL ASN LEU GLU          
SEQRES  68 A 1015  LEU TYR LYS LEU ILE ASP ASN LYS THR ASP ILE GLU GLN          
SEQRES  69 A 1015  TYR LYS ASN GLY PHE VAL ASN LEU ALA LEU PRO PHE PHE          
SEQRES  70 A 1015  GLY PHE SER GLU PRO ILE ALA SER PRO LYS GLY GLU TYR          
SEQRES  71 A 1015  ASN ASN LYS LYS TYR ASP LYS ILE TRP ASP ARG PHE ASP          
SEQRES  72 A 1015  ILE LYS GLY ASP ILE LYS LEU SER ASP LEU ILE GLU HIS          
SEQRES  73 A 1015  PHE GLU LYS ASP GLU GLY LEU GLU ILE THR MET LEU SER          
SEQRES  74 A 1015  TYR GLY VAL SER LEU LEU TYR ALA SER PHE PHE PRO PRO          
SEQRES  75 A 1015  LYS LYS LEU LYS GLU ARG LEU ASN LEU PRO ILE THR GLN          
SEQRES  76 A 1015  LEU VAL LYS LEU VAL THR LYS LYS ASP ILE PRO ALA HIS          
SEQRES  77 A 1015  VAL SER THR MET ILE LEU GLU ILE CYS ALA ASP ASP LYS          
SEQRES  78 A 1015  GLU GLY GLU ASP VAL GLU VAL PRO PHE ILE THR ILE HIS          
SEQRES  79 A 1015  LEU                                                          
SEQRES   1 C 1015  ALA ALA GLY GLU ILE ASP GLU SER LEU TYR SER ARG GLN          
SEQRES   2 C 1015  LEU TYR VAL LEU GLY LYS GLU ALA MET LEU LYS MET GLN          
SEQRES   3 C 1015  THR SER ASN VAL LEU ILE LEU GLY LEU LYS GLY LEU GLY          
SEQRES   4 C 1015  VAL GLU ILE ALA LYS ASN VAL VAL LEU ALA GLY VAL LYS          
SEQRES   5 C 1015  SER MET THR VAL PHE ASP PRO GLU PRO VAL GLN LEU ALA          
SEQRES   6 C 1015  ASP LEU SER THR GLN PHE PHE LEU THR GLU LYS ASP ILE          
SEQRES   7 C 1015  GLY GLN LYS ARG GLY ASP VAL THR ARG ALA LYS LEU ALA          
SEQRES   8 C 1015  GLU LEU ASN ALA TYR VAL PRO VAL ASN VAL LEU ASP SER          
SEQRES   9 C 1015  LEU ASP ASP VAL THR GLN LEU SER GLN PHE GLN VAL VAL          
SEQRES  10 C 1015  VAL ALA THR ASP THR VAL SER LEU GLU ASP LYS VAL LYS          
SEQRES  11 C 1015  ILE ASN GLU PHE CYS HIS SER SER GLY ILE ARG PHE ILE          
SEQRES  12 C 1015  SER SER GLU THR ARG GLY LEU PHE GLY ASN THR PHE VAL          
SEQRES  13 C 1015  ASP LEU GLY ASP GLU PHE THR VAL LEU ASP PRO THR GLY          
SEQRES  14 C 1015  GLU GLU PRO ARG THR GLY MET VAL SER ASP ILE GLU PRO          
SEQRES  15 C 1015  ASP GLY THR VAL THR MET LEU ASP ASP ASN ARG HIS GLY          
SEQRES  16 C 1015  LEU GLU ASP GLY ASN PHE VAL ARG PHE SER GLU VAL GLU          
SEQRES  17 C 1015  GLY LEU ASP LYS LEU ASN ASP GLY THR LEU PHE LYS VAL          
SEQRES  18 C 1015  GLU VAL LEU GLY PRO PHE ALA PHE ARG ILE GLY SER VAL          
SEQRES  19 C 1015  LYS GLU TYR GLY GLU TYR LYS LYS GLY GLY ILE PHE THR          
SEQRES  20 C 1015  GLU VAL LYS VAL PRO ARG LYS ILE SER PHE LYS SER LEU          
SEQRES  21 C 1015  LYS GLN GLN LEU SER ASN PRO GLU PHE VAL PHE SER ASP          
SEQRES  22 C 1015  PHE ALA LYS PHE ASP ARG ALA ALA GLN LEU HIS LEU GLY          
SEQRES  23 C 1015  PHE GLN ALA LEU HIS GLN PHE ALA VAL ARG HIS ASN GLY          
SEQRES  24 C 1015  GLU LEU PRO ARG THR MET ASN ASP GLU ASP ALA ASN GLU          
SEQRES  25 C 1015  LEU ILE LYS LEU VAL THR ASP LEU SER VAL GLN GLN PRO          
SEQRES  26 C 1015  GLU VAL LEU GLY GLU GLY VAL ASP VAL ASN GLU ASP LEU          
SEQRES  27 C 1015  ILE LYS GLU LEU SER TYR GLN ALA ARG GLY ASP ILE PRO          
SEQRES  28 C 1015  GLY VAL VAL ALA PHE PHE GLY GLY LEU VAL ALA GLN GLU          
SEQRES  29 C 1015  VAL LEU LYS ALA CYS SER GLY LYS PHE THR PRO LEU LYS          
