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Database: PDB
Entry: 6O82
LinkDB: 6O82
Original site: 6O82 
HEADER    LIGASE/PROTEIN BINDING                  08-MAR-19   6O82              
TITLE     S. POMBE UBIQUITIN E1 COMPLEX WITH A UBIQUITIN-AMP MIMIC              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-ACTIVATING ENZYME E1 1;                          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: RESIDUES 13-1012;                                          
COMPND   5 SYNONYM: POLY(A)+ RNA TRANSPORT PROTEIN 3;                           
COMPND   6 EC: 6.2.1.45;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: UBIQUITIN-60S RIBOSOMAL PROTEIN L40;                       
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: RESIDUES 1-76;                                             
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE (STRAIN 972 / ATCC    
SOURCE   3 24843);                                                              
SOURCE   4 ORGANISM_COMMON: FISSION YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 284812;                                              
SOURCE   6 STRAIN: 972 / ATCC 24843;                                            
SOURCE   7 ATCC: 24843;                                                         
SOURCE   8 GENE: PTR3, SPBC1604.21C, SPBC211.09;                                
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PSMT3;                                    
SOURCE  13 MOL_ID: 2;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE (STRAIN 972 / ATCC    
SOURCE  15 24843);                                                              
SOURCE  16 ORGANISM_COMMON: FISSION YEAST;                                      
SOURCE  17 ORGANISM_TAXID: 284812;                                              
SOURCE  18 STRAIN: 972 / ATCC 24843;                                            
SOURCE  19 ATCC: 24843;                                                         
SOURCE  20 GENE: UEP1, UBI2, SPAC1805.12C;                                      
SOURCE  21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  24 EXPRESSION_SYSTEM_PLASMID: PTXB1                                     
KEYWDS    THIOESTER, ADENYLATION, INHIBITOR, ACYL-ADENYLATE INTERMEDIATE,       
KEYWDS   2 ACETYLATION, LIGASE, NUCLEUS, PHOSPHOPROTEIN, UBL CONJUGATION        
KEYWDS   3 PATHWAY, ATP-BINDING, NUCLEOTIDE-BINDING, CYTOPLASM, ISOPEPTIDE      
KEYWDS   4 BOND, LIGASE-PROTEIN BINDING COMPLEX                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.K.OLSEN,C.D.LIMA                                                    
REVDAT   4   20-NOV-19 6O82    1       REMARK                                   
REVDAT   3   14-AUG-19 6O82    1       JRNL                                     
REVDAT   2   10-JUL-19 6O82    1       JRNL                                     
REVDAT   1   19-JUN-19 6O82    0                                                
JRNL        AUTH   Z.S.HANN,C.JI,S.K.OLSEN,X.LU,M.C.LUX,D.S.TAN,C.D.LIMA        
JRNL        TITL   STRUCTURAL BASIS FOR ADENYLATION AND THIOESTER BOND          
JRNL        TITL 2 FORMATION IN THE UBIQUITIN E1.                               
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 116 15475 2019              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   31235585                                                     
JRNL        DOI    10.1073/PNAS.1905488116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3211                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.400                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 81155                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4073                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 42.3932 -  7.9833    1.00     2875   153  0.1869 0.2047        
REMARK   3     2  7.9833 -  6.3434    1.00     2751   135  0.2012 0.2163        
REMARK   3     3  6.3434 -  5.5436    1.00     2708   153  0.1933 0.2418        
REMARK   3     4  5.5436 -  5.0376    1.00     2689   154  0.1704 0.1930        
REMARK   3     5  5.0376 -  4.6770    1.00     2699   131  0.1525 0.1812        
REMARK   3     6  4.6770 -  4.4016    1.00     2679   147  0.1423 0.1747        
REMARK   3     7  4.4016 -  4.1813    1.00     2680   122  0.1531 0.1878        
REMARK   3     8  4.1813 -  3.9995    1.00     2670   160  0.1600 0.1736        
REMARK   3     9  3.9995 -  3.8456    1.00     2672   114  0.1733 0.2237        
REMARK   3    10  3.8456 -  3.7130    1.00     2629   142  0.1873 0.2365        
REMARK   3    11  3.7130 -  3.5970    1.00     2688   120  0.1988 0.2244        
REMARK   3    12  3.5970 -  3.4942    1.00     2662   136  0.1999 0.2476        
REMARK   3    13  3.4942 -  3.4022    1.00     2672   126  0.2135 0.2435        
REMARK   3    14  3.4022 -  3.3193    1.00     2629   142  0.2206 0.2595        
REMARK   3    15  3.3193 -  3.2438    1.00     2635   165  0.2291 0.2785        
REMARK   3    16  3.2438 -  3.1748    1.00     2645   163  0.2457 0.2614        
REMARK   3    17  3.1748 -  3.1113    1.00     2583   153  0.2434 0.3185        
REMARK   3    18  3.1113 -  3.0526    1.00     2660   159  0.2373 0.2652        
REMARK   3    19  3.0526 -  2.9981    1.00     2613   136  0.2372 0.2795        
REMARK   3    20  2.9981 -  2.9473    1.00     2615   144  0.2424 0.2846        
REMARK   3    21  2.9473 -  2.8998    1.00     2652   129  0.2358 0.2616        
REMARK   3    22  2.8998 -  2.8552    1.00     2635   143  0.2347 0.2954        
REMARK   3    23  2.8552 -  2.8132    1.00     2678   120  0.2287 0.2667        
REMARK   3    24  2.8132 -  2.7736    1.00     2643   120  0.2344 0.2626        
REMARK   3    25  2.7736 -  2.7361    1.00     2585   146  0.2399 0.2681        
REMARK   3    26  2.7361 -  2.7006    1.00     2666   119  0.2569 0.3075        
REMARK   3    27  2.7006 -  2.6668    1.00     2623   151  0.2582 0.2931        
REMARK   3    28  2.6668 -  2.6347    1.00     2621   147  0.2559 0.3045        
REMARK   3    29  2.6347 -  2.6041    0.96     2525   143  0.2608 0.2844        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.970           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 14 THROUGH 538 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  24.6172  38.8931  -9.7187              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6053 T22:   0.1736                                     
REMARK   3      T33:   0.3987 T12:  -0.0486                                     
REMARK   3      T13:  -0.0504 T23:   0.0518                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6553 L22:   1.0215                                     
REMARK   3      L33:   1.3596 L12:   0.2393                                     
REMARK   3      L13:   0.4461 L23:   0.3830                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1580 S12:   0.2539 S13:   0.2837                       
REMARK   3      S21:  -0.4637 S22:   0.0427 S23:   0.0873                       
REMARK   3      S31:  -0.5483 S32:   0.1097 S33:  -0.1149                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 539 THROUGH 855 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.8416  20.6081  12.7263              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4099 T22:   0.4653                                     
REMARK   3      T33:   0.5182 T12:   0.0231                                     
REMARK   3      T13:  -0.0398 T23:  -0.0812                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5248 L22:   0.4044                                     
REMARK   3      L33:   1.0308 L12:   0.7170                                     
