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Database: PDB
Entry: 2C9W
LinkDB: 2C9W
Original site: 2C9W 
HEADER    TRANSCRIPTION REGULATION                14-DEC-05   2C9W              
TITLE     CRYSTAL STRUCTURE OF SOCS-2 IN COMPLEX WITH ELONGIN-B AND ELONGIN-C AT
TITLE    2 1.9A RESOLUTION                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPPRESSOR OF CYTOKINE SIGNALING 2;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HUMAN SOCS2, SOCS-2, CYTOKINE-INDUCIBLE SH2 PROTEIN 2, CIS- 
COMPND   5 2, STAT-INDUCED STAT INHIBITOR 2, SSI-2;                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2;           
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: HUMAN ELONGIN B, RNA POLYMERASE II TRANSCRIPTION FACTOR SIII
COMPND  11 SUBUNIT B, SIII P18, ELONGIN B, ELOB, ELONGIN 18 KDA SUBUNIT;        
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1;           
COMPND  15 CHAIN: C;                                                            
COMPND  16 SYNONYM: HUMAN ELONGIN C, RNA POLYMERASE II TRANSCRIPTION FACTOR SIII
COMPND  17 SUBUNIT C, SIII P15, ELONGIN C, ELOC, ELONGIN 15 KDA SUBUNIT;        
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: R3;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: P11;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    GROWTH REGULATION, SH2 DOMAIN, SIGNAL TRANSDUCTION INHIBITOR, NUCLEAR 
KEYWDS   2 PROTEIN, TRANSCRIPTION, TRANSCRIPTION REGULATION, UBL CONJUGATION    
KEYWDS   3 PATHWAY                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.DEBRECZENI,A.BULLOCK,A.AMOS,P.SAVITSKY,A.BARR,N.BURGESS,          
AUTHOR   2 M.SUNDSTROM,J.WEIGELT,C.ARROWSMITH,A.EDWARDS,S.KNAPP                 
REVDAT   7   09-OCT-19 2C9W    1       REMARK                                   
REVDAT   6   08-MAY-19 2C9W    1       REMARK                                   
REVDAT   5   03-APR-19 2C9W    1       REMARK                                   
REVDAT   4   28-FEB-18 2C9W    1       SOURCE JRNL                              
REVDAT   3   13-JUL-11 2C9W    1       VERSN                                    
REVDAT   2   24-FEB-09 2C9W    1       VERSN                                    
REVDAT   1   22-FEB-06 2C9W    0                                                
JRNL        AUTH   A.N.BULLOCK,J.E.DEBRECZENI,A.M.EDWARDS,M.SUNDSTROM,S.KNAPP   
JRNL        TITL   CRYSTAL STRUCTURE OF THE SOCS2-ELONGIN C-ELONGIN B COMPLEX   
JRNL        TITL 2 DEFINES A PROTOTYPICAL SOCS BOX UBIQUITIN LIGASE.            
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 103  7637 2006              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   16675548                                                     
JRNL        DOI    10.1073/PNAS.0601638103                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 91.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 33443                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1762                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2485                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 130                          
REMARK   3   BIN FREE R VALUE                    : 0.2750                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2621                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 18                                      
REMARK   3   SOLVENT ATOMS            : 172                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.55000                                              
REMARK   3    B22 (A**2) : 0.55000                                              
REMARK   3    B33 (A**2) : -0.82000                                             
REMARK   3    B12 (A**2) : 0.27000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.128         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.127         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.099         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.738         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2689 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3648 ; 1.209 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   330 ; 5.639 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   106 ;32.314 ;23.491       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   454 ;13.712 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;18.195 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   421 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1976 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1155 ; 0.192 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1846 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   196 ; 0.151 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    25 ; 0.149 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.115 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1734 ; 2.144 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2712 ; 3.094 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1091 ; 5.020 ; 7.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   936 ; 6.814 ;11.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    32        A   198                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.3520  22.2100  14.6120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0820 T22:  -0.1933                                     
REMARK   3      T33:  -0.1256 T12:  -0.0058                                     
REMARK   3      T13:   0.0215 T23:   0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4081 L22:   2.4324                                     
REMARK   3      L33:   3.7056 L12:  -0.9939                                     
REMARK   3      L13:  -0.3187 L23:   1.6787                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0509 S12:  -0.0721 S13:   0.0687                       
REMARK   3      S21:  -0.0755 S22:   0.0757 S23:  -0.3632                       
REMARK   3      S31:   0.0204 S32:   0.3356 S33:  -0.1267                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   104                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.3590  54.4210  -4.4210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0759 T22:  -0.0838                                     
REMARK   3      T33:  -0.0400 T12:   0.0638                                     
REMARK   3      T13:  -0.0061 T23:   0.0733                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6972 L22:   3.1554                                     
REMARK   3      L33:   4.2205 L12:  -1.1285                                     
REMARK   3      L13:   1.0375 L23:  -2.7598                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0919 S12:   0.1879 S13:   0.3518                       
REMARK   3      S21:   0.0585 S22:  -0.2304 S23:  -0.1896                       
REMARK   3      S31:  -0.2683 S32:   0.2143 S33:   0.1385                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    17        C   112                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.7130  44.7770  10.7460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0983 T22:  -0.2607                                     
REMARK   3      T33:  -0.1692 T12:   0.0187                                     
REMARK   3      T13:   0.0245 T23:   0.0274                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3959 L22:   3.8513                                     
REMARK   3      L33:   5.2003 L12:  -1.0894                                     
REMARK   3      L13:   1.7925 L23:  -2.2334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0283 S12:  -0.0549 S13:   0.0366                       
REMARK   3      S21:   0.2333 S22:   0.1995 S23:   0.3324                       
REMARK   3      S31:  -0.0998 S32:  -0.4512 S33:  -0.1711                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2C9W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-DEC-05.                  
