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Database: PDB
Entry: 5D2M
LinkDB: 5D2M
Original site: 5D2M 
HEADER    LIGASE,PROTEIN BINDING                  05-AUG-15   5D2M              
TITLE     COMPLEX BETWEEN HUMAN SUMO2-RANGAP1, UBC9 AND ZNF451                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUMO-CONJUGATING ENZYME UBC9;                              
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 SYNONYM: SUMO-PROTEIN LIGASE,UBIQUITIN CARRIER PROTEIN 9,UBIQUITIN   
COMPND   5 CARRIER PROTEIN I,UBIQUITIN-CONJUGATING ENZYME E2 I,UBIQUITIN-PROTEIN
COMPND   6 LIGASE I,P18;                                                        
COMPND   7 EC: 6.3.2.-;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: SMALL UBIQUITIN-RELATED MODIFIER 2;                        
COMPND  12 CHAIN: B, E;                                                         
COMPND  13 FRAGMENT: UNP RESIDUES 15-93;                                        
COMPND  14 SYNONYM: SUMO-2,HSMT3,SMT3 HOMOLOG 2,SUMO-3,SENTRIN-2,UBIQUITIN-LIKE 
COMPND  15 PROTEIN SMT3B,SMT3B;                                                 
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: RAN GTPASE-ACTIVATING PROTEIN 1;                           
COMPND  19 CHAIN: C, F;                                                         
COMPND  20 FRAGMENT: UNP RESIDUES 418-587;                                      
COMPND  21 SYNONYM: RANGAP1;                                                    
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 MOL_ID: 4;                                                           
COMPND  24 MOLECULE: ZINC FINGER PROTEIN 451;                                   
COMPND  25 CHAIN: G;                                                            
COMPND  26 FRAGMENT: UNP RESIDUES 2-56;                                         
COMPND  27 SYNONYM: COACTIVATOR FOR STEROID RECEPTORS;                          
COMPND  28 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: UBE2I, UBC9, UBCE9;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28B;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: SUMO2, SMT3B, SMT3H2;                                          
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET28B;                                   
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 GENE: RANGAP1, KIAA1835, SD;                                         
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PSMT3;                                    
SOURCE  28 MOL_ID: 4;                                                           
SOURCE  29 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  30 ORGANISM_COMMON: HUMAN;                                              
SOURCE  31 ORGANISM_TAXID: 9606;                                                
SOURCE  32 GENE: ZNF451, COASTER, KIAA0576, KIAA1702;                           
SOURCE  33 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  34 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  35 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  36 EXPRESSION_SYSTEM_PLASMID: PLOU3                                     
KEYWDS    COMPLEX, SUMO, E3 LIGASE, LIGASE, PROTEIN BINDING                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.CAPPADOCIA,C.D.LIMA                                                 
REVDAT   6   25-DEC-19 5D2M    1       REMARK                                   
REVDAT   5   01-NOV-17 5D2M    1       REMARK                                   
REVDAT   4   27-SEP-17 5D2M    1       REMARK                                   
REVDAT   3   16-DEC-15 5D2M    1       JRNL                                     
REVDAT   2   18-NOV-15 5D2M    1       JRNL                                     
REVDAT   1   04-NOV-15 5D2M    0                                                
JRNL        AUTH   L.CAPPADOCIA,A.PICHLER,C.D.LIMA                              
JRNL        TITL   STRUCTURAL BASIS FOR CATALYTIC ACTIVATION BY THE HUMAN       
JRNL        TITL 2 ZNF451 SUMO E3 LIGASE.                                       
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  22   968 2015              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   26524494                                                     
JRNL        DOI    10.1038/NSMB.3116                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.35                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 46759                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.320                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1554                            
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 46.3576 -  5.3352    0.99     4342   150  0.1803 0.1940        
REMARK   3     2  5.3352 -  4.2356    1.00     4178   143  0.1564 0.1952        
REMARK   3     3  4.2356 -  3.7005    1.00     4154   143  0.1676 0.2373        