REMARK   3      L13:  -0.0768 L23:   0.5137                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0827 S12:  -0.5200 S13:   0.2218                       
REMARK   3      S21:  -0.0018 S22:  -0.2654 S23:   0.2371                       
REMARK   3      S31:   0.0358 S32:  -0.3084 S33:   0.1705                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 856 THROUGH 1012 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  26.1577  -1.2197 -11.7710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3791 T22:   0.2630                                     
REMARK   3      T33:   0.4744 T12:  -0.0355                                     
REMARK   3      T13:   0.0188 T23:  -0.0248                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3866 L22:   2.2790                                     
REMARK   3      L33:   0.7949 L12:  -0.3396                                     
REMARK   3      L13:   0.0235 L23:   0.7646                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0472 S12:   0.0312 S13:  -0.1684                       
REMARK   3      S21:  -0.2170 S22:   0.0534 S23:   0.2437                       
REMARK   3      S31:   0.0224 S32:  -0.0710 S33:  -0.0207                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 76 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  37.6450  22.6428   7.9487              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3963 T22:   0.2020                                     
REMARK   3      T33:   0.4261 T12:  -0.0118                                     
REMARK   3      T13:   0.0139 T23:  -0.0119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8896 L22:   1.4577                                     
REMARK   3      L33:   2.8225 L12:  -0.3709                                     
REMARK   3      L13:   0.5771 L23:  -0.2269                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0076 S12:  -0.1918 S13:  -0.2224                       
REMARK   3      S21:  -0.0687 S22:   0.0530 S23:  -0.3700                       
REMARK   3      S31:   0.1675 S32:   0.3899 S33:  -0.0500                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 14 THROUGH 448 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  54.1421  13.1729  55.5066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7065 T22:   1.0239                                     
REMARK   3      T33:   0.9011 T12:  -0.0881                                     
REMARK   3      T13:  -0.2846 T23:   0.4412                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0603 L22:   1.0154                                     
REMARK   3      L33:   1.5506 L12:   0.0346                                     
REMARK   3      L13:   0.3185 L23:   0.1621                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3688 S12:  -0.9202 S13:  -0.8041                       
REMARK   3      S21:   0.2848 S22:  -0.2640 S23:  -0.4921                       
REMARK   3      S31:   0.5362 S32:   0.1399 S33:  -0.0685                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 449 THROUGH 833 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5896  33.8514  59.0106              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6212 T22:   1.2669                                     
REMARK   3      T33:   0.5356 T12:  -0.1734                                     
REMARK   3      T13:   0.0224 T23:  -0.0645                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4480 L22:   0.6149                                     
REMARK   3      L33:   0.5232 L12:   0.2990                                     
REMARK   3      L13:  -0.4032 L23:  -0.0782                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2652 S12:  -0.9162 S13:   0.1334                       
REMARK   3      S21:   0.2884 S22:  -0.2411 S23:   0.2295                       
REMARK   3      S31:  -0.0085 S32:  -0.3189 S33:  -0.0370                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 834 THROUGH 1012 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  39.9718  42.7892  33.4570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3712 T22:   0.4682                                     
REMARK   3      T33:   0.3922 T12:   0.0132                                     
REMARK   3      T13:  -0.0172 T23:  -0.0805                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3713 L22:   1.0427                                     
REMARK   3      L33:   1.7896 L12:   0.5268                                     
REMARK   3      L13:   0.1543 L23:  -0.4606                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0091 S12:  -0.5450 S13:   0.2246                       
REMARK   3      S21:   0.0375 S22:  -0.0921 S23:  -0.1225                       
REMARK   3      S31:  -0.1958 S32:  -0.2383 S33:  -0.0589                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 76 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  40.5799  14.1300  32.0799              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6058 T22:   0.4224                                     
REMARK   3      T33:   0.6177 T12:  -0.0087                                     
REMARK   3      T13:  -0.1159 T23:   0.1153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7737 L22:   1.0125                                     
REMARK   3      L33:   3.8893 L12:   1.2023                                     
REMARK   3      L13:   0.7049 L23:  -0.2230                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2897 S12:  -0.1340 S13:  -0.6848                       
REMARK   3      S21:  -0.2256 S22:  -0.1477 S23:  -0.3046                       
REMARK   3      S31:   0.9613 S32:  -0.1293 S33:  -0.1108                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6O82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000239326.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-DEC-10                          
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                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 81217                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.390                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.10100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59700                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3CMM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.15 M MGSO4, 5 MM         
REMARK 280  MGCL2, 1 MM PYROPHOSPHATE, PH 8.0, VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       91.03050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.30800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       91.03050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.30800            
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: 5620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 45190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    12                                                      
REMARK 465     ASN A    13                                                      
REMARK 465     ASN A   770                                                      
REMARK 465     GLU A   771                                                      
REMARK 465     ASN A   772                                                      
REMARK 465     GLU A   773                                                      
REMARK 465     GLU A   774                                                      
REMARK 465     ALA A   775                                                      
REMARK 465     PRO A   776                                                      
REMARK 465     GLU A   777                                                      