SEQRES  30 C 1015  GLN PHE MET TYR PHE ASP SER LEU GLU SER LEU PRO ASP          
SEQRES  31 C 1015  PRO LYS ASN PHE PRO ARG ASN GLU LYS THR THR GLN PRO          
SEQRES  32 C 1015  VAL ASN SER ARG TYR ASP ASN GLN ILE ALA VAL PHE GLY          
SEQRES  33 C 1015  LEU ASP PHE GLN LYS LYS ILE ALA ASN SER LYS VAL PHE          
SEQRES  34 C 1015  LEU VAL GLY SER GLY ALA ILE GLY CYS GLU MET LEU LYS          
SEQRES  35 C 1015  ASN TRP ALA LEU LEU GLY LEU GLY SER GLY SER ASP GLY          
SEQRES  36 C 1015  TYR ILE VAL VAL THR ASP ASN ASP SER ILE GLU LYS SER          
SEQRES  37 C 1015  ASN LEU ASN ARG GLN PHE LEU PHE ARG PRO LYS ASP VAL          
SEQRES  38 C 1015  GLY LYS ASN LYS SER GLU VAL ALA ALA GLU ALA VAL CYS          
SEQRES  39 C 1015  ALA MET ASN PRO ASP LEU LYS GLY LYS ILE ASN ALA LYS          
SEQRES  40 C 1015  ILE ASP LYS VAL GLY PRO GLU THR GLU GLU ILE PHE ASN          
SEQRES  41 C 1015  ASP SER PHE TRP GLU SER LEU ASP PHE VAL THR ASN ALA          
SEQRES  42 C 1015  LEU ASP ASN VAL ASP ALA ARG THR TYR VAL ASP ARG ARG          
SEQRES  43 C 1015  CYS VAL PHE TYR ARG LYS PRO LEU LEU GLU SER GLY THR          
SEQRES  44 C 1015  LEU GLY THR LYS GLY ASN THR GLN VAL ILE ILE PRO ARG          
SEQRES  45 C 1015  LEU THR GLU SER TYR SER SER SER ARG ASP PRO PRO GLU          
SEQRES  46 C 1015  LYS SER ILE PRO LEU CYS THR LEU ARG SER PHE PRO ASN          
SEQRES  47 C 1015  LYS ILE ASP HIS THR ILE ALA TRP ALA LYS SER LEU PHE          
SEQRES  48 C 1015  GLN GLY TYR PHE THR ASP SER ALA GLU ASN VAL ASN MET          
SEQRES  49 C 1015  TYR LEU THR GLN PRO ASN PHE VAL GLU GLN THR LEU LYS          
SEQRES  50 C 1015  GLN SER GLY ASP VAL LYS GLY VAL LEU GLU SER ILE SER          
SEQRES  51 C 1015  ASP SER LEU SER SER LYS PRO HIS ASN PHE GLU ASP CYS          
SEQRES  52 C 1015  ILE LYS TRP ALA ARG LEU GLU PHE GLU LYS LYS PHE ASN          
SEQRES  53 C 1015  HIS ASP ILE LYS GLN LEU LEU PHE ASN PHE PRO LYS ASP          
SEQRES  54 C 1015  ALA LYS THR SER ASN GLY GLU PRO PHE TRP SER GLY ALA          
SEQRES  55 C 1015  LYS ARG ALA PRO THR PRO LEU GLU PHE ASP ILE TYR ASN          
SEQRES  56 C 1015  ASN ASP HIS PHE HIS PHE VAL VAL ALA GLY ALA SER LEU          
SEQRES  57 C 1015  ARG ALA TYR ASN TYR GLY ILE LYS SER ASP ASP SER ASN          
SEQRES  58 C 1015  SER LYS PRO ASN VAL ASP GLU TYR LYS SER VAL ILE ASP          
SEQRES  59 C 1015  HIS MET ILE ILE PRO GLU PHE THR PRO ASN ALA ASN LEU          
SEQRES  60 C 1015  LYS ILE GLN VAL ASN ASP ASP ASP PRO ASP PRO ASN ALA          
SEQRES  61 C 1015  ASN ALA ALA ASN GLY SER ASP GLU ILE ASP GLN LEU VAL          
SEQRES  62 C 1015  SER SER LEU PRO ASP PRO SER THR LEU ALA GLY PHE LYS          
SEQRES  63 C 1015  LEU GLU PRO VAL ASP PHE GLU LYS ASP ASP ASP THR ASN          
SEQRES  64 C 1015  HIS HIS ILE GLU PHE ILE THR ALA CYS SER ASN CYS ARG          
SEQRES  65 C 1015  ALA GLN ASN TYR PHE ILE GLU THR ALA ASP ARG GLN LYS          
SEQRES  66 C 1015  THR LYS PHE ILE ALA GLY ARG ILE ILE PRO ALA ILE ALA          
SEQRES  67 C 1015  THR THR THR SER LEU VAL THR GLY LEU VAL ASN LEU GLU          
SEQRES  68 C 1015  LEU TYR LYS LEU ILE ASP ASN LYS THR ASP ILE GLU GLN          
SEQRES  69 C 1015  TYR LYS ASN GLY PHE VAL ASN LEU ALA LEU PRO PHE PHE          
SEQRES  70 C 1015  GLY PHE SER GLU PRO ILE ALA SER PRO LYS GLY GLU TYR          
SEQRES  71 C 1015  ASN ASN LYS LYS TYR ASP LYS ILE TRP ASP ARG PHE ASP          
