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Database: PDB
Entry: 2IZV
LinkDB: 2IZV
Original site: 2IZV 
HEADER    TRANSCRIPTION                           26-JUL-06   2IZV              
TITLE     CRYSTAL STRUCTURE OF SOCS-4 IN COMPLEX WITH ELONGIN-B AND ELONGIN-C AT
TITLE    2 2.55A RESOLUTION                                                     
CAVEAT     2IZV    ASN A 267 C-ALPHA IS PLANAR                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPPRESSOR OF CYTOKINE SIGNALING 4;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 274-437;                                          
COMPND   5 SYNONYM: SOCS-4 ELONGIN B, C COMPLEX, SOCS-4, SOCS-7, SUPPRESSOR OF  
COMPND   6 CYTOKINE SIGNALING 7;                                                
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2;           
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: RNA POLYMERASE II TRANSCRIPTION FACTOR SIII SUBUNIT B, SIII 
COMPND  12 P18, ELONGIN B, ELOB, ELONGIN 18 KDA SUBUNIT;                        
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1;           
COMPND  16 CHAIN: C;                                                            
COMPND  17 FRAGMENT: RESIDUES 17-112;                                           
COMPND  18 SYNONYM: RNA POLYMERASE II TRANSCRIPTION FACTOR SIII SUBUNIT C, SIII 
COMPND  19 P15, ELONGIN-C, ELOC, ELONGIN 15 KDA SUBUNIT;                        
COMPND  20 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 EXPRESSION_SYSTEM_VARIANT: R3;                                       
SOURCE  16 EXPRESSION_SYSTEM_VECTOR: P11;                                       
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  23 EXPRESSION_SYSTEM_VARIANT: R3;                                       
SOURCE  24 EXPRESSION_SYSTEM_VECTOR: P11                                        
KEYWDS    SIGNAL TRANSDUCTION INHIBITOR, GROWTH REGULATION, SIGNAL              
KEYWDS   2 TRANSDUCTION, SH2 DOMAIN, TRANSCRIPTION, NUCLEAR PROTEIN, UBL        
KEYWDS   3 CONJUGATION PATHWAY, TRANSCRIPTION REGULATION                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.DEBRECZENI,A.BULLOCK,E.PAPAGRIGORIOU,A.TURNBULL,A.C.W.PIKE,       
AUTHOR   2 F.GORREC,F.VON DELFT,M.SUNDSTROM,C.ARROWSMITH,J.WEIGELT,A.EDWARDS,   
AUTHOR   3 S.KNAPP                                                              
REVDAT   6   08-MAY-19 2IZV    1       REMARK                                   
REVDAT   5   28-FEB-18 2IZV    1       SOURCE JRNL                              
REVDAT   4   24-JAN-18 2IZV    1       AUTHOR                                   
REVDAT   3   13-JUL-11 2IZV    1       VERSN                                    
REVDAT   2   24-FEB-09 2IZV    1       VERSN                                    
REVDAT   1   02-AUG-06 2IZV    0                                                
JRNL        AUTH   A.N.BULLOCK,M.C.RODRIGUEZ,J.E.DEBRECZENI,Z.SONGYANG,S.KNAPP  
JRNL        TITL   STRUCTURE OF THE SOCS4-ELONGINB/C COMPLEX REVEALS A DISTINCT 
JRNL        TITL 2 SOCS BOX INTERFACE AND THE MOLECULAR BASIS FOR               
JRNL        TITL 3 SOCS-DEPENDENT EGFR DEGRADATION.                             