REMARK 465     THR A   778                                                      
REMARK 465     ALA A   779                                                      
REMARK 465     ALA A   780                                                      
REMARK 465     ASN A   781                                                      
REMARK 465     LYS A   782                                                      
REMARK 465     SER C    12                                                      
REMARK 465     ASN C    13                                                      
REMARK 465     GLY C   764                                                      
REMARK 465     ILE C   765                                                      
REMARK 465     LYS C   766                                                      
REMARK 465     ILE C   767                                                      
REMARK 465     GLN C   768                                                      
REMARK 465     VAL C   769                                                      
REMARK 465     ASN C   770                                                      
REMARK 465     GLU C   771                                                      
REMARK 465     ASN C   772                                                      
REMARK 465     GLU C   773                                                      
REMARK 465     GLU C   774                                                      
REMARK 465     ALA C   775                                                      
REMARK 465     PRO C   776                                                      
REMARK 465     GLU C   777                                                      
REMARK 465     THR C   778                                                      
REMARK 465     PRO C   795                                                      
REMARK 465     PRO C   796                                                      
REMARK 465     PRO C   797                                                      
REMARK 465     SER C   798                                                      
REMARK 465     SER C   799                                                      
REMARK 465     LEU C   800                                                      
REMARK 465     VAL C   801                                                      
REMARK 465     GLY C   802                                                      
REMARK 465     PHE C   803                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1378     O    HOH A  1395              1.97            
REMARK 500   O    HOH C  1249     O    HOH C  1254              1.97            
REMARK 500   O    HOH A  1309     O    HOH A  1381              1.99            
REMARK 500   O    HOH A  1299     O    HOH A  1340              2.01            
REMARK 500   O    HOH A  1330     O    HOH A  1376              2.01            
REMARK 500   O    HOH A  1306     O    HOH A  1374              2.02            
REMARK 500   O    HOH A  1254     O    HOH A  1317              2.02            
REMARK 500   O    HOH A  1292     O    HOH A  1382              2.02            
REMARK 500   OG   SER A   662     OE1  GLU A   664              2.04            
REMARK 500   OH   TYR A    67     O    HOH A  1201              2.05            
REMARK 500   O    GLY D    10     O    HOH D   201              2.07            
REMARK 500   O    HOH A  1202     O    HOH A  1327              2.07            
REMARK 500   O    HOH A  1339     O    HOH A  1387              2.08            
REMARK 500   O    HOH A  1365     O    HOH A  1372              2.08            
REMARK 500   O    HOH A  1307     O    HOH A  1351              2.10            
REMARK 500   O    HOH A  1367     O    HOH A  1388              2.11            
REMARK 500   O    HOH A  1204     O    HOH A  1256              2.12            
REMARK 500   O    HOH A  1273     O    HOH A  1334              2.14            
REMARK 500   O    HOH A  1243     O    HOH A  1312              2.16            
REMARK 500   OD1  ASP C   675     O    HOH C  1201              2.18            
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   NZ   LYS C   262     OE1  GLU C   489     3546     2.17            
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    ASP A  16       93.65    -67.47                                   
REMARK 500    SER A  36        0.21    -67.26                                   
REMARK 500    ASP A  68       83.74   -161.61                                   
REMARK 500    SER A  79      -21.19   -141.72                                   
REMARK 500    ASN A 169       42.98   -142.56                                   
REMARK 500    ASP A 176      -13.50   -152.37                                   
REMARK 500    ASP A 244       13.10    -67.68                                   
REMARK 500    LEU A 245      -11.47   -143.53                                   
REMARK 500    ASN A 251     -166.49     60.22                                   
REMARK 500    PHE A 377      153.98     78.42                                   
REMARK 500    ASP A 463      129.61   -171.68                                   
REMARK 500    PHE A 521       56.28    -95.57                                   
REMARK 500    ALA A 535       54.56   -141.15                                   
REMARK 500    LEU A 575      -53.71   -139.79                                   
REMARK 500    ASN A 597      -27.89   -143.67                                   
REMARK 500    LYS A 618      -68.12   -134.11                                   
REMARK 500    ASN A 632       52.98   -115.50                                   
REMARK 500    VAL A 656      -60.78   -142.54                                   
REMARK 500    ASN A 679      -70.69   -154.88                                   
REMARK 500    THR A 695     -168.71    -76.85                                   
REMARK 500    ASP A 997     -169.79    -77.78                                   
REMARK 500    GLN C  37       52.21   -109.01                                   
REMARK 500    SER C  38      115.81   -161.69                                   
REMARK 500    LYS C  46     -157.62    -87.88                                   
REMARK 500    ASP C  68       81.40   -157.59                                   
REMARK 500    ASN C 146       55.96   -115.87                                   
REMARK 500    HIS C 147       67.49     28.70                                   
REMARK 500    ASP C 165       87.77   -154.73                                   
REMARK 500    GLU C 168       33.29    -82.80                                   
REMARK 500    ASN C 169       45.39   -166.31                                   
REMARK 500    LEU C 245      -11.36   -141.08                                   
REMARK 500    ASN C 251     -163.22     56.10                                   
REMARK 500    PHE C 377      155.85     71.99                                   
REMARK 500    GLN C 382      -32.85   -139.28                                   
REMARK 500    SER C 388       50.35   -110.21                                   
REMARK 500    LEU C 575      -59.79   -142.76                                   
REMARK 500    ASN C 597      -35.55   -140.46                                   
REMARK 500    ASN C 600       11.45   -140.01                                   
REMARK 500    LYS C 618      -68.26   -127.09                                   
REMARK 500    ASN C 632       48.25   -102.37                                   
REMARK 500    VAL C 656      -54.71   -140.60                                   
REMARK 500    ASN C 679      -62.87   -137.98                                   