SEQRES  72 C 1015  ILE LYS GLY ASP ILE LYS LEU SER ASP LEU ILE GLU HIS          
SEQRES  73 C 1015  PHE GLU LYS ASP GLU GLY LEU GLU ILE THR MET LEU SER          
SEQRES  74 C 1015  TYR GLY VAL SER LEU LEU TYR ALA SER PHE PHE PRO PRO          
SEQRES  75 C 1015  LYS LYS LEU LYS GLU ARG LEU ASN LEU PRO ILE THR GLN          
SEQRES  76 C 1015  LEU VAL LYS LEU VAL THR LYS LYS ASP ILE PRO ALA HIS          
SEQRES  77 C 1015  VAL SER THR MET ILE LEU GLU ILE CYS ALA ASP ASP LYS          
SEQRES  78 C 1015  GLU GLY GLU ASP VAL GLU VAL PRO PHE ILE THR ILE HIS          
SEQRES  79 C 1015  LEU                                                          
SEQRES   1 B   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 B   76  THR LEU GLU VAL GLU SER SER ASP THR ILE ASP ASN VAL          
SEQRES   3 B   76  LYS SER LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 B   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 B   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 B   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
SEQRES   1 D   76  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 D   76  THR LEU GLU VAL GLU SER SER ASP THR ILE ASP ASN VAL          
SEQRES   3 D   76  LYS SER LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 D   76  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 D   76  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 D   76  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY                  
HET    PRO  A5119       7                                                       
HET    PRO  C5129       7                                                       
HETNAM     PRO PROLINE                                                          
FORMUL   5  PRO    2(C5 H9 N O2)                                                
FORMUL   7  HOH   *176(H2 O)                                                    
HELIX    1   1 ASP A   15  LEU A   26  1                                  12    
HELIX    2   2 GLY A   27  GLN A   35  1                                   9    
HELIX    3   3 LYS A   45  GLY A   59  1                                  15    
HELIX    4   4 GLN A   72  THR A   78  5                                   7    
HELIX    5   5 THR A   83  ILE A   87  5                                   5    
HELIX    6   6 LYS A   90  ALA A  100  1                                  11    
HELIX    7   7 GLN A  119  PHE A  123  5                                   5    
HELIX    8   8 SER A  133  GLY A  148  1                                  16    
HELIX    9   9 LEU A  219  ASP A  224  5                                   6    
HELIX   10  10 SER A  268  ASN A  275  1                                   8    
HELIX   11  11 ASP A  282  PHE A  286  5                                   5    
HELIX   12  12 ASP A  287  HIS A  306  1                                  20    
HELIX   13  13 ASN A  315  GLN A  333  1                                  19    
HELIX   14  14 ASN A  344  GLN A  354  1                                  11    
HELIX   15  15 ILE A  359  GLY A  380  1                                  22    
HELIX   16  16 LEU A  394  LEU A  397  5                                   4    
HELIX   17  17 TYR A  417  GLY A  425  1                                   9    
HELIX   18  18 GLY A  425  ASN A  434  1                                  10    
HELIX   19  19 GLY A  443  GLY A  457  1                                  15    