JRNL        REF    STRUCTURE                     V.  15  1493 2007              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   17997974                                                     
JRNL        DOI    10.1016/J.STR.2007.09.016                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.55 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) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 77.38                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 18723                          
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) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1000                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.62                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1358                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2806                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 113                                     
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) : 25.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.22000                                             
REMARK   3    B22 (A**2) : -1.22000                                             
REMARK   3    B33 (A**2) : 1.83000                                              
REMARK   3    B12 (A**2) : -0.61000                                             
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): 0.288         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.229         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.152         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.503        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2882 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1966 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3910 ; 1.438 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4791 ; 1.006 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   349 ; 6.553 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   127 ;33.785 ;23.465       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   476 ;16.155 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;18.092 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   436 ; 0.144 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3158 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   596 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   535 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1935 ; 0.190 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1397 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1487 ; 0.089 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    95 ; 0.159 ; 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):     7 ; 0.162 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    34 ; 0.217 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.135 ; 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):  1774 ; 3.518 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2881 ; 5.295 ; 7.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1131 ; 7.002 ; 9.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1029 ; 8.759 ;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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   267        A   383                          
REMARK   3    RESIDUE RANGE :   A   422        A   429                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.5008 -16.1138  61.5944              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0127 T22:  -0.0086                                     
REMARK   3      T33:  -0.0535 T12:   0.0407                                     
REMARK   3      T13:  -0.0385 T23:   0.0516                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9031 L22:   2.6757                                     
REMARK   3      L33:   1.0306 L12:   0.8146                                     
REMARK   3      L13:   0.1039 L23:   0.0303                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0394 S12:  -0.2001 S13:  -0.1057                       
REMARK   3      S21:   0.2938 S22:  -0.0036 S23:  -0.0199                       
REMARK   3      S31:   0.0146 S32:  -0.0199 S33:  -0.0358                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   384        A   421                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2349  -6.5275  47.1676              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0457 T22:  -0.0571                                     
REMARK   3      T33:   0.0138 T12:   0.0241                                     
REMARK   3      T13:  -0.0087 T23:  -0.0249                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5906 L22:   3.7599                                     
REMARK   3      L33:   1.6225 L12:  -0.2030                                     
REMARK   3      L13:  -0.9701 L23:   0.6611                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1165 S12:  -0.1975 S13:   0.1240                       
REMARK   3      S21:  -0.2094 S22:   0.0110 S23:  -0.3413                       
REMARK   3      S31:  -0.1042 S32:   0.0249 S33:  -0.1274                       
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 :   B     2        B   104                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.1863 -29.7591  27.7502              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0854 T22:  -0.0974                                     
REMARK   3      T33:  -0.0403 T12:   0.0275                                     
REMARK   3      T13:   0.0156 T23:   0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3090 L22:   3.0440                                     
REMARK   3      L33:   1.8646 L12:  -1.6996                                     
REMARK   3      L13:  -1.6951 L23:   1.9404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0512 S12:   0.1284 S13:  -0.1869                       
REMARK   3      S21:  -0.2321 S22:  -0.1623 S23:   0.0169                       
REMARK   3      S31:  -0.0674 S32:  -0.1062 S33:   0.1111                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    17        C   112                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.6390 -16.8591  32.2935              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0323 T22:  -0.1156                                     
REMARK   3      T33:  -0.0492 T12:   0.0621                                     
REMARK   3      T13:  -0.0006 T23:   0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5625 L22:   1.8708                                     
REMARK   3      L33:   2.2259 L12:  -0.4579                                     
REMARK   3      L13:  -0.2497 L23:   0.1585                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1076 S12:   0.0854 S13:   0.1179                       
REMARK   3      S21:  -0.3384 S22:  -0.1158 S23:   0.0085                       
REMARK   3      S31:  -0.0863 S32:  -0.0893 S33:   0.0082                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2IZV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUL-06.                  