REMARK 500    HIS C 717       37.63    -90.02                                   
REMARK 500    PRO C 744       -8.16    -58.18                                   
REMARK 500    ASN C 781       45.68   -158.83                                   
REMARK 500    ASP C 814      117.44   -169.81                                   
REMARK 500    GLN D  62     -160.97   -126.24                                   
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 A1397        DISTANCE =  6.37 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 465   OD2                                                    
REMARK 620 2 HOH A1217   O    83.6                                              
REMARK 620 3 HOH A1246   O    74.9  81.0                                        
REMARK 620 4 POP A1103   O4   89.2  91.4 163.0                                  
REMARK 620 5 HOH A1225   O    89.7 171.6  92.4  93.5                            
REMARK 620 6 HOH A1230   O   165.9  95.2  91.0 104.9  90.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1101  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 537   OD2                                                    
REMARK 620 2 POP A1103   O6   95.4                                              
REMARK 620 3 JZU B 101   O2S 104.6  80.9                                        
REMARK 620 4 POP A1103   O2  165.5  75.0  84.9                                  
REMARK 620 5 HOH A1262   O    84.1  82.4 161.8  83.9                            
REMARK 620 6 HOH A1293   O   103.8 160.8  93.0  86.4 100.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 465   OD2                                                    
REMARK 620 2 POP C1103   O6   69.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1101  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 537   OD2                                                    
REMARK 620 2 HOH C1210   O    72.4                                              
REMARK 620 3 POP C1103   O1  158.8  90.1                                        
REMARK 620 4 POP C1103   O4   98.3  94.1  70.5                                  
REMARK 620 5 JZU D 101   O2S 112.2 172.6  86.4  91.0                            
REMARK 620 6 HOH C1203   O   130.2 105.0  65.0 131.1  67.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue POP A 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue POP A 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1108                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1109                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1110                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue JZU B 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 1101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 1102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue POP C 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 1106                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4II3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6O83   RELATED DB: PDB                                   
DBREF  6O82 A   13  1012  UNP    O94609   UBA1_SCHPO      13   1012             
DBREF  6O82 B    1    76  UNP    P0CH07   RL402_SCHPO      1     76             
DBREF  6O82 C   13  1012  UNP    O94609   UBA1_SCHPO      13   1012             
DBREF  6O82 D    1    76  UNP    P0CH07   RL402_SCHPO      1     76             
SEQADV 6O82 SER A   12  UNP  O94609              EXPRESSION TAG                 
SEQADV 6O82 CYS B   74  UNP  P0CH07    ARG    74 ENGINEERED MUTATION            
SEQADV 6O82 SER C   12  UNP  O94609              EXPRESSION TAG                 
SEQADV 6O82 CYS D   74  UNP  P0CH07    ARG    74 ENGINEERED MUTATION            
SEQRES   1 A 1001  SER ASN THR ILE ASP GLU GLY LEU TYR SER ARG GLN LEU          
SEQRES   2 A 1001  TYR VAL LEU GLY HIS GLU ALA MET LYS GLN MET SER GLN          
SEQRES   3 A 1001  SER ASN VAL LEU ILE ILE GLY CYS LYS GLY LEU GLY VAL          
SEQRES   4 A 1001  GLU ILE ALA LYS ASN VAL CYS LEU ALA GLY VAL LYS SER          
SEQRES   5 A 1001  VAL THR LEU TYR ASP PRO GLN PRO THR ARG ILE GLU ASP          
SEQRES   6 A 1001  LEU SER SER GLN TYR PHE LEU THR GLU ASP ASP ILE GLY          
SEQRES   7 A 1001  VAL PRO ARG ALA LYS VAL THR VAL SER LYS LEU ALA GLU          
SEQRES   8 A 1001  LEU ASN GLN TYR VAL PRO VAL SER VAL VAL ASP GLU LEU          
SEQRES   9 A 1001  SER THR GLU TYR LEU LYS ASN PHE LYS CYS VAL VAL VAL          
SEQRES  10 A 1001  THR GLU THR SER LEU THR LYS GLN LEU GLU ILE ASN ASP          
SEQRES  11 A 1001  PHE THR HIS LYS ASN HIS ILE ALA TYR ILE ALA ALA ASP          
SEQRES  12 A 1001  SER ARG GLY LEU PHE GLY SER ILE PHE CYS ASP PHE GLY          
SEQRES  13 A 1001  GLU ASN PHE ILE CYS THR ASP THR ASP GLY ASN GLU PRO          
SEQRES  14 A 1001  LEU THR GLY MET ILE ALA SER ILE THR ASP ASP GLY VAL          
SEQRES  15 A 1001  VAL THR MET LEU GLU GLU THR ARG HIS GLY LEU GLU ASN          
SEQRES  16 A 1001  GLY ASP PHE VAL LYS PHE THR GLU VAL LYS GLY MET PRO          
SEQRES  17 A 1001  GLY LEU ASN ASP GLY THR PRO ARG LYS VAL GLU VAL LYS          
SEQRES  18 A 1001  GLY PRO TYR THR PHE SER ILE GLY SER VAL LYS ASP LEU          
SEQRES  19 A 1001  GLY SER ALA GLY TYR ASN GLY VAL PHE THR GLN VAL LYS          
SEQRES  20 A 1001  VAL PRO THR LYS ILE SER PHE LYS SER LEU ARG GLU SER          
SEQRES  21 A 1001  LEU LYS ASP PRO GLU TYR VAL TYR PRO ASP PHE GLY LYS          
SEQRES  22 A 1001  MET MET ARG PRO PRO GLN TYR HIS ILE ALA PHE GLN ALA          
SEQRES  23 A 1001  LEU SER ALA PHE ALA ASP ALA HIS GLU GLY SER LEU PRO          
SEQRES  24 A 1001  ARG PRO ARG ASN ASP ILE ASP ALA ALA GLU PHE PHE GLU          
SEQRES  25 A 1001  PHE CYS LYS LYS ILE ALA SER THR LEU GLN PHE ASP VAL          
SEQRES  26 A 1001  GLU LEU ASP GLU LYS LEU ILE LYS GLU ILE SER TYR GLN          
SEQRES  27 A 1001  ALA ARG GLY ASP LEU VAL ALA MET SER ALA PHE LEU GLY          
SEQRES  28 A 1001  GLY ALA VAL ALA GLN GLU VAL LEU LYS ALA THR THR SER          
SEQRES  29 A 1001  LYS PHE TYR PRO LEU LYS GLN TYR PHE TYR PHE ASP SER          
SEQRES  30 A 1001  LEU GLU SER LEU PRO SER SER VAL THR ILE SER GLU GLU          
SEQRES  31 A 1001  THR CYS LYS PRO ARG GLY CYS ARG TYR ASP GLY GLN ILE          
SEQRES  32 A 1001  ALA VAL PHE GLY SER GLU PHE GLN GLU LYS ILE ALA SER          
SEQRES  33 A 1001  LEU SER THR PHE LEU VAL GLY ALA GLY ALA ILE GLY CYS          
SEQRES  34 A 1001  GLU MET LEU LYS ASN TRP ALA MET MET GLY VAL ALA THR          
SEQRES  35 A 1001  GLY GLU SER GLY HIS ILE SER VAL THR ASP MET ASP SER          
SEQRES  36 A 1001  ILE GLU LYS SER ASN LEU ASN ARG GLN PHE LEU PHE ARG          
SEQRES  37 A 1001  PRO ARG ASP VAL GLY LYS LEU LYS SER GLU CYS ALA SER          
SEQRES  38 A 1001  THR ALA VAL SER ILE MET ASN PRO SER LEU THR GLY LYS          
SEQRES  39 A 1001  ILE THR SER TYR GLN GLU ARG VAL GLY PRO GLU SER GLU          
SEQRES  40 A 1001  GLY ILE PHE GLY ASP GLU PHE PHE GLU LYS LEU SER LEU          
SEQRES  41 A 1001  VAL THR ASN ALA LEU ASP ASN VAL GLU ALA ARG MET TYR          
SEQRES  42 A 1001  VAL ASP ARG ARG CYS VAL PHE PHE GLU LYS PRO LEU LEU          
SEQRES  43 A 1001  GLU SER GLY THR LEU GLY THR LYS GLY ASN THR GLN VAL          
SEQRES  44 A 1001  VAL VAL PRO HIS LEU THR GLU SER TYR GLY SER SER GLN          
SEQRES  45 A 1001  ASP PRO PRO GLU LYS SER PHE PRO ILE CYS THR LEU LYS          
SEQRES  46 A 1001  ASN PHE PRO ASN ARG ILE GLU HIS THR ILE ALA TRP ALA          
SEQRES  47 A 1001  ARG ASP LEU PHE GLU GLY LEU PHE LYS GLN PRO ILE ASP          
SEQRES  48 A 1001  ASN VAL ASN MET TYR LEU SER SER PRO ASN PHE LEU GLU          
SEQRES  49 A 1001  THR SER LEU LYS THR SER SER ASN PRO ARG GLU VAL LEU          
SEQRES  50 A 1001  GLU ASN ILE ARG ASP TYR LEU VAL THR GLU LYS PRO LEU          