HELIX   20  20 GLU A  475  LEU A  479  5                                   5    
HELIX   21  21 ARG A  486  VAL A  490  5                                   5    
HELIX   22  22 ASN A  493  ASN A  506  1                                  14    
HELIX   23  23 PRO A  507  LYS A  510  5                                   4    
HELIX   24  24 GLY A  521  GLU A  525  5                                   5    
HELIX   25  25 ASN A  529  LEU A  536  1                                   8    
HELIX   26  26 ASN A  545  ARG A  560  1                                  16    
HELIX   27  27 SER A  585  SER A  589  5                                   5    
HELIX   28  28 PRO A  598  SER A  604  1                                   7    
HELIX   29  29 LYS A  608  THR A  625  1                                  18    
HELIX   30  30 THR A  625  GLN A  637  1                                  13    
HELIX   31  31 ASN A  639  LYS A  646  1                                   8    
HELIX   32  32 VAL A  651  SER A  664  1                                  14    
HELIX   33  33 ASN A  668  ASN A  685  1                                  18    
HELIX   34  34 ASN A  685  PHE A  695  1                                  11    
HELIX   35  35 ASN A  724  GLY A  743  1                                  20    
HELIX   36  36 ASN A  754  ASP A  763  1                                  10    
HELIX   37  37 ILE A  798  SER A  803  1                                   6    
HELIX   38  38 ASP A  807  ALA A  812  5                                   6    
HELIX   39  39 HIS A  829  TYR A  845  1                                  17    
HELIX   40  40 ASP A  851  GLY A  860  1                                  10    
HELIX   41  41 ILE A  866  ASP A  886  1                                  21    
HELIX   42  42 ASP A  890  TYR A  894  5                                   5    
HELIX   43  43 LYS A  938  ASP A  949  1                                  12    
HELIX   44  44 PRO A  970  LEU A  978  1                                   9    
HELIX   45  45 PRO A  981  THR A  990  1                                  10    
HELIX   46  46 ASP C   15  TYR C   24  1                                  10    
HELIX   47  47 GLY C   27  GLN C   35  1                                   9    
HELIX   48  48 LYS C   45  GLY C   59  1                                  15    
HELIX   49  49 GLN C   72  THR C   78  5                                   7    
HELIX   50  50 THR C   83  ILE C   87  5                                   5    
HELIX   51  51 LYS C   90  GLU C  101  1                                  12    
HELIX   52  52 ASP C  116  PHE C  123  5                                   8    
HELIX   53  53 SER C  133  GLY C  148  1                                  16    
HELIX   54  54 LEU C  219  ASP C  224  5                                   6    
HELIX   55  55 SER C  268  ASN C  275  1                                   8    
HELIX   56  56 ASP C  282  PHE C  286  5                                   5    
HELIX   57  57 ASP C  287  HIS C  306  1                                  20    
HELIX   58  58 ASN C  315  GLN C  333  1                                  19    
HELIX   59  59 ASN C  344  GLN C  354  1                                  11    
HELIX   60  60 ILE C  359  GLY C  380  1                                  22    
HELIX   61  61 LEU C  394  LEU C  397  5                                   4    