REMARK 100 THE DEPOSITION ID IS D_1290029506.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUN-06                          
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) : 0.8984                             
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19724                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.680                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 2.710                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.72                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.980                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2C9W                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 150 UL SITTING DROP 2M NACL 10% PEK6K,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       77.38500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       44.67825            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       22.63633            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       77.38500            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       44.67825            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       22.63633            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       77.38500            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       44.67825            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       22.63633            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       89.35650            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       45.27267            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       89.35650            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       45.27267            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       89.35650            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       45.27267            
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 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     MET A   251                                                      
REMARK 465     HIS A   252                                                      
REMARK 465     HIS A   253                                                      
REMARK 465     HIS A   254                                                      
REMARK 465     HIS A   255                                                      
REMARK 465     HIS A   256                                                      
REMARK 465     HIS A   257                                                      
REMARK 465     SER A   258                                                      
REMARK 465     SER A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     VAL A   261                                                      
REMARK 465     ASP A   262                                                      
REMARK 465     LEU A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     THR A   265                                                      
REMARK 465     GLU A   266                                                      
REMARK 465     VAL A   430                                                      
REMARK 465     LEU A   431                                                      
REMARK 465     ARG A   432                                                      
REMARK 465     ILE A   433                                                      
REMARK 465     ASP A   434                                                      
REMARK 465     ALA A   435                                                      
REMARK 465     PRO A   436                                                      
REMARK 465     GLU A   437                                                      
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     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 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     GLU A 316    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 425    CD   CE   NZ                                        
REMARK 470     LYS A 427    CD   CE   NZ                                        
REMARK 470     ARG A 429    NE   CZ   NH1  NH2                                  
REMARK 470     MET B   1    CG   SD   CE                                        
REMARK 470     LYS B  19    CE   NZ                                             
REMARK 470     GLN B  65    CD   OE1  NE2                                       
REMARK 470     ASP B  82    CG   OD1  OD2                                       
REMARK 470     ASP B  83    CG   OD1  OD2                                       
REMARK 470     GLU B  98    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 104    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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A 305      123.09    -37.95                                   
REMARK 500    HIS B  10     -119.33     51.70                                   
REMARK 500    ASP B  47     -126.76     61.23                                   
REMARK 500    ALA B  71       68.76   -152.79                                   
REMARK 500    ASP B  82     -121.38     69.53                                   
REMARK 500    ASP C 111       62.20     60.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1430  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 313   O                                                      
REMARK 620 2 GLN A 315   O    90.5                                              
REMARK 620 3 TYR A 318   O   100.3  74.7                                        
REMARK 620 4 HOH A2022   O    95.5  82.2 152.0                                  
REMARK 620 5 HOH A2023   O   172.5  94.4  75.6  90.8                            
REMARK 620 6 EDO A1431   O2   80.0 162.0  91.9 113.7  93.7                      
REMARK 620 N                    1     2     3     4     5                       
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 NA A1430                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1431                 