REMARK   3     4  3.7005 -  3.3622    1.00     4115   142  0.1740 0.1958        
REMARK   3     5  3.3622 -  3.1213    1.00     4103   140  0.1937 0.2159        
REMARK   3     6  3.1213 -  2.9373    1.00     4101   141  0.2034 0.2508        
REMARK   3     7  2.9373 -  2.7902    1.00     4083   140  0.2024 0.2564        
REMARK   3     8  2.7902 -  2.6688    1.00     4091   140  0.2115 0.2520        
REMARK   3     9  2.6688 -  2.5661    1.00     4070   141  0.2205 0.2787        
REMARK   3    10  2.5661 -  2.4775    1.00     4078   139  0.2366 0.2942        
REMARK   3    11  2.4775 -  2.4000    0.96     3890   135  0.2531 0.2802        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.850           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.003           6594                                  
REMARK   3   ANGLE     :  0.743           8923                                  
REMARK   3   CHIRALITY :  0.029            987                                  
REMARK   3   PLANARITY :  0.003           1161                                  
REMARK   3   DIHEDRAL  : 12.186           2526                                  
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 1 THROUGH 157 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5053   6.9412  10.9547              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0880 T22:   0.0965                                     
REMARK   3      T33:   0.0978 T12:  -0.3702                                     
REMARK   3      T13:   0.1019 T23:   0.0910                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3595 L22:   0.5402                                     
REMARK   3      L33:   1.0876 L12:   0.0768                                     
REMARK   3      L13:  -0.0996 L23:   0.1952                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0408 S12:  -0.0917 S13:   0.1763                       
REMARK   3      S21:   0.0378 S22:   0.0373 S23:  -0.1277                       
REMARK   3      S31:  -0.2952 S32:   0.2350 S33:  -0.0092                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 93 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -32.9702  13.7146  13.9639              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4872 T22:   0.5585                                     
REMARK   3      T33:   0.4595 T12:   0.2193                                     
REMARK   3      T13:  -0.0210 T23:   0.0554                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6948 L22:   0.1509                                     
REMARK   3      L33:   0.2770 L12:  -0.3192                                     
REMARK   3      L13:  -0.2270 L23:   0.0515                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0278 S12:   0.1515 S13:   0.1426                       
REMARK   3      S21:  -0.1066 S22:   0.0125 S23:   0.2617                       
REMARK   3      S31:  -0.1158 S32:  -0.2681 S33:   0.0015                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 430 THROUGH 587 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4228  10.9323 -20.2206              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0532 T22:   0.1803                                     
REMARK   3      T33:  -0.0207 T12:  -0.4318                                     
REMARK   3      T13:   0.1438 T23:   0.4028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8733 L22:   0.3573                                     
REMARK   3      L33:   0.7670 L12:   0.2161                                     
REMARK   3      L13:  -0.2556 L23:  -0.1521                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0260 S12:  -0.2451 S13:   0.0053                       
REMARK   3      S21:   0.2182 S22:  -0.1565 S23:  -0.2180                       
REMARK   3      S31:  -0.0131 S32:   0.3671 S33:   0.0352                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 157 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -31.8470 -22.3788  17.8587              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1885 T22:   0.0509                                     
REMARK   3      T33:   0.1686 T12:  -0.1185                                     
REMARK   3      T13:   0.0556 T23:  -0.1287                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6809 L22:   0.5906                                     
REMARK   3      L33:   1.2438 L12:   0.0776                                     
REMARK   3      L13:  -0.1700 L23:  -0.1345                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0307 S12:  -0.0851 S13:  -0.1601                       
REMARK   3      S21:   0.1258 S22:  -0.1294 S23:   0.0124                       
REMARK   3      S31:   0.2471 S32:  -0.1900 S33:   0.0167                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 14 THROUGH 93 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -13.7343  -7.1747  32.7257              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1704 T22:   0.1843                                     