HELIX   62  62 TYR C  417  GLY C  425  1                                   9    
HELIX   63  63 GLY C  425  ASN C  434  1                                  10    
HELIX   64  64 GLY C  443  GLY C  457  1                                  15    
HELIX   65  65 GLU C  475  LEU C  479  5                                   5    
HELIX   66  66 ARG C  486  VAL C  490  5                                   5    
HELIX   67  67 ASN C  493  ASN C  506  1                                  14    
HELIX   68  68 PRO C  507  LYS C  510  5                                   4    
HELIX   69  69 GLY C  521  GLU C  525  5                                   5    
HELIX   70  70 ASN C  529  LEU C  536  1                                   8    
HELIX   71  71 ASN C  545  TYR C  559  1                                  15    
HELIX   72  72 SER C  585  SER C  589  5                                   5    
HELIX   73  73 PRO C  598  SER C  604  1                                   7    
HELIX   74  74 LYS C  608  THR C  625  1                                  18    
HELIX   75  75 THR C  625  GLN C  637  1                                  13    
HELIX   76  76 ASN C  639  SER C  648  1                                  10    
HELIX   77  77 ASP C  650  SER C  664  1                                  15    
HELIX   78  78 ASN C  668  ASN C  685  1                                  18    
HELIX   79  79 ASN C  685  PHE C  695  1                                  11    
HELIX   80  80 ASN C  724  TYR C  742  1                                  19    
HELIX   81  81 ASP C  748  LYS C  752  5                                   5    
HELIX   82  82 ASN C  754  HIS C  764  1                                  11    
HELIX   83  83 ILE C  798  LEU C  805  1                                   8    
HELIX   84  84 ASP C  807  LEU C  811  5                                   5    
HELIX   85  85 HIS C  829  PHE C  846  1                                  18    
HELIX   86  86 ASP C  851  GLY C  860  1                                  10    
HELIX   87  87 ILE C  866  ASP C  886  1                                  21    
HELIX   88  88 ASP C  890  TYR C  894  5                                   5    
HELIX   89  89 LYS C  938  ASP C  949  1                                  12    
HELIX   90  90 PRO C  970  LEU C  978  1                                   9    
HELIX   91  91 PRO C  981  THR C  990  1                                  10    
HELIX   92  92 THR B   22  GLY B   35  1                                  14    
HELIX   93  93 PRO B   37  GLN B   41  5                                   5    
HELIX   94  94 LEU B   56  ASN B   60  5                                   5    
HELIX   95  95 THR D   22  GLY D   35  1                                  14    
HELIX   96  96 PRO D   37  GLN D   41  5                                   5    
HELIX   97  97 LEU D   56  ASN D   60  5                                   5    
SHEET    1   A 7 VAL A 108  VAL A 110  0                                        
SHEET    2   A 7 SER A  62  PHE A  66  1  N  MET A  63   O  ASN A 109           
SHEET    3   A 7 ASN A  38  LEU A  42  1  N  ILE A  41   O  THR A  64           
SHEET    4   A 7 VAL A 125  ALA A 128  1  O  VAL A 127   N  LEU A  42           
SHEET    5   A 7 ARG A 150  ARG A 157  1  O  ILE A 152   N  ALA A 128           