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                                  
REMARK 900 RELATED ID: 2C9W   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF SOCS-2 IN COMPLEX WITH ELONGIN-B AND ELONGIN-C  
REMARK 900 AT 1.9A RESOLUTION                                                   
DBREF  2IZV A  251   273  PDB    2IZV     2IZV           251    273             
DBREF  2IZV A  274   437  UNP    Q8WXH5   SOCS4_HUMAN    274    437             
DBREF  2IZV B    1   118  UNP    Q15370   ELOB_HUMAN       1    118             
DBREF  2IZV C   16    16  PDB    2IZV     2IZV            16     16             
DBREF  2IZV C   17   112  UNP    Q15369   ELOC_HUMAN      17    112             
SEQRES   1 A  187  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  187  GLY THR GLU ASN LEU TYR PHE GLN SER MET LEU VAL PRO          
SEQRES   3 A  187  ASP LEU LEU GLN ILE ASN ASN ASN PRO CYS TYR TRP GLY          
SEQRES   4 A  187  VAL MET ASP LYS TYR ALA ALA GLU ALA LEU LEU GLU GLY          
SEQRES   5 A  187  LYS PRO GLU GLY THR PHE LEU LEU ARG ASP SER ALA GLN          
SEQRES   6 A  187  GLU ASP TYR LEU PHE SER VAL SER PHE ARG ARG TYR SER          
SEQRES   7 A  187  ARG SER LEU HIS ALA ARG ILE GLU GLN TRP ASN HIS ASN          
SEQRES   8 A  187  PHE SER PHE ASP ALA HIS ASP PRO CYS VAL PHE HIS SER          
SEQRES   9 A  187  PRO ASP ILE THR GLY LEU LEU GLU HIS TYR LYS ASP PRO          
SEQRES  10 A  187  SER ALA CYS MET PHE PHE GLU PRO LEU LEU SER THR PRO          
SEQRES  11 A  187  LEU ILE ARG THR PHE PRO PHE SER LEU GLN HIS ILE CYS          
SEQRES  12 A  187  ARG THR VAL ILE CYS ASN CYS THR THR TYR ASP GLY ILE          
SEQRES  13 A  187  ASP ALA LEU PRO ILE PRO SER SER MET LYS LEU TYR LEU          
SEQRES  14 A  187  LYS GLU TYR HIS TYR LYS SER LYS VAL ARG VAL LEU ARG          
SEQRES  15 A  187  ILE ASP ALA PRO GLU                                          
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     NA  A1430       1                                                       
HET    EDO  A1431       4                                                       
HET     CL  A1432       1                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      CL CHLORIDE ION                                                     
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   4   NA    NA 1+                                                        
FORMUL   5  EDO    C2 H6 O2                                                     
FORMUL   6   CL    CL 1-                                                        
FORMUL   7  HOH   *113(H2 O)                                                    
HELIX    1   1 ASP A  277  ASN A  284  1                                   8    
HELIX    2   2 ASP A  292  GLU A  301  1                                  10    
HELIX    3   3 ASP A  356  TYR A  364  1                                   9    
HELIX    4   4 ASP A  366  CYS A  370  5                                   5    
HELIX    5   5 SER A  388  THR A  401  1                                  14    
HELIX    6   6 THR A  402  ALA A  408  1                                   7    
HELIX    7   7 PRO A  412  LYS A  420  1                                   9    
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 PRO B  100  LYS B  104  5                                   5    
HELIX   11  11 ARG C   33  LEU C   37  1                                   5    
HELIX   12  12 SER C   39  MET C   45  1                                   7    
HELIX   13  13 PRO C   66  TYR C   83  1                                  18    
HELIX   14  14 ALA C   96  ASP C  111  1                                  16    
SHEET    1  AA 2 GLN A 271  LEU A 274  0                                        
SHEET    2  AA 2 HIS A 423  SER A 426 -1  O  TYR A 424   N  MET A 273           
SHEET    1  AB 3 TYR A 287  VAL A 290  0                                        
SHEET    2  AB 3 THR A 307  ASP A 312  1  O  LEU A 310   N  TRP A 288           
SHEET    3  AB 3 THR A 379  PRO A 380  1  O  THR A 379   N  PHE A 308           
SHEET    1  AC 4 TYR A 287  VAL A 290  0                                        
SHEET    2  AC 4 THR A 307  ASP A 312  1  O  LEU A 310   N  TRP A 288           
SHEET    3  AC 4 PHE A 320  ARG A 326 -1  O  SER A 321   N  ARG A 311           
SHEET    4  AC 4 ARG A 329  ARG A 334 -1  O  ARG A 329   N  ARG A 326           
SHEET    1  AD 2 GLU A 336  TRP A 338  0                                        
SHEET    2  AD 2 ASN A 341  SER A 343 -1  O  ASN A 341   N  TRP A 338           
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 ASP B   2  ARG B   9  1  O  PHE B   4   N  ALA B  73           
SHEET    5  BA 8 THR B  12  LYS B  19 -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        NA    NA A1430                 O   SER A 313     1555   1555  2.37  
LINK        NA    NA A1430                 O   GLN A 315     1555   1555  2.50  
LINK        NA    NA A1430                 O   TYR A 318     1555   1555  2.44  
LINK        NA    NA A1430                 O   HOH A2022     1555   1555  2.59  
LINK        NA    NA A1430                 O   HOH A2023     1555   1555  2.41  
LINK        NA    NA A1430                 O2  EDO A1431     1555   1555  2.50  
SITE     1 AC1  6 SER A 313  GLN A 315  TYR A 318  EDO A1431                    
SITE     2 AC1  6 HOH A2022  HOH A2023                                          
SITE     1 AC2  7 ASP A 312  SER A 313  TYR A 318  LEU A 319                    
SITE     2 AC2  7 GLU A 421   NA A1430  HOH A2020                               
CRYST1  154.770  154.770   67.909  90.00  90.00 120.00 H 3           9          
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      0.006461  0.003730  0.000000        0.00000                         
SCALE2      0.000000  0.007461  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014726        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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