REMARK 100 THE DEPOSITION ID IS D_1290026852.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.90008                            
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 395240                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 11.60                              
REMARK 200  R MERGE                    (I) : 0.07260                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.19                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.31000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.290                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1O4H, 1LM8                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMSO4 0.2M NACL, 0.1M CACODYLATE PH   
REMARK 280  6.5 300 NL SITTING DROPS AT 4 DEGREES, VAPOR DIFFUSION, SITTING     
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.80000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       23.40000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       23.40000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       46.80000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 SOCS FAMILY PROTEINS PARTICIPATE AT THE CLASSICAL NEGATIVE           
REMARK 400  FEEDBACK SYSTEM THAT REGULATES CYTOKINE SIGNAL TRANSDUCTION.        
REMARK 400  ELONGIN IS A GENERAL TRANSCRIPTION ELONGATION FACTOR                
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    30                                                      
REMARK 465     MET A    31                                                      
REMARK 465     ASP A   135                                                      
REMARK 465     LYS A   136                                                      
REMARK 465     ARG A   137                                                      
REMARK 465     THR A   138                                                      
REMARK 465     GLY A   139                                                      
REMARK 465     PRO A   140                                                      
REMARK 465     GLU A   141                                                      
REMARK 465     ALA A   142                                                      
REMARK 465     PRO A   143                                                      
REMARK 465     ARG A   144                                                      
REMARK 465     ASN A   145                                                      
REMARK 465     GLY A   146                                                      
REMARK 465     THR A   147                                                      
REMARK 465     VAL A   148                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B   105                                                      
REMARK 465     GLN B   106                                                      
REMARK 465     ASP B   107                                                      
REMARK 465     SER B   108                                                      
REMARK 465     GLY B   109                                                      
REMARK 465     SER B   110                                                      
REMARK 465     SER B   111                                                      
REMARK 465     ALA B   112                                                      
REMARK 465     ASN B   113                                                      
REMARK 465     GLU B   114                                                      
REMARK 465     GLN B   115                                                      
REMARK 465     ALA B   116                                                      
REMARK 465     VAL B   117                                                      
REMARK 465     GLN B   118                                                      
REMARK 465     MET C    16                                                      
REMARK 465     LEU C    46                                                      
REMARK 465     SER C    47                                                      
REMARK 465     GLY C    48                                                      
REMARK 465     PRO C    49                                                      
REMARK 465     GLY C    50                                                      
REMARK 465     GLN C    51                                                      
REMARK 465     PHE C    52                                                      
REMARK 465     ALA C    53                                                      
REMARK 465     GLU C    54                                                      
REMARK 465     ASN C    55                                                      
REMARK 465     GLU C    56                                                      
REMARK 465     THR C    57                                                      
REMARK 465     ASN C    85                                                      
REMARK 465     SER C    86                                                      
REMARK 465     SER C    87                                                      
REMARK 465     THR C    88                                                      