REMARK   3      T33:   0.1800 T12:  -0.0503                                     
REMARK   3      T13:  -0.0130 T23:  -0.0156                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1097 L22:   0.5319                                     
REMARK   3      L33:   0.9441 L12:   0.1398                                     
REMARK   3      L13:   0.3909 L23:  -0.0580                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0063 S12:  -0.0519 S13:  -0.0739                       
REMARK   3      S21:   0.0535 S22:   0.0172 S23:  -0.1227                       
REMARK   3      S31:   0.0534 S32:   0.1720 S33:  -0.0349                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 431 THROUGH 587 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -25.3614 -27.1408 -15.9448              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1067 T22:   0.1881                                     
REMARK   3      T33:   0.2010 T12:  -0.0054                                     
REMARK   3      T13:   0.0250 T23:  -0.0994                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5983 L22:   0.6760                                     
REMARK   3      L33:   1.0966 L12:  -0.1433                                     
REMARK   3      L13:  -0.0946 L23:   0.3645                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0682 S12:   0.2599 S13:  -0.1156                       
REMARK   3      S21:  -0.0466 S22:  -0.1440 S23:   0.1363                       
REMARK   3      S31:   0.0268 S32:  -0.0975 S33:   0.0199                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 30 THROUGH 39 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -36.0168  15.2745  25.6413              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3997 T22:   0.4162                                     
REMARK   3      T33:   0.3804 T12:   0.0762                                     
REMARK   3      T13:   0.0427 T23:  -0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1261 L22:   0.5827                                     
REMARK   3      L33:   0.3387 L12:  -0.8111                                     
REMARK   3      L13:  -0.6179 L23:   0.4448                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0045 S12:   0.2949 S13:   0.5683                       
REMARK   3      S21:  -0.2064 S22:  -0.0961 S23:   0.0600                       
REMARK   3      S31:  -0.2981 S32:  -0.2203 S33:   0.0965                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 40 THROUGH 50 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -22.3303  -2.8635  38.6439              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1003 T22:   0.0796                                     
REMARK   3      T33:   0.0901 T12:  -0.0679                                     
REMARK   3      T13:   0.0150 T23:  -0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5526 L22:   1.6996                                     
REMARK   3      L33:   1.0187 L12:   0.5258                                     
REMARK   3      L13:  -1.0532 L23:   0.7478                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0092 S12:  -0.2084 S13:  -0.1137                       
REMARK   3      S21:   0.1974 S22:   0.0680 S23:  -0.0800                       
REMARK   3      S31:   0.0656 S32:  -0.0695 S33:  -0.0423                       
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 5D2M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211979.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-MAY-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46766                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.350                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51430                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.830                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 3UIO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6 % (W/V) PEG 8000, 0.2 M AMMONIUM       
REMARK 280  CITRATE AND 0.1 M HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       39.12000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.49000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.53000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.49000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.12000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.53000            
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 300 REMARK: AUTHORS STATE THAT ALTHOUGH A HEPTAMERIC COMPLEX THAT        
REMARK 300 ENCOMPASSES ALL CHAINS PRESENT IN THE ASYMMETRIC UNIT WAS DETECTED   
REMARK 300 BY SIZE EXCLUSION CHROMATOGRAPHY, STRUCTURAL AND BIOCHEMICAL         
REMARK 300 ANALYSES SUGGEST THAT THE BIOLOGICAL UNIT CONSISTS OF A RANGAP1-     
REMARK 300 SUMO2/UBC9/SUMO2/ZNF451 COMPLEX COMPOSED OF CHAINS A, B, C, E AND G. 