SEQRES  51 A 1001  SER PHE GLU GLU CYS ILE MET TRP ALA ARG LEU GLN PHE          
SEQRES  52 A 1001  ASP LYS PHE PHE ASN ASN ASN ILE GLN GLN LEU LEU PHE          
SEQRES  53 A 1001  ASN PHE PRO LYS ASP SER VAL THR SER THR GLY GLN PRO          
SEQRES  54 A 1001  PHE TRP SER GLY PRO LYS ARG ALA PRO THR PRO LEU SER          
SEQRES  55 A 1001  PHE ASP ILE HIS ASN ARG GLU HIS PHE ASP PHE ILE VAL          
SEQRES  56 A 1001  ALA ALA ALA SER LEU TYR ALA PHE ASN TYR GLY LEU LYS          
SEQRES  57 A 1001  SER GLU THR ASP PRO ALA ILE TYR GLU ARG VAL LEU ALA          
SEQRES  58 A 1001  GLY TYR ASN PRO PRO PRO PHE ALA PRO LYS SER GLY ILE          
SEQRES  59 A 1001  LYS ILE GLN VAL ASN GLU ASN GLU GLU ALA PRO GLU THR          
SEQRES  60 A 1001  ALA ALA ASN LYS ASP LYS GLN GLU LEU LYS SER ILE ALA          
SEQRES  61 A 1001  ASP SER LEU PRO PRO PRO SER SER LEU VAL GLY PHE ARG          
SEQRES  62 A 1001  LEU THR PRO ALA GLU PHE GLU LYS ASP ASP ASP SER ASN          
SEQRES  63 A 1001  HIS HIS ILE ASP PHE ILE THR ALA ALA SER ASN LEU ARG          
SEQRES  64 A 1001  ALA MET ASN TYR ASP ILE THR PRO ALA ASP ARG PHE LYS          
SEQRES  65 A 1001  THR LYS PHE VAL ALA GLY LYS ILE VAL PRO ALA MET CYS          
SEQRES  66 A 1001  THR SER THR ALA VAL VAL SER GLY LEU VAL CYS LEU GLU          
SEQRES  67 A 1001  LEU VAL LYS LEU VAL ASP GLY LYS LYS LYS ILE GLU GLU          
SEQRES  68 A 1001  TYR LYS ASN GLY PHE PHE ASN LEU ALA ILE GLY LEU PHE          
SEQRES  69 A 1001  THR PHE SER ASP PRO ILE ALA SER PRO LYS MET LYS VAL          
SEQRES  70 A 1001  ASN GLY LYS GLU ILE ASP LYS ILE TRP ASP ARG TYR ASN          
SEQRES  71 A 1001  LEU PRO ASP CYS THR LEU GLN GLU LEU ILE ASP TYR PHE          
SEQRES  72 A 1001  GLN LYS GLU GLU GLY LEU GLU VAL THR MET LEU SER SER          
SEQRES  73 A 1001  GLY VAL SER LEU LEU TYR ALA ASN PHE GLN PRO PRO LYS          
SEQRES  74 A 1001  LYS LEU ALA GLU ARG LEU PRO LEU LYS ILE SER GLU LEU          
SEQRES  75 A 1001  VAL GLU GLN ILE THR LYS LYS LYS LEU GLU PRO PHE ARG          
SEQRES  76 A 1001  LYS HIS LEU VAL LEU GLU ILE CYS CYS ASP ASP ALA ASN          
SEQRES  77 A 1001  GLY GLU ASP VAL GLU VAL PRO PHE ILE CYS ILE LYS 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 CYS GLY GLY                  
SEQRES   1 C 1001  SER ASN THR ILE ASP GLU GLY LEU TYR SER ARG GLN LEU          
SEQRES   2 C 1001  TYR VAL LEU GLY HIS GLU ALA MET LYS GLN MET SER GLN          
SEQRES   3 C 1001  SER ASN VAL LEU ILE ILE GLY CYS LYS GLY LEU GLY VAL          
SEQRES   4 C 1001  GLU ILE ALA LYS ASN VAL CYS LEU ALA GLY VAL LYS SER          
SEQRES   5 C 1001  VAL THR LEU TYR ASP PRO GLN PRO THR ARG ILE GLU ASP          
SEQRES   6 C 1001  LEU SER SER GLN TYR PHE LEU THR GLU ASP ASP ILE GLY          
SEQRES   7 C 1001  VAL PRO ARG ALA LYS VAL THR VAL SER LYS LEU ALA GLU          
SEQRES   8 C 1001  LEU ASN GLN TYR VAL PRO VAL SER VAL VAL ASP GLU LEU          
SEQRES   9 C 1001  SER THR GLU TYR LEU LYS ASN PHE LYS CYS VAL VAL VAL          
SEQRES  10 C 1001  THR GLU THR SER LEU THR LYS GLN LEU GLU ILE ASN ASP          
SEQRES  11 C 1001  PHE THR HIS LYS ASN HIS ILE ALA TYR ILE ALA ALA ASP          
SEQRES  12 C 1001  SER ARG GLY LEU PHE GLY SER ILE PHE CYS ASP PHE GLY          
SEQRES  13 C 1001  GLU ASN PHE ILE CYS THR ASP THR ASP GLY ASN GLU PRO          
SEQRES  14 C 1001  LEU THR GLY MET ILE ALA SER ILE THR ASP ASP GLY VAL          
SEQRES  15 C 1001  VAL THR MET LEU GLU GLU THR ARG HIS GLY LEU GLU ASN          
SEQRES  16 C 1001  GLY ASP PHE VAL LYS PHE THR GLU VAL LYS GLY MET PRO          
SEQRES  17 C 1001  GLY LEU ASN ASP GLY THR PRO ARG LYS VAL GLU VAL LYS          
SEQRES  18 C 1001  GLY PRO TYR THR PHE SER ILE GLY SER VAL LYS ASP LEU          
SEQRES  19 C 1001  GLY SER ALA GLY TYR ASN GLY VAL PHE THR GLN VAL LYS          
SEQRES  20 C 1001  VAL PRO THR LYS ILE SER PHE LYS SER LEU ARG GLU SER          
SEQRES  21 C 1001  LEU LYS ASP PRO GLU TYR VAL TYR PRO ASP PHE GLY LYS          
SEQRES  22 C 1001  MET MET ARG PRO PRO GLN TYR HIS ILE ALA PHE GLN ALA          
SEQRES  23 C 1001  LEU SER ALA PHE ALA ASP ALA HIS GLU GLY SER LEU PRO          
SEQRES  24 C 1001  ARG PRO ARG ASN ASP ILE ASP ALA ALA GLU PHE PHE GLU          
SEQRES  25 C 1001  PHE CYS LYS LYS ILE ALA SER THR LEU GLN PHE ASP VAL          
SEQRES  26 C 1001  GLU LEU ASP GLU LYS LEU ILE LYS GLU ILE SER TYR GLN          
SEQRES  27 C 1001  ALA ARG GLY ASP LEU VAL ALA MET SER ALA PHE LEU GLY          
SEQRES  28 C 1001  GLY ALA VAL ALA GLN GLU VAL LEU LYS ALA THR THR SER          
SEQRES  29 C 1001  LYS PHE TYR PRO LEU LYS GLN TYR PHE TYR PHE ASP SER          
SEQRES  30 C 1001  LEU GLU SER LEU PRO SER SER VAL THR ILE SER GLU GLU          
SEQRES  31 C 1001  THR CYS LYS PRO ARG GLY CYS ARG TYR ASP GLY GLN ILE          
SEQRES  32 C 1001  ALA VAL PHE GLY SER GLU PHE GLN GLU LYS ILE ALA SER          
SEQRES  33 C 1001  LEU SER THR PHE LEU VAL GLY ALA GLY ALA ILE GLY CYS          
SEQRES  34 C 1001  GLU MET LEU LYS ASN TRP ALA MET MET GLY VAL ALA THR          
SEQRES  35 C 1001  GLY GLU SER GLY HIS ILE SER VAL THR ASP MET ASP SER          
SEQRES  36 C 1001  ILE GLU LYS SER ASN LEU ASN ARG GLN PHE LEU PHE ARG          
SEQRES  37 C 1001  PRO ARG ASP VAL GLY LYS LEU LYS SER GLU CYS ALA SER          
SEQRES  38 C 1001  THR ALA VAL SER ILE MET ASN PRO SER LEU THR GLY LYS          
SEQRES  39 C 1001  ILE THR SER TYR GLN GLU ARG VAL GLY PRO GLU SER GLU          
SEQRES  40 C 1001  GLY ILE PHE GLY ASP GLU PHE PHE GLU LYS LEU SER LEU          
SEQRES  41 C 1001  VAL THR ASN ALA LEU ASP ASN VAL GLU ALA ARG MET TYR          
SEQRES  42 C 1001  VAL ASP ARG ARG CYS VAL PHE PHE GLU LYS PRO LEU LEU          
SEQRES  43 C 1001  GLU SER GLY THR LEU GLY THR LYS GLY ASN THR GLN VAL          
SEQRES  44 C 1001  VAL VAL PRO HIS LEU THR GLU SER TYR GLY SER SER GLN          
SEQRES  45 C 1001  ASP PRO PRO GLU LYS SER PHE PRO ILE CYS THR LEU LYS          
SEQRES  46 C 1001  ASN PHE PRO ASN ARG ILE GLU HIS THR ILE ALA TRP ALA          
SEQRES  47 C 1001  ARG ASP LEU PHE GLU GLY LEU PHE LYS GLN PRO ILE ASP          
SEQRES  48 C 1001  ASN VAL ASN MET TYR LEU SER SER PRO ASN PHE LEU GLU          
SEQRES  49 C 1001  THR SER LEU LYS THR SER SER ASN PRO ARG GLU VAL LEU          
SEQRES  50 C 1001  GLU ASN ILE ARG ASP TYR LEU VAL THR GLU LYS PRO LEU          
SEQRES  51 C 1001  SER PHE GLU GLU CYS ILE MET TRP ALA ARG LEU GLN PHE          
SEQRES  52 C 1001  ASP LYS PHE PHE ASN ASN ASN ILE GLN GLN LEU LEU PHE          
SEQRES  53 C 1001  ASN PHE PRO LYS ASP SER VAL THR SER THR GLY GLN PRO          
SEQRES  54 C 1001  PHE TRP SER GLY PRO LYS ARG ALA PRO THR PRO LEU SER          
SEQRES  55 C 1001  PHE ASP ILE HIS ASN ARG GLU HIS PHE ASP PHE ILE VAL          
SEQRES  56 C 1001  ALA ALA ALA SER LEU TYR ALA PHE ASN TYR GLY LEU LYS          
SEQRES  57 C 1001  SER GLU THR ASP PRO ALA ILE TYR GLU ARG VAL LEU ALA          
SEQRES  58 C 1001  GLY TYR ASN PRO PRO PRO PHE ALA PRO LYS SER GLY ILE          
SEQRES  59 C 1001  LYS ILE GLN VAL ASN GLU ASN GLU GLU ALA PRO GLU THR          
SEQRES  60 C 1001  ALA ALA ASN LYS ASP LYS GLN GLU LEU LYS SER ILE ALA          
SEQRES  61 C 1001  ASP SER LEU PRO PRO PRO SER SER LEU VAL GLY PHE ARG          
SEQRES  62 C 1001  LEU THR PRO ALA GLU PHE GLU LYS ASP ASP ASP SER ASN          
SEQRES  63 C 1001  HIS HIS ILE ASP PHE ILE THR ALA ALA SER ASN LEU ARG          
SEQRES  64 C 1001  ALA MET ASN TYR ASP ILE THR PRO ALA ASP ARG PHE LYS          
SEQRES  65 C 1001  THR LYS PHE VAL ALA GLY LYS ILE VAL PRO ALA MET CYS          
SEQRES  66 C 1001  THR SER THR ALA VAL VAL SER GLY LEU VAL CYS LEU GLU          
SEQRES  67 C 1001  LEU VAL LYS LEU VAL ASP GLY LYS LYS LYS ILE GLU GLU          