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     ARG A  35    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A  41    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  59    CD   CE   NZ                                        
REMARK 470     GLU A  60    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 100    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 101    CG   OD1  OD2                                       
REMARK 470     LYS A 113    CG   CD   CE   NZ                                   
REMARK 470     SER A 114    OG                                                  
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     LYS A 117    CD   CE   NZ                                        
REMARK 470     LYS A 134    CE   NZ                                             
REMARK 470     LYS A 154    CE   NZ                                             
REMARK 470     LYS A 195    CD   CE   NZ                                        
REMARK 470     LYS B  19    CE   NZ                                             
REMARK 470     ASP B  48    CG   OD1  OD2                                       
REMARK 470     LYS B  55    CE   NZ                                             
REMARK 470     GLN B  65    CD   OE1  NE2                                       
REMARK 470     GLU B  98    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 104    CG   CD   CE   NZ                                   
REMARK 470     LYS C  43    NZ                                                  
REMARK 470     ASN C  58    CG   OD1  ND2                                       
REMARK 470     ARG C  63    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU C  89    CD   OE1  OE2                                       
REMARK 470     GLU C  92    CG   CD   OE1  OE2                                  
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    SER A  52       26.13    -72.43                                   
REMARK 500    THR A 153      -76.13   -122.00                                   
REMARK 500    HIS B  10     -115.56     51.14                                   
REMARK 500    ASP B  47     -127.52     56.70                                   
REMARK 500    ALA B  71       67.53   -150.65                                   
REMARK 500    ASP B  82     -106.39     63.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1199                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A1202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A1203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B1105                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1LM8   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF A HIF-1A-PVHL-ELONGINB- ELONGINC COMPLEX                
REMARK 900 RELATED ID: 1LQB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A HYDROXYLATED HIF-1 ALPHA PEPTIDEBOUND TO THE  
REMARK 900 PVHL/ELONGIN-C/ ELONGIN-B COMPLEX                                    
REMARK 900 RELATED ID: 1VCB   RELATED DB: PDB                                   
REMARK 900 THE VHL-ELONGINC-ELONGINB STRUCTURE                                  
DBREF  2C9W A   30    31  PDB    2C9W     2C9W            30     31             
DBREF  2C9W A   32   198  UNP    O14508   SOCS2_HUMAN     32    198             
DBREF  2C9W B    1   118  UNP    Q15370   ELOB_HUMAN       1    118             
DBREF  2C9W C   16    16  PDB    2C9W     2C9W            16     16             
DBREF  2C9W C   17   112  UNP    Q15369   ELOC_HUMAN      17    112             
SEQRES   1 A  169  SER MET GLN ALA ALA ARG LEU ALA LYS ALA LEU ARG GLU          
SEQRES   2 A  169  LEU GLY GLN THR GLY TRP TYR TRP GLY SER MET THR VAL          
SEQRES   3 A  169  ASN GLU ALA LYS GLU LYS LEU LYS GLU ALA PRO GLU GLY          
SEQRES   4 A  169  THR PHE LEU ILE ARG ASP SER SER HIS SER ASP TYR LEU          
SEQRES   5 A  169  LEU THR ILE SER VAL LYS THR SER ALA GLY PRO THR ASN          
SEQRES   6 A  169  LEU ARG ILE GLU TYR GLN ASP GLY LYS PHE ARG LEU ASP          
SEQRES   7 A  169  SER ILE ILE CYS VAL LYS SER LYS LEU LYS GLN PHE ASP          
SEQRES   8 A  169  SER VAL VAL HIS LEU ILE ASP TYR TYR VAL GLN MET CYS          
SEQRES   9 A  169  LYS ASP LYS ARG THR GLY PRO GLU ALA PRO ARG ASN GLY          
SEQRES  10 A  169  THR VAL HIS LEU TYR LEU THR LYS PRO LEU TYR THR SER          
SEQRES  11 A  169  ALA PRO SER LEU GLN HIS LEU CYS ARG LEU THR ILE ASN          
SEQRES  12 A  169  LYS CYS THR GLY ALA ILE TRP GLY LEU PRO LEU PRO THR          
SEQRES  13 A  169  ARG LEU LYS ASP TYR LEU GLU GLU TYR LYS PHE GLN VAL          
SEQRES   1 B  118  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 B  118  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 B  118  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 B  118  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 B  118  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 B  118  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 B  118  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CYS ILE GLU          
SEQRES   8 B  118  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   9 B  118  PRO GLN ASP SER GLY SER SER ALA ASN GLU GLN ALA VAL          