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, G                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     SER A   158                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     HIS B    13                                                      
REMARK 465     MET B    14                                                      
REMARK 465     ASN B    15                                                      
REMARK 465     ASP B    16                                                      
REMARK 465     HIS B    17                                                      
REMARK 465     SER C   417                                                      
REMARK 465     ASN C   418                                                      
REMARK 465     THR C   419                                                      
REMARK 465     GLY C   420                                                      
REMARK 465     GLU C   421                                                      
REMARK 465     PRO C   422                                                      
REMARK 465     ALA C   423                                                      
REMARK 465     PRO C   424                                                      
REMARK 465     VAL C   425                                                      
REMARK 465     LEU C   426                                                      
REMARK 465     SER C   427                                                      
REMARK 465     SER C   428                                                      
REMARK 465     PRO C   429                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     SER D   158                                                      
REMARK 465     GLY E    11                                                      
REMARK 465     SER E    12                                                      
REMARK 465     HIS E    13                                                      
REMARK 465     SER F   417                                                      
REMARK 465     ASN F   418                                                      
REMARK 465     THR F   419                                                      
REMARK 465     GLY F   420                                                      
REMARK 465     GLU F   421                                                      
REMARK 465     PRO F   422                                                      
REMARK 465     ALA F   423                                                      
REMARK 465     PRO F   424                                                      
REMARK 465     VAL F   425                                                      
REMARK 465     LEU F   426                                                      
REMARK 465     SER F   427                                                      
REMARK 465     SER F   428                                                      
REMARK 465     PRO F   429                                                      
REMARK 465     PRO F   430                                                      
REMARK 465     GLY G    -8                                                      
REMARK 465     ALA G    -7                                                      
REMARK 465     MET G    -6                                                      
REMARK 465     ASP G    -5                                                      
REMARK 465     HIS G    -4                                                      
REMARK 465     VAL G    -3                                                      
REMARK 465     GLU G    -2                                                      
REMARK 465     PHE G    -1                                                      
REMARK 465     GLY G     0                                                      
REMARK 465     SER G     1                                                      
REMARK 465     GLY G     2                                                      
REMARK 465     ASP G     3                                                      
REMARK 465     PRO G     4                                                      
REMARK 465     GLY G     5                                                      
REMARK 465     SER G     6                                                      
REMARK 465     GLU G     7                                                      
REMARK 465     ILE G     8                                                      
REMARK 465     ILE G     9                                                      
REMARK 465     GLU G    10                                                      
REMARK 465     SER G    11                                                      
REMARK 465     VAL G    12                                                      
REMARK 465     PRO G    13                                                      
REMARK 465     PRO G    14                                                      