SHEET    6   A 7 PHE A 160  ASP A 166 -1  O  ASP A 166   N  PHE A 151           
SHEET    7   A 7 PHE A 388  ASP A 392 -1  O  PHE A 391   N  GLY A 161           
SHEET    1   B 2 PHE A 171  VAL A 173  0                                        
SHEET    2   B 2 ARG A 262  ILE A 264 -1  O  ILE A 264   N  PHE A 171           
SHEET    1   C 7 PHE A 228  LYS A 229  0                                        
SHEET    2   C 7 PHE A 210  SER A 214 -1  N  VAL A 211   O  PHE A 228           
SHEET    3   C 7 ILE A 254  GLU A 257 -1  O  THR A 256   N  ARG A 212           
SHEET    4   C 7 THR A 183  ILE A 189 -1  N  GLY A 184   O  PHE A 255           
SHEET    5   C 7 THR A 194  MET A 197 -1  O  THR A 196   N  SER A 187           
SHEET    6   C 7 ALA A 237  ARG A 239 -1  O  PHE A 238   N  VAL A 195           
SHEET    7   C 7 GLU A 231  GLY A 234 -1  N  GLU A 231   O  ARG A 239           
SHEET    1   D 8 ILE A 513  LYS A 516  0                                        
SHEET    2   D 8 TYR A 465  THR A 469  1  N  ILE A 466   O  ASN A 514           
SHEET    3   D 8 LYS A 436  VAL A 440  1  N  LEU A 439   O  VAL A 467           
SHEET    4   D 8 PHE A 538  ASN A 541  1  O  THR A 540   N  PHE A 438           
SHEET    5   D 8 LEU A 563  LEU A 569  1  O  LEU A 564   N  ASN A 541           
SHEET    6   D 8 LYS A 572  ILE A 578 -1  O  LYS A 572   N  LEU A 569           
SHEET    7   D 8 ASN A 896  ASN A 900 -1  O  VAL A 899   N  GLY A 573           
SHEET    8   D 8 PHE A 905  SER A 909 -1  O  SER A 909   N  ASN A 896           
SHEET    1   E 2 LYS A 916  TYR A 919  0                                        
SHEET    2   E 2 LYS A 922  ASP A 925 -1  O  TYR A 924   N  GLY A 917           
SHEET    1   F 5 ARG A 930  LYS A 934  0                                        
SHEET    2   F 5 PHE A1019  HIS A1023  1  O  HIS A1023   N  ILE A 933           
SHEET    3   F 5 THR A1000  ASP A1008 -1  N  MET A1001   O  ILE A1022           
SHEET    4   F 5 GLU A 953  TYR A 959 -1  N  THR A 955   O  CYS A1006           
SHEET    5   F 5 SER A 962  ALA A 966 -1  O  LEU A 964   N  LEU A 957           
SHEET    1   G 4 ARG A 930  LYS A 934  0                                        
SHEET    2   G 4 PHE A1019  HIS A1023  1  O  HIS A1023   N  ILE A 933           
SHEET    3   G 4 THR A1000  ASP A1008 -1  N  MET A1001   O  ILE A1022           
SHEET    4   G 4 ASP A1014  VAL A1015 -1  O  VAL A1015   N  ALA A1007           
SHEET    1   H 7 VAL C 108  VAL C 110  0                                        
SHEET    2   H 7 SER C  62  PHE C  66  1  N  MET C  63   O  ASN C 109           
SHEET    3   H 7 ASN C  38  LEU C  42  1  N  VAL C  39   O  THR C  64           
SHEET    4   H 7 VAL C 125  ALA C 128  1  O  VAL C 127   N  LEU C  42           
SHEET    5   H 7 ARG C 150  ARG C 157  1  O  ILE C 152   N  ALA C 128           
SHEET    6   H 7 PHE C 160  ASP C 166 -1  O  PHE C 164   N  SER C 153           
SHEET    7   H 7 PHE C 388  ASP C 392 -1  O  PHE C 391   N  GLY C 161           
SHEET    1   I 2 PHE C 171  VAL C 173  0                                        
SHEET    2   I 2 ARG C 262  ILE C 264 -1  O  ARG C 262   N  VAL C 173           
SHEET    1   J 7 PHE C 228  LYS C 229  0                                        
SHEET    2   J 7 PHE C 210  SER C 214 -1  N  VAL C 211   O  PHE C 228           
SHEET    3   J 7 ILE C 254  VAL C 258 -1  O  THR C 256   N  ARG C 212           