SEQRES  10 B  118  GLN                                                          
SEQRES   1 C   97  MET MET TYR VAL LYS LEU ILE SER SER ASP GLY HIS GLU          
SEQRES   2 C   97  PHE ILE VAL LYS ARG GLU HIS ALA LEU THR SER GLY THR          
SEQRES   3 C   97  ILE LYS ALA MET LEU SER GLY PRO GLY GLN PHE ALA GLU          
SEQRES   4 C   97  ASN GLU THR ASN GLU VAL ASN PHE ARG GLU ILE PRO SER          
SEQRES   5 C   97  HIS VAL LEU SER LYS VAL CYS MET TYR PHE THR TYR LYS          
SEQRES   6 C   97  VAL ARG TYR THR ASN SER SER THR GLU ILE PRO GLU PHE          
SEQRES   7 C   97  PRO ILE ALA PRO GLU ILE ALA LEU GLU LEU LEU MET ALA          
SEQRES   8 C   97  ALA ASN PHE LEU ASP CYS                                      
HET    SO4  A1199       5                                                       
HET    SO4  A1200       5                                                       
HET    SO4  A1201       5                                                       
HET     NI  A1202       1                                                       
HET     NI  A1203       1                                                       
HET     NI  B1105       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      NI NICKEL (II) ION                                                  
FORMUL   4  SO4    3(O4 S 2-)                                                   
FORMUL   7   NI    3(NI 2+)                                                     
FORMUL  10  HOH   *172(H2 O)                                                    
HELIX    1   1 GLN A   32  THR A   46  1                                  15    
HELIX    2   2 THR A   54  LYS A   63  1                                  10    
HELIX    3   3 VAL A  112  LEU A  116  5                                   5    
HELIX    4   4 SER A  121  CYS A  133  1                                  13    
HELIX    5   5 SER A  162  THR A  175  1                                  14    
HELIX    6   6 ALA A  177  LEU A  181  5                                   5    
HELIX    7   7 PRO A  184  GLU A  193  1                                  10    
HELIX    8   8 THR B   23  LYS B   36  1                                  14    
HELIX    9   9 PRO B   38  ASP B   40  5                                   3    
HELIX   10  10 LEU B   57  GLY B   61  5                                   5    
HELIX   11  11 PRO B  100  LYS B  104  5                                   5    
HELIX   12  12 ARG C   33  LEU C   37  1                                   5    
HELIX   13  13 SER C   39  MET C   45  1                                   7    
HELIX   14  14 PRO C   66  TYR C   83  1                                  18    
HELIX   15  15 ALA C   96  ASP C  111  1                                  16    
SHEET    1  AA 4 PHE A  70  ASP A  74  0                                        
SHEET    2  AA 4 LEU A  82  THR A  88 -1  O  THR A  83   N  ARG A  73           
SHEET    3  AA 4 GLY A  91  GLN A 100 -1  O  GLY A  91   N  THR A  88           
SHEET    4  AA 4 LYS A 103  LEU A 106 -1  O  LYS A 103   N  GLN A 100           
SHEET    1  BA 8 GLN B  49  LEU B  50  0                                        
SHEET    2  BA 8 GLN B  42  LYS B  46 -1  O  LYS B  46   N  GLN B  49           
SHEET    3  BA 8 ALA B  73  ALA B  81 -1  O  GLY B  76   N  TYR B  45           
SHEET    4  BA 8 VAL B   3  ARG B   9  1  O  PHE B   4   N  ALA B  73           
SHEET    5  BA 8 THR B  12  ALA B  18 -1  O  THR B  12   N  ARG B   9           
SHEET    6  BA 8 GLU C  28  LYS C  32  1  O  GLU C  28   N  THR B  13           
SHEET    7  BA 8 TYR C  18  ILE C  22 -1  O  VAL C  19   N  VAL C  31           
SHEET    8  BA 8 GLU C  59  ASN C  61  1  O  VAL C  60   N  ILE C  22           
SHEET    1  BB 4 GLN B  49  LEU B  50  0                                        
SHEET    2  BB 4 GLN B  42  LYS B  46 -1  O  LYS B  46   N  GLN B  49           
SHEET    3  BB 4 ALA B  73  ALA B  81 -1  O  GLY B  76   N  TYR B  45           
SHEET    4  BB 4 THR B  84  PHE B  85 -1  O  THR B  84   N  ALA B  81           
LINK        NI    NI A1203                 SG  CYS A 111     1555   1555  2.12  
LINK        NI    NI B1105                 SG  CYS B  89     1555   1555  2.27  
SITE     1 AC1  7 VAL A  55  ARG A  73  SER A  75  SER A  76                    
SITE     2 AC1  7 THR A  83  ARG A  96  HOH A2074                               
SITE     1 AC2  4 THR A  54  ASN A  56  ARG A 105  HOH A2075                    
SITE     1 AC3  6 GLN A  45  SER A 162  ARG A 168  TYR A 190                    
SITE     2 AC3  6 HOH A2076  HOH A2077                                          
SITE     1 AC4  2 ASP A 120  HIS A 124                                          
SITE     1 AC5  1 CYS A 111                                                     
SITE     1 AC6  1 CYS B  89                                                     
CRYST1  105.290  105.290   70.200  90.00  90.00 120.00 P 32 2 1      6          
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      0.009498  0.005483  0.000000        0.00000                         
SCALE2      0.000000  0.010967  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014245        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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