REMARK 465     ALA G    15                                                      
REMARK 465     GLY G    16                                                      
REMARK 465     PRO G    17                                                      
REMARK 465     GLU G    18                                                      
REMARK 465     ALA G    19                                                      
REMARK 465     SER G    20                                                      
REMARK 465     GLU G    21                                                      
REMARK 465     SER G    22                                                      
REMARK 465     THR G    23                                                      
REMARK 465     THR G    24                                                      
REMARK 465     ASP G    25                                                      
REMARK 465     GLU G    26                                                      
REMARK 465     ASN G    27                                                      
REMARK 465     GLU G    28                                                      
REMARK 465     ASP G    29                                                      
REMARK 465     SER G    51                                                      
REMARK 465     ASP G    52                                                      
REMARK 465     ASP G    53                                                      
REMARK 465     GLU G    54                                                      
REMARK 465     GLU G    55                                                      
REMARK 465     PRO G    56                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PRO C 430    CG   CD                                             
REMARK 470     MET E  14    CG   SD   CE                                        
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   HG   CYS A   138     O    HOH A   540              1.36            
REMARK 500  HH12  ARG D   141     O    HOH D   206              1.56            
REMARK 500   O    ALA C   432     HG1  THR C   436              1.59            
REMARK 500  HH11  ARG D    14     O    HOH D   204              1.60            
REMARK 500   O    HOH D   334     O    HOH D   357              2.00            
REMARK 500   O    HOH A   483     O    HOH A   491              2.01            
REMARK 500   O    HOH E   107     O    HOH E   145              2.08            
REMARK 500   O    SER A    70     O    HOH A   401              2.08            
REMARK 500   O    HOH E   151     O    HOH E   168              2.09            
REMARK 500   O    HOH E   157     O    HOH E   177              2.12            
REMARK 500   O    ILE A   107     O    HOH A   402              2.13            
REMARK 500   O    HOH C   748     O    HOH C   799              2.13            
REMARK 500   O    HOH A   463     O    HOH A   491              2.16            
REMARK 500   O    HOH C   710     O    HOH C   797              2.17            
REMARK 500   OE1  GLU E    79     O    HOH E   101              2.17            
REMARK 500   O    ASP A   102     O    HOH A   403              2.17            
REMARK 500   O    ALA C   496     O    HOH C   701              2.18            
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    LYS A 101     -105.59   -121.51                                   
REMARK 500    ASN A 140       87.11   -159.53                                   
REMARK 500    THR C 463       30.50    -88.63                                   
REMARK 500    LYS C 528       77.12     54.71                                   
REMARK 500    LYS D 101     -102.05   -139.08                                   
REMARK 500    ASN D 140       85.14   -160.80                                   
REMARK 500    ALA F 432      -37.66   -136.09                                   
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 D 364        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH D 365        DISTANCE =  6.38 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO F 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO F 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLY E 93 and LYS F     
REMARK 800  524                                                                 
DBREF  5D2M A    1   158  UNP    P63279   UBC9_HUMAN       1    158             
DBREF  5D2M B   15    93  UNP    P61956   SUMO2_HUMAN     15     93             
DBREF  5D2M C  418   587  UNP    P46060   RAGP1_HUMAN    418    587             
DBREF  5D2M D    1   158  UNP    P63279   UBC9_HUMAN       1    158             
DBREF  5D2M E   15    93  UNP    P61956   SUMO2_HUMAN     15     93             
DBREF  5D2M F  418   587  UNP    P46060   RAGP1_HUMAN    418    587             
DBREF  5D2M G    2    56  UNP    Q9Y4E5   ZN451_HUMAN      2     56             
SEQADV 5D2M GLY A   -2  UNP  P63279              EXPRESSION TAG                 