SHEET    4   J 7 THR C 183  ILE C 189 -1  N  GLY C 184   O  PHE C 255           
SHEET    5   J 7 THR C 194  MET C 197 -1  O  THR C 196   N  SER C 187           
SHEET    6   J 7 ALA C 237  ARG C 239 -1  O  PHE C 238   N  VAL C 195           
SHEET    7   J 7 GLU C 231  GLY C 234 -1  N  GLU C 231   O  ARG C 239           
SHEET    1   K 8 ILE C 513  LYS C 516  0                                        
SHEET    2   K 8 TYR C 465  THR C 469  1  N  VAL C 468   O  LYS C 516           
SHEET    3   K 8 LYS C 436  VAL C 440  1  N  LEU C 439   O  VAL C 467           
SHEET    4   K 8 PHE C 538  ASN C 541  1  O  THR C 540   N  PHE C 438           
SHEET    5   K 8 LEU C 563  LEU C 569  1  O  LEU C 564   N  ASN C 541           
SHEET    6   K 8 LYS C 572  ILE C 578 -1  O  GLN C 576   N  GLU C 565           
SHEET    7   K 8 ASN C 896  ASN C 900 -1  O  VAL C 899   N  GLY C 573           
SHEET    8   K 8 PHE C 905  SER C 909 -1  O  SER C 909   N  ASN C 896           
SHEET    1   L 2 LYS C 916  TYR C 919  0                                        
SHEET    2   L 2 LYS C 922  ASP C 925 -1  O  TYR C 924   N  GLY C 917           
SHEET    1   M 5 ARG C 930  LYS C 934  0                                        
SHEET    2   M 5 PHE C1019  HIS C1023  1  O  PHE C1019   N  PHE C 931           
SHEET    3   M 5 THR C1000  ASP C1008 -1  N  MET C1001   O  ILE C1022           
SHEET    4   M 5 GLU C 953  TYR C 959 -1  N  GLU C 953   O  ASP C1008           
SHEET    5   M 5 SER C 962  ALA C 966 -1  O  LEU C 964   N  LEU C 957           
SHEET    1   N 4 ARG C 930  LYS C 934  0                                        
SHEET    2   N 4 PHE C1019  HIS C1023  1  O  PHE C1019   N  PHE C 931           
SHEET    3   N 4 THR C1000  ASP C1008 -1  N  MET C1001   O  ILE C1022           
SHEET    4   N 4 ASP C1014  VAL C1015 -1  O  VAL C1015   N  ALA C1007           
SHEET    1   O 5 THR B  12  GLU B  16  0                                        
SHEET    2   O 5 GLN B   2  THR B   7 -1  N  VAL B   5   O  ILE B  13           
SHEET    3   O 5 THR B  66  VAL B  70  1  O  LEU B  67   N  PHE B   4           
SHEET    4   O 5 ARG B  42  PHE B  45 -1  N  ARG B  42   O  VAL B  70           
SHEET    5   O 5 LYS B  48  GLN B  49 -1  O  LYS B  48   N  PHE B  45           
SHEET    1   P 5 THR D  12  GLU D  16  0                                        
SHEET    2   P 5 GLN D   2  THR D   7 -1  N  VAL D   5   O  ILE D  13           
SHEET    3   P 5 THR D  66  LEU D  69  1  O  LEU D  67   N  PHE D   4           
SHEET    4   P 5 LEU D  43  PHE D  45 -1  N  ILE D  44   O  HIS D  68           
SHEET    5   P 5 LYS D  48  GLN D  49 -1  O  LYS D  48   N  PHE D  45           
CISPEP   1 PRO A  785    ASP A  786          0       -12.02                     
CISPEP   2 LEU A  903    PRO A  904          0        -9.89                     
CISPEP   3 LEU C  903    PRO C  904          0       -12.47                     
SITE     1 AC1  2 ASP A 316  ASN A 320                                          
SITE     1 AC2  4 ASP C 316  ASN C 320  ILE C 323  LYS C 349                    
CRYST1  115.363  118.564  207.567  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008668  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008434  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004818        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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