SEQRES  68 C 1001  TYR LYS ASN GLY PHE PHE ASN LEU ALA ILE GLY LEU PHE          
SEQRES  69 C 1001  THR PHE SER ASP PRO ILE ALA SER PRO LYS MET LYS VAL          
SEQRES  70 C 1001  ASN GLY LYS GLU ILE ASP LYS ILE TRP ASP ARG TYR ASN          
SEQRES  71 C 1001  LEU PRO ASP CYS THR LEU GLN GLU LEU ILE ASP TYR PHE          
SEQRES  72 C 1001  GLN LYS GLU GLU GLY LEU GLU VAL THR MET LEU SER SER          
SEQRES  73 C 1001  GLY VAL SER LEU LEU TYR ALA ASN PHE GLN PRO PRO LYS          
SEQRES  74 C 1001  LYS LEU ALA GLU ARG LEU PRO LEU LYS ILE SER GLU LEU          
SEQRES  75 C 1001  VAL GLU GLN ILE THR LYS LYS LYS LEU GLU PRO PHE ARG          
SEQRES  76 C 1001  LYS HIS LEU VAL LEU GLU ILE CYS CYS ASP ASP ALA ASN          
SEQRES  77 C 1001  GLY GLU ASP VAL GLU VAL PRO PHE ILE CYS ILE LYS LEU          
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 CYS GLY GLY                  
HET     MG  A1101       1                                                       
HET     MG  A1102       1                                                       
HET    POP  A1103       9                                                       
HET    POP  A1104       9                                                       
HET    SO4  A1105       5                                                       
HET    SO4  A1106       5                                                       
HET    SO4  A1107       5                                                       
HET    SO4  A1108       5                                                       
HET    SO4  A1109       5                                                       
HET    EDO  A1110       4                                                       
HET    JZU  B 101      23                                                       
HET     MG  C1101       1                                                       
HET     MG  C1102       1                                                       
HET    POP  C1103       9                                                       
HET    SO4  C1104       5                                                       
HET    SO4  C1105       5                                                       
HET    EDO  C1106       4                                                       
HET    JZU  D 101      23                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     POP PYROPHOSPHATE 2-                                                 
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     JZU 5'-DEOXY-5'-(SULFAMOYLAMINO)ADENOSINE                            
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5   MG    4(MG 2+)                                                     
FORMUL   7  POP    3(H2 O7 P2 2-)                                               
FORMUL   9  SO4    7(O4 S 2-)                                                   
FORMUL  14  EDO    2(C2 H6 O2)                                                  
FORMUL  15  JZU    2(C10 H15 N7 O5 S)                                           
FORMUL  23  HOH   *289(H2 O)                                                    
HELIX    1 AA1 ASP A   16  GLY A   28  1                                  13    
HELIX    2 AA2 GLY A   28  SER A   36  1                                   9    
HELIX    3 AA3 LYS A   46  GLY A   60  1                                  15    
HELIX    4 AA4 ARG A   73  SER A   79  5                                   7    
HELIX    5 AA5 THR A   84  ILE A   88  5                                   5    
HELIX    6 AA6 PRO A   91  ALA A  101  1                                  11    
HELIX    7 AA7 THR A  117  PHE A  123  5                                   7    
HELIX    8 AA8 SER A  132  ASN A  146  1                                  15    
HELIX    9 AA9 MET A  218  GLY A  224  5                                   7    
HELIX   10 AB1 VAL A  242  GLY A  246  5                                   5    
HELIX   11 AB2 SER A  267  LEU A  272  1                                   6    
HELIX   12 AB3 ASP A  281  MET A  285  5                                   5    
HELIX   13 AB4 MET A  286  HIS A  305  1                                  20    
HELIX   14 AB5 ASN A  314  LEU A  332  1                                  19    
HELIX   15 AB6 ASP A  339  GLN A  349  1                                  11    
HELIX   16 AB7 LEU A  354  SER A  375  1                                  22    
HELIX   17 AB8 LEU A  389  LEU A  392  5                                   4    
HELIX   18 AB9 TYR A  410  GLY A  418  1                                   9    
HELIX   19 AC1 GLY A  418  SER A  427  1                                  10    
HELIX   20 AC2 GLY A  436  GLY A  450  1                                  15    
HELIX   21 AC3 GLU A  468  ARG A  474  5                                   7    
HELIX   22 AC4 ARG A  479  VAL A  483  5                                   5    
HELIX   23 AC5 LEU A  486  ASN A  499  1                                  14    
HELIX   24 AC6 PRO A  500  THR A  503  5                                   4    
HELIX   25 AC7 GLY A  514  GLU A  518  5                                   5    
HELIX   26 AC8 GLY A  522  LYS A  528  1                                   7    
HELIX   27 AC9 ASN A  538  PHE A  552  1                                  15    
HELIX   28 AD1 SER A  578  SER A  582  5                                   5    
HELIX   29 AD2 PRO A  591  ASN A  597  1                                   7    
HELIX   30 AD3 ARG A  601  LYS A  618  1                                  18    
HELIX   31 AD4 LYS A  618  SER A  630  1                                  13    
HELIX   32 AD5 ASN A  632  SER A  641  1                                  10    
HELIX   33 AD6 ASN A  643  VAL A  656  1                                  14    
HELIX   34 AD7 SER A  662  ASN A  679  1                                  18    
HELIX   35 AD8 ASN A  679  PHE A  689  1                                  11    
HELIX   36 AD9 ASN A  718  GLY A  737  1                                  20    
HELIX   37 AE1 ASP A  743  ALA A  752  1                                  10    
HELIX   38 AE2 LYS A  784  SER A  793  1                                  10    
HELIX   39 AE3 PRO A  796  LEU A  800  5                                   5    
HELIX   40 AE4 HIS A  818  TYR A  834  1                                  17    
HELIX   41 AE5 ASP A  840  LYS A  850  1                                  11    
HELIX   42 AE6 MET A  855  ASP A  875  1                                  21    
HELIX   43 AE7 LYS A  879  TYR A  883  5                                   5    
HELIX   44 AE8 THR A  926  GLY A  939  1                                  14    
HELIX   45 AE9 PRO A  958  GLU A  964  1                                   7    
HELIX   46 AF1 LYS A  969  LYS A  979  1                                  11    
HELIX   47 AF2 THR B   22  GLY B   35  1                                  14    
HELIX   48 AF3 PRO B   37  GLN B   41  5                                   5    
HELIX   49 AF4 LEU B   56  ASN B   60  5                                   5    
HELIX   50 AF5 TYR C   20  GLY C   28  1                                   9    
HELIX   51 AF6 GLY C   28  GLN C   37  1                                  10    
HELIX   52 AF7 LYS C   46  GLY C   60  1                                  15    
HELIX   53 AF8 ARG C   73  SER C   79  5                                   7    
HELIX   54 AF9 THR C   84  ILE C   88  5                                   5    
HELIX   55 AG1 PRO C   91  ALA C  101  1                                  11    
HELIX   56 AG2 SER C  116  PHE C  123  5                                   8    
HELIX   57 AG3 SER C  132  ASN C  146  1                                  15    