SEQADV 5D2M SER A   -1  UNP  P63279              EXPRESSION TAG                 
SEQADV 5D2M HIS A    0  UNP  P63279              EXPRESSION TAG                 
SEQADV 5D2M ARG A   14  UNP  P63279    LYS    14 ENGINEERED MUTATION            
SEQADV 5D2M GLY B   11  UNP  P61956              EXPRESSION TAG                 
SEQADV 5D2M SER B   12  UNP  P61956              EXPRESSION TAG                 
SEQADV 5D2M HIS B   13  UNP  P61956              EXPRESSION TAG                 
SEQADV 5D2M MET B   14  UNP  P61956              EXPRESSION TAG                 
SEQADV 5D2M SER C  417  UNP  P46060              EXPRESSION TAG                 
SEQADV 5D2M GLY D   -2  UNP  P63279              EXPRESSION TAG                 
SEQADV 5D2M SER D   -1  UNP  P63279              EXPRESSION TAG                 
SEQADV 5D2M HIS D    0  UNP  P63279              EXPRESSION TAG                 
SEQADV 5D2M ARG D   14  UNP  P63279    LYS    14 ENGINEERED MUTATION            
SEQADV 5D2M GLY E   11  UNP  P61956              EXPRESSION TAG                 
SEQADV 5D2M SER E   12  UNP  P61956              EXPRESSION TAG                 
SEQADV 5D2M HIS E   13  UNP  P61956              EXPRESSION TAG                 
SEQADV 5D2M MET E   14  UNP  P61956              EXPRESSION TAG                 
SEQADV 5D2M SER F  417  UNP  P46060              EXPRESSION TAG                 
SEQADV 5D2M GLY G   -8  UNP  Q9Y4E5              EXPRESSION TAG                 
SEQADV 5D2M ALA G   -7  UNP  Q9Y4E5              EXPRESSION TAG                 
SEQADV 5D2M MET G   -6  UNP  Q9Y4E5              EXPRESSION TAG                 
SEQADV 5D2M ASP G   -5  UNP  Q9Y4E5              EXPRESSION TAG                 
SEQADV 5D2M HIS G   -4  UNP  Q9Y4E5              EXPRESSION TAG                 
SEQADV 5D2M VAL G   -3  UNP  Q9Y4E5              EXPRESSION TAG                 
SEQADV 5D2M GLU G   -2  UNP  Q9Y4E5              EXPRESSION TAG                 
SEQADV 5D2M PHE G   -1  UNP  Q9Y4E5              EXPRESSION TAG                 
SEQADV 5D2M GLY G    0  UNP  Q9Y4E5              EXPRESSION TAG                 
SEQADV 5D2M SER G    1  UNP  Q9Y4E5              EXPRESSION TAG                 
SEQRES   1 A  161  GLY SER HIS MET SER GLY ILE ALA LEU SER ARG LEU ALA          
SEQRES   2 A  161  GLN GLU ARG ARG ALA TRP ARG LYS ASP HIS PRO PHE GLY          
SEQRES   3 A  161  PHE VAL ALA VAL PRO THR LYS ASN PRO ASP GLY THR MET          
SEQRES   4 A  161  ASN LEU MET ASN TRP GLU CYS ALA ILE PRO GLY LYS LYS          
SEQRES   5 A  161  GLY THR PRO TRP GLU GLY GLY LEU PHE LYS LEU ARG MET          
SEQRES   6 A  161  LEU PHE LYS ASP ASP TYR PRO SER SER PRO PRO LYS CYS          
SEQRES   7 A  161  LYS PHE GLU PRO PRO LEU PHE HIS PRO ASN VAL TYR PRO          
SEQRES   8 A  161  SER GLY THR VAL CYS LEU SER ILE LEU GLU GLU ASP LYS          
SEQRES   9 A  161  ASP TRP ARG PRO ALA ILE THR ILE LYS GLN ILE LEU LEU          
SEQRES  10 A  161  GLY ILE GLN GLU LEU LEU ASN GLU PRO ASN ILE GLN ASP          
SEQRES  11 A  161  PRO ALA GLN ALA GLU ALA TYR THR ILE TYR CYS GLN ASN          
SEQRES  12 A  161  ARG VAL GLU TYR GLU LYS ARG VAL ARG ALA GLN ALA LYS          
SEQRES  13 A  161  LYS PHE ALA PRO SER                                          
SEQRES   1 B   83  GLY SER HIS MET ASN ASP HIS ILE ASN LEU LYS VAL ALA          
SEQRES   2 B   83  GLY GLN ASP GLY SER VAL VAL GLN PHE LYS ILE LYS ARG          
SEQRES   3 B   83  HIS THR PRO LEU SER LYS LEU MET LYS ALA TYR CYS GLU          
SEQRES   4 B   83  ARG GLN GLY LEU SER MET ARG GLN ILE ARG PHE ARG PHE          
SEQRES   5 B   83  ASP GLY GLN PRO ILE ASN GLU THR ASP THR PRO ALA GLN          
SEQRES   6 B   83  LEU GLU MET GLU ASP GLU ASP THR ILE ASP VAL PHE GLN          
SEQRES   7 B   83  GLN GLN THR GLY GLY                                          
SEQRES   1 C  171  SER ASN THR GLY GLU PRO ALA PRO VAL LEU SER SER PRO          
SEQRES   2 C  171  PRO PRO ALA ASP VAL SER THR PHE LEU ALA PHE PRO SER          
SEQRES   3 C  171  PRO GLU LYS LEU LEU ARG LEU GLY PRO LYS SER SER VAL          
SEQRES   4 C  171  LEU ILE ALA GLN GLN THR ASP THR SER ASP PRO GLU LYS          
SEQRES   5 C  171  VAL VAL SER ALA PHE LEU LYS VAL SER SER VAL PHE LYS          
SEQRES   6 C  171  ASP GLU ALA THR VAL ARG MET ALA VAL GLN ASP ALA VAL          
SEQRES   7 C  171  ASP ALA LEU MET GLN LYS ALA PHE ASN SER SER SER PHE          
SEQRES   8 C  171  ASN SER ASN THR PHE LEU THR ARG LEU LEU VAL HIS MET          
SEQRES   9 C  171  GLY LEU LEU LYS SER GLU ASP LYS VAL LYS ALA ILE ALA          
SEQRES  10 C  171  ASN LEU TYR GLY PRO LEU MET ALA LEU ASN HIS MET VAL          
SEQRES  11 C  171  GLN GLN ASP TYR PHE PRO LYS ALA LEU ALA PRO LEU LEU          
SEQRES  12 C  171  LEU ALA PHE VAL THR LYS PRO ASN SER ALA LEU GLU SER          
SEQRES  13 C  171  CYS SER PHE ALA ARG HIS SER LEU LEU GLN THR LEU TYR          
SEQRES  14 C  171  LYS VAL                                                      
SEQRES   1 D  161  GLY SER HIS MET SER GLY ILE ALA LEU SER ARG LEU ALA          
SEQRES   2 D  161  GLN GLU ARG ARG ALA TRP ARG LYS ASP HIS PRO PHE GLY          
SEQRES   3 D  161  PHE VAL ALA VAL PRO THR LYS ASN PRO ASP GLY THR MET          
SEQRES   4 D  161  ASN LEU MET ASN TRP GLU CYS ALA ILE PRO GLY LYS LYS          
SEQRES   5 D  161  GLY THR PRO TRP GLU GLY GLY LEU PHE LYS LEU ARG MET          
SEQRES   6 D  161  LEU PHE LYS ASP ASP TYR PRO SER SER PRO PRO LYS CYS          
SEQRES   7 D  161  LYS PHE GLU PRO PRO LEU PHE HIS PRO ASN VAL TYR PRO          
SEQRES   8 D  161  SER GLY THR VAL CYS LEU SER ILE LEU GLU GLU ASP LYS          
SEQRES   9 D  161  ASP TRP ARG PRO ALA ILE THR ILE LYS GLN ILE LEU LEU          
SEQRES  10 D  161  GLY ILE GLN GLU LEU LEU ASN GLU PRO ASN ILE GLN ASP          
SEQRES  11 D  161  PRO ALA GLN ALA GLU ALA TYR THR ILE TYR CYS GLN ASN          
SEQRES  12 D  161  ARG VAL GLU TYR GLU LYS ARG VAL ARG ALA GLN ALA LYS          
SEQRES  13 D  161  LYS PHE ALA PRO SER                                          
SEQRES   1 E   83  GLY SER HIS MET ASN ASP HIS ILE ASN LEU LYS VAL ALA          
SEQRES   2 E   83  GLY GLN ASP GLY SER VAL VAL GLN PHE LYS ILE LYS ARG          
SEQRES   3 E   83  HIS THR PRO LEU SER LYS LEU MET LYS ALA TYR CYS GLU          
SEQRES   4 E   83  ARG GLN GLY LEU SER MET ARG GLN ILE ARG PHE ARG PHE          
SEQRES   5 E   83  ASP GLY GLN PRO ILE ASN GLU THR ASP THR PRO ALA GLN          
SEQRES   6 E   83  LEU GLU MET GLU ASP GLU ASP THR ILE ASP VAL PHE GLN          
SEQRES   7 E   83  GLN GLN THR GLY GLY                                          
SEQRES   1 F  171  SER ASN THR GLY GLU PRO ALA PRO VAL LEU SER SER PRO          
SEQRES   2 F  171  PRO PRO ALA ASP VAL SER THR PHE LEU ALA PHE PRO SER          
SEQRES   3 F  171  PRO GLU LYS LEU LEU ARG LEU GLY PRO LYS SER SER VAL          
SEQRES   4 F  171  LEU ILE ALA GLN GLN THR ASP THR SER ASP PRO GLU LYS          
SEQRES   5 F  171  VAL VAL SER ALA PHE LEU LYS VAL SER SER VAL PHE LYS          
SEQRES   6 F  171  ASP GLU ALA THR VAL ARG MET ALA VAL GLN ASP ALA VAL          
SEQRES   7 F  171  ASP ALA LEU MET GLN LYS ALA PHE ASN SER SER SER PHE          
SEQRES   8 F  171  ASN SER ASN THR PHE LEU THR ARG LEU LEU VAL HIS MET          
SEQRES   9 F  171  GLY LEU LEU LYS SER GLU ASP LYS VAL LYS ALA ILE ALA          
SEQRES  10 F  171  ASN LEU TYR GLY PRO LEU MET ALA LEU ASN HIS MET VAL          
SEQRES  11 F  171  GLN GLN ASP TYR PHE PRO LYS ALA LEU ALA PRO LEU LEU          
SEQRES  12 F  171  LEU ALA PHE VAL THR LYS PRO ASN SER ALA LEU GLU SER          
SEQRES  13 F  171  CYS SER PHE ALA ARG HIS SER LEU LEU GLN THR LEU TYR          
SEQRES  14 F  171  LYS VAL                                                      
SEQRES   1 G   65  GLY ALA MET ASP HIS VAL GLU PHE GLY SER GLY ASP PRO          
SEQRES   2 G   65  GLY SER GLU ILE ILE GLU SER VAL PRO PRO ALA GLY PRO          
SEQRES   3 G   65  GLU ALA SER GLU SER THR THR ASP GLU ASN GLU ASP ASP          
SEQRES   4 G   65  ILE GLN PHE VAL SER GLU GLY PRO LEU ARG PRO VAL LEU          
SEQRES   5 G   65  GLU TYR ILE ASP LEU VAL SER SER ASP ASP GLU GLU PRO          
HET    EDO  A 301      10                                                       
HET    EDO  C 601      10                                                       
HET    EDO  C 602      10                                                       
HET    EDO  F 601      10                                                       
HET    EDO  F 602      10                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   8  EDO    5(C2 H6 O2)                                                  
FORMUL  13  HOH   *702(H2 O)                                                    
HELIX    1 AA1 SER A    2  ASP A   19  1                                  18    
HELIX    2 AA2 LEU A   94  GLU A   98  5                                   5    
HELIX    3 AA3 THR A  108  ASN A  121  1                                  14    
HELIX    4 AA4 GLN A  130  ASN A  140  1                                  11    
HELIX    5 AA5 ASN A  140  PHE A  155  1                                  16    
HELIX    6 AA6 LEU B   40  GLY B   52  1                                  13    
HELIX    7 AA7 PRO C  431  PHE C  440  1                                  10    
HELIX    8 AA8 SER C  442  LEU C  449  1                                   8    
HELIX    9 AA9 LYS C  452  THR C  461  1                                  10    
HELIX   10 AB1 ASP C  465  SER C  478  1                                  14    
HELIX   11 AB2 GLU C  483  ASN C  503  1                                  21    
HELIX   12 AB3 ASN C  508  MET C  520  1                                  13    
HELIX   13 AB4 LEU C  535  GLN C  547  1                                  13    
HELIX   14 AB5 PRO C  552  ALA C  554  5                                   3    
HELIX   15 AB6 LEU C  555  LYS C  565  1                                  11    