HELIX   58 AG4 MET C  218  ASP C  223  5                                   6    
HELIX   59 AG5 SER C  267  ASP C  274  1                                   8    
HELIX   60 AG6 ASP C  281  MET C  285  5                                   5    
HELIX   61 AG7 ARG C  287  HIS C  305  1                                  19    
HELIX   62 AG8 ASN C  314  LEU C  332  1                                  19    
HELIX   63 AG9 ASP C  339  GLN C  349  1                                  11    
HELIX   64 AH1 LEU C  354  SER C  375  1                                  22    
HELIX   65 AH2 LEU C  389  LEU C  392  5                                   4    
HELIX   66 AH3 TYR C  410  GLY C  418  1                                   9    
HELIX   67 AH4 GLY C  418  SER C  427  1                                  10    
HELIX   68 AH5 GLY C  436  GLY C  450  1                                  15    
HELIX   69 AH6 LYS C  469  ARG C  474  5                                   6    
HELIX   70 AH7 ARG C  479  VAL C  483  5                                   5    
HELIX   71 AH8 LEU C  486  ASN C  499  1                                  14    
HELIX   72 AH9 PRO C  500  THR C  503  5                                   4    
HELIX   73 AI1 GLY C  514  GLU C  518  5                                   5    
HELIX   74 AI2 GLY C  522  LYS C  528  1                                   7    
HELIX   75 AI3 ASN C  538  PHE C  552  1                                  15    
HELIX   76 AI4 SER C  578  SER C  582  5                                   5    
HELIX   77 AI5 PRO C  591  ASN C  597  1                                   7    
HELIX   78 AI6 ARG C  601  LYS C  618  1                                  18    
HELIX   79 AI7 LYS C  618  LEU C  628  1                                  11    
HELIX   80 AI8 ASN C  632  SER C  641  1                                  10    
HELIX   81 AI9 ASN C  643  TYR C  654  1                                  12    
HELIX   82 AJ1 SER C  662  ASN C  679  1                                  18    
HELIX   83 AJ2 ASN C  679  PHE C  689  1                                  11    
HELIX   84 AJ3 ASN C  718  GLY C  737  1                                  20    
HELIX   85 AJ4 ASP C  743  ALA C  752  1                                  10    
HELIX   86 AJ5 LYS C  782  ILE C  790  1                                   9    
HELIX   87 AJ6 ALA C  791  SER C  793  5                                   3    
HELIX   88 AJ7 HIS C  818  TYR C  834  1                                  17    
HELIX   89 AJ8 ASP C  840  LYS C  850  1                                  11    
HELIX   90 AJ9 MET C  855  ASP C  875  1                                  21    
HELIX   91 AK1 LYS C  879  TYR C  883  5                                   5    
HELIX   92 AK2 THR C  926  GLU C  937  1                                  12    
HELIX   93 AK3 PRO C  958  GLU C  964  1                                   7    
HELIX   94 AK4 LYS C  969  LYS C  979  1                                  11    
HELIX   95 AK5 THR D   22  GLY D   35  1                                  14    
HELIX   96 AK6 PRO D   37  GLN D   41  5                                   5    
HELIX   97 AK7 THR D   55  ASN D   60  5                                   6    
SHEET    1 AA1 8 VAL A 109  VAL A 111  0                                        
SHEET    2 AA1 8 SER A  63  TYR A  67  1  N  LEU A  66   O  SER A 110           
SHEET    3 AA1 8 ASN A  39  ILE A  43  1  N  ILE A  42   O  THR A  65           
SHEET    4 AA1 8 CYS A 125  VAL A 128  1  O  VAL A 127   N  LEU A  41           
SHEET    5 AA1 8 ALA A 149  ARG A 156  1  O  ILE A 151   N  VAL A 128           
SHEET    6 AA1 8 PHE A 159  ASP A 165 -1  O  PHE A 159   N  ARG A 156           
SHEET    7 AA1 8 TYR A 383  ASP A 387 -1  O  PHE A 384   N  ILE A 162           
SHEET    8 AA1 8 TYR A 277  VAL A 278  1  N  VAL A 278   O  TYR A 383           
SHEET    1 AA2 2 PHE A 170  CYS A 172  0                                        
SHEET    2 AA2 2 THR A 261  ILE A 263 -1  O  ILE A 263   N  PHE A 170           
SHEET    1 AA3 7 ARG A 227  LYS A 228  0                                        
SHEET    2 AA3 7 PHE A 209  THR A 213 -1  N  VAL A 210   O  ARG A 227           
SHEET    3 AA3 7 VAL A 253  VAL A 257 -1  O  VAL A 257   N  PHE A 209           
SHEET    4 AA3 7 THR A 182  THR A 189 -1  N  GLY A 183   O  PHE A 254           
SHEET    5 AA3 7 VAL A 193  MET A 196 -1  O  THR A 195   N  ALA A 186           
SHEET    6 AA3 7 THR A 236  SER A 238 -1  O  PHE A 237   N  VAL A 194           
SHEET    7 AA3 7 GLU A 230  GLY A 233 -1  N  GLU A 230   O  SER A 238           
SHEET    1 AA4 5 ARG A 227  LYS A 228  0                                        
SHEET    2 AA4 5 PHE A 209  THR A 213 -1  N  VAL A 210   O  ARG A 227           
SHEET    3 AA4 5 VAL A 253  VAL A 257 -1  O  VAL A 257   N  PHE A 209           
SHEET    4 AA4 5 THR A 182  THR A 189 -1  N  GLY A 183   O  PHE A 254           
SHEET    5 AA4 5 ALA A 248  TYR A 250 -1  O  GLY A 249   N  ILE A 188           
SHEET    1 AA5 8 ILE A 506  TYR A 509  0                                        
SHEET    2 AA5 8 HIS A 458  THR A 462  1  N  VAL A 461   O  TYR A 509           
SHEET    3 AA5 8 SER A 429  VAL A 433  1  N  LEU A 432   O  SER A 460           
SHEET    4 AA5 8 LEU A 531  ASN A 534  1  O  THR A 533   N  PHE A 431           
SHEET    5 AA5 8 LEU A 556  LEU A 562  1  O  LEU A 557   N  ASN A 534           
SHEET    6 AA5 8 LYS A 565  VAL A 571 -1  O  LYS A 565   N  LEU A 562           
SHEET    7 AA5 8 ASN A 885  ASN A 889 -1  O  GLY A 886   N  THR A 568           
SHEET    8 AA5 8 LEU A 894  SER A 898 -1  O  SER A 898   N  ASN A 885           
SHEET    1 AA6 2 LYS A 905  VAL A 908  0                                        
SHEET    2 AA6 2 LYS A 911  ASP A 914 -1  O  ILE A 913   N  MET A 906           
SHEET    1 AA7 5 TYR A 920  PRO A 923  0                                        
SHEET    2 AA7 5 ILE A1008  LYS A1011  1  O  CYS A1009   N  TYR A 920           
SHEET    3 AA7 5 HIS A 988  ASP A 996 -1  N  LEU A 989   O  ILE A1010           
SHEET    4 AA7 5 GLU A 941  SER A 947 -1  N  THR A 943   O  CYS A 994           
SHEET    5 AA7 5 SER A 950  ALA A 954 -1  O  SER A 950   N  SER A 947           
SHEET    1 AA8 4 TYR A 920  PRO A 923  0                                        
SHEET    2 AA8 4 ILE A1008  LYS A1011  1  O  CYS A1009   N  TYR A 920           
SHEET    3 AA8 4 HIS A 988  ASP A 996 -1  N  LEU A 989   O  ILE A1010           
SHEET    4 AA8 4 ASP A1002  VAL A1003 -1  O  VAL A1003   N  CYS A 995           
SHEET    1 AA9 5 THR B  12  GLU B  16  0                                        
SHEET    2 AA9 5 GLN B   2  THR B   7 -1  N  VAL B   5   O  ILE B  13           
SHEET    3 AA9 5 THR B  66  VAL B  70  1  O  LEU B  67   N  PHE B   4           
SHEET    4 AA9 5 ARG B  42  PHE B  45 -1  N  ARG B  42   O  VAL B  70           
SHEET    5 AA9 5 LYS B  48  GLN B  49 -1  O  LYS B  48   N  PHE B  45           
SHEET    1 AB1 7 VAL C 109  VAL C 111  0                                        
SHEET    2 AB1 7 SER C  63  TYR C  67  1  N  LEU C  66   O  SER C 110           
SHEET    3 AB1 7 ASN C  39  ILE C  43  1  N  ILE C  42   O  THR C  65           
SHEET    4 AB1 7 CYS C 125  THR C 129  1  O  VAL C 127   N  LEU C  41           
SHEET    5 AB1 7 ALA C 149  ARG C 156  1  O  ILE C 151   N  VAL C 128           
SHEET    6 AB1 7 PHE C 159  ASP C 165 -1  O  PHE C 163   N  ALA C 152           
SHEET    7 AB1 7 TYR C 383  ASP C 387 -1  O  PHE C 386   N  GLY C 160           
SHEET    1 AB2 2 PHE C 170  CYS C 172  0                                        
SHEET    2 AB2 2 THR C 261  ILE C 263 -1  O  ILE C 263   N  PHE C 170           