HELIX   16 AB7 ASN C  567  SER C  572  1                                   6    
HELIX   17 AB8 CYS C  573  TYR C  585  1                                  13    
HELIX   18 AB9 SER D    2  ASP D   19  1                                  18    
HELIX   19 AC1 LEU D   94  GLU D   98  5                                   5    
HELIX   20 AC2 THR D  108  ASN D  121  1                                  14    
HELIX   21 AC3 GLN D  130  ASN D  140  1                                  11    
HELIX   22 AC4 ASN D  140  PHE D  155  1                                  16    
HELIX   23 AC5 LEU E   40  GLY E   52  1                                  13    
HELIX   24 AC6 SER E   54  ARG E   56  5                                   3    
HELIX   25 AC7 ALA F  432  PHE F  440  1                                   9    
HELIX   26 AC8 SER F  442  LEU F  449  1                                   8    
HELIX   27 AC9 LYS F  452  THR F  461  1                                  10    
HELIX   28 AD1 ASP F  465  SER F  478  1                                  14    
HELIX   29 AD2 GLU F  483  SER F  504  1                                  22    
HELIX   30 AD3 ASN F  508  MET F  520  1                                  13    
HELIX   31 AD4 LEU F  535  GLN F  547  1                                  13    
HELIX   32 AD5 PRO F  552  ALA F  554  5                                   3    
HELIX   33 AD6 LEU F  555  LYS F  565  1                                  11    
HELIX   34 AD7 ASN F  567  SER F  572  1                                   6    
HELIX   35 AD8 CYS F  573  TYR F  585  1                                  13    
SHEET    1 AA1 4 VAL A  25  LYS A  30  0                                        
SHEET    2 AA1 4 MET A  36  PRO A  46 -1  O  ASN A  37   N  THR A  29           
SHEET    3 AA1 4 LEU A  57  LEU A  63 -1  O  LEU A  60   N  CYS A  43           
SHEET    4 AA1 4 LYS A  74  PHE A  77 -1  O  LYS A  76   N  ARG A  61           
SHEET    1 AA2 6 GLN B  65  PRO B  66  0                                        
SHEET    2 AA2 6 ILE B  58  PHE B  62 -1  N  PHE B  62   O  GLN B  65           
SHEET    3 AA2 6 ASP B  82  GLN B  88 -1  O  PHE B  87   N  ARG B  59           
SHEET    4 AA2 6 ASN B  19  ALA B  23  1  N  LYS B  21   O  ILE B  84           
SHEET    5 AA2 6 SER B  28  LYS B  33 -1  O  PHE B  32   N  LEU B  20           
SHEET    6 AA2 6 GLN G  32  PRO G  38 -1  O  SER G  35   N  GLN B  31           
SHEET    1 AA3 4 VAL D  25  LYS D  30  0                                        
SHEET    2 AA3 4 MET D  36  PRO D  46 -1  O  ASN D  37   N  THR D  29           
SHEET    3 AA3 4 LEU D  57  LEU D  63 -1  O  LEU D  60   N  CYS D  43           
SHEET    4 AA3 4 LYS D  74  PHE D  77 -1  O  LYS D  76   N  ARG D  61           
SHEET    1 AA4 6 GLN E  65  PRO E  66  0                                        
SHEET    2 AA4 6 ILE E  58  PHE E  62 -1  N  PHE E  62   O  GLN E  65           
SHEET    3 AA4 6 ASP E  82  GLN E  88 -1  O  PHE E  87   N  ARG E  59           
SHEET    4 AA4 6 HIS E  17  ALA E  23  1  N  LYS E  21   O  ILE E  84           
SHEET    5 AA4 6 VAL E  29  LYS E  35 -1  O  PHE E  32   N  LEU E  20           
SHEET    6 AA4 6 VAL G  42  ASP G  47  1  O  ILE G  46   N  GLN E  31           
LINK         C   GLY B  93                 NZ  LYS C 524     1555   1555  1.37  
LINK         C   GLY E  93                 NZ  LYS F 524     1555   1555  1.32  
CISPEP   1 TYR A   68    PRO A   69          0         9.89                     
CISPEP   2 GLU A   78    PRO A   79          0        -0.18                     
CISPEP   3 TYR D   68    PRO D   69          0         2.94                     
CISPEP   4 GLU D   78    PRO D   79          0         0.47                     
SITE     1 AC1  7 LYS A  18  ASP A  19  HOH A 432  HOH A 434                    
SITE     2 AC1  7 HOH A 471  THR E  83  ARG G  40                               
SITE     1 AC2  1 GLY C 521                                                     
SITE     1 AC3  5 LYS C 481  ASP C 482  HOH C 764  HIS D  20                    
SITE     2 AC3  5 HOH D 265                                                     
SITE     1 AC4  4 GLY F 521  LEU F 522  LYS F 524  HOH F 713                    
SITE     1 AC5  5 TYR F 536  CYS F 573  SER F 574  PHE F 575                    
SITE     2 AC5  5 ALA F 576                                                     
SITE     1 AC6 12 ASN D  85  CYS D  93  ASP D 127  PRO D 128                    
SITE     2 AC6 12 ALA D 129  HOH D 239  GLY E  92  LEU F 523                    
SITE     3 AC6 12 SER F 525  EDO F 601  HOH F 707  HOH F 785                    
CRYST1   78.240  115.060  130.980  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012781  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008691  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007635        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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