SHEET    1 AB3 7 ARG C 227  LYS C 228  0                                        
SHEET    2 AB3 7 PHE C 209  THR C 213 -1  N  VAL C 210   O  ARG C 227           
SHEET    3 AB3 7 VAL C 253  GLN C 256 -1  O  THR C 255   N  LYS C 211           
SHEET    4 AB3 7 THR C 182  THR C 189 -1  N  GLY C 183   O  PHE C 254           
SHEET    5 AB3 7 VAL C 193  MET C 196 -1  O  THR C 195   N  ALA C 186           
SHEET    6 AB3 7 THR C 236  SER C 238 -1  O  PHE C 237   N  VAL C 194           
SHEET    7 AB3 7 GLU C 230  VAL C 231 -1  N  GLU C 230   O  SER C 238           
SHEET    1 AB4 5 ARG C 227  LYS C 228  0                                        
SHEET    2 AB4 5 PHE C 209  THR C 213 -1  N  VAL C 210   O  ARG C 227           
SHEET    3 AB4 5 VAL C 253  GLN C 256 -1  O  THR C 255   N  LYS C 211           
SHEET    4 AB4 5 THR C 182  THR C 189 -1  N  GLY C 183   O  PHE C 254           
SHEET    5 AB4 5 ALA C 248  TYR C 250 -1  O  GLY C 249   N  ILE C 188           
SHEET    1 AB5 8 ILE C 506  TYR C 509  0                                        
SHEET    2 AB5 8 HIS C 458  THR C 462  1  N  ILE C 459   O  THR C 507           
SHEET    3 AB5 8 SER C 429  VAL C 433  1  N  LEU C 432   O  SER C 460           
SHEET    4 AB5 8 LEU C 531  ASN C 534  1  O  THR C 533   N  PHE C 431           
SHEET    5 AB5 8 LEU C 556  LEU C 562  1  O  LEU C 557   N  VAL C 532           
SHEET    6 AB5 8 LYS C 565  VAL C 571 -1  O  GLN C 569   N  GLU C 558           
SHEET    7 AB5 8 ASN C 885  ASN C 889 -1  O  GLY C 886   N  THR C 568           
SHEET    8 AB5 8 LEU C 894  SER C 898 -1  O  SER C 898   N  ASN C 885           
SHEET    1 AB6 2 LYS C 905  VAL C 908  0                                        
SHEET    2 AB6 2 LYS C 911  ASP C 914 -1  O  ILE C 913   N  MET C 906           
SHEET    1 AB7 5 ARG C 919  PRO C 923  0                                        
SHEET    2 AB7 5 PHE C1007  LYS C1011  1  O  CYS C1009   N  TYR C 920           
SHEET    3 AB7 5 HIS C 988  ASP C 996 -1  N  LEU C 989   O  ILE C1010           
SHEET    4 AB7 5 GLU C 941  SER C 947 -1  N  THR C 943   O  CYS C 994           
SHEET    5 AB7 5 SER C 950  ALA C 954 -1  O  LEU C 952   N  LEU C 945           
SHEET    1 AB8 4 ARG C 919  PRO C 923  0                                        
SHEET    2 AB8 4 PHE C1007  LYS C1011  1  O  CYS C1009   N  TYR C 920           
SHEET    3 AB8 4 HIS C 988  ASP C 996 -1  N  LEU C 989   O  ILE C1010           
SHEET    4 AB8 4 ASP C1002  VAL C1003 -1  O  VAL C1003   N  CYS C 995           
SHEET    1 AB9 5 THR D  12  GLU D  16  0                                        
SHEET    2 AB9 5 GLN D   2  THR D   7 -1  N  VAL D   5   O  ILE D  13           
SHEET    3 AB9 5 SER D  65  VAL D  70  1  O  LEU D  67   N  PHE D   4           
SHEET    4 AB9 5 ARG D  42  PHE D  45 -1  N  ILE D  44   O  HIS D  68           
SHEET    5 AB9 5 LYS D  48  GLN D  49 -1  O  LYS D  48   N  PHE D  45           
LINK         OD2 ASP A 465                MG    MG A1102     1555   1555  2.06  
LINK         OD2 ASP A 537                MG    MG A1101     1555   1555  2.08  
LINK         C   GLY B  76                 N18 JZU B 101     1555   1555  1.35  
LINK         OD2 ASP C 465                MG    MG C1102     1555   1555  2.13  
LINK         OD2 ASP C 537                MG    MG C1101     1555   1555  2.08  
LINK         C   GLY D  76                 N18 JZU D 101     1555   1555  1.34  
LINK        MG    MG A1101                 O6  POP A1103     1555   1555  2.26  
LINK        MG    MG A1101                 O2S JZU B 101     1555   1555  2.10  
LINK        MG    MG A1101                 O2  POP A1103     1555   1555  2.07  
LINK        MG    MG A1101                 O   HOH A1262     1555   1555  2.05  
LINK        MG    MG A1101                 O   HOH A1293     1555   1555  2.11  
LINK        MG    MG A1102                 O   HOH A1217     1555   1555  2.12  
LINK        MG    MG A1102                 O   HOH A1246     1555   1555  2.33  
LINK        MG    MG A1102                 O4  POP A1103     1555   1555  2.08  
LINK        MG    MG A1102                 O   HOH A1225     1555   1555  2.09  
LINK        MG    MG A1102                 O   HOH A1230     1555   1555  2.14  
LINK        MG    MG C1101                 O   HOH C1210     1555   1555  2.21  
LINK        MG    MG C1101                 O1  POP C1103     1555   1555  2.16  
LINK        MG    MG C1101                 O4  POP C1103     1555   1555  2.35  
LINK        MG    MG C1101                 O2S JZU D 101     1555   1555  2.32  
LINK        MG    MG C1101                 O   HOH C1203     1555   1555  2.23  
LINK        MG    MG C1102                 O6  POP C1103     1555   1555  2.45  
CISPEP   1 LYS A  381    GLN A  382          0        -2.62                     
CISPEP   2 LYS C  381    GLN C  382          0        -1.23                     
SITE     1 AC1  5 ASP A 537  POP A1103  HOH A1262  HOH A1293                    
SITE     2 AC1  5 JZU B 101                                                     
SITE     1 AC2  6 ASP A 465  POP A1103  HOH A1217  HOH A1225                    
SITE     2 AC2  6 HOH A1230  HOH A1246                                          
SITE     1 AC3 17 ARG A  22  ASP A 465  ASN A 471  ARG A 474                    
SITE     2 AC3 17 GLN A 475  LYS A 487  ASP A 537   MG A1101                    
SITE     3 AC3 17  MG A1102  HOH A1217  HOH A1220  HOH A1225                    
SITE     4 AC3 17 HOH A1230  HOH A1262  HOH A1293  HOH A1313                    
SITE     5 AC3 17 JZU B 101                                                     
SITE     1 AC4  4 GLY A  28  HIS A  29  GLU A  30  HOH A1222                    
SITE     1 AC5  5 ARG A 986  HIS A 988  VAL A 990  HOH A1202                    
SITE     2 AC5  5 HOH A1204                                                     
SITE     1 AC6  4 HIS A 147  GLY A 167  GLU A 168  ASN A 169                    
SITE     1 AC7  3 THR A  14  ILE A  15  HIS A  29                               
SITE     1 AC8  3 ASN A  39  THR A  65  PHE A 123                               
SITE     1 AC9  2 LYS A 216  GLY A 217                                          
SITE     1 AD1  3 ASP A 840  ARG A 841  PHE A 842                               
SITE     1 AD2 18 ALA A 437  ASP A 463  ASP A 465  ARG A 474                    
SITE     2 AD2 18 GLN A 475  LYS A 487  ARG A 512  VAL A 513                    
SITE     3 AD2 18 ALA A 535  LEU A 536  ASP A 537  ASN A 538                    
SITE     4 AD2 18 ALA A 541   MG A1101  POP A1103  HOH A1293                    
SITE     5 AD2 18 GLY B  76  HOH B 210                                          
SITE     1 AD3  5 ASP C 537  POP C1103  HOH C1203  HOH C1210                    
SITE     2 AD3  5 JZU D 101                                                     
SITE     1 AD4  3 ASP C 465  GLU C 468  POP C1103                               
SITE     1 AD5 12 ARG C  22  ASP C 465  ASN C 471  ARG C 474                    
SITE     2 AD5 12 GLN C 475  LYS C 487  ASP C 537   MG C1101                    
SITE     3 AD5 12  MG C1102  HOH C1203  HOH C1210  JZU D 101                    
SITE     1 AD6  2 TYR C 544  ARG C 547                                          
SITE     1 AD7  4 GLU C 518  ARG C 986  LYS C 987  HIS C 988                    
SITE     1 AD8  2 HIS C  29  PHE C 842                                          
CRYST1  182.061  114.616  125.967  90.00  90.00  90.00 P 21 21 2     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      0.005493  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008725  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007939        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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